data_9BFV
# 
_entry.id   9BFV 
# 
_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   9BFV         pdb_00009bfv 10.2210/pdb9bfv/pdb 
WWPDB D_1000283281 ?            ?                   
# 
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 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-12 ? 
3 'Structure model' 1 2 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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Structure summary'   
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' struct          
2 3 'Structure model' citation        
3 3 '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' '_struct.title'                     
2 3 'Structure model' '_citation.journal_volume'          
3 3 'Structure model' '_citation.page_first'              
4 3 'Structure model' '_citation.page_last'               
5 3 '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                        9BFV 
_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 
'Knox, J.E.'        2 ?                   
'Yano, J.K.'        3 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                6041 
_citation.page_last                 6063 
_citation.title                     
;Discovery of Elironrasib (RMC-6291), a Potent and Orally Bioavailable, RAS(ON) G12C-Selective, Covalent Tricomplex Inhibitor for the Treatment of Patients with RAS G12C-Addicted Cancers.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02313 
_citation.pdbx_database_id_PubMed   39993169 
_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 'Pota, K.'          2  ? 
primary 'Tomlinson, A.C.A.' 3  ? 
primary 'Yano, J.'          4  ? 
primary 'Marquez, A.'       5  ? 
primary 'Liu, Y.'           6  ? 
primary 'Schulze, C.J.'     7  ? 
primary 'Seamon, K.J.'      8  ? 
primary 'Holderfield, M.'   9  ? 
primary 'Wei, X.'           10 ? 
primary 'Zhuang, Y.'        11 ? 
primary 'Yang, Y.C.'        12 ? 
primary 'Jiang, J.'         13 ? 
primary 'Huang, Y.'         14 ? 
primary 'Zhao, R.'          15 ? 
primary 'Ling, Y.'          16 ? 
primary 'Wang, Z.'          17 ? 
primary 'Flagella, M.'      18 ? 
primary 'Wang, Z.'          19 ? 
primary 'Singh, M.'         20 ? 
primary 'Knox, J.E.'        21 ? 
primary 'Nichols, R.'       22 ? 
primary 'Wildes, D.'        23 ? 
primary 'Smith, J.A.M.'     24 ? 
primary 'Koltun, E.S.'      25 ? 
primary 'Gill, A.L.'        26 ? 
# 
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' 19404.928 2   3.6.5.2 ? ? ? 
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 
;(3R)-1-[(2E)-4-(dimethylamino)-4-methylpent-2-enoyl]-N-[(2S)-1-{[(1P,8R,10R,14S,21M)-22-ethyl-21-{2-[(1R)-1-methoxyethyl]pyridin-3-yl}-18,18-dimethyl-9,15-dioxo-16-oxa-10,22,28-triazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),2(29),3,5,20,23,26-heptaen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-N-methylpyrrolidine-3-carboxamide (non-preferred name)
;
973.252   2   ?       ? ? ? 
5 non-polymer syn 'MAGNESIUM ION' 24.305    2   ?       ? ? ? 
6 water       nat water 18.015    906 ?       ? ? ? 
# 
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 
;SMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;SMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFL
CVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
A,B ? 
2 'polypeptide(L)' no no 
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
D,C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
4 
;(3R)-1-[(2E)-4-(dimethylamino)-4-methylpent-2-enoyl]-N-[(2S)-1-{[(1P,8R,10R,14S,21M)-22-ethyl-21-{2-[(1R)-1-methoxyethyl]pyridin-3-yl}-18,18-dimethyl-9,15-dioxo-16-oxa-10,22,28-triazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),2(29),3,5,20,23,26-heptaen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-N-methylpyrrolidine-3-carboxamide (non-preferred name)
;
A1AOV 
5 'MAGNESIUM ION' MG    
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  CYS 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 
A1AOV non-polymer         . 
;(3R)-1-[(2E)-4-(dimethylamino)-4-methylpent-2-enoyl]-N-[(2S)-1-{[(1P,8R,10R,14S,21M)-22-ethyl-21-{2-[(1R)-1-methoxyethyl]pyridin-3-yl}-18,18-dimethyl-9,15-dioxo-16-oxa-10,22,28-triazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),2(29),3,5,20,23,26-heptaen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-N-methylpyrrolidine-3-carboxamide (non-preferred name)
;
? 'C56 H76 N8 O7'     973.252 
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  CYS 13  12  12  CYS CYS 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 170 169 169 LYS LYS A . n 
B 1 1   SER 1   0   0   SER SER B . n 
B 1 2   MET 2   1   1   MET MET B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   GLU 4   3   3   GLU GLU B . n 
B 1 5   TYR 5   4   4   TYR TYR B . n 
B 1 6   LYS 6   5   5   LYS LYS B . n 
B 1 7   LEU 7   6   6   LEU LEU B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   VAL 9   8   8   VAL VAL B . n 
B 1 10  VAL 10  9   9   VAL VAL B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ALA 12  11  11  ALA ALA B . n 
B 1 13  CYS 13  12  12  CYS CYS 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 170 169 169 LYS LYS B . n 
C 2 1   SER 1   0   ?   ?   ?   D . n 
C 2 2   MET 2   1   1   MET MET D . n 
C 2 3   VAL 3   2   2   VAL VAL D . n 
C 2 4   ASN 4   3   3   ASN ASN D . n 
C 2 5   PRO 5   4   4   PRO PRO D . n 
C 2 6   THR 6   5   5   THR THR D . n 
C 2 7   VAL 7   6   6   VAL VAL D . n 
C 2 8   PHE 8   7   7   PHE PHE D . n 
C 2 9   PHE 9   8   8   PHE PHE D . n 
C 2 10  ASP 10  9   9   ASP ASP D . n 
C 2 11  ILE 11  10  10  ILE ILE D . n 
C 2 12  ALA 12  11  11  ALA ALA D . n 
C 2 13  VAL 13  12  12  VAL VAL D . n 
C 2 14  ASP 14  13  13  ASP ASP D . n 
C 2 15  GLY 15  14  14  GLY GLY D . n 
C 2 16  GLU 16  15  15  GLU GLU D . n 
C 2 17  PRO 17  16  16  PRO PRO D . n 
C 2 18  LEU 18  17  17  LEU LEU D . n 
C 2 19  GLY 19  18  18  GLY GLY D . n 
C 2 20  ARG 20  19  19  ARG ARG D . n 
C 2 21  VAL 21  20  20  VAL VAL D . n 
C 2 22  SER 22  21  21  SER SER D . n 
C 2 23  PHE 23  22  22  PHE PHE D . n 
C 2 24  GLU 24  23  23  GLU GLU D . n 
C 2 25  LEU 25  24  24  LEU LEU D . n 
C 2 26  PHE 26  25  25  PHE PHE D . n 
C 2 27  ALA 27  26  26  ALA ALA D . n 
C 2 28  ASP 28  27  27  ASP ASP D . n 
C 2 29  LYS 29  28  28  LYS LYS D . n 
C 2 30  VAL 30  29  29  VAL VAL D . n 
C 2 31  PRO 31  30  30  PRO PRO D . n 
C 2 32  LYS 32  31  31  LYS LYS D . n 
C 2 33  THR 33  32  32  THR THR D . n 
C 2 34  ALA 34  33  33  ALA ALA D . n 
C 2 35  GLU 35  34  34  GLU GLU D . n 
C 2 36  ASN 36  35  35  ASN ASN D . n 
C 2 37  PHE 37  36  36  PHE PHE D . n 
C 2 38  ARG 38  37  37  ARG ARG D . n 
C 2 39  ALA 39  38  38  ALA ALA D . n 
C 2 40  LEU 40  39  39  LEU LEU D . n 
C 2 41  SER 41  40  40  SER SER D . n 
C 2 42  THR 42  41  41  THR THR D . n 
C 2 43  GLY 43  42  42  GLY GLY D . n 
C 2 44  GLU 44  43  43  GLU GLU D . n 
C 2 45  LYS 45  44  44  LYS LYS D . n 
C 2 46  GLY 46  45  45  GLY GLY D . n 
C 2 47  PHE 47  46  46  PHE PHE D . n 
C 2 48  GLY 48  47  47  GLY GLY D . n 
C 2 49  TYR 49  48  48  TYR TYR D . n 
C 2 50  LYS 50  49  49  LYS LYS D . n 
C 2 51  GLY 51  50  50  GLY GLY D . n 
C 2 52  SER 52  51  51  SER SER D . n 
C 2 53  CYS 53  52  52  CYS CYS D . n 
C 2 54  PHE 54  53  53  PHE PHE D . n 
C 2 55  HIS 55  54  54  HIS HIS D . n 
C 2 56  ARG 56  55  55  ARG ARG D . n 
C 2 57  ILE 57  56  56  ILE ILE D . n 
C 2 58  ILE 58  57  57  ILE ILE D . n 
C 2 59  PRO 59  58  58  PRO PRO D . n 
C 2 60  GLY 60  59  59  GLY GLY D . n 
C 2 61  PHE 61  60  60  PHE PHE D . n 
C 2 62  MET 62  61  61  MET MET D . n 
C 2 63  CYS 63  62  62  CYS CYS D . n 
C 2 64  GLN 64  63  63  GLN GLN D . n 
C 2 65  GLY 65  64  64  GLY GLY D . n 
C 2 66  GLY 66  65  65  GLY GLY D . n 
C 2 67  ASP 67  66  66  ASP ASP D . n 
C 2 68  PHE 68  67  67  PHE PHE D . n 
C 2 69  THR 69  68  68  THR THR D . n 
C 2 70  ARG 70  69  69  ARG ARG D . n 
C 2 71  HIS 71  70  70  HIS HIS D . n 
C 2 72  ASN 72  71  71  ASN ASN D . n 
C 2 73  GLY 73  72  72  GLY GLY D . n 
C 2 74  THR 74  73  73  THR THR D . n 
C 2 75  GLY 75  74  74  GLY GLY D . n 
C 2 76  GLY 76  75  75  GLY GLY D . n 
C 2 77  LYS 77  76  76  LYS LYS D . n 
C 2 78  SER 78  77  77  SER SER D . n 
C 2 79  ILE 79  78  78  ILE ILE D . n 
C 2 80  TYR 80  79  79  TYR TYR D . n 
C 2 81  GLY 81  80  80  GLY GLY D . n 
C 2 82  GLU 82  81  81  GLU GLU D . n 
C 2 83  LYS 83  82  82  LYS LYS D . n 
C 2 84  PHE 84  83  83  PHE PHE D . n 
C 2 85  GLU 85  84  84  GLU GLU D . n 
C 2 86  ASP 86  85  85  ASP ASP D . n 
C 2 87  GLU 87  86  86  GLU GLU D . n 
C 2 88  ASN 88  87  87  ASN ASN D . n 
C 2 89  PHE 89  88  88  PHE PHE D . n 
C 2 90  ILE 90  89  89  ILE ILE D . n 
C 2 91  LEU 91  90  90  LEU LEU D . n 
C 2 92  LYS 92  91  91  LYS LYS D . n 
C 2 93  HIS 93  92  92  HIS HIS D . n 
C 2 94  THR 94  93  93  THR THR D . n 
C 2 95  GLY 95  94  94  GLY GLY D . n 
C 2 96  PRO 96  95  95  PRO PRO D . n 
C 2 97  GLY 97  96  96  GLY GLY D . n 
C 2 98  ILE 98  97  97  ILE ILE D . n 
C 2 99  LEU 99  98  98  LEU LEU D . n 
C 2 100 SER 100 99  99  SER SER D . n 
C 2 101 MET 101 100 100 MET MET D . n 
C 2 102 ALA 102 101 101 ALA ALA D . n 
C 2 103 ASN 103 102 102 ASN ASN D . n 
C 2 104 ALA 104 103 103 ALA ALA D . n 
C 2 105 GLY 105 104 104 GLY GLY D . n 
C 2 106 PRO 106 105 105 PRO PRO D . n 
C 2 107 ASN 107 106 106 ASN ASN D . n 
C 2 108 THR 108 107 107 THR THR D . n 
C 2 109 ASN 109 108 108 ASN ASN D . n 
C 2 110 GLY 110 109 109 GLY GLY D . n 
C 2 111 SER 111 110 110 SER SER D . n 
C 2 112 GLN 112 111 111 GLN GLN D . n 
C 2 113 PHE 113 112 112 PHE PHE D . n 
C 2 114 PHE 114 113 113 PHE PHE D . n 
C 2 115 ILE 115 114 114 ILE ILE D . n 
C 2 116 CYS 116 115 115 CYS CYS D . n 
C 2 117 THR 117 116 116 THR THR D . n 
C 2 118 ALA 118 117 117 ALA ALA D . n 
C 2 119 LYS 119 118 118 LYS LYS D . n 
C 2 120 THR 120 119 119 THR THR D . n 
C 2 121 GLU 121 120 120 GLU GLU D . n 
C 2 122 TRP 122 121 121 TRP TRP D . n 
C 2 123 LEU 123 122 122 LEU LEU D . n 
C 2 124 ASP 124 123 123 ASP ASP D . n 
C 2 125 GLY 125 124 124 GLY GLY D . n 
C 2 126 LYS 126 125 125 LYS LYS D . n 
C 2 127 HIS 127 126 126 HIS HIS D . n 
C 2 128 VAL 128 127 127 VAL VAL D . n 
C 2 129 VAL 129 128 128 VAL VAL D . n 
C 2 130 PHE 130 129 129 PHE PHE D . n 
C 2 131 GLY 131 130 130 GLY GLY D . n 
C 2 132 LYS 132 131 131 LYS LYS D . n 
C 2 133 VAL 133 132 132 VAL VAL D . n 
C 2 134 LYS 134 133 133 LYS LYS D . n 
C 2 135 GLU 135 134 134 GLU GLU D . n 
C 2 136 GLY 136 135 135 GLY GLY D . n 
C 2 137 MET 137 136 136 MET MET D . n 
C 2 138 ASN 138 137 137 ASN ASN D . n 
C 2 139 ILE 139 138 138 ILE ILE D . n 
C 2 140 VAL 140 139 139 VAL VAL D . n 
C 2 141 GLU 141 140 140 GLU GLU D . n 
C 2 142 ALA 142 141 141 ALA ALA D . n 
C 2 143 MET 143 142 142 MET MET D . n 
C 2 144 GLU 144 143 143 GLU GLU D . n 
C 2 145 ARG 145 144 144 ARG ARG D . n 
C 2 146 PHE 146 145 145 PHE PHE D . n 
C 2 147 GLY 147 146 146 GLY GLY D . n 
C 2 148 SER 148 147 147 SER SER D . n 
C 2 149 ARG 149 148 148 ARG ARG D . n 
C 2 150 ASN 150 149 149 ASN ASN D . n 
C 2 151 GLY 151 150 150 GLY GLY D . n 
C 2 152 LYS 152 151 151 LYS LYS D . n 
C 2 153 THR 153 152 152 THR THR D . n 
C 2 154 SER 154 153 153 SER SER D . n 
C 2 155 LYS 155 154 154 LYS LYS D . n 
C 2 156 LYS 156 155 155 LYS LYS D . n 
C 2 157 ILE 157 156 156 ILE ILE D . n 
C 2 158 THR 158 157 157 THR THR D . n 
C 2 159 ILE 159 158 158 ILE ILE D . n 
C 2 160 ALA 160 159 159 ALA ALA D . n 
C 2 161 ASP 161 160 160 ASP ASP D . n 
C 2 162 CYS 162 161 161 CYS CYS D . n 
C 2 163 GLY 163 162 162 GLY GLY D . n 
C 2 164 GLN 164 163 163 GLN GLN D . n 
C 2 165 LEU 165 164 164 LEU LEU D . n 
C 2 166 GLU 166 165 ?   ?   ?   D . n 
D 2 1   SER 1   0   ?   ?   ?   C . n 
D 2 2   MET 2   1   1   MET MET C . n 
D 2 3   VAL 3   2   2   VAL VAL C . n 
D 2 4   ASN 4   3   3   ASN ASN C . n 
D 2 5   PRO 5   4   4   PRO PRO C . n 
D 2 6   THR 6   5   5   THR THR C . n 
D 2 7   VAL 7   6   6   VAL VAL C . n 
D 2 8   PHE 8   7   7   PHE PHE C . n 
D 2 9   PHE 9   8   8   PHE PHE C . n 
D 2 10  ASP 10  9   9   ASP ASP C . n 
D 2 11  ILE 11  10  10  ILE ILE C . n 
D 2 12  ALA 12  11  11  ALA ALA C . n 
D 2 13  VAL 13  12  12  VAL VAL C . n 
D 2 14  ASP 14  13  13  ASP ASP C . n 
D 2 15  GLY 15  14  14  GLY GLY C . n 
D 2 16  GLU 16  15  15  GLU GLU C . n 
D 2 17  PRO 17  16  16  PRO PRO C . n 
D 2 18  LEU 18  17  17  LEU LEU C . n 
D 2 19  GLY 19  18  18  GLY GLY C . n 
D 2 20  ARG 20  19  19  ARG ARG C . n 
D 2 21  VAL 21  20  20  VAL VAL C . n 
D 2 22  SER 22  21  21  SER SER C . n 
D 2 23  PHE 23  22  22  PHE PHE C . n 
D 2 24  GLU 24  23  23  GLU GLU C . n 
D 2 25  LEU 25  24  24  LEU LEU C . n 
D 2 26  PHE 26  25  25  PHE PHE C . n 
D 2 27  ALA 27  26  26  ALA ALA C . n 
D 2 28  ASP 28  27  27  ASP ASP C . n 
D 2 29  LYS 29  28  28  LYS LYS C . n 
D 2 30  VAL 30  29  29  VAL VAL C . n 
D 2 31  PRO 31  30  30  PRO PRO C . n 
D 2 32  LYS 32  31  31  LYS LYS C . n 
D 2 33  THR 33  32  32  THR THR C . n 
D 2 34  ALA 34  33  33  ALA ALA C . n 
D 2 35  GLU 35  34  34  GLU GLU C . n 
D 2 36  ASN 36  35  35  ASN ASN C . n 
D 2 37  PHE 37  36  36  PHE PHE C . n 
D 2 38  ARG 38  37  37  ARG ARG C . n 
D 2 39  ALA 39  38  38  ALA ALA C . n 
D 2 40  LEU 40  39  39  LEU LEU C . n 
D 2 41  SER 41  40  40  SER SER C . n 
D 2 42  THR 42  41  41  THR THR C . n 
D 2 43  GLY 43  42  42  GLY GLY C . n 
D 2 44  GLU 44  43  43  GLU GLU C . n 
D 2 45  LYS 45  44  44  LYS LYS C . n 
D 2 46  GLY 46  45  45  GLY GLY C . n 
D 2 47  PHE 47  46  46  PHE PHE C . n 
D 2 48  GLY 48  47  47  GLY GLY C . n 
D 2 49  TYR 49  48  48  TYR TYR C . n 
D 2 50  LYS 50  49  49  LYS LYS C . n 
D 2 51  GLY 51  50  50  GLY GLY C . n 
D 2 52  SER 52  51  51  SER SER C . n 
D 2 53  CYS 53  52  52  CYS CYS C . n 
D 2 54  PHE 54  53  53  PHE PHE C . n 
D 2 55  HIS 55  54  54  HIS HIS C . n 
D 2 56  ARG 56  55  55  ARG ARG C . n 
D 2 57  ILE 57  56  56  ILE ILE C . n 
D 2 58  ILE 58  57  57  ILE ILE C . n 
D 2 59  PRO 59  58  58  PRO PRO C . n 
D 2 60  GLY 60  59  59  GLY GLY C . n 
D 2 61  PHE 61  60  60  PHE PHE C . n 
D 2 62  MET 62  61  61  MET MET C . n 
D 2 63  CYS 63  62  62  CYS CYS C . n 
D 2 64  GLN 64  63  63  GLN GLN C . n 
D 2 65  GLY 65  64  64  GLY GLY C . n 
D 2 66  GLY 66  65  65  GLY GLY C . n 
D 2 67  ASP 67  66  66  ASP ASP C . n 
D 2 68  PHE 68  67  67  PHE PHE C . n 
D 2 69  THR 69  68  68  THR THR C . n 
D 2 70  ARG 70  69  69  ARG ARG C . n 
D 2 71  HIS 71  70  70  HIS HIS C . n 
D 2 72  ASN 72  71  71  ASN ASN C . n 
D 2 73  GLY 73  72  72  GLY GLY C . n 
D 2 74  THR 74  73  73  THR THR C . n 
D 2 75  GLY 75  74  74  GLY GLY C . n 
D 2 76  GLY 76  75  75  GLY GLY C . n 
D 2 77  LYS 77  76  76  LYS LYS C . n 
D 2 78  SER 78  77  77  SER SER C . n 
D 2 79  ILE 79  78  78  ILE ILE C . n 
D 2 80  TYR 80  79  79  TYR TYR C . n 
D 2 81  GLY 81  80  80  GLY GLY C . n 
D 2 82  GLU 82  81  81  GLU GLU C . n 
D 2 83  LYS 83  82  82  LYS LYS C . n 
D 2 84  PHE 84  83  83  PHE PHE C . n 
D 2 85  GLU 85  84  84  GLU GLU C . n 
D 2 86  ASP 86  85  85  ASP ASP C . n 
D 2 87  GLU 87  86  86  GLU GLU C . n 
D 2 88  ASN 88  87  87  ASN ASN C . n 
D 2 89  PHE 89  88  88  PHE PHE C . n 
D 2 90  ILE 90  89  89  ILE ILE C . n 
D 2 91  LEU 91  90  90  LEU LEU C . n 
D 2 92  LYS 92  91  91  LYS LYS C . n 
D 2 93  HIS 93  92  92  HIS HIS C . n 
D 2 94  THR 94  93  93  THR THR C . n 
D 2 95  GLY 95  94  94  GLY GLY C . n 
D 2 96  PRO 96  95  95  PRO PRO C . n 
D 2 97  GLY 97  96  96  GLY GLY C . n 
D 2 98  ILE 98  97  97  ILE ILE C . n 
D 2 99  LEU 99  98  98  LEU LEU C . n 
D 2 100 SER 100 99  99  SER SER C . n 
D 2 101 MET 101 100 100 MET MET C . n 
D 2 102 ALA 102 101 101 ALA ALA C . n 
D 2 103 ASN 103 102 102 ASN ASN C . n 
D 2 104 ALA 104 103 103 ALA ALA C . n 
D 2 105 GLY 105 104 104 GLY GLY C . n 
D 2 106 PRO 106 105 105 PRO PRO C . n 
D 2 107 ASN 107 106 106 ASN ASN C . n 
D 2 108 THR 108 107 107 THR THR C . n 
D 2 109 ASN 109 108 108 ASN ASN C . n 
D 2 110 GLY 110 109 109 GLY GLY C . n 
D 2 111 SER 111 110 110 SER SER C . n 
D 2 112 GLN 112 111 111 GLN GLN C . n 
D 2 113 PHE 113 112 112 PHE PHE C . n 
D 2 114 PHE 114 113 113 PHE PHE C . n 
D 2 115 ILE 115 114 114 ILE ILE C . n 
D 2 116 CYS 116 115 115 CYS CYS C . n 
D 2 117 THR 117 116 116 THR THR C . n 
D 2 118 ALA 118 117 117 ALA ALA C . n 
D 2 119 LYS 119 118 118 LYS LYS C . n 
D 2 120 THR 120 119 119 THR THR C . n 
D 2 121 GLU 121 120 120 GLU GLU C . n 
D 2 122 TRP 122 121 121 TRP TRP C . n 
D 2 123 LEU 123 122 122 LEU LEU C . n 
D 2 124 ASP 124 123 123 ASP ASP C . n 
D 2 125 GLY 125 124 124 GLY GLY C . n 
D 2 126 LYS 126 125 125 LYS LYS C . n 
D 2 127 HIS 127 126 126 HIS HIS C . n 
D 2 128 VAL 128 127 127 VAL VAL C . n 
D 2 129 VAL 129 128 128 VAL VAL C . n 
D 2 130 PHE 130 129 129 PHE PHE C . n 
D 2 131 GLY 131 130 130 GLY GLY C . n 
D 2 132 LYS 132 131 131 LYS LYS C . n 
D 2 133 VAL 133 132 132 VAL VAL C . n 
D 2 134 LYS 134 133 133 LYS LYS C . n 
D 2 135 GLU 135 134 134 GLU GLU C . n 
D 2 136 GLY 136 135 135 GLY GLY C . n 
D 2 137 MET 137 136 136 MET MET C . n 
D 2 138 ASN 138 137 137 ASN ASN C . n 
D 2 139 ILE 139 138 138 ILE ILE C . n 
D 2 140 VAL 140 139 139 VAL VAL C . n 
D 2 141 GLU 141 140 140 GLU GLU C . n 
D 2 142 ALA 142 141 141 ALA ALA C . n 
D 2 143 MET 143 142 142 MET MET C . n 
D 2 144 GLU 144 143 143 GLU GLU C . n 
D 2 145 ARG 145 144 144 ARG ARG C . n 
D 2 146 PHE 146 145 145 PHE PHE C . n 
D 2 147 GLY 147 146 146 GLY GLY C . n 
D 2 148 SER 148 147 147 SER SER C . n 
D 2 149 ARG 149 148 148 ARG ARG C . n 
D 2 150 ASN 150 149 149 ASN ASN C . n 
D 2 151 GLY 151 150 150 GLY GLY C . n 
D 2 152 LYS 152 151 151 LYS LYS C . n 
D 2 153 THR 153 152 152 THR THR C . n 
D 2 154 SER 154 153 153 SER SER C . n 
D 2 155 LYS 155 154 154 LYS LYS C . n 
D 2 156 LYS 156 155 155 LYS LYS C . n 
D 2 157 ILE 157 156 156 ILE ILE C . n 
D 2 158 THR 158 157 157 THR THR C . n 
D 2 159 ILE 159 158 158 ILE ILE C . n 
D 2 160 ALA 160 159 159 ALA ALA C . n 
D 2 161 ASP 161 160 160 ASP ASP C . n 
D 2 162 CYS 162 161 161 CYS CYS C . n 
D 2 163 GLY 163 162 162 GLY GLY C . n 
D 2 164 GLN 164 163 163 GLN GLN C . n 
D 2 165 LEU 165 164 164 LEU LEU C . n 
D 2 166 GLU 166 165 165 GLU GLU C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AOV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AOV 
_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 A1AOV 1   202 4106 A1AOV RMC A . 
G 5 MG    1   203 1    MG    MG  A . 
H 3 GNP   1   201 201  GNP   GNP B . 
I 4 A1AOV 1   202 4106 A1AOV RMC B . 
J 5 MG    1   203 2    MG    MG  B . 
K 6 HOH   1   301 490  HOH   HOH A . 
K 6 HOH   2   302 950  HOH   HOH A . 
K 6 HOH   3   303 861  HOH   HOH A . 
K 6 HOH   4   304 262  HOH   HOH A . 
K 6 HOH   5   305 832  HOH   HOH A . 
K 6 HOH   6   306 201  HOH   HOH A . 
K 6 HOH   7   307 426  HOH   HOH A . 
K 6 HOH   8   308 245  HOH   HOH A . 
K 6 HOH   9   309 316  HOH   HOH A . 
K 6 HOH   10  310 900  HOH   HOH A . 
K 6 HOH   11  311 487  HOH   HOH A . 
K 6 HOH   12  312 933  HOH   HOH A . 
K 6 HOH   13  313 578  HOH   HOH A . 
K 6 HOH   14  314 1    HOH   HOH A . 
K 6 HOH   15  315 771  HOH   HOH A . 
K 6 HOH   16  316 611  HOH   HOH A . 
K 6 HOH   17  317 562  HOH   HOH A . 
K 6 HOH   18  318 252  HOH   HOH A . 
K 6 HOH   19  319 880  HOH   HOH A . 
K 6 HOH   20  320 174  HOH   HOH A . 
K 6 HOH   21  321 990  HOH   HOH A . 
K 6 HOH   22  322 420  HOH   HOH A . 
K 6 HOH   23  323 601  HOH   HOH A . 
K 6 HOH   24  324 534  HOH   HOH A . 
K 6 HOH   25  325 205  HOH   HOH A . 
K 6 HOH   26  326 568  HOH   HOH A . 
K 6 HOH   27  327 638  HOH   HOH A . 
K 6 HOH   28  328 537  HOH   HOH A . 
K 6 HOH   29  329 310  HOH   HOH A . 
K 6 HOH   30  330 574  HOH   HOH A . 
K 6 HOH   31  331 653  HOH   HOH A . 
K 6 HOH   32  332 431  HOH   HOH A . 
K 6 HOH   33  333 410  HOH   HOH A . 
K 6 HOH   34  334 881  HOH   HOH A . 
K 6 HOH   35  335 484  HOH   HOH A . 
K 6 HOH   36  336 921  HOH   HOH A . 
K 6 HOH   37  337 408  HOH   HOH A . 
K 6 HOH   38  338 12   HOH   HOH A . 
K 6 HOH   39  339 130  HOH   HOH A . 
K 6 HOH   40  340 155  HOH   HOH A . 
K 6 HOH   41  341 791  HOH   HOH A . 
K 6 HOH   42  342 737  HOH   HOH A . 
K 6 HOH   43  343 196  HOH   HOH A . 
K 6 HOH   44  344 24   HOH   HOH A . 
K 6 HOH   45  345 517  HOH   HOH A . 
K 6 HOH   46  346 35   HOH   HOH A . 
K 6 HOH   47  347 87   HOH   HOH A . 
K 6 HOH   48  348 493  HOH   HOH A . 
K 6 HOH   49  349 10   HOH   HOH A . 
K 6 HOH   50  350 3    HOH   HOH A . 
K 6 HOH   51  351 460  HOH   HOH A . 
K 6 HOH   52  352 290  HOH   HOH A . 
K 6 HOH   53  353 584  HOH   HOH A . 
K 6 HOH   54  354 36   HOH   HOH A . 
K 6 HOH   55  355 571  HOH   HOH A . 
K 6 HOH   56  356 348  HOH   HOH A . 
K 6 HOH   57  357 128  HOH   HOH A . 
K 6 HOH   58  358 62   HOH   HOH A . 
K 6 HOH   59  359 996  HOH   HOH A . 
K 6 HOH   60  360 42   HOH   HOH A . 
K 6 HOH   61  361 555  HOH   HOH A . 
K 6 HOH   62  362 1000 HOH   HOH A . 
K 6 HOH   63  363 647  HOH   HOH A . 
K 6 HOH   64  364 39   HOH   HOH A . 
K 6 HOH   65  365 414  HOH   HOH A . 
K 6 HOH   66  366 332  HOH   HOH A . 
K 6 HOH   67  367 271  HOH   HOH A . 
K 6 HOH   68  368 552  HOH   HOH A . 
K 6 HOH   69  369 27   HOH   HOH A . 
K 6 HOH   70  370 106  HOH   HOH A . 
K 6 HOH   71  371 17   HOH   HOH A . 
K 6 HOH   72  372 192  HOH   HOH A . 
K 6 HOH   73  373 293  HOH   HOH A . 
K 6 HOH   74  374 738  HOH   HOH A . 
K 6 HOH   75  375 448  HOH   HOH A . 
K 6 HOH   76  376 224  HOH   HOH A . 
K 6 HOH   77  377 168  HOH   HOH A . 
K 6 HOH   78  378 120  HOH   HOH A . 
K 6 HOH   79  379 644  HOH   HOH A . 
K 6 HOH   80  380 132  HOH   HOH A . 
K 6 HOH   81  381 227  HOH   HOH A . 
K 6 HOH   82  382 362  HOH   HOH A . 
K 6 HOH   83  383 485  HOH   HOH A . 
K 6 HOH   84  384 866  HOH   HOH A . 
K 6 HOH   85  385 214  HOH   HOH A . 
K 6 HOH   86  386 57   HOH   HOH A . 
K 6 HOH   87  387 194  HOH   HOH A . 
K 6 HOH   88  388 112  HOH   HOH A . 
K 6 HOH   89  389 208  HOH   HOH A . 
K 6 HOH   90  390 734  HOH   HOH A . 
K 6 HOH   91  391 538  HOH   HOH A . 
K 6 HOH   92  392 834  HOH   HOH A . 
K 6 HOH   93  393 381  HOH   HOH A . 
K 6 HOH   94  394 116  HOH   HOH A . 
K 6 HOH   95  395 119  HOH   HOH A . 
K 6 HOH   96  396 304  HOH   HOH A . 
K 6 HOH   97  397 1001 HOH   HOH A . 
K 6 HOH   98  398 803  HOH   HOH A . 
K 6 HOH   99  399 501  HOH   HOH A . 
K 6 HOH   100 400 443  HOH   HOH A . 
K 6 HOH   101 401 331  HOH   HOH A . 
K 6 HOH   102 402 668  HOH   HOH A . 
K 6 HOH   103 403 704  HOH   HOH A . 
K 6 HOH   104 404 762  HOH   HOH A . 
K 6 HOH   105 405 281  HOH   HOH A . 
K 6 HOH   106 406 579  HOH   HOH A . 
K 6 HOH   107 407 148  HOH   HOH A . 
K 6 HOH   108 408 380  HOH   HOH A . 
K 6 HOH   109 409 72   HOH   HOH A . 
K 6 HOH   110 410 373  HOH   HOH A . 
K 6 HOH   111 411 811  HOH   HOH A . 
K 6 HOH   112 412 572  HOH   HOH A . 
K 6 HOH   113 413 516  HOH   HOH A . 
K 6 HOH   114 414 104  HOH   HOH A . 
K 6 HOH   115 415 499  HOH   HOH A . 
K 6 HOH   116 416 621  HOH   HOH A . 
K 6 HOH   117 417 93   HOH   HOH A . 
K 6 HOH   118 418 4    HOH   HOH A . 
K 6 HOH   119 419 213  HOH   HOH A . 
K 6 HOH   120 420 240  HOH   HOH A . 
K 6 HOH   121 421 997  HOH   HOH A . 
K 6 HOH   122 422 231  HOH   HOH A . 
K 6 HOH   123 423 81   HOH   HOH A . 
K 6 HOH   124 424 911  HOH   HOH A . 
K 6 HOH   125 425 792  HOH   HOH A . 
K 6 HOH   126 426 790  HOH   HOH A . 
K 6 HOH   127 427 222  HOH   HOH A . 
K 6 HOH   128 428 329  HOH   HOH A . 
K 6 HOH   129 429 48   HOH   HOH A . 
K 6 HOH   130 430 178  HOH   HOH A . 
K 6 HOH   131 431 511  HOH   HOH A . 
K 6 HOH   132 432 705  HOH   HOH A . 
K 6 HOH   133 433 333  HOH   HOH A . 
K 6 HOH   134 434 429  HOH   HOH A . 
K 6 HOH   135 435 758  HOH   HOH A . 
K 6 HOH   136 436 65   HOH   HOH A . 
K 6 HOH   137 437 299  HOH   HOH A . 
K 6 HOH   138 438 678  HOH   HOH A . 
K 6 HOH   139 439 181  HOH   HOH A . 
K 6 HOH   140 440 732  HOH   HOH A . 
K 6 HOH   141 441 802  HOH   HOH A . 
K 6 HOH   142 442 266  HOH   HOH A . 
K 6 HOH   143 443 354  HOH   HOH A . 
K 6 HOH   144 444 844  HOH   HOH A . 
K 6 HOH   145 445 800  HOH   HOH A . 
K 6 HOH   146 446 220  HOH   HOH A . 
K 6 HOH   147 447 90   HOH   HOH A . 
K 6 HOH   148 448 175  HOH   HOH A . 
K 6 HOH   149 449 301  HOH   HOH A . 
K 6 HOH   150 450 752  HOH   HOH A . 
K 6 HOH   151 451 419  HOH   HOH A . 
K 6 HOH   152 452 353  HOH   HOH A . 
K 6 HOH   153 453 113  HOH   HOH A . 
K 6 HOH   154 454 108  HOH   HOH A . 
K 6 HOH   155 455 437  HOH   HOH A . 
K 6 HOH   156 456 879  HOH   HOH A . 
K 6 HOH   157 457 445  HOH   HOH A . 
K 6 HOH   158 458 223  HOH   HOH A . 
K 6 HOH   159 459 506  HOH   HOH A . 
K 6 HOH   160 460 868  HOH   HOH A . 
K 6 HOH   161 461 733  HOH   HOH A . 
K 6 HOH   162 462 573  HOH   HOH A . 
K 6 HOH   163 463 184  HOH   HOH A . 
K 6 HOH   164 464 233  HOH   HOH A . 
K 6 HOH   165 465 322  HOH   HOH A . 
K 6 HOH   166 466 1028 HOH   HOH A . 
K 6 HOH   167 467 596  HOH   HOH A . 
K 6 HOH   168 468 141  HOH   HOH A . 
K 6 HOH   169 469 930  HOH   HOH A . 
K 6 HOH   170 470 709  HOH   HOH A . 
K 6 HOH   171 471 595  HOH   HOH A . 
K 6 HOH   172 472 884  HOH   HOH A . 
K 6 HOH   173 473 989  HOH   HOH A . 
K 6 HOH   174 474 902  HOH   HOH A . 
K 6 HOH   175 475 819  HOH   HOH A . 
K 6 HOH   176 476 107  HOH   HOH A . 
K 6 HOH   177 477 609  HOH   HOH A . 
K 6 HOH   178 478 935  HOH   HOH A . 
K 6 HOH   179 479 335  HOH   HOH A . 
K 6 HOH   180 480 581  HOH   HOH A . 
K 6 HOH   181 481 400  HOH   HOH A . 
K 6 HOH   182 482 466  HOH   HOH A . 
K 6 HOH   183 483 553  HOH   HOH A . 
K 6 HOH   184 484 1027 HOH   HOH A . 
K 6 HOH   185 485 696  HOH   HOH A . 
K 6 HOH   186 486 267  HOH   HOH A . 
K 6 HOH   187 487 386  HOH   HOH A . 
K 6 HOH   188 488 489  HOH   HOH A . 
K 6 HOH   189 489 679  HOH   HOH A . 
K 6 HOH   190 490 962  HOH   HOH A . 
K 6 HOH   191 491 842  HOH   HOH A . 
K 6 HOH   192 492 746  HOH   HOH A . 
K 6 HOH   193 493 798  HOH   HOH A . 
K 6 HOH   194 494 899  HOH   HOH A . 
K 6 HOH   195 495 988  HOH   HOH A . 
K 6 HOH   196 496 998  HOH   HOH A . 
K 6 HOH   197 497 631  HOH   HOH A . 
K 6 HOH   198 498 187  HOH   HOH A . 
K 6 HOH   199 499 632  HOH   HOH A . 
K 6 HOH   200 500 1029 HOH   HOH A . 
K 6 HOH   201 501 674  HOH   HOH A . 
K 6 HOH   202 502 157  HOH   HOH A . 
K 6 HOH   203 503 636  HOH   HOH A . 
K 6 HOH   204 504 985  HOH   HOH A . 
K 6 HOH   205 505 405  HOH   HOH A . 
K 6 HOH   206 506 723  HOH   HOH A . 
K 6 HOH   207 507 708  HOH   HOH A . 
K 6 HOH   208 508 992  HOH   HOH A . 
K 6 HOH   209 509 585  HOH   HOH A . 
K 6 HOH   210 510 975  HOH   HOH A . 
K 6 HOH   211 511 814  HOH   HOH A . 
K 6 HOH   212 512 999  HOH   HOH A . 
K 6 HOH   213 513 542  HOH   HOH A . 
K 6 HOH   214 514 406  HOH   HOH A . 
K 6 HOH   215 515 739  HOH   HOH A . 
K 6 HOH   216 516 622  HOH   HOH A . 
K 6 HOH   217 517 492  HOH   HOH A . 
K 6 HOH   218 518 285  HOH   HOH A . 
K 6 HOH   219 519 645  HOH   HOH A . 
K 6 HOH   220 520 296  HOH   HOH A . 
K 6 HOH   221 521 297  HOH   HOH A . 
K 6 HOH   222 522 265  HOH   HOH A . 
K 6 HOH   223 523 518  HOH   HOH A . 
K 6 HOH   224 524 954  HOH   HOH A . 
K 6 HOH   225 525 422  HOH   HOH A . 
K 6 HOH   226 526 242  HOH   HOH A . 
K 6 HOH   227 527 913  HOH   HOH A . 
K 6 HOH   228 528 821  HOH   HOH A . 
K 6 HOH   229 529 901  HOH   HOH A . 
K 6 HOH   230 530 551  HOH   HOH A . 
K 6 HOH   231 531 974  HOH   HOH A . 
K 6 HOH   232 532 502  HOH   HOH A . 
K 6 HOH   233 533 454  HOH   HOH A . 
K 6 HOH   234 534 634  HOH   HOH A . 
K 6 HOH   235 535 995  HOH   HOH A . 
K 6 HOH   236 536 888  HOH   HOH A . 
K 6 HOH   237 537 185  HOH   HOH A . 
K 6 HOH   238 538 664  HOH   HOH A . 
K 6 HOH   239 539 569  HOH   HOH A . 
K 6 HOH   240 540 156  HOH   HOH A . 
K 6 HOH   241 541 715  HOH   HOH A . 
K 6 HOH   242 542 776  HOH   HOH A . 
K 6 HOH   243 543 978  HOH   HOH A . 
K 6 HOH   244 544 1030 HOH   HOH A . 
K 6 HOH   245 545 270  HOH   HOH A . 
K 6 HOH   246 546 497  HOH   HOH A . 
K 6 HOH   247 547 863  HOH   HOH A . 
K 6 HOH   248 548 440  HOH   HOH A . 
K 6 HOH   249 549 751  HOH   HOH A . 
K 6 HOH   250 550 651  HOH   HOH A . 
K 6 HOH   251 551 905  HOH   HOH A . 
L 6 HOH   1   301 369  HOH   HOH B . 
L 6 HOH   2   302 896  HOH   HOH B . 
L 6 HOH   3   303 580  HOH   HOH B . 
L 6 HOH   4   304 504  HOH   HOH B . 
L 6 HOH   5   305 428  HOH   HOH B . 
L 6 HOH   6   306 411  HOH   HOH B . 
L 6 HOH   7   307 277  HOH   HOH B . 
L 6 HOH   8   308 778  HOH   HOH B . 
L 6 HOH   9   309 64   HOH   HOH B . 
L 6 HOH   10  310 427  HOH   HOH B . 
L 6 HOH   11  311 575  HOH   HOH B . 
L 6 HOH   12  312 287  HOH   HOH B . 
L 6 HOH   13  313 28   HOH   HOH B . 
L 6 HOH   14  314 308  HOH   HOH B . 
L 6 HOH   15  315 904  HOH   HOH B . 
L 6 HOH   16  316 189  HOH   HOH B . 
L 6 HOH   17  317 722  HOH   HOH B . 
L 6 HOH   18  318 773  HOH   HOH B . 
L 6 HOH   19  319 292  HOH   HOH B . 
L 6 HOH   20  320 474  HOH   HOH B . 
L 6 HOH   21  321 529  HOH   HOH B . 
L 6 HOH   22  322 524  HOH   HOH B . 
L 6 HOH   23  323 718  HOH   HOH B . 
L 6 HOH   24  324 808  HOH   HOH B . 
L 6 HOH   25  325 398  HOH   HOH B . 
L 6 HOH   26  326 464  HOH   HOH B . 
L 6 HOH   27  327 812  HOH   HOH B . 
L 6 HOH   28  328 70   HOH   HOH B . 
L 6 HOH   29  329 491  HOH   HOH B . 
L 6 HOH   30  330 162  HOH   HOH B . 
L 6 HOH   31  331 452  HOH   HOH B . 
L 6 HOH   32  332 1031 HOH   HOH B . 
L 6 HOH   33  333 191  HOH   HOH B . 
L 6 HOH   34  334 612  HOH   HOH B . 
L 6 HOH   35  335 357  HOH   HOH B . 
L 6 HOH   36  336 763  HOH   HOH B . 
L 6 HOH   37  337 451  HOH   HOH B . 
L 6 HOH   38  338 922  HOH   HOH B . 
L 6 HOH   39  339 51   HOH   HOH B . 
L 6 HOH   40  340 318  HOH   HOH B . 
L 6 HOH   41  341 41   HOH   HOH B . 
L 6 HOH   42  342 30   HOH   HOH B . 
L 6 HOH   43  343 45   HOH   HOH B . 
L 6 HOH   44  344 238  HOH   HOH B . 
L 6 HOH   45  345 456  HOH   HOH B . 
L 6 HOH   46  346 226  HOH   HOH B . 
L 6 HOH   47  347 649  HOH   HOH B . 
L 6 HOH   48  348 450  HOH   HOH B . 
L 6 HOH   49  349 1002 HOH   HOH B . 
L 6 HOH   50  350 341  HOH   HOH B . 
L 6 HOH   51  351 458  HOH   HOH B . 
L 6 HOH   52  352 60   HOH   HOH B . 
L 6 HOH   53  353 350  HOH   HOH B . 
L 6 HOH   54  354 55   HOH   HOH B . 
L 6 HOH   55  355 744  HOH   HOH B . 
L 6 HOH   56  356 142  HOH   HOH B . 
L 6 HOH   57  357 390  HOH   HOH B . 
L 6 HOH   58  358 556  HOH   HOH B . 
L 6 HOH   59  359 351  HOH   HOH B . 
L 6 HOH   60  360 8    HOH   HOH B . 
L 6 HOH   61  361 147  HOH   HOH B . 
L 6 HOH   62  362 251  HOH   HOH B . 
L 6 HOH   63  363 167  HOH   HOH B . 
L 6 HOH   64  364 170  HOH   HOH B . 
L 6 HOH   65  365 365  HOH   HOH B . 
L 6 HOH   66  366 75   HOH   HOH B . 
L 6 HOH   67  367 44   HOH   HOH B . 
L 6 HOH   68  368 663  HOH   HOH B . 
L 6 HOH   69  369 101  HOH   HOH B . 
L 6 HOH   70  370 161  HOH   HOH B . 
L 6 HOH   71  371 770  HOH   HOH B . 
L 6 HOH   72  372 232  HOH   HOH B . 
L 6 HOH   73  373 1009 HOH   HOH B . 
L 6 HOH   74  374 650  HOH   HOH B . 
L 6 HOH   75  375 550  HOH   HOH B . 
L 6 HOH   76  376 138  HOH   HOH B . 
L 6 HOH   77  377 295  HOH   HOH B . 
L 6 HOH   78  378 565  HOH   HOH B . 
L 6 HOH   79  379 91   HOH   HOH B . 
L 6 HOH   80  380 59   HOH   HOH B . 
L 6 HOH   81  381 374  HOH   HOH B . 
L 6 HOH   82  382 809  HOH   HOH B . 
L 6 HOH   83  383 444  HOH   HOH B . 
L 6 HOH   84  384 602  HOH   HOH B . 
L 6 HOH   85  385 204  HOH   HOH B . 
L 6 HOH   86  386 53   HOH   HOH B . 
L 6 HOH   87  387 261  HOH   HOH B . 
L 6 HOH   88  388 912  HOH   HOH B . 
L 6 HOH   89  389 2    HOH   HOH B . 
L 6 HOH   90  390 436  HOH   HOH B . 
L 6 HOH   91  391 342  HOH   HOH B . 
L 6 HOH   92  392 425  HOH   HOH B . 
L 6 HOH   93  393 402  HOH   HOH B . 
L 6 HOH   94  394 186  HOH   HOH B . 
L 6 HOH   95  395 417  HOH   HOH B . 
L 6 HOH   96  396 477  HOH   HOH B . 
L 6 HOH   97  397 815  HOH   HOH B . 
L 6 HOH   98  398 614  HOH   HOH B . 
L 6 HOH   99  399 784  HOH   HOH B . 
L 6 HOH   100 400 254  HOH   HOH B . 
L 6 HOH   101 401 282  HOH   HOH B . 
L 6 HOH   102 402 383  HOH   HOH B . 
L 6 HOH   103 403 767  HOH   HOH B . 
L 6 HOH   104 404 217  HOH   HOH B . 
L 6 HOH   105 405 110  HOH   HOH B . 
L 6 HOH   106 406 118  HOH   HOH B . 
L 6 HOH   107 407 600  HOH   HOH B . 
L 6 HOH   108 408 576  HOH   HOH B . 
L 6 HOH   109 409 121  HOH   HOH B . 
L 6 HOH   110 410 910  HOH   HOH B . 
L 6 HOH   111 411 312  HOH   HOH B . 
L 6 HOH   112 412 1004 HOH   HOH B . 
L 6 HOH   113 413 134  HOH   HOH B . 
L 6 HOH   114 414 557  HOH   HOH B . 
L 6 HOH   115 415 243  HOH   HOH B . 
L 6 HOH   116 416 169  HOH   HOH B . 
L 6 HOH   117 417 300  HOH   HOH B . 
L 6 HOH   118 418 76   HOH   HOH B . 
L 6 HOH   119 419 462  HOH   HOH B . 
L 6 HOH   120 420 706  HOH   HOH B . 
L 6 HOH   121 421 523  HOH   HOH B . 
L 6 HOH   122 422 152  HOH   HOH B . 
L 6 HOH   123 423 212  HOH   HOH B . 
L 6 HOH   124 424 370  HOH   HOH B . 
L 6 HOH   125 425 870  HOH   HOH B . 
L 6 HOH   126 426 987  HOH   HOH B . 
L 6 HOH   127 427 67   HOH   HOH B . 
L 6 HOH   128 428 835  HOH   HOH B . 
L 6 HOH   129 429 943  HOH   HOH B . 
L 6 HOH   130 430 263  HOH   HOH B . 
L 6 HOH   131 431 347  HOH   HOH B . 
L 6 HOH   132 432 68   HOH   HOH B . 
L 6 HOH   133 433 115  HOH   HOH B . 
L 6 HOH   134 434 525  HOH   HOH B . 
L 6 HOH   135 435 239  HOH   HOH B . 
L 6 HOH   136 436 867  HOH   HOH B . 
L 6 HOH   137 437 646  HOH   HOH B . 
L 6 HOH   138 438 826  HOH   HOH B . 
L 6 HOH   139 439 560  HOH   HOH B . 
L 6 HOH   140 440 198  HOH   HOH B . 
L 6 HOH   141 441 850  HOH   HOH B . 
L 6 HOH   142 442 897  HOH   HOH B . 
L 6 HOH   143 443 986  HOH   HOH B . 
L 6 HOH   144 444 712  HOH   HOH B . 
L 6 HOH   145 445 415  HOH   HOH B . 
L 6 HOH   146 446 694  HOH   HOH B . 
L 6 HOH   147 447 919  HOH   HOH B . 
L 6 HOH   148 448 917  HOH   HOH B . 
L 6 HOH   149 449 364  HOH   HOH B . 
L 6 HOH   150 450 959  HOH   HOH B . 
L 6 HOH   151 451 755  HOH   HOH B . 
L 6 HOH   152 452 630  HOH   HOH B . 
L 6 HOH   153 453 753  HOH   HOH B . 
L 6 HOH   154 454 520  HOH   HOH B . 
L 6 HOH   155 455 620  HOH   HOH B . 
L 6 HOH   156 456 280  HOH   HOH B . 
L 6 HOH   157 457 725  HOH   HOH B . 
L 6 HOH   158 458 543  HOH   HOH B . 
L 6 HOH   159 459 1008 HOH   HOH B . 
L 6 HOH   160 460 283  HOH   HOH B . 
L 6 HOH   161 461 777  HOH   HOH B . 
L 6 HOH   162 462 993  HOH   HOH B . 
L 6 HOH   163 463 932  HOH   HOH B . 
L 6 HOH   164 464 1006 HOH   HOH B . 
L 6 HOH   165 465 741  HOH   HOH B . 
L 6 HOH   166 466 833  HOH   HOH B . 
L 6 HOH   167 467 728  HOH   HOH B . 
L 6 HOH   168 468 772  HOH   HOH B . 
L 6 HOH   169 469 669  HOH   HOH B . 
L 6 HOH   170 470 352  HOH   HOH B . 
L 6 HOH   171 471 228  HOH   HOH B . 
L 6 HOH   172 472 695  HOH   HOH B . 
L 6 HOH   173 473 608  HOH   HOH B . 
L 6 HOH   174 474 1005 HOH   HOH B . 
L 6 HOH   175 475 401  HOH   HOH B . 
L 6 HOH   176 476 219  HOH   HOH B . 
L 6 HOH   177 477 682  HOH   HOH B . 
L 6 HOH   178 478 498  HOH   HOH B . 
L 6 HOH   179 479 909  HOH   HOH B . 
L 6 HOH   180 480 465  HOH   HOH B . 
L 6 HOH   181 481 865  HOH   HOH B . 
L 6 HOH   182 482 789  HOH   HOH B . 
L 6 HOH   183 483 983  HOH   HOH B . 
L 6 HOH   184 484 309  HOH   HOH B . 
L 6 HOH   185 485 838  HOH   HOH B . 
L 6 HOH   186 486 564  HOH   HOH B . 
L 6 HOH   187 487 662  HOH   HOH B . 
L 6 HOH   188 488 89   HOH   HOH B . 
L 6 HOH   189 489 907  HOH   HOH B . 
L 6 HOH   190 490 325  HOH   HOH B . 
L 6 HOH   191 491 599  HOH   HOH B . 
L 6 HOH   192 492 944  HOH   HOH B . 
L 6 HOH   193 493 828  HOH   HOH B . 
L 6 HOH   194 494 96   HOH   HOH B . 
L 6 HOH   195 495 109  HOH   HOH B . 
L 6 HOH   196 496 864  HOH   HOH B . 
M 6 HOH   1   201 481  HOH   HOH D . 
M 6 HOH   2   202 291  HOH   HOH D . 
M 6 HOH   3   203 479  HOH   HOH D . 
M 6 HOH   4   204 389  HOH   HOH D . 
M 6 HOH   5   205 298  HOH   HOH D . 
M 6 HOH   6   206 890  HOH   HOH D . 
M 6 HOH   7   207 330  HOH   HOH D . 
M 6 HOH   8   208 438  HOH   HOH D . 
M 6 HOH   9   209 684  HOH   HOH D . 
M 6 HOH   10  210 813  HOH   HOH D . 
M 6 HOH   11  211 702  HOH   HOH D . 
M 6 HOH   12  212 675  HOH   HOH D . 
M 6 HOH   13  213 320  HOH   HOH D . 
M 6 HOH   14  214 197  HOH   HOH D . 
M 6 HOH   15  215 1015 HOH   HOH D . 
M 6 HOH   16  216 193  HOH   HOH D . 
M 6 HOH   17  217 114  HOH   HOH D . 
M 6 HOH   18  218 221  HOH   HOH D . 
M 6 HOH   19  219 657  HOH   HOH D . 
M 6 HOH   20  220 49   HOH   HOH D . 
M 6 HOH   21  221 11   HOH   HOH D . 
M 6 HOH   22  222 179  HOH   HOH D . 
M 6 HOH   23  223 248  HOH   HOH D . 
M 6 HOH   24  224 33   HOH   HOH D . 
M 6 HOH   25  225 385  HOH   HOH D . 
M 6 HOH   26  226 423  HOH   HOH D . 
M 6 HOH   27  227 29   HOH   HOH D . 
M 6 HOH   28  228 412  HOH   HOH D . 
M 6 HOH   29  229 851  HOH   HOH D . 
M 6 HOH   30  230 948  HOH   HOH D . 
M 6 HOH   31  231 176  HOH   HOH D . 
M 6 HOH   32  232 627  HOH   HOH D . 
M 6 HOH   33  233 533  HOH   HOH D . 
M 6 HOH   34  234 94   HOH   HOH D . 
M 6 HOH   35  235 95   HOH   HOH D . 
M 6 HOH   36  236 441  HOH   HOH D . 
M 6 HOH   37  237 103  HOH   HOH D . 
M 6 HOH   38  238 124  HOH   HOH D . 
M 6 HOH   39  239 7    HOH   HOH D . 
M 6 HOH   40  240 532  HOH   HOH D . 
M 6 HOH   41  241 384  HOH   HOH D . 
M 6 HOH   42  242 421  HOH   HOH D . 
M 6 HOH   43  243 970  HOH   HOH D . 
M 6 HOH   44  244 52   HOH   HOH D . 
M 6 HOH   45  245 199  HOH   HOH D . 
M 6 HOH   46  246 84   HOH   HOH D . 
M 6 HOH   47  247 519  HOH   HOH D . 
M 6 HOH   48  248 748  HOH   HOH D . 
M 6 HOH   49  249 894  HOH   HOH D . 
M 6 HOH   50  250 272  HOH   HOH D . 
M 6 HOH   51  251 610  HOH   HOH D . 
M 6 HOH   52  252 294  HOH   HOH D . 
M 6 HOH   53  253 211  HOH   HOH D . 
M 6 HOH   54  254 129  HOH   HOH D . 
M 6 HOH   55  255 140  HOH   HOH D . 
M 6 HOH   56  256 32   HOH   HOH D . 
M 6 HOH   57  257 766  HOH   HOH D . 
M 6 HOH   58  258 313  HOH   HOH D . 
M 6 HOH   59  259 22   HOH   HOH D . 
M 6 HOH   60  260 339  HOH   HOH D . 
M 6 HOH   61  261 154  HOH   HOH D . 
M 6 HOH   62  262 40   HOH   HOH D . 
M 6 HOH   63  263 685  HOH   HOH D . 
M 6 HOH   64  264 831  HOH   HOH D . 
M 6 HOH   65  265 404  HOH   HOH D . 
M 6 HOH   66  266 207  HOH   HOH D . 
M 6 HOH   67  267 360  HOH   HOH D . 
M 6 HOH   68  268 71   HOH   HOH D . 
M 6 HOH   69  269 190  HOH   HOH D . 
M 6 HOH   70  270 382  HOH   HOH D . 
M 6 HOH   71  271 269  HOH   HOH D . 
M 6 HOH   72  272 61   HOH   HOH D . 
M 6 HOH   73  273 558  HOH   HOH D . 
M 6 HOH   74  274 137  HOH   HOH D . 
M 6 HOH   75  275 177  HOH   HOH D . 
M 6 HOH   76  276 289  HOH   HOH D . 
M 6 HOH   77  277 15   HOH   HOH D . 
M 6 HOH   78  278 26   HOH   HOH D . 
M 6 HOH   79  279 449  HOH   HOH D . 
M 6 HOH   80  280 206  HOH   HOH D . 
M 6 HOH   81  281 172  HOH   HOH D . 
M 6 HOH   82  282 69   HOH   HOH D . 
M 6 HOH   83  283 840  HOH   HOH D . 
M 6 HOH   84  284 183  HOH   HOH D . 
M 6 HOH   85  285 345  HOH   HOH D . 
M 6 HOH   86  286 328  HOH   HOH D . 
M 6 HOH   87  287 143  HOH   HOH D . 
M 6 HOH   88  288 83   HOH   HOH D . 
M 6 HOH   89  289 689  HOH   HOH D . 
M 6 HOH   90  290 938  HOH   HOH D . 
M 6 HOH   91  291 229  HOH   HOH D . 
M 6 HOH   92  292 430  HOH   HOH D . 
M 6 HOH   93  293 216  HOH   HOH D . 
M 6 HOH   94  294 1010 HOH   HOH D . 
M 6 HOH   95  295 264  HOH   HOH D . 
M 6 HOH   96  296 50   HOH   HOH D . 
M 6 HOH   97  297 539  HOH   HOH D . 
M 6 HOH   98  298 21   HOH   HOH D . 
M 6 HOH   99  299 74   HOH   HOH D . 
M 6 HOH   100 300 433  HOH   HOH D . 
M 6 HOH   101 301 655  HOH   HOH D . 
M 6 HOH   102 302 244  HOH   HOH D . 
M 6 HOH   103 303 235  HOH   HOH D . 
M 6 HOH   104 304 246  HOH   HOH D . 
M 6 HOH   105 305 740  HOH   HOH D . 
M 6 HOH   106 306 375  HOH   HOH D . 
M 6 HOH   107 307 326  HOH   HOH D . 
M 6 HOH   108 308 86   HOH   HOH D . 
M 6 HOH   109 309 324  HOH   HOH D . 
M 6 HOH   110 310 1013 HOH   HOH D . 
M 6 HOH   111 311 468  HOH   HOH D . 
M 6 HOH   112 312 567  HOH   HOH D . 
M 6 HOH   113 313 361  HOH   HOH D . 
M 6 HOH   114 314 344  HOH   HOH D . 
M 6 HOH   115 315 442  HOH   HOH D . 
M 6 HOH   116 316 598  HOH   HOH D . 
M 6 HOH   117 317 149  HOH   HOH D . 
M 6 HOH   118 318 145  HOH   HOH D . 
M 6 HOH   119 319 480  HOH   HOH D . 
M 6 HOH   120 320 14   HOH   HOH D . 
M 6 HOH   121 321 288  HOH   HOH D . 
M 6 HOH   122 322 822  HOH   HOH D . 
M 6 HOH   123 323 510  HOH   HOH D . 
M 6 HOH   124 324 255  HOH   HOH D . 
M 6 HOH   125 325 100  HOH   HOH D . 
M 6 HOH   126 326 188  HOH   HOH D . 
M 6 HOH   127 327 241  HOH   HOH D . 
M 6 HOH   128 328 721  HOH   HOH D . 
M 6 HOH   129 329 259  HOH   HOH D . 
M 6 HOH   130 330 416  HOH   HOH D . 
M 6 HOH   131 331 257  HOH   HOH D . 
M 6 HOH   132 332 274  HOH   HOH D . 
M 6 HOH   133 333 105  HOH   HOH D . 
M 6 HOH   134 334 131  HOH   HOH D . 
M 6 HOH   135 335 683  HOH   HOH D . 
M 6 HOH   136 336 378  HOH   HOH D . 
M 6 HOH   137 337 535  HOH   HOH D . 
M 6 HOH   138 338 857  HOH   HOH D . 
M 6 HOH   139 339 102  HOH   HOH D . 
M 6 HOH   140 340 336  HOH   HOH D . 
M 6 HOH   141 341 150  HOH   HOH D . 
M 6 HOH   142 342 366  HOH   HOH D . 
M 6 HOH   143 343 478  HOH   HOH D . 
M 6 HOH   144 344 713  HOH   HOH D . 
M 6 HOH   145 345 726  HOH   HOH D . 
M 6 HOH   146 346 303  HOH   HOH D . 
M 6 HOH   147 347 195  HOH   HOH D . 
M 6 HOH   148 348 447  HOH   HOH D . 
M 6 HOH   149 349 215  HOH   HOH D . 
M 6 HOH   150 350 687  HOH   HOH D . 
M 6 HOH   151 351 886  HOH   HOH D . 
M 6 HOH   152 352 1014 HOH   HOH D . 
M 6 HOH   153 353 127  HOH   HOH D . 
M 6 HOH   154 354 688  HOH   HOH D . 
M 6 HOH   155 355 782  HOH   HOH D . 
M 6 HOH   156 356 845  HOH   HOH D . 
M 6 HOH   157 357 139  HOH   HOH D . 
M 6 HOH   158 358 795  HOH   HOH D . 
M 6 HOH   159 359 56   HOH   HOH D . 
M 6 HOH   160 360 925  HOH   HOH D . 
M 6 HOH   161 361 343  HOH   HOH D . 
M 6 HOH   162 362 934  HOH   HOH D . 
M 6 HOH   163 363 1011 HOH   HOH D . 
M 6 HOH   164 364 476  HOH   HOH D . 
M 6 HOH   165 365 661  HOH   HOH D . 
M 6 HOH   166 366 500  HOH   HOH D . 
M 6 HOH   167 367 549  HOH   HOH D . 
M 6 HOH   168 368 982  HOH   HOH D . 
M 6 HOH   169 369 432  HOH   HOH D . 
M 6 HOH   170 370 531  HOH   HOH D . 
M 6 HOH   171 371 727  HOH   HOH D . 
M 6 HOH   172 372 804  HOH   HOH D . 
M 6 HOH   173 373 413  HOH   HOH D . 
M 6 HOH   174 374 123  HOH   HOH D . 
M 6 HOH   175 375 1017 HOH   HOH D . 
M 6 HOH   176 376 637  HOH   HOH D . 
M 6 HOH   177 377 457  HOH   HOH D . 
M 6 HOH   178 378 505  HOH   HOH D . 
M 6 HOH   179 379 164  HOH   HOH D . 
M 6 HOH   180 380 279  HOH   HOH D . 
M 6 HOH   181 381 583  HOH   HOH D . 
M 6 HOH   182 382 659  HOH   HOH D . 
M 6 HOH   183 383 1016 HOH   HOH D . 
M 6 HOH   184 384 677  HOH   HOH D . 
M 6 HOH   185 385 514  HOH   HOH D . 
M 6 HOH   186 386 736  HOH   HOH D . 
M 6 HOH   187 387 319  HOH   HOH D . 
M 6 HOH   188 388 820  HOH   HOH D . 
M 6 HOH   189 389 1026 HOH   HOH D . 
M 6 HOH   190 390 591  HOH   HOH D . 
M 6 HOH   191 391 918  HOH   HOH D . 
M 6 HOH   192 392 284  HOH   HOH D . 
M 6 HOH   193 393 729  HOH   HOH D . 
M 6 HOH   194 394 97   HOH   HOH D . 
M 6 HOH   195 395 780  HOH   HOH D . 
M 6 HOH   196 396 754  HOH   HOH D . 
M 6 HOH   197 397 781  HOH   HOH D . 
M 6 HOH   198 398 769  HOH   HOH D . 
M 6 HOH   199 399 590  HOH   HOH D . 
M 6 HOH   200 400 843  HOH   HOH D . 
M 6 HOH   201 401 972  HOH   HOH D . 
M 6 HOH   202 402 827  HOH   HOH D . 
M 6 HOH   203 403 639  HOH   HOH D . 
M 6 HOH   204 404 545  HOH   HOH D . 
M 6 HOH   205 405 937  HOH   HOH D . 
M 6 HOH   206 406 852  HOH   HOH D . 
M 6 HOH   207 407 225  HOH   HOH D . 
M 6 HOH   208 408 859  HOH   HOH D . 
M 6 HOH   209 409 66   HOH   HOH D . 
M 6 HOH   210 410 967  HOH   HOH D . 
M 6 HOH   211 411 528  HOH   HOH D . 
M 6 HOH   212 412 624  HOH   HOH D . 
M 6 HOH   213 413 202  HOH   HOH D . 
M 6 HOH   214 414 247  HOH   HOH D . 
M 6 HOH   215 415 916  HOH   HOH D . 
M 6 HOH   216 416 724  HOH   HOH D . 
M 6 HOH   217 417 883  HOH   HOH D . 
M 6 HOH   218 418 703  HOH   HOH D . 
M 6 HOH   219 419 862  HOH   HOH D . 
M 6 HOH   220 420 577  HOH   HOH D . 
M 6 HOH   221 421 788  HOH   HOH D . 
M 6 HOH   222 422 1012 HOH   HOH D . 
M 6 HOH   223 423 849  HOH   HOH D . 
M 6 HOH   224 424 818  HOH   HOH D . 
M 6 HOH   225 425 527  HOH   HOH D . 
M 6 HOH   226 426 961  HOH   HOH D . 
M 6 HOH   227 427 761  HOH   HOH D . 
M 6 HOH   228 428 237  HOH   HOH D . 
M 6 HOH   229 429 626  HOH   HOH D . 
M 6 HOH   230 430 387  HOH   HOH D . 
M 6 HOH   231 431 940  HOH   HOH D . 
M 6 HOH   232 432 671  HOH   HOH D . 
M 6 HOH   233 433 823  HOH   HOH D . 
M 6 HOH   234 434 757  HOH   HOH D . 
M 6 HOH   235 435 787  HOH   HOH D . 
M 6 HOH   236 436 648  HOH   HOH D . 
M 6 HOH   237 437 837  HOH   HOH D . 
M 6 HOH   238 438 455  HOH   HOH D . 
M 6 HOH   239 439 756  HOH   HOH D . 
N 6 HOH   1   201 681  HOH   HOH C . 
N 6 HOH   2   202 1032 HOH   HOH C . 
N 6 HOH   3   203 633  HOH   HOH C . 
N 6 HOH   4   204 693  HOH   HOH C . 
N 6 HOH   5   205 876  HOH   HOH C . 
N 6 HOH   6   206 672  HOH   HOH C . 
N 6 HOH   7   207 200  HOH   HOH C . 
N 6 HOH   8   208 508  HOH   HOH C . 
N 6 HOH   9   209 797  HOH   HOH C . 
N 6 HOH   10  210 218  HOH   HOH C . 
N 6 HOH   11  211 939  HOH   HOH C . 
N 6 HOH   12  212 356  HOH   HOH C . 
N 6 HOH   13  213 547  HOH   HOH C . 
N 6 HOH   14  214 470  HOH   HOH C . 
N 6 HOH   15  215 617  HOH   HOH C . 
N 6 HOH   16  216 924  HOH   HOH C . 
N 6 HOH   17  217 483  HOH   HOH C . 
N 6 HOH   18  218 396  HOH   HOH C . 
N 6 HOH   19  219 338  HOH   HOH C . 
N 6 HOH   20  220 453  HOH   HOH C . 
N 6 HOH   21  221 594  HOH   HOH C . 
N 6 HOH   22  222 327  HOH   HOH C . 
N 6 HOH   23  223 393  HOH   HOH C . 
N 6 HOH   24  224 210  HOH   HOH C . 
N 6 HOH   25  225 16   HOH   HOH C . 
N 6 HOH   26  226 13   HOH   HOH C . 
N 6 HOH   27  227 446  HOH   HOH C . 
N 6 HOH   28  228 507  HOH   HOH C . 
N 6 HOH   29  229 236  HOH   HOH C . 
N 6 HOH   30  230 159  HOH   HOH C . 
N 6 HOH   31  231 395  HOH   HOH C . 
N 6 HOH   32  232 126  HOH   HOH C . 
N 6 HOH   33  233 77   HOH   HOH C . 
N 6 HOH   34  234 256  HOH   HOH C . 
N 6 HOH   35  235 5    HOH   HOH C . 
N 6 HOH   36  236 548  HOH   HOH C . 
N 6 HOH   37  237 268  HOH   HOH C . 
N 6 HOH   38  238 471  HOH   HOH C . 
N 6 HOH   39  239 73   HOH   HOH C . 
N 6 HOH   40  240 9    HOH   HOH C . 
N 6 HOH   41  241 25   HOH   HOH C . 
N 6 HOH   42  242 250  HOH   HOH C . 
N 6 HOH   43  243 37   HOH   HOH C . 
N 6 HOH   44  244 355  HOH   HOH C . 
N 6 HOH   45  245 125  HOH   HOH C . 
N 6 HOH   46  246 260  HOH   HOH C . 
N 6 HOH   47  247 54   HOH   HOH C . 
N 6 HOH   48  248 82   HOH   HOH C . 
N 6 HOH   49  249 376  HOH   HOH C . 
N 6 HOH   50  250 587  HOH   HOH C . 
N 6 HOH   51  251 80   HOH   HOH C . 
N 6 HOH   52  252 796  HOH   HOH C . 
N 6 HOH   53  253 593  HOH   HOH C . 
N 6 HOH   54  254 249  HOH   HOH C . 
N 6 HOH   55  255 536  HOH   HOH C . 
N 6 HOH   56  256 607  HOH   HOH C . 
N 6 HOH   57  257 180  HOH   HOH C . 
N 6 HOH   58  258 305  HOH   HOH C . 
N 6 HOH   59  259 43   HOH   HOH C . 
N 6 HOH   60  260 88   HOH   HOH C . 
N 6 HOH   61  261 111  HOH   HOH C . 
N 6 HOH   62  262 656  HOH   HOH C . 
N 6 HOH   63  263 286  HOH   HOH C . 
N 6 HOH   64  264 582  HOH   HOH C . 
N 6 HOH   65  265 146  HOH   HOH C . 
N 6 HOH   66  266 563  HOH   HOH C . 
N 6 HOH   67  267 99   HOH   HOH C . 
N 6 HOH   68  268 31   HOH   HOH C . 
N 6 HOH   69  269 253  HOH   HOH C . 
N 6 HOH   70  270 311  HOH   HOH C . 
N 6 HOH   71  271 23   HOH   HOH C . 
N 6 HOH   72  272 46   HOH   HOH C . 
N 6 HOH   73  273 418  HOH   HOH C . 
N 6 HOH   74  274 38   HOH   HOH C . 
N 6 HOH   75  275 334  HOH   HOH C . 
N 6 HOH   76  276 475  HOH   HOH C . 
N 6 HOH   77  277 158  HOH   HOH C . 
N 6 HOH   78  278 690  HOH   HOH C . 
N 6 HOH   79  279 486  HOH   HOH C . 
N 6 HOH   80  280 377  HOH   HOH C . 
N 6 HOH   81  281 676  HOH   HOH C . 
N 6 HOH   82  282 561  HOH   HOH C . 
N 6 HOH   83  283 34   HOH   HOH C . 
N 6 HOH   84  284 1022 HOH   HOH C . 
N 6 HOH   85  285 6    HOH   HOH C . 
N 6 HOH   86  286 307  HOH   HOH C . 
N 6 HOH   87  287 153  HOH   HOH C . 
N 6 HOH   88  288 760  HOH   HOH C . 
N 6 HOH   89  289 424  HOH   HOH C . 
N 6 HOH   90  290 658  HOH   HOH C . 
N 6 HOH   91  291 306  HOH   HOH C . 
N 6 HOH   92  292 165  HOH   HOH C . 
N 6 HOH   93  293 955  HOH   HOH C . 
N 6 HOH   94  294 144  HOH   HOH C . 
N 6 HOH   95  295 472  HOH   HOH C . 
N 6 HOH   96  296 19   HOH   HOH C . 
N 6 HOH   97  297 698  HOH   HOH C . 
N 6 HOH   98  298 337  HOH   HOH C . 
N 6 HOH   99  299 691  HOH   HOH C . 
N 6 HOH   100 300 323  HOH   HOH C . 
N 6 HOH   101 301 526  HOH   HOH C . 
N 6 HOH   102 302 496  HOH   HOH C . 
N 6 HOH   103 303 173  HOH   HOH C . 
N 6 HOH   104 304 136  HOH   HOH C . 
N 6 HOH   105 305 18   HOH   HOH C . 
N 6 HOH   106 306 742  HOH   HOH C . 
N 6 HOH   107 307 388  HOH   HOH C . 
N 6 HOH   108 308 629  HOH   HOH C . 
N 6 HOH   109 309 494  HOH   HOH C . 
N 6 HOH   110 310 79   HOH   HOH C . 
N 6 HOH   111 311 1003 HOH   HOH C . 
N 6 HOH   112 312 346  HOH   HOH C . 
N 6 HOH   113 313 461  HOH   HOH C . 
N 6 HOH   114 314 394  HOH   HOH C . 
N 6 HOH   115 315 166  HOH   HOH C . 
N 6 HOH   116 316 699  HOH   HOH C . 
N 6 HOH   117 317 203  HOH   HOH C . 
N 6 HOH   118 318 78   HOH   HOH C . 
N 6 HOH   119 319 230  HOH   HOH C . 
N 6 HOH   120 320 122  HOH   HOH C . 
N 6 HOH   121 321 20   HOH   HOH C . 
N 6 HOH   122 322 47   HOH   HOH C . 
N 6 HOH   123 323 953  HOH   HOH C . 
N 6 HOH   124 324 435  HOH   HOH C . 
N 6 HOH   125 325 618  HOH   HOH C . 
N 6 HOH   126 326 367  HOH   HOH C . 
N 6 HOH   127 327 315  HOH   HOH C . 
N 6 HOH   128 328 278  HOH   HOH C . 
N 6 HOH   129 329 234  HOH   HOH C . 
N 6 HOH   130 330 482  HOH   HOH C . 
N 6 HOH   131 331 521  HOH   HOH C . 
N 6 HOH   132 332 258  HOH   HOH C . 
N 6 HOH   133 333 654  HOH   HOH C . 
N 6 HOH   134 334 463  HOH   HOH C . 
N 6 HOH   135 335 873  HOH   HOH C . 
N 6 HOH   136 336 379  HOH   HOH C . 
N 6 HOH   137 337 409  HOH   HOH C . 
N 6 HOH   138 338 963  HOH   HOH C . 
N 6 HOH   139 339 697  HOH   HOH C . 
N 6 HOH   140 340 275  HOH   HOH C . 
N 6 HOH   141 341 407  HOH   HOH C . 
N 6 HOH   142 342 58   HOH   HOH C . 
N 6 HOH   143 343 209  HOH   HOH C . 
N 6 HOH   144 344 1025 HOH   HOH C . 
N 6 HOH   145 345 906  HOH   HOH C . 
N 6 HOH   146 346 151  HOH   HOH C . 
N 6 HOH   147 347 317  HOH   HOH C . 
N 6 HOH   148 348 895  HOH   HOH C . 
N 6 HOH   149 349 358  HOH   HOH C . 
N 6 HOH   150 350 641  HOH   HOH C . 
N 6 HOH   151 351 117  HOH   HOH C . 
N 6 HOH   152 352 92   HOH   HOH C . 
N 6 HOH   153 353 403  HOH   HOH C . 
N 6 HOH   154 354 515  HOH   HOH C . 
N 6 HOH   155 355 276  HOH   HOH C . 
N 6 HOH   156 356 765  HOH   HOH C . 
N 6 HOH   157 357 63   HOH   HOH C . 
N 6 HOH   158 358 273  HOH   HOH C . 
N 6 HOH   159 359 391  HOH   HOH C . 
N 6 HOH   160 360 872  HOH   HOH C . 
N 6 HOH   161 361 680  HOH   HOH C . 
N 6 HOH   162 362 660  HOH   HOH C . 
N 6 HOH   163 363 566  HOH   HOH C . 
N 6 HOH   164 364 768  HOH   HOH C . 
N 6 HOH   165 365 856  HOH   HOH C . 
N 6 HOH   166 366 1024 HOH   HOH C . 
N 6 HOH   167 367 1019 HOH   HOH C . 
N 6 HOH   168 368 730  HOH   HOH C . 
N 6 HOH   169 369 824  HOH   HOH C . 
N 6 HOH   170 370 731  HOH   HOH C . 
N 6 HOH   171 371 434  HOH   HOH C . 
N 6 HOH   172 372 775  HOH   HOH C . 
N 6 HOH   173 373 829  HOH   HOH C . 
N 6 HOH   174 374 98   HOH   HOH C . 
N 6 HOH   175 375 546  HOH   HOH C . 
N 6 HOH   176 376 735  HOH   HOH C . 
N 6 HOH   177 377 1023 HOH   HOH C . 
N 6 HOH   178 378 869  HOH   HOH C . 
N 6 HOH   179 379 597  HOH   HOH C . 
N 6 HOH   180 380 980  HOH   HOH C . 
N 6 HOH   181 381 716  HOH   HOH C . 
N 6 HOH   182 382 628  HOH   HOH C . 
N 6 HOH   183 383 927  HOH   HOH C . 
N 6 HOH   184 384 667  HOH   HOH C . 
N 6 HOH   185 385 135  HOH   HOH C . 
N 6 HOH   186 386 467  HOH   HOH C . 
N 6 HOH   187 387 979  HOH   HOH C . 
N 6 HOH   188 388 371  HOH   HOH C . 
N 6 HOH   189 389 1021 HOH   HOH C . 
N 6 HOH   190 390 372  HOH   HOH C . 
N 6 HOH   191 391 673  HOH   HOH C . 
N 6 HOH   192 392 160  HOH   HOH C . 
N 6 HOH   193 393 949  HOH   HOH C . 
N 6 HOH   194 394 714  HOH   HOH C . 
N 6 HOH   195 395 914  HOH   HOH C . 
N 6 HOH   196 396 779  HOH   HOH C . 
N 6 HOH   197 397 891  HOH   HOH C . 
N 6 HOH   198 398 513  HOH   HOH C . 
N 6 HOH   199 399 874  HOH   HOH C . 
N 6 HOH   200 400 892  HOH   HOH C . 
N 6 HOH   201 401 488  HOH   HOH C . 
N 6 HOH   202 402 314  HOH   HOH C . 
N 6 HOH   203 403 522  HOH   HOH C . 
N 6 HOH   204 404 509  HOH   HOH C . 
N 6 HOH   205 405 340  HOH   HOH C . 
N 6 HOH   206 406 652  HOH   HOH C . 
N 6 HOH   207 407 495  HOH   HOH C . 
N 6 HOH   208 408 349  HOH   HOH C . 
N 6 HOH   209 409 643  HOH   HOH C . 
N 6 HOH   210 410 920  HOH   HOH C . 
N 6 HOH   211 411 512  HOH   HOH C . 
N 6 HOH   212 412 908  HOH   HOH C . 
N 6 HOH   213 413 613  HOH   HOH C . 
N 6 HOH   214 414 749  HOH   HOH C . 
N 6 HOH   215 415 503  HOH   HOH C . 
N 6 HOH   216 416 439  HOH   HOH C . 
N 6 HOH   217 417 605  HOH   HOH C . 
N 6 HOH   218 418 1018 HOH   HOH C . 
N 6 HOH   219 419 807  HOH   HOH C . 
N 6 HOH   220 420 182  HOH   HOH C . 
# 
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                   90.860 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BFV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.040 
_cell.length_a_esd                 ? 
_cell.length_b                     105.180 
_cell.length_b_esd                 ? 
_cell.length_c                     66.220 
_cell.length_c_esd                 ? 
_cell.volume                       334561.850 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_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                         9BFV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BFV 
_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             2.23 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.81 
_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    '25% PEG 3350, 0.1M Bis Tris, pH 5.5, 150 mM NaCl' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-03-22 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   .953 
_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        .953 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          15.68 
_reflns.entry_id                                       9BFV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.20 
_reflns.d_resolution_low                               48.03 
_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                                     197918 
_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                           96.79 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          9.75 
_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                                .06487 
_reflns.pdbx_Rpim_I_all                                .03253 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              .05589 
_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                                    1.20 
_reflns_shell.d_res_low                                     1.243 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           .9 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             18877 
_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                               3.7 
_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                               1.601 
_reflns_shell.pdbx_Rpim_I_all                               .812 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .268 
_reflns_shell.pdbx_CC_star                                  .65 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          92.57 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.374 
_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                               24.57 
_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                                 9BFV 
_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                            1.20 
_refine.ls_d_res_low                             48.03 
_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                     197906 
_refine.ls_number_reflns_R_free                  9854 
_refine.ls_number_reflns_R_work                  188052 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.79 
_refine.ls_percent_reflns_R_free                 4.98 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1513 
_refine.ls_R_factor_R_free                       0.1887 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1493 
_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                          1.35 
_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                 21.0580 
_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                            0.1718 
_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                       1.20 
_refine_hist.d_res_low                        48.03 
_refine_hist.number_atoms_solvent             906 
_refine_hist.number_atoms_total               6354 
_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        5240 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         208 
_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' ? 0.0066  ? 5675 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9935  ? 7694 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0820  ? 821  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0077  ? 996  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.0631 ? 2147 ? 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' 1.20 1.21  . . 328 5823 91.02 . . . . 0.3409 . . . . . . . . . . . 0.3649 
'X-RAY DIFFRACTION' 1.21 1.23  . . 307 6021 92.62 . . . . 0.3177 . . . . . . . . . . . 0.3539 
'X-RAY DIFFRACTION' 1.23 1.24  . . 298 6094 94.08 . . . . 0.3056 . . . . . . . . . . . 0.3294 
'X-RAY DIFFRACTION' 1.24 1.26  . . 291 6107 94.74 . . . . 0.2973 . . . . . . . . . . . 0.3345 
'X-RAY DIFFRACTION' 1.26 1.28  . . 342 6163 95.16 . . . . 0.2678 . . . . . . . . . . . 0.3271 
'X-RAY DIFFRACTION' 1.28 1.29  . . 333 6166 95.76 . . . . 0.2508 . . . . . . . . . . . 0.2966 
'X-RAY DIFFRACTION' 1.29 1.31  . . 299 6214 95.71 . . . . 0.2488 . . . . . . . . . . . 0.3100 
'X-RAY DIFFRACTION' 1.31 1.33  . . 341 6247 96.20 . . . . 0.2198 . . . . . . . . . . . 0.2772 
'X-RAY DIFFRACTION' 1.33 1.35  . . 363 6183 96.51 . . . . 0.2109 . . . . . . . . . . . 0.2549 
'X-RAY DIFFRACTION' 1.35 1.37  . . 344 6224 96.38 . . . . 0.2131 . . . . . . . . . . . 0.2636 
'X-RAY DIFFRACTION' 1.37 1.40  . . 307 6251 96.58 . . . . 0.1981 . . . . . . . . . . . 0.2539 
'X-RAY DIFFRACTION' 1.40 1.42  . . 335 6240 96.83 . . . . 0.1899 . . . . . . . . . . . 0.2404 
'X-RAY DIFFRACTION' 1.42 1.45  . . 302 6294 96.80 . . . . 0.1860 . . . . . . . . . . . 0.2419 
'X-RAY DIFFRACTION' 1.45 1.48  . . 287 6299 97.08 . . . . 0.1815 . . . . . . . . . . . 0.2343 
'X-RAY DIFFRACTION' 1.48 1.51  . . 341 6260 97.43 . . . . 0.1687 . . . . . . . . . . . 0.2184 
'X-RAY DIFFRACTION' 1.51 1.55  . . 319 6354 97.43 . . . . 0.1567 . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 1.55 1.59  . . 338 6281 97.54 . . . . 0.1498 . . . . . . . . . . . 0.2106 
'X-RAY DIFFRACTION' 1.59 1.63  . . 341 6305 97.38 . . . . 0.1436 . . . . . . . . . . . 0.1891 
'X-RAY DIFFRACTION' 1.63 1.68  . . 346 6330 98.16 . . . . 0.1360 . . . . . . . . . . . 0.1905 
'X-RAY DIFFRACTION' 1.68 1.73  . . 337 6334 97.80 . . . . 0.1334 . . . . . . . . . . . 0.1866 
'X-RAY DIFFRACTION' 1.73 1.79  . . 371 6354 98.45 . . . . 0.1340 . . . . . . . . . . . 0.1841 
'X-RAY DIFFRACTION' 1.79 1.86  . . 349 6332 98.37 . . . . 0.1405 . . . . . . . . . . . 0.1891 
'X-RAY DIFFRACTION' 1.86 1.95  . . 313 6403 98.29 . . . . 0.1340 . . . . . . . . . . . 0.1653 
'X-RAY DIFFRACTION' 1.95 2.05  . . 292 6414 98.49 . . . . 0.1350 . . . . . . . . . . . 0.1710 
'X-RAY DIFFRACTION' 2.05 2.18  . . 366 6365 98.31 . . . . 0.1350 . . . . . . . . . . . 0.1679 
'X-RAY DIFFRACTION' 2.18 2.35  . . 305 6401 98.31 . . . . 0.1328 . . . . . . . . . . . 0.1612 
'X-RAY DIFFRACTION' 2.35 2.59  . . 319 6401 98.45 . . . . 0.1426 . . . . . . . . . . . 0.1644 
'X-RAY DIFFRACTION' 2.59 2.96  . . 355 6394 98.31 . . . . 0.1476 . . . . . . . . . . . 0.2000 
'X-RAY DIFFRACTION' 2.96 3.73  . . 344 6343 97.42 . . . . 0.1314 . . . . . . . . . . . 0.1707 
'X-RAY DIFFRACTION' 3.73 48.03 . . 341 6455 98.04 . . . . 0.1287 . . . . . . . . . . . 0.1610 
# 
_struct.entry_id                     9BFV 
_struct.title                        'Tri-complex of Compound-23, KRAS G12C, 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        9BFV 
_struct_keywords.text            
'inhibitor, complex, small GTPase, cancer, tricomplex, SIGNALING PROTEIN-INHIBITOR complex, SIGNALING PROTEIN' 
_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 5 ? 
H N N 3 ? 
I N N 4 ? 
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 9BFV A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 1 9BFV B 2 ? 170 ? P01116 1 ? 169 ? 1 169 
3 2 9BFV D 2 ? 166 ? P62937 1 ? 165 ? 1 165 
4 2 9BFV C 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 9BFV SER A 1  ? UNP P01116 ?   ?  'expression tag'      0  1 
1 9BFV CYS A 13 ? UNP P01116 GLY 12 'engineered mutation' 12 2 
2 9BFV SER B 1  ? UNP P01116 ?   ?  'expression tag'      0  3 
2 9BFV CYS B 13 ? UNP P01116 GLY 12 'engineered mutation' 12 4 
3 9BFV SER D 1  ? UNP P62937 ?   ?  'expression tag'      0  5 
4 9BFV SER C 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,C,E,F,G,K,M 
2 1 B,D,H,I,J,L,N 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? ASN A 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 TYR A 65  ? GLY A 76  ? TYR A 64  GLY A 75  1 ? 12 
HELX_P HELX_P3  AA3 ASN A 87  ? ASP A 106 ? ASN A 86  ASP A 105 1 ? 20 
HELX_P HELX_P4  AA4 ASP A 127 ? GLY A 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P5  AA5 GLY A 152 ? LYS A 170 ? GLY A 151 LYS A 169 1 ? 19 
HELX_P HELX_P6  AA6 GLY B 16  ? ASN B 27  ? GLY B 15  ASN B 26  1 ? 12 
HELX_P HELX_P7  AA7 TYR B 65  ? GLY B 76  ? TYR B 64  GLY B 75  1 ? 12 
HELX_P HELX_P8  AA8 ASN B 87  ? ASP B 93  ? ASN B 86  ASP B 92  1 ? 7  
HELX_P HELX_P9  AA9 ASP B 93  ? ASP B 106 ? ASP B 92  ASP B 105 1 ? 14 
HELX_P HELX_P10 AB1 ASP B 127 ? GLY B 139 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P11 AB2 GLY B 152 ? LYS B 170 ? GLY B 151 LYS B 169 1 ? 19 
HELX_P HELX_P12 AB3 VAL C 30  ? GLY C 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P13 AB4 THR C 120 ? ASP C 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P14 AB5 GLY C 136 ? ARG C 145 ? GLY D 135 ARG D 144 1 ? 10 
HELX_P HELX_P15 AB6 VAL D 30  ? GLY D 43  ? VAL C 29  GLY C 42  1 ? 14 
HELX_P HELX_P16 AB7 THR D 120 ? ASP D 124 ? THR C 119 ASP C 123 5 ? 5  
HELX_P HELX_P17 AB8 GLY D 136 ? ARG D 145 ? GLY C 135 ARG C 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 
covale1  covale none ? A CYS 13 SG  ? ? ? 1_555 F A1AOV . C16 ? ? A CYS 12  A A1AOV 202 1_555 ? ? ? ? ? ? ? 1.671 ? ? 
covale2  covale none ? B CYS 13 SG  ? ? ? 1_555 I A1AOV . C16 ? ? B CYS 12  B A1AOV 202 1_555 ? ? ? ? ? ? ? 1.670 ? ? 
metalc1  metalc ?    ? A SER 18 OG  ? ? ? 1_555 G MG    . MG  ? ? A SER 17  A MG    203 1_555 ? ? ? ? ? ? ? 2.080 ? ? 
metalc2  metalc ?    ? A THR 36 OG1 ? ? ? 1_555 G MG    . MG  ? ? A THR 35  A MG    203 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc3  metalc ?    ? E GNP .  O1G ? ? ? 1_555 G MG    . MG  ? ? A GNP 201 A MG    203 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc4  metalc ?    ? E GNP .  O1B ? ? ? 1_555 G MG    . MG  ? ? A GNP 201 A MG    203 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc5  metalc ?    ? G MG  .  MG  ? ? ? 1_555 K HOH   . O   ? ? A MG  203 A HOH   314 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc6  metalc ?    ? G MG  .  MG  ? ? ? 1_555 K HOH   . O   ? ? A MG  203 A HOH   350 1_555 ? ? ? ? ? ? ? 2.078 ? ? 
metalc7  metalc ?    ? B SER 18 OG  ? ? ? 1_555 J MG    . MG  ? ? B SER 17  B MG    203 1_555 ? ? ? ? ? ? ? 2.053 ? ? 
metalc8  metalc ?    ? B THR 36 OG1 ? ? ? 1_555 J MG    . MG  ? ? B THR 35  B MG    203 1_555 ? ? ? ? ? ? ? 2.082 ? ? 
metalc9  metalc ?    ? H GNP .  O2G ? ? ? 1_555 J MG    . MG  ? ? B GNP 201 B MG    203 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
metalc10 metalc ?    ? H GNP .  O1B ? ? ? 1_555 J MG    . MG  ? ? B GNP 201 B MG    203 1_555 ? ? ? ? ? ? ? 2.139 ? ? 
metalc11 metalc ?    ? J MG  .  MG  ? ? ? 1_555 L HOH   . O   ? ? B MG  203 B HOH   313 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc12 metalc ?    ? J MG  .  MG  ? ? ? 1_555 L HOH   . O   ? ? B MG  203 B HOH   360 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 OG1 ? A THR 36 ? A THR 35  ? 1_555 84.2  ? 
2  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 171.1 ? 
3  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 89.0  ? 
4  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 92.0  ? 
5  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 175.3 ? 
6  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 95.0  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 314 ? 1_555 83.0  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 314 ? 1_555 90.2  ? 
9  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 314 ? 1_555 91.5  ? 
10 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 314 ? 1_555 92.1  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 91.7  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 89.5  ? 
13 O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 93.8  ? 
14 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 87.8  ? 
15 O   ? K HOH .  ? A HOH 314 ? 1_555 MG ? G MG . ? A MG 203 ? 1_555 O   ? K HOH .  ? A HOH 350 ? 1_555 174.7 ? 
16 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 OG1 ? B THR 36 ? B THR 35  ? 1_555 84.7  ? 
17 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2G ? H GNP .  ? B GNP 201 ? 1_555 172.5 ? 
18 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O2G ? H GNP .  ? B GNP 201 ? 1_555 91.5  ? 
19 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O1B ? H GNP .  ? B GNP 201 ? 1_555 91.0  ? 
20 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O1B ? H GNP .  ? B GNP 201 ? 1_555 174.1 ? 
21 O2G ? H GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O1B ? H GNP .  ? B GNP 201 ? 1_555 93.2  ? 
22 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 313 ? 1_555 82.2  ? 
23 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 313 ? 1_555 90.5  ? 
24 O2G ? H GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 313 ? 1_555 91.4  ? 
25 O1B ? H GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 313 ? 1_555 93.0  ? 
26 OG  ? B SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 360 ? 1_555 91.7  ? 
27 OG1 ? B THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 360 ? 1_555 88.0  ? 
28 O2G ? H GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 360 ? 1_555 94.6  ? 
29 O1B ? H GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 360 ? 1_555 88.0  ? 
30 O   ? L HOH .  ? B HOH 313 ? 1_555 MG ? J MG . ? B MG 203 ? 1_555 O   ? L HOH .  ? B HOH 360 ? 1_555 173.8 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1AOV F . ? CYS A 13 ? A1AOV A 202 ? 1_555 CYS A 12 ? 1_555 C16 SG CYS 1 A1AOV None 'Covalent chemical modification' 
2 A1AOV I . ? CYS B 13 ? A1AOV B 202 ? 1_555 CYS B 12 ? 1_555 C16 SG CYS 1 A1AOV None 'Covalent chemical modification' 
# 
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 MET A 2   ? GLY A 11  ? MET A 1   GLY A 10  
AA1 4 GLY A 78  ? ALA A 84  ? GLY A 77  ALA A 83  
AA1 5 MET A 112 ? ASN A 117 ? MET A 111 ASN A 116 
AA1 6 PHE A 142 ? GLU A 144 ? PHE A 141 GLU A 143 
AA2 1 GLU B 38  ? ILE B 47  ? GLU B 37  ILE B 46  
AA2 2 GLU B 50  ? THR B 59  ? GLU B 49  THR B 58  
AA2 3 THR B 3   ? GLY B 11  ? THR B 2   GLY B 10  
AA2 4 GLY B 78  ? ALA B 84  ? GLY B 77  ALA B 83  
AA2 5 MET B 112 ? ASN B 117 ? MET B 111 ASN B 116 
AA2 6 PHE B 142 ? GLU B 144 ? PHE B 141 GLU B 143 
AA3 1 ARG C 56  ? ILE C 58  ? ARG D 55  ILE D 57  
AA3 2 MET C 62  ? GLY C 65  ? MET D 61  GLY D 64  
AA3 3 PHE C 113 ? CYS C 116 ? PHE D 112 CYS D 115 
AA3 4 ILE C 98  ? MET C 101 ? ILE D 97  MET D 100 
AA3 5 VAL C 129 ? GLU C 135 ? VAL D 128 GLU D 134 
AA3 6 GLU C 16  ? LEU C 25  ? GLU D 15  LEU D 24  
AA3 7 THR C 6   ? VAL C 13  ? THR D 5   VAL D 12  
AA3 8 ILE C 157 ? LEU C 165 ? ILE D 156 LEU D 164 
AA4 1 ARG D 56  ? ILE D 58  ? ARG C 55  ILE C 57  
AA4 2 MET D 62  ? GLY D 65  ? MET C 61  GLY C 64  
AA4 3 PHE D 113 ? CYS D 116 ? PHE C 112 CYS C 115 
AA4 4 ILE D 98  ? MET D 101 ? ILE C 97  MET C 100 
AA4 5 VAL D 129 ? VAL D 133 ? VAL C 128 VAL C 132 
AA4 6 GLU D 16  ? LEU D 25  ? GLU C 15  LEU C 24  
AA4 7 THR D 6   ? VAL D 13  ? THR C 5   VAL C 12  
AA4 8 ILE D 157 ? LEU D 165 ? ILE C 156 LEU C 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 VAL A 45  ? N VAL A 44  O CYS A 52  ? O CYS A 51  
AA1 2 3 O ASP A 55  ? O ASP A 54  N LEU A 7   ? N LEU A 6   
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 VAL B 82  ? O VAL B 81  
AA2 4 5 N PHE B 83  ? N PHE B 82  O ASN B 117 ? O ASN B 116 
AA2 5 6 N LEU B 114 ? N LEU B 113 O ILE B 143 ? O ILE B 142 
AA3 1 2 N ARG C 56  ? N ARG D 55  O GLN C 64  ? O GLN D 63  
AA3 2 3 N CYS C 63  ? N CYS D 62  O ILE C 115 ? O ILE D 114 
AA3 3 4 O CYS C 116 ? O CYS D 115 N ILE C 98  ? N ILE D 97  
AA3 4 5 N LEU C 99  ? N LEU D 98  O GLY C 131 ? O GLY D 130 
AA3 5 6 O LYS C 134 ? O LYS D 133 N SER C 22  ? N SER D 21  
AA3 6 7 O LEU C 18  ? O LEU D 17  N ILE C 11  ? N ILE D 10  
AA3 7 8 N ASP C 10  ? N ASP D 9   O ASP C 161 ? O ASP D 160 
AA4 1 2 N ARG D 56  ? N ARG C 55  O GLN D 64  ? O GLN C 63  
AA4 2 3 N CYS D 63  ? N CYS C 62  O ILE D 115 ? O ILE C 114 
AA4 3 4 O CYS D 116 ? O CYS C 115 N ILE D 98  ? N ILE C 97  
AA4 4 5 N LEU D 99  ? N LEU C 98  O GLY D 131 ? O GLY C 130 
AA4 5 6 O LYS D 132 ? O LYS C 131 N GLU D 24  ? N GLU C 23  
AA4 6 7 O LEU D 18  ? O LEU C 17  N ILE D 11  ? N ILE C 10  
AA4 7 8 N ASP D 10  ? N ASP C 9   O ASP D 161 ? O ASP C 160 
# 
_pdbx_entry_details.entry_id                   9BFV 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 ILE A 36  ? ? -94.92  -64.17 
2  1 LYS A 117 ? ? 71.90   30.30  
3  1 ILE B 36  ? ? -93.50  -64.68 
4  1 GLU B 37  ? ? -170.25 136.35 
5  1 TYR B 64  ? ? 61.23   60.89  
6  1 LYS B 117 ? ? 72.40   32.46  
7  1 PHE D 60  ? ? -132.05 -70.85 
8  1 ASN D 71  ? ? -142.34 15.67  
9  1 LYS D 133 ? ? -91.40  -62.61 
10 1 PHE C 60  ? ? -129.54 -71.09 
11 1 ASN C 71  ? ? -141.37 12.86  
12 1 LYS C 133 ? ? -97.92  -70.83 
# 
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 N5 ? A A1AOV 202 ? PLANAR . 
2 1 N5 ? B A1AOV 202 ? PLANAR . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? B HOH 496 ? 6.54 . 
2 1 O ? C HOH 420 ? 5.84 . 
# 
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 D SER 0   ? C SER 1   
2 1 Y 1 D GLU 165 ? C GLU 166 
3 1 Y 1 C SER 0   ? D SER 1   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AOV C1     C  N N 1   
A1AOV C10    C  N N 2   
A1AOV C11    C  N S 3   
A1AOV C12    C  N N 4   
A1AOV C13    C  N N 5   
A1AOV C14    C  N N 6   
A1AOV C15    C  N N 7   
A1AOV C16    C  N N 8   
A1AOV C17    C  N N 9   
A1AOV C18    C  N N 10  
A1AOV C19    C  N N 11  
A1AOV C2     C  N S 12  
A1AOV C20    C  N N 13  
A1AOV C21    C  N N 14  
A1AOV C22    C  N N 15  
A1AOV C23    C  N S 16  
A1AOV C24    C  N N 17  
A1AOV C25    C  N N 18  
A1AOV C26    C  N N 19  
A1AOV C27    C  N N 20  
A1AOV C28    C  N N 21  
A1AOV C29    C  N N 22  
A1AOV C3     C  N N 23  
A1AOV C30    C  Y N 24  
A1AOV C31    C  Y N 25  
A1AOV C32    C  Y N 26  
A1AOV C33    C  Y N 27  
A1AOV C34    C  N S 28  
A1AOV C35    C  N N 29  
A1AOV C36    C  N N 30  
A1AOV C37    C  Y N 31  
A1AOV C38    C  Y N 32  
A1AOV C39    C  Y N 33  
A1AOV C4     C  N N 34  
A1AOV C40    C  N N 35  
A1AOV C41    C  N N 36  
A1AOV C42    C  Y N 37  
A1AOV C43    C  Y N 38  
A1AOV C44    C  Y N 39  
A1AOV C45    C  Y N 40  
A1AOV C46    C  Y N 41  
A1AOV C47    C  Y N 42  
A1AOV C48    C  Y N 43  
A1AOV C49    C  Y N 44  
A1AOV C5     C  N S 45  
A1AOV C50    C  Y N 46  
A1AOV C51    C  Y N 47  
A1AOV C52    C  Y N 48  
A1AOV C53    C  Y N 49  
A1AOV C54    C  N N 50  
A1AOV C55    C  N N 51  
A1AOV C56    C  N N 52  
A1AOV C6     C  N N 53  
A1AOV C7     C  N N 54  
A1AOV C8     C  N N 55  
A1AOV C9     C  N N 56  
A1AOV N1     N  N N 57  
A1AOV N2     N  N N 58  
A1AOV N3     N  N N 59  
A1AOV N4     N  N N 60  
A1AOV N5     N  N R 61  
A1AOV N6     N  N N 62  
A1AOV N7     N  Y N 63  
A1AOV N8     N  Y N 64  
A1AOV O1     O  N N 65  
A1AOV O2     O  N N 66  
A1AOV O3     O  N N 67  
A1AOV O4     O  N N 68  
A1AOV O5     O  N N 69  
A1AOV O6     O  N N 70  
A1AOV O7     O  N N 71  
A1AOV H16    H  N N 72  
A1AOV H17    H  N N 73  
A1AOV H18    H  N N 74  
A1AOV H19    H  N N 75  
A1AOV H20    H  N N 76  
A1AOV H21    H  N N 77  
A1AOV H22    H  N N 78  
A1AOV H25    H  N N 79  
A1AOV H23    H  N N 80  
A1AOV H24    H  N N 81  
A1AOV H27    H  N N 82  
A1AOV H26    H  N N 83  
A1AOV H28    H  N N 84  
A1AOV H1     H  N N 85  
A1AOV H29    H  N N 86  
A1AOV H31    H  N N 87  
A1AOV H30    H  N N 88  
A1AOV H32    H  N N 89  
A1AOV H34    H  N N 90  
A1AOV H33    H  N N 91  
A1AOV H36    H  N N 92  
A1AOV H35    H  N N 93  
A1AOV H38    H  N N 94  
A1AOV H39    H  N N 95  
A1AOV H40    H  N N 96  
A1AOV H41    H  N N 97  
A1AOV H42    H  N N 98  
A1AOV H43    H  N N 99  
A1AOV H44    H  N N 100 
A1AOV H46    H  N N 101 
A1AOV H45    H  N N 102 
A1AOV H47    H  N N 103 
A1AOV H48    H  N N 104 
A1AOV H2     H  N N 105 
A1AOV H3     H  N N 106 
A1AOV H49    H  N N 107 
A1AOV H52    H  N N 108 
A1AOV H51    H  N N 109 
A1AOV H50    H  N N 110 
A1AOV H55    H  N N 111 
A1AOV H53    H  N N 112 
A1AOV H54    H  N N 113 
A1AOV H56    H  N N 114 
A1AOV H57    H  N N 115 
A1AOV H58    H  N N 116 
A1AOV H60    H  N N 117 
A1AOV H59    H  N N 118 
A1AOV H61    H  N N 119 
A1AOV H62    H  N N 120 
A1AOV H63    H  N N 121 
A1AOV H64    H  N N 122 
A1AOV H65    H  N N 123 
A1AOV H66    H  N N 124 
A1AOV H67    H  N N 125 
A1AOV H5     H  N N 126 
A1AOV H68    H  N N 127 
A1AOV H69    H  N N 128 
A1AOV H70    H  N N 129 
A1AOV H71    H  N N 130 
A1AOV H72    H  N N 131 
A1AOV H73    H  N N 132 
A1AOV H74    H  N N 133 
A1AOV H75    H  N N 134 
A1AOV H76    H  N N 135 
A1AOV H6     H  N N 136 
A1AOV H8     H  N N 137 
A1AOV H9     H  N N 138 
A1AOV H7     H  N N 139 
A1AOV H12    H  N N 140 
A1AOV H10    H  N N 141 
A1AOV H11    H  N N 142 
A1AOV H14    H  N N 143 
A1AOV H15    H  N N 144 
A1AOV H13    H  N N 145 
A1AOV H4     H  N N 146 
A1AOV H37    H  N N 147 
ALA   N      N  N N 148 
ALA   CA     C  N S 149 
ALA   C      C  N N 150 
ALA   O      O  N N 151 
ALA   CB     C  N N 152 
ALA   OXT    O  N N 153 
ALA   H      H  N N 154 
ALA   H2     H  N N 155 
ALA   HA     H  N N 156 
ALA   HB1    H  N N 157 
ALA   HB2    H  N N 158 
ALA   HB3    H  N N 159 
ALA   HXT    H  N N 160 
ARG   N      N  N N 161 
ARG   CA     C  N S 162 
ARG   C      C  N N 163 
ARG   O      O  N N 164 
ARG   CB     C  N N 165 
ARG   CG     C  N N 166 
ARG   CD     C  N N 167 
ARG   NE     N  N N 168 
ARG   CZ     C  N N 169 
ARG   NH1    N  N N 170 
ARG   NH2    N  N N 171 
ARG   OXT    O  N N 172 
ARG   H      H  N N 173 
ARG   H2     H  N N 174 
ARG   HA     H  N N 175 
ARG   HB2    H  N N 176 
ARG   HB3    H  N N 177 
ARG   HG2    H  N N 178 
ARG   HG3    H  N N 179 
ARG   HD2    H  N N 180 
ARG   HD3    H  N N 181 
ARG   HE     H  N N 182 
ARG   HH11   H  N N 183 
ARG   HH12   H  N N 184 
ARG   HH21   H  N N 185 
ARG   HH22   H  N N 186 
ARG   HXT    H  N N 187 
ASN   N      N  N N 188 
ASN   CA     C  N S 189 
ASN   C      C  N N 190 
ASN   O      O  N N 191 
ASN   CB     C  N N 192 
ASN   CG     C  N N 193 
ASN   OD1    O  N N 194 
ASN   ND2    N  N N 195 
ASN   OXT    O  N N 196 
ASN   H      H  N N 197 
ASN   H2     H  N N 198 
ASN   HA     H  N N 199 
ASN   HB2    H  N N 200 
ASN   HB3    H  N N 201 
ASN   HD21   H  N N 202 
ASN   HD22   H  N N 203 
ASN   HXT    H  N N 204 
ASP   N      N  N N 205 
ASP   CA     C  N S 206 
ASP   C      C  N N 207 
ASP   O      O  N N 208 
ASP   CB     C  N N 209 
ASP   CG     C  N N 210 
ASP   OD1    O  N N 211 
ASP   OD2    O  N N 212 
ASP   OXT    O  N N 213 
ASP   H      H  N N 214 
ASP   H2     H  N N 215 
ASP   HA     H  N N 216 
ASP   HB2    H  N N 217 
ASP   HB3    H  N N 218 
ASP   HD2    H  N N 219 
ASP   HXT    H  N N 220 
CYS   N      N  N N 221 
CYS   CA     C  N R 222 
CYS   C      C  N N 223 
CYS   O      O  N N 224 
CYS   CB     C  N N 225 
CYS   SG     S  N N 226 
CYS   OXT    O  N N 227 
CYS   H      H  N N 228 
CYS   H2     H  N N 229 
CYS   HA     H  N N 230 
CYS   HB2    H  N N 231 
CYS   HB3    H  N N 232 
CYS   HG     H  N N 233 
CYS   HXT    H  N N 234 
GLN   N      N  N N 235 
GLN   CA     C  N S 236 
GLN   C      C  N N 237 
GLN   O      O  N N 238 
GLN   CB     C  N N 239 
GLN   CG     C  N N 240 
GLN   CD     C  N N 241 
GLN   OE1    O  N N 242 
GLN   NE2    N  N N 243 
GLN   OXT    O  N N 244 
GLN   H      H  N N 245 
GLN   H2     H  N N 246 
GLN   HA     H  N N 247 
GLN   HB2    H  N N 248 
GLN   HB3    H  N N 249 
GLN   HG2    H  N N 250 
GLN   HG3    H  N N 251 
GLN   HE21   H  N N 252 
GLN   HE22   H  N N 253 
GLN   HXT    H  N N 254 
GLU   N      N  N N 255 
GLU   CA     C  N S 256 
GLU   C      C  N N 257 
GLU   O      O  N N 258 
GLU   CB     C  N N 259 
GLU   CG     C  N N 260 
GLU   CD     C  N N 261 
GLU   OE1    O  N N 262 
GLU   OE2    O  N N 263 
GLU   OXT    O  N N 264 
GLU   H      H  N N 265 
GLU   H2     H  N N 266 
GLU   HA     H  N N 267 
GLU   HB2    H  N N 268 
GLU   HB3    H  N N 269 
GLU   HG2    H  N N 270 
GLU   HG3    H  N N 271 
GLU   HE2    H  N N 272 
GLU   HXT    H  N N 273 
GLY   N      N  N N 274 
GLY   CA     C  N N 275 
GLY   C      C  N N 276 
GLY   O      O  N N 277 
GLY   OXT    O  N N 278 
GLY   H      H  N N 279 
GLY   H2     H  N N 280 
GLY   HA2    H  N N 281 
GLY   HA3    H  N N 282 
GLY   HXT    H  N N 283 
GNP   PG     P  N N 284 
GNP   O1G    O  N N 285 
GNP   O2G    O  N N 286 
GNP   O3G    O  N N 287 
GNP   N3B    N  N N 288 
GNP   PB     P  N R 289 
GNP   O1B    O  N N 290 
GNP   O2B    O  N N 291 
GNP   O3A    O  N N 292 
GNP   PA     P  N S 293 
GNP   O1A    O  N N 294 
GNP   O2A    O  N N 295 
GNP   "O5'"  O  N N 296 
GNP   "C5'"  C  N N 297 
GNP   "C4'"  C  N R 298 
GNP   "O4'"  O  N N 299 
GNP   "C3'"  C  N S 300 
GNP   "O3'"  O  N N 301 
GNP   "C2'"  C  N R 302 
GNP   "O2'"  O  N N 303 
GNP   "C1'"  C  N R 304 
GNP   N9     N  Y N 305 
GNP   C8     C  Y N 306 
GNP   N7     N  Y N 307 
GNP   C5     C  Y N 308 
GNP   C6     C  Y N 309 
GNP   O6     O  N N 310 
GNP   N1     N  Y N 311 
GNP   C2     C  Y N 312 
GNP   N2     N  N N 313 
GNP   N3     N  Y N 314 
GNP   C4     C  Y N 315 
GNP   HOG2   H  N N 316 
GNP   HOG3   H  N N 317 
GNP   HNB3   H  N N 318 
GNP   HOB2   H  N N 319 
GNP   HOA2   H  N N 320 
GNP   "H5'2" H  N N 321 
GNP   "H5'1" H  N N 322 
GNP   "H4'"  H  N N 323 
GNP   "H3'"  H  N N 324 
GNP   "HO3'" H  N N 325 
GNP   "H2'"  H  N N 326 
GNP   "HO2'" H  N N 327 
GNP   "H1'"  H  N N 328 
GNP   H8     H  N N 329 
GNP   HN1    H  N N 330 
GNP   HN21   H  N N 331 
GNP   HN22   H  N N 332 
HIS   N      N  N N 333 
HIS   CA     C  N S 334 
HIS   C      C  N N 335 
HIS   O      O  N N 336 
HIS   CB     C  N N 337 
HIS   CG     C  Y N 338 
HIS   ND1    N  Y N 339 
HIS   CD2    C  Y N 340 
HIS   CE1    C  Y N 341 
HIS   NE2    N  Y N 342 
HIS   OXT    O  N N 343 
HIS   H      H  N N 344 
HIS   H2     H  N N 345 
HIS   HA     H  N N 346 
HIS   HB2    H  N N 347 
HIS   HB3    H  N N 348 
HIS   HD1    H  N N 349 
HIS   HD2    H  N N 350 
HIS   HE1    H  N N 351 
HIS   HE2    H  N N 352 
HIS   HXT    H  N N 353 
HOH   O      O  N N 354 
HOH   H1     H  N N 355 
HOH   H2     H  N N 356 
ILE   N      N  N N 357 
ILE   CA     C  N S 358 
ILE   C      C  N N 359 
ILE   O      O  N N 360 
ILE   CB     C  N S 361 
ILE   CG1    C  N N 362 
ILE   CG2    C  N N 363 
ILE   CD1    C  N N 364 
ILE   OXT    O  N N 365 
ILE   H      H  N N 366 
ILE   H2     H  N N 367 
ILE   HA     H  N N 368 
ILE   HB     H  N N 369 
ILE   HG12   H  N N 370 
ILE   HG13   H  N N 371 
ILE   HG21   H  N N 372 
ILE   HG22   H  N N 373 
ILE   HG23   H  N N 374 
ILE   HD11   H  N N 375 
ILE   HD12   H  N N 376 
ILE   HD13   H  N N 377 
ILE   HXT    H  N N 378 
LEU   N      N  N N 379 
LEU   CA     C  N S 380 
LEU   C      C  N N 381 
LEU   O      O  N N 382 
LEU   CB     C  N N 383 
LEU   CG     C  N N 384 
LEU   CD1    C  N N 385 
LEU   CD2    C  N N 386 
LEU   OXT    O  N N 387 
LEU   H      H  N N 388 
LEU   H2     H  N N 389 
LEU   HA     H  N N 390 
LEU   HB2    H  N N 391 
LEU   HB3    H  N N 392 
LEU   HG     H  N N 393 
LEU   HD11   H  N N 394 
LEU   HD12   H  N N 395 
LEU   HD13   H  N N 396 
LEU   HD21   H  N N 397 
LEU   HD22   H  N N 398 
LEU   HD23   H  N N 399 
LEU   HXT    H  N N 400 
LYS   N      N  N N 401 
LYS   CA     C  N S 402 
LYS   C      C  N N 403 
LYS   O      O  N N 404 
LYS   CB     C  N N 405 
LYS   CG     C  N N 406 
LYS   CD     C  N N 407 
LYS   CE     C  N N 408 
LYS   NZ     N  N N 409 
LYS   OXT    O  N N 410 
LYS   H      H  N N 411 
LYS   H2     H  N N 412 
LYS   HA     H  N N 413 
LYS   HB2    H  N N 414 
LYS   HB3    H  N N 415 
LYS   HG2    H  N N 416 
LYS   HG3    H  N N 417 
LYS   HD2    H  N N 418 
LYS   HD3    H  N N 419 
LYS   HE2    H  N N 420 
LYS   HE3    H  N N 421 
LYS   HZ1    H  N N 422 
LYS   HZ2    H  N N 423 
LYS   HZ3    H  N N 424 
LYS   HXT    H  N N 425 
MET   N      N  N N 426 
MET   CA     C  N S 427 
MET   C      C  N N 428 
MET   O      O  N N 429 
MET   CB     C  N N 430 
MET   CG     C  N N 431 
MET   SD     S  N N 432 
MET   CE     C  N N 433 
MET   OXT    O  N N 434 
MET   H      H  N N 435 
MET   H2     H  N N 436 
MET   HA     H  N N 437 
MET   HB2    H  N N 438 
MET   HB3    H  N N 439 
MET   HG2    H  N N 440 
MET   HG3    H  N N 441 
MET   HE1    H  N N 442 
MET   HE2    H  N N 443 
MET   HE3    H  N N 444 
MET   HXT    H  N N 445 
MG    MG     MG N N 446 
PHE   N      N  N N 447 
PHE   CA     C  N S 448 
PHE   C      C  N N 449 
PHE   O      O  N N 450 
PHE   CB     C  N N 451 
PHE   CG     C  Y N 452 
PHE   CD1    C  Y N 453 
PHE   CD2    C  Y N 454 
PHE   CE1    C  Y N 455 
PHE   CE2    C  Y N 456 
PHE   CZ     C  Y N 457 
PHE   OXT    O  N N 458 
PHE   H      H  N N 459 
PHE   H2     H  N N 460 
PHE   HA     H  N N 461 
PHE   HB2    H  N N 462 
PHE   HB3    H  N N 463 
PHE   HD1    H  N N 464 
PHE   HD2    H  N N 465 
PHE   HE1    H  N N 466 
PHE   HE2    H  N N 467 
PHE   HZ     H  N N 468 
PHE   HXT    H  N N 469 
PRO   N      N  N N 470 
PRO   CA     C  N S 471 
PRO   C      C  N N 472 
PRO   O      O  N N 473 
PRO   CB     C  N N 474 
PRO   CG     C  N N 475 
PRO   CD     C  N N 476 
PRO   OXT    O  N N 477 
PRO   H      H  N N 478 
PRO   HA     H  N N 479 
PRO   HB2    H  N N 480 
PRO   HB3    H  N N 481 
PRO   HG2    H  N N 482 
PRO   HG3    H  N N 483 
PRO   HD2    H  N N 484 
PRO   HD3    H  N N 485 
PRO   HXT    H  N N 486 
SER   N      N  N N 487 
SER   CA     C  N S 488 
SER   C      C  N N 489 
SER   O      O  N N 490 
SER   CB     C  N N 491 
SER   OG     O  N N 492 
SER   OXT    O  N N 493 
SER   H      H  N N 494 
SER   H2     H  N N 495 
SER   HA     H  N N 496 
SER   HB2    H  N N 497 
SER   HB3    H  N N 498 
SER   HG     H  N N 499 
SER   HXT    H  N N 500 
THR   N      N  N N 501 
THR   CA     C  N S 502 
THR   C      C  N N 503 
THR   O      O  N N 504 
THR   CB     C  N R 505 
THR   OG1    O  N N 506 
THR   CG2    C  N N 507 
THR   OXT    O  N N 508 
THR   H      H  N N 509 
THR   H2     H  N N 510 
THR   HA     H  N N 511 
THR   HB     H  N N 512 
THR   HG1    H  N N 513 
THR   HG21   H  N N 514 
THR   HG22   H  N N 515 
THR   HG23   H  N N 516 
THR   HXT    H  N N 517 
TRP   N      N  N N 518 
TRP   CA     C  N S 519 
TRP   C      C  N N 520 
TRP   O      O  N N 521 
TRP   CB     C  N N 522 
TRP   CG     C  Y N 523 
TRP   CD1    C  Y N 524 
TRP   CD2    C  Y N 525 
TRP   NE1    N  Y N 526 
TRP   CE2    C  Y N 527 
TRP   CE3    C  Y N 528 
TRP   CZ2    C  Y N 529 
TRP   CZ3    C  Y N 530 
TRP   CH2    C  Y N 531 
TRP   OXT    O  N N 532 
TRP   H      H  N N 533 
TRP   H2     H  N N 534 
TRP   HA     H  N N 535 
TRP   HB2    H  N N 536 
TRP   HB3    H  N N 537 
TRP   HD1    H  N N 538 
TRP   HE1    H  N N 539 
TRP   HE3    H  N N 540 
TRP   HZ2    H  N N 541 
TRP   HZ3    H  N N 542 
TRP   HH2    H  N N 543 
TRP   HXT    H  N N 544 
TYR   N      N  N N 545 
TYR   CA     C  N S 546 
TYR   C      C  N N 547 
TYR   O      O  N N 548 
TYR   CB     C  N N 549 
TYR   CG     C  Y N 550 
TYR   CD1    C  Y N 551 
TYR   CD2    C  Y N 552 
TYR   CE1    C  Y N 553 
TYR   CE2    C  Y N 554 
TYR   CZ     C  Y N 555 
TYR   OH     O  N N 556 
TYR   OXT    O  N N 557 
TYR   H      H  N N 558 
TYR   H2     H  N N 559 
TYR   HA     H  N N 560 
TYR   HB2    H  N N 561 
TYR   HB3    H  N N 562 
TYR   HD1    H  N N 563 
TYR   HD2    H  N N 564 
TYR   HE1    H  N N 565 
TYR   HE2    H  N N 566 
TYR   HH     H  N N 567 
TYR   HXT    H  N N 568 
VAL   N      N  N N 569 
VAL   CA     C  N S 570 
VAL   C      C  N N 571 
VAL   O      O  N N 572 
VAL   CB     C  N N 573 
VAL   CG1    C  N N 574 
VAL   CG2    C  N N 575 
VAL   OXT    O  N N 576 
VAL   H      H  N N 577 
VAL   H2     H  N N 578 
VAL   HA     H  N N 579 
VAL   HB     H  N N 580 
VAL   HG11   H  N N 581 
VAL   HG12   H  N N 582 
VAL   HG13   H  N N 583 
VAL   HG21   H  N N 584 
VAL   HG22   H  N N 585 
VAL   HG23   H  N N 586 
VAL   HXT    H  N N 587 
# 
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 
A1AOV O1    C1     doub N N 1   
A1AOV C1    C2     sing N N 2   
A1AOV C1    N5     sing N N 3   
A1AOV C2    C3     sing N N 4   
A1AOV C2    N1     sing N N 5   
A1AOV C3    C52    sing N N 6   
A1AOV N1    C4     sing N N 7   
A1AOV C4    C5     sing N N 8   
A1AOV C4    O4     doub N N 9   
A1AOV C5    C6     sing N N 10  
A1AOV C5    N2     sing N N 11  
A1AOV C6    C7     sing N N 12  
A1AOV C6    C8     sing N N 13  
A1AOV N2    C9     sing N N 14  
A1AOV N2    C10    sing N N 15  
A1AOV C10   C11    sing N N 16  
A1AOV C10   O3     doub N N 17  
A1AOV C11   C12    sing N N 18  
A1AOV C11   C22    sing N N 19  
A1AOV C12   C13    sing N N 20  
A1AOV C13   N3     sing N N 21  
A1AOV N3    C14    sing N N 22  
A1AOV N3    C22    sing N N 23  
A1AOV C14   C15    sing N N 24  
A1AOV C14   O2     doub N N 25  
A1AOV C15   C16    doub N E 26  
A1AOV C16   C17    sing N N 27  
A1AOV C17   C18    sing N N 28  
A1AOV C17   N4     sing N N 29  
A1AOV C17   C21    sing N N 30  
A1AOV N4    C19    sing N N 31  
A1AOV N4    C20    sing N N 32  
A1AOV N5    N6     sing N N 33  
A1AOV N5    C56    sing N N 34  
A1AOV N6    C23    sing N N 35  
A1AOV C23   C24    sing N N 36  
A1AOV C23   C54    sing N N 37  
A1AOV C24   O5     sing N N 38  
A1AOV C24   O7     doub N N 39  
A1AOV O5    C25    sing N N 40  
A1AOV C25   C26    sing N N 41  
A1AOV C26   C27    sing N N 42  
A1AOV C26   C28    sing N N 43  
A1AOV C26   C29    sing N N 44  
A1AOV C29   C30    sing N N 45  
A1AOV C30   C31    doub Y N 46  
A1AOV C30   C45    sing Y N 47  
A1AOV C31   C32    sing N N 48  
A1AOV C31   N8     sing Y N 49  
A1AOV C32   C33    doub Y N 50  
A1AOV C32   C39    sing Y N 51  
A1AOV C33   C34    sing N N 52  
A1AOV C33   N7     sing Y N 53  
A1AOV C34   O6     sing N N 54  
A1AOV C34   C36    sing N N 55  
A1AOV O6    C35    sing N N 56  
A1AOV N7    C37    doub Y N 57  
A1AOV C37   C38    sing Y N 58  
A1AOV C38   C39    doub Y N 59  
A1AOV N8    C40    sing N N 60  
A1AOV N8    C42    sing Y N 61  
A1AOV C40   C41    sing N N 62  
A1AOV C42   C43    doub Y N 63  
A1AOV C42   C45    sing Y N 64  
A1AOV C43   C44    sing Y N 65  
A1AOV C44   C47    doub Y N 66  
A1AOV C45   C46    doub Y N 67  
A1AOV C46   C47    sing Y N 68  
A1AOV C47   C48    sing N N 69  
A1AOV C48   C49    doub Y N 70  
A1AOV C48   C53    sing Y N 71  
A1AOV C49   C50    sing Y N 72  
A1AOV C50   C51    doub Y N 73  
A1AOV C51   C52    sing Y N 74  
A1AOV C52   C53    doub Y N 75  
A1AOV C54   C55    sing N N 76  
A1AOV C55   C56    sing N N 77  
A1AOV C11   H16    sing N N 78  
A1AOV C12   H17    sing N N 79  
A1AOV C12   H18    sing N N 80  
A1AOV C13   H19    sing N N 81  
A1AOV C13   H20    sing N N 82  
A1AOV C15   H21    sing N N 83  
A1AOV C16   H22    sing N N 84  
A1AOV C18   H25    sing N N 85  
A1AOV C18   H23    sing N N 86  
A1AOV C18   H24    sing N N 87  
A1AOV C19   H27    sing N N 88  
A1AOV C19   H26    sing N N 89  
A1AOV C19   H28    sing N N 90  
A1AOV C2    H1     sing N N 91  
A1AOV C20   H29    sing N N 92  
A1AOV C20   H31    sing N N 93  
A1AOV C20   H30    sing N N 94  
A1AOV C21   H32    sing N N 95  
A1AOV C21   H34    sing N N 96  
A1AOV C21   H33    sing N N 97  
A1AOV C22   H36    sing N N 98  
A1AOV C22   H35    sing N N 99  
A1AOV C23   H38    sing N N 100 
A1AOV C25   H39    sing N N 101 
A1AOV C25   H40    sing N N 102 
A1AOV C27   H41    sing N N 103 
A1AOV C27   H42    sing N N 104 
A1AOV C27   H43    sing N N 105 
A1AOV C28   H44    sing N N 106 
A1AOV C28   H46    sing N N 107 
A1AOV C28   H45    sing N N 108 
A1AOV C29   H47    sing N N 109 
A1AOV C29   H48    sing N N 110 
A1AOV C3    H2     sing N N 111 
A1AOV C3    H3     sing N N 112 
A1AOV C34   H49    sing N N 113 
A1AOV C35   H52    sing N N 114 
A1AOV C35   H51    sing N N 115 
A1AOV C35   H50    sing N N 116 
A1AOV C36   H55    sing N N 117 
A1AOV C36   H53    sing N N 118 
A1AOV C36   H54    sing N N 119 
A1AOV C37   H56    sing N N 120 
A1AOV C38   H57    sing N N 121 
A1AOV C39   H58    sing N N 122 
A1AOV C40   H60    sing N N 123 
A1AOV C40   H59    sing N N 124 
A1AOV C41   H61    sing N N 125 
A1AOV C41   H62    sing N N 126 
A1AOV C41   H63    sing N N 127 
A1AOV C43   H64    sing N N 128 
A1AOV C44   H65    sing N N 129 
A1AOV C46   H66    sing N N 130 
A1AOV C49   H67    sing N N 131 
A1AOV C5    H5     sing N N 132 
A1AOV C50   H68    sing N N 133 
A1AOV C51   H69    sing N N 134 
A1AOV C53   H70    sing N N 135 
A1AOV C54   H71    sing N N 136 
A1AOV C54   H72    sing N N 137 
A1AOV C55   H73    sing N N 138 
A1AOV C55   H74    sing N N 139 
A1AOV C56   H75    sing N N 140 
A1AOV C56   H76    sing N N 141 
A1AOV C6    H6     sing N N 142 
A1AOV C7    H8     sing N N 143 
A1AOV C7    H9     sing N N 144 
A1AOV C7    H7     sing N N 145 
A1AOV C8    H12    sing N N 146 
A1AOV C8    H10    sing N N 147 
A1AOV C8    H11    sing N N 148 
A1AOV C9    H14    sing N N 149 
A1AOV C9    H15    sing N N 150 
A1AOV C9    H13    sing N N 151 
A1AOV N1    H4     sing N N 152 
A1AOV N6    H37    sing N N 153 
ALA   N     CA     sing N N 154 
ALA   N     H      sing N N 155 
ALA   N     H2     sing N N 156 
ALA   CA    C      sing N N 157 
ALA   CA    CB     sing N N 158 
ALA   CA    HA     sing N N 159 
ALA   C     O      doub N N 160 
ALA   C     OXT    sing N N 161 
ALA   CB    HB1    sing N N 162 
ALA   CB    HB2    sing N N 163 
ALA   CB    HB3    sing N N 164 
ALA   OXT   HXT    sing N N 165 
ARG   N     CA     sing N N 166 
ARG   N     H      sing N N 167 
ARG   N     H2     sing N N 168 
ARG   CA    C      sing N N 169 
ARG   CA    CB     sing N N 170 
ARG   CA    HA     sing N N 171 
ARG   C     O      doub N N 172 
ARG   C     OXT    sing N N 173 
ARG   CB    CG     sing N N 174 
ARG   CB    HB2    sing N N 175 
ARG   CB    HB3    sing N N 176 
ARG   CG    CD     sing N N 177 
ARG   CG    HG2    sing N N 178 
ARG   CG    HG3    sing N N 179 
ARG   CD    NE     sing N N 180 
ARG   CD    HD2    sing N N 181 
ARG   CD    HD3    sing N N 182 
ARG   NE    CZ     sing N N 183 
ARG   NE    HE     sing N N 184 
ARG   CZ    NH1    sing N N 185 
ARG   CZ    NH2    doub N N 186 
ARG   NH1   HH11   sing N N 187 
ARG   NH1   HH12   sing N N 188 
ARG   NH2   HH21   sing N N 189 
ARG   NH2   HH22   sing N N 190 
ARG   OXT   HXT    sing N N 191 
ASN   N     CA     sing N N 192 
ASN   N     H      sing N N 193 
ASN   N     H2     sing N N 194 
ASN   CA    C      sing N N 195 
ASN   CA    CB     sing N N 196 
ASN   CA    HA     sing N N 197 
ASN   C     O      doub N N 198 
ASN   C     OXT    sing N N 199 
ASN   CB    CG     sing N N 200 
ASN   CB    HB2    sing N N 201 
ASN   CB    HB3    sing N N 202 
ASN   CG    OD1    doub N N 203 
ASN   CG    ND2    sing N N 204 
ASN   ND2   HD21   sing N N 205 
ASN   ND2   HD22   sing N N 206 
ASN   OXT   HXT    sing N N 207 
ASP   N     CA     sing N N 208 
ASP   N     H      sing N N 209 
ASP   N     H2     sing N N 210 
ASP   CA    C      sing N N 211 
ASP   CA    CB     sing N N 212 
ASP   CA    HA     sing N N 213 
ASP   C     O      doub N N 214 
ASP   C     OXT    sing N N 215 
ASP   CB    CG     sing N N 216 
ASP   CB    HB2    sing N N 217 
ASP   CB    HB3    sing N N 218 
ASP   CG    OD1    doub N N 219 
ASP   CG    OD2    sing N N 220 
ASP   OD2   HD2    sing N N 221 
ASP   OXT   HXT    sing N N 222 
CYS   N     CA     sing N N 223 
CYS   N     H      sing N N 224 
CYS   N     H2     sing N N 225 
CYS   CA    C      sing N N 226 
CYS   CA    CB     sing N N 227 
CYS   CA    HA     sing N N 228 
CYS   C     O      doub N N 229 
CYS   C     OXT    sing N N 230 
CYS   CB    SG     sing N N 231 
CYS   CB    HB2    sing N N 232 
CYS   CB    HB3    sing N N 233 
CYS   SG    HG     sing N N 234 
CYS   OXT   HXT    sing N N 235 
GLN   N     CA     sing N N 236 
GLN   N     H      sing N N 237 
GLN   N     H2     sing N N 238 
GLN   CA    C      sing N N 239 
GLN   CA    CB     sing N N 240 
GLN   CA    HA     sing N N 241 
GLN   C     O      doub N N 242 
GLN   C     OXT    sing N N 243 
GLN   CB    CG     sing N N 244 
GLN   CB    HB2    sing N N 245 
GLN   CB    HB3    sing N N 246 
GLN   CG    CD     sing N N 247 
GLN   CG    HG2    sing N N 248 
GLN   CG    HG3    sing N N 249 
GLN   CD    OE1    doub N N 250 
GLN   CD    NE2    sing N N 251 
GLN   NE2   HE21   sing N N 252 
GLN   NE2   HE22   sing N N 253 
GLN   OXT   HXT    sing N N 254 
GLU   N     CA     sing N N 255 
GLU   N     H      sing N N 256 
GLU   N     H2     sing N N 257 
GLU   CA    C      sing N N 258 
GLU   CA    CB     sing N N 259 
GLU   CA    HA     sing N N 260 
GLU   C     O      doub N N 261 
GLU   C     OXT    sing N N 262 
GLU   CB    CG     sing N N 263 
GLU   CB    HB2    sing N N 264 
GLU   CB    HB3    sing N N 265 
GLU   CG    CD     sing N N 266 
GLU   CG    HG2    sing N N 267 
GLU   CG    HG3    sing N N 268 
GLU   CD    OE1    doub N N 269 
GLU   CD    OE2    sing N N 270 
GLU   OE2   HE2    sing N N 271 
GLU   OXT   HXT    sing N N 272 
GLY   N     CA     sing N N 273 
GLY   N     H      sing N N 274 
GLY   N     H2     sing N N 275 
GLY   CA    C      sing N N 276 
GLY   CA    HA2    sing N N 277 
GLY   CA    HA3    sing N N 278 
GLY   C     O      doub N N 279 
GLY   C     OXT    sing N N 280 
GLY   OXT   HXT    sing N N 281 
GNP   PG    O1G    doub N N 282 
GNP   PG    O2G    sing N N 283 
GNP   PG    O3G    sing N N 284 
GNP   PG    N3B    sing N N 285 
GNP   O2G   HOG2   sing N N 286 
GNP   O3G   HOG3   sing N N 287 
GNP   N3B   PB     sing N N 288 
GNP   N3B   HNB3   sing N N 289 
GNP   PB    O1B    doub N N 290 
GNP   PB    O2B    sing N N 291 
GNP   PB    O3A    sing N N 292 
GNP   O2B   HOB2   sing N N 293 
GNP   O3A   PA     sing N N 294 
GNP   PA    O1A    doub N N 295 
GNP   PA    O2A    sing N N 296 
GNP   PA    "O5'"  sing N N 297 
GNP   O2A   HOA2   sing N N 298 
GNP   "O5'" "C5'"  sing N N 299 
GNP   "C5'" "C4'"  sing N N 300 
GNP   "C5'" "H5'2" sing N N 301 
GNP   "C5'" "H5'1" sing N N 302 
GNP   "C4'" "O4'"  sing N N 303 
GNP   "C4'" "C3'"  sing N N 304 
GNP   "C4'" "H4'"  sing N N 305 
GNP   "O4'" "C1'"  sing N N 306 
GNP   "C3'" "O3'"  sing N N 307 
GNP   "C3'" "C2'"  sing N N 308 
GNP   "C3'" "H3'"  sing N N 309 
GNP   "O3'" "HO3'" sing N N 310 
GNP   "C2'" "O2'"  sing N N 311 
GNP   "C2'" "C1'"  sing N N 312 
GNP   "C2'" "H2'"  sing N N 313 
GNP   "O2'" "HO2'" sing N N 314 
GNP   "C1'" N9     sing N N 315 
GNP   "C1'" "H1'"  sing N N 316 
GNP   N9    C8     sing Y N 317 
GNP   N9    C4     sing Y N 318 
GNP   C8    N7     doub Y N 319 
GNP   C8    H8     sing N N 320 
GNP   N7    C5     sing Y N 321 
GNP   C5    C6     sing Y N 322 
GNP   C5    C4     doub Y N 323 
GNP   C6    O6     doub N N 324 
GNP   C6    N1     sing Y N 325 
GNP   N1    C2     sing Y N 326 
GNP   N1    HN1    sing N N 327 
GNP   C2    N2     sing N N 328 
GNP   C2    N3     doub Y N 329 
GNP   N2    HN21   sing N N 330 
GNP   N2    HN22   sing N N 331 
GNP   N3    C4     sing Y N 332 
HIS   N     CA     sing N N 333 
HIS   N     H      sing N N 334 
HIS   N     H2     sing N N 335 
HIS   CA    C      sing N N 336 
HIS   CA    CB     sing N N 337 
HIS   CA    HA     sing N N 338 
HIS   C     O      doub N N 339 
HIS   C     OXT    sing N N 340 
HIS   CB    CG     sing N N 341 
HIS   CB    HB2    sing N N 342 
HIS   CB    HB3    sing N N 343 
HIS   CG    ND1    sing Y N 344 
HIS   CG    CD2    doub Y N 345 
HIS   ND1   CE1    doub Y N 346 
HIS   ND1   HD1    sing N N 347 
HIS   CD2   NE2    sing Y N 348 
HIS   CD2   HD2    sing N N 349 
HIS   CE1   NE2    sing Y N 350 
HIS   CE1   HE1    sing N N 351 
HIS   NE2   HE2    sing N N 352 
HIS   OXT   HXT    sing N N 353 
HOH   O     H1     sing N N 354 
HOH   O     H2     sing N N 355 
ILE   N     CA     sing N N 356 
ILE   N     H      sing N N 357 
ILE   N     H2     sing N N 358 
ILE   CA    C      sing N N 359 
ILE   CA    CB     sing N N 360 
ILE   CA    HA     sing N N 361 
ILE   C     O      doub N N 362 
ILE   C     OXT    sing N N 363 
ILE   CB    CG1    sing N N 364 
ILE   CB    CG2    sing N N 365 
ILE   CB    HB     sing N N 366 
ILE   CG1   CD1    sing N N 367 
ILE   CG1   HG12   sing N N 368 
ILE   CG1   HG13   sing N N 369 
ILE   CG2   HG21   sing N N 370 
ILE   CG2   HG22   sing N N 371 
ILE   CG2   HG23   sing N N 372 
ILE   CD1   HD11   sing N N 373 
ILE   CD1   HD12   sing N N 374 
ILE   CD1   HD13   sing N N 375 
ILE   OXT   HXT    sing N N 376 
LEU   N     CA     sing N N 377 
LEU   N     H      sing N N 378 
LEU   N     H2     sing N N 379 
LEU   CA    C      sing N N 380 
LEU   CA    CB     sing N N 381 
LEU   CA    HA     sing N N 382 
LEU   C     O      doub N N 383 
LEU   C     OXT    sing N N 384 
LEU   CB    CG     sing N N 385 
LEU   CB    HB2    sing N N 386 
LEU   CB    HB3    sing N N 387 
LEU   CG    CD1    sing N N 388 
LEU   CG    CD2    sing N N 389 
LEU   CG    HG     sing N N 390 
LEU   CD1   HD11   sing N N 391 
LEU   CD1   HD12   sing N N 392 
LEU   CD1   HD13   sing N N 393 
LEU   CD2   HD21   sing N N 394 
LEU   CD2   HD22   sing N N 395 
LEU   CD2   HD23   sing N N 396 
LEU   OXT   HXT    sing N N 397 
LYS   N     CA     sing N N 398 
LYS   N     H      sing N N 399 
LYS   N     H2     sing N N 400 
LYS   CA    C      sing N N 401 
LYS   CA    CB     sing N N 402 
LYS   CA    HA     sing N N 403 
LYS   C     O      doub N N 404 
LYS   C     OXT    sing N N 405 
LYS   CB    CG     sing N N 406 
LYS   CB    HB2    sing N N 407 
LYS   CB    HB3    sing N N 408 
LYS   CG    CD     sing N N 409 
LYS   CG    HG2    sing N N 410 
LYS   CG    HG3    sing N N 411 
LYS   CD    CE     sing N N 412 
LYS   CD    HD2    sing N N 413 
LYS   CD    HD3    sing N N 414 
LYS   CE    NZ     sing N N 415 
LYS   CE    HE2    sing N N 416 
LYS   CE    HE3    sing N N 417 
LYS   NZ    HZ1    sing N N 418 
LYS   NZ    HZ2    sing N N 419 
LYS   NZ    HZ3    sing N N 420 
LYS   OXT   HXT    sing N N 421 
MET   N     CA     sing N N 422 
MET   N     H      sing N N 423 
MET   N     H2     sing N N 424 
MET   CA    C      sing N N 425 
MET   CA    CB     sing N N 426 
MET   CA    HA     sing N N 427 
MET   C     O      doub N N 428 
MET   C     OXT    sing N N 429 
MET   CB    CG     sing N N 430 
MET   CB    HB2    sing N N 431 
MET   CB    HB3    sing N N 432 
MET   CG    SD     sing N N 433 
MET   CG    HG2    sing N N 434 
MET   CG    HG3    sing N N 435 
MET   SD    CE     sing N N 436 
MET   CE    HE1    sing N N 437 
MET   CE    HE2    sing N N 438 
MET   CE    HE3    sing N N 439 
MET   OXT   HXT    sing N N 440 
PHE   N     CA     sing N N 441 
PHE   N     H      sing N N 442 
PHE   N     H2     sing N N 443 
PHE   CA    C      sing N N 444 
PHE   CA    CB     sing N N 445 
PHE   CA    HA     sing N N 446 
PHE   C     O      doub N N 447 
PHE   C     OXT    sing N N 448 
PHE   CB    CG     sing N N 449 
PHE   CB    HB2    sing N N 450 
PHE   CB    HB3    sing N N 451 
PHE   CG    CD1    doub Y N 452 
PHE   CG    CD2    sing Y N 453 
PHE   CD1   CE1    sing Y N 454 
PHE   CD1   HD1    sing N N 455 
PHE   CD2   CE2    doub Y N 456 
PHE   CD2   HD2    sing N N 457 
PHE   CE1   CZ     doub Y N 458 
PHE   CE1   HE1    sing N N 459 
PHE   CE2   CZ     sing Y N 460 
PHE   CE2   HE2    sing N N 461 
PHE   CZ    HZ     sing N N 462 
PHE   OXT   HXT    sing N N 463 
PRO   N     CA     sing N N 464 
PRO   N     CD     sing N N 465 
PRO   N     H      sing N N 466 
PRO   CA    C      sing N N 467 
PRO   CA    CB     sing N N 468 
PRO   CA    HA     sing N N 469 
PRO   C     O      doub N N 470 
PRO   C     OXT    sing N N 471 
PRO   CB    CG     sing N N 472 
PRO   CB    HB2    sing N N 473 
PRO   CB    HB3    sing N N 474 
PRO   CG    CD     sing N N 475 
PRO   CG    HG2    sing N N 476 
PRO   CG    HG3    sing N N 477 
PRO   CD    HD2    sing N N 478 
PRO   CD    HD3    sing N N 479 
PRO   OXT   HXT    sing N N 480 
SER   N     CA     sing N N 481 
SER   N     H      sing N N 482 
SER   N     H2     sing N N 483 
SER   CA    C      sing N N 484 
SER   CA    CB     sing N N 485 
SER   CA    HA     sing N N 486 
SER   C     O      doub N N 487 
SER   C     OXT    sing N N 488 
SER   CB    OG     sing N N 489 
SER   CB    HB2    sing N N 490 
SER   CB    HB3    sing N N 491 
SER   OG    HG     sing N N 492 
SER   OXT   HXT    sing N N 493 
THR   N     CA     sing N N 494 
THR   N     H      sing N N 495 
THR   N     H2     sing N N 496 
THR   CA    C      sing N N 497 
THR   CA    CB     sing N N 498 
THR   CA    HA     sing N N 499 
THR   C     O      doub N N 500 
THR   C     OXT    sing N N 501 
THR   CB    OG1    sing N N 502 
THR   CB    CG2    sing N N 503 
THR   CB    HB     sing N N 504 
THR   OG1   HG1    sing N N 505 
THR   CG2   HG21   sing N N 506 
THR   CG2   HG22   sing N N 507 
THR   CG2   HG23   sing N N 508 
THR   OXT   HXT    sing N N 509 
TRP   N     CA     sing N N 510 
TRP   N     H      sing N N 511 
TRP   N     H2     sing N N 512 
TRP   CA    C      sing N N 513 
TRP   CA    CB     sing N N 514 
TRP   CA    HA     sing N N 515 
TRP   C     O      doub N N 516 
TRP   C     OXT    sing N N 517 
TRP   CB    CG     sing N N 518 
TRP   CB    HB2    sing N N 519 
TRP   CB    HB3    sing N N 520 
TRP   CG    CD1    doub Y N 521 
TRP   CG    CD2    sing Y N 522 
TRP   CD1   NE1    sing Y N 523 
TRP   CD1   HD1    sing N N 524 
TRP   CD2   CE2    doub Y N 525 
TRP   CD2   CE3    sing Y N 526 
TRP   NE1   CE2    sing Y N 527 
TRP   NE1   HE1    sing N N 528 
TRP   CE2   CZ2    sing Y N 529 
TRP   CE3   CZ3    doub Y N 530 
TRP   CE3   HE3    sing N N 531 
TRP   CZ2   CH2    doub Y N 532 
TRP   CZ2   HZ2    sing N N 533 
TRP   CZ3   CH2    sing Y N 534 
TRP   CZ3   HZ3    sing N N 535 
TRP   CH2   HH2    sing N N 536 
TRP   OXT   HXT    sing N N 537 
TYR   N     CA     sing N N 538 
TYR   N     H      sing N N 539 
TYR   N     H2     sing N N 540 
TYR   CA    C      sing N N 541 
TYR   CA    CB     sing N N 542 
TYR   CA    HA     sing N N 543 
TYR   C     O      doub N N 544 
TYR   C     OXT    sing N N 545 
TYR   CB    CG     sing N N 546 
TYR   CB    HB2    sing N N 547 
TYR   CB    HB3    sing N N 548 
TYR   CG    CD1    doub Y N 549 
TYR   CG    CD2    sing Y N 550 
TYR   CD1   CE1    sing Y N 551 
TYR   CD1   HD1    sing N N 552 
TYR   CD2   CE2    doub Y N 553 
TYR   CD2   HD2    sing N N 554 
TYR   CE1   CZ     doub Y N 555 
TYR   CE1   HE1    sing N N 556 
TYR   CE2   CZ     sing Y N 557 
TYR   CE2   HE2    sing N N 558 
TYR   CZ    OH     sing N N 559 
TYR   OH    HH     sing N N 560 
TYR   OXT   HXT    sing N N 561 
VAL   N     CA     sing N N 562 
VAL   N     H      sing N N 563 
VAL   N     H2     sing N N 564 
VAL   CA    C      sing N N 565 
VAL   CA    CB     sing N N 566 
VAL   CA    HA     sing N N 567 
VAL   C     O      doub N N 568 
VAL   C     OXT    sing N N 569 
VAL   CB    CG1    sing N N 570 
VAL   CB    CG2    sing N N 571 
VAL   CB    HB     sing N N 572 
VAL   CG1   HG11   sing N N 573 
VAL   CG1   HG12   sing N N 574 
VAL   CG1   HG13   sing N N 575 
VAL   CG2   HG21   sing N N 576 
VAL   CG2   HG22   sing N N 577 
VAL   CG2   HG23   sing N N 578 
VAL   OXT   HXT    sing N N 579 
# 
_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 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BFV 
_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]   0.020816 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000312 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009508 
_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]   0.015103 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153 2.53737 ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
P  ? ? 9.51135 5.44231 ? ? 1.42069  35.72801 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . SER   A 1 1   ? -12.31600 10.79600 -2.75800  1.000 31.94190 ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 1   ? -12.40300 12.12200 -3.35500  1.000 29.26301 ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 1   ? -12.87100 12.04100 -4.81000  1.000 27.89683 ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 1   ? -12.84200 10.98500 -5.43500  1.000 31.12229 ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 1   ? -11.05200 12.83800 -3.26500  1.000 30.00435 ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? -10.03700 12.09400 -3.92100  1.000 31.50737 ? 0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 2   ? -13.30400 13.16300 -5.35000  1.000 24.79885 ? 1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 2   ? -13.78100 13.17300 -6.72100  1.000 19.77138 ? 1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 2   ? -12.92600 14.11200 -7.55300  1.000 17.05245 ? 1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 2   ? -12.00900 14.77200 -7.05500  1.000 17.08823 ? 1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 2   ? -15.27200 13.50100 -6.79200  1.000 25.70651 ? 1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 2   ? -15.62500 14.91200 -6.40500  1.000 26.21431 ? 1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 2   ? -17.41500 15.18500 -6.39300  1.000 24.01634 ? 1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 2   ? -17.90800 14.30700 -4.93300  1.000 24.75700 ? 1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 3   ? -13.20600 14.11700 -8.84500  1.000 15.82864 ? 2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 3   ? -12.56100 14.99700 -9.80100  1.000 17.81342 ? 2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 3   ? -13.66200 15.58000 -10.67200 1.000 15.17997 ? 2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 3   ? -14.62100 14.88800 -11.01000 1.000 18.38679 ? 2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 3   ? -11.56200 14.21600 -10.68400 1.000 18.76314 ? 2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 3   ? -10.70100 13.41200 -9.86100  1.000 19.94786 ? 2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 3   ? -10.69900 15.17200 -11.49300 1.000 19.51674 ? 2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 4   ? -13.50100 16.83700 -11.06100 1.000 15.81417 ? 3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 4   ? -14.46900 17.54300 -11.88500 1.000 14.78785 ? 3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 4   ? -13.90600 17.76900 -13.28400 1.000 14.98291 ? 3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 4   ? -12.70400 18.03100 -13.44800 1.000 15.19670 ? 3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 4   ? -14.80500 18.88600 -11.22800 1.000 16.10539 ? 3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 4   ? -15.91800 19.69400 -11.86500 1.000 16.89779 ? 3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 4   ? -16.37300 20.83800 -10.96000 1.000 20.80381 ? 3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 4   ? -15.91900 20.91800 -9.79900  1.000 21.61532 ? 3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 4   ? -17.17800 21.67200 -11.39500 1.000 23.68523 ? 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 5   ? -14.78200 17.67400 -14.29200 1.000 13.92479 ? 4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 5   ? -14.39700 17.80100 -15.69300 1.000 14.83985 ? 4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 5   ? -15.30400 18.80000 -16.39000 1.000 13.96542 ? 4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 5   ? -16.53200 18.68500 -16.30600 1.000 15.00064 ? 4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 5   ? -14.46500 16.45100 -16.42700 1.000 14.48937 ? 4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 5   ? -13.51600 15.46100 -15.81900 1.000 13.85714 ? 4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 5   ? -12.20300 15.35800 -16.27700 1.000 15.39689 ? 4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 5   ? -13.89400 14.66700 -14.73500 1.000 14.42689 ? 4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 5   ? -11.30200 14.47600 -15.69700 1.000 15.63306 ? 4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 5   ? -13.00300 13.78700 -14.15400 1.000 15.62878 ? 4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 5   ? -11.71000 13.70000 -14.63400 1.000 15.51363 ? 4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 5   ? -10.81200 12.82100 -14.04500 1.000 17.80634 ? 4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 6   ? -14.70800 19.73900 -17.13000 1.000 14.54458 ? 5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 6   ? -15.47000 20.74900 -17.87500 1.000 14.74431 ? 5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 6   ? -15.57100 20.31800 -19.33800 1.000 12.39901 ? 5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 6   ? -14.61000 20.43700 -20.10100 1.000 13.30592 ? 5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 6   ? -14.82300 22.12300 -17.73400 1.000 16.73567 ? 5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 6   ? -14.94700 22.71300 -16.32500 1.000 20.85684 ? 5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 6   ? -14.36700 24.11400 -16.26900 1.000 28.40092 ? 5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 6   ? -12.84500 24.09300 -16.33000 1.000 34.39463 ? 5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 6   ? -12.26500 25.47600 -16.34300 1.000 35.97463 ? 5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 7   ? -16.72600 19.77200 -19.71800 1.000 12.81411 ? 6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 7   ? -16.95600 19.26000 -21.06400 1.000 13.00080 ? 6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 7   ? -17.80700 20.25700 -21.83500 1.000 12.26923 ? 6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 7   ? -18.73700 20.84600 -21.28300 1.000 14.80864 ? 6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 7   ? -17.70200 17.92000 -21.00400 1.000 14.72265 ? 6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 7   ? -17.16900 16.88800 -20.00100 1.000 15.38584 ? 6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 7   ? -17.90500 15.56400 -20.13100 1.000 16.32124 ? 6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 7   ? -15.67200 16.69600 -20.14300 1.000 16.10131 ? 6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 8   ? -17.49000 20.43700 -23.11300 1.000 11.40776 ? 7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 8   ? -18.23400 21.35500 -23.97400 1.000 11.64426 ? 7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 8   ? -18.66100 20.57700 -25.21000 1.000 11.35574 ? 7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 8   ? -17.83400 19.91000 -25.84100 1.000 12.49833 ? 7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 8   ? -17.39100 22.58800 -24.36600 1.000 12.23256 ? 7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 8   ? -18.18500 23.51400 -25.27100 1.000 12.95536 ? 7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 8   ? -16.92600 23.33000 -23.13000 1.000 14.07066 ? 7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 9   ? -19.95100 20.64700 -25.54800 1.000 11.67106 ? 8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 9   ? -20.51100 19.92400 -26.68700 1.000 11.69396 ? 8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 9   ? -20.71400 20.92300 -27.82100 1.000 11.26738 ? 8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 9   ? -21.45000 21.90300 -27.66400 1.000 12.54884 ? 8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 9   ? -21.82900 19.22400 -26.31600 1.000 12.83725 ? 8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 9   ? -22.29900 18.35900 -27.46100 1.000 13.29874 ? 8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 9   ? -21.68400 18.40100 -25.03900 1.000 14.61318 ? 8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 10  ? -20.07000 20.67200 -28.96000 1.000 11.69065 ? 9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 10  ? -20.10100 21.54400 -30.12900 1.000 11.11411 ? 9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 10  ? -20.46800 20.73900 -31.37400 1.000 11.23378 ? 9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 10  ? -20.36800 19.51300 -31.40200 1.000 13.16537 ? 9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 10  ? -18.75800 22.28900 -30.33500 1.000 13.47032 ? 9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 10  ? -18.36800 23.07500 -29.07400 1.000 14.69371 ? 9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 10  ? -17.64800 21.32200 -30.75200 1.000 14.69886 ? 9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 11  ? -20.86900 21.45500 -32.42200 1.000 12.37439 ? 10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 11  ? -21.29300 20.79000 -33.66500 1.000 13.13219 ? 10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 11  ? -22.38100 21.59300 -34.33900 1.000 13.28371 ? 10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 11  ? -22.97700 22.47000 -33.69600 1.000 13.71048 ? 10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 12  ? -22.63800 21.26600 -35.60000 1.000 13.56187 ? 11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 12  ? -23.62100 22.03200 -36.39600 1.000 14.54580 ? 11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 12  ? -25.04400 21.89900 -35.85000 1.000 14.60135 ? 11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 12  ? -25.39200 21.02800 -35.07100 1.000 14.27919 ? 11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 12  ? -23.55300 21.55400 -37.81900 1.000 16.31199 ? 11  ALA   A CB    1 
ATOM   90   N  N     . CYS   A 1 13  ? -25.87700 22.81400 -36.32900 1.000 15.74602 ? 12  CYS   A N     1 
ATOM   91   C  CA    . CYS   A 1 13  ? -27.27400 22.83400 -35.84600 1.000 16.11428 ? 12  CYS   A CA    1 
ATOM   92   C  C     . CYS   A 1 13  ? -27.97300 21.50500 -36.13400 1.000 14.84047 ? 12  CYS   A C     1 
ATOM   93   O  O     . CYS   A 1 13  ? -27.78400 20.95000 -37.21600 1.000 16.80765 ? 12  CYS   A O     1 
ATOM   94   C  CB    . CYS   A 1 13  ? -28.05300 23.94300 -36.54500 1.000 19.25330 ? 12  CYS   A CB    1 
ATOM   95   S  SG    . CYS   A 1 13  ? -27.77500 23.98100 -38.33400 1.000 26.03483 ? 12  CYS   A SG    1 
ATOM   96   N  N     . GLY   A 1 14  ? -28.69400 21.00400 -35.15200 1.000 16.15849 ? 13  GLY   A N     1 
ATOM   97   C  CA    . GLY   A 1 14  ? -29.54200 19.82400 -35.39600 1.000 16.06516 ? 13  GLY   A CA    1 
ATOM   98   C  C     . GLY   A 1 14  ? -28.86400 18.46600 -35.36000 1.000 15.78905 ? 13  GLY   A C     1 
ATOM   99   O  O     . GLY   A 1 14  ? -29.55700 17.48300 -35.59200 1.000 18.14906 ? 13  GLY   A O     1 
ATOM   100  N  N     . VAL   A 1 15  ? -27.57700 18.38700 -35.02100 1.000 14.72310 ? 14  VAL   A N     1 
ATOM   101  C  CA    . VAL   A 1 15  ? -26.85800 17.07900 -35.09300 1.000 13.78936 ? 14  VAL   A CA    1 
ATOM   102  C  C     . VAL   A 1 15  ? -27.17200 16.20200 -33.86900 1.000 13.38562 ? 14  VAL   A C     1 
ATOM   103  O  O     . VAL   A 1 15  ? -26.91400 15.00900 -33.94000 1.000 14.56138 ? 14  VAL   A O     1 
ATOM   104  C  CB    . VAL   A 1 15  ? -25.34400 17.32300 -35.23500 1.000 12.59589 ? 14  VAL   A CB    1 
ATOM   105  C  CG1   . VAL   A 1 15  ? -24.99400 18.02000 -36.54100 1.000 14.64305 ? 14  VAL   A CG1   1 
ATOM   106  C  CG2   . VAL   A 1 15  ? -24.74600 18.07300 -34.05000 1.000 14.09554 ? 14  VAL   A CG2   1 
ATOM   107  N  N     . GLY   A 1 16  ? -27.66600 16.80400 -32.79800 1.000 13.99529 ? 15  GLY   A N     1 
ATOM   108  C  CA    . GLY   A 1 16  ? -28.03500 16.05700 -31.61600 1.000 15.65256 ? 15  GLY   A CA    1 
ATOM   109  C  C     . GLY   A 1 16  ? -27.22900 16.35900 -30.36300 1.000 13.42635 ? 15  GLY   A C     1 
ATOM   110  O  O     . GLY   A 1 16  ? -27.17000 15.52800 -29.45300 1.000 15.59400 ? 15  GLY   A O     1 
ATOM   111  N  N     . LYS   A 1 17  ? -26.64000 17.54400 -30.28400 1.000 13.59887 ? 16  LYS   A N     1 
ATOM   112  C  CA    . LYS   A 1 17  ? -25.82100 17.93100 -29.10400 1.000 13.09709 ? 16  LYS   A CA    1 
ATOM   113  C  C     . LYS   A 1 17  ? -26.68300 17.86000 -27.83900 1.000 13.48662 ? 16  LYS   A C     1 
ATOM   114  O  O     . LYS   A 1 17  ? -26.26000 17.24800 -26.85000 1.000 13.82203 ? 16  LYS   A O     1 
ATOM   115  C  CB    . LYS   A 1 17  ? -25.26700 19.35000 -29.28900 1.000 12.69136 ? 16  LYS   A CB    1 
ATOM   116  C  CG    . LYS   A 1 17  ? -24.34700 19.52900 -30.48600 1.000 12.96719 ? 16  LYS   A CG    1 
ATOM   117  C  CD    . LYS   A 1 17  ? -23.83400 20.95900 -30.59500 1.000 13.99406 ? 16  LYS   A CD    1 
ATOM   118  C  CE    . LYS   A 1 17  ? -24.89100 21.96400 -30.92400 1.000 14.91150 ? 16  LYS   A CE    1 
ATOM   119  N  NZ    . LYS   A 1 17  ? -25.49100 21.73500 -32.24000 1.000 12.73798 ? 16  LYS   A NZ    1 
ATOM   120  N  N     . SER   A 1 18  ? -27.86700 18.45800 -27.90100 1.000 14.00956 ? 17  SER   A N     1 
ATOM   121  C  CA    . SER   A 1 18  ? -28.72800 18.48700 -26.72300 1.000 15.16526 ? 17  SER   A CA    1 
ATOM   122  C  C     . SER   A 1 18  ? -29.31800 17.11100 -26.42800 1.000 15.10981 ? 17  SER   A C     1 
ATOM   123  O  O     . SER   A 1 18  ? -29.38900 16.69500 -25.26400 1.000 15.56265 ? 17  SER   A O     1 
ATOM   124  C  CB    . SER   A 1 18  ? -29.83900 19.51600 -26.92700 1.000 16.21947 ? 17  SER   A CB    1 
ATOM   125  O  OG    . SER   A 1 18  ? -29.28600 20.79800 -27.07700 1.000 15.56744 ? 17  SER   A OG    1 
ATOM   126  N  N     . ALA   A 1 19  ? -29.73700 16.38100 -27.46600 1.000 16.18741 ? 18  ALA   A N     1 
ATOM   127  C  CA    . ALA   A 1 19  ? -30.30600 15.05700 -27.22700 1.000 17.25521 ? 18  ALA   A CA    1 
ATOM   128  C  C     . ALA   A 1 19  ? -29.28300 14.12800 -26.57500 1.000 16.23211 ? 18  ALA   A C     1 
ATOM   129  O  O     . ALA   A 1 19  ? -29.61500 13.37100 -25.65400 1.000 15.73121 ? 18  ALA   A O     1 
ATOM   130  C  CB    . ALA   A 1 19  ? -30.83000 14.46800 -28.53700 1.000 17.93508 ? 18  ALA   A CB    1 
ATOM   131  N  N     . LEU   A 1 20  ? -28.02100 14.22000 -26.99600 1.000 15.51742 ? 19  LEU   A N     1 
ATOM   132  C  CA    . LEU   A 1 20  ? -26.97100 13.42400 -26.36900 1.000 15.61766 ? 19  LEU   A CA    1 
ATOM   133  C  C     . LEU   A 1 20  ? -26.80800 13.81000 -24.90900 1.000 15.65221 ? 19  LEU   A C     1 
ATOM   134  O  O     . LEU   A 1 20  ? -26.75400 12.94200 -24.01900 1.000 17.97311 ? 19  LEU   A O     1 
ATOM   135  C  CB    . LEU   A 1 20  ? -25.65800 13.63400 -27.12100 1.000 15.94611 ? 19  LEU   A CB    1 
ATOM   136  C  CG    . LEU   A 1 20  ? -25.52200 12.86600 -28.44000 1.000 15.93432 ? 19  LEU   A CG    1 
ATOM   137  C  CD1   . LEU   A 1 20  ? -24.26800 13.31000 -29.20300 1.000 16.86219 ? 19  LEU   A CD1   1 
ATOM   138  C  CD2   . LEU   A 1 20  ? -25.49900 11.36600 -28.17000 1.000 18.61716 ? 19  LEU   A CD2   1 
ATOM   139  N  N     . THR   A 1 21  ? -26.74200 15.11900 -24.64700 1.000 16.54561 ? 20  THR   A N     1 
ATOM   140  C  CA    . THR   A 1 21  ? -26.55800 15.60300 -23.28300 1.000 15.66759 ? 20  THR   A CA    1 
ATOM   141  C  C     . THR   A 1 21  ? -27.73200 15.20700 -22.39500 1.000 17.34132 ? 20  THR   A C     1 
ATOM   142  O  O     . THR   A 1 21  ? -27.53200 14.74700 -21.27000 1.000 19.53199 ? 20  THR   A O     1 
ATOM   143  C  CB    . THR   A 1 21  ? -26.36100 17.12000 -23.29000 1.000 16.65243 ? 20  THR   A CB    1 
ATOM   144  O  OG1   . THR   A 1 21  ? -25.23300 17.45200 -24.11400 1.000 16.58117 ? 20  THR   A OG1   1 
ATOM   145  C  CG2   . THR   A 1 21  ? -26.09200 17.63300 -21.87900 1.000 18.71978 ? 20  THR   A CG2   1 
ATOM   146  N  N     . ILE   A 1 22  ? -28.96500 15.36900 -22.89200 1.000 18.68791 ? 21  ILE   A N     1 
ATOM   147  C  CA    A ILE   A 1 22  ? -30.14300 15.04500 -22.08700 0.500 19.83770 ? 21  ILE   A CA    1 
ATOM   148  C  CA    B ILE   A 1 22  ? -30.13700 15.04800 -22.08000 0.500 20.48493 ? 21  ILE   A CA    1 
ATOM   149  C  C     . ILE   A 1 22  ? -30.23200 13.55000 -21.81600 1.000 19.46378 ? 21  ILE   A C     1 
ATOM   150  O  O     . ILE   A 1 22  ? -30.66100 13.12800 -20.73300 1.000 23.55440 ? 21  ILE   A O     1 
ATOM   151  C  CB    A ILE   A 1 22  ? -31.41900 15.59900 -22.74400 0.500 19.46020 ? 21  ILE   A CB    1 
ATOM   152  C  CB    B ILE   A 1 22  ? -31.42000 15.62800 -22.70600 0.500 21.35229 ? 21  ILE   A CB    1 
ATOM   153  C  CG1   A ILE   A 1 22  ? -31.43400 17.12300 -22.64100 0.500 20.70442 ? 21  ILE   A CG1   1 
ATOM   154  C  CG1   B ILE   A 1 22  ? -31.31900 17.15400 -22.79100 0.500 23.51059 ? 21  ILE   A CG1   1 
ATOM   155  C  CG2   A ILE   A 1 22  ? -32.67600 15.00500 -22.10400 0.500 20.84110 ? 21  ILE   A CG2   1 
ATOM   156  C  CG2   B ILE   A 1 22  ? -32.64900 15.23900 -21.89100 0.500 22.68624 ? 21  ILE   A CG2   1 
ATOM   157  C  CD1   A ILE   A 1 22  ? -32.35300 17.77500 -23.62900 0.500 20.90305 ? 21  ILE   A CD1   1 
ATOM   158  C  CD1   B ILE   A 1 22  ? -31.13200 17.83800 -21.44900 0.500 23.95255 ? 21  ILE   A CD1   1 
ATOM   159  N  N     . GLN   A 1 23  ? -29.83200 12.71900 -22.77800 1.000 18.83674 ? 22  GLN   A N     1 
ATOM   160  C  CA    . GLN   A 1 23  ? -29.78900 11.28800 -22.50500 1.000 20.22408 ? 22  GLN   A CA    1 
ATOM   161  C  C     . GLN   A 1 23  ? -28.79500 10.97600 -21.39800 1.000 21.37333 ? 22  GLN   A C     1 
ATOM   162  O  O     . GLN   A 1 23  ? -29.09800 10.20200 -20.48400 1.000 22.81932 ? 22  GLN   A O     1 
ATOM   163  C  CB    . GLN   A 1 23  ? -29.42400 10.51200 -23.76500 1.000 22.76468 ? 22  GLN   A CB    1 
ATOM   164  C  CG    . GLN   A 1 23  ? -30.62500 10.07200 -24.55200 1.000 25.45146 ? 22  GLN   A CG    1 
ATOM   165  C  CD    . GLN   A 1 23  ? -31.34100 8.86200  -23.96400 1.000 24.17551 ? 22  GLN   A CD    1 
ATOM   166  O  OE1   . GLN   A 1 23  ? -31.24600 8.54600  -22.76500 1.000 25.12041 ? 22  GLN   A OE1   1 
ATOM   167  N  NE2   . GLN   A 1 23  ? -32.08000 8.18200  -24.81500 1.000 25.52514 ? 22  GLN   A NE2   1 
ATOM   168  N  N     . LEU   A 1 24  ? -27.60800 11.58500 -21.45100 1.000 20.06986 ? 23  LEU   A N     1 
ATOM   169  C  CA    . LEU   A 1 24  ? -26.63100 11.37100 -20.39200 1.000 22.12258 ? 23  LEU   A CA    1 
ATOM   170  C  C     . LEU   A 1 24  ? -27.18000 11.83700 -19.04700 1.000 25.86037 ? 23  LEU   A C     1 
ATOM   171  O  O     . LEU   A 1 24  ? -27.14100 11.09600 -18.05700 1.000 29.65340 ? 23  LEU   A O     1 
ATOM   172  C  CB    . LEU   A 1 24  ? -25.32200 12.08900 -20.73300 1.000 22.69104 ? 23  LEU   A CB    1 
ATOM   173  C  CG    . LEU   A 1 24  ? -24.19200 11.78300 -19.74100 1.000 26.37925 ? 23  LEU   A CG    1 
ATOM   174  C  CD1   . LEU   A 1 24  ? -23.54700 10.44300 -20.06500 1.000 28.64896 ? 23  LEU   A CD1   1 
ATOM   175  C  CD2   . LEU   A 1 24  ? -23.16500 12.88100 -19.73700 1.000 26.25498 ? 23  LEU   A CD2   1 
ATOM   176  N  N     . ILE   A 1 25  ? -27.73100 13.05100 -19.00200 1.000 27.61857 ? 24  ILE   A N     1 
ATOM   177  C  CA    . ILE   A 1 25  ? -28.10700 13.67600 -17.73500 1.000 31.19753 ? 24  ILE   A CA    1 
ATOM   178  C  C     . ILE   A 1 25  ? -29.38900 13.06800 -17.18200 1.000 32.91771 ? 24  ILE   A C     1 
ATOM   179  O  O     . ILE   A 1 25  ? -29.48600 12.75900 -15.98700 1.000 36.00774 ? 24  ILE   A O     1 
ATOM   180  C  CB    . ILE   A 1 25  ? -28.24300 15.20300 -17.91000 1.000 30.91934 ? 24  ILE   A CB    1 
ATOM   181  C  CG1   . ILE   A 1 25  ? -26.89300 15.84200 -18.25400 1.000 32.06687 ? 24  ILE   A CG1   1 
ATOM   182  C  CG2   . ILE   A 1 25  ? -28.86500 15.83800 -16.65700 1.000 33.44764 ? 24  ILE   A CG2   1 
ATOM   183  C  CD1   . ILE   A 1 25  ? -25.84100 15.62900 -17.19800 1.000 31.91141 ? 24  ILE   A CD1   1 
ATOM   184  N  N     . GLN   A 1 26  ? -30.39800 12.90600 -18.03600 1.000 35.58854 ? 25  GLN   A N     1 
ATOM   185  C  CA    . GLN   A 1 26  ? -31.74000 12.57600 -17.58600 1.000 36.80735 ? 25  GLN   A CA    1 
ATOM   186  C  C     . GLN   A 1 26  ? -32.26100 11.23000 -18.06900 1.000 34.76399 ? 25  GLN   A C     1 
ATOM   187  O  O     . GLN   A 1 26  ? -33.34500 10.82900 -17.64300 1.000 35.59135 ? 25  GLN   A O     1 
ATOM   188  C  CB    . GLN   A 1 26  ? -32.72800 13.67900 -18.00100 1.000 40.21548 ? 25  GLN   A CB    1 
ATOM   189  C  CG    . GLN   A 1 26  ? -32.38100 15.05200 -17.45100 1.000 43.94952 ? 25  GLN   A CG    1 
ATOM   190  C  CD    . GLN   A 1 26  ? -33.16900 16.16500 -18.11200 1.000 47.60005 ? 25  GLN   A CD    1 
ATOM   191  O  OE1   . GLN   A 1 26  ? -34.05000 15.91400 -18.93400 1.000 50.31206 ? 25  GLN   A OE1   1 
ATOM   192  N  NE2   . GLN   A 1 26  ? -32.85200 17.40500 -17.75700 1.000 48.58364 ? 25  GLN   A NE2   1 
ATOM   193  N  N     . ASN   A 1 27  ? -31.54200 10.53600 -18.95000 1.000 34.93058 ? 26  ASN   A N     1 
ATOM   194  C  CA    . ASN   A 1 27  ? -31.91200 9.18800  -19.39900 1.000 37.09610 ? 26  ASN   A CA    1 
ATOM   195  C  C     . ASN   A 1 27  ? -33.26300 9.15800  -20.11600 1.000 36.04107 ? 26  ASN   A C     1 
ATOM   196  O  O     . ASN   A 1 27  ? -34.08700 8.26700  -19.89700 1.000 36.54654 ? 26  ASN   A O     1 
ATOM   197  C  CB    . ASN   A 1 27  ? -31.83600 8.16200  -18.26500 1.000 42.42471 ? 26  ASN   A CB    1 
ATOM   198  C  CG    . ASN   A 1 27  ? -30.53300 8.24900  -17.49800 1.000 49.13686 ? 26  ASN   A CG    1 
ATOM   199  O  OD1   . ASN   A 1 27  ? -29.49900 7.76400  -17.95400 1.000 52.73654 ? 26  ASN   A OD1   1 
ATOM   200  N  ND2   . ASN   A 1 27  ? -30.57600 8.87700  -16.32700 1.000 51.46146 ? 26  ASN   A ND2   1 
ATOM   201  N  N     . HIS   A 1 28  ? -33.49900 10.13900 -20.98300 1.000 34.99174 ? 27  HIS   A N     1 
ATOM   202  C  CA    . HIS   A 1 28  ? -34.64600 10.07700 -21.87400 1.000 33.39333 ? 27  HIS   A CA    1 
ATOM   203  C  C     . HIS   A 1 28  ? -34.32200 10.80600 -23.16800 1.000 28.44946 ? 27  HIS   A C     1 
ATOM   204  O  O     . HIS   A 1 28  ? -33.34600 11.55700 -23.25600 1.000 28.54065 ? 27  HIS   A O     1 
ATOM   205  C  CB    . HIS   A 1 28  ? -35.92700 10.62100 -21.23100 1.000 38.36381 ? 27  HIS   A CB    1 
ATOM   206  C  CG    . HIS   A 1 28  ? -35.94300 12.10900 -21.07500 1.000 43.87611 ? 27  HIS   A CG    1 
ATOM   207  N  ND1   . HIS   A 1 28  ? -36.26500 12.96100 -22.10800 1.000 46.15783 ? 27  HIS   A ND1   1 
ATOM   208  C  CD2   . HIS   A 1 28  ? -35.68300 12.89700 -20.00500 1.000 47.01047 ? 27  HIS   A CD2   1 
ATOM   209  C  CE1   . HIS   A 1 28  ? -36.19900 14.21000 -21.68400 1.000 45.97050 ? 27  HIS   A CE1   1 
ATOM   210  N  NE2   . HIS   A 1 28  ? -35.84800 14.19900 -20.41100 1.000 47.72974 ? 27  HIS   A NE2   1 
ATOM   211  N  N     . PHE   A 1 29  ? -35.16500 10.56500 -24.17100 1.000 27.81944 ? 28  PHE   A N     1 
ATOM   212  C  CA    . PHE   A 1 29  ? -35.06100 11.15800 -25.49500 1.000 26.46913 ? 28  PHE   A CA    1 
ATOM   213  C  C     . PHE   A 1 29  ? -36.44000 11.63000 -25.94000 1.000 32.74092 ? 28  PHE   A C     1 
ATOM   214  O  O     . PHE   A 1 29  ? -37.45100 10.98400 -25.64800 1.000 34.41203 ? 28  PHE   A O     1 
ATOM   215  C  CB    . PHE   A 1 29  ? -34.55500 10.10800 -26.48500 1.000 25.54784 ? 28  PHE   A CB    1 
ATOM   216  C  CG    . PHE   A 1 29  ? -34.58100 10.55300 -27.91500 1.000 24.33675 ? 28  PHE   A CG    1 
ATOM   217  C  CD1   . PHE   A 1 29  ? -33.55300 11.31800 -28.43300 1.000 24.39405 ? 28  PHE   A CD1   1 
ATOM   218  C  CD2   . PHE   A 1 29  ? -35.62400 10.17700 -28.75500 1.000 24.59717 ? 28  PHE   A CD2   1 
ATOM   219  C  CE1   . PHE   A 1 29  ? -33.56900 11.71800 -29.75700 1.000 23.59737 ? 28  PHE   A CE1   1 
ATOM   220  C  CE2   . PHE   A 1 29  ? -35.64400 10.57600 -30.07900 1.000 22.46775 ? 28  PHE   A CE2   1 
ATOM   221  C  CZ    . PHE   A 1 29  ? -34.61400 11.34700 -30.58000 1.000 24.03337 ? 28  PHE   A CZ    1 
ATOM   222  N  N     . VAL   A 1 30  ? -36.47900 12.75500 -26.64600 1.000 37.32374 ? 29  VAL   A N     1 
ATOM   223  C  CA    . VAL   A 1 30  ? -37.71200 13.28700 -27.21400 1.000 39.21568 ? 29  VAL   A CA    1 
ATOM   224  C  C     . VAL   A 1 30  ? -37.42300 13.72700 -28.64100 1.000 37.28159 ? 29  VAL   A C     1 
ATOM   225  O  O     . VAL   A 1 30  ? -36.37600 14.32300 -28.91600 1.000 39.65022 ? 29  VAL   A O     1 
ATOM   226  C  CB    . VAL   A 1 30  ? -38.27300 14.45700 -26.37500 1.000 41.93304 ? 29  VAL   A CB    1 
ATOM   227  C  CG1   . VAL   A 1 30  ? -39.50800 15.04500 -27.02800 1.000 42.62169 ? 29  VAL   A CG1   1 
ATOM   228  C  CG2   . VAL   A 1 30  ? -38.60700 13.99400 -24.96600 1.000 43.30996 ? 29  VAL   A CG2   1 
ATOM   229  N  N     . ASP   A 1 31  ? -38.34000 13.41500 -29.55600 1.000 34.67985 ? 30  ASP   A N     1 
ATOM   230  C  CA    A ASP   A 1 31  ? -38.09200 13.81000 -30.93300 0.500 34.91090 ? 30  ASP   A CA    1 
ATOM   231  C  CA    B ASP   A 1 31  ? -38.19100 13.78900 -30.96000 0.500 33.65157 ? 30  ASP   A CA    1 
ATOM   232  C  C     . ASP   A 1 31  ? -38.35700 15.28500 -31.19000 1.000 31.38270 ? 30  ASP   A C     1 
ATOM   233  O  O     . ASP   A 1 31  ? -37.93900 15.79100 -32.23600 1.000 28.95556 ? 30  ASP   A O     1 
ATOM   234  C  CB    A ASP   A 1 31  ? -38.84300 12.92100 -31.92600 0.500 38.80047 ? 30  ASP   A CB    1 
ATOM   235  C  CB    B ASP   A 1 31  ? -39.22400 13.04400 -31.81300 0.500 35.26386 ? 30  ASP   A CB    1 
ATOM   236  C  CG    A ASP   A 1 31  ? -37.90300 12.23800 -32.90100 0.500 40.18495 ? 30  ASP   A CG    1 
ATOM   237  C  CG    B ASP   A 1 31  ? -38.88600 11.58000 -31.99400 0.500 36.92536 ? 30  ASP   A CG    1 
ATOM   238  O  OD1   A ASP   A 1 31  ? -36.82300 12.81100 -33.18300 0.500 37.33726 ? 30  ASP   A OD1   1 
ATOM   239  O  OD1   B ASP   A 1 31  ? -37.77500 11.27700 -32.47500 0.500 37.42100 ? 30  ASP   A OD1   1 
ATOM   240  O  OD2   A ASP   A 1 31  ? -38.23400 11.13200 -33.37400 0.500 42.78098 ? 30  ASP   A OD2   1 
ATOM   241  O  OD2   B ASP   A 1 31  ? -39.73600 10.73000 -31.65500 0.500 38.63780 ? 30  ASP   A OD2   1 
ATOM   242  N  N     . GLU   A 1 32  ? -38.99000 15.99100 -30.26000 1.000 31.39941 ? 31  GLU   A N     1 
ATOM   243  C  CA    . GLU   A 1 32  ? -39.23300 17.41300 -30.44100 1.000 27.28667 ? 31  GLU   A CA    1 
ATOM   244  C  C     . GLU   A 1 32  ? -37.91800 18.18000 -30.40700 1.000 24.84239 ? 31  GLU   A C     1 
ATOM   245  O  O     . GLU   A 1 32  ? -37.08700 17.98400 -29.51700 1.000 27.92073 ? 31  GLU   A O     1 
ATOM   246  C  CB    . GLU   A 1 32  ? -40.17400 17.92700 -29.35300 1.000 30.65535 ? 31  GLU   A CB    1 
ATOM   247  C  CG    . GLU   A 1 32  ? -40.59200 19.37100 -29.54300 1.000 35.41376 ? 31  GLU   A CG    1 
ATOM   248  C  CD    . GLU   A 1 32  ? -41.93600 19.66900 -28.90800 1.000 39.22390 ? 31  GLU   A CD    1 
ATOM   249  O  OE1   . GLU   A 1 32  ? -42.53000 18.74300 -28.32000 1.000 40.80294 ? 31  GLU   A OE1   1 
ATOM   250  O  OE2   . GLU   A 1 32  ? -42.40400 20.82300 -29.00700 1.000 39.60601 ? 31  GLU   A OE2   1 
ATOM   251  N  N     . TYR   A 1 33  ? -37.72800 19.03800 -31.39900 1.000 20.04703 ? 32  TYR   A N     1 
ATOM   252  C  CA    . TYR   A 1 33  ? -36.50300 19.86500 -31.47300 1.000 17.74527 ? 32  TYR   A CA    1 
ATOM   253  C  C     . TYR   A 1 33  ? -36.70900 21.17100 -30.73300 1.000 17.96579 ? 32  TYR   A C     1 
ATOM   254  O  O     . TYR   A 1 33  ? -37.64500 21.92300 -31.04800 1.000 19.15824 ? 32  TYR   A O     1 
ATOM   255  C  CB    . TYR   A 1 33  ? -36.22500 20.10400 -32.95000 1.000 17.68655 ? 32  TYR   A CB    1 
ATOM   256  C  CG    . TYR   A 1 33  ? -35.03100 20.98300 -33.28600 1.000 17.74221 ? 32  TYR   A CG    1 
ATOM   257  C  CD1   . TYR   A 1 33  ? -33.93800 21.09500 -32.43600 1.000 18.92166 ? 32  TYR   A CD1   1 
ATOM   258  C  CD2   . TYR   A 1 33  ? -34.99900 21.68900 -34.47900 1.000 20.97062 ? 32  TYR   A CD2   1 
ATOM   259  C  CE1   . TYR   A 1 33  ? -32.85400 21.89200 -32.76000 1.000 18.16687 ? 32  TYR   A CE1   1 
ATOM   260  C  CE2   . TYR   A 1 33  ? -33.91900 22.48300 -34.81700 1.000 23.50949 ? 32  TYR   A CE2   1 
ATOM   261  C  CZ    . TYR   A 1 33  ? -32.84300 22.58300 -33.95600 1.000 19.94257 ? 32  TYR   A CZ    1 
ATOM   262  O  OH    . TYR   A 1 33  ? -31.79300 23.37400 -34.30700 1.000 19.72561 ? 32  TYR   A OH    1 
ATOM   263  N  N     . ASP   A 1 34  ? -35.87100 21.43400 -29.74900 1.000 14.62102 ? 33  ASP   A N     1 
ATOM   264  C  CA    . ASP   A 1 34  ? -35.87400 22.70700 -29.02200 1.000 15.84694 ? 33  ASP   A CA    1 
ATOM   265  C  C     . ASP   A 1 34  ? -34.50800 23.35100 -29.23900 1.000 15.25195 ? 33  ASP   A C     1 
ATOM   266  O  O     . ASP   A 1 34  ? -33.52900 23.00000 -28.55400 1.000 15.71177 ? 33  ASP   A O     1 
ATOM   267  C  CB    . ASP   A 1 34  ? -36.15000 22.46800 -27.53800 1.000 18.47488 ? 33  ASP   A CB    1 
ATOM   268  C  CG    . ASP   A 1 34  ? -36.29000 23.75300 -26.74300 1.000 21.40210 ? 33  ASP   A CG    1 
ATOM   269  O  OD1   . ASP   A 1 34  ? -36.31900 24.84000 -27.35600 1.000 21.53844 ? 33  ASP   A OD1   1 
ATOM   270  O  OD2   . ASP   A 1 34  ? -36.37900 23.66500 -25.49900 1.000 25.16239 ? 33  ASP   A OD2   1 
ATOM   271  N  N     . PRO   A 1 35  ? -34.38800 24.27900 -30.18600 1.000 15.60846 ? 34  PRO   A N     1 
ATOM   272  C  CA    . PRO   A 1 35  ? -33.07100 24.84300 -30.52300 1.000 17.19905 ? 34  PRO   A CA    1 
ATOM   273  C  C     . PRO   A 1 35  ? -32.41800 25.52600 -29.32800 1.000 16.02478 ? 34  PRO   A C     1 
ATOM   274  O  O     . PRO   A 1 35  ? -33.05400 26.28800 -28.59700 1.000 17.92247 ? 34  PRO   A O     1 
ATOM   275  C  CB    . PRO   A 1 35  ? -33.39300 25.85400 -31.63200 1.000 17.87484 ? 34  PRO   A CB    1 
ATOM   276  C  CG    . PRO   A 1 35  ? -34.73600 25.42400 -32.19800 1.000 19.46288 ? 34  PRO   A CG    1 
ATOM   277  C  CD    . PRO   A 1 35  ? -35.47200 24.77800 -31.05300 1.000 19.26593 ? 34  PRO   A CD    1 
ATOM   278  N  N     . THR   A 1 36  ? -31.13200 25.24600 -29.14000 1.000 15.24714 ? 35  THR   A N     1 
ATOM   279  C  CA    . THR   A 1 36  ? -30.41900 25.72000 -27.96300 1.000 14.22216 ? 35  THR   A CA    1 
ATOM   280  C  C     . THR   A 1 36  ? -29.95500 27.16100 -28.12300 1.000 13.53608 ? 35  THR   A C     1 
ATOM   281  O  O     . THR   A 1 36  ? -29.54000 27.57600 -29.20800 1.000 15.28925 ? 35  THR   A O     1 
ATOM   282  C  CB    . THR   A 1 36  ? -29.19200 24.84000 -27.74900 1.000 14.88862 ? 35  THR   A CB    1 
ATOM   283  O  OG1   . THR   A 1 36  ? -29.64400 23.49200 -27.58700 1.000 14.55410 ? 35  THR   A OG1   1 
ATOM   284  C  CG2   . THR   A 1 36  ? -28.37300 25.28800 -26.52100 1.000 15.35650 ? 35  THR   A CG2   1 
ATOM   285  N  N     . ILE   A 1 37  ? -30.02700 27.92200 -27.02400 1.000 13.59086 ? 36  ILE   A N     1 
ATOM   286  C  CA    . ILE   A 1 37  ? -29.26100 29.15200 -26.86200 1.000 14.07938 ? 36  ILE   A CA    1 
ATOM   287  C  C     . ILE   A 1 37  ? -27.99600 28.77700 -26.10600 1.000 14.33906 ? 36  ILE   A C     1 
ATOM   288  O  O     . ILE   A 1 37  ? -26.89400 28.88300 -26.64500 1.000 14.30817 ? 36  ILE   A O     1 
ATOM   289  C  CB    . ILE   A 1 37  ? -30.08200 30.23200 -26.12600 1.000 14.35852 ? 36  ILE   A CB    1 
ATOM   290  C  CG1   . ILE   A 1 37  ? -31.28200 30.63400 -26.98000 1.000 17.11932 ? 36  ILE   A CG1   1 
ATOM   291  C  CG2   . ILE   A 1 37  ? -29.19700 31.43100 -25.76600 1.000 16.70064 ? 36  ILE   A CG2   1 
ATOM   292  C  CD1   . ILE   A 1 37  ? -30.89700 31.41200 -28.21900 1.000 20.10150 ? 36  ILE   A CD1   1 
ATOM   293  N  N     . GLU   A 1 38  ? -28.14500 28.32300 -24.86300 1.000 12.97262 ? 37  GLU   A N     1 
ATOM   294  C  CA    . GLU   A 1 38  ? -27.02100 27.83900 -24.05900 1.000 13.46444 ? 37  GLU   A CA    1 
ATOM   295  C  C     . GLU   A 1 38  ? -27.59600 27.15700 -22.82800 1.000 14.06870 ? 37  GLU   A C     1 
ATOM   296  O  O     . GLU   A 1 38  ? -28.47900 27.71900 -22.18100 1.000 14.98047 ? 37  GLU   A O     1 
ATOM   297  C  CB    . GLU   A 1 38  ? -26.15900 29.00500 -23.58600 1.000 12.82022 ? 37  GLU   A CB    1 
ATOM   298  C  CG    . GLU   A 1 38  ? -24.86100 28.56200 -22.93700 1.000 14.37404 ? 37  GLU   A CG    1 
ATOM   299  C  CD    . GLU   A 1 38  ? -24.22400 29.68900 -22.14800 1.000 15.89637 ? 37  GLU   A CD    1 
ATOM   300  O  OE1   . GLU   A 1 38  ? -23.54500 30.53800 -22.76300 1.000 17.28190 ? 37  GLU   A OE1   1 
ATOM   301  O  OE2   . GLU   A 1 38  ? -24.43200 29.75300 -20.91900 1.000 19.63520 ? 37  GLU   A OE2   1 
ATOM   302  N  N     . ASP   A 1 39  ? -27.11500 25.96500 -22.49000 1.000 13.88848 ? 38  ASP   A N     1 
ATOM   303  C  CA    . ASP   A 1 39  ? -27.53000 25.28400 -21.27600 1.000 14.58534 ? 38  ASP   A CA    1 
ATOM   304  C  C     . ASP   A 1 39  ? -26.34100 24.58200 -20.64200 1.000 15.41823 ? 38  ASP   A C     1 
ATOM   305  O  O     . ASP   A 1 39  ? -25.40800 24.17100 -21.33000 1.000 15.53240 ? 38  ASP   A O     1 
ATOM   306  C  CB    . ASP   A 1 39  ? -28.61400 24.26500 -21.57600 1.000 17.38293 ? 38  ASP   A CB    1 
ATOM   307  C  CG    . ASP   A 1 39  ? -29.91500 24.91300 -21.95600 1.000 19.02994 ? 38  ASP   A CG    1 
ATOM   308  O  OD1   . ASP   A 1 39  ? -30.61100 25.46500 -21.06400 1.000 22.04826 ? 38  ASP   A OD1   1 
ATOM   309  O  OD2   . ASP   A 1 39  ? -30.22700 24.88000 -23.15800 1.000 22.69849 ? 38  ASP   A OD2   1 
ATOM   310  N  N     . SER   A 1 40  ? -26.38400 24.45400 -19.32100 1.000 15.71566 ? 39  SER   A N     1 
ATOM   311  C  CA    . SER   A 1 40  ? -25.29900 23.86200 -18.55600 1.000 15.57430 ? 39  SER   A CA    1 
ATOM   312  C  C     . SER   A 1 40  ? -25.87600 22.84300 -17.58900 1.000 16.44219 ? 39  SER   A C     1 
ATOM   313  O  O     . SER   A 1 40  ? -26.94000 23.06500 -17.00800 1.000 20.28204 ? 39  SER   A O     1 
ATOM   314  C  CB    . SER   A 1 40  ? -24.52400 24.92500 -17.75100 1.000 20.58823 ? 39  SER   A CB    1 
ATOM   315  O  OG    . SER   A 1 40  ? -23.82000 25.80300 -18.60600 1.000 25.67617 ? 39  SER   A OG    1 
ATOM   316  N  N     . TYR   A 1 41  ? -25.16200 21.73800 -17.39500 1.000 17.43977 ? 40  TYR   A N     1 
ATOM   317  C  CA    . TYR   A 1 41  ? -25.64100 20.65100 -16.55200 1.000 17.27326 ? 40  TYR   A CA    1 
ATOM   318  C  C     . TYR   A 1 41  ? -24.50200 20.14900 -15.68200 1.000 17.04663 ? 40  TYR   A C     1 
ATOM   319  O  O     . TYR   A 1 41  ? -23.32900 20.29200 -16.02800 1.000 17.74078 ? 40  TYR   A O     1 
ATOM   320  C  CB    . TYR   A 1 41  ? -26.14500 19.50300 -17.42100 1.000 18.14998 ? 40  TYR   A CB    1 
ATOM   321  C  CG    . TYR   A 1 41  ? -27.22900 19.93700 -18.37700 1.000 18.60742 ? 40  TYR   A CG    1 
ATOM   322  C  CD1   . TYR   A 1 41  ? -28.55600 19.96700 -17.97200 1.000 23.25239 ? 40  TYR   A CD1   1 
ATOM   323  C  CD2   . TYR   A 1 41  ? -26.93100 20.32900 -19.67200 1.000 17.50102 ? 40  TYR   A CD2   1 
ATOM   324  C  CE1   . TYR   A 1 41  ? -29.56100 20.37000 -18.82400 1.000 24.54731 ? 40  TYR   A CE1   1 
ATOM   325  C  CE2   . TYR   A 1 41  ? -27.94000 20.73100 -20.54400 1.000 18.11344 ? 40  TYR   A CE2   1 
ATOM   326  C  CZ    . TYR   A 1 41  ? -29.25400 20.74800 -20.11000 1.000 20.88686 ? 40  TYR   A CZ    1 
ATOM   327  O  OH    . TYR   A 1 41  ? -30.27400 21.14700 -20.94800 1.000 23.54988 ? 40  TYR   A OH    1 
ATOM   328  N  N     . ARG   A 1 42  ? -24.85900 19.54600 -14.54900 1.000 19.26491 ? 41  ARG   A N     1 
ATOM   329  C  CA    . ARG   A 1 42  ? -23.90400 18.90200 -13.65500 1.000 19.28613 ? 41  ARG   A CA    1 
ATOM   330  C  C     . ARG   A 1 42  ? -24.41100 17.51100 -13.30700 1.000 18.69732 ? 41  ARG   A C     1 
ATOM   331  O  O     . ARG   A 1 42  ? -25.60000 17.33400 -13.00300 1.000 20.33490 ? 41  ARG   A O     1 
ATOM   332  C  CB    . ARG   A 1 42  ? -23.69500 19.73200 -12.37100 1.000 19.42291 ? 41  ARG   A CB    1 
ATOM   333  C  CG    . ARG   A 1 42  ? -22.88500 21.01500 -12.62900 1.000 22.15335 ? 41  ARG   A CG    1 
ATOM   334  C  CD    . ARG   A 1 42  ? -22.98400 22.05300 -11.50900 1.000 24.54267 ? 41  ARG   A CD    1 
ATOM   335  N  NE    . ARG   A 1 42  ? -22.39000 21.62500 -10.24700 1.000 25.00700 ? 41  ARG   A NE    1 
ATOM   336  C  CZ    . ARG   A 1 42  ? -21.11500 21.78600 -9.90900  1.000 23.58878 ? 41  ARG   A CZ    1 
ATOM   337  N  NH1   . ARG   A 1 42  ? -20.23100 22.29800 -10.75200 1.000 27.10560 ? 41  ARG   A NH1   1 
ATOM   338  N  NH2   . ARG   A 1 42  ? -20.71900 21.43100 -8.69000  1.000 23.13132 ? 41  ARG   A NH2   1 
ATOM   339  N  N     . LYS   A 1 43  ? -23.51900 16.52600 -13.35400 1.000 17.21050 ? 42  LYS   A N     1 
ATOM   340  C  CA    . LYS   A 1 43  ? -23.90200 15.17700 -12.96700 1.000 18.39025 ? 42  LYS   A CA    1 
ATOM   341  C  C     . LYS   A 1 43  ? -22.70800 14.43500 -12.38900 1.000 16.90044 ? 42  LYS   A C     1 
ATOM   342  O  O     . LYS   A 1 43  ? -21.61300 14.46500 -12.94800 1.000 16.36419 ? 42  LYS   A O     1 
ATOM   343  C  CB    . LYS   A 1 43  ? -24.45000 14.38200 -14.15600 1.000 22.97028 ? 42  LYS   A CB    1 
ATOM   344  C  CG    . LYS   A 1 43  ? -24.96200 13.00800 -13.76100 1.000 29.45694 ? 42  LYS   A CG    1 
ATOM   345  C  CD    . LYS   A 1 43  ? -25.51500 12.23600 -14.93800 1.000 32.10767 ? 42  LYS   A CD    1 
ATOM   346  C  CE    . LYS   A 1 43  ? -26.04300 10.88900 -14.46800 1.000 37.08378 ? 42  LYS   A CE    1 
ATOM   347  N  NZ    . LYS   A 1 43  ? -26.52500 10.03900 -15.59100 1.000 38.05109 ? 42  LYS   A NZ    1 
ATOM   348  N  N     . GLN   A 1 44  ? -22.94800 13.70700 -11.31000 1.000 17.24896 ? 43  GLN   A N     1 
ATOM   349  C  CA    . GLN   A 1 44  ? -21.92600 12.85600 -10.71600 1.000 16.70939 ? 43  GLN   A CA    1 
ATOM   350  C  C     . GLN   A 1 44  ? -22.04100 11.44100 -11.27300 1.000 17.53615 ? 43  GLN   A C     1 
ATOM   351  O  O     . GLN   A 1 44  ? -23.12700 10.86000 -11.28500 1.000 19.21554 ? 43  GLN   A O     1 
ATOM   352  C  CB    . GLN   A 1 44  ? -22.11000 12.84000 -9.20200  1.000 19.18489 ? 43  GLN   A CB    1 
ATOM   353  C  CG    . GLN   A 1 44  ? -21.07800 12.04200 -8.44600  1.000 24.22541 ? 43  GLN   A CG    1 
ATOM   354  C  CD    . GLN   A 1 44  ? -21.37200 12.01100 -6.96500  1.000 28.50621 ? 43  GLN   A CD    1 
ATOM   355  O  OE1   . GLN   A 1 44  ? -21.85000 12.99300 -6.40300  1.000 28.94570 ? 43  GLN   A OE1   1 
ATOM   356  N  NE2   . GLN   A 1 44  ? -21.11100 10.87700 -6.32900  1.000 31.15299 ? 43  GLN   A NE2   1 
ATOM   357  N  N     . VAL   A 1 45  ? -20.91400 10.88000 -11.70900 1.000 18.05561 ? 44  VAL   A N     1 
ATOM   358  C  CA    . VAL   A 1 45  ? -20.85800 9.54400  -12.29500 1.000 16.90973 ? 44  VAL   A CA    1 
ATOM   359  C  C     . VAL   A 1 45  ? -19.59300 8.84700  -11.80400 1.000 17.42141 ? 44  VAL   A C     1 
ATOM   360  O  O     . VAL   A 1 45  ? -18.68600 9.46800  -11.24700 1.000 20.07526 ? 44  VAL   A O     1 
ATOM   361  C  CB    . VAL   A 1 45  ? -20.87200 9.58800  -13.84100 1.000 17.40918 ? 44  VAL   A CB    1 
ATOM   362  C  CG1   . VAL   A 1 45  ? -22.12100 10.27600 -14.36500 1.000 21.71684 ? 44  VAL   A CG1   1 
ATOM   363  C  CG2   . VAL   A 1 45  ? -19.62500 10.29300 -14.34900 1.000 21.18657 ? 44  VAL   A CG2   1 
ATOM   364  N  N     . VAL   A 1 46  ? -19.53500 7.53200  -12.01800 1.000 19.95625 ? 45  VAL   A N     1 
ATOM   365  C  CA    . VAL   A 1 46  ? -18.33200 6.74700  -11.75800 1.000 18.77784 ? 45  VAL   A CA    1 
ATOM   366  C  C     . VAL   A 1 46  ? -17.74100 6.34300  -13.09900 1.000 19.15923 ? 45  VAL   A C     1 
ATOM   367  O  O     . VAL   A 1 46  ? -18.43500 5.76100  -13.94200 1.000 20.83221 ? 45  VAL   A O     1 
ATOM   368  C  CB    . VAL   A 1 46  ? -18.62900 5.51600  -10.88500 1.000 21.92582 ? 45  VAL   A CB    1 
ATOM   369  C  CG1   . VAL   A 1 46  ? -17.38800 4.60900  -10.77300 1.000 23.66246 ? 45  VAL   A CG1   1 
ATOM   370  C  CG2   . VAL   A 1 46  ? -19.08700 5.95400  -9.49400  1.000 25.13262 ? 45  VAL   A CG2   1 
ATOM   371  N  N     . ILE   A 1 47  ? -16.46600 6.66000  -13.30000 1.000 18.95748 ? 46  ILE   A N     1 
ATOM   372  C  CA    . ILE   A 1 47  ? -15.75900 6.33100  -14.53200 1.000 19.37863 ? 46  ILE   A CA    1 
ATOM   373  C  C     . ILE   A 1 47  ? -14.44600 5.67400  -14.13300 1.000 20.51972 ? 46  ILE   A C     1 
ATOM   374  O  O     . ILE   A 1 47  ? -13.64500 6.27500  -13.40300 1.000 21.31403 ? 46  ILE   A O     1 
ATOM   375  C  CB    . ILE   A 1 47  ? -15.50000 7.58000  -15.39400 1.000 18.28867 ? 46  ILE   A CB    1 
ATOM   376  C  CG1   . ILE   A 1 47  ? -16.81300 8.25000  -15.80700 1.000 17.61978 ? 46  ILE   A CG1   1 
ATOM   377  C  CG2   . ILE   A 1 47  ? -14.68000 7.22700  -16.63100 1.000 19.78636 ? 46  ILE   A CG2   1 
ATOM   378  C  CD1   . ILE   A 1 47  ? -16.60300 9.58500  -16.46800 1.000 17.81794 ? 46  ILE   A CD1   1 
ATOM   379  N  N     . ASP   A 1 48  ? -14.22800 4.44100  -14.58900 1.000 21.59977 ? 47  ASP   A N     1 
ATOM   380  C  CA    . ASP   A 1 48  ? -13.00100 3.71100  -14.26300 1.000 24.09534 ? 47  ASP   A CA    1 
ATOM   381  C  C     . ASP   A 1 48  ? -12.79200 3.64800  -12.75500 1.000 25.60580 ? 47  ASP   A C     1 
ATOM   382  O  O     . ASP   A 1 48  ? -11.68000 3.82800  -12.25300 1.000 27.11962 ? 47  ASP   A O     1 
ATOM   383  C  CB    . ASP   A 1 48  ? -11.77600 4.30800  -14.96600 1.000 25.89670 ? 47  ASP   A CB    1 
ATOM   384  C  CG    . ASP   A 1 48  ? -11.92000 4.33700  -16.48000 1.000 30.71500 ? 47  ASP   A CG    1 
ATOM   385  O  OD1   . ASP   A 1 48  ? -12.76600 3.59200  -17.01900 1.000 31.60723 ? 47  ASP   A OD1   1 
ATOM   386  O  OD2   . ASP   A 1 48  ? -11.17600 5.09900  -17.13400 1.000 34.16789 ? 47  ASP   A OD2   1 
ATOM   387  N  N     . GLY   A 1 49  ? -13.88300 3.42200  -12.02500 1.000 25.63113 ? 48  GLY   A N     1 
ATOM   388  C  CA    . GLY   A 1 49  ? -13.82500 3.27100  -10.58800 1.000 24.92001 ? 48  GLY   A CA    1 
ATOM   389  C  C     . GLY   A 1 49  ? -13.64700 4.55500  -9.81100  1.000 27.72198 ? 48  GLY   A C     1 
ATOM   390  O  O     . GLY   A 1 49  ? -13.61700 4.51100  -8.57700  1.000 31.16270 ? 48  GLY   A O     1 
ATOM   391  N  N     . GLU   A 1 50  ? -13.52300 5.69200  -10.48300 1.000 25.63444 ? 49  GLU   A N     1 
ATOM   392  C  CA    . GLU   A 1 50  ? -13.31100 6.97100  -9.82400  1.000 23.91275 ? 49  GLU   A CA    1 
ATOM   393  C  C     . GLU   A 1 50  ? -14.58400 7.79800  -9.91800  1.000 20.39583 ? 49  GLU   A C     1 
ATOM   394  O  O     . GLU   A 1 50  ? -15.26100 7.79900  -10.95400 1.000 20.68587 ? 49  GLU   A O     1 
ATOM   395  C  CB    . GLU   A 1 50  ? -12.14500 7.73100  -10.47100 1.000 26.43787 ? 49  GLU   A CB    1 
ATOM   396  C  CG    . GLU   A 1 50  ? -10.84300 6.94000  -10.59500 1.000 31.51217 ? 49  GLU   A CG    1 
ATOM   397  C  CD    . GLU   A 1 50  ? -10.16100 6.68900  -9.25800  1.000 36.85911 ? 49  GLU   A CD    1 
ATOM   398  O  OE1   . GLU   A 1 50  ? -10.56400 7.29500  -8.24400  1.000 38.98467 ? 49  GLU   A OE1   1 
ATOM   399  O  OE2   . GLU   A 1 50  ? -9.21000  5.88000  -9.22600  1.000 42.72802 ? 49  GLU   A OE2   1 
ATOM   400  N  N     . THR   A 1 51  ? -14.89700 8.51800  -8.84500  1.000 20.25263 ? 50  THR   A N     1 
ATOM   401  C  CA    . THR   A 1 51  ? -16.05300 9.40600  -8.84400  1.000 18.52627 ? 50  THR   A CA    1 
ATOM   402  C  C     . THR   A 1 51  ? -15.73100 10.69800 -9.58500  1.000 18.72506 ? 50  THR   A C     1 
ATOM   403  O  O     . THR   A 1 51  ? -14.74800 11.38200 -9.27600  1.000 18.23887 ? 50  THR   A O     1 
ATOM   404  C  CB    . THR   A 1 51  ? -16.49700 9.70900  -7.41200  1.000 21.79408 ? 50  THR   A CB    1 
ATOM   405  O  OG1   . THR   A 1 51  ? -16.81000 8.47800  -6.75700  1.000 24.81096 ? 50  THR   A OG1   1 
ATOM   406  C  CG2   . THR   A 1 51  ? -17.73600 10.61300 -7.41800  1.000 23.12338 ? 50  THR   A CG2   1 
ATOM   407  N  N     . CYS   A 1 52  ? -16.59600 11.05300 -10.53500 1.000 18.10915 ? 51  CYS   A N     1 
ATOM   408  C  CA    . CYS   A 1 52  ? -16.37900 12.18300 -11.42300 1.000 15.95766 ? 51  CYS   A CA    1 
ATOM   409  C  C     . CYS   A 1 52  ? -17.59500 13.08700 -11.39700 1.000 17.52667 ? 51  CYS   A C     1 
ATOM   410  O  O     . CYS   A 1 52  ? -18.73300 12.61300 -11.43300 1.000 21.07525 ? 51  CYS   A O     1 
ATOM   411  C  CB    . CYS   A 1 52  ? -16.12700 11.72900 -12.87200 1.000 17.15635 ? 51  CYS   A CB    1 
ATOM   412  S  SG    . CYS   A 1 52  ? -14.65400 10.66900 -13.04200 1.000 19.09113 ? 51  CYS   A SG    1 
ATOM   413  N  N     . LEU   A 1 53  ? -17.34500 14.38400 -11.33100 1.000 14.83673 ? 52  LEU   A N     1 
ATOM   414  C  CA    . LEU   A 1 53  ? -18.37800 15.40500 -11.45900 1.000 14.23278 ? 52  LEU   A CA    1 
ATOM   415  C  C     . LEU   A 1 53  ? -18.25300 16.01500 -12.85500 1.000 14.18742 ? 52  LEU   A C     1 
ATOM   416  O  O     . LEU   A 1 53  ? -17.24600 16.65900 -13.17400 1.000 15.24962 ? 52  LEU   A O     1 
ATOM   417  C  CB    . LEU   A 1 53  ? -18.20100 16.45200 -10.36500 1.000 17.66303 ? 52  LEU   A CB    1 
ATOM   418  C  CG    . LEU   A 1 53  ? -19.30200 17.50200 -10.25100 1.000 19.84087 ? 52  LEU   A CG    1 
ATOM   419  C  CD1   . LEU   A 1 53  ? -20.65500 16.84300 -10.05200 1.000 23.32222 ? 52  LEU   A CD1   1 
ATOM   420  C  CD2   . LEU   A 1 53  ? -19.00500 18.40500 -9.08000  1.000 20.41555 ? 52  LEU   A CD2   1 
ATOM   421  N  N     . LEU   A 1 54  ? -19.26100 15.79100 -13.69800 1.000 14.52902 ? 53  LEU   A N     1 
ATOM   422  C  CA    . LEU   A 1 54  ? -19.22900 16.27200 -15.07000 1.000 16.85832 ? 53  LEU   A CA    1 
ATOM   423  C  C     . LEU   A 1 54  ? -19.97500 17.59200 -15.12900 1.000 15.58502 ? 53  LEU   A C     1 
ATOM   424  O  O     . LEU   A 1 54  ? -21.13900 17.66600 -14.71700 1.000 17.15167 ? 53  LEU   A O     1 
ATOM   425  C  CB    . LEU   A 1 54  ? -19.88300 15.26300 -16.01000 1.000 16.25601 ? 53  LEU   A CB    1 
ATOM   426  C  CG    . LEU   A 1 54  ? -19.40800 13.81700 -15.96000 1.000 19.71465 ? 53  LEU   A CG    1 
ATOM   427  C  CD1   . LEU   A 1 54  ? -20.06600 12.99900 -17.04700 1.000 20.85486 ? 53  LEU   A CD1   1 
ATOM   428  C  CD2   . LEU   A 1 54  ? -17.87800 13.69600 -16.05500 1.000 20.09115 ? 53  LEU   A CD2   1 
ATOM   429  N  N     . ASP   A 1 55  ? -19.29700 18.62900 -15.61900 1.000 13.92125 ? 54  ASP   A N     1 
ATOM   430  C  CA    . ASP   A 1 55  ? -19.93400 19.89300 -15.95100 1.000 17.47400 ? 54  ASP   A CA    1 
ATOM   431  C  C     . ASP   A 1 55  ? -20.06800 19.88000 -17.45900 1.000 16.44177 ? 54  ASP   A C     1 
ATOM   432  O  O     . ASP   A 1 55  ? -19.06100 19.77900 -18.16600 1.000 19.88171 ? 54  ASP   A O     1 
ATOM   433  C  CB    . ASP   A 1 55  ? -19.04200 21.08400 -15.59800 1.000 19.20944 ? 54  ASP   A CB    1 
ATOM   434  C  CG    . ASP   A 1 55  ? -18.69200 21.16200 -14.14700 1.000 29.39196 ? 54  ASP   A CG    1 
ATOM   435  O  OD1   . ASP   A 1 55  ? -19.43800 20.63900 -13.29400 1.000 34.55322 ? 54  ASP   A OD1   1 
ATOM   436  O  OD2   . ASP   A 1 55  ? -17.64800 21.78200 -13.87400 1.000 33.13833 ? 54  ASP   A OD2   1 
ATOM   437  N  N     . ILE   A 1 56  ? -21.28500 19.96100 -17.96500 1.000 15.08207 ? 55  ILE   A N     1 
ATOM   438  C  CA    . ILE   A 1 56  ? -21.48500 19.90200 -19.40700 1.000 14.48352 ? 55  ILE   A CA    1 
ATOM   439  C  C     . ILE   A 1 56  ? -22.07800 21.21700 -19.87800 1.000 13.60289 ? 55  ILE   A C     1 
ATOM   440  O  O     . ILE   A 1 56  ? -23.15400 21.61400 -19.41600 1.000 15.55500 ? 55  ILE   A O     1 
ATOM   441  C  CB    . ILE   A 1 56  ? -22.35600 18.70900 -19.82300 1.000 17.08775 ? 55  ILE   A CB    1 
ATOM   442  C  CG1   . ILE   A 1 56  ? -21.76000 17.41300 -19.25700 1.000 21.30985 ? 55  ILE   A CG1   1 
ATOM   443  C  CG2   . ILE   A 1 56  ? -22.46900 18.64500 -21.34900 1.000 18.24359 ? 55  ILE   A CG2   1 
ATOM   444  C  CD1   . ILE   A 1 56  ? -22.61400 16.23500 -19.48200 1.000 26.23851 ? 55  ILE   A CD1   1 
ATOM   445  N  N     . LEU   A 1 57  ? -21.39800 21.86100 -20.82700 1.000 12.56261 ? 56  LEU   A N     1 
ATOM   446  C  CA    . LEU   A 1 57  ? -21.89100 23.06500 -21.49000 1.000 11.67710 ? 56  LEU   A CA    1 
ATOM   447  C  C     . LEU   A 1 57  ? -22.41800 22.63500 -22.84900 1.000 11.63925 ? 56  LEU   A C     1 
ATOM   448  O  O     . LEU   A 1 57  ? -21.65600 22.17900 -23.71100 1.000 13.02385 ? 56  LEU   A O     1 
ATOM   449  C  CB    . LEU   A 1 57  ? -20.78200 24.09700 -21.63200 1.000 13.51162 ? 56  LEU   A CB    1 
ATOM   450  C  CG    . LEU   A 1 57  ? -21.20800 25.38200 -22.33200 1.000 15.98056 ? 56  LEU   A CG    1 
ATOM   451  C  CD1   . LEU   A 1 57  ? -22.22000 26.15400 -21.52400 1.000 17.97383 ? 56  LEU   A CD1   1 
ATOM   452  C  CD2   . LEU   A 1 57  ? -19.99200 26.23900 -22.57500 1.000 20.01718 ? 56  LEU   A CD2   1 
ATOM   453  N  N     . ASP   A 1 58  ? -23.72200 22.79000 -23.03500 1.000 12.18392 ? 57  ASP   A N     1 
ATOM   454  C  CA    . ASP   A 1 58  ? -24.39800 22.45100 -24.28300 1.000 13.37593 ? 57  ASP   A CA    1 
ATOM   455  C  C     . ASP   A 1 58  ? -24.53000 23.74300 -25.08900 1.000 13.25766 ? 57  ASP   A C     1 
ATOM   456  O  O     . ASP   A 1 58  ? -25.28100 24.64600 -24.70500 1.000 14.31815 ? 57  ASP   A O     1 
ATOM   457  C  CB    . ASP   A 1 58  ? -25.76000 21.85000 -23.93600 1.000 16.89393 ? 57  ASP   A CB    1 
ATOM   458  C  CG    . ASP   A 1 58  ? -26.53000 21.38000 -25.14900 1.000 16.44690 ? 57  ASP   A CG    1 
ATOM   459  O  OD1   . ASP   A 1 58  ? -25.92600 21.19400 -26.22900 1.000 16.45454 ? 57  ASP   A OD1   1 
ATOM   460  O  OD2   . ASP   A 1 58  ? -27.77400 21.20600 -25.03400 1.000 18.54123 ? 57  ASP   A OD2   1 
ATOM   461  N  N     . THR   A 1 59  ? -23.75600 23.86000 -26.16800 1.000 13.00345 ? 58  THR   A N     1 
ATOM   462  C  CA    . THR   A 1 59  ? -23.72300 25.08000 -26.96600 1.000 13.33009 ? 58  THR   A CA    1 
ATOM   463  C  C     . THR   A 1 59  ? -24.69600 25.00300 -28.13800 1.000 12.29119 ? 58  THR   A C     1 
ATOM   464  O  O     . THR   A 1 59  ? -25.13100 23.92600 -28.54600 1.000 14.02025 ? 58  THR   A O     1 
ATOM   465  C  CB    . THR   A 1 59  ? -22.31400 25.35300 -27.52300 1.000 13.97724 ? 58  THR   A CB    1 
ATOM   466  O  OG1   . THR   A 1 59  ? -22.00100 24.41000 -28.56100 1.000 14.83730 ? 58  THR   A OG1   1 
ATOM   467  C  CG2   . THR   A 1 59  ? -21.25900 25.31600 -26.42300 1.000 15.16273 ? 58  THR   A CG2   1 
ATOM   468  N  N     . ALA   A 1 60  ? -25.02600 26.17200 -28.68200 1.000 13.61994 ? 59  ALA   A N     1 
ATOM   469  C  CA    . ALA   A 1 60  ? -25.85200 26.24600 -29.87900 1.000 14.25679 ? 59  ALA   A CA    1 
ATOM   470  C  C     . ALA   A 1 60  ? -25.00700 25.93200 -31.11500 1.000 15.54882 ? 59  ALA   A C     1 
ATOM   471  O  O     . ALA   A 1 60  ? -23.80600 26.20400 -31.15600 1.000 17.30248 ? 59  ALA   A O     1 
ATOM   472  C  CB    . ALA   A 1 60  ? -26.43400 27.65000 -30.01500 1.000 15.69118 ? 59  ALA   A CB    1 
ATOM   473  N  N     . GLY   A 1 61  ? -25.63200 25.39700 -32.15300 1.000 16.16143 ? 60  GLY   A N     1 
ATOM   474  C  CA    . GLY   A 1 61  ? -24.91400 25.13200 -33.41500 1.000 20.02324 ? 60  GLY   A CA    1 
ATOM   475  C  C     . GLY   A 1 61  ? -24.77100 26.35100 -34.30600 1.000 30.06866 ? 60  GLY   A C     1 
ATOM   476  O  O     . GLY   A 1 61  ? -24.71600 26.17400 -35.51800 1.000 39.49704 ? 60  GLY   A O     1 
ATOM   477  N  N     . GLN   A 1 62  ? -24.74100 27.54100 -33.74500 1.000 31.24008 ? 61  GLN   A N     1 
ATOM   478  C  CA    . GLN   A 1 62  ? -24.51400 28.74400 -34.53000 1.000 35.94772 ? 61  GLN   A CA    1 
ATOM   479  C  C     . GLN   A 1 62  ? -23.04700 29.15200 -34.43800 1.000 37.69711 ? 61  GLN   A C     1 
ATOM   480  O  O     . GLN   A 1 62  ? -22.33600 28.78000 -33.50500 1.000 38.68048 ? 61  GLN   A O     1 
ATOM   481  C  CB    . GLN   A 1 62  ? -25.41600 29.87200 -34.02800 1.000 39.75882 ? 61  GLN   A CB    1 
ATOM   482  C  CG    . GLN   A 1 62  ? -25.17200 30.28000 -32.59500 1.000 43.54748 ? 61  GLN   A CG    1 
ATOM   483  C  CD    . GLN   A 1 62  ? -24.08600 31.32800 -32.48100 1.000 48.09867 ? 61  GLN   A CD    1 
ATOM   484  O  OE1   . GLN   A 1 62  ? -23.99300 32.22900 -33.31600 1.000 51.32194 ? 61  GLN   A OE1   1 
ATOM   485  N  NE2   . GLN   A 1 62  ? -23.24400 31.20600 -31.46300 1.000 49.06960 ? 61  GLN   A NE2   1 
ATOM   486  N  N     . GLU   A 1 63  ? -22.59700 29.93700 -35.41400 1.000 42.88760 ? 62  GLU   A N     1 
ATOM   487  C  CA    . GLU   A 1 63  ? -21.20300 30.36100 -35.44700 1.000 50.40048 ? 62  GLU   A CA    1 
ATOM   488  C  C     . GLU   A 1 63  ? -20.98900 31.86400 -35.33000 1.000 48.71845 ? 62  GLU   A C     1 
ATOM   489  O  O     . GLU   A 1 63  ? -19.84100 32.31300 -35.42400 1.000 49.75522 ? 62  GLU   A O     1 
ATOM   490  C  CB    . GLU   A 1 63  ? -20.49800 29.83500 -36.70700 1.000 59.87040 ? 62  GLU   A CB    1 
ATOM   491  C  CG    . GLU   A 1 63  ? -21.38600 29.72300 -37.93900 1.000 68.79393 ? 62  GLU   A CG    1 
ATOM   492  C  CD    . GLU   A 1 63  ? -21.75500 28.28400 -38.25500 1.000 75.85168 ? 62  GLU   A CD    1 
ATOM   493  O  OE1   . GLU   A 1 63  ? -21.84000 27.47300 -37.31000 1.000 78.96979 ? 62  GLU   A OE1   1 
ATOM   494  O  OE2   . GLU   A 1 63  ? -21.94800 27.96200 -39.44800 1.000 77.98478 ? 62  GLU   A OE2   1 
ATOM   495  N  N     . GLU   A 1 64  ? -22.04100 32.65200 -35.09700 1.000 45.76920 ? 63  GLU   A N     1 
ATOM   496  C  CA    . GLU   A 1 64  ? -21.93400 34.09900 -35.27400 1.000 47.56325 ? 63  GLU   A CA    1 
ATOM   497  C  C     . GLU   A 1 64  ? -21.16500 34.77400 -34.13900 1.000 43.33582 ? 63  GLU   A C     1 
ATOM   498  O  O     . GLU   A 1 64  ? -20.38000 35.69800 -34.38300 1.000 48.36918 ? 63  GLU   A O     1 
ATOM   499  C  CB    . GLU   A 1 64  ? -23.32400 34.71600 -35.43900 1.000 53.81168 ? 63  GLU   A CB    1 
ATOM   500  C  CG    . GLU   A 1 64  ? -24.11500 34.15900 -36.61500 1.000 59.17318 ? 63  GLU   A CG    1 
ATOM   501  C  CD    . GLU   A 1 64  ? -25.51300 34.74200 -36.71000 1.000 63.98772 ? 63  GLU   A CD    1 
ATOM   502  O  OE1   . GLU   A 1 64  ? -25.73800 35.84600 -36.16700 1.000 64.87717 ? 63  GLU   A OE1   1 
ATOM   503  O  OE2   . GLU   A 1 64  ? -26.38800 34.09300 -37.32500 1.000 65.60750 ? 63  GLU   A OE2   1 
ATOM   504  N  N     . TYR   A 1 65  ? -21.36200 34.32600 -32.89900 1.000 33.97711 ? 64  TYR   A N     1 
ATOM   505  C  CA    . TYR   A 1 65  ? -20.90400 35.04800 -31.70300 1.000 29.46090 ? 64  TYR   A CA    1 
ATOM   506  C  C     . TYR   A 1 65  ? -19.53300 34.53300 -31.26900 1.000 26.71649 ? 64  TYR   A C     1 
ATOM   507  O  O     . TYR   A 1 65  ? -19.38800 33.76400 -30.31800 1.000 26.82679 ? 64  TYR   A O     1 
ATOM   508  C  CB    . TYR   A 1 65  ? -21.95900 34.93500 -30.59600 1.000 26.56154 ? 64  TYR   A CB    1 
ATOM   509  C  CG    . TYR   A 1 65  ? -23.26900 35.51500 -31.06900 1.000 24.19902 ? 64  TYR   A CG    1 
ATOM   510  C  CD1   . TYR   A 1 65  ? -23.43700 36.88100 -31.14100 1.000 25.67047 ? 64  TYR   A CD1   1 
ATOM   511  C  CD2   . TYR   A 1 65  ? -24.30100 34.69800 -31.51100 1.000 26.12049 ? 64  TYR   A CD2   1 
ATOM   512  C  CE1   . TYR   A 1 65  ? -24.61400 37.43100 -31.62000 1.000 26.20429 ? 64  TYR   A CE1   1 
ATOM   513  C  CE2   . TYR   A 1 65  ? -25.49200 35.23600 -31.97900 1.000 23.50885 ? 64  TYR   A CE2   1 
ATOM   514  C  CZ    . TYR   A 1 65  ? -25.63600 36.60500 -32.04200 1.000 23.72397 ? 64  TYR   A CZ    1 
ATOM   515  O  OH    . TYR   A 1 65  ? -26.79600 37.16900 -32.51500 1.000 24.06440 ? 64  TYR   A OH    1 
ATOM   516  N  N     . SER   A 1 66  ? -18.50000 35.00900 -31.96700 1.000 26.38665 ? 65  SER   A N     1 
ATOM   517  C  CA    . SER   A 1 66  ? -17.16400 34.45700 -31.76600 1.000 27.00859 ? 65  SER   A CA    1 
ATOM   518  C  C     . SER   A 1 66  ? -16.58500 34.81700 -30.40100 1.000 24.96643 ? 65  SER   A C     1 
ATOM   519  O  O     . SER   A 1 66  ? -15.84100 34.02000 -29.82700 1.000 25.89962 ? 65  SER   A O     1 
ATOM   520  C  CB    . SER   A 1 66  ? -16.22500 34.88100 -32.89800 1.000 30.90615 ? 65  SER   A CB    1 
ATOM   521  O  OG    . SER   A 1 66  ? -15.93800 36.26600 -32.83700 1.000 35.85776 ? 65  SER   A OG    1 
ATOM   522  N  N     . ALA   A 1 67  ? -16.89800 35.99900 -29.86400 1.000 26.26070 ? 66  ALA   A N     1 
ATOM   523  C  CA    . ALA   A 1 67  ? -16.38500 36.35100 -28.54300 1.000 26.45391 ? 66  ALA   A CA    1 
ATOM   524  C  C     . ALA   A 1 67  ? -16.85700 35.34800 -27.50000 1.000 23.54576 ? 66  ALA   A C     1 
ATOM   525  O  O     . ALA   A 1 67  ? -16.06100 34.83000 -26.71100 1.000 24.24219 ? 66  ALA   A O     1 
ATOM   526  C  CB    . ALA   A 1 67  ? -16.80500 37.77000 -28.16000 1.000 29.32553 ? 66  ALA   A CB    1 
ATOM   527  N  N     A MET   A 1 68  ? -18.15700 35.05400 -27.49300 0.380 21.56096 ? 67  MET   A N     1 
ATOM   528  N  N     B MET   A 1 68  ? -18.15700 35.05000 -27.49200 0.620 21.48522 ? 67  MET   A N     1 
ATOM   529  C  CA    A MET   A 1 68  ? -18.70300 34.08300 -26.54900 0.380 20.06944 ? 67  MET   A CA    1 
ATOM   530  C  CA    B MET   A 1 68  ? -18.69000 34.08300 -26.53500 0.620 19.93660 ? 67  MET   A CA    1 
ATOM   531  C  C     A MET   A 1 68  ? -18.15300 32.68400 -26.80900 0.380 18.76592 ? 67  MET   A C     1 
ATOM   532  C  C     B MET   A 1 68  ? -18.15300 32.67900 -26.80600 0.620 18.37952 ? 67  MET   A C     1 
ATOM   533  O  O     A MET   A 1 68  ? -17.73500 31.98300 -25.87900 0.380 18.83641 ? 67  MET   A O     1 
ATOM   534  O  O     B MET   A 1 68  ? -17.74600 31.96600 -25.87900 0.620 19.92570 ? 67  MET   A O     1 
ATOM   535  C  CB    A MET   A 1 68  ? -20.22600 34.08700 -26.65100 0.380 22.15038 ? 67  MET   A CB    1 
ATOM   536  C  CB    B MET   A 1 68  ? -20.21700 34.09300 -26.58800 0.620 21.73123 ? 67  MET   A CB    1 
ATOM   537  C  CG    A MET   A 1 68  ? -20.86600 35.27900 -25.97800 0.380 21.58093 ? 67  MET   A CG    1 
ATOM   538  C  CG    B MET   A 1 68  ? -20.85700 33.29400 -25.46500 0.620 19.78290 ? 67  MET   A CG    1 
ATOM   539  S  SD    A MET   A 1 68  ? -20.83200 35.11300 -24.18700 0.380 24.10899 ? 67  MET   A SD    1 
ATOM   540  S  SD    B MET   A 1 68  ? -20.54600 34.02500 -23.84000 0.620 20.86781 ? 67  MET   A SD    1 
ATOM   541  C  CE    A MET   A 1 68  ? -21.79500 33.61500 -23.98200 0.380 25.37254 ? 67  MET   A CE    1 
ATOM   542  C  CE    B MET   A 1 68  ? -21.90600 35.19100 -23.75700 0.620 21.71196 ? 67  MET   A CE    1 
ATOM   543  N  N     . ARG   A 1 69  ? -18.15800 32.25500 -28.07100 1.000 18.40833 ? 68  ARG   A N     1 
ATOM   544  C  CA    . ARG   A 1 69  ? -17.70200 30.90900 -28.39100 1.000 19.25391 ? 68  ARG   A CA    1 
ATOM   545  C  C     . ARG   A 1 69  ? -16.22700 30.71400 -28.05600 1.000 16.59672 ? 68  ARG   A C     1 
ATOM   546  O  O     . ARG   A 1 69  ? -15.82800 29.63700 -27.59000 1.000 16.75033 ? 68  ARG   A O     1 
ATOM   547  C  CB    . ARG   A 1 69  ? -18.01700 30.58900 -29.84500 1.000 23.68923 ? 68  ARG   A CB    1 
ATOM   548  C  CG    . ARG   A 1 69  ? -19.52100 30.57600 -30.08800 1.000 29.08672 ? 68  ARG   A CG    1 
ATOM   549  C  CD    . ARG   A 1 69  ? -19.87700 29.99500 -31.43900 1.000 31.96028 ? 68  ARG   A CD    1 
ATOM   550  N  NE    . ARG   A 1 69  ? -19.31100 28.66300 -31.59300 1.000 32.52745 ? 68  ARG   A NE    1 
ATOM   551  C  CZ    . ARG   A 1 69  ? -19.90700 27.54200 -31.20400 1.000 34.54389 ? 68  ARG   A CZ    1 
ATOM   552  N  NH1   . ARG   A 1 69  ? -21.11500 27.55100 -30.66000 1.000 36.26238 ? 68  ARG   A NH1   1 
ATOM   553  N  NH2   . ARG   A 1 69  ? -19.27500 26.38300 -31.36300 1.000 33.76686 ? 68  ARG   A NH2   1 
ATOM   554  N  N     . ASP   A 1 70  ? -15.40000 31.73900 -28.26900 1.000 17.40775 ? 69  ASP   A N     1 
ATOM   555  C  CA    . ASP   A 1 70  ? -14.00700 31.62300 -27.86000 1.000 16.00421 ? 69  ASP   A CA    1 
ATOM   556  C  C     . ASP   A 1 70  ? -13.88900 31.42500 -26.35300 1.000 16.52798 ? 69  ASP   A C     1 
ATOM   557  O  O     . ASP   A 1 70  ? -13.05000 30.64500 -25.88900 1.000 15.56016 ? 69  ASP   A O     1 
ATOM   558  C  CB    . ASP   A 1 70  ? -13.22000 32.87000 -28.26500 1.000 17.75801 ? 69  ASP   A CB    1 
ATOM   559  C  CG    . ASP   A 1 70  ? -12.98600 32.97700 -29.76700 1.000 22.39971 ? 69  ASP   A CG    1 
ATOM   560  O  OD1   . ASP   A 1 70  ? -13.33700 32.04600 -30.52600 1.000 24.27336 ? 69  ASP   A OD1   1 
ATOM   561  O  OD2   . ASP   A 1 70  ? -12.44100 34.01800 -30.17700 1.000 24.98463 ? 69  ASP   A OD2   1 
ATOM   562  N  N     . GLN   A 1 71  ? -14.70300 32.13600 -25.56200 1.000 15.85342 ? 70  GLN   A N     1 
ATOM   563  C  CA    . GLN   A 1 71  ? -14.65000 31.93700 -24.11500 1.000 15.04102 ? 70  GLN   A CA    1 
ATOM   564  C  C     . GLN   A 1 71  ? -15.08500 30.52500 -23.73000 1.000 13.61809 ? 70  GLN   A C     1 
ATOM   565  O  O     . GLN   A 1 71  ? -14.49100 29.91700 -22.84000 1.000 13.83587 ? 70  GLN   A O     1 
ATOM   566  C  CB    . GLN   A 1 71  ? -15.43400 33.01500 -23.35100 1.000 17.20333 ? 70  GLN   A CB    1 
ATOM   567  C  CG    . GLN   A 1 71  ? -15.18300 32.93900 -21.84700 1.000 18.62841 ? 70  GLN   A CG    1 
ATOM   568  C  CD    . GLN   A 1 71  ? -13.71000 33.14800 -21.48600 1.000 17.17703 ? 70  GLN   A CD    1 
ATOM   569  O  OE1   . GLN   A 1 71  ? -13.08700 34.13600 -21.88100 1.000 19.25837 ? 70  GLN   A OE1   1 
ATOM   570  N  NE2   . GLN   A 1 71  ? -13.14800 32.21100 -20.74600 1.000 18.68984 ? 70  GLN   A NE2   1 
ATOM   571  N  N     . TYR   A 1 72  ? -16.09800 29.97300 -24.40700 1.000 13.67800 ? 71  TYR   A N     1 
ATOM   572  C  CA    . TYR   A 1 72  ? -16.44900 28.57000 -24.17500 1.000 14.58954 ? 71  TYR   A CA    1 
ATOM   573  C  C     . TYR   A 1 72  ? -15.22900 27.67600 -24.35700 1.000 13.59174 ? 71  TYR   A C     1 
ATOM   574  O  O     . TYR   A 1 72  ? -15.00000 26.74100 -23.58000 1.000 13.80011 ? 71  TYR   A O     1 
ATOM   575  C  CB    . TYR   A 1 72  ? -17.48500 28.10600 -25.19900 1.000 15.37815 ? 71  TYR   A CB    1 
ATOM   576  C  CG    . TYR   A 1 72  ? -18.87500 28.71700 -25.17400 1.000 15.23378 ? 71  TYR   A CG    1 
ATOM   577  C  CD1   . TYR   A 1 72  ? -19.37500 29.38800 -24.05900 1.000 15.73838 ? 71  TYR   A CD1   1 
ATOM   578  C  CD2   . TYR   A 1 72  ? -19.69900 28.58700 -26.28100 1.000 15.29134 ? 71  TYR   A CD2   1 
ATOM   579  C  CE1   . TYR   A 1 72  ? -20.67700 29.91300 -24.06300 1.000 15.30818 ? 71  TYR   A CE1   1 
ATOM   580  C  CE2   . TYR   A 1 72  ? -20.99300 29.09200 -26.29500 1.000 14.90388 ? 71  TYR   A CE2   1 
ATOM   581  C  CZ    . TYR   A 1 72  ? -21.47000 29.75500 -25.19200 1.000 14.60956 ? 71  TYR   A CZ    1 
ATOM   582  O  OH    . TYR   A 1 72  ? -22.77000 30.23700 -25.23500 1.000 15.53029 ? 71  TYR   A OH    1 
ATOM   583  N  N     . MET   A 1 73  ? -14.44600 27.94000 -25.40700 1.000 14.46295 ? 72  MET   A N     1 
ATOM   584  C  CA    . MET   A 1 73  ? -13.29000 27.10500 -25.70800 1.000 12.82967 ? 72  MET   A CA    1 
ATOM   585  C  C     . MET   A 1 73  ? -12.14600 27.34100 -24.73400 1.000 12.90026 ? 72  MET   A C     1 
ATOM   586  O  O     . MET   A 1 73  ? -11.47000 26.39000 -24.34900 1.000 14.51732 ? 72  MET   A O     1 
ATOM   587  C  CB    . MET   A 1 73  ? -12.87600 27.32500 -27.15400 1.000 15.01277 ? 72  MET   A CB    1 
ATOM   588  C  CG    . MET   A 1 73  ? -13.97200 26.85300 -28.08900 1.000 16.86271 ? 72  MET   A CG    1 
ATOM   589  S  SD    . MET   A 1 73  ? -13.55400 27.14000 -29.80000 1.000 19.03902 ? 72  MET   A SD    1 
ATOM   590  C  CE    . MET   A 1 73  ? -15.00300 26.47100 -30.60800 1.000 22.16047 ? 72  MET   A CE    1 
ATOM   591  N  N     . ARG   A 1 74  ? -11.94400 28.58500 -24.29400 1.000 13.34247 ? 73  ARG   A N     1 
ATOM   592  C  CA    . ARG   A 1 74  ? -10.89400 28.85000 -23.31400 1.000 15.02249 ? 73  ARG   A CA    1 
ATOM   593  C  C     . ARG   A 1 74  ? -11.16100 28.12600 -22.00500 1.000 15.88947 ? 73  ARG   A C     1 
ATOM   594  O  O     . ARG   A 1 74  ? -10.24500 27.52700 -21.41600 1.000 16.68809 ? 73  ARG   A O     1 
ATOM   595  C  CB    . ARG   A 1 74  ? -10.74400 30.35600 -23.07600 1.000 18.14960 ? 73  ARG   A CB    1 
ATOM   596  C  CG    . ARG   A 1 74  ? -9.88300  31.06900 -24.11200 1.000 21.30732 ? 73  ARG   A CG    1 
ATOM   597  C  CD    . ARG   A 1 74  ? -9.50300  32.46400 -23.64400 1.000 23.37291 ? 73  ARG   A CD    1 
ATOM   598  N  NE    . ARG   A 1 74  ? -10.65500 33.35300 -23.61500 1.000 24.28996 ? 73  ARG   A NE    1 
ATOM   599  C  CZ    . ARG   A 1 74  ? -11.05700 34.08800 -24.64200 1.000 27.57574 ? 73  ARG   A CZ    1 
ATOM   600  N  NH1   . ARG   A 1 74  ? -10.41100 34.07200 -25.80100 1.000 24.71509 ? 73  ARG   A NH1   1 
ATOM   601  N  NH2   . ARG   A 1 74  ? -12.13100 34.86400 -24.50200 1.000 27.60255 ? 73  ARG   A NH2   1 
ATOM   602  N  N     . THR   A 1 75  ? -12.40400 28.18500 -21.52400 1.000 14.56048 ? 74  THR   A N     1 
ATOM   603  C  CA    . THR   A 1 75  ? -12.76100 27.57500 -20.24100 1.000 15.96750 ? 74  THR   A CA    1 
ATOM   604  C  C     . THR   A 1 75  ? -12.86500 26.04800 -20.33500 1.000 14.71682 ? 74  THR   A C     1 
ATOM   605  O  O     . THR   A 1 75  ? -12.51700 25.33200 -19.38700 1.000 16.20033 ? 74  THR   A O     1 
ATOM   606  C  CB    . THR   A 1 75  ? -14.07800 28.21200 -19.73600 1.000 16.34557 ? 74  THR   A CB    1 
ATOM   607  O  OG1   . THR   A 1 75  ? -13.85400 29.59900 -19.47300 1.000 19.39579 ? 74  THR   A OG1   1 
ATOM   608  C  CG2   . THR   A 1 75  ? -14.59900 27.52200 -18.46800 1.000 20.72889 ? 74  THR   A CG2   1 
ATOM   609  N  N     . GLY   A 1 76  ? -13.37400 25.53200 -21.45000 1.000 13.88707 ? 75  GLY   A N     1 
ATOM   610  C  CA    . GLY   A 1 76  ? -13.61100 24.09900 -21.55400 1.000 13.65226 ? 75  GLY   A CA    1 
ATOM   611  C  C     . GLY   A 1 76  ? -12.31600 23.30400 -21.52500 1.000 13.86190 ? 75  GLY   A C     1 
ATOM   612  O  O     . GLY   A 1 76  ? -11.28800 23.72900 -22.05100 1.000 14.88147 ? 75  GLY   A O     1 
ATOM   613  N  N     . GLU   A 1 77  ? -12.37900 22.11800 -20.91800 1.000 12.09736 ? 76  GLU   A N     1 
ATOM   614  C  CA    . GLU   A 1 77  ? -11.23200 21.22000 -20.85300 1.000 13.08596 ? 76  GLU   A CA    1 
ATOM   615  C  C     . GLU   A 1 77  ? -11.25500 20.14000 -21.92300 1.000 13.33906 ? 76  GLU   A C     1 
ATOM   616  O  O     . GLU   A 1 77  ? -10.19100 19.66600 -22.33700 1.000 15.67796 ? 76  GLU   A O     1 
ATOM   617  C  CB    . GLU   A 1 77  ? -11.17200 20.57600 -19.45900 1.000 15.34136 ? 76  GLU   A CB    1 
ATOM   618  C  CG    . GLU   A 1 77  ? -10.80100 21.59600 -18.38900 1.000 19.81007 ? 76  GLU   A CG    1 
ATOM   619  C  CD    . GLU   A 1 77  ? -10.94300 21.09800 -16.96900 1.000 23.02350 ? 76  GLU   A CD    1 
ATOM   620  O  OE1   . GLU   A 1 77  ? -11.83600 20.27100 -16.69000 1.000 22.40650 ? 76  GLU   A OE1   1 
ATOM   621  O  OE2   . GLU   A 1 77  ? -10.14300 21.55500 -16.12700 1.000 24.43902 ? 76  GLU   A OE2   1 
ATOM   622  N  N     . GLY   A 1 78  ? -12.43000 19.72400 -22.36000 1.000 11.95243 ? 77  GLY   A N     1 
ATOM   623  C  CA    . GLY   A 1 78  ? -12.55000 18.71500 -23.40400 1.000 12.94850 ? 77  GLY   A CA    1 
ATOM   624  C  C     . GLY   A 1 78  ? -13.78600 18.98900 -24.22200 1.000 12.16502 ? 77  GLY   A C     1 
ATOM   625  O  O     . GLY   A 1 78  ? -14.75500 19.57200 -23.72400 1.000 12.10491 ? 77  GLY   A O     1 
ATOM   626  N  N     . PHE   A 1 79  ? -13.74100 18.59200 -25.50000 1.000 11.30239 ? 78  PHE   A N     1 
ATOM   627  C  CA    . PHE   A 1 79  ? -14.76200 18.95000 -26.48800 1.000 11.73136 ? 78  PHE   A CA    1 
ATOM   628  C  C     . PHE   A 1 79  ? -15.32000 17.70500 -27.15100 1.000 12.19099 ? 78  PHE   A C     1 
ATOM   629  O  O     . PHE   A 1 79  ? -14.56200 16.88000 -27.68300 1.000 13.39089 ? 78  PHE   A O     1 
ATOM   630  C  CB    . PHE   A 1 79  ? -14.20200 19.95500 -27.50300 1.000 12.45573 ? 78  PHE   A CB    1 
ATOM   631  C  CG    . PHE   A 1 79  ? -13.69200 21.17700 -26.82700 1.000 12.38522 ? 78  PHE   A CG    1 
ATOM   632  C  CD1   . PHE   A 1 79  ? -12.40600 21.21600 -26.29000 1.000 13.52611 ? 78  PHE   A CD1   1 
ATOM   633  C  CD2   . PHE   A 1 79  ? -14.53700 22.26600 -26.62500 1.000 12.63720 ? 78  PHE   A CD2   1 
ATOM   634  C  CE1   . PHE   A 1 79  ? -11.97600 22.33500 -25.58000 1.000 13.12561 ? 78  PHE   A CE1   1 
ATOM   635  C  CE2   . PHE   A 1 79  ? -14.10000 23.39600 -25.92100 1.000 13.30026 ? 78  PHE   A CE2   1 
ATOM   636  C  CZ    . PHE   A 1 79  ? -12.82000 23.43000 -25.40800 1.000 13.24981 ? 78  PHE   A CZ    1 
ATOM   637  N  N     . LEU   A 1 80  ? -16.64400 17.56800 -27.10300 1.000 11.93838 ? 79  LEU   A N     1 
ATOM   638  C  CA    . LEU   A 1 80  ? -17.35400 16.54800 -27.86200 1.000 12.99829 ? 79  LEU   A CA    1 
ATOM   639  C  C     . LEU   A 1 80  ? -17.74500 17.22200 -29.16800 1.000 12.81234 ? 79  LEU   A C     1 
ATOM   640  O  O     . LEU   A 1 80  ? -18.56600 18.14400 -29.16600 1.000 14.42770 ? 79  LEU   A O     1 
ATOM   641  C  CB    . LEU   A 1 80  ? -18.60600 16.11300 -27.10300 1.000 16.59427 ? 79  LEU   A CB    1 
ATOM   642  C  CG    . LEU   A 1 80  ? -19.06800 14.67500 -27.22300 1.000 21.60211 ? 79  LEU   A CG    1 
ATOM   643  C  CD1   . LEU   A 1 80  ? -18.03000 13.69000 -26.64400 1.000 20.97410 ? 79  LEU   A CD1   1 
ATOM   644  C  CD2   . LEU   A 1 80  ? -20.40000 14.56000 -26.51900 1.000 22.62513 ? 79  LEU   A CD2   1 
ATOM   645  N  N     . CYS   A 1 81  ? -17.12700 16.79100 -30.27900 1.000 13.11391 ? 80  CYS   A N     1 
ATOM   646  C  CA    . CYS   A 1 81  ? -17.37100 17.39700 -31.58500 1.000 13.47017 ? 80  CYS   A CA    1 
ATOM   647  C  C     . CYS   A 1 81  ? -18.33100 16.49500 -32.34000 1.000 12.79898 ? 80  CYS   A C     1 
ATOM   648  O  O     . CYS   A 1 81  ? -17.94700 15.42300 -32.80400 1.000 13.18695 ? 80  CYS   A O     1 
ATOM   649  C  CB    . CYS   A 1 81  ? -16.06700 17.57300 -32.35400 1.000 14.98681 ? 80  CYS   A CB    1 
ATOM   650  S  SG    . CYS   A 1 81  ? -14.90800 18.70000 -31.54300 1.000 17.67153 ? 80  CYS   A SG    1 
ATOM   651  N  N     . VAL   A 1 82  ? -19.57900 16.93300 -32.45400 1.000 13.11390 ? 81  VAL   A N     1 
ATOM   652  C  CA    . VAL   A 1 82  ? -20.67200 16.08200 -32.91300 1.000 12.81991 ? 81  VAL   A CA    1 
ATOM   653  C  C     . VAL   A 1 82  ? -21.02400 16.42400 -34.35400 1.000 13.44529 ? 81  VAL   A C     1 
ATOM   654  O  O     . VAL   A 1 82  ? -21.17100 17.60400 -34.70900 1.000 14.27651 ? 81  VAL   A O     1 
ATOM   655  C  CB    . VAL   A 1 82  ? -21.90500 16.25500 -32.00900 1.000 12.78249 ? 81  VAL   A CB    1 
ATOM   656  C  CG1   . VAL   A 1 82  ? -22.98400 15.26800 -32.40800 1.000 14.46944 ? 81  VAL   A CG1   1 
ATOM   657  C  CG2   . VAL   A 1 82  ? -21.52800 16.05000 -30.53400 1.000 14.24016 ? 81  VAL   A CG2   1 
ATOM   658  N  N     . PHE   A 1 83  ? -21.19400 15.39100 -35.17700 1.000 12.99491 ? 82  PHE   A N     1 
ATOM   659  C  CA    . PHE   A 1 83  ? -21.84900 15.53300 -36.47300 1.000 13.22822 ? 82  PHE   A CA    1 
ATOM   660  C  C     . PHE   A 1 83  ? -22.93400 14.46900 -36.54500 1.000 13.42340 ? 82  PHE   A C     1 
ATOM   661  O  O     . PHE   A 1 83  ? -22.98600 13.57700 -35.70500 1.000 14.59243 ? 82  PHE   A O     1 
ATOM   662  C  CB    . PHE   A 1 83  ? -20.88200 15.40500 -37.66300 1.000 13.97436 ? 82  PHE   A CB    1 
ATOM   663  C  CG    . PHE   A 1 83  ? -20.33700 14.00800 -37.87500 1.000 14.77713 ? 82  PHE   A CG    1 
ATOM   664  C  CD1   . PHE   A 1 83  ? -19.25900 13.55100 -37.13200 1.000 15.61897 ? 82  PHE   A CD1   1 
ATOM   665  C  CD2   . PHE   A 1 83  ? -20.87600 13.16600 -38.83900 1.000 14.41119 ? 82  PHE   A CD2   1 
ATOM   666  C  CE1   . PHE   A 1 83  ? -18.74200 12.27800 -37.32800 1.000 15.67876 ? 82  PHE   A CE1   1 
ATOM   667  C  CE2   . PHE   A 1 83  ? -20.37100 11.88900 -39.02300 1.000 16.24363 ? 82  PHE   A CE2   1 
ATOM   668  C  CZ    . PHE   A 1 83  ? -19.29900 11.44700 -38.27000 1.000 14.87863 ? 82  PHE   A CZ    1 
ATOM   669  N  N     . ALA   A 1 84  ? -23.82300 14.56700 -37.53400 1.000 13.84328 ? 83  ALA   A N     1 
ATOM   670  C  CA    . ALA   A 1 84  ? -24.87100 13.57100 -37.72900 1.000 14.79851 ? 83  ALA   A CA    1 
ATOM   671  C  C     . ALA   A 1 84  ? -24.54100 12.74800 -38.96000 1.000 14.22507 ? 83  ALA   A C     1 
ATOM   672  O  O     . ALA   A 1 84  ? -24.17600 13.30500 -40.00300 1.000 14.68696 ? 83  ALA   A O     1 
ATOM   673  C  CB    . ALA   A 1 84  ? -26.23800 14.23300 -37.91300 1.000 15.45095 ? 83  ALA   A CB    1 
ATOM   674  N  N     . ILE   A 1 85  ? -24.70000 11.42500 -38.85000 1.000 14.99542 ? 84  ILE   A N     1 
ATOM   675  C  CA    . ILE   A 1 85  ? -24.29200 10.52100 -39.92800 1.000 16.70353 ? 84  ILE   A CA    1 
ATOM   676  C  C     . ILE   A 1 85  ? -25.15100 10.65300 -41.17200 1.000 17.88562 ? 84  ILE   A C     1 
ATOM   677  O  O     . ILE   A 1 85  ? -24.79800 10.08000 -42.21500 1.000 18.98224 ? 84  ILE   A O     1 
ATOM   678  C  CB    . ILE   A 1 85  ? -24.16700 9.06000  -39.44900 1.000 18.78097 ? 84  ILE   A CB    1 
ATOM   679  C  CG1   . ILE   A 1 85  ? -25.49300 8.54200  -38.89300 1.000 21.64384 ? 84  ILE   A CG1   1 
ATOM   680  C  CG2   . ILE   A 1 85  ? -23.07000 8.95800  -38.38600 1.000 19.67649 ? 84  ILE   A CG2   1 
ATOM   681  C  CD1   . ILE   A 1 85  ? -26.41300 7.90400  -39.92200 1.000 24.93589 ? 84  ILE   A CD1   1 
ATOM   682  N  N     . ASN   A 1 86  ? -26.27300 11.37000 -41.08600 1.000 16.65762 ? 85  ASN   A N     1 
ATOM   683  C  CA    . ASN   A 1 86  ? -27.11700 11.64200 -42.24400 1.000 16.69061 ? 85  ASN   A CA    1 
ATOM   684  C  C     . ASN   A 1 86  ? -27.04100 13.10000 -42.67700 1.000 15.86771 ? 85  ASN   A C     1 
ATOM   685  O  O     . ASN   A 1 86  ? -27.94000 13.58100 -43.37100 1.000 17.28050 ? 85  ASN   A O     1 
ATOM   686  C  CB    . ASN   A 1 86  ? -28.56200 11.22400 -41.97800 1.000 18.52665 ? 85  ASN   A CB    1 
ATOM   687  C  CG    . ASN   A 1 86  ? -29.21900 12.02800 -40.87200 1.000 17.86507 ? 85  ASN   A CG    1 
ATOM   688  O  OD1   . ASN   A 1 86  ? -28.54800 12.72600 -40.09800 1.000 17.53148 ? 85  ASN   A OD1   1 
ATOM   689  N  ND2   . ASN   A 1 86  ? -30.55300 11.94300 -40.79600 1.000 19.69349 ? 85  ASN   A ND2   1 
ATOM   690  N  N     . ASN   A 1 87  ? -25.96000 13.79800 -42.32700 1.000 14.53412 ? 86  ASN   A N     1 
ATOM   691  C  CA    . ASN   A 1 87  ? -25.79600 15.21700 -42.64700 1.000 16.37882 ? 86  ASN   A CA    1 
ATOM   692  C  C     . ASN   A 1 87  ? -24.33100 15.41300 -43.04200 1.000 16.14024 ? 86  ASN   A C     1 
ATOM   693  O  O     . ASN   A 1 87  ? -23.46100 15.63500 -42.19300 1.000 15.97195 ? 86  ASN   A O     1 
ATOM   694  C  CB    . ASN   A 1 87  ? -26.18800 16.03900 -41.42700 1.000 18.30845 ? 86  ASN   A CB    1 
ATOM   695  C  CG    . ASN   A 1 87  ? -26.05300 17.53400 -41.63300 1.000 18.60155 ? 86  ASN   A CG    1 
ATOM   696  O  OD1   . ASN   A 1 87  ? -25.41400 18.00600 -42.57500 1.000 19.32331 ? 86  ASN   A OD1   1 
ATOM   697  N  ND2   . ASN   A 1 87  ? -26.62000 18.29300 -40.70400 1.000 20.92267 ? 86  ASN   A ND2   1 
ATOM   698  N  N     . THR   A 1 88  ? -24.06300 15.34300 -44.34700 1.000 16.63579 ? 87  THR   A N     1 
ATOM   699  C  CA    . THR   A 1 88  ? -22.68200 15.44200 -44.81900 1.000 14.96261 ? 87  THR   A CA    1 
ATOM   700  C  C     . THR   A 1 88  ? -22.07200 16.80800 -44.51600 1.000 16.30624 ? 87  THR   A C     1 
ATOM   701  O  O     . THR   A 1 88  ? -20.89600 16.89400 -44.14400 1.000 17.29893 ? 87  THR   A O     1 
ATOM   702  C  CB    . THR   A 1 88  ? -22.61800 15.11200 -46.31000 1.000 18.99313 ? 87  THR   A CB    1 
ATOM   703  O  OG1   . THR   A 1 88  ? -22.97500 13.73900 -46.48400 1.000 21.63926 ? 87  THR   A OG1   1 
ATOM   704  C  CG2   . THR   A 1 88  ? -21.21100 15.34300 -46.87100 1.000 19.85865 ? 87  THR   A CG2   1 
ATOM   705  N  N     . LYS   A 1 89  ? -22.84500 17.88900 -44.66400 1.000 17.96637 ? 88  LYS   A N     1 
ATOM   706  C  CA    . LYS   A 1 89  ? -22.32600 19.20700 -44.30900 1.000 17.02110 ? 88  LYS   A CA    1 
ATOM   707  C  C     . LYS   A 1 89  ? -21.85800 19.24900 -42.85500 1.000 16.64168 ? 88  LYS   A C     1 
ATOM   708  O  O     . LYS   A 1 89  ? -20.80300 19.82500 -42.54100 1.000 17.35646 ? 88  LYS   A O     1 
ATOM   709  C  CB    . LYS   A 1 89  ? -23.37300 20.28800 -44.60100 1.000 20.76034 ? 88  LYS   A CB    1 
ATOM   710  C  CG    . LYS   A 1 89  ? -22.96500 21.67500 -44.16000 1.000 25.54558 ? 88  LYS   A CG    1 
ATOM   711  C  CD    . LYS   A 1 89  ? -21.77000 22.19700 -44.93200 1.000 28.39993 ? 88  LYS   A CD    1 
ATOM   712  C  CE    . LYS   A 1 89  ? -21.78400 23.73200 -44.99700 1.000 30.66330 ? 88  LYS   A CE    1 
ATOM   713  N  NZ    . LYS   A 1 89  ? -21.69900 24.38400 -43.65700 1.000 30.58950 ? 88  LYS   A NZ    1 
ATOM   714  N  N     . SER   A 1 90  ? -22.61000 18.62600 -41.95000 1.000 16.41914 ? 89  SER   A N     1 
ATOM   715  C  CA    . SER   A 1 90  ? -22.19600 18.65200 -40.54900 1.000 15.60188 ? 89  SER   A CA    1 
ATOM   716  C  C     . SER   A 1 90  ? -20.85600 17.95800 -40.35100 1.000 15.02666 ? 89  SER   A C     1 
ATOM   717  O  O     . SER   A 1 90  ? -20.05000 18.38200 -39.51400 1.000 16.68893 ? 89  SER   A O     1 
ATOM   718  C  CB    . SER   A 1 90  ? -23.27800 18.07100 -39.63600 1.000 16.39669 ? 89  SER   A CB    1 
ATOM   719  O  OG    . SER   A 1 90  ? -23.34700 16.65900 -39.68900 1.000 15.71393 ? 89  SER   A OG    1 
ATOM   720  N  N     . PHE   A 1 91  ? -20.59100 16.90400 -41.12900 1.000 14.06841 ? 90  PHE   A N     1 
ATOM   721  C  CA    . PHE   A 1 91  ? -19.28900 16.24800 -41.06300 1.000 14.78437 ? 90  PHE   A CA    1 
ATOM   722  C  C     . PHE   A 1 91  ? -18.20300 17.14200 -41.64600 1.000 15.79872 ? 90  PHE   A C     1 
ATOM   723  O  O     . PHE   A 1 91  ? -17.11600 17.26500 -41.06900 1.000 17.29787 ? 90  PHE   A O     1 
ATOM   724  C  CB    . PHE   A 1 91  ? -19.36600 14.89800 -41.78600 1.000 16.26814 ? 90  PHE   A CB    1 
ATOM   725  C  CG    . PHE   A 1 91  ? -18.05800 14.14500 -41.82900 1.000 14.99042 ? 90  PHE   A CG    1 
ATOM   726  C  CD1   . PHE   A 1 91  ? -17.52400 13.57300 -40.68500 1.000 17.11124 ? 90  PHE   A CD1   1 
ATOM   727  C  CD2   . PHE   A 1 91  ? -17.37000 14.00200 -43.02300 1.000 19.77637 ? 90  PHE   A CD2   1 
ATOM   728  C  CE1   . PHE   A 1 91  ? -16.32700 12.88000 -40.72300 1.000 19.11851 ? 90  PHE   A CE1   1 
ATOM   729  C  CE2   . PHE   A 1 91  ? -16.16800 13.31500 -43.07100 1.000 21.90732 ? 90  PHE   A CE2   1 
ATOM   730  C  CZ    . PHE   A 1 91  ? -15.64600 12.75400 -41.91200 1.000 22.32546 ? 90  PHE   A CZ    1 
ATOM   731  N  N     . GLU   A 1 92  ? -18.48800 17.78700 -42.77700 1.000 18.12821 ? 91  GLU   A N     1 
ATOM   732  C  CA    . GLU   A 1 92  ? -17.54700 18.74100 -43.35200 1.000 22.27120 ? 91  GLU   A CA    1 
ATOM   733  C  C     . GLU   A 1 92  ? -17.28000 19.90800 -42.40600 1.000 22.79125 ? 91  GLU   A C     1 
ATOM   734  O  O     . GLU   A 1 92  ? -16.19500 20.50500 -42.45100 1.000 28.91965 ? 91  GLU   A O     1 
ATOM   735  C  CB    . GLU   A 1 92  ? -18.06900 19.22600 -44.71000 1.000 24.03523 ? 91  GLU   A CB    1 
ATOM   736  C  CG    . GLU   A 1 92  ? -18.11000 18.10800 -45.76200 1.000 28.47867 ? 91  GLU   A CG    1 
ATOM   737  C  CD    . GLU   A 1 92  ? -18.92500 18.45400 -47.00700 1.000 36.90413 ? 91  GLU   A CD    1 
ATOM   738  O  OE1   . GLU   A 1 92  ? -19.56900 19.52700 -47.04200 1.000 37.97281 ? 91  GLU   A OE1   1 
ATOM   739  O  OE2   . GLU   A 1 92  ? -18.92000 17.63900 -47.95800 1.000 40.17449 ? 91  GLU   A OE2   1 
ATOM   740  N  N     . ASP   A 1 93  ? -18.24000 20.24700 -41.53900 1.000 21.27945 ? 92  ASP   A N     1 
ATOM   741  C  CA    . ASP   A 1 93  ? -18.04100 21.34800 -40.59500 1.000 22.37603 ? 92  ASP   A CA    1 
ATOM   742  C  C     . ASP   A 1 93  ? -17.04100 21.00100 -39.49900 1.000 21.58654 ? 92  ASP   A C     1 
ATOM   743  O  O     . ASP   A 1 93  ? -16.48500 21.91300 -38.87800 1.000 21.72131 ? 92  ASP   A O     1 
ATOM   744  C  CB    . ASP   A 1 93  ? -19.37000 21.75800 -39.93400 1.000 22.57285 ? 92  ASP   A CB    1 
ATOM   745  C  CG    . ASP   A 1 93  ? -20.31900 22.49200 -40.88400 1.000 25.57725 ? 92  ASP   A CG    1 
ATOM   746  O  OD1   . ASP   A 1 93  ? -19.86300 23.03400 -41.92100 1.000 26.47311 ? 92  ASP   A OD1   1 
ATOM   747  O  OD2   . ASP   A 1 93  ? -21.54100 22.53500 -40.57300 1.000 29.03213 ? 92  ASP   A OD2   1 
ATOM   748  N  N     . ILE   A 1 94  ? -16.77900 19.70900 -39.26700 1.000 18.73924 ? 93  ILE   A N     1 
ATOM   749  C  CA    . ILE   A 1 94  ? -15.99000 19.30300 -38.10400 1.000 16.99749 ? 93  ILE   A CA    1 
ATOM   750  C  C     . ILE   A 1 94  ? -14.62800 19.98100 -38.08700 1.000 17.07480 ? 93  ILE   A C     1 
ATOM   751  O  O     . ILE   A 1 94  ? -14.17900 20.45800 -37.03900 1.000 16.94633 ? 93  ILE   A O     1 
ATOM   752  C  CB    . ILE   A 1 94  ? -15.86100 17.77300 -38.01800 1.000 16.70235 ? 93  ILE   A CB    1 
ATOM   753  C  CG1   . ILE   A 1 94  ? -17.18700 17.13400 -37.59400 1.000 16.60458 ? 93  ILE   A CG1   1 
ATOM   754  C  CG2   . ILE   A 1 94  ? -14.69200 17.38200 -37.05900 1.000 18.70343 ? 93  ILE   A CG2   1 
ATOM   755  C  CD1   . ILE   A 1 94  ? -17.60700 17.44400 -36.15600 1.000 17.99494 ? 93  ILE   A CD1   1 
ATOM   756  N  N     . HIS   A 1 95  ? -13.94400 20.03800 -39.23800 1.000 17.60624 ? 94  HIS   A N     1 
ATOM   757  C  CA    . HIS   A 1 95  ? -12.58200 20.56400 -39.20900 1.000 19.27428 ? 94  HIS   A CA    1 
ATOM   758  C  C     . HIS   A 1 95  ? -12.54100 22.01500 -38.74300 1.000 19.46801 ? 94  HIS   A C     1 
ATOM   759  O  O     . HIS   A 1 95  ? -11.56900 22.42500 -38.10600 1.000 21.11525 ? 94  HIS   A O     1 
ATOM   760  C  CB    . HIS   A 1 95  ? -11.86000 20.36200 -40.54100 1.000 24.49839 ? 94  HIS   A CB    1 
ATOM   761  C  CG    . HIS   A 1 95  ? -12.35500 21.24700 -41.63500 1.000 29.37867 ? 94  HIS   A CG    1 
ATOM   762  N  ND1   . HIS   A 1 95  ? -11.75700 22.44900 -41.94800 1.000 32.03405 ? 94  HIS   A ND1   1 
ATOM   763  C  CD2   . HIS   A 1 95  ? -13.38600 21.10000 -42.49800 1.000 31.53318 ? 94  HIS   A CD2   1 
ATOM   764  C  CE1   . HIS   A 1 95  ? -12.40400 23.00800 -42.95600 1.000 33.47858 ? 94  HIS   A CE1   1 
ATOM   765  N  NE2   . HIS   A 1 95  ? -13.39400 22.20700 -43.31100 1.000 33.92190 ? 94  HIS   A NE2   1 
ATOM   766  N  N     . HIS   A 1 96  ? -13.60000 22.78900 -39.00400 1.000 18.41112 ? 95  HIS   A N     1 
ATOM   767  C  CA    . HIS   A 1 96  ? -13.66300 24.16500 -38.51100 1.000 19.79466 ? 95  HIS   A CA    1 
ATOM   768  C  C     . HIS   A 1 96  ? -13.67400 24.21100 -36.98800 1.000 18.08262 ? 95  HIS   A C     1 
ATOM   769  O  O     . HIS   A 1 96  ? -12.99800 25.05500 -36.38300 1.000 19.52663 ? 95  HIS   A O     1 
ATOM   770  C  CB    . HIS   A 1 96  ? -14.91300 24.85900 -39.04800 1.000 26.84887 ? 95  HIS   A CB    1 
ATOM   771  C  CG    . HIS   A 1 96  ? -14.89600 25.07400 -40.52800 1.000 39.65052 ? 95  HIS   A CG    1 
ATOM   772  N  ND1   . HIS   A 1 96  ? -16.02400 24.94700 -41.31000 1.000 45.63604 ? 95  HIS   A ND1   1 
ATOM   773  C  CD2   . HIS   A 1 96  ? -13.89000 25.41300 -41.36900 1.000 43.52498 ? 95  HIS   A CD2   1 
ATOM   774  C  CE1   . HIS   A 1 96  ? -15.71300 25.19300 -42.57100 1.000 47.08802 ? 95  HIS   A CE1   1 
ATOM   775  N  NE2   . HIS   A 1 96  ? -14.42400 25.47900 -42.63300 1.000 46.62746 ? 95  HIS   A NE2   1 
ATOM   776  N  N     . TYR   A 1 97  ? -14.45500 23.33600 -36.34800 1.000 17.96225 ? 96  TYR   A N     1 
ATOM   777  C  CA    . TYR   A 1 97  ? -14.46700 23.28900 -34.88500 1.000 18.04751 ? 96  TYR   A CA    1 
ATOM   778  C  C     . TYR   A 1 97  ? -13.09700 22.92600 -34.32600 1.000 18.95660 ? 96  TYR   A C     1 
ATOM   779  O  O     . TYR   A 1 97  ? -12.61100 23.56300 -33.38400 1.000 19.23848 ? 96  TYR   A O     1 
ATOM   780  C  CB    . TYR   A 1 97  ? -15.53900 22.31100 -34.39500 1.000 19.57739 ? 96  TYR   A CB    1 
ATOM   781  C  CG    . TYR   A 1 97  ? -16.95300 22.77500 -34.69300 1.000 20.26198 ? 96  TYR   A CG    1 
ATOM   782  C  CD1   . TYR   A 1 97  ? -17.58400 23.70400 -33.88100 1.000 22.40430 ? 96  TYR   A CD1   1 
ATOM   783  C  CD2   . TYR   A 1 97  ? -17.65100 22.29000 -35.78900 1.000 23.09579 ? 96  TYR   A CD2   1 
ATOM   784  C  CE1   . TYR   A 1 97  ? -18.85800 24.13800 -34.15400 1.000 22.59092 ? 96  TYR   A CE1   1 
ATOM   785  C  CE2   . TYR   A 1 97  ? -18.92600 22.72500 -36.07200 1.000 26.36361 ? 96  TYR   A CE2   1 
ATOM   786  C  CZ    . TYR   A 1 97  ? -19.52100 23.64700 -35.24800 1.000 24.50695 ? 96  TYR   A CZ    1 
ATOM   787  O  OH    . TYR   A 1 97  ? -20.79300 24.07600 -35.52200 1.000 27.33282 ? 96  TYR   A OH    1 
ATOM   788  N  N     . ARG   A 1 98  ? -12.44400 21.91500 -34.90400 1.000 19.14181 ? 97  ARG   A N     1 
ATOM   789  C  CA    . ARG   A 1 98  ? -11.12500 21.54600 -34.40700 1.000 18.30178 ? 97  ARG   A CA    1 
ATOM   790  C  C     . ARG   A 1 98  ? -10.13400 22.68700 -34.58700 1.000 16.72941 ? 97  ARG   A C     1 
ATOM   791  O  O     . ARG   A 1 98  ? -9.34200  22.97100 -33.68800 1.000 18.62122 ? 97  ARG   A O     1 
ATOM   792  C  CB    . ARG   A 1 98  ? -10.60700 20.27200 -35.07400 1.000 21.21696 ? 97  ARG   A CB    1 
ATOM   793  C  CG    . ARG   A 1 98  ? -9.22500  19.88800 -34.52500 1.000 22.60834 ? 97  ARG   A CG    1 
ATOM   794  C  CD    . ARG   A 1 98  ? -8.78100  18.50100 -34.92100 1.000 24.78148 ? 97  ARG   A CD    1 
ATOM   795  N  NE    . ARG   A 1 98  ? -7.35200  18.31900 -34.68000 1.000 26.48153 ? 97  ARG   A NE    1 
ATOM   796  C  CZ    . ARG   A 1 98  ? -6.81800  18.01500 -33.50400 1.000 29.77457 ? 97  ARG   A CZ    1 
ATOM   797  N  NH1   . ARG   A 1 98  ? -7.57000  17.81400 -32.43400 1.000 32.47324 ? 97  ARG   A NH1   1 
ATOM   798  N  NH2   . ARG   A 1 98  ? -5.49500  17.91900 -33.39600 1.000 31.15474 ? 97  ARG   A NH2   1 
ATOM   799  N  N     . GLU   A 1 99  ? -10.17400 23.36300 -35.73500 1.000 16.74483 ? 98  GLU   A N     1 
ATOM   800  C  CA    . GLU   A 1 99  ? -9.27200  24.48800 -35.95700 1.000 17.98959 ? 98  GLU   A CA    1 
ATOM   801  C  C     . GLU   A 1 99  ? -9.52500  25.60900 -34.95600 1.000 17.08088 ? 98  GLU   A C     1 
ATOM   802  O  O     . GLU   A 1 99  ? -8.57700  26.20600 -34.43400 1.000 17.09401 ? 98  GLU   A O     1 
ATOM   803  C  CB    . GLU   A 1 99  ? -9.42200  25.00000 -37.38700 1.000 20.19779 ? 98  GLU   A CB    1 
ATOM   804  C  CG    . GLU   A 1 99  ? -8.95100  24.01100 -38.42900 1.000 24.08291 ? 98  GLU   A CG    1 
ATOM   805  C  CD    . GLU   A 1 99  ? -9.53300  24.28400 -39.80000 1.000 33.38808 ? 98  GLU   A CD    1 
ATOM   806  O  OE1   . GLU   A 1 99  ? -10.04900 25.40300 -40.01700 1.000 38.17951 ? 98  GLU   A OE1   1 
ATOM   807  O  OE2   . GLU   A 1 99  ? -9.48100  23.37100 -40.65400 1.000 35.79740 ? 98  GLU   A OE2   1 
ATOM   808  N  N     . GLN   A 1 100 ? -10.79500 25.93600 -34.69600 1.000 16.56652 ? 99  GLN   A N     1 
ATOM   809  C  CA    A GLN   A 1 100 ? -11.12100 26.98800 -33.73400 0.500 17.83281 ? 99  GLN   A CA    1 
ATOM   810  C  CA    B GLN   A 1 100 ? -11.07500 27.00700 -33.74700 0.500 15.96071 ? 99  GLN   A CA    1 
ATOM   811  C  C     . GLN   A 1 100 ? -10.62700 26.64200 -32.33400 1.000 15.88447 ? 99  GLN   A C     1 
ATOM   812  O  O     . GLN   A 1 100 ? -10.06900 27.49200 -31.63000 1.000 15.09582 ? 99  GLN   A O     1 
ATOM   813  C  CB    A GLN   A 1 100 ? -12.63200 27.19500 -33.70400 0.500 21.25675 ? 99  GLN   A CB    1 
ATOM   814  C  CB    B GLN   A 1 100 ? -12.54600 27.41900 -33.79000 0.500 16.21923 ? 99  GLN   A CB    1 
ATOM   815  C  CG    A GLN   A 1 100 ? -13.20400 27.78900 -34.97500 0.500 25.26047 ? 99  GLN   A CG    1 
ATOM   816  C  CG    B GLN   A 1 100 ? -12.84200 28.74400 -33.06600 0.500 16.79865 ? 99  GLN   A CG    1 
ATOM   817  C  CD    A GLN   A 1 100 ? -14.70400 27.59000 -35.08100 0.500 29.86707 ? 99  GLN   A CD    1 
ATOM   818  C  CD    B GLN   A 1 100 ? -12.12500 29.95500 -33.67900 0.500 19.73296 ? 99  GLN   A CD    1 
ATOM   819  O  OE1   A GLN   A 1 100 ? -15.33900 27.06500 -34.16300 0.500 31.52897 ? 99  GLN   A OE1   1 
ATOM   820  O  OE1   B GLN   A 1 100 ? -11.64500 29.90800 -34.81500 0.500 19.96857 ? 99  GLN   A OE1   1 
ATOM   821  N  NE2   A GLN   A 1 100 ? -15.28000 28.00300 -36.20800 0.500 29.32850 ? 99  GLN   A NE2   1 
ATOM   822  N  NE2   B GLN   A 1 100 ? -12.05100 31.04300 -32.92200 0.500 21.02848 ? 99  GLN   A NE2   1 
ATOM   823  N  N     . ILE   A 1 101 ? -10.85100 25.39600 -31.90100 1.000 15.93854 ? 100 ILE   A N     1 
ATOM   824  C  CA    . ILE   A 1 101 ? -10.40900 24.98200 -30.56600 1.000 15.12311 ? 100 ILE   A CA    1 
ATOM   825  C  C     . ILE   A 1 101 ? -8.88800  25.07100 -30.45900 1.000 13.45484 ? 100 ILE   A C     1 
ATOM   826  O  O     . ILE   A 1 101 ? -8.34300  25.60200 -29.48500 1.000 15.88084 ? 100 ILE   A O     1 
ATOM   827  C  CB    . ILE   A 1 101 ? -10.92800 23.56800 -30.23900 1.000 15.60428 ? 100 ILE   A CB    1 
ATOM   828  C  CG1   . ILE   A 1 101 ? -12.46000 23.57700 -30.16800 1.000 16.89126 ? 100 ILE   A CG1   1 
ATOM   829  C  CG2   . ILE   A 1 101 ? -10.29000 23.04100 -28.95700 1.000 18.82679 ? 100 ILE   A CG2   1 
ATOM   830  C  CD1   . ILE   A 1 101 ? -13.09200 22.20600 -30.32800 1.000 16.54418 ? 100 ILE   A CD1   1 
ATOM   831  N  N     . LYS   A 1 102 ? -8.17300  24.57600 -31.47500 1.000 15.06952 ? 101 LYS   A N     1 
ATOM   832  C  CA    . LYS   A 1 102 ? -6.71300  24.63700 -31.42200 1.000 14.86711 ? 101 LYS   A CA    1 
ATOM   833  C  C     . LYS   A 1 102 ? -6.21800  26.07900 -31.39800 1.000 13.93497 ? 101 LYS   A C     1 
ATOM   834  O  O     . LYS   A 1 102 ? -5.25800  26.40200 -30.69500 1.000 14.29376 ? 101 LYS   A O     1 
ATOM   835  C  CB    . LYS   A 1 102 ? -6.13100  23.90800 -32.62800 1.000 17.37256 ? 101 LYS   A CB    1 
ATOM   836  C  CG    . LYS   A 1 102 ? -6.32900  22.39000 -32.59500 1.000 21.22155 ? 101 LYS   A CG    1 
ATOM   837  C  CD    . LYS   A 1 102 ? -5.89500  21.73400 -33.89500 1.000 25.80002 ? 101 LYS   A CD    1 
ATOM   838  C  CE    . LYS   A 1 102 ? -4.41500  21.94300 -34.11500 1.000 29.89016 ? 101 LYS   A CE    1 
ATOM   839  N  NZ    . LYS   A 1 102 ? -3.94400  21.46300 -35.44900 1.000 32.83705 ? 101 LYS   A NZ    1 
ATOM   840  N  N     . ARG   A 1 103 ? -6.85200  26.95100 -32.18000 1.000 14.17578 ? 102 ARG   A N     1 
ATOM   841  C  CA    . ARG   A 1 103 ? -6.47000  28.35800 -32.24400 1.000 16.84966 ? 102 ARG   A CA    1 
ATOM   842  C  C     . ARG   A 1 103 ? -6.69400  29.05100 -30.90600 1.000 15.29043 ? 102 ARG   A C     1 
ATOM   843  O  O     . ARG   A 1 103 ? -5.80100  29.73600 -30.38700 1.000 15.91343 ? 102 ARG   A O     1 
ATOM   844  C  CB    . ARG   A 1 103 ? -7.29800  29.01400 -33.35100 1.000 19.07746 ? 102 ARG   A CB    1 
ATOM   845  C  CG    . ARG   A 1 103 ? -7.21300  30.52000 -33.45000 1.000 23.38234 ? 102 ARG   A CG    1 
ATOM   846  C  CD    . ARG   A 1 103 ? -8.13700  31.01800 -34.57900 1.000 24.78952 ? 102 ARG   A CD    1 
ATOM   847  N  NE    . ARG   A 1 103 ? -7.62200  30.65800 -35.89700 1.000 25.83118 ? 102 ARG   A NE    1 
ATOM   848  C  CZ    . ARG   A 1 103 ? -8.22100  29.85100 -36.76900 1.000 26.30311 ? 102 ARG   A CZ    1 
ATOM   849  N  NH1   . ARG   A 1 103 ? -9.40400  29.30400 -36.51900 1.000 27.92497 ? 102 ARG   A NH1   1 
ATOM   850  N  NH2   . ARG   A 1 103 ? -7.62200  29.59400 -37.93000 1.000 23.37922 ? 102 ARG   A NH2   1 
ATOM   851  N  N     . VAL   A 1 104 ? -7.87700  28.85700 -30.32200 1.000 17.40300 ? 103 VAL   A N     1 
ATOM   852  C  CA    . VAL   A 1 104 ? -8.22800  29.55100 -29.09500 1.000 17.86517 ? 103 VAL   A CA    1 
ATOM   853  C  C     . VAL   A 1 104 ? -7.37900  29.06200 -27.93100 1.000 18.55937 ? 103 VAL   A C     1 
ATOM   854  O  O     . VAL   A 1 104 ? -6.93700  29.85600 -27.09000 1.000 20.91031 ? 103 VAL   A O     1 
ATOM   855  C  CB    . VAL   A 1 104 ? -9.73500  29.39700 -28.81300 1.000 19.13002 ? 103 VAL   A CB    1 
ATOM   856  C  CG1   . VAL   A 1 104 ? -10.05500 29.95100 -27.44400 1.000 22.00875 ? 103 VAL   A CG1   1 
ATOM   857  C  CG2   . VAL   A 1 104 ? -10.56100 30.11100 -29.87500 1.000 21.15374 ? 103 VAL   A CG2   1 
ATOM   858  N  N     . LYS   A 1 105 ? -7.12900  27.76100 -27.86400 1.000 17.85707 ? 104 LYS   A N     1 
ATOM   859  C  CA    . LYS   A 1 105 ? -6.35800  27.19700 -26.77000 1.000 17.57935 ? 104 LYS   A CA    1 
ATOM   860  C  C     . LYS   A 1 105 ? -4.86600  27.12300 -27.08300 1.000 17.19663 ? 104 LYS   A C     1 
ATOM   861  O  O     . LYS   A 1 105 ? -4.08600  26.68100 -26.23500 1.000 19.28080 ? 104 LYS   A O     1 
ATOM   862  C  CB    . LYS   A 1 105 ? -6.94900  25.85100 -26.36700 1.000 20.03039 ? 104 LYS   A CB    1 
ATOM   863  C  CG    . LYS   A 1 105 ? -8.44600  25.97300 -26.01200 1.000 18.88107 ? 104 LYS   A CG    1 
ATOM   864  C  CD    . LYS   A 1 105 ? -9.07200  24.65700 -25.55100 1.000 17.88630 ? 104 LYS   A CD    1 
ATOM   865  C  CE    . LYS   A 1 105 ? -8.68900  24.30300 -24.12300 1.000 16.03806 ? 104 LYS   A CE    1 
ATOM   866  N  NZ    . LYS   A 1 105 ? -9.11000  25.28900 -23.06500 1.000 16.14037 ? 104 LYS   A NZ    1 
ATOM   867  N  N     . ASP   A 1 106 ? -4.46500  27.56100 -28.27300 1.000 15.84937 ? 105 ASP   A N     1 
ATOM   868  C  CA    . ASP   A 1 106 ? -3.06100  27.66000 -28.66100 1.000 14.43686 ? 105 ASP   A CA    1 
ATOM   869  C  C     . ASP   A 1 106 ? -2.34100  26.33300 -28.46300 1.000 16.03314 ? 105 ASP   A C     1 
ATOM   870  O  O     . ASP   A 1 106 ? -1.26500  26.26800 -27.86700 1.000 17.95615 ? 105 ASP   A O     1 
ATOM   871  C  CB    . ASP   A 1 106 ? -2.35700  28.80000 -27.92000 1.000 16.47648 ? 105 ASP   A CB    1 
ATOM   872  C  CG    . ASP   A 1 106 ? -0.95600  29.04200 -28.44600 1.000 16.36615 ? 105 ASP   A CG    1 
ATOM   873  O  OD1   . ASP   A 1 106 ? -0.76300  28.98100 -29.67800 1.000 16.29816 ? 105 ASP   A OD1   1 
ATOM   874  O  OD2   . ASP   A 1 106 ? -0.03500  29.29200 -27.64000 1.000 17.59320 ? 105 ASP   A OD2   1 
ATOM   875  N  N     . SER   A 1 107 ? -2.94500  25.26000 -28.97400 1.000 15.63510 ? 106 SER   A N     1 
ATOM   876  C  CA    . SER   A 1 107 ? -2.38400  23.93400 -28.76200 1.000 19.60388 ? 106 SER   A CA    1 
ATOM   877  C  C     . SER   A 1 107 ? -2.81400  23.00700 -29.88600 1.000 19.72334 ? 106 SER   A C     1 
ATOM   878  O  O     . SER   A 1 107 ? -3.94100  23.09700 -30.37100 1.000 20.73878 ? 106 SER   A O     1 
ATOM   879  C  CB    . SER   A 1 107 ? -2.85000  23.34100 -27.43000 1.000 25.92890 ? 106 SER   A CB    1 
ATOM   880  O  OG    . SER   A 1 107 ? -2.30500  22.04700 -27.23000 1.000 30.75300 ? 106 SER   A OG    1 
ATOM   881  N  N     . GLU   A 1 108 ? -1.92700  22.10000 -30.28100 1.000 23.43735 ? 107 GLU   A N     1 
ATOM   882  C  CA    . GLU   A 1 108 ? -2.32100  21.04000 -31.20000 1.000 28.95603 ? 107 GLU   A CA    1 
ATOM   883  C  C     . GLU   A 1 108 ? -2.81200  19.78700 -30.49200 1.000 26.60281 ? 107 GLU   A C     1 
ATOM   884  O  O     . GLU   A 1 108 ? -3.19300  18.82400 -31.16700 1.000 30.25714 ? 107 GLU   A O     1 
ATOM   885  C  CB    . GLU   A 1 108 ? -1.18300  20.68900 -32.16500 1.000 33.52833 ? 107 GLU   A CB    1 
ATOM   886  C  CG    . GLU   A 1 108 ? -0.90900  21.76800 -33.20800 1.000 36.23621 ? 107 GLU   A CG    1 
ATOM   887  C  CD    . GLU   A 1 108 ? -0.23900  21.22000 -34.45600 1.000 41.89141 ? 107 GLU   A CD    1 
ATOM   888  O  OE1   . GLU   A 1 108 ? 0.94500   20.82800 -34.37800 1.000 41.75661 ? 107 GLU   A OE1   1 
ATOM   889  O  OE2   . GLU   A 1 108 ? -0.90300  21.17100 -35.51500 1.000 44.07313 ? 107 GLU   A OE2   1 
ATOM   890  N  N     . ASP   A 1 109 ? -2.82900  19.77900 -29.15700 1.000 24.92738 ? 108 ASP   A N     1 
ATOM   891  C  CA    . ASP   A 1 109 ? -3.21000  18.61300 -28.35700 1.000 27.32840 ? 108 ASP   A CA    1 
ATOM   892  C  C     . ASP   A 1 109 ? -4.26400  19.06500 -27.34800 1.000 26.61422 ? 108 ASP   A C     1 
ATOM   893  O  O     . ASP   A 1 109 ? -3.93600  19.44900 -26.22200 1.000 31.03954 ? 108 ASP   A O     1 
ATOM   894  C  CB    . ASP   A 1 109 ? -1.96100  18.05000 -27.66100 1.000 36.34517 ? 108 ASP   A CB    1 
ATOM   895  C  CG    . ASP   A 1 109 ? -2.20200  16.70300 -27.01300 1.000 45.49803 ? 108 ASP   A CG    1 
ATOM   896  O  OD1   . ASP   A 1 109 ? -3.25300  16.08200 -27.28000 1.000 49.86728 ? 108 ASP   A OD1   1 
ATOM   897  O  OD2   . ASP   A 1 109 ? -1.33000  16.26100 -26.23200 1.000 48.43205 ? 108 ASP   A OD2   1 
ATOM   898  N  N     . VAL   A 1 110 ? -5.52800  19.04500 -27.75700 1.000 21.18102 ? 109 VAL   A N     1 
ATOM   899  C  CA    . VAL   A 1 110 ? -6.65000  19.42400 -26.90600 1.000 16.96117 ? 109 VAL   A CA    1 
ATOM   900  C  C     . VAL   A 1 110 ? -7.54700  18.19900 -26.76600 1.000 13.40558 ? 109 VAL   A C     1 
ATOM   901  O  O     . VAL   A 1 110 ? -7.86200  17.55800 -27.77300 1.000 14.82252 ? 109 VAL   A O     1 
ATOM   902  C  CB    . VAL   A 1 110 ? -7.45100  20.60800 -27.48200 1.000 16.89523 ? 109 VAL   A CB    1 
ATOM   903  C  CG1   . VAL   A 1 110 ? -8.63700  20.93600 -26.56400 1.000 16.94422 ? 109 VAL   A CG1   1 
ATOM   904  C  CG2   . VAL   A 1 110 ? -6.53100  21.83700 -27.69000 1.000 20.11796 ? 109 VAL   A CG2   1 
ATOM   905  N  N     . PRO   A 1 111 ? -7.96000  17.82500 -25.55100 1.000 14.38187 ? 110 PRO   A N     1 
ATOM   906  C  CA    . PRO   A 1 111 ? -8.84800  16.65700 -25.41000 1.000 14.20017 ? 110 PRO   A CA    1 
ATOM   907  C  C     . PRO   A 1 111 ? -10.12400 16.84800 -26.20900 1.000 12.06283 ? 110 PRO   A C     1 
ATOM   908  O  O     . PRO   A 1 111 ? -10.85900 17.82900 -26.02500 1.000 12.73600 ? 110 PRO   A O     1 
ATOM   909  C  CB    . PRO   A 1 111 ? -9.12600  16.61500 -23.90400 1.000 14.46054 ? 110 PRO   A CB    1 
ATOM   910  C  CG    . PRO   A 1 111 ? -7.90000  17.24500 -23.30900 1.000 15.26785 ? 110 PRO   A CG    1 
ATOM   911  C  CD    . PRO   A 1 111 ? -7.57000  18.37800 -24.24100 1.000 14.66157 ? 110 PRO   A CD    1 
ATOM   912  N  N     . MET   A 1 112 ? -10.37200 15.90300 -27.11300 1.000 13.31019 ? 111 MET   A N     1 
ATOM   913  C  CA    . MET   A 1 112 ? -11.57600 15.95400 -27.92200 1.000 13.80202 ? 111 MET   A CA    1 
ATOM   914  C  C     . MET   A 1 112 ? -11.93300 14.56300 -28.42400 1.000 13.58576 ? 111 MET   A C     1 
ATOM   915  O  O     . MET   A 1 112 ? -11.07400 13.68200 -28.54800 1.000 14.66938 ? 111 MET   A O     1 
ATOM   916  C  CB    . MET   A 1 112 ? -11.54000 17.00300 -29.04600 1.000 23.74258 ? 111 MET   A CB    1 
ATOM   917  C  CG    . MET   A 1 112 ? -10.55000 16.86600 -30.15100 1.000 27.61888 ? 111 MET   A CG    1 
ATOM   918  S  SD    . MET   A 1 112 ? -10.83700 18.25800 -31.32100 1.000 25.85914 ? 111 MET   A SD    1 
ATOM   919  C  CE    . MET   A 1 112 ? -10.21900 19.66200 -30.41400 1.000 27.11514 ? 111 MET   A CE    1 
ATOM   920  N  N     . VAL   A 1 113 ? -13.22200 14.37200 -28.68800 1.000 12.73342 ? 112 VAL   A N     1 
ATOM   921  C  CA    . VAL   A 1 113 ? -13.74700 13.11200 -29.20300 1.000 11.72190 ? 112 VAL   A CA    1 
ATOM   922  C  C     . VAL   A 1 113 ? -14.65900 13.45700 -30.36800 1.000 12.98291 ? 112 VAL   A C     1 
ATOM   923  O  O     . VAL   A 1 113 ? -15.44900 14.40400 -30.28000 1.000 13.24464 ? 112 VAL   A O     1 
ATOM   924  C  CB    . VAL   A 1 113 ? -14.51800 12.34500 -28.11000 1.000 14.15667 ? 112 VAL   A CB    1 
ATOM   925  C  CG1   . VAL   A 1 113 ? -15.27900 11.16000 -28.69000 1.000 17.33775 ? 112 VAL   A CG1   1 
ATOM   926  C  CG2   . VAL   A 1 113 ? -13.57100 11.86800 -27.02000 1.000 15.43710 ? 112 VAL   A CG2   1 
ATOM   927  N  N     . LEU   A 1 114 ? -14.50900 12.73400 -31.47700 1.000 13.39739 ? 113 LEU   A N     1 
ATOM   928  C  CA    . LEU   A 1 114 ? -15.37800 12.90200 -32.63300 1.000 14.15546 ? 113 LEU   A CA    1 
ATOM   929  C  C     . LEU   A 1 114 ? -16.57100 11.97100 -32.47600 1.000 13.94131 ? 113 LEU   A C     1 
ATOM   930  O  O     . LEU   A 1 114 ? -16.39400 10.77900 -32.22900 1.000 14.45390 ? 113 LEU   A O     1 
ATOM   931  C  CB    . LEU   A 1 114 ? -14.62200 12.57600 -33.92000 1.000 14.97084 ? 113 LEU   A CB    1 
ATOM   932  C  CG    . LEU   A 1 114 ? -15.43000 12.74400 -35.20900 1.000 15.47846 ? 113 LEU   A CG    1 
ATOM   933  C  CD1   . LEU   A 1 114 ? -15.79300 14.21200 -35.39500 1.000 17.72860 ? 113 LEU   A CD1   1 
ATOM   934  C  CD2   . LEU   A 1 114 ? -14.64600 12.19400 -36.38100 1.000 17.22962 ? 113 LEU   A CD2   1 
ATOM   935  N  N     . VAL   A 1 115 ? -17.78100 12.52300 -32.58800 1.000 13.04876 ? 114 VAL   A N     1 
ATOM   936  C  CA    . VAL   A 1 115 ? -19.01200 11.76600 -32.35900 1.000 12.61826 ? 114 VAL   A CA    1 
ATOM   937  C  C     . VAL   A 1 115 ? -19.85700 11.81700 -33.62000 1.000 13.87491 ? 114 VAL   A C     1 
ATOM   938  O  O     . VAL   A 1 115 ? -20.21900 12.91000 -34.08600 1.000 15.55905 ? 114 VAL   A O     1 
ATOM   939  C  CB    . VAL   A 1 115 ? -19.81100 12.30300 -31.16000 1.000 13.73407 ? 114 VAL   A CB    1 
ATOM   940  C  CG1   . VAL   A 1 115 ? -21.16300 11.57600 -31.05100 1.000 16.47649 ? 114 VAL   A CG1   1 
ATOM   941  C  CG2   . VAL   A 1 115 ? -19.01300 12.18700 -29.86000 1.000 15.99150 ? 114 VAL   A CG2   1 
ATOM   942  N  N     . GLY   A 1 116 ? -20.18800 10.64300 -34.15000 1.000 14.67765 ? 115 GLY   A N     1 
ATOM   943  C  CA    . GLY   A 1 116 ? -21.11800 10.54800 -35.26500 1.000 14.71097 ? 115 GLY   A CA    1 
ATOM   944  C  C     . GLY   A 1 116 ? -22.45900 10.06400 -34.76100 1.000 14.63671 ? 115 GLY   A C     1 
ATOM   945  O  O     . GLY   A 1 116 ? -22.61200 8.87900  -34.44400 1.000 17.43586 ? 115 GLY   A O     1 
ATOM   946  N  N     . ASN   A 1 117 ? -23.42000 10.97800 -34.66700 1.000 15.72189 ? 116 ASN   A N     1 
ATOM   947  C  CA    . ASN   A 1 117 ? -24.69900 10.73300 -34.01700 1.000 16.25949 ? 116 ASN   A CA    1 
ATOM   948  C  C     . ASN   A 1 117 ? -25.78000 10.37900 -35.04000 1.000 16.44480 ? 116 ASN   A C     1 
ATOM   949  O  O     . ASN   A 1 117 ? -25.60300 10.53300 -36.25000 1.000 16.60394 ? 116 ASN   A O     1 
ATOM   950  C  CB    . ASN   A 1 117 ? -25.09700 11.96600 -33.19000 1.000 14.35969 ? 116 ASN   A CB    1 
ATOM   951  C  CG    . ASN   A 1 117 ? -26.30500 11.72200 -32.30600 1.000 14.29140 ? 116 ASN   A CG    1 
ATOM   952  O  OD1   . ASN   A 1 117 ? -26.39600 10.69600 -31.63500 1.000 15.47000 ? 116 ASN   A OD1   1 
ATOM   953  N  ND2   . ASN   A 1 117 ? -27.26300 12.65100 -32.33800 1.000 16.31130 ? 116 ASN   A ND2   1 
ATOM   954  N  N     . LYS   A 1 118 ? -26.92300 9.92500  -34.51900 1.000 16.92527 ? 117 LYS   A N     1 
ATOM   955  C  CA    . LYS   A 1 118 ? -28.09600 9.50000  -35.29600 1.000 17.84008 ? 117 LYS   A CA    1 
ATOM   956  C  C     . LYS   A 1 118 ? -27.87300 8.17400  -36.01600 1.000 17.86937 ? 117 LYS   A C     1 
ATOM   957  O  O     . LYS   A 1 118 ? -28.48600 7.90100  -37.05100 1.000 18.40220 ? 117 LYS   A O     1 
ATOM   958  C  CB    . LYS   A 1 118 ? -28.63900 10.59200 -36.23600 1.000 17.82176 ? 117 LYS   A CB    1 
ATOM   959  C  CG    . LYS   A 1 118 ? -28.81000 11.95100 -35.57500 1.000 16.71509 ? 117 LYS   A CG    1 
ATOM   960  C  CD    . LYS   A 1 118 ? -29.69400 12.88800 -36.39400 1.000 16.75928 ? 117 LYS   A CD    1 
ATOM   961  C  CE    . LYS   A 1 118 ? -29.74900 14.29400 -35.78600 1.000 15.86201 ? 117 LYS   A CE    1 
ATOM   962  N  NZ    . LYS   A 1 118 ? -30.72000 15.15700 -36.53700 1.000 17.75931 ? 117 LYS   A NZ    1 
ATOM   963  N  N     . CYS   A 1 119 ? -27.04600 7.29600  -35.44500 1.000 18.04924 ? 118 CYS   A N     1 
ATOM   964  C  CA    A CYS   A 1 119 ? -26.72900 6.04300  -36.11600 0.500 18.68042 ? 118 CYS   A CA    1 
ATOM   965  C  CA    B CYS   A 1 119 ? -26.72500 6.03600  -36.09700 0.500 18.82246 ? 118 CYS   A CA    1 
ATOM   966  C  C     . CYS   A 1 119 ? -27.91100 5.08400  -36.18100 1.000 19.52928 ? 118 CYS   A C     1 
ATOM   967  O  O     . CYS   A 1 119 ? -27.81700 4.06500  -36.87000 1.000 21.66953 ? 118 CYS   A O     1 
ATOM   968  C  CB    A CYS   A 1 119 ? -25.50900 5.37700  -35.47400 0.500 21.24012 ? 118 CYS   A CB    1 
ATOM   969  C  CB    B CYS   A 1 119 ? -25.53300 5.37100  -35.41400 0.500 21.48100 ? 118 CYS   A CB    1 
ATOM   970  S  SG    A CYS   A 1 119 ? -25.81200 4.71600  -33.83800 0.500 23.34335 ? 118 CYS   A SG    1 
ATOM   971  S  SG    B CYS   A 1 119 ? -23.98200 6.17400  -35.81600 0.500 23.09179 ? 118 CYS   A SG    1 
ATOM   972  N  N     . ASP   A 1 120 ? -29.01700 5.39000  -35.51300 1.000 20.96568 ? 119 ASP   A N     1 
ATOM   973  C  CA    . ASP   A 1 120 ? -30.21800 4.57700  -35.62700 1.000 21.12748 ? 119 ASP   A CA    1 
ATOM   974  C  C     . ASP   A 1 120 ? -30.96600 4.81700  -36.93100 1.000 22.22114 ? 119 ASP   A C     1 
ATOM   975  O  O     . ASP   A 1 120 ? -31.84600 4.01900  -37.27700 1.000 23.07624 ? 119 ASP   A O     1 
ATOM   976  C  CB    . ASP   A 1 120 ? -31.15800 4.90900  -34.47500 1.000 21.60740 ? 119 ASP   A CB    1 
ATOM   977  C  CG    . ASP   A 1 120 ? -31.52600 6.37700  -34.44500 1.000 19.73297 ? 119 ASP   A CG    1 
ATOM   978  O  OD1   . ASP   A 1 120 ? -30.69700 7.20100  -34.00100 1.000 20.23420 ? 119 ASP   A OD1   1 
ATOM   979  O  OD2   . ASP   A 1 120 ? -32.63300 6.71300  -34.90100 1.000 22.05883 ? 119 ASP   A OD2   1 
ATOM   980  N  N     . LEU   A 1 121 ? -30.63300 5.91200  -37.68700 1.000 21.95228 ? 120 LEU   A N     1 
ATOM   981  C  CA    . LEU   A 1 121 ? -31.48600 6.28700  -38.80800 1.000 22.00057 ? 120 LEU   A CA    1 
ATOM   982  C  C     . LEU   A 1 121 ? -31.07800 5.56300  -40.09000 1.000 22.94332 ? 120 LEU   A C     1 
ATOM   983  O  O     . LEU   A 1 121 ? -29.91800 5.18800  -40.25700 1.000 25.98162 ? 120 LEU   A O     1 
ATOM   984  C  CB    . LEU   A 1 121 ? -31.41100 7.79600  -39.03300 1.000 21.87713 ? 120 LEU   A CB    1 
ATOM   985  C  CG    . LEU   A 1 121 ? -32.09600 8.62500  -37.94100 1.000 23.61599 ? 120 LEU   A CG    1 
ATOM   986  C  CD1   . LEU   A 1 121 ? -31.96000 10.10700 -38.20700 1.000 24.74681 ? 120 LEU   A CD1   1 
ATOM   987  C  CD2   . LEU   A 1 121 ? -33.57000 8.24300  -37.80500 1.000 24.43586 ? 120 LEU   A CD2   1 
ATOM   988  N  N     . PRO   A 1 122 ? -32.01000 5.35900  -41.01900 1.000 22.27031 ? 121 PRO   A N     1 
ATOM   989  C  CA    . PRO   A 1 122 ? -31.71200 4.62500  -42.26000 1.000 24.01932 ? 121 PRO   A CA    1 
ATOM   990  C  C     . PRO   A 1 122 ? -31.21000 5.48900  -43.41000 1.000 23.75890 ? 121 PRO   A C     1 
ATOM   991  O  O     . PRO   A 1 122 ? -31.16900 5.00800  -44.54800 1.000 25.33020 ? 121 PRO   A O     1 
ATOM   992  C  CB    . PRO   A 1 122 ? -33.09200 4.05000  -42.61400 1.000 24.04818 ? 121 PRO   A CB    1 
ATOM   993  C  CG    . PRO   A 1 122 ? -34.03000 5.10000  -42.17100 1.000 22.42705 ? 121 PRO   A CG    1 
ATOM   994  C  CD    . PRO   A 1 122 ? -33.45200 5.63300  -40.88600 1.000 20.88730 ? 121 PRO   A CD    1 
ATOM   995  N  N     . SER   A 1 123 ? -30.82200 6.73100  -43.14600 1.000 21.91029 ? 122 SER   A N     1 
ATOM   996  C  CA    . SER   A 1 123 ? -30.53900 7.72700  -44.17400 1.000 22.48496 ? 122 SER   A CA    1 
ATOM   997  C  C     . SER   A 1 123 ? -29.07200 8.17300  -44.18300 1.000 20.64715 ? 122 SER   A C     1 
ATOM   998  O  O     . SER   A 1 123 ? -28.76100 9.29900  -44.58300 1.000 20.07801 ? 122 SER   A O     1 
ATOM   999  C  CB    . SER   A 1 123 ? -31.46700 8.92400  -43.96400 1.000 23.02887 ? 122 SER   A CB    1 
ATOM   1000 O  OG    . SER   A 1 123 ? -31.40400 9.35200  -42.60500 1.000 23.14334 ? 122 SER   A OG    1 
ATOM   1001 N  N     . ARG   A 1 124 ? -28.16300 7.29000  -43.77100 1.000 19.93894 ? 123 ARG   A N     1 
ATOM   1002 C  CA    . ARG   A 1 124 ? -26.74400 7.61500  -43.67200 1.000 20.78644 ? 123 ARG   A CA    1 
ATOM   1003 C  C     . ARG   A 1 124 ? -26.18900 8.16700  -44.98000 1.000 20.24874 ? 123 ARG   A C     1 
ATOM   1004 O  O     . ARG   A 1 124 ? -26.45900 7.64500  -46.06900 1.000 22.50994 ? 123 ARG   A O     1 
ATOM   1005 C  CB    . ARG   A 1 124 ? -25.96400 6.35600  -43.30300 1.000 22.11867 ? 123 ARG   A CB    1 
ATOM   1006 C  CG    . ARG   A 1 124 ? -24.48100 6.59900  -43.10400 1.000 24.12097 ? 123 ARG   A CG    1 
ATOM   1007 C  CD    . ARG   A 1 124 ? -23.72700 5.29900  -42.85600 1.000 25.57538 ? 123 ARG   A CD    1 
ATOM   1008 N  NE    . ARG   A 1 124 ? -23.93100 4.76300  -41.51600 1.000 26.78634 ? 123 ARG   A NE    1 
ATOM   1009 C  CZ    . ARG   A 1 124 ? -23.20000 5.09900  -40.46100 1.000 26.76475 ? 123 ARG   A CZ    1 
ATOM   1010 N  NH1   . ARG   A 1 124 ? -22.26300 6.02700  -40.54200 1.000 25.76956 ? 123 ARG   A NH1   1 
ATOM   1011 N  NH2   . ARG   A 1 124 ? -23.40700 4.48100  -39.29900 1.000 28.42340 ? 123 ARG   A NH2   1 
ATOM   1012 N  N     . THR   A 1 125 ? -25.39800 9.23300  -44.85300 1.000 17.19957 ? 124 THR   A N     1 
ATOM   1013 C  CA    . THR   A 1 125 ? -24.62700 9.80000  -45.94600 1.000 18.01154 ? 124 THR   A CA    1 
ATOM   1014 C  C     . THR   A 1 125 ? -23.13000 9.83700  -45.66600 1.000 19.80001 ? 124 THR   A C     1 
ATOM   1015 O  O     . THR   A 1 125 ? -22.35500 10.03300 -46.60700 1.000 22.13145 ? 124 THR   A O     1 
ATOM   1016 C  CB    . THR   A 1 125 ? -25.10300 11.23100 -46.26400 1.000 19.31376 ? 124 THR   A CB    1 
ATOM   1017 O  OG1   . THR   A 1 125 ? -24.86000 12.09300 -45.13800 1.000 19.35331 ? 124 THR   A OG1   1 
ATOM   1018 C  CG2   . THR   A 1 125 ? -26.58400 11.26000 -46.55700 1.000 19.10683 ? 124 THR   A CG2   1 
ATOM   1019 N  N     . VAL   A 1 126 ? -22.70400 9.67000  -44.41200 1.000 19.69443 ? 125 VAL   A N     1 
ATOM   1020 C  CA    . VAL   A 1 126 ? -21.29400 9.69100  -44.04100 1.000 19.10798 ? 125 VAL   A CA    1 
ATOM   1021 C  C     . VAL   A 1 126 ? -20.89500 8.27900  -43.61800 1.000 21.57349 ? 125 VAL   A C     1 
ATOM   1022 O  O     . VAL   A 1 126 ? -21.44200 7.73900  -42.64900 1.000 22.00298 ? 125 VAL   A O     1 
ATOM   1023 C  CB    . VAL   A 1 126 ? -21.03100 10.70800 -42.91300 1.000 18.08284 ? 125 VAL   A CB    1 
ATOM   1024 C  CG1   . VAL   A 1 126 ? -19.56700 10.69500 -42.55200 1.000 20.82331 ? 125 VAL   A CG1   1 
ATOM   1025 C  CG2   . VAL   A 1 126 ? -21.43400 12.09600 -43.34100 1.000 20.47876 ? 125 VAL   A CG2   1 
ATOM   1026 N  N     . ASP   A 1 127 ? -19.93300 7.68600  -44.32500 1.000 25.90605 ? 126 ASP   A N     1 
ATOM   1027 C  CA    . ASP   A 1 127 ? -19.47700 6.34400  -43.97900 1.000 29.47857 ? 126 ASP   A CA    1 
ATOM   1028 C  C     . ASP   A 1 127 ? -18.68400 6.36500  -42.67700 1.000 28.74851 ? 126 ASP   A C     1 
ATOM   1029 O  O     . ASP   A 1 127 ? -17.92600 7.30200  -42.40900 1.000 27.00003 ? 126 ASP   A O     1 
ATOM   1030 C  CB    . ASP   A 1 127 ? -18.56900 5.78800  -45.08000 1.000 38.75922 ? 126 ASP   A CB    1 
ATOM   1031 C  CG    . ASP   A 1 127 ? -19.25900 5.67600  -46.41800 1.000 50.91934 ? 126 ASP   A CG    1 
ATOM   1032 O  OD1   . ASP   A 1 127 ? -20.47400 5.38500  -46.44200 1.000 58.50488 ? 126 ASP   A OD1   1 
ATOM   1033 O  OD2   . ASP   A 1 127 ? -18.57600 5.86400  -47.45100 1.000 53.17400 ? 126 ASP   A OD2   1 
ATOM   1034 N  N     . THR   A 1 128 ? -18.85200 5.31200  -41.87100 1.000 27.66794 ? 127 THR   A N     1 
ATOM   1035 C  CA    . THR   A 1 128 ? -18.05500 5.16800  -40.65300 1.000 25.65828 ? 127 THR   A CA    1 
ATOM   1036 C  C     . THR   A 1 128 ? -16.56400 5.23500  -40.95600 1.000 25.80602 ? 127 THR   A C     1 
ATOM   1037 O  O     . THR   A 1 128 ? -15.80500 5.87500  -40.22000 1.000 23.23270 ? 127 THR   A O     1 
ATOM   1038 C  CB    . THR   A 1 128 ? -18.39000 3.84600  -39.96100 1.000 26.91970 ? 127 THR   A CB    1 
ATOM   1039 O  OG1   . THR   A 1 128 ? -19.80700 3.72600  -39.79700 1.000 30.23178 ? 127 THR   A OG1   1 
ATOM   1040 C  CG2   . THR   A 1 128 ? -17.73000 3.77200  -38.59600 1.000 28.90010 ? 127 THR   A CG2   1 
ATOM   1041 N  N     . LYS   A 1 129 ? -16.12600 4.57400  -42.03400 1.000 25.86789 ? 128 LYS   A N     1 
ATOM   1042 C  CA    . LYS   A 1 129 ? -14.71600 4.60700  -42.40900 1.000 27.34437 ? 128 LYS   A CA    1 
ATOM   1043 C  C     . LYS   A 1 129 ? -14.21100 6.03200  -42.60600 1.000 25.85867 ? 128 LYS   A C     1 
ATOM   1044 O  O     . LYS   A 1 129 ? -13.10200 6.36600  -42.16800 1.000 26.27971 ? 128 LYS   A O     1 
ATOM   1045 C  CB    . LYS   A 1 129 ? -14.48200 3.76300  -43.66300 1.000 33.87017 ? 128 LYS   A CB    1 
ATOM   1046 C  CG    . LYS   A 1 129 ? -13.79600 2.44800  -43.37500 1.000 41.01682 ? 128 LYS   A CG    1 
ATOM   1047 C  CD    . LYS   A 1 129 ? -12.43300 2.68000  -42.74200 1.000 45.24871 ? 128 LYS   A CD    1 
ATOM   1048 C  CE    . LYS   A 1 129 ? -11.96500 1.45400  -41.97100 1.000 46.33453 ? 128 LYS   A CE    1 
ATOM   1049 N  NZ    . LYS   A 1 129 ? -11.97100 0.21500  -42.80400 1.000 47.41428 ? 128 LYS   A NZ    1 
ATOM   1050 N  N     . GLN   A 1 130 ? -15.00500 6.88600  -43.26700 1.000 27.32362 ? 129 GLN   A N     1 
ATOM   1051 C  CA    A GLN   A 1 130 ? -14.56500 8.25800  -43.48900 0.500 27.62104 ? 129 GLN   A CA    1 
ATOM   1052 C  CA    B GLN   A 1 130 ? -14.60000 8.27400  -43.48900 0.500 27.54043 ? 129 GLN   A CA    1 
ATOM   1053 C  C     . GLN   A 1 130 ? -14.34200 8.97800  -42.16600 1.000 25.64928 ? 129 GLN   A C     1 
ATOM   1054 O  O     . GLN   A 1 130 ? -13.35000 9.70400  -42.00400 1.000 23.57905 ? 129 GLN   A O     1 
ATOM   1055 C  CB    A GLN   A 1 130 ? -15.57600 9.00800  -44.35700 0.500 31.22159 ? 129 GLN   A CB    1 
ATOM   1056 C  CB    B GLN   A 1 130 ? -15.70100 9.03100  -44.23500 0.500 30.63076 ? 129 GLN   A CB    1 
ATOM   1057 C  CG    A GLN   A 1 130 ? -15.04300 10.31000 -44.94700 0.500 33.60355 ? 129 GLN   A CG    1 
ATOM   1058 C  CG    B GLN   A 1 130 ? -16.10400 8.49400  -45.59300 0.500 32.57151 ? 129 GLN   A CG    1 
ATOM   1059 C  CD    A GLN   A 1 130 ? -16.09200 11.07400 -45.73700 0.500 35.65996 ? 129 GLN   A CD    1 
ATOM   1060 C  CD    B GLN   A 1 130 ? -17.22500 9.32000  -46.21500 0.500 35.72882 ? 129 GLN   A CD    1 
ATOM   1061 O  OE1   A GLN   A 1 130 ? -17.22600 10.62000 -45.88300 0.500 35.44458 ? 129 GLN   A OE1   1 
ATOM   1062 O  OE1   B GLN   A 1 130 ? -18.34900 8.84600  -46.37900 0.500 35.88173 ? 129 GLN   A OE1   1 
ATOM   1063 N  NE2   A GLN   A 1 130 ? -15.71700 12.24100 -46.24800 0.500 36.93004 ? 129 GLN   A NE2   1 
ATOM   1064 N  NE2   B GLN   A 1 130 ? -16.92000 10.56800 -46.55100 0.500 36.94937 ? 129 GLN   A NE2   1 
ATOM   1065 N  N     . ALA   A 1 131 ? -15.24400 8.78500  -41.20700 1.000 22.21086 ? 130 ALA   A N     1 
ATOM   1066 C  CA    . ALA   A 1 131 ? -15.09900 9.44700  -39.91900 1.000 20.88350 ? 130 ALA   A CA    1 
ATOM   1067 C  C     . ALA   A 1 131 ? -13.94400 8.85000  -39.12300 1.000 19.08614 ? 130 ALA   A C     1 
ATOM   1068 O  O     . ALA   A 1 131 ? -13.20100 9.58300  -38.45700 1.000 19.31607 ? 130 ALA   A O     1 
ATOM   1069 C  CB    . ALA   A 1 131 ? -16.41100 9.36500  -39.13900 1.000 21.13697 ? 130 ALA   A CB    1 
ATOM   1070 N  N     . GLN   A 1 132 ? -13.78100 7.52300  -39.17500 1.000 20.43814 ? 131 GLN   A N     1 
ATOM   1071 C  CA    . GLN   A 1 132 ? -12.64800 6.87500  -38.52000 1.000 20.22159 ? 131 GLN   A CA    1 
ATOM   1072 C  C     . GLN   A 1 132 ? -11.33000 7.45400  -39.02400 1.000 19.27708 ? 131 GLN   A C     1 
ATOM   1073 O  O     . GLN   A 1 132 ? -10.42600 7.76200  -38.23200 1.000 21.24356 ? 131 GLN   A O     1 
ATOM   1074 C  CB    . GLN   A 1 132 ? -12.71200 5.36300  -38.76700 1.000 26.27894 ? 131 GLN   A CB    1 
ATOM   1075 C  CG    . GLN   A 1 132 ? -13.92800 4.66700  -38.12900 1.000 34.04664 ? 131 GLN   A CG    1 
ATOM   1076 C  CD    . GLN   A 1 132 ? -14.03400 3.16700  -38.44300 1.000 41.59837 ? 131 GLN   A CD    1 
ATOM   1077 O  OE1   . GLN   A 1 132 ? -13.69900 2.71400  -39.54100 1.000 44.10536 ? 131 GLN   A OE1   1 
ATOM   1078 N  NE2   . GLN   A 1 132 ? -14.51600 2.39400  -37.46800 1.000 43.65782 ? 131 GLN   A NE2   1 
ATOM   1079 N  N     . ASP   A 1 133 ? -11.20700 7.61200  -40.34700 1.000 21.33010 ? 132 ASP   A N     1 
ATOM   1080 C  CA    . ASP   A 1 133 ? -9.98300  8.14900  -40.93700 1.000 22.67196 ? 132 ASP   A CA    1 
ATOM   1081 C  C     . ASP   A 1 133 ? -9.73500  9.58800  -40.50600 1.000 21.87482 ? 132 ASP   A C     1 
ATOM   1082 O  O     . ASP   A 1 133 ? -8.58600  9.97300  -40.25300 1.000 22.13075 ? 132 ASP   A O     1 
ATOM   1083 C  CB    . ASP   A 1 133 ? -10.06200 8.07600  -42.46300 1.000 26.18212 ? 132 ASP   A CB    1 
ATOM   1084 C  CG    . ASP   A 1 133 ? -9.98000  6.64900  -42.99600 1.000 30.63282 ? 132 ASP   A CG    1 
ATOM   1085 O  OD1   . ASP   A 1 133 ? -9.63100  5.71800  -42.23300 1.000 32.64015 ? 132 ASP   A OD1   1 
ATOM   1086 O  OD2   . ASP   A 1 133 ? -10.27200 6.46000  -44.19600 1.000 32.64051 ? 132 ASP   A OD2   1 
ATOM   1087 N  N     . LEU   A 1 134 ? -10.79000 10.40900 -40.44700 1.000 21.75416 ? 133 LEU   A N     1 
ATOM   1088 C  CA    . LEU   A 1 134 ? -10.62000 11.78300 -39.98700 1.000 20.23592 ? 133 LEU   A CA    1 
ATOM   1089 C  C     . LEU   A 1 134 ? -10.11600 11.81400 -38.54900 1.000 17.44865 ? 133 LEU   A C     1 
ATOM   1090 O  O     . LEU   A 1 134 ? -9.15600  12.53100 -38.22900 1.000 20.30352 ? 133 LEU   A O     1 
ATOM   1091 C  CB    . LEU   A 1 134 ? -11.93400 12.55300 -40.11500 1.000 20.73397 ? 133 LEU   A CB    1 
ATOM   1092 C  CG    . LEU   A 1 134 ? -11.76400 14.04000 -39.82200 1.000 20.38325 ? 133 LEU   A CG    1 
ATOM   1093 C  CD1   . LEU   A 1 134 ? -10.82200 14.70000 -40.83400 1.000 22.36387 ? 133 LEU   A CD1   1 
ATOM   1094 C  CD2   . LEU   A 1 134 ? -13.11900 14.73700 -39.79300 1.000 21.66018 ? 133 LEU   A CD2   1 
ATOM   1095 N  N     . ALA   A 1 135 ? -10.75000 11.03300 -37.67000 1.000 18.85127 ? 134 ALA   A N     1 
ATOM   1096 C  CA    . ALA   A 1 135 ? -10.32500 10.98200 -36.27600 1.000 18.66285 ? 134 ALA   A CA    1 
ATOM   1097 C  C     . ALA   A 1 135 ? -8.88400  10.51600 -36.15700 1.000 18.64382 ? 134 ALA   A C     1 
ATOM   1098 O  O     . ALA   A 1 135 ? -8.11200  11.06400 -35.36000 1.000 19.55142 ? 134 ALA   A O     1 
ATOM   1099 C  CB    . ALA   A 1 135 ? -11.24600 10.05900 -35.49000 1.000 17.81502 ? 134 ALA   A CB    1 
ATOM   1100 N  N     . ARG   A 1 136 ? -8.49700  9.51500  -36.95100 1.000 21.03615 ? 135 ARG   A N     1 
ATOM   1101 C  CA    . ARG   A 1 136 ? -7.11300  9.06000  -36.92900 1.000 21.32051 ? 135 ARG   A CA    1 
ATOM   1102 C  C     . ARG   A 1 136 ? -6.15300  10.18500 -37.31200 1.000 21.16293 ? 135 ARG   A C     1 
ATOM   1103 O  O     . ARG   A 1 136 ? -5.08700  10.33800 -36.69900 1.000 22.28353 ? 135 ARG   A O     1 
ATOM   1104 C  CB    . ARG   A 1 136 ? -6.94700  7.86000  -37.85800 1.000 25.44983 ? 135 ARG   A CB    1 
ATOM   1105 C  CG    . ARG   A 1 136 ? -5.55400  7.27600  -37.81500 1.000 30.66893 ? 135 ARG   A CG    1 
ATOM   1106 C  CD    . ARG   A 1 136 ? -5.32500  6.29000  -38.95200 1.000 37.79480 ? 135 ARG   A CD    1 
ATOM   1107 N  NE    . ARG   A 1 136 ? -4.03800  5.61600  -38.84200 1.000 45.33312 ? 135 ARG   A NE    1 
ATOM   1108 C  CZ    . ARG   A 1 136 ? -3.82200  4.53900  -38.09900 1.000 51.66647 ? 135 ARG   A CZ    1 
ATOM   1109 N  NH1   . ARG   A 1 136 ? -4.78500  4.00200  -37.36500 1.000 54.09480 ? 135 ARG   A NH1   1 
ATOM   1110 N  NH2   . ARG   A 1 136 ? -2.61100  3.99100  -38.08600 1.000 52.93688 ? 135 ARG   A NH2   1 
ATOM   1111 N  N     . SER   A 1 137 ? -6.52700  10.99800 -38.30800 1.000 21.29369 ? 136 SER   A N     1 
ATOM   1112 C  CA    . SER   A 1 137 ? -5.66100  12.09200 -38.74300 1.000 22.12727 ? 136 SER   A CA    1 
ATOM   1113 C  C     . SER   A 1 137 ? -5.49600  13.14500 -37.65300 1.000 22.91376 ? 136 SER   A C     1 
ATOM   1114 O  O     . SER   A 1 137 ? -4.48200  13.85800 -37.62000 1.000 24.67002 ? 136 SER   A O     1 
ATOM   1115 C  CB    . SER   A 1 137 ? -6.20100  12.71500 -40.03500 1.000 22.00371 ? 136 SER   A CB    1 
ATOM   1116 O  OG    . SER   A 1 137 ? -7.28300  13.59400 -39.77600 1.000 24.03435 ? 136 SER   A OG    1 
ATOM   1117 N  N     . TYR   A 1 138 ? -6.47200  13.24600 -36.75400 1.000 21.79798 ? 137 TYR   A N     1 
ATOM   1118 C  CA    . TYR   A 1 138 ? -6.43900  14.16700 -35.62800 1.000 21.22143 ? 137 TYR   A CA    1 
ATOM   1119 C  C     . TYR   A 1 138 ? -5.82100  13.54900 -34.38700 1.000 21.15893 ? 137 TYR   A C     1 
ATOM   1120 O  O     . TYR   A 1 138 ? -5.55400  14.27400 -33.42000 1.000 21.97384 ? 137 TYR   A O     1 
ATOM   1121 C  CB    . TYR   A 1 138 ? -7.87200  14.57300 -35.26800 1.000 20.96519 ? 137 TYR   A CB    1 
ATOM   1122 C  CG    . TYR   A 1 138 ? -8.57200  15.43900 -36.28100 1.000 23.54933 ? 137 TYR   A CG    1 
ATOM   1123 C  CD1   . TYR   A 1 138 ? -7.87100  16.13500 -37.26300 1.000 23.02567 ? 137 TYR   A CD1   1 
ATOM   1124 C  CD2   . TYR   A 1 138 ? -9.95000  15.57700 -36.23500 1.000 22.64385 ? 137 TYR   A CD2   1 
ATOM   1125 C  CE1   . TYR   A 1 138 ? -8.54400  16.94900 -38.17800 1.000 22.98262 ? 137 TYR   A CE1   1 
ATOM   1126 C  CE2   . TYR   A 1 138 ? -10.62100 16.37600 -37.13100 1.000 22.07337 ? 137 TYR   A CE2   1 
ATOM   1127 C  CZ    . TYR   A 1 138 ? -9.92300  17.05600 -38.10100 1.000 23.70531 ? 137 TYR   A CZ    1 
ATOM   1128 O  OH    . TYR   A 1 138 ? -10.63400 17.85300 -38.97600 1.000 25.49224 ? 137 TYR   A OH    1 
ATOM   1129 N  N     . GLY   A 1 139 ? -5.63200  12.23000 -34.37900 1.000 19.77896 ? 138 GLY   A N     1 
ATOM   1130 C  CA    . GLY   A 1 139 ? -5.19700  11.52500 -33.19100 1.000 21.27719 ? 138 GLY   A CA    1 
ATOM   1131 C  C     . GLY   A 1 139 ? -6.21000  11.46900 -32.07300 1.000 20.03087 ? 138 GLY   A C     1 
ATOM   1132 O  O     . GLY   A 1 139 ? -5.81000  11.46500 -30.90800 1.000 22.27704 ? 138 GLY   A O     1 
ATOM   1133 N  N     . ILE   A 1 140 ? -7.50400  11.42400 -32.38500 1.000 17.90630 ? 139 ILE   A N     1 
ATOM   1134 C  CA    . ILE   A 1 140 ? -8.54500  11.46900 -31.35600 1.000 17.06988 ? 139 ILE   A CA    1 
ATOM   1135 C  C     . ILE   A 1 140 ? -9.49700  10.28700 -31.53400 1.000 17.42888 ? 139 ILE   A C     1 
ATOM   1136 O  O     . ILE   A 1 140 ? -9.60900  9.72000  -32.63300 1.000 18.48325 ? 139 ILE   A O     1 
ATOM   1137 C  CB    . ILE   A 1 140 ? -9.32300  12.80800 -31.38100 1.000 17.06266 ? 139 ILE   A CB    1 
ATOM   1138 C  CG1   . ILE   A 1 140 ? -10.15600 12.93800 -32.66000 1.000 17.74048 ? 139 ILE   A CG1   1 
ATOM   1139 C  CG2   . ILE   A 1 140 ? -8.37100  13.99400 -31.19100 1.000 18.32423 ? 139 ILE   A CG2   1 
ATOM   1140 C  CD1   . ILE   A 1 140 ? -10.98600 14.20800 -32.71900 1.000 19.21950 ? 139 ILE   A CD1   1 
ATOM   1141 N  N     . PRO   A 1 141 ? -10.22600 9.91200  -30.47100 1.000 16.49004 ? 140 PRO   A N     1 
ATOM   1142 C  CA    . PRO   A 1 141 ? -11.19500 8.81700  -30.60900 1.000 16.16258 ? 140 PRO   A CA    1 
ATOM   1143 C  C     . PRO   A 1 141 ? -12.39500 9.21400  -31.46100 1.000 16.01423 ? 140 PRO   A C     1 
ATOM   1144 O  O     . PRO   A 1 141 ? -12.76800 10.38900 -31.55200 1.000 16.35142 ? 140 PRO   A O     1 
ATOM   1145 C  CB    . PRO   A 1 141 ? -11.63400 8.54600  -29.16500 1.000 17.97114 ? 140 PRO   A CB    1 
ATOM   1146 C  CG    . PRO   A 1 141 ? -10.52800 9.09200  -28.31700 1.000 17.57598 ? 140 PRO   A CG    1 
ATOM   1147 C  CD    . PRO   A 1 141 ? -10.11300 10.33500 -29.05800 1.000 15.84506 ? 140 PRO   A CD    1 
ATOM   1148 N  N     . PHE   A 1 142 ? -13.00800 8.20700  -32.08000 1.000 17.24609 ? 141 PHE   A N     1 
ATOM   1149 C  CA    . PHE   A 1 142 ? -14.26000 8.35800  -32.81100 1.000 17.99009 ? 141 PHE   A CA    1 
ATOM   1150 C  C     . PHE   A 1 142 ? -15.27900 7.38300  -32.24700 1.000 16.72449 ? 141 PHE   A C     1 
ATOM   1151 O  O     . PHE   A 1 142 ? -14.97000 6.20600  -32.04500 1.000 18.89437 ? 141 PHE   A O     1 
ATOM   1152 C  CB    . PHE   A 1 142 ? -14.07100 8.09200  -34.30400 1.000 19.33466 ? 141 PHE   A CB    1 
ATOM   1153 C  CG    . PHE   A 1 142 ? -15.36600 7.99000  -35.05200 1.000 17.78976 ? 141 PHE   A CG    1 
ATOM   1154 C  CD1   . PHE   A 1 142 ? -16.27200 9.04900  -35.05400 1.000 19.62783 ? 141 PHE   A CD1   1 
ATOM   1155 C  CD2   . PHE   A 1 142 ? -15.68800 6.84400  -35.75300 1.000 23.81657 ? 141 PHE   A CD2   1 
ATOM   1156 C  CE1   . PHE   A 1 142 ? -17.46900 8.95600  -35.72600 1.000 20.22486 ? 141 PHE   A CE1   1 
ATOM   1157 C  CE2   . PHE   A 1 142 ? -16.89400 6.75800  -36.44200 1.000 23.62272 ? 141 PHE   A CE2   1 
ATOM   1158 C  CZ    . PHE   A 1 142 ? -17.77800 7.81400  -36.42700 1.000 21.99661 ? 141 PHE   A CZ    1 
ATOM   1159 N  N     . ILE   A 1 143 ? -16.49200 7.86600  -31.99200 1.000 16.37886 ? 142 ILE   A N     1 
ATOM   1160 C  CA    . ILE   A 1 143 ? -17.53900 7.04900  -31.38800 1.000 18.99108 ? 142 ILE   A CA    1 
ATOM   1161 C  C     . ILE   A 1 143 ? -18.84400 7.32200  -32.11500 1.000 18.40014 ? 142 ILE   A C     1 
ATOM   1162 O  O     . ILE   A 1 143 ? -19.23200 8.48400  -32.29100 1.000 17.19962 ? 142 ILE   A O     1 
ATOM   1163 C  CB    . ILE   A 1 143 ? -17.67100 7.31000  -29.87600 1.000 21.25422 ? 142 ILE   A CB    1 
ATOM   1164 C  CG1   . ILE   A 1 143 ? -16.36500 6.89400  -29.17900 1.000 25.63764 ? 142 ILE   A CG1   1 
ATOM   1165 C  CG2   . ILE   A 1 143 ? -18.87000 6.56600  -29.28100 1.000 21.70576 ? 142 ILE   A CG2   1 
ATOM   1166 C  CD1   . ILE   A 1 143 ? -16.32100 7.16300  -27.70800 1.000 27.07433 ? 142 ILE   A CD1   1 
ATOM   1167 N  N     . GLU   A 1 144 ? -19.51000 6.25800  -32.56400 1.000 19.49544 ? 143 GLU   A N     1 
ATOM   1168 C  CA    . GLU   A 1 144 ? -20.82800 6.38400  -33.17000 1.000 19.91190 ? 143 GLU   A CA    1 
ATOM   1169 C  C     . GLU   A 1 144 ? -21.89300 6.27200  -32.08700 1.000 20.94088 ? 143 GLU   A C     1 
ATOM   1170 O  O     . GLU   A 1 144 ? -21.83800 5.36800  -31.23800 1.000 22.48883 ? 143 GLU   A O     1 
ATOM   1171 C  CB    . GLU   A 1 144 ? -21.03800 5.32300  -34.25300 1.000 26.38454 ? 143 GLU   A CB    1 
ATOM   1172 C  CG    . GLU   A 1 144 ? -20.31000 5.64400  -35.56500 1.000 32.74392 ? 143 GLU   A CG    1 
ATOM   1173 C  CD    . GLU   A 1 144 ? -20.97600 5.06200  -36.81900 1.000 37.56667 ? 143 GLU   A CD    1 
ATOM   1174 O  OE1   . GLU   A 1 144 ? -21.73400 4.07100  -36.71000 1.000 40.30563 ? 143 GLU   A OE1   1 
ATOM   1175 O  OE2   . GLU   A 1 144 ? -20.73800 5.61000  -37.92300 1.000 36.83951 ? 143 GLU   A OE2   1 
ATOM   1176 N  N     . THR   A 1 145 ? -22.87400 7.17400  -32.12800 1.000 18.21371 ? 144 THR   A N     1 
ATOM   1177 C  CA    . THR   A 1 145 ? -23.89300 7.22800  -31.09000 1.000 17.38571 ? 144 THR   A CA    1 
ATOM   1178 C  C     . THR   A 1 145 ? -25.28500 7.30300  -31.69600 1.000 17.83031 ? 144 THR   A C     1 
ATOM   1179 O  O     . THR   A 1 145 ? -25.47000 7.67600  -32.85400 1.000 18.79476 ? 144 THR   A O     1 
ATOM   1180 C  CB    . THR   A 1 145 ? -23.73300 8.46500  -30.19100 1.000 16.36139 ? 144 THR   A CB    1 
ATOM   1181 O  OG1   . THR   A 1 145 ? -23.85500 9.66200  -30.97500 1.000 15.77973 ? 144 THR   A OG1   1 
ATOM   1182 C  CG2   . THR   A 1 145 ? -22.38000 8.48200  -29.51200 1.000 17.73894 ? 144 THR   A CG2   1 
ATOM   1183 N  N     . SER   A 1 146 ? -26.26900 6.98200  -30.86300 1.000 17.20045 ? 145 SER   A N     1 
ATOM   1184 C  CA    . SER   A 1 146 ? -27.64900 7.37100  -31.09400 1.000 17.79298 ? 145 SER   A CA    1 
ATOM   1185 C  C     . SER   A 1 146 ? -28.23400 7.86600  -29.78100 1.000 17.91455 ? 145 SER   A C     1 
ATOM   1186 O  O     . SER   A 1 146 ? -28.34500 7.09800  -28.82000 1.000 19.20738 ? 145 SER   A O     1 
ATOM   1187 C  CB    . SER   A 1 146 ? -28.45400 6.17700  -31.58700 1.000 20.38270 ? 145 SER   A CB    1 
ATOM   1188 O  OG    . SER   A 1 146 ? -29.81900 6.53300  -31.60400 1.000 20.04592 ? 145 SER   A OG    1 
ATOM   1189 N  N     . ALA   A 1 147 ? -28.59400 9.15100  -29.72700 1.000 18.39555 ? 146 ALA   A N     1 
ATOM   1190 C  CA    . ALA   A 1 147 ? -29.31400 9.64700  -28.55800 1.000 17.35996 ? 146 ALA   A CA    1 
ATOM   1191 C  C     . ALA   A 1 147 ? -30.68500 9.01000  -28.43000 1.000 17.98637 ? 146 ALA   A C     1 
ATOM   1192 O  O     . ALA   A 1 147 ? -31.24300 8.97200  -27.32400 1.000 23.24413 ? 146 ALA   A O     1 
ATOM   1193 C  CB    . ALA   A 1 147 ? -29.48700 11.16000 -28.64300 1.000 19.11283 ? 146 ALA   A CB    1 
ATOM   1194 N  N     . LYS   A 1 148 ? -31.24300 8.51000  -29.53200 1.000 19.93202 ? 147 LYS   A N     1 
ATOM   1195 C  CA    . LYS   A 1 148 ? -32.56000 7.89100  -29.46600 1.000 22.33740 ? 147 LYS   A CA    1 
ATOM   1196 C  C     . LYS   A 1 148 ? -32.51100 6.54200  -28.75100 1.000 24.22757 ? 147 LYS   A C     1 
ATOM   1197 O  O     . LYS   A 1 148 ? -33.32600 6.27300  -27.85600 1.000 26.18020 ? 147 LYS   A O     1 
ATOM   1198 C  CB    . LYS   A 1 148 ? -33.16000 7.76700  -30.86700 1.000 22.94960 ? 147 LYS   A CB    1 
ATOM   1199 C  CG    . LYS   A 1 148 ? -34.53400 7.12300  -30.88100 1.000 25.93931 ? 147 LYS   A CG    1 
ATOM   1200 C  CD    . LYS   A 1 148 ? -35.15400 7.17100  -32.26400 1.000 29.01908 ? 147 LYS   A CD    1 
ATOM   1201 C  CE    . LYS   A 1 148 ? -36.46800 6.39600  -32.29800 1.000 32.12808 ? 147 LYS   A CE    1 
ATOM   1202 N  NZ    . LYS   A 1 148 ? -37.02800 6.34200  -33.67400 1.000 36.89214 ? 147 LYS   A NZ    1 
ATOM   1203 N  N     . THR   A 1 149 ? -31.56500 5.67500  -29.12900 1.000 23.09754 ? 148 THR   A N     1 
ATOM   1204 C  CA    . THR   A 1 149 ? -31.47500 4.34200  -28.54300 1.000 24.58320 ? 148 THR   A CA    1 
ATOM   1205 C  C     . THR   A 1 149 ? -30.52900 4.28400  -27.35700 1.000 23.85841 ? 148 THR   A C     1 
ATOM   1206 O  O     . THR   A 1 149 ? -30.47300 3.25500  -26.67600 1.000 26.98696 ? 148 THR   A O     1 
ATOM   1207 C  CB    . THR   A 1 149 ? -30.97900 3.33000  -29.57800 1.000 24.82679 ? 148 THR   A CB    1 
ATOM   1208 O  OG1   . THR   A 1 149 ? -29.60400 3.60200  -29.87700 1.000 25.39997 ? 148 THR   A OG1   1 
ATOM   1209 C  CG2   . THR   A 1 149 ? -31.80600 3.39700  -30.85500 1.000 25.65799 ? 148 THR   A CG2   1 
ATOM   1210 N  N     . ARG   A 1 150 ? -29.78600 5.35600  -27.10700 1.000 23.22097 ? 149 ARG   A N     1 
ATOM   1211 C  CA    . ARG   A 1 150 ? -28.72800 5.48500  -26.11100 1.000 25.10783 ? 149 ARG   A CA    1 
ATOM   1212 C  C     . ARG   A 1 150 ? -27.42800 4.78700  -26.51000 1.000 24.75845 ? 149 ARG   A C     1 
ATOM   1213 O  O     . ARG   A 1 150 ? -26.46800 4.84600  -25.73900 1.000 23.45764 ? 149 ARG   A O     1 
ATOM   1214 C  CB    . ARG   A 1 150 ? -29.13700 5.14400  -24.66600 1.000 28.30361 ? 149 ARG   A CB    1 
ATOM   1215 C  CG    . ARG   A 1 150 ? -28.80700 6.26400  -23.68400 1.000 33.96603 ? 149 ARG   A CG    1 
ATOM   1216 C  CD    . ARG   A 1 150 ? -29.39900 6.00500  -22.30100 1.000 36.69080 ? 149 ARG   A CD    1 
ATOM   1217 N  NE    . ARG   A 1 150 ? -28.95600 7.00100  -21.33000 1.000 38.99333 ? 149 ARG   A NE    1 
ATOM   1218 C  CZ    . ARG   A 1 150 ? -27.79700 6.94400  -20.68800 1.000 41.40411 ? 149 ARG   A CZ    1 
ATOM   1219 N  NH1   . ARG   A 1 150 ? -26.94500 5.95300  -20.89000 1.000 40.60109 ? 149 ARG   A NH1   1 
ATOM   1220 N  NH2   . ARG   A 1 150 ? -27.48200 7.90900  -19.82800 1.000 42.75925 ? 149 ARG   A NH2   1 
ATOM   1221 N  N     . GLN   A 1 151 ? -27.33700 4.17900  -27.69300 1.000 23.35326 ? 150 GLN   A N     1 
ATOM   1222 C  CA    . GLN   A 1 151 ? -26.08000 3.56100  -28.11000 1.000 23.61319 ? 150 GLN   A CA    1 
ATOM   1223 C  C     . GLN   A 1 151 ? -24.93300 4.56700  -28.05600 1.000 21.55051 ? 150 GLN   A C     1 
ATOM   1224 O  O     . GLN   A 1 151 ? -25.00700 5.65600  -28.63700 1.000 20.22447 ? 150 GLN   A O     1 
ATOM   1225 C  CB    . GLN   A 1 151 ? -26.18700 3.01000  -29.53100 1.000 27.25710 ? 150 GLN   A CB    1 
ATOM   1226 C  CG    . GLN   A 1 151 ? -24.84100 2.53600  -30.07100 1.000 33.15021 ? 150 GLN   A CG    1 
ATOM   1227 C  CD    . GLN   A 1 151 ? -24.84800 2.30200  -31.56800 1.000 39.15916 ? 150 GLN   A CD    1 
ATOM   1228 O  OE1   . GLN   A 1 151 ? -23.90500 2.67100  -32.27100 1.000 41.69337 ? 150 GLN   A OE1   1 
ATOM   1229 N  NE2   . GLN   A 1 151 ? -25.91200 1.68900  -32.06400 1.000 39.94999 ? 150 GLN   A NE2   1 
ATOM   1230 N  N     . GLY   A 1 152 ? -23.86700 4.19900  -27.34800 1.000 21.40130 ? 151 GLY   A N     1 
ATOM   1231 C  CA    . GLY   A 1 152 ? -22.63500 4.95500  -27.36500 1.000 20.39772 ? 151 GLY   A CA    1 
ATOM   1232 C  C     . GLY   A 1 152 ? -22.62900 6.22400  -26.54200 1.000 19.67363 ? 151 GLY   A C     1 
ATOM   1233 O  O     . GLY   A 1 152 ? -21.59100 6.89600  -26.48900 1.000 18.99424 ? 151 GLY   A O     1 
ATOM   1234 N  N     . VAL   A 1 153 ? -23.74600 6.58300  -25.90700 1.000 20.17516 ? 152 VAL   A N     1 
ATOM   1235 C  CA    . VAL   A 1 153 ? -23.83800 7.87400  -25.23000 1.000 19.57522 ? 152 VAL   A CA    1 
ATOM   1236 C  C     . VAL   A 1 153 ? -22.86900 7.94500  -24.05400 1.000 18.81689 ? 152 VAL   A C     1 
ATOM   1237 O  O     . VAL   A 1 153 ? -22.06700 8.87800  -23.95400 1.000 18.02883 ? 152 VAL   A O     1 
ATOM   1238 C  CB    . VAL   A 1 153 ? -25.28700 8.17200  -24.80300 1.000 19.21142 ? 152 VAL   A CB    1 
ATOM   1239 C  CG1   . VAL   A 1 153 ? -25.33700 9.42900  -23.94600 1.000 21.75789 ? 152 VAL   A CG1   1 
ATOM   1240 C  CG2   . VAL   A 1 153 ? -26.19500 8.30500  -26.02400 1.000 20.92583 ? 152 VAL   A CG2   1 
ATOM   1241 N  N     . ASP   A 1 154 ? -22.94800 6.97900  -23.13000 1.000 19.30574 ? 153 ASP   A N     1 
ATOM   1242 C  CA    . ASP   A 1 154 ? -22.00100 6.96300  -22.02100 1.000 19.34481 ? 153 ASP   A CA    1 
ATOM   1243 C  C     . ASP   A 1 154 ? -20.56800 6.87400  -22.53700 1.000 18.98866 ? 153 ASP   A C     1 
ATOM   1244 O  O     . ASP   A 1 154 ? -19.67900 7.58300  -22.05000 1.000 18.90202 ? 153 ASP   A O     1 
ATOM   1245 C  CB    . ASP   A 1 154 ? -22.30600 5.79800  -21.07300 1.000 22.83782 ? 153 ASP   A CB    1 
ATOM   1246 C  CG    . ASP   A 1 154 ? -23.56500 6.01200  -20.23600 1.000 26.00992 ? 153 ASP   A CG    1 
ATOM   1247 O  OD1   . ASP   A 1 154 ? -24.07800 7.14500  -20.16900 1.000 29.42224 ? 153 ASP   A OD1   1 
ATOM   1248 O  OD2   . ASP   A 1 154 ? -24.04400 5.02800  -19.63300 1.000 30.36297 ? 153 ASP   A OD2   1 
ATOM   1249 N  N     . ASP   A 1 155 ? -20.33500 6.01900  -23.53800 1.000 18.49558 ? 154 ASP   A N     1 
ATOM   1250 C  CA    . ASP   A 1 155 ? -18.99600 5.83200  -24.08500 1.000 18.85099 ? 154 ASP   A CA    1 
ATOM   1251 C  C     . ASP   A 1 155 ? -18.42300 7.14200  -24.61700 1.000 18.29243 ? 154 ASP   A C     1 
ATOM   1252 O  O     . ASP   A 1 155 ? -17.23400 7.42100  -24.43900 1.000 16.00162 ? 154 ASP   A O     1 
ATOM   1253 C  CB    . ASP   A 1 155 ? -19.06000 4.78100  -25.19500 1.000 22.86274 ? 154 ASP   A CB    1 
ATOM   1254 C  CG    . ASP   A 1 155 ? -17.69700 4.21000  -25.56600 1.000 25.29429 ? 154 ASP   A CG    1 
ATOM   1255 O  OD1   . ASP   A 1 155 ? -16.75300 4.28700  -24.75000 1.000 26.80260 ? 154 ASP   A OD1   1 
ATOM   1256 O  OD2   . ASP   A 1 155 ? -17.57800 3.66300  -26.68500 1.000 27.67484 ? 154 ASP   A OD2   1 
ATOM   1257 N  N     . ALA   A 1 156 ? -19.24700 7.95400  -25.29100 1.000 15.86790 ? 155 ALA   A N     1 
ATOM   1258 C  CA    . ALA   A 1 156 ? -18.74300 9.21100  -25.84300 1.000 16.55198 ? 155 ALA   A CA    1 
ATOM   1259 C  C     . ALA   A 1 156 ? -18.29300 10.16800 -24.73700 1.000 15.40820 ? 155 ALA   A C     1 
ATOM   1260 O  O     . ALA   A 1 156 ? -17.18000 10.70300 -24.77400 1.000 14.45497 ? 155 ALA   A O     1 
ATOM   1261 C  CB    . ALA   A 1 156 ? -19.81800 9.85100  -26.71800 1.000 17.71542 ? 155 ALA   A CB    1 
ATOM   1262 N  N     . PHE   A 1 157 ? -19.15600 10.40900 -23.74700 1.000 15.20010 ? 156 PHE   A N     1 
ATOM   1263 C  CA    . PHE   A 1 157 ? -18.78700 11.32300 -22.66900 1.000 15.38289 ? 156 PHE   A CA    1 
ATOM   1264 C  C     . PHE   A 1 157 ? -17.67400 10.75100 -21.80100 1.000 15.85604 ? 156 PHE   A C     1 
ATOM   1265 O  O     . PHE   A 1 157 ? -16.76700 11.48900 -21.39400 1.000 15.87113 ? 156 PHE   A O     1 
ATOM   1266 C  CB    . PHE   A 1 157 ? -19.99600 11.67900 -21.80900 1.000 16.35446 ? 156 PHE   A CB    1 
ATOM   1267 C  CG    . PHE   A 1 157 ? -20.97300 12.60900 -22.49200 1.000 15.06060 ? 156 PHE   A CG    1 
ATOM   1268 C  CD1   . PHE   A 1 157 ? -20.80300 13.98700 -22.41900 1.000 16.26475 ? 156 PHE   A CD1   1 
ATOM   1269 C  CD2   . PHE   A 1 157 ? -22.07100 12.10800 -23.19600 1.000 16.57229 ? 156 PHE   A CD2   1 
ATOM   1270 C  CE1   . PHE   A 1 157 ? -21.70300 14.86400 -23.05200 1.000 16.32570 ? 156 PHE   A CE1   1 
ATOM   1271 C  CE2   . PHE   A 1 157 ? -22.97900 12.97200 -23.80800 1.000 16.98204 ? 156 PHE   A CE2   1 
ATOM   1272 C  CZ    . PHE   A 1 157 ? -22.79200 14.35000 -23.74200 1.000 16.47453 ? 156 PHE   A CZ    1 
ATOM   1273 N  N     . TYR   A 1 158 ? -17.73500 9.45600  -21.47400 1.000 15.17256 ? 157 TYR   A N     1 
ATOM   1274 C  CA    . TYR   A 1 158 ? -16.69700 8.88400  -20.61100 1.000 15.55085 ? 157 TYR   A CA    1 
ATOM   1275 C  C     . TYR   A 1 158 ? -15.35200 8.84500  -21.32100 1.000 15.15639 ? 157 TYR   A C     1 
ATOM   1276 O  O     . TYR   A 1 158 ? -14.30900 9.07000  -20.69600 1.000 16.30537 ? 157 TYR   A O     1 
ATOM   1277 C  CB    . TYR   A 1 158 ? -17.07200 7.48300  -20.13400 1.000 17.58524 ? 157 TYR   A CB    1 
ATOM   1278 C  CG    . TYR   A 1 158 ? -18.26600 7.38800  -19.21200 1.000 20.38005 ? 157 TYR   A CG    1 
ATOM   1279 C  CD1   . TYR   A 1 158 ? -19.03600 8.49600  -18.90300 1.000 20.65991 ? 157 TYR   A CD1   1 
ATOM   1280 C  CD2   . TYR   A 1 158 ? -18.62300 6.16400  -18.65400 1.000 22.50004 ? 157 TYR   A CD2   1 
ATOM   1281 C  CE1   . TYR   A 1 158 ? -20.13700 8.39100  -18.06300 1.000 24.38464 ? 157 TYR   A CE1   1 
ATOM   1282 C  CE2   . TYR   A 1 158 ? -19.70900 6.05100  -17.80900 1.000 24.88005 ? 157 TYR   A CE2   1 
ATOM   1283 C  CZ    . TYR   A 1 158 ? -20.46300 7.16800  -17.51900 1.000 24.81760 ? 157 TYR   A CZ    1 
ATOM   1284 O  OH    . TYR   A 1 158 ? -21.54600 7.04600  -16.67500 1.000 27.83645 ? 157 TYR   A OH    1 
ATOM   1285 N  N     . THR   A 1 159 ? -15.35000 8.57200  -22.62800 1.000 14.71830 ? 158 THR   A N     1 
ATOM   1286 C  CA    . THR   A 1 159 ? -14.08800 8.61200  -23.36400 1.000 15.32086 ? 158 THR   A CA    1 
ATOM   1287 C  C     . THR   A 1 159 ? -13.48900 10.01100 -23.32800 1.000 13.73919 ? 158 THR   A C     1 
ATOM   1288 O  O     . THR   A 1 159 ? -12.27600 10.16100 -23.16100 1.000 15.66611 ? 158 THR   A O     1 
ATOM   1289 C  CB    . THR   A 1 159 ? -14.27900 8.10900  -24.80300 1.000 15.72335 ? 158 THR   A CB    1 
ATOM   1290 O  OG1   . THR   A 1 159 ? -14.59900 6.70700  -24.80000 1.000 17.08175 ? 158 THR   A OG1   1 
ATOM   1291 C  CG2   . THR   A 1 159 ? -13.00600 8.29500  -25.60800 1.000 18.39705 ? 158 THR   A CG2   1 
ATOM   1292 N  N     . LEU   A 1 160 ? -14.33200 11.04700 -23.43600 1.000 13.12241 ? 159 LEU   A N     1 
ATOM   1293 C  CA    . LEU   A 1 160 ? -13.82100 12.40900 -23.34900 1.000 13.32442 ? 159 LEU   A CA    1 
ATOM   1294 C  C     . LEU   A 1 160 ? -13.17700 12.67700 -21.99000 1.000 14.46223 ? 159 LEU   A C     1 
ATOM   1295 O  O     . LEU   A 1 160 ? -12.09500 13.28200 -21.91900 1.000 13.94719 ? 159 LEU   A O     1 
ATOM   1296 C  CB    . LEU   A 1 160 ? -14.91800 13.42500 -23.66500 1.000 14.34467 ? 159 LEU   A CB    1 
ATOM   1297 C  CG    . LEU   A 1 160 ? -14.45200 14.88500 -23.68600 1.000 12.78513 ? 159 LEU   A CG    1 
ATOM   1298 C  CD1   . LEU   A 1 160 ? -13.30500 15.11800 -24.68400 1.000 15.40662 ? 159 LEU   A CD1   1 
ATOM   1299 C  CD2   . LEU   A 1 160 ? -15.63200 15.78000 -24.04000 1.000 15.30634 ? 159 LEU   A CD2   1 
ATOM   1300 N  N     . VAL   A 1 161 ? -13.81500 12.22600 -20.89900 1.000 14.05823 ? 160 VAL   A N     1 
ATOM   1301 C  CA    . VAL   A 1 161 ? -13.20900 12.36500 -19.57600 1.000 15.34447 ? 160 VAL   A CA    1 
ATOM   1302 C  C     . VAL   A 1 161 ? -11.84900 11.68600 -19.54400 1.000 14.93340 ? 160 VAL   A C     1 
ATOM   1303 O  O     . VAL   A 1 161 ? -10.86300 12.24900 -19.04800 1.000 15.72844 ? 160 VAL   A O     1 
ATOM   1304 C  CB    . VAL   A 1 161 ? -14.14100 11.79500 -18.49300 1.000 15.17817 ? 160 VAL   A CB    1 
ATOM   1305 C  CG1   . VAL   A 1 161 ? -13.40100 11.68200 -17.15200 1.000 15.34233 ? 160 VAL   A CG1   1 
ATOM   1306 C  CG2   . VAL   A 1 161 ? -15.39100 12.66000 -18.36400 1.000 16.52511 ? 160 VAL   A CG2   1 
ATOM   1307 N  N     . ARG   A 1 162 ? -11.76500 10.47700 -20.10200 1.000 15.52659 ? 161 ARG   A N     1 
ATOM   1308 C  CA    . ARG   A 1 162 ? -10.48600 9.76800  -20.11600 1.000 17.89383 ? 161 ARG   A CA    1 
ATOM   1309 C  C     . ARG   A 1 162 ? -9.42800  10.53900 -20.89700 1.000 16.36539 ? 161 ARG   A C     1 
ATOM   1310 O  O     . ARG   A 1 162 ? -8.25200  10.54200 -20.51600 1.000 18.04608 ? 161 ARG   A O     1 
ATOM   1311 C  CB    . ARG   A 1 162 ? -10.66200 8.36400  -20.70100 1.000 19.12164 ? 161 ARG   A CB    1 
ATOM   1312 C  CG    . ARG   A 1 162 ? -11.52000 7.46000  -19.84300 1.000 18.61704 ? 161 ARG   A CG    1 
ATOM   1313 C  CD    . ARG   A 1 162 ? -11.46200 6.02500  -20.29600 1.000 21.42913 ? 161 ARG   A CD    1 
ATOM   1314 N  NE    . ARG   A 1 162 ? -12.46700 5.22500  -19.60400 1.000 22.66259 ? 161 ARG   A NE    1 
ATOM   1315 C  CZ    . ARG   A 1 162 ? -13.68000 4.98100  -20.08000 1.000 25.67172 ? 161 ARG   A CZ    1 
ATOM   1316 N  NH1   . ARG   A 1 162 ? -14.03400 5.36600  -21.29700 1.000 25.99123 ? 161 ARG   A NH1   1 
ATOM   1317 N  NH2   . ARG   A 1 162 ? -14.56500 4.36000  -19.31000 1.000 27.23328 ? 161 ARG   A NH2   1 
ATOM   1318 N  N     . GLU   A 1 163 ? -9.82900  11.21500 -21.98000 1.000 15.56187 ? 162 GLU   A N     1 
ATOM   1319 C  CA    . GLU   A 1 163 ? -8.87700  12.01200 -22.74800 1.000 16.40464 ? 162 GLU   A CA    1 
ATOM   1320 C  C     . GLU   A 1 163 ? -8.37400  13.20500 -21.94300 1.000 15.68329 ? 162 GLU   A C     1 
ATOM   1321 O  O     . GLU   A 1 163 ? -7.19100  13.56200 -22.03200 1.000 17.26100 ? 162 GLU   A O     1 
ATOM   1322 C  CB    . GLU   A 1 163 ? -9.51400  12.46700 -24.05800 1.000 15.93010 ? 162 GLU   A CB    1 
ATOM   1323 C  CG    . GLU   A 1 163 ? -9.82000  11.31900 -25.02400 1.000 17.63125 ? 162 GLU   A CG    1 
ATOM   1324 C  CD    . GLU   A 1 163 ? -8.55900  10.66000 -25.53500 1.000 19.50618 ? 162 GLU   A CD    1 
ATOM   1325 O  OE1   . GLU   A 1 163 ? -7.76800  11.33700 -26.21700 1.000 22.70141 ? 162 GLU   A OE1   1 
ATOM   1326 O  OE2   . GLU   A 1 163 ? -8.34800  9.46300  -25.25100 1.000 25.16746 ? 162 GLU   A OE2   1 
ATOM   1327 N  N     . ILE   A 1 164 ? -9.25400  13.85100 -21.17000 1.000 14.58993 ? 163 ILE   A N     1 
ATOM   1328 C  CA    . ILE   A 1 164 ? -8.81300  14.96600 -20.32900 1.000 15.56883 ? 163 ILE   A CA    1 
ATOM   1329 C  C     . ILE   A 1 164 ? -7.85400  14.45600 -19.26500 1.000 15.62791 ? 163 ILE   A C     1 
ATOM   1330 O  O     . ILE   A 1 164 ? -6.81100  15.06300 -18.98400 1.000 16.60595 ? 163 ILE   A O     1 
ATOM   1331 C  CB    . ILE   A 1 164 ? -10.01500 15.66600 -19.67200 1.000 15.57125 ? 163 ILE   A CB    1 
ATOM   1332 C  CG1   . ILE   A 1 164 ? -10.92300 16.28100 -20.72800 1.000 14.60032 ? 163 ILE   A CG1   1 
ATOM   1333 C  CG2   . ILE   A 1 164 ? -9.52600  16.71700 -18.66500 1.000 15.61547 ? 163 ILE   A CG2   1 
ATOM   1334 C  CD1   . ILE   A 1 164 ? -12.25300 16.70400 -20.15600 1.000 15.45507 ? 163 ILE   A CD1   1 
ATOM   1335 N  N     . ARG   A 1 165 ? -8.21000  13.33300 -18.64000 1.000 17.28370 ? 164 ARG   A N     1 
ATOM   1336 C  CA    . ARG   A 1 165 ? -7.38200  12.78100 -17.57500 1.000 20.12081 ? 164 ARG   A CA    1 
ATOM   1337 C  C     . ARG   A 1 165 ? -5.99200  12.45400 -18.09400 1.000 21.60126 ? 164 ARG   A C     1 
ATOM   1338 O  O     . ARG   A 1 165 ? -4.98600  12.81500 -17.47200 1.000 21.37110 ? 164 ARG   A O     1 
ATOM   1339 C  CB    . ARG   A 1 165 ? -8.04800  11.53900 -16.98200 1.000 21.83821 ? 164 ARG   A CB    1 
ATOM   1340 C  CG    . ARG   A 1 165 ? -7.26600  10.90000 -15.83900 1.000 24.14715 ? 164 ARG   A CG    1 
ATOM   1341 C  CD    . ARG   A 1 165 ? -8.03800  9.76700  -15.17300 1.000 29.48552 ? 164 ARG   A CD    1 
ATOM   1342 N  NE    . ARG   A 1 165 ? -7.20900  9.07200  -14.19300 1.000 34.43418 ? 164 ARG   A NE    1 
ATOM   1343 C  CZ    . ARG   A 1 165 ? -7.50600  7.89500  -13.65700 1.000 38.55952 ? 164 ARG   A CZ    1 
ATOM   1344 N  NH1   . ARG   A 1 165 ? -8.61400  7.24800  -13.98000 1.000 40.84836 ? 164 ARG   A NH1   1 
ATOM   1345 N  NH2   . ARG   A 1 165 ? -6.66500  7.34800  -12.78200 1.000 37.38022 ? 164 ARG   A NH2   1 
ATOM   1346 N  N     . LYS   A 1 166 ? -5.91700  11.79400 -19.25300 1.000 22.43783 ? 165 LYS   A N     1 
ATOM   1347 C  CA    . LYS   A 1 166 ? -4.61600  11.47400 -19.83400 1.000 24.29821 ? 165 LYS   A CA    1 
ATOM   1348 C  C     . LYS   A 1 166 ? -3.82800  12.73900 -20.13700 1.000 22.52056 ? 165 LYS   A C     1 
ATOM   1349 O  O     . LYS   A 1 166 ? -2.62600  12.81200 -19.85500 1.000 23.87463 ? 165 LYS   A O     1 
ATOM   1350 C  CB    . LYS   A 1 166 ? -4.79900  10.64900 -21.11000 1.000 28.01129 ? 165 LYS   A CB    1 
ATOM   1351 C  CG    . LYS   A 1 166 ? -5.47600  9.31200  -20.88700 1.000 38.80212 ? 165 LYS   A CG    1 
ATOM   1352 C  CD    . LYS   A 1 166 ? -5.85300  8.64200  -22.20000 1.000 46.45807 ? 165 LYS   A CD    1 
ATOM   1353 C  CE    . LYS   A 1 166 ? -4.67200  7.88600  -22.78200 1.000 52.21631 ? 165 LYS   A CE    1 
ATOM   1354 N  NZ    . LYS   A 1 166 ? -4.09600  6.92300  -21.79500 1.000 54.94345 ? 165 LYS   A NZ    1 
ATOM   1355 N  N     . HIS   A 1 167 ? -4.48700  13.74500 -20.71700 1.000 21.15408 ? 166 HIS   A N     1 
ATOM   1356 C  CA    . HIS   A 1 167 ? -3.80800  15.00000 -21.03300 1.000 20.19078 ? 166 HIS   A CA    1 
ATOM   1357 C  C     . HIS   A 1 167 ? -3.26900  15.68200 -19.77600 1.000 20.67778 ? 166 HIS   A C     1 
ATOM   1358 O  O     . HIS   A 1 167 ? -2.12700  16.15500 -19.75500 1.000 22.04691 ? 166 HIS   A O     1 
ATOM   1359 C  CB    . HIS   A 1 167 ? -4.77300  15.91500 -21.79900 1.000 22.65353 ? 166 HIS   A CB    1 
ATOM   1360 C  CG    . HIS   A 1 167 ? -4.22000  17.27700 -22.09900 1.000 26.34108 ? 166 HIS   A CG    1 
ATOM   1361 N  ND1   . HIS   A 1 167 ? -4.50700  18.38600 -21.33000 1.000 30.99643 ? 166 HIS   A ND1   1 
ATOM   1362 C  CD2   . HIS   A 1 167 ? -3.40900  17.71100 -23.09300 1.000 30.67620 ? 166 HIS   A CD2   1 
ATOM   1363 C  CE1   . HIS   A 1 167 ? -3.89200  19.44100 -21.83300 1.000 31.88412 ? 166 HIS   A CE1   1 
ATOM   1364 N  NE2   . HIS   A 1 167 ? -3.22100  19.06000 -22.90400 1.000 33.81561 ? 166 HIS   A NE2   1 
ATOM   1365 N  N     . LYS   A 1 168 ? -4.06200  15.72200 -18.70600 1.000 19.84254 ? 167 LYS   A N     1 
ATOM   1366 C  CA    . LYS   A 1 168 ? -3.62100  16.42300 -17.50600 1.000 19.99558 ? 167 LYS   A CA    1 
ATOM   1367 C  C     . LYS   A 1 168 ? -2.48500  15.69300 -16.80100 1.000 25.18041 ? 167 LYS   A C     1 
ATOM   1368 O  O     . LYS   A 1 168 ? -1.65000  16.33800 -16.15800 1.000 25.28788 ? 167 LYS   A O     1 
ATOM   1369 C  CB    . LYS   A 1 168 ? -4.79400  16.64400 -16.56100 1.000 19.22989 ? 167 LYS   A CB    1 
ATOM   1370 C  CG    . LYS   A 1 168 ? -5.77400  17.69200 -17.03800 1.000 17.34787 ? 167 LYS   A CG    1 
ATOM   1371 C  CD    . LYS   A 1 168 ? -6.79500  17.97400 -15.93300 1.000 18.71055 ? 167 LYS   A CD    1 
ATOM   1372 C  CE    . LYS   A 1 168 ? -7.68100  19.16600 -16.24400 1.000 21.71760 ? 167 LYS   A CE    1 
ATOM   1373 N  NZ    . LYS   A 1 168 ? -8.47300  19.55800 -15.04100 1.000 22.31587 ? 167 LYS   A NZ    1 
ATOM   1374 N  N     . GLU   A 1 169 ? -2.42000  14.36600 -16.91700 1.000 30.40475 ? 168 GLU   A N     1 
ATOM   1375 C  CA    . GLU   A 1 169 ? -1.42400  13.56500 -16.21000 1.000 36.91472 ? 168 GLU   A CA    1 
ATOM   1376 C  C     . GLU   A 1 169 ? -0.18000  13.25500 -17.02900 1.000 41.31931 ? 168 GLU   A C     1 
ATOM   1377 O  O     . GLU   A 1 169 ? 0.71100   12.57400 -16.51000 1.000 45.08776 ? 168 GLU   A O     1 
ATOM   1378 C  CB    . GLU   A 1 169 ? -2.03200  12.23900 -15.75300 1.000 40.02604 ? 168 GLU   A CB    1 
ATOM   1379 C  CG    . GLU   A 1 169 ? -2.87400  12.33700 -14.51900 1.000 42.76429 ? 168 GLU   A CG    1 
ATOM   1380 C  CD    . GLU   A 1 169 ? -3.36500  10.98300 -14.05300 1.000 44.43796 ? 168 GLU   A CD    1 
ATOM   1381 O  OE1   . GLU   A 1 169 ? -4.09700  10.31300 -14.81800 1.000 44.10268 ? 168 GLU   A OE1   1 
ATOM   1382 O  OE2   . GLU   A 1 169 ? -3.00700  10.58900 -12.92400 1.000 46.43568 ? 168 GLU   A OE2   1 
ATOM   1383 N  N     . LYS   A 1 170 ? -0.09500  13.72500 -18.27300 1.000 45.75357 ? 169 LYS   A N     1 
ATOM   1384 C  CA    . LYS   A 1 170 ? 1.01700   13.42100 -19.18400 1.000 52.78794 ? 169 LYS   A CA    1 
ATOM   1385 C  C     . LYS   A 1 170 ? 2.37900   13.37200 -18.49600 1.000 59.63281 ? 169 LYS   A C     1 
ATOM   1386 O  O     . LYS   A 1 170 ? 2.89400   14.40300 -18.06500 1.000 62.72823 ? 169 LYS   A O     1 
ATOM   1387 C  CB    . LYS   A 1 170 ? 1.08000   14.45500 -20.31400 1.000 53.89649 ? 169 LYS   A CB    1 
ATOM   1388 C  CG    . LYS   A 1 170 ? 0.46700   14.01100 -21.62900 1.000 55.15573 ? 169 LYS   A CG    1 
ATOM   1389 C  CD    . LYS   A 1 170 ? 1.11200   14.74600 -22.79800 1.000 56.08732 ? 169 LYS   A CD    1 
ATOM   1390 C  CE    . LYS   A 1 170 ? 0.55700   14.26900 -24.13200 1.000 57.35394 ? 169 LYS   A CE    1 
ATOM   1391 N  NZ    . LYS   A 1 170 ? 1.37700   14.73500 -25.28600 1.000 57.71195 ? 169 LYS   A NZ    1 
ATOM   1392 O  OXT   . LYS   A 1 170 ? 2.98800   12.31100 -18.35100 1.000 60.96687 ? 169 LYS   A OXT   1 
ATOM   1393 N  N     . SER   B 1 1   ? -11.37200 41.55600 -25.22300 1.000 49.16263 ? 0   SER   B N     1 
ATOM   1394 C  CA    . SER   B 1 1   ? -11.73200 40.15600 -25.02900 1.000 42.64935 ? 0   SER   B CA    1 
ATOM   1395 C  C     . SER   B 1 1   ? -12.62800 40.00100 -23.79700 1.000 36.81867 ? 0   SER   B C     1 
ATOM   1396 O  O     . SER   B 1 1   ? -13.21500 40.97200 -23.30700 1.000 37.36019 ? 0   SER   B O     1 
ATOM   1397 C  CB    . SER   B 1 1   ? -10.46400 39.29600 -24.89900 1.000 44.76782 ? 0   SER   B CB    1 
ATOM   1398 O  OG    . SER   B 1 1   ? -10.74600 37.90600 -24.93600 1.000 44.70633 ? 0   SER   B OG    1 
ATOM   1399 N  N     . MET   B 1 2   ? -12.74500 38.77600 -23.30200 1.000 28.63669 ? 1   MET   B N     1 
ATOM   1400 C  CA    . MET   B 1 2   ? -13.42800 38.53800 -22.04400 1.000 21.91343 ? 1   MET   B CA    1 
ATOM   1401 C  C     . MET   B 1 2   ? -12.67400 37.47300 -21.26700 1.000 17.11911 ? 1   MET   B C     1 
ATOM   1402 O  O     . MET   B 1 2   ? -11.74300 36.83500 -21.77400 1.000 16.63770 ? 1   MET   B O     1 
ATOM   1403 C  CB    . MET   B 1 2   ? -14.91300 38.19500 -22.22300 1.000 28.44359 ? 1   MET   B CB    1 
ATOM   1404 C  CG    . MET   B 1 2   ? -15.22200 36.77900 -22.67300 1.000 27.67388 ? 1   MET   B CG    1 
ATOM   1405 S  SD    . MET   B 1 2   ? -17.01300 36.49100 -22.59400 1.000 31.53933 ? 1   MET   B SD    1 
ATOM   1406 C  CE    . MET   B 1 2   ? -17.57900 37.43000 -24.00500 1.000 36.44724 ? 1   MET   B CE    1 
ATOM   1407 N  N     . THR   B 1 3   ? -13.06500 37.32600 -20.00700 1.000 14.65485 ? 2   THR   B N     1 
ATOM   1408 C  CA    . THR   B 1 3   ? -12.57600 36.28900 -19.10900 1.000 13.91775 ? 2   THR   B CA    1 
ATOM   1409 C  C     . THR   B 1 3   ? -13.79300 35.62100 -18.46000 1.000 12.94638 ? 2   THR   B C     1 
ATOM   1410 O  O     . THR   B 1 3   ? -14.93900 36.01700 -18.68200 1.000 16.60293 ? 2   THR   B O     1 
ATOM   1411 C  CB    . THR   B 1 3   ? -11.66500 36.89000 -18.02800 1.000 17.46040 ? 2   THR   B CB    1 
ATOM   1412 O  OG1   . THR   B 1 3   ? -12.38300 37.92800 -17.35500 1.000 20.50382 ? 2   THR   B OG1   1 
ATOM   1413 C  CG2   . THR   B 1 3   ? -10.38700 37.48000 -18.62100 1.000 18.62299 ? 2   THR   B CG2   1 
ATOM   1414 N  N     . GLU   B 1 4   ? -13.54500 34.59100 -17.66300 1.000 13.10109 ? 3   GLU   B N     1 
ATOM   1415 C  CA    . GLU   B 1 4   ? -14.60400 33.88100 -16.95800 1.000 12.89870 ? 3   GLU   B CA    1 
ATOM   1416 C  C     . GLU   B 1 4   ? -14.10100 33.53100 -15.56600 1.000 12.81698 ? 3   GLU   B C     1 
ATOM   1417 O  O     . GLU   B 1 4   ? -12.93500 33.16300 -15.40600 1.000 14.20693 ? 3   GLU   B O     1 
ATOM   1418 C  CB    . GLU   B 1 4   ? -14.98600 32.61800 -17.73400 1.000 14.82471 ? 3   GLU   B CB    1 
ATOM   1419 C  CG    . GLU   B 1 4   ? -16.03200 31.73600 -17.08800 1.000 15.66942 ? 3   GLU   B CG    1 
ATOM   1420 C  CD    . GLU   B 1 4   ? -16.60100 30.70700 -18.06900 1.000 18.50969 ? 3   GLU   B CD    1 
ATOM   1421 O  OE1   . GLU   B 1 4   ? -16.16100 30.67300 -19.23500 1.000 20.29419 ? 3   GLU   B OE1   1 
ATOM   1422 O  OE2   . GLU   B 1 4   ? -17.50000 29.93000 -17.68900 1.000 22.90526 ? 3   GLU   B OE2   1 
ATOM   1423 N  N     . TYR   B 1 5   ? -14.96600 33.68200 -14.55700 1.000 11.96586 ? 4   TYR   B N     1 
ATOM   1424 C  CA    . TYR   B 1 5   ? -14.58600 33.43500 -13.16700 1.000 14.15971 ? 4   TYR   B CA    1 
ATOM   1425 C  C     . TYR   B 1 5   ? -15.57900 32.48700 -12.52000 1.000 13.14548 ? 4   TYR   B C     1 
ATOM   1426 O  O     . TYR   B 1 5   ? -16.79700 32.70600 -12.61200 1.000 14.02532 ? 4   TYR   B O     1 
ATOM   1427 C  CB    . TYR   B 1 5   ? -14.56400 34.73900 -12.34900 1.000 15.33715 ? 4   TYR   B CB    1 
ATOM   1428 C  CG    . TYR   B 1 5   ? -13.60900 35.74000 -12.94500 1.000 13.38515 ? 4   TYR   B CG    1 
ATOM   1429 C  CD1   . TYR   B 1 5   ? -12.24200 35.55200 -12.83900 1.000 16.15487 ? 4   TYR   B CD1   1 
ATOM   1430 C  CD2   . TYR   B 1 5   ? -14.07100 36.84600 -13.63700 1.000 15.68895 ? 4   TYR   B CD2   1 
ATOM   1431 C  CE1   . TYR   B 1 5   ? -11.35800 36.44400 -13.40900 1.000 16.43796 ? 4   TYR   B CE1   1 
ATOM   1432 C  CE2   . TYR   B 1 5   ? -13.19600 37.75100 -14.19900 1.000 17.25274 ? 4   TYR   B CE2   1 
ATOM   1433 C  CZ    . TYR   B 1 5   ? -11.84300 37.54700 -14.07900 1.000 16.07719 ? 4   TYR   B CZ    1 
ATOM   1434 O  OH    . TYR   B 1 5   ? -10.99200 38.46600 -14.66900 1.000 15.55996 ? 4   TYR   B OH    1 
ATOM   1435 N  N     A LYS   B 1 6   ? -15.06400 31.44900 -11.86100 0.500 12.61567 ? 5   LYS   B N     1 
ATOM   1436 N  N     B LYS   B 1 6   ? -15.06100 31.48200 -11.81700 0.500 15.12414 ? 5   LYS   B N     1 
ATOM   1437 C  CA    A LYS   B 1 6   ? -15.86900 30.51900 -11.07300 0.500 13.69592 ? 5   LYS   B CA    1 
ATOM   1438 C  CA    B LYS   B 1 6   ? -15.87600 30.52300 -11.07300 0.500 15.19649 ? 5   LYS   B CA    1 
ATOM   1439 C  C     A LYS   B 1 6   ? -15.93300 31.03400 -9.63700  0.500 13.99430 ? 5   LYS   B C     1 
ATOM   1440 C  C     B LYS   B 1 6   ? -15.95200 30.98000 -9.62000  0.500 14.41792 ? 5   LYS   B C     1 
ATOM   1441 O  O     A LYS   B 1 6   ? -14.94300 30.97500 -8.90100  0.500 14.50273 ? 5   LYS   B O     1 
ATOM   1442 O  O     B LYS   B 1 6   ? -14.99600 30.83200 -8.85400  0.500 14.92935 ? 5   LYS   B O     1 
ATOM   1443 C  CB    A LYS   B 1 6   ? -15.25800 29.11900 -11.10600 0.500 15.05743 ? 5   LYS   B CB    1 
ATOM   1444 C  CB    B LYS   B 1 6   ? -15.28500 29.12300 -11.19600 0.500 17.09039 ? 5   LYS   B CB    1 
ATOM   1445 C  CG    A LYS   B 1 6   ? -15.01400 28.55700 -12.50500 0.500 20.33478 ? 5   LYS   B CG    1 
ATOM   1446 C  CG    B LYS   B 1 6   ? -15.19700 28.64300 -12.63900 0.500 21.12827 ? 5   LYS   B CG    1 
ATOM   1447 C  CD    A LYS   B 1 6   ? -16.30300 28.24700 -13.25100 0.500 23.80378 ? 5   LYS   B CD    1 
ATOM   1448 C  CD    B LYS   B 1 6   ? -14.29600 27.42000 -12.78000 0.500 26.11430 ? 5   LYS   B CD    1 
ATOM   1449 C  CE    A LYS   B 1 6   ? -16.01600 27.55600 -14.58500 0.500 24.67288 ? 5   LYS   B CE    1 
ATOM   1450 C  CE    B LYS   B 1 6   ? -14.88600 26.18300 -12.12900 0.500 29.49055 ? 5   LYS   B CE    1 
ATOM   1451 N  NZ    A LYS   B 1 6   ? -17.17600 27.61100 -15.52000 0.500 25.00218 ? 5   LYS   B NZ    1 
ATOM   1452 N  NZ    B LYS   B 1 6   ? -14.02000 25.00900 -12.38000 0.500 32.09738 ? 5   LYS   B NZ    1 
ATOM   1453 N  N     . LEU   B 1 7   ? -17.09000 31.55300 -9.24400  1.000 13.62782 ? 6   LEU   B N     1 
ATOM   1454 C  CA    . LEU   B 1 7   ? -17.30300 32.08400 -7.90700  1.000 13.56250 ? 6   LEU   B CA    1 
ATOM   1455 C  C     . LEU   B 1 7   ? -18.16100 31.10100 -7.13200  1.000 13.48231 ? 6   LEU   B C     1 
ATOM   1456 O  O     . LEU   B 1 7   ? -19.08200 30.50700 -7.69400  1.000 16.63672 ? 6   LEU   B O     1 
ATOM   1457 C  CB    . LEU   B 1 7   ? -18.02400 33.43700 -7.97800  1.000 14.74344 ? 6   LEU   B CB    1 
ATOM   1458 C  CG    . LEU   B 1 7   ? -17.39500 34.48300 -8.91800  1.000 13.34836 ? 6   LEU   B CG    1 
ATOM   1459 C  CD1   . LEU   B 1 7   ? -18.13000 35.81400 -8.76800  1.000 15.71205 ? 6   LEU   B CD1   1 
ATOM   1460 C  CD2   . LEU   B 1 7   ? -15.89300 34.63900 -8.66900  1.000 16.61364 ? 6   LEU   B CD2   1 
ATOM   1461 N  N     . VAL   B 1 8   ? -17.82900 30.89300 -5.85700  1.000 12.86015 ? 7   VAL   B N     1 
ATOM   1462 C  CA    . VAL   B 1 8   ? -18.56000 29.96700 -4.99700  1.000 14.49194 ? 7   VAL   B CA    1 
ATOM   1463 C  C     . VAL   B 1 8   ? -19.04000 30.73400 -3.77200  1.000 13.33809 ? 7   VAL   B C     1 
ATOM   1464 O  O     . VAL   B 1 8   ? -18.24700 31.40900 -3.10400  1.000 14.82937 ? 7   VAL   B O     1 
ATOM   1465 C  CB    . VAL   B 1 8   ? -17.68500 28.76800 -4.58600  1.000 14.68136 ? 7   VAL   B CB    1 
ATOM   1466 C  CG1   . VAL   B 1 8   ? -18.49500 27.78100 -3.70800  1.000 14.62421 ? 7   VAL   B CG1   1 
ATOM   1467 C  CG2   . VAL   B 1 8   ? -17.15200 28.07300 -5.82100  1.000 14.08984 ? 7   VAL   B CG2   1 
ATOM   1468 N  N     . VAL   B 1 9   ? -20.33000 30.60800 -3.46000  1.000 13.81165 ? 8   VAL   B N     1 
ATOM   1469 C  CA    . VAL   B 1 9   ? -20.93000 31.30700 -2.33100  1.000 13.98977 ? 8   VAL   B CA    1 
ATOM   1470 C  C     . VAL   B 1 9   ? -21.15200 30.29000 -1.21900  1.000 14.85405 ? 8   VAL   B C     1 
ATOM   1471 O  O     . VAL   B 1 9   ? -21.87900 29.30400 -1.40900  1.000 15.97799 ? 8   VAL   B O     1 
ATOM   1472 C  CB    . VAL   B 1 9   ? -22.25400 31.97200 -2.73000  1.000 15.14545 ? 8   VAL   B CB    1 
ATOM   1473 C  CG1   . VAL   B 1 9   ? -22.78100 32.81600 -1.57100  1.000 16.57873 ? 8   VAL   B CG1   1 
ATOM   1474 C  CG2   . VAL   B 1 9   ? -22.08800 32.79500 -4.02400  1.000 17.85318 ? 8   VAL   B CG2   1 
ATOM   1475 N  N     . VAL   B 1 10  ? -20.51000 30.51500 -0.07000  1.000 15.21070 ? 9   VAL   B N     1 
ATOM   1476 C  CA    . VAL   B 1 10  ? -20.56300 29.61400 1.07400   1.000 15.64395 ? 9   VAL   B CA    1 
ATOM   1477 C  C     . VAL   B 1 10  ? -20.98000 30.38800 2.32000   1.000 15.34104 ? 9   VAL   B C     1 
ATOM   1478 O  O     . VAL   B 1 10  ? -20.92200 31.61800 2.36400   1.000 16.32135 ? 9   VAL   B O     1 
ATOM   1479 C  CB    . VAL   B 1 10  ? -19.21600 28.88700 1.30500   1.000 16.26632 ? 9   VAL   B CB    1 
ATOM   1480 C  CG1   . VAL   B 1 10  ? -18.79000 28.12700 0.06200   1.000 16.89067 ? 9   VAL   B CG1   1 
ATOM   1481 C  CG2   . VAL   B 1 10  ? -18.15100 29.85500 1.77300   1.000 18.60523 ? 9   VAL   B CG2   1 
ATOM   1482 N  N     . GLY   B 1 11  ? -21.41400 29.62800 3.32200   1.000 16.76818 ? 10  GLY   B N     1 
ATOM   1483 C  CA    . GLY   B 1 11  ? -21.89800 30.25000 4.56400   1.000 16.11152 ? 10  GLY   B CA    1 
ATOM   1484 C  C     . GLY   B 1 11  ? -22.99200 29.42600 5.20200   1.000 15.96598 ? 10  GLY   B C     1 
ATOM   1485 O  O     . GLY   B 1 11  ? -23.55300 28.56000 4.53700   1.000 17.73218 ? 10  GLY   B O     1 
ATOM   1486 N  N     . ALA   B 1 12  ? -23.27000 29.70800 6.47200   1.000 17.96817 ? 11  ALA   B N     1 
ATOM   1487 C  CA    . ALA   B 1 12  ? -24.25600 28.90800 7.23000   1.000 17.32698 ? 11  ALA   B CA    1 
ATOM   1488 C  C     . ALA   B 1 12  ? -25.65900 29.01500 6.65400   1.000 18.61079 ? 11  ALA   B C     1 
ATOM   1489 O  O     . ALA   B 1 12  ? -25.98700 29.93100 5.91400   1.000 19.15399 ? 11  ALA   B O     1 
ATOM   1490 C  CB    . ALA   B 1 12  ? -24.25400 29.36900 8.66200   1.000 19.86323 ? 11  ALA   B CB    1 
ATOM   1491 N  N     . CYS   B 1 13  ? -26.50500 28.09800 7.10900   1.000 18.66136 ? 12  CYS   B N     1 
ATOM   1492 C  CA    . CYS   B 1 13  ? -27.90300 28.08800 6.64400   1.000 19.66289 ? 12  CYS   B CA    1 
ATOM   1493 C  C     . CYS   B 1 13  ? -28.61300 29.42000 6.89000   1.000 21.85382 ? 12  CYS   B C     1 
ATOM   1494 O  O     . CYS   B 1 13  ? -28.45000 29.99000 7.97100   1.000 22.16625 ? 12  CYS   B O     1 
ATOM   1495 C  CB    . CYS   B 1 13  ? -28.68400 27.01500 7.38500   1.000 22.65876 ? 12  CYS   B CB    1 
ATOM   1496 S  SG    . CYS   B 1 13  ? -28.36500 27.01000 9.16800   1.000 32.87436 ? 12  CYS   B SG    1 
ATOM   1497 N  N     . GLY   B 1 14  ? -29.33400 29.88400 5.88400   1.000 22.32472 ? 13  GLY   B N     1 
ATOM   1498 C  CA    . GLY   B 1 14  ? -30.18300 31.08100 6.04500   1.000 22.46646 ? 13  GLY   B CA    1 
ATOM   1499 C  C     . GLY   B 1 14  ? -29.47300 32.41900 6.08900   1.000 22.38725 ? 13  GLY   B C     1 
ATOM   1500 O  O     . GLY   B 1 14  ? -30.15000 33.39900 6.37200   1.000 26.16450 ? 13  GLY   B O     1 
ATOM   1501 N  N     . VAL   B 1 15  ? -28.17900 32.48400 5.80000   1.000 20.40341 ? 14  VAL   B N     1 
ATOM   1502 C  CA    . VAL   B 1 15  ? -27.48000 33.79500 5.93400   1.000 20.63540 ? 14  VAL   B CA    1 
ATOM   1503 C  C     . VAL   B 1 15  ? -27.81400 34.69400 4.72800   1.000 20.91623 ? 14  VAL   B C     1 
ATOM   1504 O  O     . VAL   B 1 15  ? -27.58100 35.89100 4.84200   1.000 24.17877 ? 14  VAL   B O     1 
ATOM   1505 C  CB    . VAL   B 1 15  ? -25.96400 33.62700 6.12400   1.000 18.20361 ? 14  VAL   B CB    1 
ATOM   1506 C  CG1   . VAL   B 1 15  ? -25.64400 32.89400 7.42000   1.000 21.53864 ? 14  VAL   B CG1   1 
ATOM   1507 C  CG2   . VAL   B 1 15  ? -25.30500 32.93400 4.93700   1.000 18.37573 ? 14  VAL   B CG2   1 
ATOM   1508 N  N     . GLY   B 1 16  ? -28.30700 34.12000 3.64100   1.000 20.08940 ? 15  GLY   B N     1 
ATOM   1509 C  CA    . GLY   B 1 16  ? -28.63700 34.88800 2.46700   1.000 20.61882 ? 15  GLY   B CA    1 
ATOM   1510 C  C     . GLY   B 1 16  ? -27.78900 34.62200 1.24400   1.000 20.01352 ? 15  GLY   B C     1 
ATOM   1511 O  O     . GLY   B 1 16  ? -27.71600 35.49000 0.36500   1.000 21.49044 ? 15  GLY   B O     1 
ATOM   1512 N  N     . LYS   B 1 17  ? -27.16100 33.45800 1.17100   1.000 18.23355 ? 16  LYS   B N     1 
ATOM   1513 C  CA    . LYS   B 1 17  ? -26.32000 33.10200 -0.00300  1.000 18.92551 ? 16  LYS   B CA    1 
ATOM   1514 C  C     . LYS   B 1 17  ? -27.16300 33.17900 -1.27900  1.000 18.57467 ? 16  LYS   B C     1 
ATOM   1515 O  O     . LYS   B 1 17  ? -26.72600 33.80600 -2.25700  1.000 19.33197 ? 16  LYS   B O     1 
ATOM   1516 C  CB    . LYS   B 1 17  ? -25.80200 31.68100 0.19900   1.000 16.06663 ? 16  LYS   B CB    1 
ATOM   1517 C  CG    . LYS   B 1 17  ? -24.86100 31.48400 1.36700   1.000 17.54915 ? 16  LYS   B CG    1 
ATOM   1518 C  CD    . LYS   B 1 17  ? -24.38800 30.04100 1.46100   1.000 19.27258 ? 16  LYS   B CD    1 
ATOM   1519 C  CE    . LYS   B 1 17  ? -25.49500 29.07800 1.75400   1.000 19.30398 ? 16  LYS   B CE    1 
ATOM   1520 N  NZ    . LYS   B 1 17  ? -26.05200 29.23100 3.09900   1.000 16.86869 ? 16  LYS   B NZ    1 
ATOM   1521 N  N     . SER   B 1 18  ? -28.33400 32.56100 -1.25400  1.000 18.34340 ? 17  SER   B N     1 
ATOM   1522 C  CA    . SER   B 1 18  ? -29.17100 32.52600 -2.44600  1.000 18.13519 ? 17  SER   B CA    1 
ATOM   1523 C  C     . SER   B 1 18  ? -29.78400 33.89100 -2.73300  1.000 19.43874 ? 17  SER   B C     1 
ATOM   1524 O  O     . SER   B 1 18  ? -29.84500 34.32000 -3.89300  1.000 20.86934 ? 17  SER   B O     1 
ATOM   1525 C  CB    . SER   B 1 18  ? -30.27300 31.48500 -2.25500  1.000 17.77966 ? 17  SER   B CB    1 
ATOM   1526 O  OG    . SER   B 1 18  ? -29.72900 30.19300 -2.12400  1.000 17.83294 ? 17  SER   B OG    1 
ATOM   1527 N  N     . ALA   B 1 19  ? -30.23200 34.59700 -1.69500  1.000 20.23435 ? 18  ALA   B N     1 
ATOM   1528 C  CA    . ALA   B 1 19  ? -30.80400 35.92100 -1.90800  1.000 22.80595 ? 18  ALA   B CA    1 
ATOM   1529 C  C     . ALA   B 1 19  ? -29.79200 36.86500 -2.55400  1.000 22.41826 ? 18  ALA   B C     1 
ATOM   1530 O  O     . ALA   B 1 19  ? -30.13600 37.63700 -3.45800  1.000 23.61057 ? 18  ALA   B O     1 
ATOM   1531 C  CB    . ALA   B 1 19  ? -31.33500 36.47500 -0.58600  1.000 25.27334 ? 18  ALA   B CB    1 
ATOM   1532 N  N     . LEU   B 1 20  ? -28.53500 36.81700 -2.10400  1.000 21.91421 ? 19  LEU   B N     1 
ATOM   1533 C  CA    . LEU   B 1 20  ? -27.48400 37.62300 -2.72700  1.000 22.27971 ? 19  LEU   B CA    1 
ATOM   1534 C  C     . LEU   B 1 20  ? -27.29200 37.23500 -4.18600  1.000 22.19767 ? 19  LEU   B C     1 
ATOM   1535 O  O     . LEU   B 1 20  ? -27.20000 38.09900 -5.07100  1.000 23.58483 ? 19  LEU   B O     1 
ATOM   1536 C  CB    . LEU   B 1 20  ? -26.17500 37.46400 -1.95100  1.000 22.25717 ? 19  LEU   B CB    1 
ATOM   1537 C  CG    . LEU   B 1 20  ? -26.08300 38.15800 -0.58200  1.000 21.58493 ? 19  LEU   B CG    1 
ATOM   1538 C  CD1   . LEU   B 1 20  ? -24.83600 37.70000 0.17600   1.000 23.36904 ? 19  LEU   B CD1   1 
ATOM   1539 C  CD2   . LEU   B 1 20  ? -26.10800 39.67900 -0.73200  1.000 24.16640 ? 19  LEU   B CD2   1 
ATOM   1540 N  N     . THR   B 1 21  ? -27.22800 35.93200 -4.45600  1.000 21.02566 ? 20  THR   B N     1 
ATOM   1541 C  CA    . THR   B 1 21  ? -27.01600 35.46200 -5.81900  1.000 21.14591 ? 20  THR   B CA    1 
ATOM   1542 C  C     . THR   B 1 21  ? -28.17900 35.86000 -6.72300  1.000 21.60679 ? 20  THR   B C     1 
ATOM   1543 O  O     . THR   B 1 21  ? -27.97800 36.33100 -7.84700  1.000 22.98724 ? 20  THR   B O     1 
ATOM   1544 C  CB    . THR   B 1 21  ? -26.82200 33.94500 -5.80700  1.000 19.88956 ? 20  THR   B CB    1 
ATOM   1545 O  OG1   . THR   B 1 21  ? -25.69000 33.62100 -4.99000  1.000 21.38821 ? 20  THR   B OG1   1 
ATOM   1546 C  CG2   . THR   B 1 21  ? -26.56700 33.42000 -7.22900  1.000 21.81341 ? 20  THR   B CG2   1 
ATOM   1547 N  N     . ILE   B 1 22  ? -29.40800 35.67300 -6.24700  1.000 23.93233 ? 21  ILE   B N     1 
ATOM   1548 C  CA    . ILE   B 1 22  ? -30.56200 35.97100 -7.08400  1.000 26.72947 ? 21  ILE   B CA    1 
ATOM   1549 C  C     . ILE   B 1 22  ? -30.67800 37.46700 -7.34400  1.000 27.56025 ? 21  ILE   B C     1 
ATOM   1550 O  O     . ILE   B 1 22  ? -31.08300 37.88600 -8.43700  1.000 28.48561 ? 21  ILE   B O     1 
ATOM   1551 C  CB    . ILE   B 1 22  ? -31.82800 35.34400 -6.47100  1.000 27.32297 ? 21  ILE   B CB    1 
ATOM   1552 C  CG1   . ILE   B 1 22  ? -31.73700 33.82100 -6.57300  1.000 29.21809 ? 21  ILE   B CG1   1 
ATOM   1553 C  CG2   . ILE   B 1 22  ? -33.09300 35.87200 -7.15500  1.000 28.03775 ? 21  ILE   B CG2   1 
ATOM   1554 C  CD1   . ILE   B 1 22  ? -32.64300 33.10100 -5.61400  1.000 33.87076 ? 21  ILE   B CD1   1 
ATOM   1555 N  N     . GLN   B 1 23  ? -30.29900 38.30200 -6.37400  1.000 26.36797 ? 22  GLN   B N     1 
ATOM   1556 C  CA    . GLN   B 1 23  ? -30.25700 39.73500 -6.64800  1.000 28.12921 ? 22  GLN   B CA    1 
ATOM   1557 C  C     . GLN   B 1 23  ? -29.27000 40.05600 -7.75900  1.000 28.90454 ? 22  GLN   B C     1 
ATOM   1558 O  O     . GLN   B 1 23  ? -29.53700 40.91200 -8.60700  1.000 31.16136 ? 22  GLN   B O     1 
ATOM   1559 C  CB    . GLN   B 1 23  ? -29.91900 40.51500 -5.38200  1.000 28.73770 ? 22  GLN   B CB    1 
ATOM   1560 C  CG    . GLN   B 1 23  ? -31.13200 40.88900 -4.56500  1.000 30.20130 ? 22  GLN   B CG    1 
ATOM   1561 C  CD    . GLN   B 1 23  ? -31.88200 42.10200 -5.12500  1.000 32.16558 ? 22  GLN   B CD    1 
ATOM   1562 O  OE1   . GLN   B 1 23  ? -31.75500 42.45600 -6.30100  1.000 32.66766 ? 22  GLN   B OE1   1 
ATOM   1563 N  NE2   . GLN   B 1 23  ? -32.66400 42.74400 -4.27400  1.000 32.31282 ? 22  GLN   B NE2   1 
ATOM   1564 N  N     . LEU   B 1 24  ? -28.12800 39.38000 -7.77700  1.000 28.62418 ? 23  LEU   B N     1 
ATOM   1565 C  CA    . LEU   B 1 24  ? -27.15100 39.62900 -8.83100  1.000 30.18229 ? 23  LEU   B CA    1 
ATOM   1566 C  C     . LEU   B 1 24  ? -27.65800 39.13400 -10.18200 1.000 29.94450 ? 23  LEU   B C     1 
ATOM   1567 O  O     . LEU   B 1 24  ? -27.58300 39.85300 -11.18800 1.000 32.47805 ? 23  LEU   B O     1 
ATOM   1568 C  CB    . LEU   B 1 24  ? -25.82700 38.95300 -8.48300  1.000 30.36468 ? 23  LEU   B CB    1 
ATOM   1569 C  CG    . LEU   B 1 24  ? -24.67000 39.27500 -9.43600  1.000 31.77474 ? 23  LEU   B CG    1 
ATOM   1570 C  CD1   . LEU   B 1 24  ? -24.13200 40.67300 -9.17700  1.000 33.72510 ? 23  LEU   B CD1   1 
ATOM   1571 C  CD2   . LEU   B 1 24  ? -23.57100 38.26400 -9.29500  1.000 33.09115 ? 23  LEU   B CD2   1 
ATOM   1572 N  N     . ILE   B 1 25  ? -28.16800 37.90100 -10.22800 1.000 32.60713 ? 24  ILE   B N     1 
ATOM   1573 C  CA    . ILE   B 1 25  ? -28.57900 37.31000 -11.49900 1.000 34.03840 ? 24  ILE   B CA    1 
ATOM   1574 C  C     . ILE   B 1 25  ? -29.85800 37.96100 -12.00800 1.000 35.78072 ? 24  ILE   B C     1 
ATOM   1575 O  O     . ILE   B 1 25  ? -29.96600 38.31400 -13.18700 1.000 38.47286 ? 24  ILE   B O     1 
ATOM   1576 C  CB    . ILE   B 1 25  ? -28.73700 35.78200 -11.37100 1.000 31.36158 ? 24  ILE   B CB    1 
ATOM   1577 C  CG1   . ILE   B 1 25  ? -27.43900 35.14400 -10.88500 1.000 29.16941 ? 24  ILE   B CG1   1 
ATOM   1578 C  CG2   . ILE   B 1 25  ? -29.14600 35.17800 -12.71500 1.000 32.27008 ? 24  ILE   B CG2   1 
ATOM   1579 C  CD1   . ILE   B 1 25  ? -26.28400 35.37400 -11.82400 1.000 26.95464 ? 24  ILE   B CD1   1 
ATOM   1580 N  N     . GLN   B 1 26  ? -30.84500 38.13100 -11.12800 1.000 36.31725 ? 25  GLN   B N     1 
ATOM   1581 C  CA    . GLN   B 1 26  ? -32.20200 38.44600 -11.55300 1.000 38.65552 ? 25  GLN   B CA    1 
ATOM   1582 C  C     . GLN   B 1 26  ? -32.74800 39.77400 -11.04500 1.000 38.52580 ? 25  GLN   B C     1 
ATOM   1583 O  O     . GLN   B 1 26  ? -33.86800 40.13600 -11.41700 1.000 39.30739 ? 25  GLN   B O     1 
ATOM   1584 C  CB    . GLN   B 1 26  ? -33.15600 37.30900 -11.16100 1.000 40.23914 ? 25  GLN   B CB    1 
ATOM   1585 C  CG    . GLN   B 1 26  ? -32.75900 35.95500 -11.72600 1.000 43.52345 ? 25  GLN   B CG    1 
ATOM   1586 C  CD    . GLN   B 1 26  ? -33.49900 34.81800 -11.06500 1.000 46.90750 ? 25  GLN   B CD    1 
ATOM   1587 O  OE1   . GLN   B 1 26  ? -34.25800 35.02700 -10.11900 1.000 49.15089 ? 25  GLN   B OE1   1 
ATOM   1588 N  NE2   . GLN   B 1 26  ? -33.28400 33.60300 -11.55600 1.000 47.99468 ? 25  GLN   B NE2   1 
ATOM   1589 N  N     . ASN   B 1 27  ? -32.01400 40.49700 -10.20000 1.000 37.47402 ? 26  ASN   B N     1 
ATOM   1590 C  CA    . ASN   B 1 27  ? -32.41700 41.83600 -9.75600  1.000 37.29797 ? 26  ASN   B CA    1 
ATOM   1591 C  C     . ASN   B 1 27  ? -33.73400 41.83100 -8.98000  1.000 35.89272 ? 26  ASN   B C     1 
ATOM   1592 O  O     . ASN   B 1 27  ? -34.57500 42.70700 -9.16300  1.000 35.93260 ? 26  ASN   B O     1 
ATOM   1593 C  CB    . ASN   B 1 27  ? -32.48400 42.83500 -10.91600 1.000 42.92292 ? 26  ASN   B CB    1 
ATOM   1594 C  CG    . ASN   B 1 27  ? -31.11900 43.24800 -11.41100 1.000 50.95376 ? 26  ASN   B CG    1 
ATOM   1595 O  OD1   . ASN   B 1 27  ? -30.51500 42.56900 -12.24300 1.000 53.91754 ? 26  ASN   B OD1   1 
ATOM   1596 N  ND2   . ASN   B 1 27  ? -30.62500 44.37300 -10.90700 1.000 52.93344 ? 26  ASN   B ND2   1 
ATOM   1597 N  N     . HIS   B 1 28  ? -33.92300 40.85500 -8.09900  1.000 34.09489 ? 27  HIS   B N     1 
ATOM   1598 C  CA    . HIS   B 1 28  ? -35.10300 40.88600 -7.24400  1.000 36.64960 ? 27  HIS   B CA    1 
ATOM   1599 C  C     . HIS   B 1 28  ? -34.84500 40.07900 -5.97900  1.000 34.27032 ? 27  HIS   B C     1 
ATOM   1600 O  O     . HIS   B 1 28  ? -33.88700 39.30500 -5.89100  1.000 33.82066 ? 27  HIS   B O     1 
ATOM   1601 C  CB    . HIS   B 1 28  ? -36.37200 40.43100 -7.97900  1.000 42.80053 ? 27  HIS   B CB    1 
ATOM   1602 C  CG    . HIS   B 1 28  ? -36.41000 38.96600 -8.27900  1.000 48.78866 ? 27  HIS   B CG    1 
ATOM   1603 N  ND1   . HIS   B 1 28  ? -36.74800 38.02200 -7.33300  1.000 52.36926 ? 27  HIS   B ND1   1 
ATOM   1604 C  CD2   . HIS   B 1 28  ? -36.16200 38.28300 -9.42100  1.000 51.06168 ? 27  HIS   B CD2   1 
ATOM   1605 C  CE1   . HIS   B 1 28  ? -36.70000 36.82000 -7.87700  1.000 53.38959 ? 27  HIS   B CE1   1 
ATOM   1606 N  NE2   . HIS   B 1 28  ? -36.34700 36.95000 -9.14400  1.000 53.31103 ? 27  HIS   B NE2   1 
ATOM   1607 N  N     . PHE   B 1 29  ? -35.73100 40.27400 -5.00100  1.000 34.61068 ? 28  PHE   B N     1 
ATOM   1608 C  CA    . PHE   B 1 29  ? -35.63300 39.68800 -3.67300  1.000 34.34222 ? 28  PHE   B CA    1 
ATOM   1609 C  C     . PHE   B 1 29  ? -37.02000 39.25100 -3.22900  1.000 37.59475 ? 28  PHE   B C     1 
ATOM   1610 O  O     . PHE   B 1 29  ? -38.00200 39.95900 -3.46500  1.000 38.73960 ? 28  PHE   B O     1 
ATOM   1611 C  CB    . PHE   B 1 29  ? -35.10400 40.73500 -2.67800  1.000 34.26249 ? 28  PHE   B CB    1 
ATOM   1612 C  CG    . PHE   B 1 29  ? -35.13300 40.28900 -1.23800  1.000 33.90301 ? 28  PHE   B CG    1 
ATOM   1613 C  CD1   . PHE   B 1 29  ? -34.07200 39.58300 -0.70000  1.000 34.87987 ? 28  PHE   B CD1   1 
ATOM   1614 C  CD2   . PHE   B 1 29  ? -36.21000 40.59500 -0.41300  1.000 32.98190 ? 28  PHE   B CD2   1 
ATOM   1615 C  CE1   . PHE   B 1 29  ? -34.09000 39.17900 0.61900   1.000 34.76309 ? 28  PHE   B CE1   1 
ATOM   1616 C  CE2   . PHE   B 1 29  ? -36.22600 40.18500 0.91000   1.000 33.35035 ? 28  PHE   B CE2   1 
ATOM   1617 C  CZ    . PHE   B 1 29  ? -35.16700 39.48200 1.42400   1.000 34.73672 ? 28  PHE   B CZ    1 
ATOM   1618 N  N     . VAL   B 1 30  ? -37.09700 38.09000 -2.57900  1.000 37.79611 ? 29  VAL   B N     1 
ATOM   1619 C  CA    . VAL   B 1 30  ? -38.32100 37.63100 -1.93500  1.000 42.13977 ? 29  VAL   B CA    1 
ATOM   1620 C  C     . VAL   B 1 30  ? -38.00700 37.30000 -0.48500  1.000 42.94303 ? 29  VAL   B C     1 
ATOM   1621 O  O     . VAL   B 1 30  ? -36.90500 36.84900 -0.15400  1.000 44.14350 ? 29  VAL   B O     1 
ATOM   1622 C  CB    . VAL   B 1 30  ? -38.98600 36.42600 -2.64600  1.000 43.18497 ? 29  VAL   B CB    1 
ATOM   1623 C  CG1   . VAL   B 1 30  ? -39.38600 36.79600 -4.07200  1.000 43.16840 ? 29  VAL   B CG1   1 
ATOM   1624 C  CG2   . VAL   B 1 30  ? -38.07100 35.20300 -2.62400  1.000 44.02361 ? 29  VAL   B CG2   1 
ATOM   1625 N  N     . ASP   B 1 31  ? -38.98500 37.54900 0.38900   1.000 42.40784 ? 30  ASP   B N     1 
ATOM   1626 C  CA    . ASP   B 1 31  ? -38.84100 37.16400 1.78700   1.000 40.93399 ? 30  ASP   B CA    1 
ATOM   1627 C  C     . ASP   B 1 31  ? -38.90600 35.65300 1.97200   1.000 41.20261 ? 30  ASP   B C     1 
ATOM   1628 O  O     . ASP   B 1 31  ? -38.45300 35.14400 3.00300   1.000 41.03378 ? 30  ASP   B O     1 
ATOM   1629 C  CB    . ASP   B 1 31  ? -39.90600 37.86100 2.63900   1.000 44.99335 ? 30  ASP   B CB    1 
ATOM   1630 C  CG    . ASP   B 1 31  ? -39.60800 39.33300 2.85600   1.000 49.36986 ? 30  ASP   B CG    1 
ATOM   1631 O  OD1   . ASP   B 1 31  ? -38.49100 39.66300 3.30600   1.000 50.26685 ? 30  ASP   B OD1   1 
ATOM   1632 O  OD2   . ASP   B 1 31  ? -40.49100 40.16600 2.57500   1.000 52.37327 ? 30  ASP   B OD2   1 
ATOM   1633 N  N     . GLU   B 1 32  ? -39.42200 34.92800 0.98300   1.000 40.33255 ? 31  GLU   B N     1 
ATOM   1634 C  CA    . GLU   B 1 32  ? -39.62400 33.49700 1.13400   1.000 38.75921 ? 31  GLU   B CA    1 
ATOM   1635 C  C     . GLU   B 1 32  ? -38.29400 32.75000 1.11400   1.000 31.19931 ? 31  GLU   B C     1 
ATOM   1636 O  O     . GLU   B 1 32  ? -37.39900 33.05300 0.32100   1.000 30.89728 ? 31  GLU   B O     1 
ATOM   1637 C  CB    . GLU   B 1 32  ? -40.54100 32.98000 0.02800   1.000 44.15294 ? 31  GLU   B CB    1 
ATOM   1638 C  CG    . GLU   B 1 32  ? -41.02600 31.56000 0.25300   1.000 47.68524 ? 31  GLU   B CG    1 
ATOM   1639 C  CD    . GLU   B 1 32  ? -42.36000 31.29400 -0.41600  1.000 50.59466 ? 31  GLU   B CD    1 
ATOM   1640 O  OE1   . GLU   B 1 32  ? -42.71200 32.02900 -1.36500  1.000 52.23828 ? 31  GLU   B OE1   1 
ATOM   1641 O  OE2   . GLU   B 1 32  ? -43.06100 30.35900 0.02000   1.000 49.18076 ? 31  GLU   B OE2   1 
ATOM   1642 N  N     . TYR   B 1 33  ? -38.18500 31.78200 2.01800   1.000 27.24648 ? 32  TYR   B N     1 
ATOM   1643 C  CA    . TYR   B 1 33  ? -36.96700 30.94600 2.13800   1.000 24.08134 ? 32  TYR   B CA    1 
ATOM   1644 C  C     . TYR   B 1 33  ? -37.15100 29.65600 1.38300   1.000 23.92678 ? 32  TYR   B C     1 
ATOM   1645 O  O     . TYR   B 1 33  ? -38.07100 28.88800 1.66200   1.000 23.82668 ? 32  TYR   B O     1 
ATOM   1646 C  CB    . TYR   B 1 33  ? -36.73200 30.69900 3.63400   1.000 23.69312 ? 32  TYR   B CB    1 
ATOM   1647 C  CG    . TYR   B 1 33  ? -35.51600 29.86700 4.01800   1.000 23.33701 ? 32  TYR   B CG    1 
ATOM   1648 C  CD1   . TYR   B 1 33  ? -34.43800 29.70500 3.15700   1.000 23.52016 ? 32  TYR   B CD1   1 
ATOM   1649 C  CD2   . TYR   B 1 33  ? -35.43600 29.26200 5.26400   1.000 24.21484 ? 32  TYR   B CD2   1 
ATOM   1650 C  CE1   . TYR   B 1 33  ? -33.33100 28.95300 3.51500   1.000 23.55532 ? 32  TYR   B CE1   1 
ATOM   1651 C  CE2   . TYR   B 1 33  ? -34.33600 28.51000 5.63400   1.000 24.84577 ? 32  TYR   B CE2   1 
ATOM   1652 C  CZ    . TYR   B 1 33  ? -33.27900 28.35200 4.75800   1.000 23.31865 ? 32  TYR   B CZ    1 
ATOM   1653 O  OH    . TYR   B 1 33  ? -32.19700 27.61500 5.14100   1.000 23.75598 ? 32  TYR   B OH    1 
ATOM   1654 N  N     . ASP   B 1 34  ? -36.29200 29.42800 0.40400   1.000 21.97205 ? 33  ASP   B N     1 
ATOM   1655 C  CA    . ASP   B 1 34  ? -36.27700 28.17800 -0.35200  1.000 22.52469 ? 33  ASP   B CA    1 
ATOM   1656 C  C     . ASP   B 1 34  ? -34.92200 27.53000 -0.11500  1.000 20.62010 ? 33  ASP   B C     1 
ATOM   1657 O  O     . ASP   B 1 34  ? -33.93800 27.89200 -0.78200  1.000 20.03100 ? 33  ASP   B O     1 
ATOM   1658 C  CB    . ASP   B 1 34  ? -36.48100 28.47000 -1.83700  1.000 23.49924 ? 33  ASP   B CB    1 
ATOM   1659 C  CG    . ASP   B 1 34  ? -36.56100 27.20900 -2.67800  1.000 26.69216 ? 33  ASP   B CG    1 
ATOM   1660 O  OD1   . ASP   B 1 34  ? -36.61300 26.09300 -2.10600  1.000 27.73587 ? 33  ASP   B OD1   1 
ATOM   1661 O  OD2   . ASP   B 1 34  ? -36.56500 27.34100 -3.92000  1.000 32.23977 ? 33  ASP   B OD2   1 
ATOM   1662 N  N     . PRO   B 1 35  ? -34.81500 26.59000 0.82900   1.000 20.55251 ? 34  PRO   B N     1 
ATOM   1663 C  CA    . PRO   B 1 35  ? -33.50400 26.01000 1.18100   1.000 19.63957 ? 34  PRO   B CA    1 
ATOM   1664 C  C     . PRO   B 1 35  ? -32.83600 25.35100 -0.01800  1.000 19.26739 ? 34  PRO   B C     1 
ATOM   1665 O  O     . PRO   B 1 35  ? -33.45400 24.58100 -0.75600  1.000 22.15572 ? 34  PRO   B O     1 
ATOM   1666 C  CB    . PRO   B 1 35  ? -33.84900 24.98300 2.26900   1.000 21.01346 ? 34  PRO   B CB    1 
ATOM   1667 C  CG    . PRO   B 1 35  ? -35.15600 25.47300 2.84600   1.000 22.46070 ? 34  PRO   B CG    1 
ATOM   1668 C  CD    . PRO   B 1 35  ? -35.90100 26.09900 1.69800   1.000 22.70561 ? 34  PRO   B CD    1 
ATOM   1669 N  N     . THR   B 1 36  ? -31.55400 25.65800 -0.19900  1.000 16.77735 ? 35  THR   B N     1 
ATOM   1670 C  CA    . THR   B 1 36  ? -30.79500 25.21200 -1.36500  1.000 18.02321 ? 35  THR   B CA    1 
ATOM   1671 C  C     . THR   B 1 36  ? -30.31800 23.77300 -1.22700  1.000 15.47650 ? 35  THR   B C     1 
ATOM   1672 O  O     . THR   B 1 36  ? -29.91800 23.32700 -0.14300  1.000 17.18665 ? 35  THR   B O     1 
ATOM   1673 C  CB    . THR   B 1 36  ? -29.59800 26.14200 -1.54400  1.000 17.37583 ? 35  THR   B CB    1 
ATOM   1674 O  OG1   . THR   B 1 36  ? -30.10500 27.46200 -1.72600  1.000 17.89518 ? 35  THR   B OG1   1 
ATOM   1675 C  CG2   . THR   B 1 36  ? -28.73500 25.75500 -2.76900  1.000 16.80725 ? 35  THR   B CG2   1 
ATOM   1676 N  N     . ILE   B 1 37  ? -30.36900 23.04300 -2.34000  1.000 16.10981 ? 36  ILE   B N     1 
ATOM   1677 C  CA    . ILE   B 1 37  ? -29.58300 21.82500 -2.50900  1.000 15.28750 ? 36  ILE   B CA    1 
ATOM   1678 C  C     . ILE   B 1 37  ? -28.29700 22.24800 -3.20400  1.000 14.41506 ? 36  ILE   B C     1 
ATOM   1679 O  O     . ILE   B 1 37  ? -27.21100 22.18000 -2.61600  1.000 16.18393 ? 36  ILE   B O     1 
ATOM   1680 C  CB    . ILE   B 1 37  ? -30.35500 20.75700 -3.30700  1.000 17.47701 ? 36  ILE   B CB    1 
ATOM   1681 C  CG1   . ILE   B 1 37  ? -31.54900 20.25100 -2.50000  1.000 20.14158 ? 36  ILE   B CG1   1 
ATOM   1682 C  CG2   . ILE   B 1 37  ? -29.44100 19.59800 -3.67300  1.000 18.83691 ? 36  ILE   B CG2   1 
ATOM   1683 C  CD1   . ILE   B 1 37  ? -31.13800 19.41500 -1.31100  1.000 21.81206 ? 36  ILE   B CD1   1 
ATOM   1684 N  N     . GLU   B 1 38  ? -28.41900 22.73100 -4.44000  1.000 15.63174 ? 37  GLU   B N     1 
ATOM   1685 C  CA    . GLU   B 1 38  ? -27.29100 23.26400 -5.19500  1.000 14.86233 ? 37  GLU   B CA    1 
ATOM   1686 C  C     . GLU   B 1 38  ? -27.85100 23.93100 -6.43500  1.000 15.18193 ? 37  GLU   B C     1 
ATOM   1687 O  O     . GLU   B 1 38  ? -28.73600 23.37500 -7.08900  1.000 17.36249 ? 37  GLU   B O     1 
ATOM   1688 C  CB    . GLU   B 1 38  ? -26.33100 22.15000 -5.63700  1.000 15.65236 ? 37  GLU   B CB    1 
ATOM   1689 C  CG    . GLU   B 1 38  ? -25.03100 22.65500 -6.26800  1.000 16.13586 ? 37  GLU   B CG    1 
ATOM   1690 C  CD    . GLU   B 1 38  ? -24.31700 21.53900 -6.98600  1.000 17.11129 ? 37  GLU   B CD    1 
ATOM   1691 O  OE1   . GLU   B 1 38  ? -23.71700 20.67200 -6.30100  1.000 18.70363 ? 37  GLU   B OE1   1 
ATOM   1692 O  OE2   . GLU   B 1 38  ? -24.37600 21.51300 -8.23700  1.000 17.38141 ? 37  GLU   B OE2   1 
ATOM   1693 N  N     . ASP   B 1 39  ? -27.33500 25.11300 -6.75900  1.000 16.59658 ? 38  ASP   B N     1 
ATOM   1694 C  CA    . ASP   B 1 39  ? -27.74800 25.82500 -7.95700  1.000 17.60893 ? 38  ASP   B CA    1 
ATOM   1695 C  C     . ASP   B 1 39  ? -26.55400 26.55400 -8.54000  1.000 16.02918 ? 38  ASP   B C     1 
ATOM   1696 O  O     . ASP   B 1 39  ? -25.62800 26.93800 -7.82300  1.000 15.51309 ? 38  ASP   B O     1 
ATOM   1697 C  CB    . ASP   B 1 39  ? -28.84500 26.84300 -7.65000  1.000 19.41746 ? 38  ASP   B CB    1 
ATOM   1698 C  CG    . ASP   B 1 39  ? -30.15300 26.18600 -7.29000  1.000 21.87276 ? 38  ASP   B CG    1 
ATOM   1699 O  OD1   . ASP   B 1 39  ? -30.77300 25.56000 -8.17800  1.000 24.71587 ? 38  ASP   B OD1   1 
ATOM   1700 O  OD2   . ASP   B 1 39  ? -30.54900 26.27700 -6.11100  1.000 25.50468 ? 38  ASP   B OD2   1 
ATOM   1701 N  N     . SER   B 1 40  ? -26.58200 26.72000 -9.85200  1.000 16.89489 ? 39  SER   B N     1 
ATOM   1702 C  CA    . SER   B 1 40  ? -25.51800 27.39300 -10.57800 1.000 17.77330 ? 39  SER   B CA    1 
ATOM   1703 C  C     . SER   B 1 40  ? -26.13200 28.37900 -11.55500 1.000 17.91792 ? 39  SER   B C     1 
ATOM   1704 O  O     . SER   B 1 40  ? -27.18600 28.11500 -12.14200 1.000 20.79490 ? 39  SER   B O     1 
ATOM   1705 C  CB    . SER   B 1 40  ? -24.67700 26.39600 -11.38200 1.000 20.39475 ? 39  SER   B CB    1 
ATOM   1706 O  OG    . SER   B 1 40  ? -23.91500 25.57200 -10.52700 1.000 23.74143 ? 39  SER   B OG    1 
ATOM   1707 N  N     . TYR   B 1 41  ? -25.44200 29.49700 -11.76200 1.000 18.62218 ? 40  TYR   B N     1 
ATOM   1708 C  CA    . TYR   B 1 41  ? -25.94700 30.56400 -12.60700 1.000 20.83951 ? 40  TYR   B CA    1 
ATOM   1709 C  C     . TYR   B 1 41  ? -24.78400 31.11400 -13.40300 1.000 19.17764 ? 40  TYR   B C     1 
ATOM   1710 O  O     . TYR   B 1 41  ? -23.63100 30.98400 -13.00300 1.000 18.46366 ? 40  TYR   B O     1 
ATOM   1711 C  CB    . TYR   B 1 41  ? -26.54100 31.70400 -11.77600 1.000 21.79748 ? 40  TYR   B CB    1 
ATOM   1712 C  CG    . TYR   B 1 41  ? -27.62000 31.26200 -10.81700 1.000 22.62447 ? 40  TYR   B CG    1 
ATOM   1713 C  CD1   . TYR   B 1 41  ? -27.29200 30.83700 -9.54000  1.000 23.86454 ? 40  TYR   B CD1   1 
ATOM   1714 C  CD2   . TYR   B 1 41  ? -28.96200 31.27400 -11.18600 1.000 26.00713 ? 40  TYR   B CD2   1 
ATOM   1715 C  CE1   . TYR   B 1 41  ? -28.27200 30.42700 -8.65200  1.000 24.88282 ? 40  TYR   B CE1   1 
ATOM   1716 C  CE2   . TYR   B 1 41  ? -29.95200 30.86800 -10.31000 1.000 28.33714 ? 40  TYR   B CE2   1 
ATOM   1717 C  CZ    . TYR   B 1 41  ? -29.60400 30.44200 -9.04500  1.000 27.05723 ? 40  TYR   B CZ    1 
ATOM   1718 O  OH    . TYR   B 1 41  ? -30.59100 30.03800 -8.17300  1.000 29.73519 ? 40  TYR   B OH    1 
ATOM   1719 N  N     . ARG   B 1 42  ? -25.10100 31.73800 -14.53100 1.000 18.06319 ? 41  ARG   B N     1 
ATOM   1720 C  CA    . ARG   B 1 42  ? -24.10700 32.37600 -15.38500 1.000 18.58432 ? 41  ARG   B CA    1 
ATOM   1721 C  C     . ARG   B 1 42  ? -24.63100 33.74500 -15.77700 1.000 17.57468 ? 41  ARG   B C     1 
ATOM   1722 O  O     . ARG   B 1 42  ? -25.82100 33.89200 -16.06400 1.000 18.39739 ? 41  ARG   B O     1 
ATOM   1723 C  CB    . ARG   B 1 42  ? -23.83900 31.54000 -16.65400 1.000 20.40345 ? 41  ARG   B CB    1 
ATOM   1724 C  CG    . ARG   B 1 42  ? -23.03900 30.26300 -16.41700 1.000 20.75706 ? 41  ARG   B CG    1 
ATOM   1725 C  CD    . ARG   B 1 42  ? -23.09800 29.27400 -17.59400 1.000 22.31389 ? 41  ARG   B CD    1 
ATOM   1726 N  NE    . ARG   B 1 42  ? -22.48800 29.74300 -18.83700 1.000 22.84838 ? 41  ARG   B NE    1 
ATOM   1727 C  CZ    . ARG   B 1 42  ? -21.18500 29.70400 -19.10900 1.000 22.90730 ? 41  ARG   B CZ    1 
ATOM   1728 N  NH1   . ARG   B 1 42  ? -20.29500 29.36100 -18.19400 1.000 25.13763 ? 41  ARG   B NH1   1 
ATOM   1729 N  NH2   . ARG   B 1 42  ? -20.76800 30.02300 -20.33200 1.000 23.16502 ? 41  ARG   B NH2   1 
ATOM   1730 N  N     . LYS   B 1 43  ? -23.73800 34.74100 -15.81100 1.000 16.14402 ? 42  LYS   B N     1 
ATOM   1731 C  CA    . LYS   B 1 43  ? -24.11400 36.10100 -16.17300 1.000 16.14689 ? 42  LYS   B CA    1 
ATOM   1732 C  C     . LYS   B 1 43  ? -22.90000 36.82100 -16.73500 1.000 15.77004 ? 42  LYS   B C     1 
ATOM   1733 O  O     . LYS   B 1 43  ? -21.79700 36.70900 -16.19400 1.000 17.09301 ? 42  LYS   B O     1 
ATOM   1734 C  CB    . LYS   B 1 43  ? -24.63000 36.89700 -14.96300 1.000 20.01281 ? 42  LYS   B CB    1 
ATOM   1735 C  CG    . LYS   B 1 43  ? -25.27000 38.22200 -15.33800 1.000 25.48029 ? 42  LYS   B CG    1 
ATOM   1736 C  CD    . LYS   B 1 43  ? -25.60700 39.06500 -14.11700 1.000 28.67532 ? 42  LYS   B CD    1 
ATOM   1737 C  CE    . LYS   B 1 43  ? -26.48100 40.25100 -14.50100 1.000 34.22274 ? 42  LYS   B CE    1 
ATOM   1738 N  NZ    . LYS   B 1 43  ? -26.59600 41.24200 -13.40800 1.000 38.02242 ? 42  LYS   B NZ    1 
ATOM   1739 N  N     . GLN   B 1 44  ? -23.10300 37.55300 -17.82100 1.000 15.27707 ? 43  GLN   B N     1 
ATOM   1740 C  CA    . GLN   B 1 44  ? -22.05400 38.37200 -18.41100 1.000 15.10368 ? 43  GLN   B CA    1 
ATOM   1741 C  C     . GLN   B 1 44  ? -22.14800 39.78200 -17.84800 1.000 15.52454 ? 43  GLN   B C     1 
ATOM   1742 O  O     . GLN   B 1 44  ? -23.22300 40.38600 -17.85600 1.000 18.87632 ? 43  GLN   B O     1 
ATOM   1743 C  CB    . GLN   B 1 44  ? -22.24700 38.41500 -19.92300 1.000 15.98507 ? 43  GLN   B CB    1 
ATOM   1744 C  CG    . GLN   B 1 44  ? -21.16600 39.19300 -20.62900 1.000 19.30572 ? 43  GLN   B CG    1 
ATOM   1745 C  CD    . GLN   B 1 44  ? -21.41100 39.27600 -22.11800 1.000 25.89381 ? 43  GLN   B CD    1 
ATOM   1746 O  OE1   . GLN   B 1 44  ? -21.85300 38.31100 -22.73400 1.000 29.75401 ? 43  GLN   B OE1   1 
ATOM   1747 N  NE2   . GLN   B 1 44  ? -21.14300 40.43900 -22.70300 1.000 30.20448 ? 43  GLN   B NE2   1 
ATOM   1748 N  N     . VAL   B 1 45  ? -21.02800 40.30700 -17.34900 1.000 15.78343 ? 44  VAL   B N     1 
ATOM   1749 C  CA    . VAL   B 1 45  ? -20.99100 41.62200 -16.72200 1.000 16.38695 ? 44  VAL   B CA    1 
ATOM   1750 C  C     . VAL   B 1 45  ? -19.73500 42.34300 -17.18900 1.000 16.12809 ? 44  VAL   B C     1 
ATOM   1751 O  O     . VAL   B 1 45  ? -18.84000 41.75700 -17.79500 1.000 16.96171 ? 44  VAL   B O     1 
ATOM   1752 C  CB    . VAL   B 1 45  ? -21.03600 41.56000 -15.17300 1.000 17.96099 ? 44  VAL   B CB    1 
ATOM   1753 C  CG1   . VAL   B 1 45  ? -22.30800 40.87500 -14.68500 1.000 20.02610 ? 44  VAL   B CG1   1 
ATOM   1754 C  CG2   . VAL   B 1 45  ? -19.78800 40.87000 -14.63900 1.000 19.25757 ? 44  VAL   B CG2   1 
ATOM   1755 N  N     . VAL   B 1 46  ? -19.67500 43.63700 -16.89700 1.000 17.85867 ? 45  VAL   B N     1 
ATOM   1756 C  CA    . VAL   B 1 46  ? -18.48100 44.44400 -17.13200 1.000 17.27405 ? 45  VAL   B CA    1 
ATOM   1757 C  C     . VAL   B 1 46  ? -18.03900 44.99200 -15.78100 1.000 15.98295 ? 45  VAL   B C     1 
ATOM   1758 O  O     . VAL   B 1 46  ? -18.79400 45.72100 -15.12600 1.000 19.68135 ? 45  VAL   B O     1 
ATOM   1759 C  CB    . VAL   B 1 46  ? -18.72400 45.58500 -18.13300 1.000 20.01698 ? 45  VAL   B CB    1 
ATOM   1760 C  CG1   . VAL   B 1 46  ? -17.41000 46.33900 -18.38500 1.000 21.87494 ? 45  VAL   B CG1   1 
ATOM   1761 C  CG2   . VAL   B 1 46  ? -19.28700 45.05000 -19.43300 1.000 19.40909 ? 45  VAL   B CG2   1 
ATOM   1762 N  N     . ILE   B 1 47  ? -16.82700 44.64600 -15.36200 1.000 14.38103 ? 46  ILE   B N     1 
ATOM   1763 C  CA    . ILE   B 1 47  ? -16.28300 45.08100 -14.07900 1.000 15.75678 ? 46  ILE   B CA    1 
ATOM   1764 C  C     . ILE   B 1 47  ? -15.00500 45.85300 -14.35900 1.000 15.17713 ? 46  ILE   B C     1 
ATOM   1765 O  O     . ILE   B 1 47  ? -14.06400 45.30900 -14.95500 1.000 15.51954 ? 46  ILE   B O     1 
ATOM   1766 C  CB    . ILE   B 1 47  ? -16.00800 43.88800 -13.15200 1.000 16.24008 ? 46  ILE   B CB    1 
ATOM   1767 C  CG1   . ILE   B 1 47  ? -17.30400 43.11800 -12.84000 1.000 15.51278 ? 46  ILE   B CG1   1 
ATOM   1768 C  CG2   . ILE   B 1 47  ? -15.28900 44.34700 -11.86200 1.000 17.04341 ? 46  ILE   B CG2   1 
ATOM   1769 C  CD1   . ILE   B 1 47  ? -17.04900 41.78800 -12.17400 1.000 17.09990 ? 46  ILE   B CD1   1 
ATOM   1770 N  N     . ASP   B 1 48  ? -14.96700 47.11700 -13.93300 1.000 16.92761 ? 47  ASP   B N     1 
ATOM   1771 C  CA    . ASP   B 1 48  ? -13.81600 47.99600 -14.19700 1.000 17.33071 ? 47  ASP   B CA    1 
ATOM   1772 C  C     . ASP   B 1 48  ? -13.44500 48.03800 -15.68000 1.000 18.54558 ? 47  ASP   B C     1 
ATOM   1773 O  O     . ASP   B 1 48  ? -12.27200 48.04500 -16.04500 1.000 19.97945 ? 47  ASP   B O     1 
ATOM   1774 C  CB    . ASP   B 1 48  ? -12.59300 47.64200 -13.34400 1.000 17.40179 ? 47  ASP   B CB    1 
ATOM   1775 C  CG    . ASP   B 1 48  ? -12.87500 47.67600 -11.87800 1.000 17.19585 ? 47  ASP   B CG    1 
ATOM   1776 O  OD1   . ASP   B 1 48  ? -13.85300 48.33300 -11.48000 1.000 19.64759 ? 47  ASP   B OD1   1 
ATOM   1777 O  OD2   . ASP   B 1 48  ? -12.10600 47.05200 -11.12100 1.000 20.16978 ? 47  ASP   B OD2   1 
ATOM   1778 N  N     . GLY   B 1 49  ? -14.45400 48.07600 -16.54400 1.000 17.63876 ? 48  GLY   B N     1 
ATOM   1779 C  CA    . GLY   B 1 49  ? -14.22600 48.17200 -17.96900 1.000 19.13616 ? 48  GLY   B CA    1 
ATOM   1780 C  C     . GLY   B 1 49  ? -13.88200 46.87400 -18.66500 1.000 19.65801 ? 48  GLY   B C     1 
ATOM   1781 O  O     . GLY   B 1 49  ? -13.68300 46.88500 -19.88700 1.000 23.13437 ? 48  GLY   B O     1 
ATOM   1782 N  N     . GLU   B 1 50  ? -13.79000 45.75800 -17.94300 1.000 16.51889 ? 49  GLU   B N     1 
ATOM   1783 C  CA    . GLU   B 1 50  ? -13.41400 44.47800 -18.53400 1.000 17.06148 ? 49  GLU   B CA    1 
ATOM   1784 C  C     . GLU   B 1 50  ? -14.57300 43.49700 -18.47000 1.000 16.42834 ? 49  GLU   B C     1 
ATOM   1785 O  O     . GLU   B 1 50  ? -15.06700 43.18600 -17.38100 1.000 18.06246 ? 49  GLU   B O     1 
ATOM   1786 C  CB    . GLU   B 1 50  ? -12.18400 43.90400 -17.83800 1.000 22.53562 ? 49  GLU   B CB    1 
ATOM   1787 C  CG    . GLU   B 1 50  ? -10.92300 44.67700 -18.20000 1.000 30.28292 ? 49  GLU   B CG    1 
ATOM   1788 C  CD    . GLU   B 1 50  ? -10.53300 44.51800 -19.67600 1.000 40.98257 ? 49  GLU   B CD    1 
ATOM   1789 O  OE1   . GLU   B 1 50  ? -10.96500 43.52900 -20.31900 1.000 44.22007 ? 49  GLU   B OE1   1 
ATOM   1790 O  OE2   . GLU   B 1 50  ? -9.79000  45.38500 -20.19300 1.000 44.57303 ? 49  GLU   B OE2   1 
ATOM   1791 N  N     . THR   B 1 51  ? -14.96700 42.97300 -19.62400 1.000 15.40299 ? 50  THR   B N     1 
ATOM   1792 C  CA    . THR   B 1 51  ? -16.09900 42.05800 -19.70300 1.000 15.36930 ? 50  THR   B CA    1 
ATOM   1793 C  C     . THR   B 1 51  ? -15.72200 40.68100 -19.18000 1.000 14.28098 ? 50  THR   B C     1 
ATOM   1794 O  O     . THR   B 1 51  ? -14.62100 40.17000 -19.43300 1.000 15.75938 ? 50  THR   B O     1 
ATOM   1795 C  CB    . THR   B 1 51  ? -16.56700 41.94300 -21.15900 1.000 18.78208 ? 50  THR   B CB    1 
ATOM   1796 O  OG1   . THR   B 1 51  ? -16.92100 43.24500 -21.64200 1.000 21.96269 ? 50  THR   B OG1   1 
ATOM   1797 C  CG2   . THR   B 1 51  ? -17.77800 41.00800 -21.28500 1.000 21.25314 ? 50  THR   B CG2   1 
ATOM   1798 N  N     . CYS   B 1 52  ? -16.65000 40.06900 -18.44300 1.000 14.77753 ? 51  CYS   B N     1 
ATOM   1799 C  CA    . CYS   B 1 52  ? -16.39700 38.71500 -17.98800 1.000 15.45119 ? 51  CYS   B CA    1 
ATOM   1800 C  C     . CYS   B 1 52  ? -17.69900 37.95600 -17.82300 1.000 15.17225 ? 51  CYS   B C     1 
ATOM   1801 O  O     . CYS   B 1 52  ? -18.78900 38.53700 -17.71200 1.000 15.98392 ? 51  CYS   B O     1 
ATOM   1802 C  CB    . CYS   B 1 52  ? -15.56700 38.67400 -16.70000 1.000 17.52842 ? 51  CYS   B CB    1 
ATOM   1803 S  SG    . CYS   B 1 52  ? -16.32500 39.58600 -15.36300 1.000 19.13354 ? 51  CYS   B SG    1 
ATOM   1804 N  N     . LEU   B 1 53  ? -17.56300 36.63600 -17.84500 1.000 14.12951 ? 52  LEU   B N     1 
ATOM   1805 C  CA    . LEU   B 1 53  ? -18.64200 35.72000 -17.52600 1.000 14.68263 ? 52  LEU   B CA    1 
ATOM   1806 C  C     . LEU   B 1 53  ? -18.45400 35.29500 -16.08300 1.000 14.87882 ? 52  LEU   B C     1 
ATOM   1807 O  O     . LEU   B 1 53  ? -17.38700 34.79300 -15.71900 1.000 15.91715 ? 52  LEU   B O     1 
ATOM   1808 C  CB    . LEU   B 1 53  ? -18.54100 34.48300 -18.41000 1.000 19.28789 ? 52  LEU   B CB    1 
ATOM   1809 C  CG    . LEU   B 1 53  ? -19.19400 34.46500 -19.77700 1.000 27.00917 ? 52  LEU   B CG    1 
ATOM   1810 C  CD1   . LEU   B 1 53  ? -18.88400 33.15100 -20.46100 1.000 25.71317 ? 52  LEU   B CD1   1 
ATOM   1811 C  CD2   . LEU   B 1 53  ? -20.69300 34.62000 -19.57600 1.000 27.66850 ? 52  LEU   B CD2   1 
ATOM   1812 N  N     . LEU   B 1 54  ? -19.48900 35.47000 -15.27100 1.000 14.22002 ? 53  LEU   B N     1 
ATOM   1813 C  CA    . LEU   B 1 54  ? -19.47800 34.96800 -13.90700 1.000 15.39579 ? 53  LEU   B CA    1 
ATOM   1814 C  C     . LEU   B 1 54  ? -20.23900 33.65600 -13.88300 1.000 15.80995 ? 53  LEU   B C     1 
ATOM   1815 O  O     . LEU   B 1 54  ? -21.39400 33.59200 -14.33100 1.000 16.97570 ? 53  LEU   B O     1 
ATOM   1816 C  CB    . LEU   B 1 54  ? -20.11900 35.94600 -12.92200 1.000 16.60748 ? 53  LEU   B CB    1 
ATOM   1817 C  CG    . LEU   B 1 54  ? -19.55400 37.36300 -12.91800 1.000 18.25536 ? 53  LEU   B CG    1 
ATOM   1818 C  CD1   . LEU   B 1 54  ? -20.19400 38.16800 -11.79800 1.000 19.28843 ? 53  LEU   B CD1   1 
ATOM   1819 C  CD2   . LEU   B 1 54  ? -18.05000 37.33100 -12.78300 1.000 17.83019 ? 53  LEU   B CD2   1 
ATOM   1820 N  N     . ASP   B 1 55  ? -19.58700 32.61200 -13.37800 1.000 14.59507 ? 54  ASP   B N     1 
ATOM   1821 C  CA    . ASP   B 1 55  ? -20.23200 31.33500 -13.09800 1.000 15.25178 ? 54  ASP   B CA    1 
ATOM   1822 C  C     . ASP   B 1 55  ? -20.35300 31.26500 -11.59100 1.000 15.08618 ? 54  ASP   B C     1 
ATOM   1823 O  O     . ASP   B 1 55  ? -19.33900 31.15500 -10.90200 1.000 19.17183 ? 54  ASP   B O     1 
ATOM   1824 C  CB    . ASP   B 1 55  ? -19.37500 30.16600 -13.56500 1.000 19.27246 ? 54  ASP   B CB    1 
ATOM   1825 C  CG    . ASP   B 1 55  ? -18.98900 30.27600 -14.99800 1.000 30.45942 ? 54  ASP   B CG    1 
ATOM   1826 O  OD1   . ASP   B 1 55  ? -19.79200 30.77800 -15.81500 1.000 38.44527 ? 54  ASP   B OD1   1 
ATOM   1827 O  OD2   . ASP   B 1 55  ? -17.86300 29.86600 -15.29400 1.000 32.48982 ? 54  ASP   B OD2   1 
ATOM   1828 N  N     . ILE   B 1 56  ? -21.57400 31.32100 -11.07300 1.000 14.79327 ? 55  ILE   B N     1 
ATOM   1829 C  CA    . ILE   B 1 56  ? -21.78200 31.36800 -9.63400  1.000 15.68932 ? 55  ILE   B CA    1 
ATOM   1830 C  C     . ILE   B 1 56  ? -22.35200 30.03600 -9.17500  1.000 14.02269 ? 55  ILE   B C     1 
ATOM   1831 O  O     . ILE   B 1 56  ? -23.41000 29.59800 -9.65000  1.000 16.99154 ? 55  ILE   B O     1 
ATOM   1832 C  CB    . ILE   B 1 56  ? -22.67700 32.54500 -9.22900  1.000 18.67112 ? 55  ILE   B CB    1 
ATOM   1833 C  CG1   . ILE   B 1 56  ? -22.02800 33.84800 -9.70800  1.000 23.41169 ? 55  ILE   B CG1   1 
ATOM   1834 C  CG2   . ILE   B 1 56  ? -22.89800 32.54700 -7.71300  1.000 19.70678 ? 55  ILE   B CG2   1 
ATOM   1835 C  CD1   . ILE   B 1 56  ? -22.90000 35.00700 -9.57200  1.000 25.30368 ? 55  ILE   B CD1   1 
ATOM   1836 N  N     . LEU   B 1 57  ? -21.66200 29.40200 -8.23900  1.000 13.93071 ? 56  LEU   B N     1 
ATOM   1837 C  CA    . LEU   B 1 57  ? -22.13200 28.18100 -7.59000  1.000 13.41343 ? 56  LEU   B CA    1 
ATOM   1838 C  C     . LEU   B 1 57  ? -22.69600 28.55900 -6.22400  1.000 12.68673 ? 56  LEU   B C     1 
ATOM   1839 O  O     . LEU   B 1 57  ? -21.95700 29.01800 -5.34100  1.000 14.88947 ? 56  LEU   B O     1 
ATOM   1840 C  CB    . LEU   B 1 57  ? -20.99500 27.17200 -7.46100  1.000 13.79995 ? 56  LEU   B CB    1 
ATOM   1841 C  CG    . LEU   B 1 57  ? -21.33700 25.84500 -6.78900  1.000 17.17305 ? 56  LEU   B CG    1 
ATOM   1842 C  CD1   . LEU   B 1 57  ? -22.40400 25.07000 -7.54300  1.000 17.49262 ? 56  LEU   B CD1   1 
ATOM   1843 C  CD2   . LEU   B 1 57  ? -20.07600 25.01200 -6.65600  1.000 19.03810 ? 56  LEU   B CD2   1 
ATOM   1844 N  N     . ASP   B 1 58  ? -24.00400 28.37300 -6.06400  1.000 13.70669 ? 57  ASP   B N     1 
ATOM   1845 C  CA    . ASP   B 1 58  ? -24.71600 28.70700 -4.84300  1.000 16.73535 ? 57  ASP   B CA    1 
ATOM   1846 C  C     . ASP   B 1 58  ? -24.84400 27.40600 -4.06200  1.000 14.48914 ? 57  ASP   B C     1 
ATOM   1847 O  O     . ASP   B 1 58  ? -25.60600 26.51500 -4.45600  1.000 16.32875 ? 57  ASP   B O     1 
ATOM   1848 C  CB    . ASP   B 1 58  ? -26.09500 29.25900 -5.21700  1.000 18.42891 ? 57  ASP   B CB    1 
ATOM   1849 C  CG    . ASP   B 1 58  ? -26.90600 29.70500 -4.01900  1.000 19.12603 ? 57  ASP   B CG    1 
ATOM   1850 O  OD1   . ASP   B 1 58  ? -26.32500 29.97200 -2.95500  1.000 20.26825 ? 57  ASP   B OD1   1 
ATOM   1851 O  OD2   . ASP   B 1 58  ? -28.14200 29.80700 -4.15900  1.000 20.71198 ? 57  ASP   B OD2   1 
ATOM   1852 N  N     . THR   B 1 59  ? -24.09100 27.28000 -2.97100  1.000 15.78556 ? 58  THR   B N     1 
ATOM   1853 C  CA    . THR   B 1 59  ? -24.05800 26.04400 -2.19800  1.000 14.33617 ? 58  THR   B CA    1 
ATOM   1854 C  C     . THR   B 1 59  ? -25.08700 26.08900 -1.07000  1.000 14.73773 ? 58  THR   B C     1 
ATOM   1855 O  O     . THR   B 1 59  ? -25.56200 27.15200 -0.67000  1.000 17.24949 ? 58  THR   B O     1 
ATOM   1856 C  CB    . THR   B 1 59  ? -22.66300 25.80400 -1.59500  1.000 15.20905 ? 58  THR   B CB    1 
ATOM   1857 O  OG1   . THR   B 1 59  ? -22.40000 26.77000 -0.56300  1.000 16.50015 ? 58  THR   B OG1   1 
ATOM   1858 C  CG2   . THR   B 1 59  ? -21.56100 25.84000 -2.65600  1.000 16.21470 ? 58  THR   B CG2   1 
ATOM   1859 N  N     . ALA   B 1 60  ? -25.39100 24.91200 -0.53100  1.000 16.08003 ? 59  ALA   B N     1 
ATOM   1860 C  CA    . ALA   B 1 60  ? -26.26300 24.80900 0.63100   1.000 16.22267 ? 59  ALA   B CA    1 
ATOM   1861 C  C     . ALA   B 1 60  ? -25.49400 25.15100 1.89900   1.000 18.96953 ? 59  ALA   B C     1 
ATOM   1862 O  O     . ALA   B 1 60  ? -24.27700 24.96500 1.97900   1.000 19.17795 ? 59  ALA   B O     1 
ATOM   1863 C  CB    . ALA   B 1 60  ? -26.80700 23.38400 0.76200   1.000 17.94393 ? 59  ALA   B CB    1 
ATOM   1864 N  N     . GLY   B 1 61  ? -26.20600 25.60100 2.93700   1.000 19.38345 ? 60  GLY   B N     1 
ATOM   1865 C  CA    . GLY   B 1 61  ? -25.56300 25.84800 4.24400   1.000 25.69658 ? 60  GLY   B CA    1 
ATOM   1866 C  C     . GLY   B 1 61  ? -25.24600 24.56100 4.99400   1.000 28.95040 ? 60  GLY   B C     1 
ATOM   1867 O  O     . GLY   B 1 61  ? -24.51500 24.64200 5.98000   1.000 34.34496 ? 60  GLY   B O     1 
ATOM   1868 N  N     . GLN   B 1 62  ? -25.69100 23.42000 4.49500   1.000 27.41165 ? 61  GLN   B N     1 
ATOM   1869 C  CA    . GLN   B 1 62  ? -25.45700 22.18100 5.21500   1.000 31.10290 ? 61  GLN   B CA    1 
ATOM   1870 C  C     . GLN   B 1 62  ? -23.97100 21.83400 5.21800   1.000 30.54334 ? 61  GLN   B C     1 
ATOM   1871 O  O     . GLN   B 1 62  ? -23.20100 22.23900 4.34200   1.000 30.14470 ? 61  GLN   B O     1 
ATOM   1872 C  CB    . GLN   B 1 62  ? -26.28000 21.05800 4.59200   1.000 33.88139 ? 61  GLN   B CB    1 
ATOM   1873 C  CG    . GLN   B 1 62  ? -25.84600 20.65700 3.21100   1.000 33.99146 ? 61  GLN   B CG    1 
ATOM   1874 C  CD    . GLN   B 1 62  ? -24.78300 19.58400 3.25400   1.000 34.79899 ? 61  GLN   B CD    1 
ATOM   1875 O  OE1   . GLN   B 1 62  ? -24.82500 18.68900 4.09800   1.000 39.10426 ? 61  GLN   B OE1   1 
ATOM   1876 N  NE2   . GLN   B 1 62  ? -23.81200 19.68000 2.36100   1.000 29.23079 ? 61  GLN   B NE2   1 
ATOM   1877 N  N     . GLU   B 1 63  ? -23.57600 21.04200 6.21500   1.000 33.89117 ? 62  GLU   B N     1 
ATOM   1878 C  CA    . GLU   B 1 63  ? -22.17500 20.74000 6.45900   1.000 39.13793 ? 62  GLU   B CA    1 
ATOM   1879 C  C     . GLU   B 1 63  ? -21.78000 19.30600 6.13100   1.000 35.91166 ? 62  GLU   B C     1 
ATOM   1880 O  O     . GLU   B 1 63  ? -20.58500 18.99300 6.14500   1.000 38.59767 ? 62  GLU   B O     1 
ATOM   1881 C  CB    . GLU   B 1 63  ? -21.82700 21.06300 7.91900   1.000 47.10123 ? 62  GLU   B CB    1 
ATOM   1882 C  CG    . GLU   B 1 63  ? -22.28800 22.45900 8.32600   1.000 53.11526 ? 62  GLU   B CG    1 
ATOM   1883 C  CD    . GLU   B 1 63  ? -21.99100 22.79300 9.77100   1.000 58.37892 ? 62  GLU   B CD    1 
ATOM   1884 O  OE1   . GLU   B 1 63  ? -22.59300 22.16500 10.66800  1.000 59.48056 ? 62  GLU   B OE1   1 
ATOM   1885 O  OE2   . GLU   B 1 63  ? -21.15400 23.68900 10.00700  1.000 61.16951 ? 62  GLU   B OE2   1 
ATOM   1886 N  N     . GLU   B 1 64  ? -22.73500 18.43100 5.83100   1.000 30.95980 ? 63  GLU   B N     1 
ATOM   1887 C  CA    . GLU   B 1 64  ? -22.39900 17.05700 5.49500   1.000 30.34934 ? 63  GLU   B CA    1 
ATOM   1888 C  C     . GLU   B 1 64  ? -21.83700 16.98600 4.07100   1.000 26.29692 ? 63  GLU   B C     1 
ATOM   1889 O  O     . GLU   B 1 64  ? -21.67900 17.99600 3.37400   1.000 27.57068 ? 63  GLU   B O     1 
ATOM   1890 C  CB    . GLU   B 1 64  ? -23.62100 16.15400 5.66300   1.000 38.66880 ? 63  GLU   B CB    1 
ATOM   1891 C  CG    . GLU   B 1 64  ? -24.54100 16.55000 6.81100   1.000 48.09384 ? 63  GLU   B CG    1 
ATOM   1892 C  CD    . GLU   B 1 64  ? -23.83400 16.57400 8.15100   1.000 56.95291 ? 63  GLU   B CD    1 
ATOM   1893 O  OE1   . GLU   B 1 64  ? -23.60100 15.48900 8.72300   1.000 60.83490 ? 63  GLU   B OE1   1 
ATOM   1894 O  OE2   . GLU   B 1 64  ? -23.50600 17.67900 8.63200   1.000 59.94404 ? 63  GLU   B OE2   1 
ATOM   1895 N  N     . TYR   B 1 65  ? -21.52100 15.76600 3.64300   1.000 22.36692 ? 64  TYR   B N     1 
ATOM   1896 C  CA    . TYR   B 1 65  ? -21.04700 15.48600 2.29000   1.000 20.05184 ? 64  TYR   B CA    1 
ATOM   1897 C  C     . TYR   B 1 65  ? -19.74100 16.21700 2.00000   1.000 19.19764 ? 64  TYR   B C     1 
ATOM   1898 O  O     . TYR   B 1 65  ? -19.62500 17.01100 1.06500   1.000 19.61413 ? 64  TYR   B O     1 
ATOM   1899 C  CB    . TYR   B 1 65  ? -22.13600 15.78700 1.25800   1.000 19.06688 ? 64  TYR   B CB    1 
ATOM   1900 C  CG    . TYR   B 1 65  ? -23.44700 15.19400 1.70800   1.000 18.65502 ? 64  TYR   B CG    1 
ATOM   1901 C  CD1   . TYR   B 1 65  ? -23.60500 13.82000 1.78000   1.000 20.75590 ? 64  TYR   B CD1   1 
ATOM   1902 C  CD2   . TYR   B 1 65  ? -24.50400 15.99700 2.10500   1.000 19.23078 ? 64  TYR   B CD2   1 
ATOM   1903 C  CE1   . TYR   B 1 65  ? -24.79000 13.25500 2.21000   1.000 21.75084 ? 64  TYR   B CE1   1 
ATOM   1904 C  CE2   . TYR   B 1 65  ? -25.71600 15.43700 2.54300   1.000 21.08780 ? 64  TYR   B CE2   1 
ATOM   1905 C  CZ    . TYR   B 1 65  ? -25.83900 14.07100 2.58900   1.000 21.23759 ? 64  TYR   B CZ    1 
ATOM   1906 O  OH    . TYR   B 1 65  ? -27.00800 13.49900 3.02300   1.000 21.20653 ? 64  TYR   B OH    1 
ATOM   1907 N  N     . SER   B 1 66  ? -18.73100 15.88300 2.79900   1.000 20.73037 ? 65  SER   B N     1 
ATOM   1908 C  CA    . SER   B 1 66  ? -17.45400 16.57800 2.69700   1.000 21.88152 ? 65  SER   B CA    1 
ATOM   1909 C  C     . SER   B 1 66  ? -16.78900 16.36300 1.34100   1.000 20.94954 ? 65  SER   B C     1 
ATOM   1910 O  O     . SER   B 1 66  ? -16.06800 17.24900 0.86500   1.000 20.92789 ? 65  SER   B O     1 
ATOM   1911 C  CB    . SER   B 1 66  ? -16.52000 16.15100 3.83000   1.000 25.88404 ? 65  SER   B CB    1 
ATOM   1912 O  OG    . SER   B 1 66  ? -16.11600 14.80500 3.67300   1.000 29.81582 ? 65  SER   B OG    1 
ATOM   1913 N  N     . ALA   B 1 67  ? -17.00700 15.20500 0.70600   1.000 20.00752 ? 66  ALA   B N     1 
ATOM   1914 C  CA    . ALA   B 1 67  ? -16.41800 14.98800 -0.61400  1.000 20.56921 ? 66  ALA   B CA    1 
ATOM   1915 C  C     . ALA   B 1 67  ? -16.96400 15.98700 -1.62700  1.000 18.91962 ? 66  ALA   B C     1 
ATOM   1916 O  O     . ALA   B 1 67  ? -16.20400 16.55200 -2.42500  1.000 19.85472 ? 66  ALA   B O     1 
ATOM   1917 C  CB    . ALA   B 1 67  ? -16.64500 13.54600 -1.08400  1.000 24.72375 ? 66  ALA   B CB    1 
ATOM   1918 N  N     . MET   B 1 68  ? -18.27500 16.22800 -1.60500  1.000 16.49441 ? 67  MET   B N     1 
ATOM   1919 C  CA    . MET   B 1 68  ? -18.84400 17.21500 -2.51900  1.000 16.37306 ? 67  MET   B CA    1 
ATOM   1920 C  C     . MET   B 1 68  ? -18.42500 18.63100 -2.13400  1.000 16.20962 ? 67  MET   B C     1 
ATOM   1921 O  O     . MET   B 1 68  ? -18.08900 19.44900 -3.00600  1.000 16.46112 ? 67  MET   B O     1 
ATOM   1922 C  CB    . MET   B 1 68  ? -20.37000 17.09000 -2.54200  1.000 17.02584 ? 67  MET   B CB    1 
ATOM   1923 C  CG    . MET   B 1 68  ? -21.02500 17.95800 -3.60200  1.000 22.03245 ? 67  MET   B CG    1 
ATOM   1924 S  SD    . MET   B 1 68  ? -20.60000 17.33800 -5.23600  1.000 27.10541 ? 67  MET   B SD    1 
ATOM   1925 C  CE    . MET   B 1 68  ? -21.59600 15.86500 -5.28700  1.000 30.01088 ? 67  MET   B CE    1 
ATOM   1926 N  N     . ARG   B 1 69  ? -18.44600 18.95400 -0.84000  1.000 16.79244 ? 68  ARG   B N     1 
ATOM   1927 C  CA    . ARG   B 1 69  ? -18.05100 20.30000 -0.43000  1.000 17.40005 ? 68  ARG   B CA    1 
ATOM   1928 C  C     . ARG   B 1 69  ? -16.58800 20.58100 -0.76100  1.000 17.88877 ? 68  ARG   B C     1 
ATOM   1929 O  O     . ARG   B 1 69  ? -16.25000 21.69100 -1.19300  1.000 18.77616 ? 68  ARG   B O     1 
ATOM   1930 C  CB    . ARG   B 1 69  ? -18.33400 20.51200 1.05700   1.000 22.09416 ? 68  ARG   B CB    1 
ATOM   1931 C  CG    . ARG   B 1 69  ? -19.81800 20.46900 1.41500   1.000 26.68284 ? 68  ARG   B CG    1 
ATOM   1932 C  CD    . ARG   B 1 69  ? -20.16000 21.39200 2.57600   1.000 34.93126 ? 68  ARG   B CD    1 
ATOM   1933 N  NE    . ARG   B 1 69  ? -20.31500 22.77500 2.13300   1.000 40.07323 ? 68  ARG   B NE    1 
ATOM   1934 C  CZ    . ARG   B 1 69  ? -19.49500 23.77700 2.42500   1.000 43.94223 ? 68  ARG   B CZ    1 
ATOM   1935 N  NH1   . ARG   B 1 69  ? -18.44100 23.60900 3.20900   1.000 44.73356 ? 68  ARG   B NH1   1 
ATOM   1936 N  NH2   . ARG   B 1 69  ? -19.74400 24.98300 1.92300   1.000 43.43222 ? 68  ARG   B NH2   1 
ATOM   1937 N  N     . ASP   B 1 70  ? -15.70700 19.59100 -0.57000  1.000 17.87806 ? 69  ASP   B N     1 
ATOM   1938 C  CA    . ASP   B 1 70  ? -14.30900 19.76300 -0.96400  1.000 18.24130 ? 69  ASP   B CA    1 
ATOM   1939 C  C     . ASP   B 1 70  ? -14.19000 20.03300 -2.45700  1.000 18.57433 ? 69  ASP   B C     1 
ATOM   1940 O  O     . ASP   B 1 70  ? -13.39800 20.88600 -2.87900  1.000 18.51333 ? 69  ASP   B O     1 
ATOM   1941 C  CB    . ASP   B 1 70  ? -13.47400 18.53200 -0.59800  1.000 20.16521 ? 69  ASP   B CB    1 
ATOM   1942 C  CG    . ASP   B 1 70  ? -13.21400 18.41000 0.89200   1.000 22.82291 ? 69  ASP   B CG    1 
ATOM   1943 O  OD1   . ASP   B 1 70  ? -13.56100 19.33500 1.65900   1.000 24.82405 ? 69  ASP   B OD1   1 
ATOM   1944 O  OD2   . ASP   B 1 70  ? -12.65300 17.36700 1.28500   1.000 24.51281 ? 69  ASP   B OD2   1 
ATOM   1945 N  N     . GLN   B 1 71  ? -14.97900 19.32500 -3.27500  1.000 16.48443 ? 70  GLN   B N     1 
ATOM   1946 C  CA    . GLN   B 1 71  ? -14.92800 19.55100 -4.71700  1.000 15.37634 ? 70  GLN   B CA    1 
ATOM   1947 C  C     . GLN   B 1 71  ? -15.33900 20.97800 -5.07000  1.000 13.92490 ? 70  GLN   B C     1 
ATOM   1948 O  O     . GLN   B 1 71  ? -14.74800 21.59800 -5.96000  1.000 14.54994 ? 70  GLN   B O     1 
ATOM   1949 C  CB    . GLN   B 1 71  ? -15.78600 18.51300 -5.46000  1.000 17.20423 ? 70  GLN   B CB    1 
ATOM   1950 C  CG    . GLN   B 1 71  ? -15.64800 18.59000 -6.98200  1.000 16.80321 ? 70  GLN   B CG    1 
ATOM   1951 C  CD    . GLN   B 1 71  ? -14.20500 18.41600 -7.44300  1.000 17.04234 ? 70  GLN   B CD    1 
ATOM   1952 O  OE1   . GLN   B 1 71  ? -13.55300 17.42500 -7.12100  1.000 19.82745 ? 70  GLN   B OE1   1 
ATOM   1953 N  NE2   . GLN   B 1 71  ? -13.70100 19.38000 -8.18800  1.000 16.12521 ? 70  GLN   B NE2   1 
ATOM   1954 N  N     . TYR   B 1 72  ? -16.36500 21.51000 -4.39500  1.000 14.57149 ? 71  TYR   B N     1 
ATOM   1955 C  CA    . TYR   B 1 72  ? -16.76400 22.89400 -4.63700  1.000 14.17595 ? 71  TYR   B CA    1 
ATOM   1956 C  C     . TYR   B 1 72  ? -15.57600 23.82800 -4.48100  1.000 15.50794 ? 71  TYR   B C     1 
ATOM   1957 O  O     . TYR   B 1 72  ? -15.38000 24.76500 -5.27000  1.000 16.35526 ? 71  TYR   B O     1 
ATOM   1958 C  CB    . TYR   B 1 72  ? -17.80500 23.31300 -3.59900  1.000 15.25155 ? 71  TYR   B CB    1 
ATOM   1959 C  CG    . TYR   B 1 72  ? -19.16400 22.66400 -3.69400  1.000 14.36202 ? 71  TYR   B CG    1 
ATOM   1960 C  CD1   . TYR   B 1 72  ? -19.60100 22.03400 -4.85600  1.000 13.75057 ? 71  TYR   B CD1   1 
ATOM   1961 C  CD2   . TYR   B 1 72  ? -20.01600 22.68500 -2.59700  1.000 15.12551 ? 71  TYR   B CD2   1 
ATOM   1962 C  CE1   . TYR   B 1 72  ? -20.87400 21.44500 -4.91800  1.000 15.75105 ? 71  TYR   B CE1   1 
ATOM   1963 C  CE2   . TYR   B 1 72  ? -21.27800 22.12300 -2.65500  1.000 15.24829 ? 71  TYR   B CE2   1 
ATOM   1964 C  CZ    . TYR   B 1 72  ? -21.70100 21.51000 -3.81400  1.000 16.03065 ? 71  TYR   B CZ    1 
ATOM   1965 O  OH    . TYR   B 1 72  ? -22.97800 20.96400 -3.84000  1.000 17.16943 ? 71  TYR   B OH    1 
ATOM   1966 N  N     . MET   B 1 73  ? -14.78500 23.59800 -3.45000  1.000 15.49211 ? 72  MET   B N     1 
ATOM   1967 C  CA    A MET   B 1 73  ? -13.65200 24.47100 -3.18900  0.500 14.96371 ? 72  MET   B CA    1 
ATOM   1968 C  CA    B MET   B 1 73  ? -13.65300 24.47200 -3.19800  0.500 15.14503 ? 72  MET   B CA    1 
ATOM   1969 C  C     . MET   B 1 73  ? -12.50200 24.20000 -4.14800  1.000 14.42594 ? 72  MET   B C     1 
ATOM   1970 O  O     . MET   B 1 73  ? -11.79800 25.13300 -4.54100  1.000 15.72506 ? 72  MET   B O     1 
ATOM   1971 C  CB    A MET   B 1 73  ? -13.20200 24.31800 -1.73500  0.500 15.82395 ? 72  MET   B CB    1 
ATOM   1972 C  CB    B MET   B 1 73  ? -13.21600 24.32200 -1.75000  0.500 15.49644 ? 72  MET   B CB    1 
ATOM   1973 C  CG    A MET   B 1 73  ? -14.33900 24.29600 -0.70000  0.500 17.59769 ? 72  MET   B CG    1 
ATOM   1974 C  CG    B MET   B 1 73  ? -14.26500 24.81600 -0.79600  0.500 18.24335 ? 72  MET   B CG    1 
ATOM   1975 S  SD    A MET   B 1 73  ? -15.53000 25.64900 -0.83900  0.500 17.59301 ? 72  MET   B SD    1 
ATOM   1976 S  SD    B MET   B 1 73  ? -13.92600 24.42600 0.91000   0.500 20.55090 ? 72  MET   B SD    1 
ATOM   1977 C  CE    A MET   B 1 73  ? -16.87800 25.01300 0.15000   0.500 17.44246 ? 72  MET   B CE    1 
ATOM   1978 C  CE    B MET   B 1 73  ? -15.30100 25.29000 1.67200   0.500 22.20863 ? 72  MET   B CE    1 
ATOM   1979 N  N     . ARG   B 1 74  ? -12.31100 22.94300 -4.53500  1.000 14.85571 ? 73  ARG   B N     1 
ATOM   1980 C  CA    . ARG   B 1 74  ? -11.22000 22.59700 -5.43300  1.000 15.94804 ? 73  ARG   B CA    1 
ATOM   1981 C  C     . ARG   B 1 74  ? -11.28600 23.38100 -6.73600  1.000 16.63050 ? 73  ARG   B C     1 
ATOM   1982 O  O     . ARG   B 1 74  ? -10.26900 23.89600 -7.21200  1.000 18.46850 ? 73  ARG   B O     1 
ATOM   1983 C  CB    . ARG   B 1 74  ? -11.28000 21.09800 -5.70700  1.000 18.52220 ? 73  ARG   B CB    1 
ATOM   1984 C  CG    . ARG   B 1 74  ? -10.16100 20.57300 -6.56300  1.000 19.80202 ? 73  ARG   B CG    1 
ATOM   1985 C  CD    . ARG   B 1 74  ? -9.72600  19.19200 -6.10500  1.000 23.02181 ? 73  ARG   B CD    1 
ATOM   1986 N  NE    . ARG   B 1 74  ? -10.85900 18.30300 -5.90900  1.000 25.13527 ? 73  ARG   B NE    1 
ATOM   1987 C  CZ    . ARG   B 1 74  ? -11.14600 17.69300 -4.76600  1.000 26.37293 ? 73  ARG   B CZ    1 
ATOM   1988 N  NH1   . ARG   B 1 74  ? -10.36000 17.79900 -3.70600  1.000 26.41286 ? 73  ARG   B NH1   1 
ATOM   1989 N  NH2   . ARG   B 1 74  ? -12.25100 16.96100 -4.68400  1.000 27.21876 ? 73  ARG   B NH2   1 
ATOM   1990 N  N     . THR   B 1 75  ? -12.46000 23.48300 -7.34200  1.000 15.22382 ? 74  THR   B N     1 
ATOM   1991 C  CA    . THR   B 1 75  ? -12.51800 24.16300 -8.62200  1.000 18.09272 ? 74  THR   B CA    1 
ATOM   1992 C  C     . THR   B 1 75  ? -13.02100 25.59400 -8.54900  1.000 16.14923 ? 74  THR   B C     1 
ATOM   1993 O  O     . THR   B 1 75  ? -12.97600 26.29200 -9.56500  1.000 17.58478 ? 74  THR   B O     1 
ATOM   1994 C  CB    . THR   B 1 75  ? -13.32400 23.36000 -9.61900  1.000 19.95133 ? 74  THR   B CB    1 
ATOM   1995 O  OG1   . THR   B 1 75  ? -14.60400 23.09800 -9.05100  1.000 19.32206 ? 74  THR   B OG1   1 
ATOM   1996 C  CG2   . THR   B 1 75  ? -12.61300 22.05500 -9.92700  1.000 23.98188 ? 74  THR   B CG2   1 
ATOM   1997 N  N     . GLY   B 1 76  ? -13.47500 26.06000 -7.39000  1.000 15.07583 ? 75  GLY   B N     1 
ATOM   1998 C  CA    . GLY   B 1 76  ? -13.80700 27.46600 -7.26100  1.000 13.98798 ? 75  GLY   B CA    1 
ATOM   1999 C  C     . GLY   B 1 76  ? -12.55100 28.32300 -7.31500  1.000 13.47880 ? 75  GLY   B C     1 
ATOM   2000 O  O     . GLY   B 1 76  ? -11.50300 27.96300 -6.77600  1.000 14.76343 ? 75  GLY   B O     1 
ATOM   2001 N  N     . GLU   B 1 77  ? -12.66300 29.47100 -7.98600  1.000 13.65948 ? 76  GLU   B N     1 
ATOM   2002 C  CA    . GLU   B 1 77  ? -11.55600 30.41300 -8.07100  1.000 13.67013 ? 76  GLU   B CA    1 
ATOM   2003 C  C     . GLU   B 1 77  ? -11.62500 31.49200 -7.00500  1.000 14.40666 ? 76  GLU   B C     1 
ATOM   2004 O  O     . GLU   B 1 77  ? -10.58400 32.04700 -6.62200  1.000 16.26364 ? 76  GLU   B O     1 
ATOM   2005 C  CB    . GLU   B 1 77  ? -11.55200 31.08500 -9.44600  1.000 15.32016 ? 76  GLU   B CB    1 
ATOM   2006 C  CG    . GLU   B 1 77  ? -11.15200 30.17700 -10.57000 1.000 19.54695 ? 76  GLU   B CG    1 
ATOM   2007 C  CD    . GLU   B 1 77  ? -11.19500 30.91400 -11.88900 1.000 21.60610 ? 76  GLU   B CD    1 
ATOM   2008 O  OE1   . GLU   B 1 77  ? -12.29300 31.09300 -12.43000 1.000 20.28902 ? 76  GLU   B OE1   1 
ATOM   2009 O  OE2   . GLU   B 1 77  ? -10.13700 31.36100 -12.37000 1.000 27.99153 ? 76  GLU   B OE2   1 
ATOM   2010 N  N     . GLY   B 1 78  ? -12.82200 31.84500 -6.55900  1.000 13.83240 ? 77  GLY   B N     1 
ATOM   2011 C  CA    . GLY   B 1 78  ? -12.98300 32.82700 -5.50000  1.000 14.90191 ? 77  GLY   B CA    1 
ATOM   2012 C  C     . GLY   B 1 78  ? -14.22000 32.49900 -4.70000  1.000 13.25125 ? 77  GLY   B C     1 
ATOM   2013 O  O     . GLY   B 1 78  ? -15.17000 31.89800 -5.21600  1.000 14.80715 ? 77  GLY   B O     1 
ATOM   2014 N  N     . PHE   B 1 79  ? -14.21100 32.90600 -3.43400  1.000 13.98862 ? 78  PHE   B N     1 
ATOM   2015 C  CA    . PHE   B 1 79  ? -15.22300 32.49000 -2.46700  1.000 15.05471 ? 78  PHE   B CA    1 
ATOM   2016 C  C     . PHE   B 1 79  ? -15.83000 33.70000 -1.79300  1.000 14.36334 ? 78  PHE   B C     1 
ATOM   2017 O  O     . PHE   B 1 79  ? -15.10600 34.56500 -1.28800  1.000 15.07690 ? 78  PHE   B O     1 
ATOM   2018 C  CB    . PHE   B 1 79  ? -14.62600 31.51400 -1.43900  1.000 15.08658 ? 78  PHE   B CB    1 
ATOM   2019 C  CG    . PHE   B 1 79  ? -14.07700 30.30600 -2.10400  1.000 13.00987 ? 78  PHE   B CG    1 
ATOM   2020 C  CD1   . PHE   B 1 79  ? -12.78100 30.30900 -2.61700  1.000 14.52095 ? 78  PHE   B CD1   1 
ATOM   2021 C  CD2   . PHE   B 1 79  ? -14.89000 29.20800 -2.34300  1.000 13.64083 ? 78  PHE   B CD2   1 
ATOM   2022 C  CE1   . PHE   B 1 79  ? -12.28900 29.21900 -3.32000  1.000 14.25696 ? 78  PHE   B CE1   1 
ATOM   2023 C  CE2   . PHE   B 1 79  ? -14.40300 28.10800 -3.02600  1.000 14.43940 ? 78  PHE   B CE2   1 
ATOM   2024 C  CZ    . PHE   B 1 79  ? -13.11000 28.11400 -3.53400  1.000 14.08651 ? 78  PHE   B CZ    1 
ATOM   2025 N  N     . LEU   B 1 80  ? -17.16100 33.75900 -1.80400  1.000 15.10775 ? 79  LEU   B N     1 
ATOM   2026 C  CA    . LEU   B 1 80  ? -17.90500 34.73100 -1.01900  1.000 16.92537 ? 79  LEU   B CA    1 
ATOM   2027 C  C     . LEU   B 1 80  ? -18.29100 34.01600 0.26200   1.000 17.04763 ? 79  LEU   B C     1 
ATOM   2028 O  O     . LEU   B 1 80  ? -19.07900 33.06700 0.23100   1.000 19.10202 ? 79  LEU   B O     1 
ATOM   2029 C  CB    . LEU   B 1 80  ? -19.14400 35.15600 -1.79600  1.000 22.34364 ? 79  LEU   B CB    1 
ATOM   2030 C  CG    . LEU   B 1 80  ? -19.51000 36.63400 -1.79500  1.000 24.76305 ? 79  LEU   B CG    1 
ATOM   2031 C  CD1   . LEU   B 1 80  ? -18.34300 37.51500 -2.25600  1.000 23.12480 ? 79  LEU   B CD1   1 
ATOM   2032 C  CD2   . LEU   B 1 80  ? -20.73500 36.85600 -2.65800  1.000 25.39690 ? 79  LEU   B CD2   1 
ATOM   2033 N  N     . CYS   B 1 81  ? -17.68200 34.41700 1.37300   1.000 16.28341 ? 80  CYS   B N     1 
ATOM   2034 C  CA    . CYS   B 1 81  ? -17.91500 33.78800 2.66700   1.000 16.51866 ? 80  CYS   B CA    1 
ATOM   2035 C  C     . CYS   B 1 81  ? -18.90200 34.67100 3.41300   1.000 16.54871 ? 80  CYS   B C     1 
ATOM   2036 O  O     . CYS   B 1 81  ? -18.53000 35.74400 3.88800   1.000 18.10697 ? 80  CYS   B O     1 
ATOM   2037 C  CB    . CYS   B 1 81  ? -16.60400 33.66200 3.43700   1.000 19.70035 ? 80  CYS   B CB    1 
ATOM   2038 S  SG    . CYS   B 1 81  ? -15.39600 32.53900 2.67500   1.000 23.06942 ? 80  CYS   B SG    1 
ATOM   2039 N  N     . VAL   B 1 82  ? -20.15400 34.21900 3.49900   1.000 17.97767 ? 81  VAL   B N     1 
ATOM   2040 C  CA    . VAL   B 1 82  ? -21.28500 35.03100 3.93700   1.000 17.93636 ? 81  VAL   B CA    1 
ATOM   2041 C  C     . VAL   B 1 82  ? -21.66500 34.63700 5.35400   1.000 18.42911 ? 81  VAL   B C     1 
ATOM   2042 O  O     . VAL   B 1 82  ? -21.79100 33.44500 5.66500   1.000 18.21136 ? 81  VAL   B O     1 
ATOM   2043 C  CB    . VAL   B 1 82  ? -22.48800 34.85200 2.99000   1.000 19.17703 ? 81  VAL   B CB    1 
ATOM   2044 C  CG1   . VAL   B 1 82  ? -23.59800 35.83700 3.35000   1.000 19.41624 ? 81  VAL   B CG1   1 
ATOM   2045 C  CG2   . VAL   B 1 82  ? -22.05900 35.03900 1.53400   1.000 20.33227 ? 81  VAL   B CG2   1 
ATOM   2046 N  N     . PHE   B 1 83  ? -21.86300 35.63200 6.21000   1.000 18.57277 ? 82  PHE   B N     1 
ATOM   2047 C  CA    . PHE   B 1 83  ? -22.54800 35.44500 7.48000   1.000 19.57962 ? 82  PHE   B CA    1 
ATOM   2048 C  C     . PHE   B 1 83  ? -23.65900 36.47900 7.53400   1.000 20.92719 ? 82  PHE   B C     1 
ATOM   2049 O  O     . PHE   B 1 83  ? -23.73000 37.37900 6.68700   1.000 22.33873 ? 82  PHE   B O     1 
ATOM   2050 C  CB    . PHE   B 1 83  ? -21.60300 35.56600 8.69000   1.000 20.38681 ? 82  PHE   B CB    1 
ATOM   2051 C  CG    . PHE   B 1 83  ? -21.08200 36.95400 8.92800   1.000 21.05233 ? 82  PHE   B CG    1 
ATOM   2052 C  CD1   . PHE   B 1 83  ? -20.01900 37.45700 8.17700   1.000 22.47066 ? 82  PHE   B CD1   1 
ATOM   2053 C  CD2   . PHE   B 1 83  ? -21.64000 37.76200 9.91000   1.000 22.57101 ? 82  PHE   B CD2   1 
ATOM   2054 C  CE1   . PHE   B 1 83  ? -19.54200 38.74200 8.39400   1.000 23.10847 ? 82  PHE   B CE1   1 
ATOM   2055 C  CE2   . PHE   B 1 83  ? -21.16200 39.05000 10.12700  1.000 23.41635 ? 82  PHE   B CE2   1 
ATOM   2056 C  CZ    . PHE   B 1 83  ? -20.10900 39.53500 9.37100   1.000 24.14097 ? 82  PHE   B CZ    1 
ATOM   2057 N  N     . ALA   B 1 84  ? -24.54700 36.34500 8.51500   1.000 20.80610 ? 83  ALA   B N     1 
ATOM   2058 C  CA    . ALA   B 1 84  ? -25.60900 37.31900 8.70300   1.000 22.49150 ? 83  ALA   B CA    1 
ATOM   2059 C  C     . ALA   B 1 84  ? -25.28900 38.14100 9.93600   1.000 22.75177 ? 83  ALA   B C     1 
ATOM   2060 O  O     . ALA   B 1 84  ? -24.88600 37.59200 10.96800  1.000 21.49765 ? 83  ALA   B O     1 
ATOM   2061 C  CB    . ALA   B 1 84  ? -26.97200 36.64200 8.86800   1.000 22.92799 ? 83  ALA   B CB    1 
ATOM   2062 N  N     . ILE   B 1 85  ? -25.48100 39.46000 9.83100   1.000 24.22454 ? 84  ILE   B N     1 
ATOM   2063 C  CA    . ILE   B 1 85  ? -25.12400 40.35200 10.92800  1.000 25.31071 ? 84  ILE   B CA    1 
ATOM   2064 C  C     . ILE   B 1 85  ? -25.99600 40.16100 12.15800  1.000 27.08269 ? 84  ILE   B C     1 
ATOM   2065 O  O     . ILE   B 1 85  ? -25.65600 40.68600 13.22200  1.000 30.25201 ? 84  ILE   B O     1 
ATOM   2066 C  CB    . ILE   B 1 85  ? -25.04900 41.82300 10.46400  1.000 27.92488 ? 84  ILE   B CB    1 
ATOM   2067 C  CG1   . ILE   B 1 85  ? -26.39100 42.28800 9.89100   1.000 28.84300 ? 84  ILE   B CG1   1 
ATOM   2068 C  CG2   . ILE   B 1 85  ? -23.95900 41.99000 9.41900   1.000 27.90696 ? 84  ILE   B CG2   1 
ATOM   2069 C  CD1   . ILE   B 1 85  ? -27.32100 42.91400 10.89800  1.000 32.08641 ? 84  ILE   B CD1   1 
ATOM   2070 N  N     . ASN   B 1 86  ? -27.11200 39.43600 12.03900  1.000 25.80110 ? 85  ASN   B N     1 
ATOM   2071 C  CA    . ASN   B 1 86  ? -27.97500 39.12800 13.17300  1.000 25.29121 ? 85  ASN   B CA    1 
ATOM   2072 C  C     . ASN   B 1 86  ? -27.90300 37.65800 13.56900  1.000 22.09335 ? 85  ASN   B C     1 
ATOM   2073 O  O     . ASN   B 1 86  ? -28.83000 37.14100 14.20500  1.000 23.15222 ? 85  ASN   B O     1 
ATOM   2074 C  CB    . ASN   B 1 86  ? -29.41500 39.54800 12.88500  1.000 26.96801 ? 85  ASN   B CB    1 
ATOM   2075 C  CG    . ASN   B 1 86  ? -30.05000 38.74600 11.77200  1.000 27.23671 ? 85  ASN   B CG    1 
ATOM   2076 O  OD1   . ASN   B 1 86  ? -29.36500 38.09000 10.98900  1.000 26.96866 ? 85  ASN   B OD1   1 
ATOM   2077 N  ND2   . ASN   B 1 86  ? -31.37300 38.81000 11.68100  1.000 27.23947 ? 85  ASN   B ND2   1 
ATOM   2078 N  N     . ASN   B 1 87  ? -26.80400 36.98200 13.22000  1.000 22.98856 ? 86  ASN   B N     1 
ATOM   2079 C  CA    . ASN   B 1 87  ? -26.60900 35.56100 13.51400  1.000 20.64435 ? 86  ASN   B CA    1 
ATOM   2080 C  C     . ASN   B 1 87  ? -25.15200 35.39900 13.94600  1.000 23.79053 ? 86  ASN   B C     1 
ATOM   2081 O  O     . ASN   B 1 87  ? -24.25200 35.23100 13.11700  1.000 23.05831 ? 86  ASN   B O     1 
ATOM   2082 C  CB    . ASN   B 1 87  ? -26.94600 34.72100 12.29100  1.000 21.62409 ? 86  ASN   B CB    1 
ATOM   2083 C  CG    . ASN   B 1 87  ? -26.79100 33.22800 12.52900  1.000 23.65781 ? 86  ASN   B CG    1 
ATOM   2084 O  OD1   . ASN   B 1 87  ? -26.19000 32.78500 13.50900  1.000 23.29190 ? 86  ASN   B OD1   1 
ATOM   2085 N  ND2   . ASN   B 1 87  ? -27.31800 32.43600 11.59800  1.000 25.60151 ? 86  ASN   B ND2   1 
ATOM   2086 N  N     . THR   B 1 88  ? -24.93200 35.44600 15.25900  1.000 24.06929 ? 87  THR   B N     1 
ATOM   2087 C  CA    . THR   B 1 88  ? -23.57600 35.37100 15.78700  1.000 23.69648 ? 87  THR   B CA    1 
ATOM   2088 C  C     . THR   B 1 88  ? -22.92200 34.03400 15.45800  1.000 22.18466 ? 87  THR   B C     1 
ATOM   2089 O  O     . THR   B 1 88  ? -21.73700 33.98800 15.11500  1.000 24.36108 ? 87  THR   B O     1 
ATOM   2090 C  CB    . THR   B 1 88  ? -23.60000 35.64400 17.29000  1.000 27.95260 ? 87  THR   B CB    1 
ATOM   2091 O  OG1   . THR   B 1 88  ? -23.92600 37.02300 17.49300  1.000 28.83416 ? 87  THR   B OG1   1 
ATOM   2092 C  CG2   . THR   B 1 88  ? -22.25300 35.34200 17.92600  1.000 28.12482 ? 87  THR   B CG2   1 
ATOM   2093 N  N     . LYS   B 1 89  ? -23.68100 32.93700 15.52900  1.000 23.09729 ? 88  LYS   B N     1 
ATOM   2094 C  CA    . LYS   B 1 89  ? -23.10900 31.63700 15.18600  1.000 23.19266 ? 88  LYS   B CA    1 
ATOM   2095 C  C     . LYS   B 1 89  ? -22.60300 31.61400 13.74600  1.000 23.95069 ? 88  LYS   B C     1 
ATOM   2096 O  O     . LYS   B 1 89  ? -21.52700 31.06900 13.46400  1.000 24.30671 ? 88  LYS   B O     1 
ATOM   2097 C  CB    . LYS   B 1 89  ? -24.14000 30.53400 15.41500  1.000 26.39200 ? 88  LYS   B CB    1 
ATOM   2098 C  CG    . LYS   B 1 89  ? -23.67600 29.14400 15.02900  1.000 30.43620 ? 88  LYS   B CG    1 
ATOM   2099 C  CD    . LYS   B 1 89  ? -22.55400 28.65100 15.91600  1.000 34.36901 ? 88  LYS   B CD    1 
ATOM   2100 C  CE    . LYS   B 1 89  ? -22.41400 27.13500 15.82800  1.000 37.32110 ? 88  LYS   B CE    1 
ATOM   2101 N  NZ    . LYS   B 1 89  ? -22.20100 26.66200 14.43100  1.000 38.85673 ? 88  LYS   B NZ    1 
ATOM   2102 N  N     . SER   B 1 90  ? -23.35300 32.21100 12.81600  1.000 22.84295 ? 89  SER   B N     1 
ATOM   2103 C  CA    . SER   B 1 90  ? -22.90100 32.19900 11.42800  1.000 20.90634 ? 89  SER   B CA    1 
ATOM   2104 C  C     . SER   B 1 90  ? -21.57100 32.91800 11.27500  1.000 22.35116 ? 89  SER   B C     1 
ATOM   2105 O  O     . SER   B 1 90  ? -20.74000 32.51500 10.45300  1.000 22.48017 ? 89  SER   B O     1 
ATOM   2106 C  CB    . SER   B 1 90  ? -23.95400 32.81300 10.51000  1.000 21.51660 ? 89  SER   B CB    1 
ATOM   2107 O  OG    . SER   B 1 90  ? -23.99000 34.22100 10.63200  1.000 22.69792 ? 89  SER   B OG    1 
ATOM   2108 N  N     . PHE   B 1 91  ? -21.34800 33.97200 12.06400  1.000 21.66350 ? 90  PHE   B N     1 
ATOM   2109 C  CA    . PHE   B 1 91  ? -20.06500 34.66800 12.04400  1.000 23.78959 ? 90  PHE   B CA    1 
ATOM   2110 C  C     . PHE   B 1 91  ? -18.97000 33.80200 12.65600  1.000 23.11961 ? 90  PHE   B C     1 
ATOM   2111 O  O     . PHE   B 1 91  ? -17.85800 33.71900 12.12500  1.000 24.16777 ? 90  PHE   B O     1 
ATOM   2112 C  CB    . PHE   B 1 91  ? -20.20500 35.99900 12.79400  1.000 25.85583 ? 90  PHE   B CB    1 
ATOM   2113 C  CG    . PHE   B 1 91  ? -18.93400 36.78900 12.89200  1.000 26.68039 ? 90  PHE   B CG    1 
ATOM   2114 C  CD1   . PHE   B 1 91  ? -18.33800 37.31000 11.75500  1.000 27.08372 ? 90  PHE   B CD1   1 
ATOM   2115 C  CD2   . PHE   B 1 91  ? -18.34200 37.02000 14.11700  1.000 30.21988 ? 90  PHE   B CD2   1 
ATOM   2116 C  CE1   . PHE   B 1 91  ? -17.16800 38.04700 11.84100  1.000 31.07422 ? 90  PHE   B CE1   1 
ATOM   2117 C  CE2   . PHE   B 1 91  ? -17.17800 37.75600 14.21700  1.000 31.98118 ? 90  PHE   B CE2   1 
ATOM   2118 C  CZ    . PHE   B 1 91  ? -16.58700 38.27100 13.07300  1.000 33.00337 ? 90  PHE   B CZ    1 
ATOM   2119 N  N     . GLU   B 1 92  ? -19.27000 33.14300 13.77400  1.000 24.68660 ? 91  GLU   B N     1 
ATOM   2120 C  CA    . GLU   B 1 92  ? -18.31700 32.22800 14.38700  1.000 27.77015 ? 91  GLU   B CA    1 
ATOM   2121 C  C     . GLU   B 1 92  ? -17.98800 31.05400 13.47800  1.000 27.36580 ? 91  GLU   B C     1 
ATOM   2122 O  O     . GLU   B 1 92  ? -16.90300 30.47900 13.60200  1.000 32.31703 ? 91  GLU   B O     1 
ATOM   2123 C  CB    . GLU   B 1 92  ? -18.86900 31.72500 15.72300  1.000 29.78974 ? 91  GLU   B CB    1 
ATOM   2124 C  CG    . GLU   B 1 92  ? -19.17100 32.84100 16.71600  1.000 32.88844 ? 91  GLU   B CG    1 
ATOM   2125 C  CD    . GLU   B 1 92  ? -19.96400 32.37100 17.92800  1.000 37.00435 ? 91  GLU   B CD    1 
ATOM   2126 O  OE1   . GLU   B 1 92  ? -20.54800 31.26500 17.88600  1.000 37.14258 ? 91  GLU   B OE1   1 
ATOM   2127 O  OE2   . GLU   B 1 92  ? -20.00300 33.12100 18.92600  1.000 38.67505 ? 91  GLU   B OE2   1 
ATOM   2128 N  N     . ASP   B 1 93  ? -18.89200 30.69500 12.56000  1.000 25.98920 ? 92  ASP   B N     1 
ATOM   2129 C  CA    . ASP   B 1 93  ? -18.65000 29.61500 11.60900  1.000 28.02489 ? 92  ASP   B CA    1 
ATOM   2130 C  C     . ASP   B 1 93  ? -17.67100 29.99600 10.50500  1.000 24.87237 ? 92  ASP   B C     1 
ATOM   2131 O  O     . ASP   B 1 93  ? -17.21200 29.11100 9.77900   1.000 24.85082 ? 92  ASP   B O     1 
ATOM   2132 C  CB    . ASP   B 1 93  ? -19.96800 29.18200 10.95100  1.000 33.72258 ? 92  ASP   B CB    1 
ATOM   2133 C  CG    . ASP   B 1 93  ? -20.88600 28.41100 11.89000  1.000 38.74453 ? 92  ASP   B CG    1 
ATOM   2134 O  OD1   . ASP   B 1 93  ? -20.43700 27.96900 12.97000  1.000 34.30875 ? 92  ASP   B OD1   1 
ATOM   2135 O  OD2   . ASP   B 1 93  ? -22.07500 28.24400 11.53500  1.000 44.93252 ? 92  ASP   B OD2   1 
ATOM   2136 N  N     . ILE   B 1 94  ? -17.34800 31.28100 10.35100  1.000 21.79743 ? 93  ILE   B N     1 
ATOM   2137 C  CA    . ILE   B 1 94  ? -16.62700 31.71500 9.15400   1.000 23.41315 ? 93  ILE   B CA    1 
ATOM   2138 C  C     . ILE   B 1 94  ? -15.25100 31.06200 9.06300   1.000 21.95862 ? 93  ILE   B C     1 
ATOM   2139 O  O     . ILE   B 1 94  ? -14.83100 30.62100 7.98400   1.000 20.94125 ? 93  ILE   B O     1 
ATOM   2140 C  CB    . ILE   B 1 94  ? -16.54500 33.25000 9.07300   1.000 25.00246 ? 93  ILE   B CB    1 
ATOM   2141 C  CG1   . ILE   B 1 94  ? -17.89600 33.84700 8.67000   1.000 24.10818 ? 93  ILE   B CG1   1 
ATOM   2142 C  CG2   . ILE   B 1 94  ? -15.46800 33.67200 8.05800   1.000 25.78120 ? 93  ILE   B CG2   1 
ATOM   2143 C  CD1   . ILE   B 1 94  ? -18.27600 33.60200 7.21800   1.000 23.57880 ? 93  ILE   B CD1   1 
ATOM   2144 N  N     . HIS   B 1 95  ? -14.52700 30.98600 10.18700  1.000 22.42694 ? 94  HIS   B N     1 
ATOM   2145 C  CA    . HIS   B 1 95  ? -13.16000 30.47100 10.13300  1.000 24.23741 ? 94  HIS   B CA    1 
ATOM   2146 C  C     . HIS   B 1 95  ? -13.10500 29.03500 9.62400   1.000 24.53331 ? 94  HIS   B C     1 
ATOM   2147 O  O     . HIS   B 1 95  ? -12.11000 28.64400 9.00700   1.000 23.12402 ? 94  HIS   B O     1 
ATOM   2148 C  CB    . HIS   B 1 95  ? -12.45200 30.62500 11.48300  1.000 27.95530 ? 94  HIS   B CB    1 
ATOM   2149 C  CG    . HIS   B 1 95  ? -12.95100 29.69800 12.54400  1.000 33.21851 ? 94  HIS   B CG    1 
ATOM   2150 N  ND1   . HIS   B 1 95  ? -12.32800 28.50500 12.84300  1.000 33.79707 ? 94  HIS   B ND1   1 
ATOM   2151 C  CD2   . HIS   B 1 95  ? -14.00700 29.79400 13.38500  1.000 35.61865 ? 94  HIS   B CD2   1 
ATOM   2152 C  CE1   . HIS   B 1 95  ? -12.98200 27.90500 13.82300  1.000 36.44558 ? 94  HIS   B CE1   1 
ATOM   2153 N  NE2   . HIS   B 1 95  ? -14.00300 28.66700 14.17200  1.000 36.71668 ? 94  HIS   B NE2   1 
ATOM   2154 N  N     . HIS   B 1 96  ? -14.16400 28.24700 9.84600   1.000 24.52642 ? 95  HIS   B N     1 
ATOM   2155 C  CA    . HIS   B 1 96  ? -14.19500 26.88200 9.32400   1.000 30.52996 ? 95  HIS   B CA    1 
ATOM   2156 C  C     . HIS   B 1 96  ? -14.17800 26.86800 7.79900   1.000 24.80095 ? 95  HIS   B C     1 
ATOM   2157 O  O     . HIS   B 1 96  ? -13.49800 26.03400 7.18900   1.000 24.02167 ? 95  HIS   B O     1 
ATOM   2158 C  CB    . HIS   B 1 96  ? -15.42000 26.13100 9.85300   1.000 40.58506 ? 95  HIS   B CB    1 
ATOM   2159 C  CG    . HIS   B 1 96  ? -15.30700 25.70600 11.28500  1.000 52.30348 ? 95  HIS   B CG    1 
ATOM   2160 N  ND1   . HIS   B 1 96  ? -14.33500 24.83500 11.73000  1.000 56.99701 ? 95  HIS   B ND1   1 
ATOM   2161 C  CD2   . HIS   B 1 96  ? -16.06100 26.01200 12.36800  1.000 57.15982 ? 95  HIS   B CD2   1 
ATOM   2162 C  CE1   . HIS   B 1 96  ? -14.48800 24.63100 13.02700  1.000 59.38178 ? 95  HIS   B CE1   1 
ATOM   2163 N  NE2   . HIS   B 1 96  ? -15.52800 25.33500 13.43900  1.000 59.26894 ? 95  HIS   B NE2   1 
ATOM   2164 N  N     . TYR   B 1 97  ? -14.93300 27.77100 7.16200   1.000 23.90603 ? 96  TYR   B N     1 
ATOM   2165 C  CA    . TYR   B 1 97  ? -14.90700 27.85200 5.70300   1.000 21.22164 ? 96  TYR   B CA    1 
ATOM   2166 C  C     . TYR   B 1 97  ? -13.52200 28.22900 5.19300   1.000 21.19242 ? 96  TYR   B C     1 
ATOM   2167 O  O     . TYR   B 1 97  ? -13.02000 27.62000 4.24000   1.000 21.30374 ? 96  TYR   B O     1 
ATOM   2168 C  CB    . TYR   B 1 97  ? -15.96000 28.83900 5.18500   1.000 23.19769 ? 96  TYR   B CB    1 
ATOM   2169 C  CG    . TYR   B 1 97  ? -17.38600 28.41300 5.46300   1.000 23.92191 ? 96  TYR   B CG    1 
ATOM   2170 C  CD1   . TYR   B 1 97  ? -17.98300 27.40700 4.72100   1.000 23.42932 ? 96  TYR   B CD1   1 
ATOM   2171 C  CD2   . TYR   B 1 97  ? -18.12900 29.01500 6.46900   1.000 26.95479 ? 96  TYR   B CD2   1 
ATOM   2172 C  CE1   . TYR   B 1 97  ? -19.28200 27.00400 4.97600   1.000 25.61753 ? 96  TYR   B CE1   1 
ATOM   2173 C  CE2   . TYR   B 1 97  ? -19.42900 28.62700 6.73100   1.000 29.05839 ? 96  TYR   B CE2   1 
ATOM   2174 C  CZ    . TYR   B 1 97  ? -20.00300 27.62100 5.97800   1.000 29.05890 ? 96  TYR   B CZ    1 
ATOM   2175 O  OH    . TYR   B 1 97  ? -21.29700 27.22900 6.23100   1.000 31.69702 ? 96  TYR   B OH    1 
ATOM   2176 N  N     . ARG   B 1 98  ? -12.88700 29.23100 5.81000   1.000 22.67265 ? 97  ARG   B N     1 
ATOM   2177 C  CA    . ARG   B 1 98  ? -11.56100 29.63100 5.34600   1.000 25.12403 ? 97  ARG   B CA    1 
ATOM   2178 C  C     . ARG   B 1 98  ? -10.54500 28.51200 5.53000   1.000 21.13456 ? 97  ARG   B C     1 
ATOM   2179 O  O     . ARG   B 1 98  ? -9.72000  28.26800 4.64200   1.000 20.77231 ? 97  ARG   B O     1 
ATOM   2180 C  CB    . ARG   B 1 98  ? -11.07900 30.91300 6.02200   1.000 27.19808 ? 97  ARG   B CB    1 
ATOM   2181 C  CG    . ARG   B 1 98  ? -9.69000  31.31300 5.52700   1.000 28.30399 ? 97  ARG   B CG    1 
ATOM   2182 C  CD    . ARG   B 1 98  ? -9.28300  32.69600 5.97700   1.000 30.67513 ? 97  ARG   B CD    1 
ATOM   2183 N  NE    . ARG   B 1 98  ? -7.85200  32.92300 5.81600   1.000 34.96513 ? 97  ARG   B NE    1 
ATOM   2184 C  CZ    . ARG   B 1 98  ? -7.29100  33.43100 4.72800   1.000 37.44506 ? 97  ARG   B CZ    1 
ATOM   2185 N  NH1   . ARG   B 1 98  ? -8.01100  33.76100 3.66800   1.000 40.17738 ? 97  ARG   B NH1   1 
ATOM   2186 N  NH2   . ARG   B 1 98  ? -5.97200  33.61500 4.70100   1.000 37.26388 ? 97  ARG   B NH2   1 
ATOM   2187 N  N     . GLU   B 1 99  ? -10.60300 27.80200 6.65900   1.000 20.78932 ? 98  GLU   B N     1 
ATOM   2188 C  CA    . GLU   B 1 99  ? -9.69100  26.67900 6.85500   1.000 20.07643 ? 98  GLU   B CA    1 
ATOM   2189 C  C     . GLU   B 1 99  ? -9.93000  25.58600 5.81900   1.000 18.58344 ? 98  GLU   B C     1 
ATOM   2190 O  O     . GLU   B 1 99  ? -8.97300  24.99600 5.30600   1.000 21.11367 ? 98  GLU   B O     1 
ATOM   2191 C  CB    . GLU   B 1 99  ? -9.83200  26.10800 8.26700   1.000 22.39251 ? 98  GLU   B CB    1 
ATOM   2192 C  CG    . GLU   B 1 99  ? -9.33300  27.01700 9.38900   1.000 27.47283 ? 98  GLU   B CG    1 
ATOM   2193 C  CD    . GLU   B 1 99  ? -10.00900 26.72900 10.73100  1.000 34.13028 ? 98  GLU   B CD    1 
ATOM   2194 O  OE1   . GLU   B 1 99  ? -10.67100 25.67600 10.86400  1.000 34.94451 ? 98  GLU   B OE1   1 
ATOM   2195 O  OE2   . GLU   B 1 99  ? -9.88400  27.56200 11.65700  1.000 38.81021 ? 98  GLU   B OE2   1 
ATOM   2196 N  N     . GLN   B 1 100 ? -11.20200 25.27900 5.52300   1.000 17.35398 ? 99  GLN   B N     1 
ATOM   2197 C  CA    . GLN   B 1 100 ? -11.50600 24.25700 4.52400   1.000 17.28069 ? 99  GLN   B CA    1 
ATOM   2198 C  C     . GLN   B 1 100 ? -10.97300 24.65500 3.15000   1.000 17.23006 ? 99  GLN   B C     1 
ATOM   2199 O  O     . GLN   B 1 100 ? -10.37000 23.84000 2.44000   1.000 17.30329 ? 99  GLN   B O     1 
ATOM   2200 C  CB    . GLN   B 1 100 ? -13.01600 24.01900 4.46900   1.000 20.63731 ? 99  GLN   B CB    1 
ATOM   2201 C  CG    . GLN   B 1 100 ? -13.42500 22.73900 3.74600   1.000 32.85214 ? 99  GLN   B CG    1 
ATOM   2202 C  CD    . GLN   B 1 100 ? -14.93800 22.59700 3.60900   1.000 40.75456 ? 99  GLN   B CD    1 
ATOM   2203 O  OE1   . GLN   B 1 100 ? -15.70000 23.38200 4.18000   1.000 43.72777 ? 99  GLN   B OE1   1 
ATOM   2204 N  NE2   . GLN   B 1 100 ? -15.37700 21.60300 2.83500   1.000 42.76398 ? 99  GLN   B NE2   1 
ATOM   2205 N  N     . ILE   B 1 101 ? -11.17200 25.91300 2.76200   1.000 16.53495 ? 100 ILE   B N     1 
ATOM   2206 C  CA    . ILE   B 1 101 ? -10.71000 26.37200 1.45300   1.000 16.54470 ? 100 ILE   B CA    1 
ATOM   2207 C  C     . ILE   B 1 101 ? -9.19000  26.26700 1.36100   1.000 16.07598 ? 100 ILE   B C     1 
ATOM   2208 O  O     . ILE   B 1 101 ? -8.63900  25.76600 0.37000   1.000 16.87818 ? 100 ILE   B O     1 
ATOM   2209 C  CB    . ILE   B 1 101 ? -11.21400 27.80300 1.20000   1.000 17.83376 ? 100 ILE   B CB    1 
ATOM   2210 C  CG1   . ILE   B 1 101 ? -12.73600 27.79900 1.04700   1.000 18.85587 ? 100 ILE   B CG1   1 
ATOM   2211 C  CG2   . ILE   B 1 101 ? -10.55400 28.40200 -0.03800  1.000 19.34858 ? 100 ILE   B CG2   1 
ATOM   2212 C  CD1   . ILE   B 1 101 ? -13.39100 29.15000 1.29400   1.000 21.14092 ? 100 ILE   B CD1   1 
ATOM   2213 N  N     . LYS   B 1 102 ? -8.49400  26.72700 2.40200   1.000 16.65591 ? 101 LYS   B N     1 
ATOM   2214 C  CA    . LYS   B 1 102 ? -7.03300  26.68800 2.39500   1.000 16.82246 ? 101 LYS   B CA    1 
ATOM   2215 C  C     . LYS   B 1 102 ? -6.51200  25.25600 2.31700   1.000 18.20462 ? 101 LYS   B C     1 
ATOM   2216 O  O     . LYS   B 1 102 ? -5.53900  24.98200 1.60700   1.000 17.59481 ? 101 LYS   B O     1 
ATOM   2217 C  CB    . LYS   B 1 102 ? -6.48100  27.40700 3.62200   1.000 19.85281 ? 101 LYS   B CB    1 
ATOM   2218 C  CG    . LYS   B 1 102 ? -6.70800  28.91800 3.59500   1.000 22.43007 ? 101 LYS   B CG    1 
ATOM   2219 C  CD    . LYS   B 1 102 ? -6.30500  29.57100 4.90700   1.000 30.57066 ? 101 LYS   B CD    1 
ATOM   2220 C  CE    . LYS   B 1 102 ? -4.84800  29.30500 5.25000   1.000 36.20751 ? 101 LYS   B CE    1 
ATOM   2221 N  NZ    . LYS   B 1 102 ? -4.54400  29.59700 6.68100   1.000 40.12175 ? 101 LYS   B NZ    1 
ATOM   2222 N  N     . ARG   B 1 103 ? -7.14300  24.32400 3.03500   1.000 16.34084 ? 102 ARG   B N     1 
ATOM   2223 C  CA    . ARG   B 1 103 ? -6.63800  22.95800 2.99900   1.000 18.58025 ? 102 ARG   B CA    1 
ATOM   2224 C  C     . ARG   B 1 103 ? -6.91200  22.30000 1.65400   1.000 15.42086 ? 102 ARG   B C     1 
ATOM   2225 O  O     . ARG   B 1 103 ? -6.02300  21.64700 1.09400   1.000 15.69436 ? 102 ARG   B O     1 
ATOM   2226 C  CB    . ARG   B 1 103 ? -7.13400  22.12700 4.18800   1.000 23.59715 ? 102 ARG   B CB    1 
ATOM   2227 C  CG    . ARG   B 1 103 ? -8.58600  21.77500 4.19700   1.000 27.67698 ? 102 ARG   B CG    1 
ATOM   2228 C  CD    . ARG   B 1 103 ? -8.86900  20.73400 5.28100   1.000 30.36901 ? 102 ARG   B CD    1 
ATOM   2229 N  NE    . ARG   B 1 103 ? -10.29900 20.52800 5.45500   1.000 30.82818 ? 102 ARG   B NE    1 
ATOM   2230 C  CZ    . ARG   B 1 103 ? -11.02900 21.13300 6.38300   1.000 35.01345 ? 102 ARG   B CZ    1 
ATOM   2231 N  NH1   . ARG   B 1 103 ? -10.47600 21.92700 7.28700   1.000 34.44095 ? 102 ARG   B NH1   1 
ATOM   2232 N  NH2   . ARG   B 1 103 ? -12.34600 20.94100 6.39900   1.000 36.70614 ? 102 ARG   B NH2   1 
ATOM   2233 N  N     . VAL   B 1 104 ? -8.12000  22.49300 1.10500   1.000 15.94011 ? 103 VAL   B N     1 
ATOM   2234 C  CA    . VAL   B 1 104 ? -8.46600  21.86200 -0.16300  1.000 15.24743 ? 103 VAL   B CA    1 
ATOM   2235 C  C     . VAL   B 1 104 ? -7.59700  22.40600 -1.28600  1.000 15.79863 ? 103 VAL   B C     1 
ATOM   2236 O  O     . VAL   B 1 104 ? -7.14900  21.65800 -2.16600  1.000 17.53370 ? 103 VAL   B O     1 
ATOM   2237 C  CB    . VAL   B 1 104 ? -9.97000  22.02900 -0.46500  1.000 15.98622 ? 103 VAL   B CB    1 
ATOM   2238 C  CG1   . VAL   B 1 104 ? -10.26700 21.58900 -1.88300  1.000 15.70724 ? 103 VAL   B CG1   1 
ATOM   2239 C  CG2   . VAL   B 1 104 ? -10.79800 21.22000 0.52000   1.000 16.70786 ? 103 VAL   B CG2   1 
ATOM   2240 N  N     . LYS   B 1 105 ? -7.35400  23.70900 -1.27800  1.000 16.07097 ? 104 LYS   B N     1 
ATOM   2241 C  CA    . LYS   B 1 105 ? -6.59200  24.35100 -2.34300  1.000 16.33809 ? 104 LYS   B CA    1 
ATOM   2242 C  C     . LYS   B 1 105 ? -5.10000  24.40200 -2.04600  1.000 17.95446 ? 104 LYS   B C     1 
ATOM   2243 O  O     . LYS   B 1 105 ? -4.32600  24.88200 -2.88900  1.000 18.54623 ? 104 LYS   B O     1 
ATOM   2244 C  CB    . LYS   B 1 105 ? -7.19200  25.72500 -2.65500  1.000 18.02006 ? 104 LYS   B CB    1 
ATOM   2245 C  CG    . LYS   B 1 105 ? -8.68400  25.61700 -3.03100  1.000 18.60958 ? 104 LYS   B CG    1 
ATOM   2246 C  CD    . LYS   B 1 105 ? -9.26100  26.91300 -3.55000  1.000 19.05890 ? 104 LYS   B CD    1 
ATOM   2247 C  CE    . LYS   B 1 105 ? -8.80900  27.22500 -4.96300  1.000 18.62995 ? 104 LYS   B CE    1 
ATOM   2248 N  NZ    . LYS   B 1 105 ? -9.33200  26.26200 -5.97400  1.000 18.44680 ? 104 LYS   B NZ    1 
ATOM   2249 N  N     . ASP   B 1 106 ? -4.68500  23.86100 -0.89800  1.000 16.89548 ? 105 ASP   B N     1 
ATOM   2250 C  CA    . ASP   B 1 106 ? -3.27800  23.76900 -0.53400  1.000 17.42625 ? 105 ASP   B CA    1 
ATOM   2251 C  C     . ASP   B 1 106 ? -2.59200  25.12800 -0.65900  1.000 18.29276 ? 105 ASP   B C     1 
ATOM   2252 O  O     . ASP   B 1 106 ? -1.53900  25.26700 -1.28800  1.000 18.78468 ? 105 ASP   B O     1 
ATOM   2253 C  CB    . ASP   B 1 106 ? -2.58600  22.69900 -1.38000  1.000 18.67471 ? 105 ASP   B CB    1 
ATOM   2254 C  CG    . ASP   B 1 106 ? -1.14200  22.46800 -0.97600  1.000 20.44418 ? 105 ASP   B CG    1 
ATOM   2255 O  OD1   . ASP   B 1 106 ? -0.87400  22.41200 0.23800   1.000 19.62503 ? 105 ASP   B OD1   1 
ATOM   2256 O  OD2   . ASP   B 1 106 ? -0.27800  22.33200 -1.87600  1.000 20.94608 ? 105 ASP   B OD2   1 
ATOM   2257 N  N     . SER   B 1 107 ? -3.20500  26.14300 -0.05400  1.000 18.58474 ? 106 SER   B N     1 
ATOM   2258 C  CA    . SER   B 1 107 ? -2.68100  27.49700 -0.15200  1.000 19.03750 ? 106 SER   B CA    1 
ATOM   2259 C  C     . SER   B 1 107 ? -3.19100  28.34600 0.99900   1.000 20.68084 ? 106 SER   B C     1 
ATOM   2260 O  O     . SER   B 1 107 ? -4.32400  28.18600 1.45000   1.000 24.13443 ? 106 SER   B O     1 
ATOM   2261 C  CB    . SER   B 1 107 ? -3.09600  28.16200 -1.46600  1.000 22.85720 ? 106 SER   B CB    1 
ATOM   2262 O  OG    . SER   B 1 107 ? -2.65000  29.50700 -1.51100  1.000 25.63727 ? 106 SER   B OG    1 
ATOM   2263 N  N     . GLU   B 1 108 ? -2.35800  29.28300 1.43300   1.000 26.20130 ? 107 GLU   B N     1 
ATOM   2264 C  CA    . GLU   B 1 108 ? -2.78600  30.26700 2.41500   1.000 29.97942 ? 107 GLU   B CA    1 
ATOM   2265 C  C     . GLU   B 1 108 ? -3.30900  31.54500 1.77800   1.000 30.14209 ? 107 GLU   B C     1 
ATOM   2266 O  O     . GLU   B 1 108 ? -3.73300  32.45600 2.50000   1.000 32.73838 ? 107 GLU   B O     1 
ATOM   2267 C  CB    . GLU   B 1 108 ? -1.64400  30.58900 3.38200   1.000 34.93335 ? 107 GLU   B CB    1 
ATOM   2268 C  CG    . GLU   B 1 108 ? -1.24000  29.40600 4.24400   1.000 40.86037 ? 107 GLU   B CG    1 
ATOM   2269 C  CD    . GLU   B 1 108 ? -0.51400  29.83400 5.49700   1.000 47.56477 ? 107 GLU   B CD    1 
ATOM   2270 O  OE1   . GLU   B 1 108 ? 0.64900   30.28100 5.38500   1.000 51.11713 ? 107 GLU   B OE1   1 
ATOM   2271 O  OE2   . GLU   B 1 108 ? -1.11400  29.74400 6.59200   1.000 49.62266 ? 107 GLU   B OE2   1 
ATOM   2272 N  N     . ASP   B 1 109 ? -3.29200  31.63500 0.45100   1.000 28.67771 ? 108 ASP   B N     1 
ATOM   2273 C  CA    . ASP   B 1 109 ? -3.69700  32.84500 -0.26400  1.000 28.64388 ? 108 ASP   B CA    1 
ATOM   2274 C  C     . ASP   B 1 109 ? -4.69200  32.43700 -1.34300  1.000 23.76212 ? 108 ASP   B C     1 
ATOM   2275 O  O     . ASP   B 1 109 ? -4.29800  32.12000 -2.46800  1.000 28.17699 ? 108 ASP   B O     1 
ATOM   2276 C  CB    . ASP   B 1 109 ? -2.47800  33.53200 -0.86400  1.000 36.49977 ? 108 ASP   B CB    1 
ATOM   2277 C  CG    . ASP   B 1 109 ? -2.81600  34.86400 -1.49400  1.000 44.56005 ? 108 ASP   B CG    1 
ATOM   2278 O  OD1   . ASP   B 1 109 ? -3.89900  35.40600 -1.18900  1.000 47.92962 ? 108 ASP   B OD1   1 
ATOM   2279 O  OD2   . ASP   B 1 109 ? -2.00100  35.36300 -2.29700  1.000 48.23761 ? 108 ASP   B OD2   1 
ATOM   2280 N  N     . VAL   B 1 110 ? -5.97600  32.44900 -1.00300  1.000 19.70032 ? 109 VAL   B N     1 
ATOM   2281 C  CA    . VAL   B 1 110 ? -7.04700  32.10200 -1.92600  1.000 17.83335 ? 109 VAL   B CA    1 
ATOM   2282 C  C     . VAL   B 1 110 ? -7.97600  33.31000 -2.02400  1.000 17.13253 ? 109 VAL   B C     1 
ATOM   2283 O  O     . VAL   B 1 110 ? -8.34300  33.87300 -0.99300  1.000 17.44209 ? 109 VAL   B O     1 
ATOM   2284 C  CB    . VAL   B 1 110 ? -7.84000  30.86400 -1.47100  1.000 17.26565 ? 109 VAL   B CB    1 
ATOM   2285 C  CG1   . VAL   B 1 110 ? -8.92400  30.52500 -2.48600  1.000 18.80443 ? 109 VAL   B CG1   1 
ATOM   2286 C  CG2   . VAL   B 1 110 ? -6.90500  29.66700 -1.24900  1.000 20.19541 ? 109 VAL   B CG2   1 
ATOM   2287 N  N     . PRO   B 1 111 ? -8.38500  33.72800 -3.22000  1.000 16.38709 ? 110 PRO   B N     1 
ATOM   2288 C  CA    . PRO   B 1 111 ? -9.27400  34.89900 -3.31700  1.000 16.12873 ? 110 PRO   B CA    1 
ATOM   2289 C  C     . PRO   B 1 111 ? -10.58500 34.66600 -2.58100  1.000 15.55569 ? 110 PRO   B C     1 
ATOM   2290 O  O     . PRO   B 1 111 ? -11.29700 33.68900 -2.82100  1.000 15.06675 ? 110 PRO   B O     1 
ATOM   2291 C  CB    . PRO   B 1 111 ? -9.48800  35.04600 -4.82700  1.000 16.85158 ? 110 PRO   B CB    1 
ATOM   2292 C  CG    . PRO   B 1 111 ? -8.23700  34.46500 -5.43100  1.000 16.36054 ? 110 PRO   B CG    1 
ATOM   2293 C  CD    . PRO   B 1 111 ? -7.93200  33.28500 -4.55200  1.000 16.66952 ? 110 PRO   B CD    1 
ATOM   2294 N  N     . MET   B 1 112 ? -10.89800 35.57400 -1.66400  1.000 14.74634 ? 111 MET   B N     1 
ATOM   2295 C  CA    . MET   B 1 112 ? -12.14100 35.47100 -0.92500  1.000 15.33607 ? 111 MET   B CA    1 
ATOM   2296 C  C     . MET   B 1 112 ? -12.51000 36.83600 -0.37100  1.000 15.78470 ? 111 MET   B C     1 
ATOM   2297 O  O     . MET   B 1 112 ? -11.66500 37.72900 -0.22100  1.000 17.29008 ? 111 MET   B O     1 
ATOM   2298 C  CB    . MET   B 1 112 ? -12.10800 34.34900 0.13000   1.000 21.62509 ? 111 MET   B CB    1 
ATOM   2299 C  CG    . MET   B 1 112 ? -11.14200 34.49000 1.27600   1.000 26.54516 ? 111 MET   B CG    1 
ATOM   2300 S  SD    . MET   B 1 112 ? -11.31000 33.07700 2.42700   1.000 28.15803 ? 111 MET   B SD    1 
ATOM   2301 C  CE    . MET   B 1 112 ? -10.65700 31.72900 1.45400   1.000 33.10521 ? 111 MET   B CE    1 
ATOM   2302 N  N     . VAL   B 1 113 ? -13.80300 36.99100 -0.10200  1.000 15.70328 ? 112 VAL   B N     1 
ATOM   2303 C  CA    . VAL   B 1 113 ? -14.36600 38.21500 0.45700   1.000 17.09071 ? 112 VAL   B CA    1 
ATOM   2304 C  C     . VAL   B 1 113 ? -15.28200 37.81400 1.60400   1.000 17.63031 ? 112 VAL   B C     1 
ATOM   2305 O  O     . VAL   B 1 113 ? -16.09900 36.89300 1.46600   1.000 18.18743 ? 112 VAL   B O     1 
ATOM   2306 C  CB    . VAL   B 1 113 ? -15.14500 39.02300 -0.59800  1.000 18.48835 ? 112 VAL   B CB    1 
ATOM   2307 C  CG1   . VAL   B 1 113 ? -15.88100 40.16700 0.04100   1.000 19.18483 ? 112 VAL   B CG1   1 
ATOM   2308 C  CG2   . VAL   B 1 113 ? -14.19700 39.57300 -1.64800  1.000 20.35851 ? 112 VAL   B CG2   1 
ATOM   2309 N  N     . LEU   B 1 114 ? -15.12700 38.48100 2.73900   1.000 18.79646 ? 113 LEU   B N     1 
ATOM   2310 C  CA    . LEU   B 1 114 ? -16.03800 38.28800 3.85700   1.000 20.58939 ? 113 LEU   B CA    1 
ATOM   2311 C  C     . LEU   B 1 114 ? -17.25500 39.18800 3.67400   1.000 18.67760 ? 113 LEU   B C     1 
ATOM   2312 O  O     . LEU   B 1 114 ? -17.11900 40.40100 3.49300   1.000 20.73442 ? 113 LEU   B O     1 
ATOM   2313 C  CB    . LEU   B 1 114 ? -15.32800 38.60900 5.17000   1.000 21.94764 ? 113 LEU   B CB    1 
ATOM   2314 C  CG    . LEU   B 1 114 ? -16.13900 38.40700 6.44800   1.000 21.38453 ? 113 LEU   B CG    1 
ATOM   2315 C  CD1   . LEU   B 1 114 ? -16.43500 36.93400 6.69400   1.000 20.29196 ? 113 LEU   B CD1   1 
ATOM   2316 C  CD2   . LEU   B 1 114 ? -15.39600 39.01000 7.63600   1.000 23.21386 ? 113 LEU   B CD2   1 
ATOM   2317 N  N     . VAL   B 1 115 ? -18.44900 38.59800 3.72600   1.000 18.45206 ? 114 VAL   B N     1 
ATOM   2318 C  CA    . VAL   B 1 115 ? -19.70000 39.30900 3.46400   1.000 19.70604 ? 114 VAL   B CA    1 
ATOM   2319 C  C     . VAL   B 1 115 ? -20.58400 39.23800 4.70000   1.000 21.93412 ? 114 VAL   B C     1 
ATOM   2320 O  O     . VAL   B 1 115 ? -20.97200 38.14300 5.12100   1.000 21.69755 ? 114 VAL   B O     1 
ATOM   2321 C  CB    . VAL   B 1 115 ? -20.41900 38.73900 2.22800   1.000 20.79927 ? 114 VAL   B CB    1 
ATOM   2322 C  CG1   . VAL   B 1 115 ? -21.74000 39.43600 1.99500   1.000 22.99540 ? 114 VAL   B CG1   1 
ATOM   2323 C  CG2   . VAL   B 1 115 ? -19.54600 38.90400 0.99100   1.000 19.40447 ? 114 VAL   B CG2   1 
ATOM   2324 N  N     . GLY   B 1 116 ? -20.88700 40.40300 5.28400   1.000 23.53821 ? 115 GLY   B N     1 
ATOM   2325 C  CA    . GLY   B 1 116 ? -21.88100 40.48400 6.34300   1.000 25.15689 ? 115 GLY   B CA    1 
ATOM   2326 C  C     . GLY   B 1 116 ? -23.22400 40.91400 5.78500   1.000 24.77385 ? 115 GLY   B C     1 
ATOM   2327 O  O     . GLY   B 1 116 ? -23.43200 42.09500 5.48900   1.000 27.57709 ? 115 GLY   B O     1 
ATOM   2328 N  N     . ASN   B 1 117 ? -24.13500 39.96100 5.61500   1.000 23.68200 ? 116 ASN   B N     1 
ATOM   2329 C  CA    . ASN   B 1 117 ? -25.40900 40.20300 4.95300   1.000 22.33770 ? 116 ASN   B CA    1 
ATOM   2330 C  C     . ASN   B 1 117 ? -26.51400 40.51700 5.97100   1.000 24.82820 ? 116 ASN   B C     1 
ATOM   2331 O  O     . ASN   B 1 117 ? -26.35900 40.33500 7.18100   1.000 24.27993 ? 116 ASN   B O     1 
ATOM   2332 C  CB    . ASN   B 1 117 ? -25.76900 38.98900 4.08700   1.000 22.94361 ? 116 ASN   B CB    1 
ATOM   2333 C  CG    . ASN   B 1 117 ? -26.99100 39.22400 3.20900   1.000 23.05345 ? 116 ASN   B CG    1 
ATOM   2334 O  OD1   . ASN   B 1 117 ? -27.10300 40.25700 2.54200   1.000 24.19894 ? 116 ASN   B OD1   1 
ATOM   2335 N  ND2   . ASN   B 1 117 ? -27.91100 38.26200 3.20000   1.000 24.74319 ? 116 ASN   B ND2   1 
ATOM   2336 N  N     . LYS   B 1 118 ? -27.64100 41.01000 5.44700   1.000 24.99676 ? 117 LYS   B N     1 
ATOM   2337 C  CA    . LYS   B 1 118 ? -28.82200 41.41300 6.22300   1.000 26.79590 ? 117 LYS   B CA    1 
ATOM   2338 C  C     . LYS   B 1 118 ? -28.60500 42.70800 7.00200   1.000 29.78732 ? 117 LYS   B C     1 
ATOM   2339 O  O     . LYS   B 1 118 ? -29.18800 42.89900 8.07600   1.000 31.58376 ? 117 LYS   B O     1 
ATOM   2340 C  CB    . LYS   B 1 118 ? -29.38100 40.29900 7.12300   1.000 26.30820 ? 117 LYS   B CB    1 
ATOM   2341 C  CG    . LYS   B 1 118 ? -29.55800 38.94700 6.40800   1.000 25.83624 ? 117 LYS   B CG    1 
ATOM   2342 C  CD    . LYS   B 1 118 ? -30.39600 37.97400 7.23600   1.000 25.01835 ? 117 LYS   B CD    1 
ATOM   2343 C  CE    . LYS   B 1 118 ? -30.46900 36.59700 6.57900   1.000 23.37968 ? 117 LYS   B CE    1 
ATOM   2344 N  NZ    . LYS   B 1 118 ? -31.37600 35.68500 7.31900   1.000 23.41398 ? 117 LYS   B NZ    1 
ATOM   2345 N  N     . CYS   B 1 119 ? -27.79900 43.62700 6.46400   1.000 31.40146 ? 118 CYS   B N     1 
ATOM   2346 C  CA    A CYS   B 1 119 ? -27.52700 44.87600 7.16800   0.500 32.46767 ? 118 CYS   B CA    1 
ATOM   2347 C  CA    B CYS   B 1 119 ? -27.52700 44.88000 7.15900   0.500 33.37002 ? 118 CYS   B CA    1 
ATOM   2348 C  C     . CYS   B 1 119 ? -28.72700 45.81300 7.20400   1.000 34.67209 ? 118 CYS   B C     1 
ATOM   2349 O  O     . CYS   B 1 119 ? -28.66700 46.83700 7.88900   1.000 36.69761 ? 118 CYS   B O     1 
ATOM   2350 C  CB    A CYS   B 1 119 ? -26.27400 45.56900 6.61100   0.500 31.48694 ? 118 CYS   B CB    1 
ATOM   2351 C  CB    B CYS   B 1 119 ? -26.32500 45.58200 6.54200   0.500 34.15199 ? 118 CYS   B CB    1 
ATOM   2352 S  SG    A CYS   B 1 119 ? -26.40300 46.24800 4.94000   0.500 32.29646 ? 118 CYS   B SG    1 
ATOM   2353 S  SG    B CYS   B 1 119 ? -24.81600 44.69500 6.86600   0.500 36.33526 ? 118 CYS   B SG    1 
ATOM   2354 N  N     . ASP   B 1 120 ? -29.81300 45.48300 6.50300   1.000 34.96334 ? 119 ASP   B N     1 
ATOM   2355 C  CA    . ASP   B 1 120 ? -31.04100 46.25800 6.62600   1.000 36.35640 ? 119 ASP   B CA    1 
ATOM   2356 C  C     . ASP   B 1 120 ? -31.77500 45.97600 7.92900   1.000 35.93904 ? 119 ASP   B C     1 
ATOM   2357 O  O     . ASP   B 1 120 ? -32.64700 46.76100 8.32000   1.000 37.17053 ? 119 ASP   B O     1 
ATOM   2358 C  CB    . ASP   B 1 120 ? -31.98600 45.91000 5.48000   1.000 36.43601 ? 119 ASP   B CB    1 
ATOM   2359 C  CG    . ASP   B 1 120 ? -32.29000 44.43100 5.41900   1.000 36.55517 ? 119 ASP   B CG    1 
ATOM   2360 O  OD1   . ASP   B 1 120 ? -31.40400 43.66800 4.98900   1.000 34.81369 ? 119 ASP   B OD1   1 
ATOM   2361 O  OD2   . ASP   B 1 120 ? -33.39600 44.02800 5.83700   1.000 36.10534 ? 119 ASP   B OD2   1 
ATOM   2362 N  N     . LEU   B 1 121 ? -31.45200 44.87900 8.60700   1.000 36.12500 ? 120 LEU   B N     1 
ATOM   2363 C  CA    . LEU   B 1 121 ? -32.25500 44.46000 9.74400   1.000 36.54013 ? 120 LEU   B CA    1 
ATOM   2364 C  C     . LEU   B 1 121 ? -31.83200 45.18500 11.01900  1.000 38.00329 ? 120 LEU   B C     1 
ATOM   2365 O  O     . LEU   B 1 121 ? -30.64900 45.47000 11.22100  1.000 39.57269 ? 120 LEU   B O     1 
ATOM   2366 C  CB    . LEU   B 1 121 ? -32.12600 42.95800 9.94400   1.000 34.67097 ? 120 LEU   B CB    1 
ATOM   2367 C  CG    . LEU   B 1 121 ? -32.90300 42.13900 8.91600   1.000 33.98123 ? 120 LEU   B CG    1 
ATOM   2368 C  CD1   . LEU   B 1 121 ? -32.73900 40.65400 9.18700   1.000 35.88218 ? 120 LEU   B CD1   1 
ATOM   2369 C  CD2   . LEU   B 1 121 ? -34.37800 42.53900 8.91300   1.000 31.95908 ? 120 LEU   B CD2   1 
ATOM   2370 N  N     . PRO   B 1 122 ? -32.79100 45.47700 11.91000  1.000 36.46886 ? 121 PRO   B N     1 
ATOM   2371 C  CA    . PRO   B 1 122 ? -32.46700 46.19900 13.14800  1.000 36.63796 ? 121 PRO   B CA    1 
ATOM   2372 C  C     . PRO   B 1 122 ? -32.09900 45.29600 14.31900  1.000 36.07653 ? 121 PRO   B C     1 
ATOM   2373 O  O     . PRO   B 1 122 ? -32.14700 45.74000 15.47000  1.000 37.68793 ? 121 PRO   B O     1 
ATOM   2374 C  CB    . PRO   B 1 122 ? -33.77800 46.92800 13.45500  1.000 34.23233 ? 121 PRO   B CB    1 
ATOM   2375 C  CG    . PRO   B 1 122 ? -34.82300 45.96500 12.97800  1.000 34.15148 ? 121 PRO   B CG    1 
ATOM   2376 C  CD    . PRO   B 1 122 ? -34.24700 45.31900 11.73300  1.000 34.19163 ? 121 PRO   B CD    1 
ATOM   2377 N  N     . SER   B 1 123 ? -31.75100 44.04000 14.06000  1.000 35.26937 ? 122 SER   B N     1 
ATOM   2378 C  CA    . SER   B 1 123 ? -31.50000 43.05000 15.10400  1.000 34.97166 ? 122 SER   B CA    1 
ATOM   2379 C  C     . SER   B 1 123 ? -30.04600 42.58200 15.11300  1.000 33.09318 ? 122 SER   B C     1 
ATOM   2380 O  O     . SER   B 1 123 ? -29.75400 41.42200 15.41000  1.000 31.19848 ? 122 SER   B O     1 
ATOM   2381 C  CB    . SER   B 1 123 ? -32.44300 41.85900 14.95300  1.000 35.37985 ? 122 SER   B CB    1 
ATOM   2382 O  OG    . SER   B 1 123 ? -32.30400 41.28900 13.66100  1.000 34.34028 ? 122 SER   B OG    1 
ATOM   2383 N  N     . ARG   B 1 124 ? -29.11500 43.48900 14.81000  1.000 31.36147 ? 123 ARG   B N     1 
ATOM   2384 C  CA    . ARG   B 1 124 ? -27.70500 43.12900 14.69800  1.000 31.47156 ? 123 ARG   B CA    1 
ATOM   2385 C  C     . ARG   B 1 124 ? -27.15000 42.54400 15.99600  1.000 30.64142 ? 123 ARG   B C     1 
ATOM   2386 O  O     . ARG   B 1 124 ? -27.45600 43.00900 17.10000  1.000 33.40511 ? 123 ARG   B O     1 
ATOM   2387 C  CB    . ARG   B 1 124 ? -26.90000 44.37100 14.32000  1.000 31.73898 ? 123 ARG   B CB    1 
ATOM   2388 C  CG    . ARG   B 1 124 ? -25.39600 44.20500 14.43700  1.000 33.72797 ? 123 ARG   B CG    1 
ATOM   2389 C  CD    . ARG   B 1 124 ? -24.67400 45.49500 14.09900  1.000 35.97362 ? 123 ARG   B CD    1 
ATOM   2390 N  NE    . ARG   B 1 124 ? -24.95200 45.93800 12.73900  1.000 36.72972 ? 123 ARG   B NE    1 
ATOM   2391 C  CZ    . ARG   B 1 124 ? -24.18000 45.67300 11.69400  1.000 37.06153 ? 123 ARG   B CZ    1 
ATOM   2392 N  NH1   . ARG   B 1 124 ? -23.08500 44.94300 11.81600  1.000 34.32062 ? 123 ARG   B NH1   1 
ATOM   2393 N  NH2   . ARG   B 1 124 ? -24.51100 46.16000 10.50100  1.000 38.77806 ? 123 ARG   B NH2   1 
ATOM   2394 N  N     . THR   B 1 125 ? -26.32400 41.51100 15.85300  1.000 29.12835 ? 124 THR   B N     1 
ATOM   2395 C  CA    . THR   B 1 125 ? -25.58100 40.92300 16.95600  1.000 29.31975 ? 124 THR   B CA    1 
ATOM   2396 C  C     . THR   B 1 125 ? -24.07500 40.90700 16.73400  1.000 29.71371 ? 124 THR   B C     1 
ATOM   2397 O  O     . THR   B 1 125 ? -23.33200 40.72500 17.70200  1.000 31.07539 ? 124 THR   B O     1 
ATOM   2398 C  CB    . THR   B 1 125 ? -26.06200 39.48700 17.23000  1.000 27.95249 ? 124 THR   B CB    1 
ATOM   2399 O  OG1   . THR   B 1 125 ? -25.78600 38.66400 16.08900  1.000 28.13616 ? 124 THR   B OG1   1 
ATOM   2400 C  CG2   . THR   B 1 125 ? -27.56200 39.47300 17.52300  1.000 27.87696 ? 124 THR   B CG2   1 
ATOM   2401 N  N     . VAL   B 1 126 ? -23.60900 41.09500 15.49900  1.000 28.94336 ? 125 VAL   B N     1 
ATOM   2402 C  CA    . VAL   B 1 126 ? -22.18700 41.11500 15.17100  1.000 30.38766 ? 125 VAL   B CA    1 
ATOM   2403 C  C     . VAL   B 1 126 ? -21.81800 42.54100 14.78500  1.000 34.47503 ? 125 VAL   B C     1 
ATOM   2404 O  O     . VAL   B 1 126 ? -22.35500 43.08600 13.81200  1.000 34.55794 ? 125 VAL   B O     1 
ATOM   2405 C  CB    . VAL   B 1 126 ? -21.86400 40.13900 14.02800  1.000 28.43516 ? 125 VAL   B CB    1 
ATOM   2406 C  CG1   . VAL   B 1 126 ? -20.36200 40.09700 13.76300  1.000 28.81480 ? 125 VAL   B CG1   1 
ATOM   2407 C  CG2   . VAL   B 1 126 ? -22.40200 38.75300 14.35500  1.000 29.04173 ? 125 VAL   B CG2   1 
ATOM   2408 N  N     . ASP   B 1 127 ? -20.89400 43.14100 15.53500  1.000 38.32201 ? 126 ASP   B N     1 
ATOM   2409 C  CA    . ASP   B 1 127 ? -20.45600 44.49800 15.24200  1.000 40.65026 ? 126 ASP   B CA    1 
ATOM   2410 C  C     . ASP   B 1 127 ? -19.63700 44.54300 13.95800  1.000 39.44406 ? 126 ASP   B C     1 
ATOM   2411 O  O     . ASP   B 1 127 ? -18.88300 43.62000 13.64200  1.000 40.03738 ? 126 ASP   B O     1 
ATOM   2412 C  CB    . ASP   B 1 127 ? -19.59500 45.03200 16.38400  1.000 46.04659 ? 126 ASP   B CB    1 
ATOM   2413 C  CG    . ASP   B 1 127 ? -20.36800 45.17200 17.67500  1.000 53.49181 ? 126 ASP   B CG    1 
ATOM   2414 O  OD1   . ASP   B 1 127 ? -21.61600 45.20300 17.61200  1.000 56.08540 ? 126 ASP   B OD1   1 
ATOM   2415 O  OD2   . ASP   B 1 127 ? -19.73000 45.25700 18.74700  1.000 55.70653 ? 126 ASP   B OD2   1 
ATOM   2416 N  N     . THR   B 1 128 ? -19.77900 45.65400 13.22700  1.000 40.10985 ? 127 THR   B N     1 
ATOM   2417 C  CA    . THR   B 1 128 ? -18.95900 45.88000 12.03900  1.000 40.58688 ? 127 THR   B CA    1 
ATOM   2418 C  C     . THR   B 1 128 ? -17.47400 45.76700 12.35800  1.000 39.46863 ? 127 THR   B C     1 
ATOM   2419 O  O     . THR   B 1 128 ? -16.71800 45.13600 11.61100  1.000 39.00014 ? 127 THR   B O     1 
ATOM   2420 C  CB    . THR   B 1 128 ? -19.27200 47.25300 11.43700  1.000 42.61917 ? 127 THR   B CB    1 
ATOM   2421 O  OG1   . THR   B 1 128 ? -20.63800 47.29200 11.01100  1.000 43.69218 ? 127 THR   B OG1   1 
ATOM   2422 C  CG2   . THR   B 1 128 ? -18.36900 47.53500 10.24200  1.000 43.97935 ? 127 THR   B CG2   1 
ATOM   2423 N  N     . LYS   B 1 129 ? -17.04100 46.36200 13.47500  1.000 39.12050 ? 128 LYS   B N     1 
ATOM   2424 C  CA    . LYS   B 1 129 ? -15.62100 46.34600 13.81600  1.000 41.02636 ? 128 LYS   B CA    1 
ATOM   2425 C  C     . LYS   B 1 129 ? -15.10300 44.92200 13.99100  1.000 39.55804 ? 128 LYS   B C     1 
ATOM   2426 O  O     . LYS   B 1 129 ? -13.99100 44.60000 13.55600  1.000 38.33010 ? 128 LYS   B O     1 
ATOM   2427 C  CB    . LYS   B 1 129 ? -15.35400 47.18400 15.06800  1.000 41.97310 ? 128 LYS   B CB    1 
ATOM   2428 C  CG    . LYS   B 1 129 ? -13.92000 47.07700 15.55600  1.000 44.49082 ? 128 LYS   B CG    1 
ATOM   2429 C  CD    . LYS   B 1 129 ? -13.62500 48.00200 16.71700  1.000 48.22627 ? 128 LYS   B CD    1 
ATOM   2430 C  CE    . LYS   B 1 129 ? -12.20200 47.78000 17.20700  1.000 51.48573 ? 128 LYS   B CE    1 
ATOM   2431 N  NZ    . LYS   B 1 129 ? -11.24700 47.66200 16.06300  1.000 53.35273 ? 128 LYS   B NZ    1 
ATOM   2432 N  N     . GLN   B 1 130 ? -15.89600 44.05200 14.61800  1.000 39.00892 ? 129 GLN   B N     1 
ATOM   2433 C  CA    . GLN   B 1 130 ? -15.46600 42.67000 14.80800  1.000 40.50052 ? 129 GLN   B CA    1 
ATOM   2434 C  C     . GLN   B 1 130 ? -15.22500 41.98200 13.47200  1.000 35.80291 ? 129 GLN   B C     1 
ATOM   2435 O  O     . GLN   B 1 130 ? -14.25100 41.23800 13.30900  1.000 34.19280 ? 129 GLN   B O     1 
ATOM   2436 C  CB    . GLN   B 1 130 ? -16.52100 41.91200 15.60600  1.000 46.96625 ? 129 GLN   B CB    1 
ATOM   2437 C  CG    . GLN   B 1 130 ? -16.06900 40.56200 16.08600  1.000 53.23251 ? 129 GLN   B CG    1 
ATOM   2438 C  CD    . GLN   B 1 130 ? -17.06100 39.95100 17.04600  1.000 58.39472 ? 129 GLN   B CD    1 
ATOM   2439 O  OE1   . GLN   B 1 130 ? -18.01000 40.61200 17.47800  1.000 60.90462 ? 129 GLN   B OE1   1 
ATOM   2440 N  NE2   . GLN   B 1 130 ? -16.85200 38.68500 17.38800  1.000 60.35842 ? 129 GLN   B NE2   1 
ATOM   2441 N  N     . ALA   B 1 131 ? -16.09900 42.22700 12.50200  1.000 32.83786 ? 130 ALA   B N     1 
ATOM   2442 C  CA    . ALA   B 1 131 ? -15.94200 41.60300 11.19400  1.000 32.23574 ? 130 ALA   B CA    1 
ATOM   2443 C  C     . ALA   B 1 131 ? -14.79600 42.23600 10.41600  1.000 31.20712 ? 130 ALA   B C     1 
ATOM   2444 O  O     . ALA   B 1 131 ? -14.07100 41.54500 9.69200   1.000 31.11145 ? 130 ALA   B O     1 
ATOM   2445 C  CB    . ALA   B 1 131 ? -17.25200 41.70400 10.42300  1.000 34.06107 ? 130 ALA   B CB    1 
ATOM   2446 N  N     . GLN   B 1 132 ? -14.61000 43.54700 10.56100  1.000 31.03897 ? 131 GLN   B N     1 
ATOM   2447 C  CA    . GLN   B 1 132 ? -13.46000 44.19100 9.93400   1.000 32.77605 ? 131 GLN   B CA    1 
ATOM   2448 C  C     . GLN   B 1 132 ? -12.15600 43.61100 10.46600  1.000 33.11302 ? 131 GLN   B C     1 
ATOM   2449 O  O     . GLN   B 1 132 ? -11.23000 43.32500 9.69700   1.000 32.92916 ? 131 GLN   B O     1 
ATOM   2450 C  CB    . GLN   B 1 132 ? -13.51900 45.70000 10.17200  1.000 37.80794 ? 131 GLN   B CB    1 
ATOM   2451 C  CG    . GLN   B 1 132 ? -14.67400 46.39100 9.46300   1.000 42.65006 ? 131 GLN   B CG    1 
ATOM   2452 C  CD    . GLN   B 1 132 ? -14.80200 47.85300 9.83200   1.000 48.71710 ? 131 GLN   B CD    1 
ATOM   2453 O  OE1   . GLN   B 1 132 ? -14.46100 48.25800 10.94500  1.000 50.68876 ? 131 GLN   B OE1   1 
ATOM   2454 N  NE2   . GLN   B 1 132 ? -15.29800 48.65900 8.89800   1.000 50.29590 ? 131 GLN   B NE2   1 
ATOM   2455 N  N     . ASP   B 1 133 ? -12.07400 43.41700 11.78600  1.000 31.91075 ? 132 ASP   B N     1 
ATOM   2456 C  CA    . ASP   B 1 133 ? -10.86100 42.87000 12.38300  1.000 35.78041 ? 132 ASP   B CA    1 
ATOM   2457 C  C     . ASP   B 1 133 ? -10.59300 41.45300 11.88900  1.000 33.11921 ? 132 ASP   B C     1 
ATOM   2458 O  O     . ASP   B 1 133 ? -9.44400  41.09200 11.61500  1.000 35.40695 ? 132 ASP   B O     1 
ATOM   2459 C  CB    . ASP   B 1 133 ? -10.96700 42.89400 13.91000  1.000 38.85799 ? 132 ASP   B CB    1 
ATOM   2460 C  CG    . ASP   B 1 133 ? -11.07600 44.31200 14.47600  1.000 43.15544 ? 132 ASP   B CG    1 
ATOM   2461 O  OD1   . ASP   B 1 133 ? -10.60400 45.26400 13.82000  1.000 45.26325 ? 132 ASP   B OD1   1 
ATOM   2462 O  OD2   . ASP   B 1 133 ? -11.63100 44.47800 15.58600  1.000 44.54515 ? 132 ASP   B OD2   1 
ATOM   2463 N  N     . LEU   B 1 134 ? -11.64100 40.63500 11.77700  1.000 32.49749 ? 133 LEU   B N     1 
ATOM   2464 C  CA    . LEU   B 1 134 ? -11.46200 39.28400 11.25600  1.000 30.73421 ? 133 LEU   B CA    1 
ATOM   2465 C  C     . LEU   B 1 134 ? -10.93200 39.31100 9.82800   1.000 29.30931 ? 133 LEU   B C     1 
ATOM   2466 O  O     . LEU   B 1 134 ? -9.94800  38.63500 9.50300   1.000 30.33422 ? 133 LEU   B O     1 
ATOM   2467 C  CB    . LEU   B 1 134 ? -12.77900 38.51300 11.32100  1.000 31.51755 ? 133 LEU   B CB    1 
ATOM   2468 C  CG    . LEU   B 1 134 ? -12.62200 37.06100 10.88100  1.000 34.66620 ? 133 LEU   B CG    1 
ATOM   2469 C  CD1   . LEU   B 1 134 ? -11.62600 36.36800 11.79200  1.000 36.73376 ? 133 LEU   B CD1   1 
ATOM   2470 C  CD2   . LEU   B 1 134 ? -13.95700 36.33800 10.86000  1.000 33.80816 ? 133 LEU   B CD2   1 
ATOM   2471 N  N     . ALA   B 1 135 ? -11.57600 40.09100 8.95700   1.000 27.81642 ? 134 ALA   B N     1 
ATOM   2472 C  CA    . ALA   B 1 135 ? -11.12600 40.17100 7.57000   1.000 28.06170 ? 134 ALA   B CA    1 
ATOM   2473 C  C     . ALA   B 1 135 ? -9.69300  40.67800 7.48300   1.000 29.69875 ? 134 ALA   B C     1 
ATOM   2474 O  O     . ALA   B 1 135 ? -8.90700  40.20100 6.65600   1.000 30.05751 ? 134 ALA   B O     1 
ATOM   2475 C  CB    . ALA   B 1 135 ? -12.06800 41.06200 6.76600   1.000 27.58043 ? 134 ALA   B CB    1 
ATOM   2476 N  N     . ARG   B 1 136 ? -9.33000  41.64300 8.33100   1.000 30.61121 ? 135 ARG   B N     1 
ATOM   2477 C  CA    . ARG   B 1 136 ? -7.95500  42.13100 8.33100   1.000 33.22221 ? 135 ARG   B CA    1 
ATOM   2478 C  C     . ARG   B 1 136 ? -6.98400  41.03900 8.76100   1.000 31.98176 ? 135 ARG   B C     1 
ATOM   2479 O  O     . ARG   B 1 136 ? -5.87800  40.93100 8.21900   1.000 33.04742 ? 135 ARG   B O     1 
ATOM   2480 C  CB    . ARG   B 1 136 ? -7.82900  43.35200 9.23800   1.000 35.71024 ? 135 ARG   B CB    1 
ATOM   2481 C  CG    . ARG   B 1 136 ? -6.48400  44.05400 9.12400   1.000 40.00872 ? 135 ARG   B CG    1 
ATOM   2482 C  CD    . ARG   B 1 136 ? -6.36600  45.19900 10.11500  1.000 47.25267 ? 135 ARG   B CD    1 
ATOM   2483 N  NE    . ARG   B 1 136 ? -7.46500  46.14800 9.98700   1.000 53.33556 ? 135 ARG   B NE    1 
ATOM   2484 C  CZ    . ARG   B 1 136 ? -8.45700  46.27000 10.86000  1.000 57.41865 ? 135 ARG   B CZ    1 
ATOM   2485 N  NH1   . ARG   B 1 136 ? -8.51300  45.52400 11.95200  1.000 58.46616 ? 135 ARG   B NH1   1 
ATOM   2486 N  NH2   . ARG   B 1 136 ? -9.41500  47.16400 10.63200  1.000 59.38651 ? 135 ARG   B NH2   1 
ATOM   2487 N  N     . SER   B 1 137 ? -7.37800  40.21700 9.73700   1.000 32.93467 ? 136 SER   B N     1 
ATOM   2488 C  CA    . SER   B 1 137 ? -6.52500  39.10300 10.13800  1.000 35.21045 ? 136 SER   B CA    1 
ATOM   2489 C  C     . SER   B 1 137 ? -6.31500  38.12400 8.98900   1.000 35.42883 ? 136 SER   B C     1 
ATOM   2490 O  O     . SER   B 1 137 ? -5.27600  37.45800 8.92200   1.000 38.40999 ? 136 SER   B O     1 
ATOM   2491 C  CB    . SER   B 1 137 ? -7.11200  38.39100 11.35900  1.000 37.90292 ? 136 SER   B CB    1 
ATOM   2492 O  OG    . SER   B 1 137 ? -8.20500  37.56500 10.99400  1.000 39.15721 ? 136 SER   B OG    1 
ATOM   2493 N  N     . TYR   B 1 138 ? -7.27800  38.03500 8.06900   1.000 32.49166 ? 137 TYR   B N     1 
ATOM   2494 C  CA    . TYR   B 1 138 ? -7.17800  37.16500 6.90600   1.000 32.76139 ? 137 TYR   B CA    1 
ATOM   2495 C  C     . TYR   B 1 138 ? -6.52200  37.83600 5.70900   1.000 32.10964 ? 137 TYR   B C     1 
ATOM   2496 O  O     . TYR   B 1 138 ? -6.15700  37.14000 4.75500   1.000 33.13949 ? 137 TYR   B O     1 
ATOM   2497 C  CB    . TYR   B 1 138 ? -8.57000  36.68700 6.49200   1.000 31.62461 ? 137 TYR   B CB    1 
ATOM   2498 C  CG    . TYR   B 1 138 ? -9.21600  35.74700 7.47800   1.000 31.31036 ? 137 TYR   B CG    1 
ATOM   2499 C  CD1   . TYR   B 1 138 ? -8.46100  35.08300 8.44100   1.000 32.28692 ? 137 TYR   B CD1   1 
ATOM   2500 C  CD2   . TYR   B 1 138 ? -10.58300 35.50700 7.43600   1.000 31.70938 ? 137 TYR   B CD2   1 
ATOM   2501 C  CE1   . TYR   B 1 138 ? -9.06300  34.21100 9.34500   1.000 32.04629 ? 137 TYR   B CE1   1 
ATOM   2502 C  CE2   . TYR   B 1 138 ? -11.18400 34.64100 8.32400   1.000 31.48310 ? 137 TYR   B CE2   1 
ATOM   2503 C  CZ    . TYR   B 1 138 ? -10.42000 33.99800 9.27600   1.000 32.03207 ? 137 TYR   B CZ    1 
ATOM   2504 O  OH    . TYR   B 1 138 ? -11.03100 33.13500 10.15600  1.000 36.26118 ? 137 TYR   B OH    1 
ATOM   2505 N  N     . GLY   B 1 139 ? -6.37300  39.15800 5.73200   1.000 30.31797 ? 138 GLY   B N     1 
ATOM   2506 C  CA    . GLY   B 1 139 ? -5.87800  39.87900 4.57600   1.000 28.41203 ? 138 GLY   B CA    1 
ATOM   2507 C  C     . GLY   B 1 139 ? -6.86300  39.93200 3.43000   1.000 27.80575 ? 138 GLY   B C     1 
ATOM   2508 O  O     . GLY   B 1 139 ? -6.45200  39.92600 2.25900   1.000 27.80253 ? 138 GLY   B O     1 
ATOM   2509 N  N     . ILE   B 1 140 ? -8.15600  39.98000 3.73400   1.000 24.39244 ? 139 ILE   B N     1 
ATOM   2510 C  CA    . ILE   B 1 140 ? -9.18800  39.93700 2.69800   1.000 24.74677 ? 139 ILE   B CA    1 
ATOM   2511 C  C     . ILE   B 1 140 ? -10.15300 41.09700 2.90900   1.000 23.91249 ? 139 ILE   B C     1 
ATOM   2512 O  O     . ILE   B 1 140 ? -10.26700 41.65000 4.01500   1.000 24.49778 ? 139 ILE   B O     1 
ATOM   2513 C  CB    . ILE   B 1 140 ? -9.94200  38.58500 2.69100   1.000 24.44190 ? 139 ILE   B CB    1 
ATOM   2514 C  CG1   . ILE   B 1 140 ? -10.82100 38.44100 3.94100   1.000 24.54846 ? 139 ILE   B CG1   1 
ATOM   2515 C  CG2   . ILE   B 1 140 ? -8.97100  37.41200 2.51700   1.000 24.06209 ? 139 ILE   B CG2   1 
ATOM   2516 C  CD1   . ILE   B 1 140 ? -11.64600 37.16500 3.97500   1.000 27.76927 ? 139 ILE   B CD1   1 
ATOM   2517 N  N     . PRO   B 1 141 ? -10.88700 41.47200 1.86800   1.000 24.30938 ? 140 PRO   B N     1 
ATOM   2518 C  CA    . PRO   B 1 141 ? -11.88500 42.52900 2.02300   1.000 24.20264 ? 140 PRO   B CA    1 
ATOM   2519 C  C     . PRO   B 1 141 ? -13.07700 42.07400 2.84900   1.000 24.47789 ? 140 PRO   B C     1 
ATOM   2520 O  O     . PRO   B 1 141 ? -13.43200 40.89200 2.89500   1.000 25.21744 ? 140 PRO   B O     1 
ATOM   2521 C  CB    . PRO   B 1 141 ? -12.32000 42.82000 0.58300   1.000 25.15292 ? 140 PRO   B CB    1 
ATOM   2522 C  CG    . PRO   B 1 141 ? -11.21600 42.28800 -0.26300  1.000 24.27421 ? 140 PRO   B CG    1 
ATOM   2523 C  CD    . PRO   B 1 141 ? -10.72100 41.08600 0.45900   1.000 24.16016 ? 140 PRO   B CD    1 
ATOM   2524 N  N     . PHE   B 1 142 ? -13.69800 43.04800 3.50200   1.000 25.55386 ? 141 PHE   B N     1 
ATOM   2525 C  CA    . PHE   B 1 142 ? -14.96200 42.86500 4.19400   1.000 25.33367 ? 141 PHE   B CA    1 
ATOM   2526 C  C     . PHE   B 1 142 ? -15.97700 43.81600 3.58200   1.000 27.38141 ? 141 PHE   B C     1 
ATOM   2527 O  O     . PHE   B 1 142 ? -15.68100 44.99600 3.37400   1.000 29.13785 ? 141 PHE   B O     1 
ATOM   2528 C  CB    . PHE   B 1 142 ? -14.82700 43.14200 5.69100   1.000 26.91466 ? 141 PHE   B CB    1 
ATOM   2529 C  CG    . PHE   B 1 142 ? -16.13900 43.19700 6.40200   1.000 30.55669 ? 141 PHE   B CG    1 
ATOM   2530 C  CD1   . PHE   B 1 142 ? -16.98300 42.09400 6.41000   1.000 29.82020 ? 141 PHE   B CD1   1 
ATOM   2531 C  CD2   . PHE   B 1 142 ? -16.53900 44.35000 7.05200   1.000 32.30372 ? 141 PHE   B CD2   1 
ATOM   2532 C  CE1   . PHE   B 1 142 ? -18.20500 42.14000 7.06700   1.000 31.07497 ? 141 PHE   B CE1   1 
ATOM   2533 C  CE2   . PHE   B 1 142 ? -17.75100 44.41000 7.70400   1.000 33.02872 ? 141 PHE   B CE2   1 
ATOM   2534 C  CZ    . PHE   B 1 142 ? -18.59000 43.30000 7.71200   1.000 33.40725 ? 141 PHE   B CZ    1 
ATOM   2535 N  N     . ILE   B 1 143 ? -17.16300 43.30700 3.27500   1.000 25.89405 ? 142 ILE   B N     1 
ATOM   2536 C  CA    . ILE   B 1 143 ? -18.22700 44.14800 2.74500   1.000 26.68027 ? 142 ILE   B CA    1 
ATOM   2537 C  C     . ILE   B 1 143 ? -19.55400 43.77900 3.39000   1.000 26.06764 ? 142 ILE   B C     1 
ATOM   2538 O  O     . ILE   B 1 143 ? -19.89200 42.59700 3.51900   1.000 24.56382 ? 142 ILE   B O     1 
ATOM   2539 C  CB    . ILE   B 1 143 ? -18.32200 44.08300 1.21200   1.000 32.20985 ? 142 ILE   B CB    1 
ATOM   2540 C  CG1   . ILE   B 1 143 ? -19.47400 44.96900 0.74500   1.000 34.52062 ? 142 ILE   B CG1   1 
ATOM   2541 C  CG2   . ILE   B 1 143 ? -18.49400 42.66300 0.75200   1.000 34.44255 ? 142 ILE   B CG2   1 
ATOM   2542 C  CD1   . ILE   B 1 143 ? -19.89100 44.70600 -0.63600  1.000 35.07709 ? 142 ILE   B CD1   1 
ATOM   2543 N  N     . GLU   B 1 144 ? -20.30700 44.80500 3.78500   1.000 30.22809 ? 143 GLU   B N     1 
ATOM   2544 C  CA    . GLU   B 1 144 ? -21.65200 44.63400 4.30900   1.000 34.01985 ? 143 GLU   B CA    1 
ATOM   2545 C  C     . GLU   B 1 144 ? -22.67100 44.74800 3.18500   1.000 31.84109 ? 143 GLU   B C     1 
ATOM   2546 O  O     . GLU   B 1 144 ? -22.53600 45.58700 2.28500   1.000 33.35184 ? 143 GLU   B O     1 
ATOM   2547 C  CB    . GLU   B 1 144 ? -21.94100 45.68800 5.37700   1.000 38.72491 ? 143 GLU   B CB    1 
ATOM   2548 C  CG    . GLU   B 1 144 ? -21.40300 45.32100 6.74600   1.000 43.05696 ? 143 GLU   B CG    1 
ATOM   2549 C  CD    . GLU   B 1 144 ? -22.03500 46.12700 7.85800   1.000 46.91368 ? 143 GLU   B CD    1 
ATOM   2550 O  OE1   . GLU   B 1 144 ? -22.54100 47.23800 7.58600   1.000 51.59805 ? 143 GLU   B OE1   1 
ATOM   2551 O  OE2   . GLU   B 1 144 ? -22.03300 45.63100 9.00100   1.000 46.24837 ? 143 GLU   B OE2   1 
ATOM   2552 N  N     . THR   B 1 145 ? -23.69300 43.89400 3.24000   1.000 29.28853 ? 144 THR   B N     1 
ATOM   2553 C  CA    . THR   B 1 145 ? -24.67100 43.79800 2.16700   1.000 29.27840 ? 144 THR   B CA    1 
ATOM   2554 C  C     . THR   B 1 145 ? -26.07000 43.64600 2.74100   1.000 29.88466 ? 144 THR   B C     1 
ATOM   2555 O  O     . THR   B 1 145 ? -26.26700 43.23300 3.89200   1.000 29.16114 ? 144 THR   B O     1 
ATOM   2556 C  CB    . THR   B 1 145 ? -24.41700 42.60200 1.22600   1.000 26.99332 ? 144 THR   B CB    1 
ATOM   2557 O  OG1   . THR   B 1 145 ? -24.63100 41.37200 1.93600   1.000 27.18502 ? 144 THR   B OG1   1 
ATOM   2558 C  CG2   . THR   B 1 145 ? -22.99900 42.61100 0.67400   1.000 26.82449 ? 144 THR   B CG2   1 
ATOM   2559 N  N     . SER   B 1 146 ? -27.04400 43.98000 1.90300   1.000 28.17890 ? 145 SER   B N     1 
ATOM   2560 C  CA    . SER   B 1 146 ? -28.43600 43.61300 2.12800   1.000 28.82521 ? 145 SER   B CA    1 
ATOM   2561 C  C     . SER   B 1 146 ? -28.99400 43.12000 0.80400   1.000 27.64911 ? 145 SER   B C     1 
ATOM   2562 O  O     . SER   B 1 146 ? -29.15300 43.90600 -0.13400  1.000 30.07308 ? 145 SER   B O     1 
ATOM   2563 C  CB    . SER   B 1 146 ? -29.25100 44.79100 2.64000   1.000 28.63930 ? 145 SER   B CB    1 
ATOM   2564 O  OG    . SER   B 1 146 ? -30.63000 44.47000 2.59200   1.000 30.37582 ? 145 SER   B OG    1 
ATOM   2565 N  N     . ALA   B 1 147 ? -29.28800 41.82300 0.71900   1.000 27.33678 ? 146 ALA   B N     1 
ATOM   2566 C  CA    . ALA   B 1 147 ? -29.95900 41.32600 -0.47300  1.000 29.06523 ? 146 ALA   B CA    1 
ATOM   2567 C  C     . ALA   B 1 147 ? -31.35800 41.90600 -0.61100  1.000 29.95501 ? 146 ALA   B C     1 
ATOM   2568 O  O     . ALA   B 1 147 ? -31.90200 41.93100 -1.71900  1.000 31.46020 ? 146 ALA   B O     1 
ATOM   2569 C  CB    . ALA   B 1 147 ? -30.01800 39.79800 -0.46600  1.000 28.22352 ? 146 ALA   B CB    1 
ATOM   2570 N  N     . LYS   B 1 148 ? -31.94800 42.38300 0.48800   1.000 31.11630 ? 147 LYS   B N     1 
ATOM   2571 C  CA    . LYS   B 1 148 ? -33.29300 42.94200 0.42500   1.000 34.10017 ? 147 LYS   B CA    1 
ATOM   2572 C  C     . LYS   B 1 148 ? -33.30500 44.29700 -0.27700  1.000 36.61922 ? 147 LYS   B C     1 
ATOM   2573 O  O     . LYS   B 1 148 ? -34.10700 44.52300 -1.19200  1.000 37.90274 ? 147 LYS   B O     1 
ATOM   2574 C  CB    . LYS   B 1 148 ? -33.87500 43.04400 1.83100   1.000 34.34285 ? 147 LYS   B CB    1 
ATOM   2575 C  CG    . LYS   B 1 148 ? -35.26100 43.66300 1.87600   1.000 35.14355 ? 147 LYS   B CG    1 
ATOM   2576 C  CD    . LYS   B 1 148 ? -35.85900 43.57500 3.27400   1.000 36.39957 ? 147 LYS   B CD    1 
ATOM   2577 C  CE    . LYS   B 1 148 ? -37.27400 44.14200 3.31900   1.000 39.02805 ? 147 LYS   B CE    1 
ATOM   2578 N  NZ    . LYS   B 1 148 ? -37.83300 44.11300 4.69700   1.000 42.54700 ? 147 LYS   B NZ    1 
ATOM   2579 N  N     . THR   B 1 149 ? -32.43200 45.21800 0.13500   1.000 35.75763 ? 148 THR   B N     1 
ATOM   2580 C  CA    . THR   B 1 149 ? -32.37500 46.54500 -0.47400  1.000 36.31628 ? 148 THR   B CA    1 
ATOM   2581 C  C     . THR   B 1 149 ? -31.42100 46.60500 -1.65400  1.000 36.48349 ? 148 THR   B C     1 
ATOM   2582 O  O     . THR   B 1 149 ? -31.32800 47.65100 -2.30500  1.000 38.42423 ? 148 THR   B O     1 
ATOM   2583 C  CB    . THR   B 1 149 ? -31.94100 47.60400 0.54600   1.000 36.28820 ? 148 THR   B CB    1 
ATOM   2584 O  OG1   . THR   B 1 149 ? -30.56300 47.39300 0.88700   1.000 37.05396 ? 148 THR   B OG1   1 
ATOM   2585 C  CG2   . THR   B 1 149 ? -32.82000 47.55400 1.79900   1.000 37.17098 ? 148 THR   B CG2   1 
ATOM   2586 N  N     . ARG   B 1 150 ? -30.71100 45.51300 -1.93300  1.000 36.02374 ? 149 ARG   B N     1 
ATOM   2587 C  CA    . ARG   B 1 150 ? -29.67400 45.39500 -2.95200  1.000 36.26336 ? 149 ARG   B CA    1 
ATOM   2588 C  C     . ARG   B 1 150 ? -28.38300 46.12200 -2.58100  1.000 36.14435 ? 149 ARG   B C     1 
ATOM   2589 O  O     . ARG   B 1 150 ? -27.42800 46.10700 -3.37500  1.000 34.98567 ? 149 ARG   B O     1 
ATOM   2590 C  CB    . ARG   B 1 150 ? -30.15100 45.77500 -4.36500  1.000 37.63585 ? 149 ARG   B CB    1 
ATOM   2591 C  CG    . ARG   B 1 150 ? -29.58600 44.86700 -5.45100  1.000 42.20779 ? 149 ARG   B CG    1 
ATOM   2592 C  CD    . ARG   B 1 150 ? -30.11100 45.22400 -6.82900  1.000 43.01513 ? 149 ARG   B CD    1 
ATOM   2593 N  NE    . ARG   B 1 150 ? -29.64900 44.27100 -7.83100  1.000 44.93101 ? 149 ARG   B NE    1 
ATOM   2594 C  CZ    . ARG   B 1 150 ? -28.43900 44.28900 -8.37200  1.000 46.54278 ? 149 ARG   B CZ    1 
ATOM   2595 N  NH1   . ARG   B 1 150 ? -27.53800 45.19200 -8.02000  1.000 47.10857 ? 149 ARG   B NH1   1 
ATOM   2596 N  NH2   . ARG   B 1 150 ? -28.12300 43.37800 -9.28800  1.000 47.15857 ? 149 ARG   B NH2   1 
ATOM   2597 N  N     . GLN   B 1 151 ? -28.30900 46.73900 -1.40400  1.000 35.21577 ? 150 GLN   B N     1 
ATOM   2598 C  CA    . GLN   B 1 151 ? -27.10700 47.45600 -0.99800  1.000 37.43435 ? 150 GLN   B CA    1 
ATOM   2599 C  C     . GLN   B 1 151 ? -25.90300 46.52300 -0.96700  1.000 33.66835 ? 150 GLN   B C     1 
ATOM   2600 O  O     . GLN   B 1 151 ? -25.94200 45.45600 -0.35100  1.000 32.41157 ? 150 GLN   B O     1 
ATOM   2601 C  CB    . GLN   B 1 151 ? -27.31300 48.05400 0.39300   1.000 42.71290 ? 150 GLN   B CB    1 
ATOM   2602 C  CG    . GLN   B 1 151 ? -26.01800 48.50700 1.04800   1.000 51.47248 ? 150 GLN   B CG    1 
ATOM   2603 C  CD    . GLN   B 1 151 ? -26.19100 48.88300 2.50600   1.000 59.21153 ? 150 GLN   B CD    1 
ATOM   2604 O  OE1   . GLN   B 1 151 ? -27.31100 49.06400 2.98700   1.000 60.34404 ? 150 GLN   B OE1   1 
ATOM   2605 N  NE2   . GLN   B 1 151 ? -25.07600 48.99800 3.22100   1.000 61.69719 ? 150 GLN   B NE2   1 
ATOM   2606 N  N     . GLY   B 1 152 ? -24.83200 46.92600 -1.64700  1.000 31.63824 ? 151 GLY   B N     1 
ATOM   2607 C  CA    . GLY   B 1 152 ? -23.57400 46.21100 -1.60300  1.000 29.30196 ? 151 GLY   B CA    1 
ATOM   2608 C  C     . GLY   B 1 152 ? -23.51500 44.92500 -2.39600  1.000 29.03829 ? 151 GLY   B C     1 
ATOM   2609 O  O     . GLY   B 1 152 ? -22.46500 44.27400 -2.39500  1.000 28.70043 ? 151 GLY   B O     1 
ATOM   2610 N  N     . VAL   B 1 153 ? -24.59900 44.52500 -3.06300  1.000 26.85472 ? 152 VAL   B N     1 
ATOM   2611 C  CA    . VAL   B 1 153 ? -24.61000 43.23200 -3.74900  1.000 26.34025 ? 152 VAL   B CA    1 
ATOM   2612 C  C     . VAL   B 1 153 ? -23.58100 43.21500 -4.87900  1.000 23.23264 ? 152 VAL   B C     1 
ATOM   2613 O  O     . VAL   B 1 153 ? -22.70100 42.34300 -4.93000  1.000 22.84039 ? 152 VAL   B O     1 
ATOM   2614 C  CB    . VAL   B 1 153 ? -26.02600 42.88900 -4.24300  1.000 28.26908 ? 152 VAL   B CB    1 
ATOM   2615 C  CG1   . VAL   B 1 153 ? -26.00600 41.61800 -5.07000  1.000 30.22750 ? 152 VAL   B CG1   1 
ATOM   2616 C  CG2   . VAL   B 1 153 ? -26.97300 42.72800 -3.06500  1.000 28.75106 ? 152 VAL   B CG2   1 
ATOM   2617 N  N     . ASP   B 1 154 ? -23.67000 44.17900 -5.80200  1.000 26.29622 ? 153 ASP   B N     1 
ATOM   2618 C  CA    . ASP   B 1 154 ? -22.67300 44.23400 -6.86700  1.000 26.23124 ? 153 ASP   B CA    1 
ATOM   2619 C  C     . ASP   B 1 154 ? -21.27500 44.37800 -6.28700  1.000 26.02767 ? 153 ASP   B C     1 
ATOM   2620 O  O     . ASP   B 1 154 ? -20.33400 43.71000 -6.73500  1.000 25.20370 ? 153 ASP   B O     1 
ATOM   2621 C  CB    . ASP   B 1 154 ? -22.96400 45.38900 -7.82900  1.000 27.27719 ? 153 ASP   B CB    1 
ATOM   2622 C  CG    . ASP   B 1 154 ? -24.19600 45.15600 -8.68300  1.000 30.14950 ? 153 ASP   B CG    1 
ATOM   2623 O  OD1   . ASP   B 1 154 ? -24.61200 43.99500 -8.85700  1.000 33.06617 ? 153 ASP   B OD1   1 
ATOM   2624 O  OD2   . ASP   B 1 154 ? -24.73900 46.14700 -9.20700  1.000 35.36457 ? 153 ASP   B OD2   1 
ATOM   2625 N  N     . ASP   B 1 155 ? -21.12500 45.23500 -5.27500  1.000 25.69496 ? 154 ASP   B N     1 
ATOM   2626 C  CA    . ASP   B 1 155 ? -19.81300 45.44900 -4.67700  1.000 27.58003 ? 154 ASP   B CA    1 
ATOM   2627 C  C     . ASP   B 1 155 ? -19.21800 44.14400 -4.16400  1.000 23.32143 ? 154 ASP   B C     1 
ATOM   2628 O  O     . ASP   B 1 155 ? -18.02200 43.89600 -4.32900  1.000 22.39994 ? 154 ASP   B O     1 
ATOM   2629 C  CB    . ASP   B 1 155 ? -19.89500 46.47400 -3.54400  1.000 34.16841 ? 154 ASP   B CB    1 
ATOM   2630 C  CG    . ASP   B 1 155 ? -20.10800 47.89600 -4.03300  1.000 47.67804 ? 154 ASP   B CG    1 
ATOM   2631 O  OD1   . ASP   B 1 155 ? -19.80400 48.19100 -5.21100  1.000 52.88043 ? 154 ASP   B OD1   1 
ATOM   2632 O  OD2   . ASP   B 1 155 ? -20.56600 48.72700 -3.21600  1.000 52.39095 ? 154 ASP   B OD2   1 
ATOM   2633 N  N     . ALA   B 1 156 ? -20.03800 43.28600 -3.55300  1.000 22.20668 ? 155 ALA   B N     1 
ATOM   2634 C  CA    . ALA   B 1 156 ? -19.51700 42.03600 -3.00800  1.000 23.09987 ? 155 ALA   B CA    1 
ATOM   2635 C  C     . ALA   B 1 156 ? -18.95900 41.14600 -4.11500  1.000 20.27065 ? 155 ALA   B C     1 
ATOM   2636 O  O     . ALA   B 1 156 ? -17.81700 40.67500 -4.04000  1.000 19.71614 ? 155 ALA   B O     1 
ATOM   2637 C  CB    . ALA   B 1 156 ? -20.61900 41.31000 -2.23600  1.000 22.54179 ? 155 ALA   B CB    1 
ATOM   2638 N  N     . PHE   B 1 157 ? -19.74100 40.92800 -5.17200  1.000 20.65290 ? 156 PHE   B N     1 
ATOM   2639 C  CA    . PHE   B 1 157 ? -19.27600 40.05300 -6.24300  1.000 19.52259 ? 156 PHE   B CA    1 
ATOM   2640 C  C     . PHE   B 1 157 ? -18.14700 40.69600 -7.03900  1.000 18.17485 ? 156 PHE   B C     1 
ATOM   2641 O  O     . PHE   B 1 157 ? -17.18400 40.01300 -7.41000  1.000 16.99285 ? 156 PHE   B O     1 
ATOM   2642 C  CB    . PHE   B 1 157 ? -20.44100 39.65900 -7.14700  1.000 19.31593 ? 156 PHE   B CB    1 
ATOM   2643 C  CG    . PHE   B 1 157 ? -21.39000 38.65300 -6.52600  1.000 18.02646 ? 156 PHE   B CG    1 
ATOM   2644 C  CD1   . PHE   B 1 157 ? -21.13600 37.29000 -6.59700  1.000 19.71262 ? 156 PHE   B CD1   1 
ATOM   2645 C  CD2   . PHE   B 1 157 ? -22.52900 39.07600 -5.86300  1.000 19.47620 ? 156 PHE   B CD2   1 
ATOM   2646 C  CE1   . PHE   B 1 157 ? -22.01100 36.37300 -6.03000  1.000 19.60913 ? 156 PHE   B CE1   1 
ATOM   2647 C  CE2   . PHE   B 1 157 ? -23.40600 38.16500 -5.29400  1.000 21.06811 ? 156 PHE   B CE2   1 
ATOM   2648 C  CZ    . PHE   B 1 157 ? -23.15000 36.81600 -5.37400  1.000 19.15969 ? 156 PHE   B CZ    1 
ATOM   2649 N  N     . TYR   B 1 158 ? -18.23400 42.01000 -7.28700  1.000 18.28311 ? 157 TYR   B N     1 
ATOM   2650 C  CA    . TYR   B 1 158 ? -17.19700 42.68500 -8.06600  1.000 18.71042 ? 157 TYR   B CA    1 
ATOM   2651 C  C     . TYR   B 1 158 ? -15.88100 42.73000 -7.30100  1.000 17.43562 ? 157 TYR   B C     1 
ATOM   2652 O  O     . TYR   B 1 158 ? -14.80200 42.57200 -7.89900  1.000 16.38399 ? 157 TYR   B O     1 
ATOM   2653 C  CB    . TYR   B 1 158 ? -17.63100 44.10100 -8.45300  1.000 19.21133 ? 157 TYR   B CB    1 
ATOM   2654 C  CG    . TYR   B 1 158 ? -18.75100 44.19000 -9.46800  1.000 21.56096 ? 157 TYR   B CG    1 
ATOM   2655 C  CD1   . TYR   B 1 158 ? -19.46600 43.06600 -9.87000  1.000 22.56867 ? 157 TYR   B CD1   1 
ATOM   2656 C  CD2   . TYR   B 1 158 ? -19.09100 45.41500 -10.03000 1.000 25.05450 ? 157 TYR   B CD2   1 
ATOM   2657 C  CE1   . TYR   B 1 158 ? -20.48900 43.16500 -10.80200 1.000 24.24771 ? 157 TYR   B CE1   1 
ATOM   2658 C  CE2   . TYR   B 1 158 ? -20.10500 45.51800 -10.95700 1.000 25.67959 ? 157 TYR   B CE2   1 
ATOM   2659 C  CZ    . TYR   B 1 158 ? -20.80200 44.39400 -11.33600 1.000 26.17371 ? 157 TYR   B CZ    1 
ATOM   2660 O  OH    . TYR   B 1 158 ? -21.81000 44.51700 -12.26300 1.000 29.41819 ? 157 TYR   B OH    1 
ATOM   2661 N  N     . THR   B 1 159 ? -15.95000 42.96200 -5.98500  1.000 17.54578 ? 158 THR   B N     1 
ATOM   2662 C  CA    . THR   B 1 159 ? -14.74400 42.92900 -5.16700  1.000 17.93011 ? 158 THR   B CA    1 
ATOM   2663 C  C     . THR   B 1 159 ? -14.09700 41.55400 -5.21300  1.000 15.84981 ? 158 THR   B C     1 
ATOM   2664 O  O     . THR   B 1 159 ? -12.86600 41.44100 -5.29900  1.000 17.94785 ? 158 THR   B O     1 
ATOM   2665 C  CB    . THR   B 1 159 ? -15.06600 43.33900 -3.72900  1.000 20.89220 ? 158 THR   B CB    1 
ATOM   2666 O  OG1   . THR   B 1 159 ? -15.52600 44.69600 -3.71300  1.000 23.01880 ? 158 THR   B OG1   1 
ATOM   2667 C  CG2   . THR   B 1 159 ? -13.83500 43.21200 -2.83200  1.000 23.65709 ? 158 THR   B CG2   1 
ATOM   2668 N  N     . LEU   B 1 160 ? -14.90700 40.49100 -5.22800  1.000 15.91113 ? 159 LEU   B N     1 
ATOM   2669 C  CA    . LEU   B 1 160 ? -14.33200 39.15500 -5.32500  1.000 15.33368 ? 159 LEU   B CA    1 
ATOM   2670 C  C     . LEU   B 1 160 ? -13.62500 38.95800 -6.66500  1.000 16.28908 ? 159 LEU   B C     1 
ATOM   2671 O  O     . LEU   B 1 160 ? -12.53400 38.38200 -6.71300  1.000 15.79451 ? 159 LEU   B O     1 
ATOM   2672 C  CB    . LEU   B 1 160 ? -15.40200 38.08700 -5.08900  1.000 16.16031 ? 159 LEU   B CB    1 
ATOM   2673 C  CG    . LEU   B 1 160 ? -14.92100 36.63300 -5.18900  1.000 14.68624 ? 159 LEU   B CG    1 
ATOM   2674 C  CD1   . LEU   B 1 160 ? -13.81700 36.32900 -4.16900  1.000 16.23901 ? 159 LEU   B CD1   1 
ATOM   2675 C  CD2   . LEU   B 1 160 ? -16.10900 35.72800 -4.95800  1.000 16.26566 ? 159 LEU   B CD2   1 
ATOM   2676 N  N     . VAL   B 1 161 ? -14.22700 39.43400 -7.76200  1.000 15.45828 ? 160 VAL   B N     1 
ATOM   2677 C  CA    . VAL   B 1 161 ? -13.54000 39.39900 -9.05600  1.000 15.69300 ? 160 VAL   B CA    1 
ATOM   2678 C  C     . VAL   B 1 161 ? -12.21700 40.14800 -8.99300  1.000 15.83607 ? 160 VAL   B C     1 
ATOM   2679 O  O     . VAL   B 1 161 ? -11.19200 39.65300 -9.47700  1.000 15.49628 ? 160 VAL   B O     1 
ATOM   2680 C  CB    . VAL   B 1 161 ? -14.45400 39.91000 -10.18200 1.000 16.29102 ? 160 VAL   B CB    1 
ATOM   2681 C  CG1   . VAL   B 1 161 ? -13.64400 40.12600 -11.48800 1.000 15.97594 ? 160 VAL   B CG1   1 
ATOM   2682 C  CG2   . VAL   B 1 161 ? -15.59200 38.93200 -10.41200 1.000 16.29831 ? 160 VAL   B CG2   1 
ATOM   2683 N  N     . ARG   B 1 162 ? -12.21400 41.34000 -8.38500  1.000 14.64282 ? 161 ARG   B N     1 
ATOM   2684 C  CA    . ARG   B 1 162 ? -10.97000 42.09000 -8.22400  1.000 16.64175 ? 161 ARG   B CA    1 
ATOM   2685 C  C     . ARG   B 1 162 ? -9.94000  41.30700 -7.41900  1.000 15.49194 ? 161 ARG   B C     1 
ATOM   2686 O  O     . ARG   B 1 162 ? -8.74900  41.33500 -7.74300  1.000 16.85466 ? 161 ARG   B O     1 
ATOM   2687 C  CB    . ARG   B 1 162 ? -11.23700 43.45700 -7.58500  1.000 17.27372 ? 161 ARG   B CB    1 
ATOM   2688 C  CG    . ARG   B 1 162 ? -12.11400 44.37400 -8.41800  1.000 17.29058 ? 161 ARG   B CG    1 
ATOM   2689 C  CD    . ARG   B 1 162 ? -12.27200 45.75300 -7.80400  1.000 24.24693 ? 161 ARG   B CD    1 
ATOM   2690 N  NE    . ARG   B 1 162 ? -13.20700 46.55400 -8.58400  1.000 23.53353 ? 161 ARG   B NE    1 
ATOM   2691 C  CZ    . ARG   B 1 162 ? -14.45500 46.80800 -8.22700  1.000 25.68135 ? 161 ARG   B CZ    1 
ATOM   2692 N  NH1   . ARG   B 1 162 ? -14.92300 46.45000 -7.03900  1.000 27.85566 ? 161 ARG   B NH1   1 
ATOM   2693 N  NH2   . ARG   B 1 162 ? -15.25800 47.42400 -9.08300  1.000 23.05748 ? 161 ARG   B NH2   1 
ATOM   2694 N  N     . GLU   B 1 163 ? -10.37900 40.58500 -6.37500  1.000 16.04455 ? 162 GLU   B N     1 
ATOM   2695 C  CA    . GLU   B 1 163 ? -9.45300  39.74600 -5.61500  1.000 16.42263 ? 162 GLU   B CA    1 
ATOM   2696 C  C     . GLU   B 1 163 ? -8.84900  38.64000 -6.47500  1.000 15.89100 ? 162 GLU   B C     1 
ATOM   2697 O  O     . GLU   B 1 163 ? -7.65800  38.32800 -6.33700  1.000 16.83482 ? 162 GLU   B O     1 
ATOM   2698 C  CB    . GLU   B 1 163 ? -10.12900 39.15700 -4.37900  1.000 18.12270 ? 162 GLU   B CB    1 
ATOM   2699 C  CG    . GLU   B 1 163 ? -10.43400 40.18700 -3.33700  1.000 20.32491 ? 162 GLU   B CG    1 
ATOM   2700 C  CD    . GLU   B 1 163 ? -9.16900  40.83600 -2.80300  1.000 21.77689 ? 162 GLU   B CD    1 
ATOM   2701 O  OE1   . GLU   B 1 163 ? -8.31800  40.12700 -2.22200  1.000 22.76753 ? 162 GLU   B OE1   1 
ATOM   2702 O  OE2   . GLU   B 1 163 ? -9.00800  42.05700 -2.99200  1.000 25.17543 ? 162 GLU   B OE2   1 
ATOM   2703 N  N     . ILE   B 1 164 ? -9.65300  38.03000 -7.36100  1.000 15.45868 ? 163 ILE   B N     1 
ATOM   2704 C  CA    . ILE   B 1 164 ? -9.10700  37.04300 -8.29300  1.000 15.53543 ? 163 ILE   B CA    1 
ATOM   2705 C  C     . ILE   B 1 164 ? -8.09900  37.69200 -9.23500  1.000 14.83359 ? 163 ILE   B C     1 
ATOM   2706 O  O     . ILE   B 1 164 ? -6.98700  37.18600 -9.41400  1.000 16.24972 ? 163 ILE   B O     1 
ATOM   2707 C  CB    . ILE   B 1 164 ? -10.22500 36.30900 -9.06100  1.000 14.95586 ? 163 ILE   B CB    1 
ATOM   2708 C  CG1   . ILE   B 1 164 ? -11.13900 35.55400 -8.09300  1.000 15.48570 ? 163 ILE   B CG1   1 
ATOM   2709 C  CG2   . ILE   B 1 164 ? -9.62300  35.39500 -10.12200 1.000 15.46541 ? 163 ILE   B CG2   1 
ATOM   2710 C  CD1   . ILE   B 1 164 ? -12.38000 35.01200 -8.76000  1.000 15.84943 ? 163 ILE   B CD1   1 
ATOM   2711 N  N     . ARG   B 1 165 ? -8.47200  38.83100 -9.83300  1.000 15.55261 ? 164 ARG   B N     1 
ATOM   2712 C  CA    . ARG   B 1 165 ? -7.56900  39.53300 -10.74400 1.000 16.77282 ? 164 ARG   B CA    1 
ATOM   2713 C  C     . ARG   B 1 165 ? -6.27400  39.92300 -10.04000 1.000 16.65890 ? 164 ARG   B C     1 
ATOM   2714 O  O     . ARG   B 1 165 ? -5.18600  39.75500 -10.59700 1.000 18.09997 ? 164 ARG   B O     1 
ATOM   2715 C  CB    . ARG   B 1 165 ? -8.27300  40.75900 -11.33000 1.000 16.17328 ? 164 ARG   B CB    1 
ATOM   2716 C  CG    . ARG   B 1 165 ? -9.41500  40.40300 -12.28700 1.000 15.96180 ? 164 ARG   B CG    1 
ATOM   2717 C  CD    . ARG   B 1 165 ? -10.21100 41.61700 -12.73900 1.000 16.41273 ? 164 ARG   B CD    1 
ATOM   2718 N  NE    . ARG   B 1 165 ? -11.19300 41.24400 -13.75600 1.000 16.79403 ? 164 ARG   B NE    1 
ATOM   2719 C  CZ    . ARG   B 1 165 ? -12.14700 42.04400 -14.21500 1.000 17.00536 ? 164 ARG   B CZ    1 
ATOM   2720 N  NH1   . ARG   B 1 165 ? -12.29100 43.27400 -13.76200 1.000 18.79342 ? 164 ARG   B NH1   1 
ATOM   2721 N  NH2   . ARG   B 1 165 ? -12.97100 41.59600 -15.15800 1.000 17.42733 ? 164 ARG   B NH2   1 
ATOM   2722 N  N     . LYS   B 1 166 ? -6.37000  40.42500 -8.80600  1.000 17.73369 ? 165 LYS   B N     1 
ATOM   2723 C  CA    . LYS   B 1 166 ? -5.17400  40.75800 -8.03400  1.000 18.82788 ? 165 LYS   B CA    1 
ATOM   2724 C  C     . LYS   B 1 166 ? -4.31400  39.52400 -7.80400  1.000 17.66193 ? 165 LYS   B C     1 
ATOM   2725 O  O     . LYS   B 1 166 ? -3.08700  39.57700 -7.95200  1.000 19.82550 ? 165 LYS   B O     1 
ATOM   2726 C  CB    . LYS   B 1 166 ? -5.57700  41.38100 -6.69500  1.000 21.85163 ? 165 LYS   B CB    1 
ATOM   2727 C  CG    . LYS   B 1 166 ? -4.43200  41.57500 -5.70600  1.000 29.96822 ? 165 LYS   B CG    1 
ATOM   2728 C  CD    . LYS   B 1 166 ? -4.94200  41.89700 -4.29700  1.000 37.17536 ? 165 LYS   B CD    1 
ATOM   2729 C  CE    . LYS   B 1 166 ? -5.77800  43.16600 -4.27100  1.000 41.03143 ? 165 LYS   B CE    1 
ATOM   2730 N  NZ    . LYS   B 1 166 ? -6.35700  43.42900 -2.91900  1.000 44.14165 ? 165 LYS   B NZ    1 
ATOM   2731 N  N     . HIS   B 1 167 ? -4.94600  38.40200 -7.46100  1.000 16.96211 ? 166 HIS   B N     1 
ATOM   2732 C  CA    . HIS   B 1 167 ? -4.22000  37.16200 -7.21500  1.000 18.37195 ? 166 HIS   B CA    1 
ATOM   2733 C  C     . HIS   B 1 167 ? -3.49200  36.68600 -8.46600  1.000 19.62383 ? 166 HIS   B C     1 
ATOM   2734 O  O     . HIS   B 1 167 ? -2.32700  36.28000 -8.39600  1.000 23.11149 ? 166 HIS   B O     1 
ATOM   2735 C  CB    . HIS   B 1 167 ? -5.20400  36.10100 -6.72500  1.000 20.89109 ? 166 HIS   B CB    1 
ATOM   2736 C  CG    . HIS   B 1 167 ? -4.57100  34.79100 -6.39000  1.000 24.40885 ? 166 HIS   B CG    1 
ATOM   2737 N  ND1   . HIS   B 1 167 ? -4.71600  33.67000 -7.17800  1.000 29.53966 ? 166 HIS   B ND1   1 
ATOM   2738 C  CD2   . HIS   B 1 167 ? -3.80600  34.41700 -5.33900  1.000 29.49428 ? 166 HIS   B CD2   1 
ATOM   2739 C  CE1   . HIS   B 1 167 ? -4.05500  32.66400 -6.63300  1.000 31.70106 ? 166 HIS   B CE1   1 
ATOM   2740 N  NE2   . HIS   B 1 167 ? -3.49500  33.09100 -5.51600  1.000 32.86508 ? 166 HIS   B NE2   1 
ATOM   2741 N  N     . LYS   B 1 168 ? -4.15700  36.74400 -9.62800  1.000 18.28773 ? 167 LYS   B N     1 
ATOM   2742 C  CA    A LYS   B 1 168 ? -3.54000  36.27100 -10.86100 0.500 19.15927 ? 167 LYS   B CA    1 
ATOM   2743 C  CA    B LYS   B 1 168 ? -3.55400  36.28300 -10.87500 0.500 20.68383 ? 167 LYS   B CA    1 
ATOM   2744 C  C     . LYS   B 1 168 ? -2.41000  37.17900 -11.31500 1.000 21.37881 ? 167 LYS   B C     1 
ATOM   2745 O  O     . LYS   B 1 168 ? -1.52500  36.72900 -12.05000 1.000 21.87577 ? 167 LYS   B O     1 
ATOM   2746 C  CB    A LYS   B 1 168 ? -4.59000  36.12500 -11.96600 0.500 16.97442 ? 167 LYS   B CB    1 
ATOM   2747 C  CB    B LYS   B 1 168 ? -4.59400  36.26700 -11.99000 0.500 21.61981 ? 167 LYS   B CB    1 
ATOM   2748 C  CG    A LYS   B 1 168 ? -5.64200  35.04800 -11.69000 0.500 17.56934 ? 167 LYS   B CG    1 
ATOM   2749 C  CG    B LYS   B 1 168 ? -5.58900  35.12200 -11.97000 0.500 23.71801 ? 167 LYS   B CG    1 
ATOM   2750 C  CD    A LYS   B 1 168 ? -6.45000  34.71900 -12.94300 0.500 19.34803 ? 167 LYS   B CD    1 
ATOM   2751 C  CD    B LYS   B 1 168 ? -6.41900  35.21800 -13.23200 0.500 26.41433 ? 167 LYS   B CD    1 
ATOM   2752 C  CE    A LYS   B 1 168 ? -5.54000  34.19100 -14.05900 0.500 20.96382 ? 167 LYS   B CE    1 
ATOM   2753 C  CE    B LYS   B 1 168 ? -7.59000  34.26800 -13.27800 0.500 28.53089 ? 167 LYS   B CE    1 
ATOM   2754 N  NZ    A LYS   B 1 168 ? -6.24400  33.56800 -15.22700 0.500 21.88416 ? 167 LYS   B NZ    1 
ATOM   2755 N  NZ    B LYS   B 1 168 ? -8.28500  34.42100 -14.59600 0.500 29.54156 ? 167 LYS   B NZ    1 
ATOM   2756 N  N     . GLU   B 1 169 ? -2.42400  38.44700 -10.90800 1.000 24.29276 ? 168 GLU   B N     1 
ATOM   2757 C  CA    . GLU   B 1 169 ? -1.37700  39.36500 -11.31700 1.000 31.00671 ? 168 GLU   B CA    1 
ATOM   2758 C  C     . GLU   B 1 169 ? -0.07300  39.11000 -10.57800 1.000 35.02915 ? 168 GLU   B C     1 
ATOM   2759 O  O     . GLU   B 1 169 ? 0.99100   39.50600 -11.06700 1.000 38.76357 ? 168 GLU   B O     1 
ATOM   2760 C  CB    . GLU   B 1 169 ? -1.84500  40.80500 -11.10200 1.000 37.54484 ? 168 GLU   B CB    1 
ATOM   2761 C  CG    . GLU   B 1 169 ? -1.22000  41.81000 -12.05400 1.000 47.14237 ? 168 GLU   B CG    1 
ATOM   2762 C  CD    . GLU   B 1 169 ? -1.85200  43.18000 -11.93300 1.000 53.85823 ? 168 GLU   B CD    1 
ATOM   2763 O  OE1   . GLU   B 1 169 ? -2.08100  43.62600 -10.79000 1.000 55.26282 ? 168 GLU   B OE1   1 
ATOM   2764 O  OE2   . GLU   B 1 169 ? -2.13500  43.80300 -12.98000 1.000 56.98168 ? 168 GLU   B OE2   1 
ATOM   2765 N  N     . LYS   B 1 170 ? -0.12800  38.43800 -9.43200  1.000 37.45992 ? 169 LYS   B N     1 
ATOM   2766 C  CA    . LYS   B 1 170 ? 1.06100   38.22500 -8.60800  1.000 43.37022 ? 169 LYS   B CA    1 
ATOM   2767 C  C     . LYS   B 1 170 ? 2.07900   37.31100 -9.29600  1.000 44.58129 ? 169 LYS   B C     1 
ATOM   2768 O  O     . LYS   B 1 170 ? 1.72200   36.45800 -10.11300 1.000 44.80266 ? 169 LYS   B O     1 
ATOM   2769 C  CB    . LYS   B 1 170 ? 0.66100   37.65800 -7.24200  1.000 48.37339 ? 169 LYS   B CB    1 
ATOM   2770 C  CG    . LYS   B 1 170 ? 1.35700   38.32300 -6.06100  1.000 53.44362 ? 169 LYS   B CG    1 
ATOM   2771 C  CD    . LYS   B 1 170 ? 0.61400   38.06500 -4.75600  1.000 56.69227 ? 169 LYS   B CD    1 
ATOM   2772 C  CE    . LYS   B 1 170 ? 1.42900   38.51100 -3.54300  1.000 58.92828 ? 169 LYS   B CE    1 
ATOM   2773 N  NZ    . LYS   B 1 170 ? 1.77100   39.96600 -3.55900  1.000 59.94151 ? 169 LYS   B NZ    1 
ATOM   2774 O  OXT   . LYS   B 1 170 ? 3.28900   37.40500 -9.05200  1.000 44.70497 ? 169 LYS   B OXT   1 
ATOM   2775 N  N     . MET   C 2 2   ? -48.80800 55.88900 -50.53700 1.000 61.69936 ? 1   MET   D N     1 
ATOM   2776 C  CA    . MET   C 2 2   ? -49.74600 55.59100 -49.46100 1.000 61.88575 ? 1   MET   D CA    1 
ATOM   2777 C  C     . MET   C 2 2   ? -49.02900 55.55000 -48.10600 1.000 59.10056 ? 1   MET   D C     1 
ATOM   2778 O  O     . MET   C 2 2   ? -47.80300 55.43800 -48.04100 1.000 59.05131 ? 1   MET   D O     1 
ATOM   2779 C  CB    . MET   C 2 2   ? -50.47200 54.27000 -49.73400 1.000 64.35086 ? 1   MET   D CB    1 
ATOM   2780 C  CG    . MET   C 2 2   ? -51.81400 54.11000 -49.02200 1.000 66.80271 ? 1   MET   D CG    1 
ATOM   2781 S  SD    . MET   C 2 2   ? -53.17700 54.98200 -49.82700 1.000 70.15958 ? 1   MET   D SD    1 
ATOM   2782 C  CE    . MET   C 2 2   ? -53.09800 56.59700 -49.04900 1.000 70.63208 ? 1   MET   D CE    1 
ATOM   2783 N  N     . VAL   C 2 3   ? -49.80300 55.63600 -47.03000 1.000 54.47219 ? 2   VAL   D N     1 
ATOM   2784 C  CA    . VAL   C 2 3   ? -49.26700 55.77300 -45.68100 1.000 49.41086 ? 2   VAL   D CA    1 
ATOM   2785 C  C     . VAL   C 2 3   ? -48.92200 54.40000 -45.11500 1.000 42.28820 ? 2   VAL   D C     1 
ATOM   2786 O  O     . VAL   C 2 3   ? -49.58400 53.39700 -45.40800 1.000 41.63113 ? 2   VAL   D O     1 
ATOM   2787 C  CB    . VAL   C 2 3   ? -50.25700 56.55200 -44.78700 1.000 51.42087 ? 2   VAL   D CB    1 
ATOM   2788 C  CG1   . VAL   C 2 3   ? -51.48500 55.70700 -44.46800 1.000 51.87999 ? 2   VAL   D CG1   1 
ATOM   2789 C  CG2   . VAL   C 2 3   ? -49.57800 57.03700 -43.52200 1.000 52.32292 ? 2   VAL   D CG2   1 
ATOM   2790 N  N     . ASN   C 2 4   ? -47.86100 54.35700 -44.30300 1.000 35.79721 ? 3   ASN   D N     1 
ATOM   2791 C  CA    . ASN   C 2 4   ? -47.40800 53.10200 -43.70900 1.000 31.42033 ? 3   ASN   D CA    1 
ATOM   2792 C  C     . ASN   C 2 4   ? -48.47900 52.54300 -42.77800 1.000 29.92403 ? 3   ASN   D C     1 
ATOM   2793 O  O     . ASN   C 2 4   ? -49.03100 53.28700 -41.95500 1.000 31.15865 ? 3   ASN   D O     1 
ATOM   2794 C  CB    . ASN   C 2 4   ? -46.12400 53.31000 -42.90500 1.000 26.94096 ? 3   ASN   D CB    1 
ATOM   2795 C  CG    . ASN   C 2 4   ? -44.88700 53.39400 -43.77500 1.000 28.89657 ? 3   ASN   D CG    1 
ATOM   2796 O  OD1   . ASN   C 2 4   ? -44.88900 52.96900 -44.93200 1.000 27.34753 ? 3   ASN   D OD1   1 
ATOM   2797 N  ND2   . ASN   C 2 4   ? -43.81100 53.93500 -43.21100 1.000 26.94758 ? 3   ASN   D ND2   1 
ATOM   2798 N  N     . PRO   C 2 5   ? -48.78100 51.25500 -42.85300 1.000 26.27134 ? 4   PRO   D N     1 
ATOM   2799 C  CA    . PRO   C 2 5   ? -49.81600 50.70700 -41.97700 1.000 24.12028 ? 4   PRO   D CA    1 
ATOM   2800 C  C     . PRO   C 2 5   ? -49.33400 50.58600 -40.54200 1.000 20.25577 ? 4   PRO   D C     1 
ATOM   2801 O  O     . PRO   C 2 5   ? -48.13400 50.50200 -40.26400 1.000 20.72985 ? 4   PRO   D O     1 
ATOM   2802 C  CB    . PRO   C 2 5   ? -50.11000 49.33300 -42.58700 1.000 26.09970 ? 4   PRO   D CB    1 
ATOM   2803 C  CG    . PRO   C 2 5   ? -48.89900 48.96700 -43.32700 1.000 25.63447 ? 4   PRO   D CG    1 
ATOM   2804 C  CD    . PRO   C 2 5   ? -48.19600 50.23100 -43.73700 1.000 25.15369 ? 4   PRO   D CD    1 
ATOM   2805 N  N     . THR   C 2 6   ? -50.29700 50.60600 -39.62700 1.000 20.62953 ? 5   THR   D N     1 
ATOM   2806 C  CA    A THR   C 2 6   ? -50.06200 50.40200 -38.20300 0.500 20.66846 ? 5   THR   D CA    1 
ATOM   2807 C  CA    B THR   C 2 6   ? -50.03900 50.38700 -38.21400 0.500 22.31338 ? 5   THR   D CA    1 
ATOM   2808 C  C     . THR   C 2 6   ? -50.81100 49.15100 -37.77500 1.000 19.08604 ? 5   THR   D C     1 
ATOM   2809 O  O     . THR   C 2 6   ? -51.97000 48.96900 -38.14800 1.000 19.61240 ? 5   THR   D O     1 
ATOM   2810 C  CB    A THR   C 2 6   ? -50.59300 51.58400 -37.37500 0.500 21.51070 ? 5   THR   D CB    1 
ATOM   2811 C  CB    B THR   C 2 6   ? -50.45300 51.60400 -37.36700 0.500 26.38338 ? 5   THR   D CB    1 
ATOM   2812 O  OG1   A THR   C 2 6   ? -50.01100 52.81300 -37.82600 0.500 25.70961 ? 5   THR   D OG1   1 
ATOM   2813 O  OG1   B THR   C 2 6   ? -51.85800 51.83800 -37.50200 0.500 28.28368 ? 5   THR   D OG1   1 
ATOM   2814 C  CG2   A THR   C 2 6   ? -50.28300 51.38800 -35.89400 0.500 20.31703 ? 5   THR   D CG2   1 
ATOM   2815 C  CG2   B THR   C 2 6   ? -49.70800 52.85500 -37.81500 0.500 29.69358 ? 5   THR   D CG2   1 
ATOM   2816 N  N     . VAL   C 2 7   ? -50.15400 48.28900 -36.99800 1.000 17.85462 ? 6   VAL   D N     1 
ATOM   2817 C  CA    . VAL   C 2 7   ? -50.80400 47.09900 -36.46400 1.000 17.77395 ? 6   VAL   D CA    1 
ATOM   2818 C  C     . VAL   C 2 7   ? -50.58900 47.07000 -34.95900 1.000 16.40632 ? 6   VAL   D C     1 
ATOM   2819 O  O     . VAL   C 2 7   ? -49.70800 47.74200 -34.41800 1.000 17.77157 ? 6   VAL   D O     1 
ATOM   2820 C  CB    . VAL   C 2 7   ? -50.36100 45.77000 -37.12800 1.000 19.91981 ? 6   VAL   D CB    1 
ATOM   2821 C  CG1   . VAL   C 2 7   ? -50.74100 45.73500 -38.60000 1.000 20.54549 ? 6   VAL   D CG1   1 
ATOM   2822 C  CG2   . VAL   C 2 7   ? -48.88900 45.58000 -36.97100 1.000 19.00070 ? 6   VAL   D CG2   1 
ATOM   2823 N  N     . PHE   C 2 8   ? -51.43500 46.31100 -34.27700 1.000 17.73474 ? 7   PHE   D N     1 
ATOM   2824 C  CA    . PHE   C 2 8   ? -51.36500 46.20400 -32.82900 1.000 18.12050 ? 7   PHE   D CA    1 
ATOM   2825 C  C     . PHE   C 2 8   ? -51.35300 44.74700 -32.39400 1.000 15.39983 ? 7   PHE   D C     1 
ATOM   2826 O  O     . PHE   C 2 8   ? -51.92700 43.87500 -33.05700 1.000 15.09770 ? 7   PHE   D O     1 
ATOM   2827 C  CB    . PHE   C 2 8   ? -52.53800 46.92000 -32.12700 1.000 19.49504 ? 7   PHE   D CB    1 
ATOM   2828 C  CG    . PHE   C 2 8   ? -53.85600 46.18300 -32.21700 1.000 19.33371 ? 7   PHE   D CG    1 
ATOM   2829 C  CD1   . PHE   C 2 8   ? -54.71500 46.38700 -33.28600 1.000 21.22706 ? 7   PHE   D CD1   1 
ATOM   2830 C  CD2   . PHE   C 2 8   ? -54.22500 45.26700 -31.23500 1.000 21.16576 ? 7   PHE   D CD2   1 
ATOM   2831 C  CE1   . PHE   C 2 8   ? -55.92600 45.70200 -33.36900 1.000 22.46066 ? 7   PHE   D CE1   1 
ATOM   2832 C  CE2   . PHE   C 2 8   ? -55.42000 44.57700 -31.31500 1.000 21.89394 ? 7   PHE   D CE2   1 
ATOM   2833 C  CZ    . PHE   C 2 8   ? -56.27800 44.80200 -32.38100 1.000 21.75111 ? 7   PHE   D CZ    1 
ATOM   2834 N  N     . PHE   C 2 9   ? -50.69400 44.51000 -31.25700 1.000 15.30972 ? 8   PHE   D N     1 
ATOM   2835 C  CA    . PHE   C 2 9   ? -50.78000 43.26800 -30.50200 1.000 14.00063 ? 8   PHE   D CA    1 
ATOM   2836 C  C     . PHE   C 2 9   ? -51.27900 43.61800 -29.10500 1.000 15.11042 ? 8   PHE   D C     1 
ATOM   2837 O  O     . PHE   C 2 9   ? -50.72200 44.51300 -28.45000 1.000 16.55968 ? 8   PHE   D O     1 
ATOM   2838 C  CB    . PHE   C 2 9   ? -49.38800 42.67200 -30.25400 1.000 14.13851 ? 8   PHE   D CB    1 
ATOM   2839 C  CG    . PHE   C 2 9   ? -48.69700 42.07700 -31.45700 1.000 14.44448 ? 8   PHE   D CG    1 
ATOM   2840 C  CD1   . PHE   C 2 9   ? -49.31900 41.93200 -32.68300 1.000 15.50531 ? 8   PHE   D CD1   1 
ATOM   2841 C  CD2   . PHE   C 2 9   ? -47.39000 41.62800 -31.31400 1.000 14.91332 ? 8   PHE   D CD2   1 
ATOM   2842 C  CE1   . PHE   C 2 9   ? -48.64900 41.36900 -33.76800 1.000 15.51085 ? 8   PHE   D CE1   1 
ATOM   2843 C  CE2   . PHE   C 2 9   ? -46.71100 41.07000 -32.37800 1.000 14.99986 ? 8   PHE   D CE2   1 
ATOM   2844 C  CZ    . PHE   C 2 9   ? -47.34400 40.92700 -33.61000 1.000 15.52492 ? 8   PHE   D CZ    1 
ATOM   2845 N  N     . ASP   C 2 10  ? -52.29600 42.90100 -28.63200 1.000 14.99208 ? 9   ASP   D N     1 
ATOM   2846 C  CA    . ASP   C 2 10  ? -52.66100 42.92200 -27.21600 1.000 17.22609 ? 9   ASP   D CA    1 
ATOM   2847 C  C     . ASP   C 2 10  ? -51.96000 41.75300 -26.53700 1.000 15.49772 ? 9   ASP   D C     1 
ATOM   2848 O  O     . ASP   C 2 10  ? -52.23800 40.59100 -26.84100 1.000 16.00287 ? 9   ASP   D O     1 
ATOM   2849 C  CB    . ASP   C 2 10  ? -54.17600 42.84500 -27.03700 1.000 17.54831 ? 9   ASP   D CB    1 
ATOM   2850 C  CG    . ASP   C 2 10  ? -54.86800 44.13000 -27.43300 1.000 21.56054 ? 9   ASP   D CG    1 
ATOM   2851 O  OD1   . ASP   C 2 10  ? -54.29900 45.23000 -27.19200 1.000 23.90114 ? 9   ASP   D OD1   1 
ATOM   2852 O  OD2   . ASP   C 2 10  ? -55.98500 44.03600 -27.97200 1.000 25.78364 ? 9   ASP   D OD2   1 
ATOM   2853 N  N     . ILE   C 2 11  ? -51.02700 42.06200 -25.64700 1.000 14.29830 ? 10  ILE   D N     1 
ATOM   2854 C  CA    . ILE   C 2 11  ? -50.16800 41.06400 -25.02400 1.000 14.37739 ? 10  ILE   D CA    1 
ATOM   2855 C  C     . ILE   C 2 11  ? -50.82500 40.59800 -23.74000 1.000 14.11550 ? 10  ILE   D C     1 
ATOM   2856 O  O     . ILE   C 2 11  ? -51.33000 41.41600 -22.95900 1.000 16.33675 ? 10  ILE   D O     1 
ATOM   2857 C  CB    . ILE   C 2 11  ? -48.79000 41.67900 -24.72200 1.000 14.90725 ? 10  ILE   D CB    1 
ATOM   2858 C  CG1   . ILE   C 2 11  ? -48.13500 42.19300 -26.00700 1.000 15.39441 ? 10  ILE   D CG1   1 
ATOM   2859 C  CG2   . ILE   C 2 11  ? -47.89300 40.65700 -24.01200 1.000 16.24616 ? 10  ILE   D CG2   1 
ATOM   2860 C  CD1   . ILE   C 2 11  ? -47.83300 41.12100 -27.00900 1.000 15.96425 ? 10  ILE   D CD1   1 
ATOM   2861 N  N     . ALA   C 2 12  ? -50.76300 39.29100 -23.49200 1.000 13.82267 ? 11  ALA   D N     1 
ATOM   2862 C  CA    . ALA   C 2 12  ? -51.27800 38.70900 -22.26400 1.000 13.67290 ? 11  ALA   D CA    1 
ATOM   2863 C  C     . ALA   C 2 12  ? -50.20600 37.85900 -21.59700 1.000 14.50338 ? 11  ALA   D C     1 
ATOM   2864 O  O     . ALA   C 2 12  ? -49.29800 37.32900 -22.25100 1.000 15.21563 ? 11  ALA   D O     1 
ATOM   2865 C  CB    . ALA   C 2 12  ? -52.52000 37.85500 -22.54600 1.000 16.77015 ? 11  ALA   D CB    1 
ATOM   2866 N  N     . VAL   C 2 13  ? -50.31700 37.74600 -20.27600 1.000 15.16234 ? 12  VAL   D N     1 
ATOM   2867 C  CA    . VAL   C 2 13  ? -49.40100 36.96800 -19.45400 1.000 15.42045 ? 12  VAL   D CA    1 
ATOM   2868 C  C     . VAL   C 2 13  ? -50.25400 35.93000 -18.74900 1.000 16.21288 ? 12  VAL   D C     1 
ATOM   2869 O  O     . VAL   C 2 13  ? -51.08900 36.28500 -17.90800 1.000 16.04994 ? 12  VAL   D O     1 
ATOM   2870 C  CB    . VAL   C 2 13  ? -48.67800 37.85500 -18.42900 1.000 16.73189 ? 12  VAL   D CB    1 
ATOM   2871 C  CG1   . VAL   C 2 13  ? -47.80600 37.03300 -17.50100 1.000 16.40469 ? 12  VAL   D CG1   1 
ATOM   2872 C  CG2   . VAL   C 2 13  ? -47.87600 38.93400 -19.11700 1.000 17.96647 ? 12  VAL   D CG2   1 
ATOM   2873 N  N     . ASP   C 2 14  ? -50.06700 34.65200 -19.09200 1.000 16.53232 ? 13  ASP   D N     1 
ATOM   2874 C  CA    . ASP   C 2 14  ? -50.96000 33.59700 -18.61700 1.000 17.79441 ? 13  ASP   D CA    1 
ATOM   2875 C  C     . ASP   C 2 14  ? -52.42600 33.99900 -18.78100 1.000 16.81360 ? 13  ASP   D C     1 
ATOM   2876 O  O     . ASP   C 2 14  ? -53.25700 33.73800 -17.91200 1.000 20.51455 ? 13  ASP   D O     1 
ATOM   2877 C  CB    . ASP   C 2 14  ? -50.64900 33.18200 -17.17300 1.000 20.13545 ? 13  ASP   D CB    1 
ATOM   2878 C  CG    . ASP   C 2 14  ? -49.31200 32.46800 -17.03400 1.000 22.09371 ? 13  ASP   D CG    1 
ATOM   2879 O  OD1   . ASP   C 2 14  ? -48.80600 31.91400 -18.03500 1.000 23.53609 ? 13  ASP   D OD1   1 
ATOM   2880 O  OD2   . ASP   C 2 14  ? -48.76800 32.46100 -15.91100 1.000 23.20772 ? 13  ASP   D OD2   1 
ATOM   2881 N  N     . GLY   C 2 15  ? -52.75000 34.63400 -19.90900 1.000 16.24864 ? 14  GLY   D N     1 
ATOM   2882 C  CA    . GLY   C 2 15  ? -54.11300 35.02200 -20.21700 1.000 17.56693 ? 14  GLY   D CA    1 
ATOM   2883 C  C     . GLY   C 2 15  ? -54.55700 36.37400 -19.68300 1.000 17.70229 ? 14  GLY   D C     1 
ATOM   2884 O  O     . GLY   C 2 15  ? -55.59900 36.87400 -20.12500 1.000 19.70634 ? 14  GLY   D O     1 
ATOM   2885 N  N     . GLU   C 2 16  ? -53.80700 36.98900 -18.73900 1.000 16.30237 ? 15  GLU   D N     1 
ATOM   2886 C  CA    . GLU   C 2 16  ? -54.21900 38.28700 -18.18900 1.000 15.99756 ? 15  GLU   D CA    1 
ATOM   2887 C  C     . GLU   C 2 16  ? -53.64800 39.41200 -19.03700 1.000 16.06985 ? 15  GLU   D C     1 
ATOM   2888 O  O     . GLU   C 2 16  ? -52.46200 39.37900 -19.36200 1.000 15.63230 ? 15  GLU   D O     1 
ATOM   2889 C  CB    . GLU   C 2 16  ? -53.72100 38.45800 -16.76600 1.000 15.30936 ? 15  GLU   D CB    1 
ATOM   2890 C  CG    . GLU   C 2 16  ? -54.47600 37.63800 -15.74800 1.000 17.69627 ? 15  GLU   D CG    1 
ATOM   2891 C  CD    . GLU   C 2 16  ? -55.91500 38.13000 -15.53600 1.000 18.70865 ? 15  GLU   D CD    1 
ATOM   2892 O  OE1   . GLU   C 2 16  ? -56.24900 39.29500 -15.88000 1.000 21.71890 ? 15  GLU   D OE1   1 
ATOM   2893 O  OE2   . GLU   C 2 16  ? -56.72200 37.34300 -15.04000 1.000 19.00949 ? 15  GLU   D OE2   1 
ATOM   2894 N  N     . PRO   C 2 17  ? -54.43500 40.43000 -19.38300 1.000 16.43686 ? 16  PRO   D N     1 
ATOM   2895 C  CA    A PRO   C 2 17  ? -53.92600 41.49600 -20.25900 0.500 18.05799 ? 16  PRO   D CA    1 
ATOM   2896 C  CA    B PRO   C 2 17  ? -53.91900 41.48600 -20.26300 0.500 17.35221 ? 16  PRO   D CA    1 
ATOM   2897 C  C     . PRO   C 2 17  ? -52.75000 42.21500 -19.61700 1.000 17.10705 ? 16  PRO   D C     1 
ATOM   2898 O  O     . PRO   C 2 17  ? -52.77800 42.55500 -18.43400 1.000 19.93371 ? 16  PRO   D O     1 
ATOM   2899 C  CB    A PRO   C 2 17  ? -55.12900 42.43400 -20.42700 0.500 20.72850 ? 16  PRO   D CB    1 
ATOM   2900 C  CB    B PRO   C 2 17  ? -55.12800 42.40600 -20.46300 0.500 18.31356 ? 16  PRO   D CB    1 
ATOM   2901 C  CG    A PRO   C 2 17  ? -56.31600 41.66000 -19.97000 0.500 21.52184 ? 16  PRO   D CG    1 
ATOM   2902 C  CG    B PRO   C 2 17  ? -55.98300 42.15200 -19.25900 0.500 16.87028 ? 16  PRO   D CG    1 
ATOM   2903 C  CD    A PRO   C 2 17  ? -55.84100 40.63700 -18.99200 0.500 19.80816 ? 16  PRO   D CD    1 
ATOM   2904 C  CD    B PRO   C 2 17  ? -55.82100 40.69200 -18.95800 0.500 18.49279 ? 16  PRO   D CD    1 
ATOM   2905 N  N     . LEU   C 2 18  ? -51.70600 42.42000 -20.39900 1.000 15.93332 ? 17  LEU   D N     1 
ATOM   2906 C  CA    . LEU   C 2 18  ? -50.55600 43.21000 -19.99000 1.000 16.61528 ? 17  LEU   D CA    1 
ATOM   2907 C  C     . LEU   C 2 18  ? -50.62400 44.61400 -20.57800 1.000 16.11924 ? 17  LEU   D C     1 
ATOM   2908 O  O     . LEU   C 2 18  ? -50.51400 45.60000 -19.84200 1.000 18.10761 ? 17  LEU   D O     1 
ATOM   2909 C  CB    . LEU   C 2 18  ? -49.25900 42.51700 -20.42200 1.000 16.77797 ? 17  LEU   D CB    1 
ATOM   2910 C  CG    . LEU   C 2 18  ? -47.93900 43.19500 -20.01700 1.000 17.60897 ? 17  LEU   D CG    1 
ATOM   2911 C  CD1   . LEU   C 2 18  ? -47.75200 43.18900 -18.49800 1.000 20.01099 ? 17  LEU   D CD1   1 
ATOM   2912 C  CD2   . LEU   C 2 18  ? -46.75300 42.49700 -20.70500 1.000 17.75928 ? 17  LEU   D CD2   1 
ATOM   2913 N  N     . GLY   C 2 19  ? -50.87800 44.71300 -21.87600 1.000 17.02993 ? 18  GLY   D N     1 
ATOM   2914 C  CA    . GLY   C 2 19  ? -51.03700 45.98600 -22.54800 1.000 17.47561 ? 18  GLY   D CA    1 
ATOM   2915 C  C     . GLY   C 2 19  ? -50.94000 45.79500 -24.04600 1.000 16.29921 ? 18  GLY   D C     1 
ATOM   2916 O  O     . GLY   C 2 19  ? -50.70600 44.68400 -24.54800 1.000 17.03473 ? 18  GLY   D O     1 
ATOM   2917 N  N     . ARG   C 2 20  ? -51.12300 46.90300 -24.75900 1.000 16.76348 ? 19  ARG   D N     1 
ATOM   2918 C  CA    . ARG   C 2 20  ? -51.09900 46.92200 -26.21800 1.000 15.88454 ? 19  ARG   D CA    1 
ATOM   2919 C  C     . ARG   C 2 20  ? -49.77300 47.48000 -26.72100 1.000 17.59816 ? 19  ARG   D C     1 
ATOM   2920 O  O     . ARG   C 2 20  ? -49.28500 48.50100 -26.22400 1.000 19.87357 ? 19  ARG   D O     1 
ATOM   2921 C  CB    . ARG   C 2 20  ? -52.23500 47.79900 -26.75300 1.000 18.57595 ? 19  ARG   D CB    1 
ATOM   2922 C  CG    . ARG   C 2 20  ? -52.21100 47.97600 -28.26400 1.000 18.82837 ? 19  ARG   D CG    1 
ATOM   2923 C  CD    . ARG   C 2 20  ? -53.50500 48.58600 -28.77800 1.000 19.71817 ? 19  ARG   D CD    1 
ATOM   2924 N  NE    . ARG   C 2 20  ? -54.59700 47.62500 -28.69500 1.000 21.17306 ? 19  ARG   D NE    1 
ATOM   2925 C  CZ    . ARG   C 2 20  ? -55.73900 47.73900 -29.35600 1.000 22.82922 ? 19  ARG   D CZ    1 
ATOM   2926 N  NH1   . ARG   C 2 20  ? -55.99300 48.79000 -30.11900 1.000 24.76214 ? 19  ARG   D NH1   1 
ATOM   2927 N  NH2   . ARG   C 2 20  ? -56.64300 46.76700 -29.25900 1.000 23.18134 ? 19  ARG   D NH2   1 
ATOM   2928 N  N     . VAL   C 2 21  ? -49.19000 46.81000 -27.71700 1.000 15.71377 ? 20  VAL   D N     1 
ATOM   2929 C  CA    . VAL   C 2 21  ? -48.03800 47.31900 -28.45100 1.000 16.55504 ? 20  VAL   D CA    1 
ATOM   2930 C  C     . VAL   C 2 21  ? -48.50800 47.57800 -29.87400 1.000 16.32885 ? 20  VAL   D C     1 
ATOM   2931 O  O     . VAL   C 2 21  ? -49.13300 46.70800 -30.49000 1.000 16.98475 ? 20  VAL   D O     1 
ATOM   2932 C  CB    . VAL   C 2 21  ? -46.88100 46.30600 -28.45500 1.000 16.49276 ? 20  VAL   D CB    1 
ATOM   2933 C  CG1   . VAL   C 2 21  ? -45.68000 46.87800 -29.19600 1.000 17.61509 ? 20  VAL   D CG1   1 
ATOM   2934 C  CG2   . VAL   C 2 21  ? -46.49900 45.88100 -27.03300 1.000 18.47159 ? 20  VAL   D CG2   1 
ATOM   2935 N  N     . SER   C 2 22  ? -48.23600 48.76700 -30.39200 1.000 17.14933 ? 21  SER   D N     1 
ATOM   2936 C  CA    . SER   C 2 22  ? -48.52300 49.04600 -31.78900 1.000 18.19339 ? 21  SER   D CA    1 
ATOM   2937 C  C     . SER   C 2 22  ? -47.22300 49.27000 -32.54700 1.000 16.77277 ? 21  SER   D C     1 
ATOM   2938 O  O     . SER   C 2 22  ? -46.21400 49.69500 -31.97400 1.000 18.63064 ? 21  SER   D O     1 
ATOM   2939 C  CB    . SER   C 2 22  ? -49.43400 50.26100 -31.96700 1.000 20.33798 ? 21  SER   D CB    1 
ATOM   2940 O  OG    . SER   C 2 22  ? -48.77500 51.45800 -31.60200 1.000 23.33896 ? 21  SER   D OG    1 
ATOM   2941 N  N     . PHE   C 2 23  ? -47.25700 48.96300 -33.84100 1.000 16.04701 ? 22  PHE   D N     1 
ATOM   2942 C  CA    . PHE   C 2 23  ? -46.07900 49.04200 -34.69500 1.000 15.81245 ? 22  PHE   D CA    1 
ATOM   2943 C  C     . PHE   C 2 23  ? -46.39800 49.83800 -35.94900 1.000 16.73802 ? 22  PHE   D C     1 
ATOM   2944 O  O     . PHE   C 2 23  ? -47.47600 49.69100 -36.53200 1.000 18.16699 ? 22  PHE   D O     1 
ATOM   2945 C  CB    . PHE   C 2 23  ? -45.64300 47.65200 -35.17100 1.000 17.16975 ? 22  PHE   D CB    1 
ATOM   2946 C  CG    . PHE   C 2 23  ? -45.49100 46.63800 -34.07400 1.000 16.31293 ? 22  PHE   D CG    1 
ATOM   2947 C  CD1   . PHE   C 2 23  ? -44.27700 46.49100 -33.41100 1.000 15.91656 ? 22  PHE   D CD1   1 
ATOM   2948 C  CD2   . PHE   C 2 23  ? -46.54500 45.80600 -33.72600 1.000 18.01248 ? 22  PHE   D CD2   1 
ATOM   2949 C  CE1   . PHE   C 2 23  ? -44.11000 45.54700 -32.42200 1.000 16.11906 ? 22  PHE   D CE1   1 
ATOM   2950 C  CE2   . PHE   C 2 23  ? -46.39200 44.84400 -32.73800 1.000 17.68226 ? 22  PHE   D CE2   1 
ATOM   2951 C  CZ    . PHE   C 2 23  ? -45.17200 44.72200 -32.08000 1.000 16.77615 ? 22  PHE   D CZ    1 
ATOM   2952 N  N     . GLU   C 2 24  ? -45.46000 50.68000 -36.36700 1.000 17.49753 ? 23  GLU   D N     1 
ATOM   2953 C  CA    . GLU   C 2 24  ? -45.46000 51.21300 -37.72600 1.000 17.61772 ? 23  GLU   D CA    1 
ATOM   2954 C  C     . GLU   C 2 24  ? -44.70300 50.22100 -38.60100 1.000 16.38049 ? 23  GLU   D C     1 
ATOM   2955 O  O     . GLU   C 2 24  ? -43.58800 49.81500 -38.25900 1.000 16.81284 ? 23  GLU   D O     1 
ATOM   2956 C  CB    . GLU   C 2 24  ? -44.74000 52.55800 -37.79000 1.000 18.86059 ? 23  GLU   D CB    1 
ATOM   2957 C  CG    . GLU   C 2 24  ? -44.76300 53.16800 -39.18700 1.000 20.83186 ? 23  GLU   D CG    1 
ATOM   2958 C  CD    . GLU   C 2 24  ? -43.96700 54.45800 -39.30400 1.000 24.21334 ? 23  GLU   D CD    1 
ATOM   2959 O  OE1   . GLU   C 2 24  ? -43.54500 55.01600 -38.25800 1.000 26.11702 ? 23  GLU   D OE1   1 
ATOM   2960 O  OE2   . GLU   C 2 24  ? -43.75900 54.92000 -40.45200 1.000 25.25940 ? 23  GLU   D OE2   1 
ATOM   2961 N  N     . LEU   C 2 25  ? -45.31200 49.81800 -39.70900 1.000 16.46956 ? 24  LEU   D N     1 
ATOM   2962 C  CA    . LEU   C 2 25  ? -44.67500 48.92100 -40.66200 1.000 17.14639 ? 24  LEU   D CA    1 
ATOM   2963 C  C     . LEU   C 2 25  ? -44.19900 49.73400 -41.85500 1.000 16.75324 ? 24  LEU   D C     1 
ATOM   2964 O  O     . LEU   C 2 25  ? -44.97600 50.48200 -42.46700 1.000 18.60774 ? 24  LEU   D O     1 
ATOM   2965 C  CB    . LEU   C 2 25  ? -45.63300 47.82100 -41.11900 1.000 17.14599 ? 24  LEU   D CB    1 
ATOM   2966 C  CG    . LEU   C 2 25  ? -46.33100 47.03400 -40.00700 1.000 16.80893 ? 24  LEU   D CG    1 
ATOM   2967 C  CD1   . LEU   C 2 25  ? -47.26000 46.00700 -40.62500 1.000 18.76282 ? 24  LEU   D CD1   1 
ATOM   2968 C  CD2   . LEU   C 2 25  ? -45.36600 46.39100 -39.00800 1.000 16.36606 ? 24  LEU   D CD2   1 
ATOM   2969 N  N     . PHE   C 2 26  ? -42.92500 49.58000 -42.18600 1.000 17.95075 ? 25  PHE   D N     1 
ATOM   2970 C  CA    . PHE   C 2 26  ? -42.29300 50.43300 -43.19000 1.000 19.94770 ? 25  PHE   D CA    1 
ATOM   2971 C  C     . PHE   C 2 26  ? -42.58100 49.92500 -44.60700 1.000 20.02934 ? 25  PHE   D C     1 
ATOM   2972 O  O     . PHE   C 2 26  ? -41.69100 49.52500 -45.36000 1.000 22.73976 ? 25  PHE   D O     1 
ATOM   2973 C  CB    . PHE   C 2 26  ? -40.80100 50.53500 -42.91400 1.000 19.68079 ? 25  PHE   D CB    1 
ATOM   2974 C  CG    . PHE   C 2 26  ? -40.47000 51.09400 -41.55800 1.000 22.82232 ? 25  PHE   D CG    1 
ATOM   2975 C  CD1   . PHE   C 2 26  ? -41.16800 52.17300 -41.04100 1.000 24.82425 ? 25  PHE   D CD1   1 
ATOM   2976 C  CD2   . PHE   C 2 26  ? -39.45500 50.53800 -40.80400 1.000 22.95811 ? 25  PHE   D CD2   1 
ATOM   2977 C  CE1   . PHE   C 2 26  ? -40.85200 52.68000 -39.79100 1.000 26.55585 ? 25  PHE   D CE1   1 
ATOM   2978 C  CE2   . PHE   C 2 26  ? -39.12900 51.04800 -39.56100 1.000 24.35721 ? 25  PHE   D CE2   1 
ATOM   2979 C  CZ    . PHE   C 2 26  ? -39.82700 52.11800 -39.05700 1.000 24.88896 ? 25  PHE   D CZ    1 
ATOM   2980 N  N     . ALA   C 2 27  ? -43.86600 49.97000 -44.97600 1.000 21.65108 ? 26  ALA   D N     1 
ATOM   2981 C  CA    . ALA   C 2 27  ? -44.25500 49.55000 -46.31900 1.000 21.11555 ? 26  ALA   D CA    1 
ATOM   2982 C  C     . ALA   C 2 27  ? -43.59700 50.41700 -47.38700 1.000 23.01815 ? 26  ALA   D C     1 
ATOM   2983 O  O     . ALA   C 2 27  ? -43.37700 49.95800 -48.51500 1.000 24.11505 ? 26  ALA   D O     1 
ATOM   2984 C  CB    . ALA   C 2 27  ? -45.77400 49.60400 -46.46100 1.000 22.26164 ? 26  ALA   D CB    1 
ATOM   2985 N  N     . ASP   C 2 28  ? -43.27300 51.66700 -47.05000 1.000 22.65352 ? 27  ASP   D N     1 
ATOM   2986 C  CA    . ASP   C 2 28  ? -42.66100 52.55700 -48.02900 1.000 23.29984 ? 27  ASP   D CA    1 
ATOM   2987 C  C     . ASP   C 2 28  ? -41.26200 52.10100 -48.42900 1.000 25.70278 ? 27  ASP   D C     1 
ATOM   2988 O  O     . ASP   C 2 28  ? -40.79800 52.42600 -49.52700 1.000 29.39694 ? 27  ASP   D O     1 
ATOM   2989 C  CB    . ASP   C 2 28  ? -42.63900 53.99300 -47.50700 1.000 25.91348 ? 27  ASP   D CB    1 
ATOM   2990 C  CG    . ASP   C 2 28  ? -42.04300 54.11700 -46.10900 1.000 29.78727 ? 27  ASP   D CG    1 
ATOM   2991 O  OD1   . ASP   C 2 28  ? -41.73200 53.09100 -45.46600 1.000 30.49472 ? 27  ASP   D OD1   1 
ATOM   2992 O  OD2   . ASP   C 2 28  ? -41.88400 55.27500 -45.65500 1.000 37.77618 ? 27  ASP   D OD2   1 
ATOM   2993 N  N     . LYS   C 2 29  ? -40.57300 51.36700 -47.56000 1.000 25.02275 ? 28  LYS   D N     1 
ATOM   2994 C  CA    . LYS   C 2 29  ? -39.21700 50.91600 -47.84100 1.000 23.32619 ? 28  LYS   D CA    1 
ATOM   2995 C  C     . LYS   C 2 29  ? -39.06800 49.41100 -47.93400 1.000 20.96215 ? 28  LYS   D C     1 
ATOM   2996 O  O     . LYS   C 2 29  ? -38.13500 48.93800 -48.58600 1.000 21.03502 ? 28  LYS   D O     1 
ATOM   2997 C  CB    . LYS   C 2 29  ? -38.24200 51.44200 -46.78000 1.000 26.81147 ? 28  LYS   D CB    1 
ATOM   2998 C  CG    . LYS   C 2 29  ? -38.12500 52.95200 -46.78700 1.000 30.73570 ? 28  LYS   D CG    1 
ATOM   2999 C  CD    . LYS   C 2 29  ? -37.21700 53.44400 -45.68500 1.000 35.28095 ? 28  LYS   D CD    1 
ATOM   3000 C  CE    . LYS   C 2 29  ? -37.20900 54.96500 -45.62600 1.000 35.24845 ? 28  LYS   D CE    1 
ATOM   3001 N  NZ    . LYS   C 2 29  ? -36.53700 55.44500 -44.39700 1.000 35.74445 ? 28  LYS   D NZ    1 
ATOM   3002 N  N     . VAL   C 2 30  ? -39.93700 48.65000 -47.28200 1.000 18.11133 ? 29  VAL   D N     1 
ATOM   3003 C  CA    . VAL   C 2 30  ? -39.82600 47.19800 -47.25400 1.000 19.31819 ? 29  VAL   D CA    1 
ATOM   3004 C  C     . VAL   C 2 30  ? -41.21600 46.62500 -47.51900 1.000 18.09493 ? 29  VAL   D C     1 
ATOM   3005 O  O     . VAL   C 2 30  ? -41.78900 45.95500 -46.65100 1.000 18.50169 ? 29  VAL   D O     1 
ATOM   3006 C  CB    . VAL   C 2 30  ? -39.27000 46.73600 -45.89600 1.000 19.05946 ? 29  VAL   D CB    1 
ATOM   3007 C  CG1   . VAL   C 2 30  ? -38.53000 45.45000 -46.06400 1.000 21.53504 ? 29  VAL   D CG1   1 
ATOM   3008 C  CG2   . VAL   C 2 30  ? -38.36300 47.81100 -45.25600 1.000 21.41760 ? 29  VAL   D CG2   1 
ATOM   3009 N  N     . PRO   C 2 31  ? -41.80100 46.85800 -48.69300 1.000 18.67550 ? 30  PRO   D N     1 
ATOM   3010 C  CA    . PRO   C 2 31  ? -43.23700 46.56200 -48.85200 1.000 16.48601 ? 30  PRO   D CA    1 
ATOM   3011 C  C     . PRO   C 2 31  ? -43.61100 45.09800 -48.70500 1.000 17.92110 ? 30  PRO   D C     1 
ATOM   3012 O  O     . PRO   C 2 31  ? -44.62400 44.79600 -48.06500 1.000 18.50925 ? 30  PRO   D O     1 
ATOM   3013 C  CB    . PRO   C 2 31  ? -43.55200 47.10200 -50.25900 1.000 20.24893 ? 30  PRO   D CB    1 
ATOM   3014 C  CG    . PRO   C 2 31  ? -42.23900 47.15900 -50.95400 1.000 21.00137 ? 30  PRO   D CG    1 
ATOM   3015 C  CD    . PRO   C 2 31  ? -41.23500 47.49100 -49.90200 1.000 20.57609 ? 30  PRO   D CD    1 
ATOM   3016 N  N     . LYS   C 2 32  ? -42.83800 44.17600 -49.28600 1.000 18.89128 ? 31  LYS   D N     1 
ATOM   3017 C  CA    A LYS   C 2 32  ? -43.22000 42.77000 -49.23100 0.500 19.05557 ? 31  LYS   D CA    1 
ATOM   3018 C  CA    B LYS   C 2 32  ? -43.21600 42.76600 -49.22900 0.500 19.56016 ? 31  LYS   D CA    1 
ATOM   3019 C  C     . LYS   C 2 32  ? -43.15400 42.23400 -47.80400 1.000 17.16883 ? 31  LYS   D C     1 
ATOM   3020 O  O     . LYS   C 2 32  ? -44.02700 41.46400 -47.37600 1.000 16.48380 ? 31  LYS   D O     1 
ATOM   3021 C  CB    A LYS   C 2 32  ? -42.31600 41.95700 -50.15600 0.500 20.34932 ? 31  LYS   D CB    1 
ATOM   3022 C  CB    B LYS   C 2 32  ? -42.29900 41.94500 -50.13100 0.500 21.57932 ? 31  LYS   D CB    1 
ATOM   3023 C  CG    A LYS   C 2 32  ? -42.74500 40.51800 -50.33000 0.500 20.45475 ? 31  LYS   D CG    1 
ATOM   3024 C  CG    B LYS   C 2 32  ? -42.32400 42.37900 -51.57800 0.500 23.95802 ? 31  LYS   D CG    1 
ATOM   3025 C  CD    A LYS   C 2 32  ? -41.90200 39.82300 -51.39000 0.500 22.33398 ? 31  LYS   D CD    1 
ATOM   3026 C  CD    B LYS   C 2 32  ? -41.27000 41.63800 -52.38600 0.500 25.23026 ? 31  LYS   D CD    1 
ATOM   3027 C  CE    A LYS   C 2 32  ? -42.03000 38.31200 -51.32400 0.500 22.43445 ? 31  LYS   D CE    1 
ATOM   3028 C  CE    B LYS   C 2 32  ? -41.19800 42.15000 -53.82100 0.500 25.53756 ? 31  LYS   D CE    1 
ATOM   3029 N  NZ    A LYS   C 2 32  ? -40.98500 37.68000 -52.18000 0.500 23.86111 ? 31  LYS   D NZ    1 
ATOM   3030 N  NZ    B LYS   C 2 32  ? -40.07300 41.53600 -54.58400 0.500 25.69294 ? 31  LYS   D NZ    1 
ATOM   3031 N  N     . THR   C 2 33  ? -42.13200 42.63600 -47.05500 1.000 16.27653 ? 32  THR   D N     1 
ATOM   3032 C  CA    . THR   C 2 33  ? -41.96900 42.15900 -45.68800 1.000 15.68484 ? 32  THR   D CA    1 
ATOM   3033 C  C     . THR   C 2 33  ? -42.99300 42.81700 -44.77500 1.000 14.41463 ? 32  THR   D C     1 
ATOM   3034 O  O     . THR   C 2 33  ? -43.58100 42.16200 -43.90800 1.000 15.65093 ? 32  THR   D O     1 
ATOM   3035 C  CB    . THR   C 2 33  ? -40.53600 42.44500 -45.22500 1.000 15.51954 ? 32  THR   D CB    1 
ATOM   3036 O  OG1   . THR   C 2 33  ? -39.60700 41.93600 -46.19300 1.000 16.63876 ? 32  THR   D OG1   1 
ATOM   3037 C  CG2   . THR   C 2 33  ? -40.25800 41.80400 -43.87600 1.000 16.28362 ? 32  THR   D CG2   1 
ATOM   3038 N  N     . ALA   C 2 34  ? -43.26600 44.10400 -44.99400 1.000 15.48418 ? 33  ALA   D N     1 
ATOM   3039 C  CA    . ALA   C 2 34  ? -44.30100 44.76000 -44.20300 1.000 16.04021 ? 33  ALA   D CA    1 
ATOM   3040 C  C     . ALA   C 2 34  ? -45.66900 44.13500 -44.45800 1.000 14.23410 ? 33  ALA   D C     1 
ATOM   3041 O  O     . ALA   C 2 34  ? -46.45500 43.93700 -43.52200 1.000 15.53977 ? 33  ALA   D O     1 
ATOM   3042 C  CB    . ALA   C 2 34  ? -44.32500 46.25800 -44.50600 1.000 18.46451 ? 33  ALA   D CB    1 
ATOM   3043 N  N     . GLU   C 2 35  ? -45.97900 43.83500 -45.72300 1.000 16.09152 ? 34  GLU   D N     1 
ATOM   3044 C  CA    . GLU   C 2 35  ? -47.28500 43.27800 -46.05300 1.000 16.67689 ? 34  GLU   D CA    1 
ATOM   3045 C  C     . GLU   C 2 35  ? -47.48600 41.91600 -45.39400 1.000 16.79116 ? 34  GLU   D C     1 
ATOM   3046 O  O     . GLU   C 2 35  ? -48.57500 41.62000 -44.89000 1.000 16.50430 ? 34  GLU   D O     1 
ATOM   3047 C  CB    . GLU   C 2 35  ? -47.45100 43.18200 -47.56700 1.000 18.63253 ? 34  GLU   D CB    1 
ATOM   3048 C  CG    . GLU   C 2 35  ? -48.69400 42.40600 -48.01500 1.000 21.18420 ? 34  GLU   D CG    1 
ATOM   3049 C  CD    . GLU   C 2 35  ? -50.01100 43.03700 -47.57800 1.000 24.30796 ? 34  GLU   D CD    1 
ATOM   3050 O  OE1   . GLU   C 2 35  ? -50.02500 44.20200 -47.11900 1.000 22.87645 ? 34  GLU   D OE1   1 
ATOM   3051 O  OE2   . GLU   C 2 35  ? -51.04700 42.35400 -47.69900 1.000 26.56212 ? 34  GLU   D OE2   1 
ATOM   3052 N  N     . ASN   C 2 36  ? -46.44500 41.07600 -45.37500 1.000 15.15051 ? 35  ASN   D N     1 
ATOM   3053 C  CA    . ASN   C 2 36  ? -46.54400 39.78900 -44.68700 1.000 15.21926 ? 35  ASN   D CA    1 
ATOM   3054 C  C     . ASN   C 2 36  ? -46.94000 39.97100 -43.23000 1.000 14.95235 ? 35  ASN   D C     1 
ATOM   3055 O  O     . ASN   C 2 36  ? -47.90300 39.35700 -42.75200 1.000 14.69992 ? 35  ASN   D O     1 
ATOM   3056 C  CB    . ASN   C 2 36  ? -45.20700 39.06000 -44.79000 1.000 14.89388 ? 35  ASN   D CB    1 
ATOM   3057 C  CG    . ASN   C 2 36  ? -45.22100 37.69200 -44.10700 1.000 15.06235 ? 35  ASN   D CG    1 
ATOM   3058 O  OD1   . ASN   C 2 36  ? -46.00200 36.79000 -44.46700 1.000 16.46427 ? 35  ASN   D OD1   1 
ATOM   3059 N  ND2   . ASN   C 2 36  ? -44.30900 37.51300 -43.15000 1.000 15.13346 ? 35  ASN   D ND2   1 
ATOM   3060 N  N     . PHE   C 2 37  ? -46.23300 40.84900 -42.51900 1.000 14.55741 ? 36  PHE   D N     1 
ATOM   3061 C  CA    . PHE   C 2 37  ? -46.51700 41.04400 -41.10500 1.000 14.78858 ? 36  PHE   D CA    1 
ATOM   3062 C  C     . PHE   C 2 37  ? -47.90400 41.63800 -40.91300 1.000 14.22613 ? 36  PHE   D C     1 
ATOM   3063 O  O     . PHE   C 2 37  ? -48.63600 41.23300 -39.99800 1.000 14.69226 ? 36  PHE   D O     1 
ATOM   3064 C  CB    . PHE   C 2 37  ? -45.43700 41.93800 -40.48600 1.000 14.05792 ? 36  PHE   D CB    1 
ATOM   3065 C  CG    . PHE   C 2 37  ? -45.47400 42.01100 -38.99600 1.000 14.59384 ? 36  PHE   D CG    1 
ATOM   3066 C  CD1   . PHE   C 2 37  ? -44.73900 41.13600 -38.24000 1.000 13.47161 ? 36  PHE   D CD1   1 
ATOM   3067 C  CD2   . PHE   C 2 37  ? -46.21200 42.98300 -38.34600 1.000 15.34509 ? 36  PHE   D CD2   1 
ATOM   3068 C  CE1   . PHE   C 2 37  ? -44.74200 41.21100 -36.85800 1.000 14.53614 ? 36  PHE   D CE1   1 
ATOM   3069 C  CE2   . PHE   C 2 37  ? -46.21300 43.06200 -36.96800 1.000 16.10964 ? 36  PHE   D CE2   1 
ATOM   3070 C  CZ    . PHE   C 2 37  ? -45.46100 42.17800 -36.22400 1.000 16.15854 ? 36  PHE   D CZ    1 
ATOM   3071 N  N     . ARG   C 2 38  ? -48.29200 42.58100 -41.77900 1.000 14.46007 ? 37  ARG   D N     1 
ATOM   3072 C  CA    . ARG   C 2 38  ? -49.62300 43.16500 -41.68100 1.000 14.93494 ? 37  ARG   D CA    1 
ATOM   3073 C  C     . ARG   C 2 38  ? -50.70300 42.09500 -41.82100 1.000 14.32994 ? 37  ARG   D C     1 
ATOM   3074 O  O     . ARG   C 2 38  ? -51.63500 42.02200 -41.00200 1.000 14.77737 ? 37  ARG   D O     1 
ATOM   3075 C  CB    . ARG   C 2 38  ? -49.79000 44.24600 -42.75100 1.000 17.61130 ? 37  ARG   D CB    1 
ATOM   3076 C  CG    . ARG   C 2 38  ? -51.08800 45.01700 -42.60500 1.000 17.05242 ? 37  ARG   D CG    1 
ATOM   3077 C  CD    . ARG   C 2 38  ? -51.52600 45.70100 -43.91100 1.000 19.22051 ? 37  ARG   D CD    1 
ATOM   3078 N  NE    . ARG   C 2 38  ? -51.83900 44.72800 -44.95200 1.000 18.52427 ? 37  ARG   D NE    1 
ATOM   3079 C  CZ    . ARG   C 2 38  ? -52.93500 43.97700 -44.97700 1.000 20.88626 ? 37  ARG   D CZ    1 
ATOM   3080 N  NH1   . ARG   C 2 38  ? -53.91500 44.14500 -44.09900 1.000 20.69834 ? 37  ARG   D NH1   1 
ATOM   3081 N  NH2   . ARG   C 2 38  ? -53.04600 43.01900 -45.89500 1.000 20.10685 ? 37  ARG   D NH2   1 
ATOM   3082 N  N     . ALA   C 2 39  ? -50.60300 41.26000 -42.86500 1.000 15.85600 ? 38  ALA   D N     1 
ATOM   3083 C  CA    . ALA   C 2 39  ? -51.62900 40.25100 -43.11500 1.000 16.04298 ? 38  ALA   D CA    1 
ATOM   3084 C  C     . ALA   C 2 39  ? -51.65000 39.19000 -42.01800 1.000 16.14546 ? 38  ALA   D C     1 
ATOM   3085 O  O     . ALA   C 2 39  ? -52.72200 38.69700 -41.64500 1.000 17.30764 ? 38  ALA   D O     1 
ATOM   3086 C  CB    . ALA   C 2 39  ? -51.41800 39.61100 -44.49000 1.000 16.60772 ? 38  ALA   D CB    1 
ATOM   3087 N  N     . LEU   C 2 40  ? -50.48300 38.82400 -41.48400 1.000 14.88907 ? 39  LEU   D N     1 
ATOM   3088 C  CA    . LEU   C 2 40  ? -50.44300 37.86000 -40.38300 1.000 14.68336 ? 39  LEU   D CA    1 
ATOM   3089 C  C     . LEU   C 2 40  ? -51.06600 38.44100 -39.11700 1.000 14.88738 ? 39  LEU   D C     1 
ATOM   3090 O  O     . LEU   C 2 40  ? -51.60800 37.69900 -38.29300 1.000 15.68064 ? 39  LEU   D O     1 
ATOM   3091 C  CB    . LEU   C 2 40  ? -48.99500 37.40000 -40.14400 1.000 14.06174 ? 39  LEU   D CB    1 
ATOM   3092 C  CG    . LEU   C 2 40  ? -48.41800 36.55700 -41.29000 1.000 14.39646 ? 39  LEU   D CG    1 
ATOM   3093 C  CD1   . LEU   C 2 40  ? -46.94900 36.27000 -41.00700 1.000 15.65001 ? 39  LEU   D CD1   1 
ATOM   3094 C  CD2   . LEU   C 2 40  ? -49.19200 35.26000 -41.49800 1.000 16.14096 ? 39  LEU   D CD2   1 
ATOM   3095 N  N     . SER   C 2 41  ? -51.00100 39.76800 -38.95500 1.000 16.28114 ? 40  SER   D N     1 
ATOM   3096 C  CA    . SER   C 2 41  ? -51.60000 40.43800 -37.80500 1.000 15.30534 ? 40  SER   D CA    1 
ATOM   3097 C  C     . SER   C 2 41  ? -53.11900 40.54300 -37.91900 1.000 16.14802 ? 40  SER   D C     1 
ATOM   3098 O  O     . SER   C 2 41  ? -53.80700 40.49100 -36.89600 1.000 18.54568 ? 40  SER   D O     1 
ATOM   3099 C  CB    . SER   C 2 41  ? -50.98400 41.82600 -37.62400 1.000 17.57284 ? 40  SER   D CB    1 
ATOM   3100 O  OG    . SER   C 2 41  ? -49.59600 41.72000 -37.31700 1.000 16.05899 ? 40  SER   D OG    1 
ATOM   3101 N  N     . THR   C 2 42  ? -53.66700 40.69400 -39.12900 1.000 16.57411 ? 41  THR   D N     1 
ATOM   3102 C  CA    . THR   C 2 42  ? -55.12000 40.74600 -39.26700 1.000 17.99224 ? 41  THR   D CA    1 
ATOM   3103 C  C     . THR   C 2 42  ? -55.74700 39.36200 -39.33800 1.000 17.60788 ? 41  THR   D C     1 
ATOM   3104 O  O     . THR   C 2 42  ? -56.95100 39.22100 -39.08500 1.000 19.66206 ? 41  THR   D O     1 
ATOM   3105 C  CB    . THR   C 2 42  ? -55.53700 41.49200 -40.54100 1.000 17.83133 ? 41  THR   D CB    1 
ATOM   3106 O  OG1   . THR   C 2 42  ? -55.12200 40.74400 -41.69800 1.000 18.17642 ? 41  THR   D OG1   1 
ATOM   3107 C  CG2   . THR   C 2 42  ? -54.96100 42.89900 -40.58300 1.000 20.89778 ? 41  THR   D CG2   1 
ATOM   3108 N  N     . GLY   C 2 43  ? -54.96600 38.34500 -39.69500 1.000 18.23330 ? 42  GLY   D N     1 
ATOM   3109 C  CA    . GLY   C 2 43  ? -55.48000 37.00400 -39.88300 1.000 19.56923 ? 42  GLY   D CA    1 
ATOM   3110 C  C     . GLY   C 2 43  ? -56.25100 36.81200 -41.16500 1.000 21.77027 ? 42  GLY   D C     1 
ATOM   3111 O  O     . GLY   C 2 43  ? -56.89000 35.76600 -41.33800 1.000 21.59138 ? 42  GLY   D O     1 
ATOM   3112 N  N     . GLU   C 2 44  ? -56.18500 37.77900 -42.08500 1.000 20.21041 ? 43  GLU   D N     1 
ATOM   3113 C  CA    . GLU   C 2 44  ? -57.06000 37.77600 -43.25400 1.000 20.23314 ? 43  GLU   D CA    1 
ATOM   3114 C  C     . GLU   C 2 44  ? -56.81000 36.61600 -44.21400 1.000 21.46629 ? 43  GLU   D C     1 
ATOM   3115 O  O     . GLU   C 2 44  ? -57.68800 36.32500 -45.03700 1.000 23.14324 ? 43  GLU   D O     1 
ATOM   3116 C  CB    . GLU   C 2 44  ? -56.95600 39.11200 -43.98500 1.000 20.75694 ? 43  GLU   D CB    1 
ATOM   3117 C  CG    . GLU   C 2 44  ? -55.59400 39.41600 -44.57600 1.000 20.60954 ? 43  GLU   D CG    1 
ATOM   3118 C  CD    . GLU   C 2 44  ? -55.47300 40.87600 -44.97900 1.000 21.93684 ? 43  GLU   D CD    1 
ATOM   3119 O  OE1   . GLU   C 2 44  ? -55.58700 41.74900 -44.09100 1.000 23.56670 ? 43  GLU   D OE1   1 
ATOM   3120 O  OE2   . GLU   C 2 44  ? -55.27100 41.14900 -46.17700 1.000 24.14330 ? 43  GLU   D OE2   1 
ATOM   3121 N  N     . LYS   C 2 45  ? -55.64800 35.96500 -44.15500 1.000 20.04074 ? 44  LYS   D N     1 
ATOM   3122 C  CA    . LYS   C 2 45  ? -55.39200 34.81500 -45.01300 1.000 20.29866 ? 44  LYS   D CA    1 
ATOM   3123 C  C     . LYS   C 2 45  ? -55.90500 33.51200 -44.41600 1.000 21.94303 ? 44  LYS   D C     1 
ATOM   3124 O  O     . LYS   C 2 45  ? -55.77300 32.46400 -45.05400 1.000 23.67376 ? 44  LYS   D O     1 
ATOM   3125 C  CB    . LYS   C 2 45  ? -53.89600 34.67900 -45.31500 1.000 21.44370 ? 44  LYS   D CB    1 
ATOM   3126 C  CG    . LYS   C 2 45  ? -53.23700 35.94200 -45.85800 1.000 21.84224 ? 44  LYS   D CG    1 
ATOM   3127 C  CD    . LYS   C 2 45  ? -53.82000 36.37900 -47.19800 1.000 24.55893 ? 44  LYS   D CD    1 
ATOM   3128 C  CE    . LYS   C 2 45  ? -53.00900 37.53700 -47.77300 1.000 29.05366 ? 44  LYS   D CE    1 
ATOM   3129 N  NZ    . LYS   C 2 45  ? -53.59100 38.07200 -49.03400 1.000 31.25076 ? 44  LYS   D NZ    1 
ATOM   3130 N  N     . GLY   C 2 46  ? -56.47800 33.54900 -43.21400 1.000 21.26056 ? 45  GLY   D N     1 
ATOM   3131 C  CA    . GLY   C 2 46  ? -56.91800 32.34900 -42.53300 1.000 21.63368 ? 45  GLY   D CA    1 
ATOM   3132 C  C     . GLY   C 2 46  ? -55.93400 31.78900 -41.52700 1.000 22.43572 ? 45  GLY   D C     1 
ATOM   3133 O  O     . GLY   C 2 46  ? -56.20400 30.73500 -40.94300 1.000 23.32029 ? 45  GLY   D O     1 
ATOM   3134 N  N     . PHE   C 2 47  ? -54.80600 32.46000 -41.30700 1.000 19.77037 ? 46  PHE   D N     1 
ATOM   3135 C  CA    . PHE   C 2 47  ? -53.81400 32.05600 -40.31400 1.000 18.29198 ? 46  PHE   D CA    1 
ATOM   3136 C  C     . PHE   C 2 47  ? -53.05400 33.30700 -39.89400 1.000 16.81638 ? 46  PHE   D C     1 
ATOM   3137 O  O     . PHE   C 2 47  ? -53.12500 34.34200 -40.56600 1.000 18.08007 ? 46  PHE   D O     1 
ATOM   3138 C  CB    . PHE   C 2 47  ? -52.85500 31.00100 -40.88100 1.000 17.95945 ? 46  PHE   D CB    1 
ATOM   3139 C  CG    . PHE   C 2 47  ? -52.26500 31.37300 -42.21000 1.000 18.79911 ? 46  PHE   D CG    1 
ATOM   3140 C  CD1   . PHE   C 2 47  ? -51.12400 32.15700 -42.29000 1.000 19.40680 ? 46  PHE   D CD1   1 
ATOM   3141 C  CD2   . PHE   C 2 47  ? -52.85400 30.93600 -43.39000 1.000 20.04110 ? 46  PHE   D CD2   1 
ATOM   3142 C  CE1   . PHE   C 2 47  ? -50.58200 32.49200 -43.51600 1.000 20.36574 ? 46  PHE   D CE1   1 
ATOM   3143 C  CE2   . PHE   C 2 47  ? -52.31500 31.26500 -44.61600 1.000 22.28976 ? 46  PHE   D CE2   1 
ATOM   3144 C  CZ    . PHE   C 2 47  ? -51.18600 32.05400 -44.68400 1.000 21.91917 ? 46  PHE   D CZ    1 
ATOM   3145 N  N     . GLY   C 2 48  ? -52.32600 33.22200 -38.78300 1.000 16.61771 ? 47  GLY   D N     1 
ATOM   3146 C  CA    . GLY   C 2 48  ? -51.54100 34.37800 -38.37600 1.000 16.28651 ? 47  GLY   D CA    1 
ATOM   3147 C  C     . GLY   C 2 48  ? -51.22000 34.35200 -36.89300 1.000 14.67805 ? 47  GLY   D C     1 
ATOM   3148 O  O     . GLY   C 2 48  ? -51.30800 33.31300 -36.23800 1.000 14.81220 ? 47  GLY   D O     1 
ATOM   3149 N  N     . TYR   C 2 49  ? -50.86600 35.54000 -36.39200 1.000 13.71237 ? 48  TYR   D N     1 
ATOM   3150 C  CA    . TYR   C 2 49  ? -50.25300 35.66200 -35.07300 1.000 13.41946 ? 48  TYR   D CA    1 
ATOM   3151 C  C     . TYR   C 2 49  ? -51.21700 35.48100 -33.89500 1.000 12.84165 ? 48  TYR   D C     1 
ATOM   3152 O  O     . TYR   C 2 49  ? -50.75200 35.18700 -32.79100 1.000 14.48389 ? 48  TYR   D O     1 
ATOM   3153 C  CB    . TYR   C 2 49  ? -49.56600 37.01800 -34.94500 1.000 13.30581 ? 48  TYR   D CB    1 
ATOM   3154 C  CG    . TYR   C 2 49  ? -48.38000 37.22600 -35.86600 1.000 13.69426 ? 48  TYR   D CG    1 
ATOM   3155 C  CD1   . TYR   C 2 49  ? -47.34400 36.29400 -35.91600 1.000 13.54772 ? 48  TYR   D CD1   1 
ATOM   3156 C  CD2   . TYR   C 2 49  ? -48.26200 38.37700 -36.64100 1.000 14.05153 ? 48  TYR   D CD2   1 
ATOM   3157 C  CE1   . TYR   C 2 49  ? -46.24300 36.48800 -36.75000 1.000 12.78653 ? 48  TYR   D CE1   1 
ATOM   3158 C  CE2   . TYR   C 2 49  ? -47.15800 38.58400 -37.45300 1.000 14.13993 ? 48  TYR   D CE2   1 
ATOM   3159 C  CZ    . TYR   C 2 49  ? -46.15700 37.63800 -37.50200 1.000 13.73709 ? 48  TYR   D CZ    1 
ATOM   3160 O  OH    . TYR   C 2 49  ? -45.07900 37.83600 -38.31900 1.000 12.96897 ? 48  TYR   D OH    1 
ATOM   3161 N  N     . LYS   C 2 50  ? -52.52600 35.69500 -34.06900 1.000 12.49478 ? 49  LYS   D N     1 
ATOM   3162 C  CA    . LYS   C 2 50  ? -53.42600 35.68800 -32.92300 1.000 14.30387 ? 49  LYS   D CA    1 
ATOM   3163 C  C     . LYS   C 2 50  ? -53.35200 34.36200 -32.17700 1.000 13.49270 ? 49  LYS   D C     1 
ATOM   3164 O  O     . LYS   C 2 50  ? -53.55100 33.29000 -32.76200 1.000 16.13120 ? 49  LYS   D O     1 
ATOM   3165 C  CB    . LYS   C 2 50  ? -54.86300 35.93800 -33.38100 1.000 16.12421 ? 49  LYS   D CB    1 
ATOM   3166 C  CG    . LYS   C 2 50  ? -55.80900 36.16400 -32.22200 1.000 16.52714 ? 49  LYS   D CG    1 
ATOM   3167 C  CD    . LYS   C 2 50  ? -57.10800 36.75400 -32.74100 1.000 19.60602 ? 49  LYS   D CD    1 
ATOM   3168 C  CE    . LYS   C 2 50  ? -58.12900 36.89400 -31.64000 1.000 20.90596 ? 49  LYS   D CE    1 
ATOM   3169 N  NZ    . LYS   C 2 50  ? -59.36400 37.55800 -32.17000 1.000 27.12655 ? 49  LYS   D NZ    1 
ATOM   3170 N  N     . GLY   C 2 51  ? -53.08200 34.44400 -30.87200 1.000 13.51269 ? 50  GLY   D N     1 
ATOM   3171 C  CA    . GLY   C 2 51  ? -52.95300 33.27900 -30.02400 1.000 14.33749 ? 50  GLY   D CA    1 
ATOM   3172 C  C     . GLY   C 2 51  ? -51.53100 32.78700 -29.83200 1.000 14.24740 ? 50  GLY   D C     1 
ATOM   3173 O  O     . GLY   C 2 51  ? -51.28300 32.01700 -28.90000 1.000 14.14348 ? 50  GLY   D O     1 
ATOM   3174 N  N     . SER   C 2 52  ? -50.59500 33.19000 -30.69400 1.000 13.55619 ? 51  SER   D N     1 
ATOM   3175 C  CA    . SER   C 2 52  ? -49.23300 32.67800 -30.61900 1.000 13.49969 ? 51  SER   D CA    1 
ATOM   3176 C  C     . SER   C 2 52  ? -48.45400 33.36300 -29.50100 1.000 13.56368 ? 51  SER   D C     1 
ATOM   3177 O  O     . SER   C 2 52  ? -48.87800 34.37300 -28.93300 1.000 14.94608 ? 51  SER   D O     1 
ATOM   3178 C  CB    . SER   C 2 52  ? -48.52200 32.81500 -31.96700 1.000 14.80200 ? 51  SER   D CB    1 
ATOM   3179 O  OG    . SER   C 2 52  ? -48.30200 34.17200 -32.31400 1.000 15.05255 ? 51  SER   D OG    1 
ATOM   3180 N  N     A CYS   C 2 53  ? -47.25400 32.83300 -29.25300 0.500 15.00855 ? 52  CYS   D N     1 
ATOM   3181 N  N     B CYS   C 2 53  ? -47.31200 32.79000 -29.15000 0.500 14.21251 ? 52  CYS   D N     1 
ATOM   3182 C  CA    A CYS   C 2 53  ? -46.45400 33.09100 -28.06100 0.500 13.61061 ? 52  CYS   D CA    1 
ATOM   3183 C  CA    B CYS   C 2 53  ? -46.59000 33.30100 -27.99700 0.500 13.32776 ? 52  CYS   D CA    1 
ATOM   3184 C  C     A CYS   C 2 53  ? -45.16700 33.84200 -28.39900 0.500 12.80444 ? 52  CYS   D C     1 
ATOM   3185 C  C     B CYS   C 2 53  ? -45.23700 33.88400 -28.38400 0.500 13.07201 ? 52  CYS   D C     1 
ATOM   3186 O  O     A CYS   C 2 53  ? -44.58500 33.66100 -29.47800 0.500 12.80729 ? 52  CYS   D O     1 
ATOM   3187 O  O     B CYS   C 2 53  ? -44.69300 33.62800 -29.46700 0.500 15.79394 ? 52  CYS   D O     1 
ATOM   3188 C  CB    A CYS   C 2 53  ? -46.09800 31.73100 -27.44400 0.500 15.16442 ? 52  CYS   D CB    1 
ATOM   3189 C  CB    B CYS   C 2 53  ? -46.40700 32.22900 -26.92200 0.500 13.95963 ? 52  CYS   D CB    1 
ATOM   3190 S  SG    A CYS   C 2 53  ? -44.94900 31.67100 -26.06200 0.500 16.64897 ? 52  CYS   D SG    1 
ATOM   3191 S  SG    B CYS   C 2 53  ? -45.04000 31.14400 -27.25200 0.500 14.18831 ? 52  CYS   D SG    1 
ATOM   3192 N  N     . PHE   C 2 54  ? -44.71300 34.68900 -27.47100 1.000 12.55682 ? 53  PHE   D N     1 
ATOM   3193 C  CA    . PHE   C 2 54  ? -43.31600 35.14100 -27.49200 1.000 13.11048 ? 53  PHE   D CA    1 
ATOM   3194 C  C     . PHE   C 2 54  ? -42.53700 34.05000 -26.77400 1.000 12.72634 ? 53  PHE   D C     1 
ATOM   3195 O  O     . PHE   C 2 54  ? -42.51700 33.99200 -25.54900 1.000 14.87165 ? 53  PHE   D O     1 
ATOM   3196 C  CB    . PHE   C 2 54  ? -43.16300 36.49200 -26.79600 1.000 13.94566 ? 53  PHE   D CB    1 
ATOM   3197 C  CG    . PHE   C 2 54  ? -43.51700 37.66000 -27.67300 1.000 12.85486 ? 53  PHE   D CG    1 
ATOM   3198 C  CD1   . PHE   C 2 54  ? -44.84000 38.04800 -27.81000 1.000 13.68500 ? 53  PHE   D CD1   1 
ATOM   3199 C  CD2   . PHE   C 2 54  ? -42.54700 38.31900 -28.41500 1.000 14.40026 ? 53  PHE   D CD2   1 
ATOM   3200 C  CE1   . PHE   C 2 54  ? -45.20200 39.11600 -28.63900 1.000 15.10569 ? 53  PHE   D CE1   1 
ATOM   3201 C  CE2   . PHE   C 2 54  ? -42.89100 39.39100 -29.22500 1.000 15.67231 ? 53  PHE   D CE2   1 
ATOM   3202 C  CZ    . PHE   C 2 54  ? -44.21700 39.79100 -29.34500 1.000 16.31807 ? 53  PHE   D CZ    1 
ATOM   3203 N  N     . HIS   C 2 55  ? -41.91500 33.15500 -27.54100 1.000 12.45109 ? 54  HIS   D N     1 
ATOM   3204 C  CA    . HIS   C 2 55  ? -41.30200 31.97000 -26.96300 1.000 13.50876 ? 54  HIS   D CA    1 
ATOM   3205 C  C     . HIS   C 2 55  ? -39.87700 32.20800 -26.49500 1.000 13.53210 ? 54  HIS   D C     1 
ATOM   3206 O  O     . HIS   C 2 55  ? -39.36100 31.40800 -25.71600 1.000 14.52736 ? 54  HIS   D O     1 
ATOM   3207 C  CB    . HIS   C 2 55  ? -41.30100 30.83800 -27.99000 1.000 14.09015 ? 54  HIS   D CB    1 
ATOM   3208 C  CG    . HIS   C 2 55  ? -40.47800 31.13600 -29.19400 1.000 13.78939 ? 54  HIS   D CG    1 
ATOM   3209 N  ND1   . HIS   C 2 55  ? -40.95800 31.89100 -30.24000 1.000 15.22617 ? 54  HIS   D ND1   1 
ATOM   3210 C  CD2   . HIS   C 2 55  ? -39.21000 30.79400 -29.51900 1.000 15.02798 ? 54  HIS   D CD2   1 
ATOM   3211 C  CE1   . HIS   C 2 55  ? -40.02000 31.98800 -31.17000 1.000 15.27490 ? 54  HIS   D CE1   1 
ATOM   3212 N  NE2   . HIS   C 2 55  ? -38.94800 31.34300 -30.74800 1.000 15.10921 ? 54  HIS   D NE2   1 
ATOM   3213 N  N     . ARG   C 2 56  ? -39.21500 33.25700 -26.96700 1.000 12.72539 ? 55  ARG   D N     1 
ATOM   3214 C  CA    . ARG   C 2 56  ? -37.81200 33.48700 -26.63800 1.000 13.47862 ? 55  ARG   D CA    1 
ATOM   3215 C  C     . ARG   C 2 56  ? -37.63800 34.95100 -26.26900 1.000 12.61614 ? 55  ARG   D C     1 
ATOM   3216 O  O     . ARG   C 2 56  ? -37.74900 35.82700 -27.12900 1.000 13.90133 ? 55  ARG   D O     1 
ATOM   3217 C  CB    . ARG   C 2 56  ? -36.89800 33.11200 -27.81300 1.000 14.31256 ? 55  ARG   D CB    1 
ATOM   3218 C  CG    . ARG   C 2 56  ? -35.42500 33.30300 -27.52400 1.000 14.81627 ? 55  ARG   D CG    1 
ATOM   3219 C  CD    . ARG   C 2 56  ? -34.56000 33.08300 -28.76300 1.000 13.92703 ? 55  ARG   D CD    1 
ATOM   3220 N  NE    . ARG   C 2 56  ? -34.51900 31.69200 -29.18100 1.000 15.84231 ? 55  ARG   D NE    1 
ATOM   3221 C  CZ    . ARG   C 2 56  ? -33.77600 31.24600 -30.18400 1.000 16.12529 ? 55  ARG   D CZ    1 
ATOM   3222 N  NH1   . ARG   C 2 56  ? -33.06200 32.07100 -30.93600 1.000 15.99357 ? 55  ARG   D NH1   1 
ATOM   3223 N  NH2   . ARG   C 2 56  ? -33.75000 29.94100 -30.44300 1.000 23.00650 ? 55  ARG   D NH2   1 
ATOM   3224 N  N     . ILE   C 2 57  ? -37.40800 35.21700 -24.98600 1.000 13.04400 ? 56  ILE   D N     1 
ATOM   3225 C  CA    . ILE   C 2 57  ? -37.25700 36.57900 -24.47800 1.000 13.61621 ? 56  ILE   D CA    1 
ATOM   3226 C  C     . ILE   C 2 57  ? -35.93600 36.60500 -23.72400 1.000 14.43908 ? 56  ILE   D C     1 
ATOM   3227 O  O     . ILE   C 2 57  ? -35.77400 35.88500 -22.73000 1.000 14.86532 ? 56  ILE   D O     1 
ATOM   3228 C  CB    . ILE   C 2 57  ? -38.41900 36.99900 -23.56600 1.000 14.88732 ? 56  ILE   D CB    1 
ATOM   3229 C  CG1   . ILE   C 2 57  ? -39.74700 36.97400 -24.33800 1.000 15.23203 ? 56  ILE   D CG1   1 
ATOM   3230 C  CG2   . ILE   C 2 57  ? -38.12300 38.35300 -22.96100 1.000 16.49791 ? 56  ILE   D CG2   1 
ATOM   3231 C  CD1   . ILE   C 2 57  ? -40.95100 37.34200 -23.49000 1.000 17.95641 ? 56  ILE   D CD1   1 
ATOM   3232 N  N     . ILE   C 2 58  ? -34.97500 37.38100 -24.21900 1.000 14.76734 ? 57  ILE   D N     1 
ATOM   3233 C  CA    . ILE   C 2 58  ? -33.67100 37.44800 -23.56800 1.000 15.86477 ? 57  ILE   D CA    1 
ATOM   3234 C  C     . ILE   C 2 58  ? -33.45100 38.88900 -23.13600 1.000 16.51259 ? 57  ILE   D C     1 
ATOM   3235 O  O     . ILE   C 2 58  ? -33.25100 39.77300 -23.98400 1.000 17.62741 ? 57  ILE   D O     1 
ATOM   3236 C  CB    . ILE   C 2 58  ? -32.55000 36.92900 -24.47600 1.000 15.91416 ? 57  ILE   D CB    1 
ATOM   3237 C  CG1   . ILE   C 2 58  ? -32.80700 35.46000 -24.83000 1.000 16.52488 ? 57  ILE   D CG1   1 
ATOM   3238 C  CG2   . ILE   C 2 58  ? -31.22600 37.06300 -23.75900 1.000 17.07475 ? 57  ILE   D CG2   1 
ATOM   3239 C  CD1   . ILE   C 2 58  ? -31.72800 34.82600 -25.67100 1.000 18.50518 ? 57  ILE   D CD1   1 
ATOM   3240 N  N     . PRO   C 2 59  ? -33.50400 39.16400 -21.83800 1.000 17.30868 ? 58  PRO   D N     1 
ATOM   3241 C  CA    . PRO   C 2 59  ? -33.36300 40.54100 -21.36500 1.000 20.79944 ? 58  PRO   D CA    1 
ATOM   3242 C  C     . PRO   C 2 59  ? -32.05300 41.15500 -21.83600 1.000 22.63062 ? 58  PRO   D C     1 
ATOM   3243 O  O     . PRO   C 2 59  ? -31.00200 40.50900 -21.84600 1.000 24.98575 ? 58  PRO   D O     1 
ATOM   3244 C  CB    . PRO   C 2 59  ? -33.41200 40.39400 -19.83700 1.000 22.29722 ? 58  PRO   D CB    1 
ATOM   3245 C  CG    . PRO   C 2 59  ? -34.20400 39.11400 -19.61500 1.000 21.73807 ? 58  PRO   D CG    1 
ATOM   3246 C  CD    . PRO   C 2 59  ? -33.76100 38.21300 -20.74200 1.000 20.10630 ? 58  PRO   D CD    1 
ATOM   3247 N  N     . GLY   C 2 60  ? -32.13300 42.41600 -22.24400 1.000 22.54834 ? 59  GLY   D N     1 
ATOM   3248 C  CA    . GLY   C 2 60  ? -31.00500 43.12300 -22.80300 1.000 24.32516 ? 59  GLY   D CA    1 
ATOM   3249 C  C     . GLY   C 2 60  ? -30.85800 42.97800 -24.30000 1.000 21.52310 ? 59  GLY   D C     1 
ATOM   3250 O  O     . GLY   C 2 60  ? -29.99200 43.64400 -24.88800 1.000 22.38371 ? 59  GLY   D O     1 
ATOM   3251 N  N     . PHE   C 2 61  ? -31.68900 42.15100 -24.93900 1.000 17.66252 ? 60  PHE   D N     1 
ATOM   3252 C  CA    . PHE   C 2 61  ? -31.54000 41.90400 -26.36600 1.000 16.92374 ? 60  PHE   D CA    1 
ATOM   3253 C  C     . PHE   C 2 61  ? -32.85800 42.02100 -27.12400 1.000 15.13777 ? 60  PHE   D C     1 
ATOM   3254 O  O     . PHE   C 2 61  ? -33.02000 42.96500 -27.90500 1.000 16.59633 ? 60  PHE   D O     1 
ATOM   3255 C  CB    . PHE   C 2 61  ? -30.86800 40.55300 -26.62600 1.000 17.00432 ? 60  PHE   D CB    1 
ATOM   3256 C  CG    . PHE   C 2 61  ? -29.44900 40.47000 -26.12200 1.000 17.57450 ? 60  PHE   D CG    1 
ATOM   3257 C  CD1   . PHE   C 2 61  ? -28.39700 40.91300 -26.90400 1.000 18.73356 ? 60  PHE   D CD1   1 
ATOM   3258 C  CD2   . PHE   C 2 61  ? -29.17300 39.92600 -24.88700 1.000 18.97789 ? 60  PHE   D CD2   1 
ATOM   3259 C  CE1   . PHE   C 2 61  ? -27.09300 40.83400 -26.44800 1.000 19.02699 ? 60  PHE   D CE1   1 
ATOM   3260 C  CE2   . PHE   C 2 61  ? -27.86500 39.85000 -24.42100 1.000 20.54940 ? 60  PHE   D CE2   1 
ATOM   3261 C  CZ    . PHE   C 2 61  ? -26.82800 40.29800 -25.20900 1.000 20.05108 ? 60  PHE   D CZ    1 
ATOM   3262 N  N     . MET   C 2 62  ? -33.78300 41.07500 -26.94600 1.000 15.47586 ? 61  MET   D N     1 
ATOM   3263 C  CA    . MET   C 2 62  ? -34.98000 41.10700 -27.77500 1.000 13.65426 ? 61  MET   D CA    1 
ATOM   3264 C  C     . MET   C 2 62  ? -36.07200 40.21900 -27.19600 1.000 14.44368 ? 61  MET   D C     1 
ATOM   3265 O  O     . MET   C 2 62  ? -35.82500 39.34200 -26.36200 1.000 14.45646 ? 61  MET   D O     1 
ATOM   3266 C  CB    . MET   C 2 62  ? -34.68600 40.65100 -29.21300 1.000 15.13293 ? 61  MET   D CB    1 
ATOM   3267 C  CG    . MET   C 2 62  ? -34.71300 39.12700 -29.41000 1.000 16.17811 ? 61  MET   D CG    1 
ATOM   3268 S  SD    . MET   C 2 62  ? -33.38400 38.21800 -28.56000 1.000 15.65732 ? 61  MET   D SD    1 
ATOM   3269 C  CE    . MET   C 2 62  ? -34.19000 36.61600 -28.43900 1.000 17.08466 ? 61  MET   D CE    1 
ATOM   3270 N  N     . CYS   C 2 63  ? -37.28000 40.43600 -27.71400 1.000 13.78777 ? 62  CYS   D N     1 
ATOM   3271 C  CA    . CYS   C 2 63  ? -38.42900 39.55500 -27.52300 1.000 13.39563 ? 62  CYS   D CA    1 
ATOM   3272 C  C     . CYS   C 2 63  ? -38.80200 38.97200 -28.88200 1.000 11.37491 ? 62  CYS   D C     1 
ATOM   3273 O  O     . CYS   C 2 63  ? -39.09500 39.72600 -29.82300 1.000 13.90340 ? 62  CYS   D O     1 
ATOM   3274 C  CB    . CYS   C 2 63  ? -39.62000 40.35900 -27.00000 1.000 14.84826 ? 62  CYS   D CB    1 
ATOM   3275 S  SG    . CYS   C 2 63  ? -39.37000 41.14500 -25.40200 1.000 16.74535 ? 62  CYS   D SG    1 
ATOM   3276 N  N     . GLN   C 2 64  ? -38.80300 37.64100 -28.98400 1.000 11.67046 ? 63  GLN   D N     1 
ATOM   3277 C  CA    . GLN   C 2 64  ? -39.01700 36.94200 -30.24700 1.000 12.40790 ? 63  GLN   D CA    1 
ATOM   3278 C  C     . GLN   C 2 64  ? -40.27600 36.09100 -30.18000 1.000 12.40099 ? 63  GLN   D C     1 
ATOM   3279 O  O     . GLN   C 2 64  ? -40.51200 35.37800 -29.20300 1.000 12.63367 ? 63  GLN   D O     1 
ATOM   3280 C  CB    . GLN   C 2 64  ? -37.78400 36.09200 -30.58100 1.000 12.73348 ? 63  GLN   D CB    1 
ATOM   3281 C  CG    . GLN   C 2 64  ? -37.88700 35.29100 -31.87100 1.000 12.37299 ? 63  GLN   D CG    1 
ATOM   3282 C  CD    . GLN   C 2 64  ? -36.61300 34.51400 -32.17600 1.000 12.78361 ? 63  GLN   D CD    1 
ATOM   3283 O  OE1   . GLN   C 2 64  ? -35.53300 34.86300 -31.70300 1.000 14.24860 ? 63  GLN   D OE1   1 
ATOM   3284 N  NE2   . GLN   C 2 64  ? -36.73300 33.45500 -32.97800 1.000 13.32785 ? 63  GLN   D NE2   1 
ATOM   3285 N  N     . GLY   C 2 65  ? -41.06400 36.14000 -31.25300 1.000 11.68161 ? 64  GLY   D N     1 
ATOM   3286 C  CA    . GLY   C 2 65  ? -42.25500 35.31800 -31.33200 1.000 12.63411 ? 64  GLY   D CA    1 
ATOM   3287 C  C     . GLY   C 2 65  ? -42.61700 34.95900 -32.75400 1.000 11.77323 ? 64  GLY   D C     1 
ATOM   3288 O  O     . GLY   C 2 65  ? -41.76900 35.03800 -33.65700 1.000 13.33037 ? 64  GLY   D O     1 
ATOM   3289 N  N     . GLY   C 2 66  ? -43.87500 34.57500 -32.97900 1.000 13.96461 ? 65  GLY   D N     1 
ATOM   3290 C  CA    . GLY   C 2 66  ? -44.37000 34.37900 -34.32400 1.000 14.28223 ? 65  GLY   D CA    1 
ATOM   3291 C  C     . GLY   C 2 66  ? -44.55100 32.94700 -34.80700 1.000 14.01208 ? 65  GLY   D C     1 
ATOM   3292 O  O     . GLY   C 2 66  ? -44.92700 32.76300 -35.97200 1.000 15.60036 ? 65  GLY   D O     1 
ATOM   3293 N  N     . ASP   C 2 67  ? -44.31200 31.92700 -33.97300 1.000 12.93908 ? 66  ASP   D N     1 
ATOM   3294 C  CA    . ASP   C 2 67  ? -44.49400 30.53700 -34.42200 1.000 12.78877 ? 66  ASP   D CA    1 
ATOM   3295 C  C     . ASP   C 2 67  ? -45.92700 30.10800 -34.14700 1.000 13.04549 ? 66  ASP   D C     1 
ATOM   3296 O  O     . ASP   C 2 67  ? -46.23900 29.59700 -33.07200 1.000 14.99219 ? 66  ASP   D O     1 
ATOM   3297 C  CB    . ASP   C 2 67  ? -43.52600 29.58400 -33.73500 1.000 13.72655 ? 66  ASP   D CB    1 
ATOM   3298 C  CG    . ASP   C 2 67  ? -43.74500 28.13100 -34.13800 1.000 14.32180 ? 66  ASP   D CG    1 
ATOM   3299 O  OD1   . ASP   C 2 67  ? -44.63500 27.82300 -34.96800 1.000 15.02858 ? 66  ASP   D OD1   1 
ATOM   3300 O  OD2   . ASP   C 2 67  ? -42.99500 27.27600 -33.63700 1.000 14.52983 ? 66  ASP   D OD2   1 
ATOM   3301 N  N     . PHE   C 2 68  ? -46.79600 30.27800 -35.13700 1.000 12.84995 ? 67  PHE   D N     1 
ATOM   3302 C  CA    . PHE   C 2 68  ? -48.19100 29.86500 -35.03300 1.000 13.62520 ? 67  PHE   D CA    1 
ATOM   3303 C  C     . PHE   C 2 68  ? -48.46800 28.50800 -35.67100 1.000 13.64917 ? 67  PHE   D C     1 
ATOM   3304 O  O     . PHE   C 2 68  ? -49.62200 28.06800 -35.68200 1.000 14.68715 ? 67  PHE   D O     1 
ATOM   3305 C  CB    . PHE   C 2 68  ? -49.14700 30.94600 -35.58700 1.000 14.67140 ? 67  PHE   D CB    1 
ATOM   3306 C  CG    . PHE   C 2 68  ? -48.89700 31.29600 -37.01900 1.000 14.50893 ? 67  PHE   D CG    1 
ATOM   3307 C  CD1   . PHE   C 2 68  ? -49.41700 30.51400 -38.04400 1.000 16.00963 ? 67  PHE   D CD1   1 
ATOM   3308 C  CD2   . PHE   C 2 68  ? -48.18000 32.44200 -37.34000 1.000 16.27334 ? 67  PHE   D CD2   1 
ATOM   3309 C  CE1   . PHE   C 2 68  ? -49.19100 30.85400 -39.36700 1.000 17.28810 ? 67  PHE   D CE1   1 
ATOM   3310 C  CE2   . PHE   C 2 68  ? -47.95900 32.78800 -38.65700 1.000 17.34104 ? 67  PHE   D CE2   1 
ATOM   3311 C  CZ    . PHE   C 2 68  ? -48.45200 31.98900 -39.67100 1.000 17.71117 ? 67  PHE   D CZ    1 
ATOM   3312 N  N     . THR   C 2 69  ? -47.45300 27.84100 -36.21800 1.000 14.15543 ? 68  THR   D N     1 
ATOM   3313 C  CA    . THR   C 2 69  ? -47.68600 26.55200 -36.86200 1.000 15.75415 ? 68  THR   D CA    1 
ATOM   3314 C  C     . THR   C 2 69  ? -47.25400 25.37400 -36.00300 1.000 16.30900 ? 68  THR   D C     1 
ATOM   3315 O  O     . THR   C 2 69  ? -47.97700 24.38800 -35.90500 1.000 20.53933 ? 68  THR   D O     1 
ATOM   3316 C  CB    . THR   C 2 69  ? -47.03500 26.47200 -38.24800 1.000 16.50448 ? 68  THR   D CB    1 
ATOM   3317 O  OG1   . THR   C 2 69  ? -45.62000 26.53300 -38.10200 1.000 18.43657 ? 68  THR   D OG1   1 
ATOM   3318 C  CG2   . THR   C 2 69  ? -47.50500 27.59300 -39.15700 1.000 18.77766 ? 68  THR   D CG2   1 
ATOM   3319 N  N     . ARG   C 2 70  ? -46.07100 25.44100 -35.40500 1.000 15.35388 ? 69  ARG   D N     1 
ATOM   3320 C  CA    . ARG   C 2 70  ? -45.59600 24.36900 -34.54100 1.000 14.64543 ? 69  ARG   D CA    1 
ATOM   3321 C  C     . ARG   C 2 70  ? -45.69900 24.70900 -33.06100 1.000 14.26090 ? 69  ARG   D C     1 
ATOM   3322 O  O     . ARG   C 2 70  ? -45.64400 23.79500 -32.23400 1.000 17.19144 ? 69  ARG   D O     1 
ATOM   3323 C  CB    . ARG   C 2 70  ? -44.14100 24.01700 -34.87000 1.000 16.17418 ? 69  ARG   D CB    1 
ATOM   3324 C  CG    . ARG   C 2 70  ? -43.88700 23.56100 -36.29800 1.000 21.98149 ? 69  ARG   D CG    1 
ATOM   3325 C  CD    . ARG   C 2 70  ? -44.27600 22.10400 -36.51000 1.000 28.99269 ? 69  ARG   D CD    1 
ATOM   3326 N  NE    . ARG   C 2 70  ? -45.71200 21.92700 -36.69100 1.000 39.17898 ? 69  ARG   D NE    1 
ATOM   3327 C  CZ    . ARG   C 2 70  ? -46.34700 22.11700 -37.84100 1.000 45.57947 ? 69  ARG   D CZ    1 
ATOM   3328 N  NH1   . ARG   C 2 70  ? -45.70800 22.53400 -38.92200 1.000 49.21302 ? 69  ARG   D NH1   1 
ATOM   3329 N  NH2   . ARG   C 2 70  ? -47.65600 21.88800 -37.90700 1.000 47.28740 ? 69  ARG   D NH2   1 
ATOM   3330 N  N     . HIS   C 2 71  ? -45.86500 25.99200 -32.70900 1.000 14.56107 ? 70  HIS   D N     1 
ATOM   3331 C  CA    . HIS   C 2 71  ? -46.05300 26.40400 -31.31300 1.000 15.44814 ? 70  HIS   D CA    1 
ATOM   3332 C  C     . HIS   C 2 71  ? -44.88800 25.99000 -30.42100 1.000 16.58899 ? 70  HIS   D C     1 
ATOM   3333 O  O     . HIS   C 2 71  ? -45.06400 25.75400 -29.22200 1.000 18.93179 ? 70  HIS   D O     1 
ATOM   3334 C  CB    . HIS   C 2 71  ? -47.37900 25.86900 -30.75200 1.000 15.84030 ? 70  HIS   D CB    1 
ATOM   3335 C  CG    . HIS   C 2 71  ? -48.54600 26.08000 -31.66200 1.000 17.07664 ? 70  HIS   D CG    1 
ATOM   3336 N  ND1   . HIS   C 2 71  ? -49.29100 27.23700 -31.65600 1.000 16.71479 ? 70  HIS   D ND1   1 
ATOM   3337 C  CD2   . HIS   C 2 71  ? -49.09200 25.28500 -32.61500 1.000 18.30384 ? 70  HIS   D CD2   1 
ATOM   3338 C  CE1   . HIS   C 2 71  ? -50.24200 27.15000 -32.57100 1.000 18.68086 ? 70  HIS   D CE1   1 
ATOM   3339 N  NE2   . HIS   C 2 71  ? -50.14100 25.97600 -33.16800 1.000 18.43734 ? 70  HIS   D NE2   1 
ATOM   3340 N  N     . ASN   C 2 72  ? -43.68800 25.90200 -30.98500 1.000 14.93400 ? 71  ASN   D N     1 
ATOM   3341 C  CA    . ASN   C 2 72  ? -42.54500 25.46100 -30.19300 1.000 16.14913 ? 71  ASN   D CA    1 
ATOM   3342 C  C     . ASN   C 2 72  ? -41.26300 26.21000 -30.55000 1.000 16.17866 ? 71  ASN   D C     1 
ATOM   3343 O  O     . ASN   C 2 72  ? -40.16900 25.75000 -30.19400 1.000 16.83997 ? 71  ASN   D O     1 
ATOM   3344 C  CB    . ASN   C 2 72  ? -42.35800 23.93800 -30.29400 1.000 18.92483 ? 71  ASN   D CB    1 
ATOM   3345 C  CG    . ASN   C 2 72  ? -41.90900 23.50200 -31.66900 1.000 19.57513 ? 71  ASN   D CG    1 
ATOM   3346 O  OD1   . ASN   C 2 72  ? -41.69000 24.33200 -32.55300 1.000 17.67575 ? 71  ASN   D OD1   1 
ATOM   3347 N  ND2   . ASN   C 2 72  ? -41.79100 22.19500 -31.86700 1.000 22.90540 ? 71  ASN   D ND2   1 
ATOM   3348 N  N     . GLY   C 2 73  ? -41.36700 27.33600 -31.25100 1.000 14.73613 ? 72  GLY   D N     1 
ATOM   3349 C  CA    . GLY   C 2 73  ? -40.21200 28.12000 -31.63100 1.000 14.85019 ? 72  GLY   D CA    1 
ATOM   3350 C  C     . GLY   C 2 73  ? -39.51000 27.66600 -32.89300 1.000 14.97620 ? 72  GLY   D C     1 
ATOM   3351 O  O     . GLY   C 2 73  ? -38.52700 28.30200 -33.29600 1.000 14.90814 ? 72  GLY   D O     1 
ATOM   3352 N  N     . THR   C 2 74  ? -39.97500 26.60100 -33.54900 1.000 13.87857 ? 73  THR   D N     1 
ATOM   3353 C  CA    . THR   C 2 74  ? -39.30700 26.12700 -34.75000 1.000 15.88195 ? 73  THR   D CA    1 
ATOM   3354 C  C     . THR   C 2 74  ? -40.06200 26.44900 -36.02300 1.000 15.19768 ? 73  THR   D C     1 
ATOM   3355 O  O     . THR   C 2 74  ? -39.49700 26.28500 -37.10900 1.000 15.32929 ? 73  THR   D O     1 
ATOM   3356 C  CB    . THR   C 2 74  ? -39.06200 24.60700 -34.69600 1.000 15.05247 ? 73  THR   D CB    1 
ATOM   3357 O  OG1   . THR   C 2 74  ? -40.31700 23.89100 -34.75100 1.000 16.41566 ? 73  THR   D OG1   1 
ATOM   3358 C  CG2   . THR   C 2 74  ? -38.28100 24.23700 -33.45000 1.000 19.35827 ? 73  THR   D CG2   1 
ATOM   3359 N  N     . GLY   C 2 75  ? -41.31900 26.86200 -35.92600 1.000 14.41716 ? 74  GLY   D N     1 
ATOM   3360 C  CA    . GLY   C 2 75  ? -42.16400 26.91800 -37.09600 1.000 16.20395 ? 74  GLY   D CA    1 
ATOM   3361 C  C     . GLY   C 2 75  ? -42.50000 28.32200 -37.52400 1.000 16.72602 ? 74  GLY   D C     1 
ATOM   3362 O  O     . GLY   C 2 75  ? -41.75900 29.27000 -37.26100 1.000 15.64897 ? 74  GLY   D O     1 
ATOM   3363 N  N     . GLY   C 2 76  ? -43.65300 28.46200 -38.15700 1.000 21.64892 ? 75  GLY   D N     1 
ATOM   3364 C  CA    . GLY   C 2 76  ? -44.11100 29.67500 -38.79300 1.000 21.96274 ? 75  GLY   D CA    1 
ATOM   3365 C  C     . GLY   C 2 76  ? -44.12800 29.54700 -40.31100 1.000 20.07170 ? 75  GLY   D C     1 
ATOM   3366 O  O     . GLY   C 2 76  ? -43.51600 28.65800 -40.90500 1.000 22.48378 ? 75  GLY   D O     1 
ATOM   3367 N  N     . LYS   C 2 77  ? -44.85600 30.45800 -40.94100 1.000 17.49478 ? 76  LYS   D N     1 
ATOM   3368 C  CA    . LYS   C 2 77  ? -44.95900 30.49100 -42.39300 1.000 17.25059 ? 76  LYS   D CA    1 
ATOM   3369 C  C     . LYS   C 2 77  ? -45.39400 31.88800 -42.80800 1.000 16.65607 ? 76  LYS   D C     1 
ATOM   3370 O  O     . LYS   C 2 77  ? -45.99300 32.62500 -42.02300 1.000 15.94065 ? 76  LYS   D O     1 
ATOM   3371 C  CB    . LYS   C 2 77  ? -45.91900 29.42600 -42.93200 1.000 21.10726 ? 76  LYS   D CB    1 
ATOM   3372 C  CG    . LYS   C 2 77  ? -47.38200 29.63300 -42.63100 1.000 21.03811 ? 76  LYS   D CG    1 
ATOM   3373 C  CD    . LYS   C 2 77  ? -48.23500 28.53300 -43.24700 1.000 22.15237 ? 76  LYS   D CD    1 
ATOM   3374 C  CE    . LYS   C 2 77  ? -49.70200 28.72400 -42.96400 1.000 25.15813 ? 76  LYS   D CE    1 
ATOM   3375 N  NZ    . LYS   C 2 77  ? -50.56000 27.71000 -43.65400 1.000 26.78672 ? 76  LYS   D NZ    1 
ATOM   3376 N  N     . SER   C 2 78  ? -45.03700 32.26400 -44.02800 1.000 15.54063 ? 77  SER   D N     1 
ATOM   3377 C  CA    . SER   C 2 78  ? -45.38500 33.57200 -44.55900 1.000 13.96346 ? 77  SER   D CA    1 
ATOM   3378 C  C     . SER   C 2 78  ? -46.65700 33.47000 -45.39500 1.000 15.81350 ? 77  SER   D C     1 
ATOM   3379 O  O     . SER   C 2 78  ? -47.18900 32.38500 -45.64400 1.000 17.46334 ? 77  SER   D O     1 
ATOM   3380 C  CB    . SER   C 2 78  ? -44.23000 34.11300 -45.39900 1.000 15.59921 ? 77  SER   D CB    1 
ATOM   3381 O  OG    . SER   C 2 78  ? -44.25000 33.61600 -46.72400 1.000 17.47375 ? 77  SER   D OG    1 
ATOM   3382 N  N     . ILE   C 2 79  ? -47.15500 34.62700 -45.83600 1.000 16.91733 ? 78  ILE   D N     1 
ATOM   3383 C  CA    . ILE   C 2 79  ? -48.28700 34.65000 -46.76000 1.000 17.79070 ? 78  ILE   D CA    1 
ATOM   3384 C  C     . ILE   C 2 79  ? -47.87300 34.29800 -48.17600 1.000 19.33633 ? 78  ILE   D C     1 
ATOM   3385 O  O     . ILE   C 2 79  ? -48.74000 34.18500 -49.05300 1.000 21.39266 ? 78  ILE   D O     1 
ATOM   3386 C  CB    . ILE   C 2 79  ? -49.00700 36.01400 -46.74000 1.000 17.48138 ? 78  ILE   D CB    1 
ATOM   3387 C  CG1   . ILE   C 2 79  ? -48.11900 37.12300 -47.32700 1.000 18.79065 ? 78  ILE   D CG1   1 
ATOM   3388 C  CG2   . ILE   C 2 79  ? -49.44000 36.35300 -45.32600 1.000 17.60072 ? 78  ILE   D CG2   1 
ATOM   3389 C  CD1   . ILE   C 2 79  ? -48.85300 38.44000 -47.54400 1.000 18.26973 ? 78  ILE   D CD1   1 
ATOM   3390 N  N     . TYR   C 2 80  ? -46.57500 34.12300 -48.42100 1.000 17.99263 ? 79  TYR   D N     1 
ATOM   3391 C  CA    . TYR   C 2 80  ? -46.04100 33.82000 -49.74200 1.000 19.73062 ? 79  TYR   D CA    1 
ATOM   3392 C  C     . TYR   C 2 80  ? -45.61000 32.37100 -49.88800 1.000 21.53976 ? 79  TYR   D C     1 
ATOM   3393 O  O     . TYR   C 2 80  ? -45.13300 31.98000 -50.95900 1.000 25.86666 ? 79  TYR   D O     1 
ATOM   3394 C  CB    . TYR   C 2 80  ? -44.83600 34.72400 -50.04100 1.000 20.57521 ? 79  TYR   D CB    1 
ATOM   3395 C  CG    . TYR   C 2 80  ? -45.07600 36.20000 -49.78300 1.000 18.66663 ? 79  TYR   D CG    1 
ATOM   3396 C  CD1   . TYR   C 2 80  ? -45.97500 36.93200 -50.55600 1.000 19.67972 ? 79  TYR   D CD1   1 
ATOM   3397 C  CD2   . TYR   C 2 80  ? -44.38900 36.86900 -48.77700 1.000 18.22405 ? 79  TYR   D CD2   1 
ATOM   3398 C  CE1   . TYR   C 2 80  ? -46.19200 38.27900 -50.32100 1.000 18.55703 ? 79  TYR   D CE1   1 
ATOM   3399 C  CE2   . TYR   C 2 80  ? -44.59800 38.21900 -48.52900 1.000 18.04761 ? 79  TYR   D CE2   1 
ATOM   3400 C  CZ    . TYR   C 2 80  ? -45.50600 38.91800 -49.30700 1.000 18.53624 ? 79  TYR   D CZ    1 
ATOM   3401 O  OH    . TYR   C 2 80  ? -45.72900 40.25400 -49.08400 1.000 18.53253 ? 79  TYR   D OH    1 
ATOM   3402 N  N     . GLY   C 2 81  ? -45.75900 31.56900 -48.85100 1.000 20.01398 ? 80  GLY   D N     1 
ATOM   3403 C  CA    . GLY   C 2 81  ? -45.23600 30.22500 -48.80800 1.000 21.01496 ? 80  GLY   D CA    1 
ATOM   3404 C  C     . GLY   C 2 81  ? -44.49100 30.02700 -47.51800 1.000 17.17360 ? 80  GLY   D C     1 
ATOM   3405 O  O     . GLY   C 2 81  ? -44.52800 30.86500 -46.60800 1.000 19.10800 ? 80  GLY   D O     1 
ATOM   3406 N  N     . GLU   C 2 82  ? -43.78700 28.91000 -47.42100 1.000 17.59447 ? 81  GLU   D N     1 
ATOM   3407 C  CA    . GLU   C 2 82  ? -43.11800 28.62700 -46.16200 1.000 16.31407 ? 81  GLU   D CA    1 
ATOM   3408 C  C     . GLU   C 2 82  ? -42.03900 29.65300 -45.86300 1.000 17.17899 ? 81  GLU   D C     1 
ATOM   3409 O  O     . GLU   C 2 82  ? -41.80700 29.98000 -44.69600 1.000 20.46408 ? 81  GLU   D O     1 
ATOM   3410 C  CB    . GLU   C 2 82  ? -42.54100 27.22300 -46.18700 1.000 18.18219 ? 81  GLU   D CB    1 
ATOM   3411 C  CG    . GLU   C 2 82  ? -43.60900 26.13900 -46.14000 1.000 18.11085 ? 81  GLU   D CG    1 
ATOM   3412 C  CD    . GLU   C 2 82  ? -43.02500 24.74400 -46.16400 1.000 18.98297 ? 81  GLU   D CD    1 
ATOM   3413 O  OE1   . GLU   C 2 82  ? -41.78300 24.62200 -46.04400 1.000 21.45534 ? 81  GLU   D OE1   1 
ATOM   3414 O  OE2   . GLU   C 2 82  ? -43.79300 23.76000 -46.32300 1.000 20.55936 ? 81  GLU   D OE2   1 
ATOM   3415 N  N     . LYS   C 2 83  ? -41.37400 30.15400 -46.89100 1.000 16.18050 ? 82  LYS   D N     1 
ATOM   3416 C  CA    . LYS   C 2 83  ? -40.25300 31.06800 -46.73700 1.000 18.33166 ? 82  LYS   D CA    1 
ATOM   3417 C  C     . LYS   C 2 83  ? -40.29300 32.09000 -47.85900 1.000 17.96174 ? 82  LYS   D C     1 
ATOM   3418 O  O     . LYS   C 2 83  ? -40.83800 31.83800 -48.93600 1.000 19.23678 ? 82  LYS   D O     1 
ATOM   3419 C  CB    . LYS   C 2 83  ? -38.90300 30.32600 -46.82600 1.000 24.93420 ? 82  LYS   D CB    1 
ATOM   3420 C  CG    . LYS   C 2 83  ? -38.47600 29.53200 -45.59500 1.000 35.99883 ? 82  LYS   D CG    1 
ATOM   3421 C  CD    . LYS   C 2 83  ? -39.04900 28.11700 -45.55000 1.000 43.07530 ? 82  LYS   D CD    1 
ATOM   3422 C  CE    . LYS   C 2 83  ? -38.38000 27.27400 -44.46300 1.000 46.96033 ? 82  LYS   D CE    1 
ATOM   3423 N  NZ    . LYS   C 2 83  ? -38.41900 27.91500 -43.12300 1.000 46.68748 ? 82  LYS   D NZ    1 
ATOM   3424 N  N     . PHE   C 2 84  ? -39.68500 33.24400 -47.61400 1.000 16.35680 ? 83  PHE   D N     1 
ATOM   3425 C  CA    . PHE   C 2 84  ? -39.48300 34.22300 -48.67700 1.000 16.22655 ? 83  PHE   D CA    1 
ATOM   3426 C  C     . PHE   C 2 84  ? -38.12400 34.89300 -48.51800 1.000 16.75433 ? 83  PHE   D C     1 
ATOM   3427 O  O     . PHE   C 2 84  ? -37.51300 34.87800 -47.44300 1.000 15.50722 ? 83  PHE   D O     1 
ATOM   3428 C  CB    . PHE   C 2 84  ? -40.65300 35.22100 -48.84300 1.000 16.99441 ? 83  PHE   D CB    1 
ATOM   3429 C  CG    . PHE   C 2 84  ? -40.85300 36.16400 -47.67300 1.000 16.78866 ? 83  PHE   D CG    1 
ATOM   3430 C  CD1   . PHE   C 2 84  ? -41.43700 35.72800 -46.49000 1.000 18.12345 ? 83  PHE   D CD1   1 
ATOM   3431 C  CD2   . PHE   C 2 84  ? -40.49700 37.50100 -47.77300 1.000 17.84638 ? 83  PHE   D CD2   1 
ATOM   3432 C  CE1   . PHE   C 2 84  ? -41.64600 36.60400 -45.42300 1.000 15.99388 ? 83  PHE   D CE1   1 
ATOM   3433 C  CE2   . PHE   C 2 84  ? -40.68700 38.38800 -46.71100 1.000 16.91305 ? 83  PHE   D CE2   1 
ATOM   3434 C  CZ    . PHE   C 2 84  ? -41.27500 37.94300 -45.53200 1.000 16.86575 ? 83  PHE   D CZ    1 
ATOM   3435 N  N     . GLU   C 2 85  ? -37.66200 35.49900 -49.60700 1.000 17.94541 ? 84  GLU   D N     1 
ATOM   3436 C  CA    . GLU   C 2 85  ? -36.30100 36.00800 -49.64700 1.000 18.72039 ? 84  GLU   D CA    1 
ATOM   3437 C  C     . GLU   C 2 85  ? -36.15400 37.26200 -48.78500 1.000 16.82627 ? 84  GLU   D C     1 
ATOM   3438 O  O     . GLU   C 2 85  ? -37.12400 37.96600 -48.48200 1.000 18.61152 ? 84  GLU   D O     1 
ATOM   3439 C  CB    . GLU   C 2 85  ? -35.88100 36.32200 -51.08300 1.000 24.51543 ? 84  GLU   D CB    1 
ATOM   3440 C  CG    . GLU   C 2 85  ? -36.71800 37.36900 -51.78200 1.000 35.11266 ? 84  GLU   D CG    1 
ATOM   3441 C  CD    . GLU   C 2 85  ? -36.31500 37.54700 -53.24000 1.000 44.22582 ? 84  GLU   D CD    1 
ATOM   3442 O  OE1   . GLU   C 2 85  ? -35.79700 36.58000 -53.84800 1.000 46.58717 ? 84  GLU   D OE1   1 
ATOM   3443 O  OE2   . GLU   C 2 85  ? -36.51500 38.65500 -53.78200 1.000 47.91688 ? 84  GLU   D OE2   1 
ATOM   3444 N  N     . ASP   C 2 86  ? -34.91000 37.53000 -48.38700 1.000 16.91959 ? 85  ASP   D N     1 
ATOM   3445 C  CA    . ASP   C 2 86  ? -34.56600 38.80900 -47.77200 1.000 15.71662 ? 85  ASP   D CA    1 
ATOM   3446 C  C     . ASP   C 2 86  ? -34.78100 39.94500 -48.76800 1.000 17.53959 ? 85  ASP   D C     1 
ATOM   3447 O  O     . ASP   C 2 86  ? -34.10800 40.01900 -49.79800 1.000 19.09313 ? 85  ASP   D O     1 
ATOM   3448 C  CB    . ASP   C 2 86  ? -33.11100 38.77300 -47.31900 1.000 17.16317 ? 85  ASP   D CB    1 
ATOM   3449 C  CG    . ASP   C 2 86  ? -32.86000 37.72200 -46.25800 1.000 15.26581 ? 85  ASP   D CG    1 
ATOM   3450 O  OD1   . ASP   C 2 86  ? -33.66300 37.64100 -45.30100 1.000 16.48426 ? 85  ASP   D OD1   1 
ATOM   3451 O  OD2   . ASP   C 2 86  ? -31.84400 36.98700 -46.34800 1.000 16.62460 ? 85  ASP   D OD2   1 
ATOM   3452 N  N     . GLU   C 2 87  ? -35.72000 40.83100 -48.45400 1.000 17.01179 ? 86  GLU   D N     1 
ATOM   3453 C  CA    . GLU   C 2 87  ? -36.15400 41.85300 -49.39900 1.000 19.09250 ? 86  GLU   D CA    1 
ATOM   3454 C  C     . GLU   C 2 87  ? -35.08800 42.92000 -49.59300 1.000 17.99653 ? 86  GLU   D C     1 
ATOM   3455 O  O     . GLU   C 2 87  ? -34.73800 43.25800 -50.72700 1.000 18.69589 ? 86  GLU   D O     1 
ATOM   3456 C  CB    . GLU   C 2 87  ? -37.45800 42.47100 -48.90200 1.000 19.01926 ? 86  GLU   D CB    1 
ATOM   3457 C  CG    . GLU   C 2 87  ? -38.04900 43.46400 -49.85700 1.000 19.41229 ? 86  GLU   D CG    1 
ATOM   3458 C  CD    . GLU   C 2 87  ? -39.41800 43.89900 -49.43700 1.000 17.79763 ? 86  GLU   D CD    1 
ATOM   3459 O  OE1   . GLU   C 2 87  ? -39.80500 43.60900 -48.28900 1.000 18.98219 ? 86  GLU   D OE1   1 
ATOM   3460 O  OE2   . GLU   C 2 87  ? -40.11000 44.54200 -50.24400 1.000 20.80187 ? 86  GLU   D OE2   1 
ATOM   3461 N  N     . ASN   C 2 88  ? -34.59300 43.49200 -48.50200 1.000 16.29945 ? 87  ASN   D N     1 
ATOM   3462 C  CA    . ASN   C 2 88  ? -33.49400 44.44700 -48.57400 1.000 16.58003 ? 87  ASN   D CA    1 
ATOM   3463 C  C     . ASN   C 2 88  ? -32.92400 44.57100 -47.17300 1.000 17.24657 ? 87  ASN   D C     1 
ATOM   3464 O  O     . ASN   C 2 88  ? -33.51900 44.10400 -46.20200 1.000 17.97233 ? 87  ASN   D O     1 
ATOM   3465 C  CB    . ASN   C 2 88  ? -33.90800 45.80700 -49.17200 1.000 17.71498 ? 87  ASN   D CB    1 
ATOM   3466 C  CG    . ASN   C 2 88  ? -34.87800 46.57200 -48.30100 1.000 18.09001 ? 87  ASN   D CG    1 
ATOM   3467 O  OD1   . ASN   C 2 88  ? -34.57900 46.88400 -47.15300 1.000 18.44037 ? 87  ASN   D OD1   1 
ATOM   3468 N  ND2   . ASN   C 2 88  ? -36.03600 46.91400 -48.85900 1.000 18.53270 ? 87  ASN   D ND2   1 
ATOM   3469 N  N     . PHE   C 2 89  ? -31.76000 45.20800 -47.07600 1.000 18.07544 ? 88  PHE   D N     1 
ATOM   3470 C  CA    . PHE   C 2 89  ? -31.17000 45.50500 -45.77800 1.000 18.29411 ? 88  PHE   D CA    1 
ATOM   3471 C  C     . PHE   C 2 89  ? -31.00000 47.00600 -45.59400 1.000 19.57154 ? 88  PHE   D C     1 
ATOM   3472 O  O     . PHE   C 2 89  ? -30.03500 47.47800 -44.99100 1.000 20.16906 ? 88  PHE   D O     1 
ATOM   3473 C  CB    . PHE   C 2 89  ? -29.87000 44.73500 -45.55700 1.000 18.90880 ? 88  PHE   D CB    1 
ATOM   3474 C  CG    . PHE   C 2 89  ? -30.04400 43.25200 -45.62100 1.000 17.89772 ? 88  PHE   D CG    1 
ATOM   3475 C  CD1   . PHE   C 2 89  ? -30.73300 42.57700 -44.61300 1.000 18.49693 ? 88  PHE   D CD1   1 
ATOM   3476 C  CD2   . PHE   C 2 89  ? -29.51500 42.52500 -46.67300 1.000 21.61374 ? 88  PHE   D CD2   1 
ATOM   3477 C  CE1   . PHE   C 2 89  ? -30.89400 41.20500 -44.66300 1.000 17.56734 ? 88  PHE   D CE1   1 
ATOM   3478 C  CE2   . PHE   C 2 89  ? -29.68100 41.15900 -46.73500 1.000 21.34880 ? 88  PHE   D CE2   1 
ATOM   3479 C  CZ    . PHE   C 2 89  ? -30.36100 40.49800 -45.73300 1.000 20.42424 ? 88  PHE   D CZ    1 
ATOM   3480 N  N     . ILE   C 2 90  ? -31.97400 47.77200 -46.08800 1.000 18.74598 ? 89  ILE   D N     1 
ATOM   3481 C  CA    . ILE   C 2 90  ? -31.87000 49.23000 -46.04200 1.000 19.15395 ? 89  ILE   D CA    1 
ATOM   3482 C  C     . ILE   C 2 90  ? -31.82700 49.72900 -44.60700 1.000 20.19747 ? 89  ILE   D C     1 
ATOM   3483 O  O     . ILE   C 2 90  ? -31.01600 50.59600 -44.25800 1.000 23.78838 ? 89  ILE   D O     1 
ATOM   3484 C  CB    . ILE   C 2 90  ? -33.01800 49.87600 -46.83300 1.000 19.14954 ? 89  ILE   D CB    1 
ATOM   3485 C  CG1   . ILE   C 2 90  ? -32.83200 49.63900 -48.33000 1.000 21.16648 ? 89  ILE   D CG1   1 
ATOM   3486 C  CG2   . ILE   C 2 90  ? -33.06700 51.35500 -46.53500 1.000 21.48923 ? 89  ILE   D CG2   1 
ATOM   3487 C  CD1   . ILE   C 2 90  ? -34.07500 49.92500 -49.12400 1.000 23.93384 ? 89  ILE   D CD1   1 
ATOM   3488 N  N     . LEU   C 2 91  ? -32.69400 49.20100 -43.75800 1.000 19.23803 ? 90  LEU   D N     1 
ATOM   3489 C  CA    . LEU   C 2 91  ? -32.82900 49.68700 -42.39800 1.000 17.82747 ? 90  LEU   D CA    1 
ATOM   3490 C  C     . LEU   C 2 91  ? -31.99100 48.84500 -41.44200 1.000 18.77309 ? 90  LEU   D C     1 
ATOM   3491 O  O     . LEU   C 2 91  ? -31.78600 47.64200 -41.64500 1.000 18.40060 ? 90  LEU   D O     1 
ATOM   3492 C  CB    . LEU   C 2 91  ? -34.29600 49.65600 -41.98300 1.000 18.09952 ? 90  LEU   D CB    1 
ATOM   3493 C  CG    . LEU   C 2 91  ? -35.18500 50.58200 -42.81700 1.000 19.38566 ? 90  LEU   D CG    1 
ATOM   3494 C  CD1   . LEU   C 2 91  ? -36.61800 50.33700 -42.46700 1.000 20.56969 ? 90  LEU   D CD1   1 
ATOM   3495 C  CD2   . LEU   C 2 91  ? -34.83500 52.03400 -42.59800 1.000 21.15750 ? 90  LEU   D CD2   1 
ATOM   3496 N  N     . LYS   C 2 92  ? -31.51600 49.48700 -40.38500 1.000 19.06364 ? 91  LYS   D N     1 
ATOM   3497 C  CA    . LYS   C 2 92  ? -30.57400 48.87100 -39.46700 1.000 19.59355 ? 91  LYS   D CA    1 
ATOM   3498 C  C     . LYS   C 2 92  ? -31.18400 48.74500 -38.07500 1.000 16.88283 ? 91  LYS   D C     1 
ATOM   3499 O  O     . LYS   C 2 92  ? -32.19300 49.37800 -37.73500 1.000 17.84082 ? 91  LYS   D O     1 
ATOM   3500 C  CB    . LYS   C 2 92  ? -29.25900 49.66500 -39.41200 1.000 21.56792 ? 91  LYS   D CB    1 
ATOM   3501 C  CG    . LYS   C 2 92  ? -28.65000 50.00000 -40.76800 1.000 26.88700 ? 91  LYS   D CG    1 
ATOM   3502 C  CD    . LYS   C 2 92  ? -28.32600 48.77600 -41.61200 1.000 30.94021 ? 91  LYS   D CD    1 
ATOM   3503 C  CE    . LYS   C 2 92  ? -27.59000 49.20900 -42.88100 1.000 33.07466 ? 91  LYS   D CE    1 
ATOM   3504 N  NZ    . LYS   C 2 92  ? -27.38400 48.11200 -43.87900 1.000 35.77606 ? 91  LYS   D NZ    1 
ATOM   3505 N  N     . HIS   C 2 93  ? -30.53100 47.91300 -37.26100 1.000 17.04593 ? 92  HIS   D N     1 
ATOM   3506 C  CA    . HIS   C 2 93  ? -30.96800 47.63600 -35.89500 1.000 16.71908 ? 92  HIS   D CA    1 
ATOM   3507 C  C     . HIS   C 2 93  ? -30.32100 48.70100 -35.01200 1.000 19.52529 ? 92  HIS   D C     1 
ATOM   3508 O  O     . HIS   C 2 93  ? -29.28200 48.48900 -34.37900 1.000 25.03031 ? 92  HIS   D O     1 
ATOM   3509 C  CB    . HIS   C 2 93  ? -30.56800 46.22400 -35.46400 1.000 16.61967 ? 92  HIS   D CB    1 
ATOM   3510 C  CG    . HIS   C 2 93  ? -31.11300 45.12900 -36.33300 1.000 15.25865 ? 92  HIS   D CG    1 
ATOM   3511 N  ND1   . HIS   C 2 93  ? -30.56300 44.81000 -37.55700 1.000 15.39758 ? 92  HIS   D ND1   1 
ATOM   3512 C  CD2   . HIS   C 2 93  ? -32.16400 44.28400 -36.16200 1.000 15.72274 ? 92  HIS   D CD2   1 
ATOM   3513 C  CE1   . HIS   C 2 93  ? -31.23700 43.80100 -38.09000 1.000 15.40845 ? 92  HIS   D CE1   1 
ATOM   3514 N  NE2   . HIS   C 2 93  ? -32.21800 43.46600 -37.26800 1.000 14.85052 ? 92  HIS   D NE2   1 
ATOM   3515 N  N     . THR   C 2 94  ? -30.95400 49.87500 -34.97100 1.000 18.42567 ? 93  THR   D N     1 
ATOM   3516 C  CA    . THR   C 2 94  ? -30.35000 51.05500 -34.35900 1.000 20.61481 ? 93  THR   D CA    1 
ATOM   3517 C  C     . THR   C 2 94  ? -30.66300 51.22700 -32.87900 1.000 21.14280 ? 93  THR   D C     1 
ATOM   3518 O  O     . THR   C 2 94  ? -30.04300 52.08100 -32.23600 1.000 24.33911 ? 93  THR   D O     1 
ATOM   3519 C  CB    . THR   C 2 94  ? -30.77600 52.32900 -35.09700 1.000 20.32057 ? 93  THR   D CB    1 
ATOM   3520 O  OG1   . THR   C 2 94  ? -32.20300 52.34700 -35.20100 1.000 22.51333 ? 93  THR   D OG1   1 
ATOM   3521 C  CG2   . THR   C 2 94  ? -30.16800 52.37200 -36.48500 1.000 23.09965 ? 93  THR   D CG2   1 
ATOM   3522 N  N     . GLY   C 2 95  ? -31.60500 50.47200 -32.31600 1.000 19.62606 ? 94  GLY   D N     1 
ATOM   3523 C  CA    . GLY   C 2 95  ? -31.94800 50.65100 -30.92400 1.000 19.90869 ? 94  GLY   D CA    1 
ATOM   3524 C  C     . GLY   C 2 95  ? -33.22000 49.94700 -30.50000 1.000 17.81770 ? 94  GLY   D C     1 
ATOM   3525 O  O     . GLY   C 2 95  ? -33.80200 49.15700 -31.24500 1.000 17.00608 ? 94  GLY   D O     1 
ATOM   3526 N  N     . PRO   C 2 96  ? -33.65800 50.20400 -29.26700 1.000 18.93660 ? 95  PRO   D N     1 
ATOM   3527 C  CA    . PRO   C 2 96  ? -34.88400 49.56800 -28.77000 1.000 18.98727 ? 95  PRO   D CA    1 
ATOM   3528 C  C     . PRO   C 2 96  ? -36.07900 49.89800 -29.64900 1.000 18.47870 ? 95  PRO   D C     1 
ATOM   3529 O  O     . PRO   C 2 96  ? -36.19300 51.00300 -30.19000 1.000 21.36323 ? 95  PRO   D O     1 
ATOM   3530 C  CB    . PRO   C 2 96  ? -35.04700 50.15400 -27.36200 1.000 21.43803 ? 95  PRO   D CB    1 
ATOM   3531 C  CG    . PRO   C 2 96  ? -33.67300 50.59600 -26.97400 1.000 22.68817 ? 95  PRO   D CG    1 
ATOM   3532 C  CD    . PRO   C 2 96  ? -32.99900 51.04200 -28.25000 1.000 20.94556 ? 95  PRO   D CD    1 
ATOM   3533 N  N     . GLY   C 2 97  ? -36.96700 48.91500 -29.80300 1.000 16.48430 ? 96  GLY   D N     1 
ATOM   3534 C  CA    . GLY   C 2 97  ? -38.20200 49.09200 -30.53700 1.000 16.34435 ? 96  GLY   D CA    1 
ATOM   3535 C  C     . GLY   C 2 97  ? -38.15900 48.67100 -31.99100 1.000 15.42773 ? 96  GLY   D C     1 
ATOM   3536 O  O     . GLY   C 2 97  ? -39.21500 48.62300 -32.63700 1.000 16.50469 ? 96  GLY   D O     1 
ATOM   3537 N  N     . ILE   C 2 98  ? -36.97400 48.41100 -32.54900 1.000 15.52412 ? 97  ILE   D N     1 
ATOM   3538 C  CA    . ILE   C 2 98  ? -36.88200 47.93600 -33.92700 1.000 15.74309 ? 97  ILE   D CA    1 
ATOM   3539 C  C     . ILE   C 2 98  ? -37.56800 46.57800 -34.07100 1.000 15.37480 ? 97  ILE   D C     1 
ATOM   3540 O  O     . ILE   C 2 98  ? -37.37800 45.67200 -33.24900 1.000 15.90457 ? 97  ILE   D O     1 
ATOM   3541 C  CB    . ILE   C 2 98  ? -35.39700 47.87600 -34.32600 1.000 16.50689 ? 97  ILE   D CB    1 
ATOM   3542 C  CG1   . ILE   C 2 98  ? -34.81800 49.29100 -34.49100 1.000 18.51852 ? 97  ILE   D CG1   1 
ATOM   3543 C  CG2   . ILE   C 2 98  ? -35.21500 47.03800 -35.58300 1.000 17.41637 ? 97  ILE   D CG2   1 
ATOM   3544 C  CD1   . ILE   C 2 98  ? -35.43900 50.11600 -35.63100 1.000 22.35319 ? 97  ILE   D CD1   1 
ATOM   3545 N  N     . LEU   C 2 99  ? -38.34600 46.42500 -35.14600 1.000 13.02953 ? 98  LEU   D N     1 
ATOM   3546 C  CA    . LEU   C 2 99  ? -39.04000 45.19000 -35.50100 1.000 14.14963 ? 98  LEU   D CA    1 
ATOM   3547 C  C     . LEU   C 2 99  ? -38.36400 44.58600 -36.73200 1.000 12.68466 ? 98  LEU   D C     1 
ATOM   3548 O  O     . LEU   C 2 99  ? -38.21600 45.25600 -37.76500 1.000 13.88785 ? 98  LEU   D O     1 
ATOM   3549 C  CB    . LEU   C 2 99  ? -40.51100 45.50100 -35.78400 1.000 14.47837 ? 98  LEU   D CB    1 
ATOM   3550 C  CG    . LEU   C 2 99  ? -41.42800 44.35100 -36.21000 1.000 14.00619 ? 98  LEU   D CG    1 
ATOM   3551 C  CD1   . LEU   C 2 99  ? -41.53300 43.28800 -35.10200 1.000 16.66273 ? 98  LEU   D CD1   1 
ATOM   3552 C  CD2   . LEU   C 2 99  ? -42.79200 44.91400 -36.58900 1.000 15.23732 ? 98  LEU   D CD2   1 
ATOM   3553 N  N     . SER   C 2 100 ? -37.94300 43.33200 -36.61600 1.000 12.62797 ? 99  SER   D N     1 
ATOM   3554 C  CA    . SER   C 2 100 ? -37.08500 42.70900 -37.60500 1.000 12.85616 ? 99  SER   D CA    1 
ATOM   3555 C  C     . SER   C 2 100 ? -37.46400 41.23300 -37.74200 1.000 13.74759 ? 99  SER   D C     1 
ATOM   3556 O  O     . SER   C 2 100 ? -38.03100 40.62400 -36.82600 1.000 12.74856 ? 99  SER   D O     1 
ATOM   3557 C  CB    . SER   C 2 100 ? -35.61500 42.88700 -37.18400 1.000 14.29803 ? 99  SER   D CB    1 
ATOM   3558 O  OG    . SER   C 2 100 ? -34.73600 42.34400 -38.14500 1.000 14.13170 ? 99  SER   D OG    1 
ATOM   3559 N  N     . MET   C 2 101 ? -37.13600 40.64800 -38.89600 1.000 12.06610 ? 100 MET   D N     1 
ATOM   3560 C  CA    . MET   C 2 101 ? -37.46900 39.24800 -39.16700 1.000 12.62838 ? 100 MET   D CA    1 
ATOM   3561 C  C     . MET   C 2 101 ? -36.44100 38.30500 -38.55600 1.000 13.15455 ? 100 MET   D C     1 
ATOM   3562 O  O     . MET   C 2 101 ? -35.23200 38.48400 -38.72600 1.000 14.07366 ? 100 MET   D O     1 
ATOM   3563 C  CB    . MET   C 2 101 ? -37.56900 38.97100 -40.66400 1.000 13.65866 ? 100 MET   D CB    1 
ATOM   3564 C  CG    . MET   C 2 101 ? -38.77600 39.59900 -41.35600 1.000 15.27289 ? 100 MET   D CG    1 
ATOM   3565 S  SD    . MET   C 2 101 ? -40.35800 39.17900 -40.59100 1.000 14.82959 ? 100 MET   D SD    1 
ATOM   3566 C  CE    . MET   C 2 101 ? -40.60700 37.53500 -41.19100 1.000 16.37852 ? 100 MET   D CE    1 
ATOM   3567 N  N     . ALA   C 2 102 ? -36.92800 37.27700 -37.86600 1.000 12.07685 ? 101 ALA   D N     1 
ATOM   3568 C  CA    . ALA   C 2 102 ? -36.08300 36.16400 -37.46600 1.000 11.06900 ? 101 ALA   D CA    1 
ATOM   3569 C  C     . ALA   C 2 102 ? -35.89300 35.25200 -38.67600 1.000 12.12424 ? 101 ALA   D C     1 
ATOM   3570 O  O     . ALA   C 2 102 ? -36.68300 35.27600 -39.62500 1.000 13.90087 ? 101 ALA   D O     1 
ATOM   3571 C  CB    . ALA   C 2 102 ? -36.75700 35.38400 -36.33100 1.000 12.39091 ? 101 ALA   D CB    1 
ATOM   3572 N  N     . ASN   C 2 103 ? -34.82100 34.45900 -38.66600 1.000 12.91955 ? 102 ASN   D N     1 
ATOM   3573 C  CA    . ASN   C 2 103 ? -34.61100 33.56600 -39.80500 1.000 13.46530 ? 102 ASN   D CA    1 
ATOM   3574 C  C     . ASN   C 2 103 ? -33.66000 32.44600 -39.40600 1.000 13.43259 ? 102 ASN   D C     1 
ATOM   3575 O  O     . ASN   C 2 103 ? -33.09400 32.43900 -38.30700 1.000 14.52803 ? 102 ASN   D O     1 
ATOM   3576 C  CB    . ASN   C 2 103 ? -34.12900 34.33700 -41.04700 1.000 13.53308 ? 102 ASN   D CB    1 
ATOM   3577 C  CG    . ASN   C 2 103 ? -32.76100 34.94900 -40.85800 1.000 14.87922 ? 102 ASN   D CG    1 
ATOM   3578 O  OD1   . ASN   C 2 103 ? -31.82200 34.27700 -40.40500 1.000 14.56850 ? 102 ASN   D OD1   1 
ATOM   3579 N  ND2   . ASN   C 2 103 ? -32.64200 36.23700 -41.17900 1.000 15.13066 ? 102 ASN   D ND2   1 
ATOM   3580 N  N     . ALA   C 2 104 ? -33.47600 31.50700 -40.33000 1.000 14.38965 ? 103 ALA   D N     1 
ATOM   3581 C  CA    . ALA   C 2 104 ? -32.55200 30.39300 -40.15200 1.000 14.93203 ? 103 ALA   D CA    1 
ATOM   3582 C  C     . ALA   C 2 104 ? -31.44800 30.44900 -41.19700 1.000 17.54544 ? 103 ALA   D C     1 
ATOM   3583 O  O     . ALA   C 2 104 ? -30.98500 29.41400 -41.69500 1.000 21.35756 ? 103 ALA   D O     1 
ATOM   3584 C  CB    . ALA   C 2 104 ? -33.28900 29.05400 -40.21200 1.000 15.92578 ? 103 ALA   D CB    1 
ATOM   3585 N  N     . GLY   C 2 105 ? -31.02200 31.65600 -41.55300 1.000 15.95224 ? 104 GLY   D N     1 
ATOM   3586 C  CA    . GLY   C 2 105 ? -30.05500 31.84900 -42.61200 1.000 16.52069 ? 104 GLY   D CA    1 
ATOM   3587 C  C     . GLY   C 2 105 ? -30.63000 32.65100 -43.76200 1.000 15.61598 ? 104 GLY   D C     1 
ATOM   3588 O  O     . GLY   C 2 105 ? -31.77500 33.09600 -43.71000 1.000 15.96191 ? 104 GLY   D O     1 
ATOM   3589 N  N     . PRO   C 2 106 ? -29.85900 32.83400 -44.83600 1.000 17.83623 ? 105 PRO   D N     1 
ATOM   3590 C  CA    . PRO   C 2 106 ? -30.32000 33.69700 -45.92800 1.000 17.70990 ? 105 PRO   D CA    1 
ATOM   3591 C  C     . PRO   C 2 106 ? -31.62100 33.20600 -46.54400 1.000 15.50243 ? 105 PRO   D C     1 
ATOM   3592 O  O     . PRO   C 2 106 ? -31.80300 32.00900 -46.80300 1.000 17.83095 ? 105 PRO   D O     1 
ATOM   3593 C  CB    . PRO   C 2 106 ? -29.17400 33.62800 -46.94200 1.000 19.73343 ? 105 PRO   D CB    1 
ATOM   3594 C  CG    . PRO   C 2 106 ? -27.96100 33.30200 -46.13400 1.000 20.40684 ? 105 PRO   D CG    1 
ATOM   3595 C  CD    . PRO   C 2 106 ? -28.45800 32.41200 -45.00900 1.000 19.29375 ? 105 PRO   D CD    1 
ATOM   3596 N  N     . ASN   C 2 107 ? -32.51900 34.15300 -46.80300 1.000 15.82667 ? 106 ASN   D N     1 
ATOM   3597 C  CA    . ASN   C 2 107 ? -33.73500 33.89500 -47.57700 1.000 16.60758 ? 106 ASN   D CA    1 
ATOM   3598 C  C     . ASN   C 2 107 ? -34.62600 32.82100 -46.94300 1.000 17.04502 ? 106 ASN   D C     1 
ATOM   3599 O  O     . ASN   C 2 107 ? -35.14900 31.94000 -47.62900 1.000 17.87656 ? 106 ASN   D O     1 
ATOM   3600 C  CB    . ASN   C 2 107 ? -33.38900 33.56600 -49.03400 1.000 17.73218 ? 106 ASN   D CB    1 
ATOM   3601 C  CG    . ASN   C 2 107 ? -32.53300 34.64400 -49.66100 1.000 18.37096 ? 106 ASN   D CG    1 
ATOM   3602 O  OD1   . ASN   C 2 107 ? -32.88600 35.81900 -49.63200 1.000 18.81451 ? 106 ASN   D OD1   1 
ATOM   3603 N  ND2   . ASN   C 2 107 ? -31.36800 34.26400 -50.15700 1.000 22.70215 ? 106 ASN   D ND2   1 
ATOM   3604 N  N     . THR   C 2 108 ? -34.82200 32.91500 -45.61600 1.000 16.03135 ? 107 THR   D N     1 
ATOM   3605 C  CA    . THR   C 2 108 ? -35.66100 31.96100 -44.89100 1.000 15.15690 ? 107 THR   D CA    1 
ATOM   3606 C  C     . THR   C 2 108 ? -36.70900 32.67300 -44.04700 1.000 14.80953 ? 107 THR   D C     1 
ATOM   3607 O  O     . THR   C 2 108 ? -37.15500 32.14400 -43.03500 1.000 18.00326 ? 107 THR   D O     1 
ATOM   3608 C  CB    . THR   C 2 108 ? -34.83300 30.98800 -44.03800 1.000 15.25370 ? 107 THR   D CB    1 
ATOM   3609 O  OG1   . THR   C 2 108 ? -34.04900 31.71200 -43.06800 1.000 15.69335 ? 107 THR   D OG1   1 
ATOM   3610 C  CG2   . THR   C 2 108 ? -33.93600 30.10200 -44.92200 1.000 15.71821 ? 107 THR   D CG2   1 
ATOM   3611 N  N     . ASN   C 2 109 ? -37.11300 33.87100 -44.44300 1.000 14.31802 ? 108 ASN   D N     1 
ATOM   3612 C  CA    . ASN   C 2 109 ? -38.13600 34.57400 -43.67800 1.000 14.02533 ? 108 ASN   D CA    1 
ATOM   3613 C  C     . ASN   C 2 109 ? -39.44400 33.81600 -43.73300 1.000 13.86250 ? 108 ASN   D C     1 
ATOM   3614 O  O     . ASN   C 2 109 ? -39.83800 33.32700 -44.78900 1.000 16.53834 ? 108 ASN   D O     1 
ATOM   3615 C  CB    . ASN   C 2 109 ? -38.35200 35.96000 -44.25300 1.000 15.73345 ? 108 ASN   D CB    1 
ATOM   3616 C  CG    . ASN   C 2 109 ? -37.10300 36.76800 -44.22800 1.000 15.83853 ? 108 ASN   D CG    1 
ATOM   3617 O  OD1   . ASN   C 2 109 ? -36.68600 37.21400 -43.17000 1.000 16.78851 ? 108 ASN   D OD1   1 
ATOM   3618 N  ND2   . ASN   C 2 109 ? -36.47500 36.94600 -45.39200 1.000 17.49197 ? 108 ASN   D ND2   1 
ATOM   3619 N  N     . GLY   C 2 110 ? -40.12700 33.75200 -42.59300 1.000 13.88587 ? 109 GLY   D N     1 
ATOM   3620 C  CA    . GLY   C 2 110 ? -41.40600 33.08500 -42.51100 1.000 14.73226 ? 109 GLY   D CA    1 
ATOM   3621 C  C     . GLY   C 2 110 ? -42.40600 33.97500 -41.80800 1.000 13.23532 ? 109 GLY   D C     1 
ATOM   3622 O  O     . GLY   C 2 110 ? -42.89200 34.95700 -42.38100 1.000 15.85458 ? 109 GLY   D O     1 
ATOM   3623 N  N     . SER   C 2 111 ? -42.69600 33.66100 -40.54800 1.000 13.08229 ? 110 SER   D N     1 
ATOM   3624 C  CA    . SER   C 2 111 ? -43.48100 34.54200 -39.70200 1.000 13.54278 ? 110 SER   D CA    1 
ATOM   3625 C  C     . SER   C 2 111 ? -42.77000 34.97900 -38.43700 1.000 12.51282 ? 110 SER   D C     1 
ATOM   3626 O  O     . SER   C 2 111 ? -43.18100 35.98100 -37.84600 1.000 13.08770 ? 110 SER   D O     1 
ATOM   3627 C  CB    . SER   C 2 111 ? -44.80600 33.88100 -39.30400 1.000 13.45283 ? 110 SER   D CB    1 
ATOM   3628 O  OG    . SER   C 2 111 ? -44.53500 32.64100 -38.71000 1.000 14.24665 ? 110 SER   D OG    1 
ATOM   3629 N  N     . GLN   C 2 112 ? -41.72500 34.27600 -37.99900 1.000 12.53291 ? 111 GLN   D N     1 
ATOM   3630 C  CA    . GLN   C 2 112 ? -41.09000 34.67300 -36.74800 1.000 12.34622 ? 111 GLN   D CA    1 
ATOM   3631 C  C     . GLN   C 2 112 ? -40.41300 36.03500 -36.90300 1.000 11.96594 ? 111 GLN   D C     1 
ATOM   3632 O  O     . GLN   C 2 112 ? -39.83800 36.36300 -37.94900 1.000 12.93146 ? 111 GLN   D O     1 
ATOM   3633 C  CB    . GLN   C 2 112 ? -40.12300 33.60200 -36.22800 1.000 12.91355 ? 111 GLN   D CB    1 
ATOM   3634 C  CG    . GLN   C 2 112 ? -40.80700 32.34900 -35.71100 1.000 14.44832 ? 111 GLN   D CG    1 
ATOM   3635 C  CD    . GLN   C 2 112 ? -39.83800 31.46300 -34.95500 1.000 12.06082 ? 111 GLN   D CD    1 
ATOM   3636 O  OE1   . GLN   C 2 112 ? -39.05200 31.95500 -34.14300 1.000 13.56367 ? 111 GLN   D OE1   1 
ATOM   3637 N  NE2   . GLN   C 2 112 ? -39.90000 30.15900 -35.19600 1.000 13.66272 ? 111 GLN   D NE2   1 
ATOM   3638 N  N     . PHE   C 2 113 ? -40.42800 36.80600 -35.82000 1.000 11.75810 ? 112 PHE   D N     1 
ATOM   3639 C  CA    . PHE   C 2 113 ? -39.96900 38.18500 -35.80200 1.000 12.65886 ? 112 PHE   D CA    1 
ATOM   3640 C  C     . PHE   C 2 113 ? -39.39800 38.45000 -34.41800 1.000 12.21687 ? 112 PHE   D C     1 
ATOM   3641 O  O     . PHE   C 2 113 ? -39.62300 37.68500 -33.47700 1.000 12.01998 ? 112 PHE   D O     1 
ATOM   3642 C  CB    . PHE   C 2 113 ? -41.15300 39.14600 -36.05300 1.000 13.62478 ? 112 PHE   D CB    1 
ATOM   3643 C  CG    . PHE   C 2 113 ? -42.19800 39.08100 -34.97200 1.000 12.28103 ? 112 PHE   D CG    1 
ATOM   3644 C  CD1   . PHE   C 2 113 ? -43.22500 38.13900 -35.04000 1.000 14.14835 ? 112 PHE   D CD1   1 
ATOM   3645 C  CD2   . PHE   C 2 113 ? -42.10600 39.89000 -33.85000 1.000 12.45288 ? 112 PHE   D CD2   1 
ATOM   3646 C  CE1   . PHE   C 2 113 ? -44.14800 38.02300 -34.01600 1.000 13.83877 ? 112 PHE   D CE1   1 
ATOM   3647 C  CE2   . PHE   C 2 113 ? -43.01900 39.78600 -32.82500 1.000 13.53937 ? 112 PHE   D CE2   1 
ATOM   3648 C  CZ    . PHE   C 2 113 ? -44.04600 38.85100 -32.90200 1.000 14.30254 ? 112 PHE   D CZ    1 
ATOM   3649 N  N     . PHE   C 2 114 ? -38.69800 39.57500 -34.28000 1.000 11.76108 ? 113 PHE   D N     1 
ATOM   3650 C  CA    . PHE   C 2 114 ? -38.24400 40.00100 -32.96200 1.000 11.83352 ? 113 PHE   D CA    1 
ATOM   3651 C  C     . PHE   C 2 114 ? -38.37500 41.50300 -32.81200 1.000 11.90599 ? 113 PHE   D C     1 
ATOM   3652 O  O     . PHE   C 2 114 ? -38.30000 42.25800 -33.79100 1.000 14.07554 ? 113 PHE   D O     1 
ATOM   3653 C  CB    . PHE   C 2 114 ? -36.83800 39.49000 -32.61400 1.000 12.72482 ? 113 PHE   D CB    1 
ATOM   3654 C  CG    . PHE   C 2 114 ? -35.76500 39.98100 -33.53200 1.000 12.21870 ? 113 PHE   D CG    1 
ATOM   3655 C  CD1   . PHE   C 2 114 ? -35.60400 39.44900 -34.81000 1.000 13.04196 ? 113 PHE   D CD1   1 
ATOM   3656 C  CD2   . PHE   C 2 114 ? -34.88400 40.96100 -33.10500 1.000 14.28086 ? 113 PHE   D CD2   1 
ATOM   3657 C  CE1   . PHE   C 2 114 ? -34.58100 39.89700 -35.65700 1.000 14.29103 ? 113 PHE   D CE1   1 
ATOM   3658 C  CE2   . PHE   C 2 114 ? -33.85800 41.42800 -33.95400 1.000 15.24214 ? 113 PHE   D CE2   1 
ATOM   3659 C  CZ    . PHE   C 2 114 ? -33.71700 40.89700 -35.22200 1.000 13.99638 ? 113 PHE   D CZ    1 
ATOM   3660 N  N     . ILE   C 2 115 ? -38.58100 41.91700 -31.56300 1.000 12.42700 ? 114 ILE   D N     1 
ATOM   3661 C  CA    . ILE   C 2 115 ? -38.58200 43.31900 -31.17200 1.000 12.78540 ? 114 ILE   D CA    1 
ATOM   3662 C  C     . ILE   C 2 115 ? -37.31100 43.56000 -30.36500 1.000 14.03975 ? 114 ILE   D C     1 
ATOM   3663 O  O     . ILE   C 2 115 ? -37.10100 42.92600 -29.32000 1.000 13.60783 ? 114 ILE   D O     1 
ATOM   3664 C  CB    . ILE   C 2 115 ? -39.80700 43.65900 -30.31200 1.000 13.90194 ? 114 ILE   D CB    1 
ATOM   3665 C  CG1   . ILE   C 2 115 ? -41.11600 43.19900 -30.98000 1.000 16.44268 ? 114 ILE   D CG1   1 
ATOM   3666 C  CG2   . ILE   C 2 115 ? -39.79400 45.15400 -29.96900 1.000 16.73027 ? 114 ILE   D CG2   1 
ATOM   3667 C  CD1   . ILE   C 2 115 ? -42.34400 43.22600 -30.03800 1.000 16.16331 ? 114 ILE   D CD1   1 
ATOM   3668 N  N     . CYS   C 2 116 ? -36.45500 44.46300 -30.84100 1.000 14.27662 ? 115 CYS   D N     1 
ATOM   3669 C  CA    . CYS   C 2 116 ? -35.23800 44.76400 -30.10200 1.000 14.37977 ? 115 CYS   D CA    1 
ATOM   3670 C  C     . CYS   C 2 116 ? -35.55100 45.52600 -28.82700 1.000 16.07045 ? 115 CYS   D C     1 
ATOM   3671 O  O     . CYS   C 2 116 ? -36.40400 46.41800 -28.80900 1.000 16.88656 ? 115 CYS   D O     1 
ATOM   3672 C  CB    . CYS   C 2 116 ? -34.29200 45.59900 -30.96100 1.000 15.97860 ? 115 CYS   D CB    1 
ATOM   3673 S  SG    . CYS   C 2 116 ? -33.80400 44.76300 -32.45400 1.000 18.64444 ? 115 CYS   D SG    1 
ATOM   3674 N  N     . THR   C 2 117 ? -34.84200 45.17700 -27.75400 1.000 16.66209 ? 116 THR   D N     1 
ATOM   3675 C  CA    . THR   C 2 117 ? -34.86700 45.99000 -26.54300 1.000 17.71791 ? 116 THR   D CA    1 
ATOM   3676 C  C     . THR   C 2 117 ? -33.56100 46.74300 -26.34300 1.000 17.84191 ? 116 THR   D C     1 
ATOM   3677 O  O     . THR   C 2 117 ? -33.38900 47.41400 -25.32800 1.000 19.93944 ? 116 THR   D O     1 
ATOM   3678 C  CB    . THR   C 2 117 ? -35.22100 45.14700 -25.32000 1.000 19.40636 ? 116 THR   D CB    1 
ATOM   3679 O  OG1   . THR   C 2 117 ? -34.27600 44.08000 -25.18800 1.000 20.09842 ? 116 THR   D OG1   1 
ATOM   3680 C  CG2   . THR   C 2 117 ? -36.63600 44.57900 -25.46000 1.000 19.28709 ? 116 THR   D CG2   1 
ATOM   3681 N  N     . ALA   C 2 118 ? -32.65700 46.65000 -27.30700 1.000 18.20996 ? 117 ALA   D N     1 
ATOM   3682 C  CA    . ALA   C 2 118 ? -31.37700 47.33700 -27.29200 1.000 20.14640 ? 117 ALA   D CA    1 
ATOM   3683 C  C     . ALA   C 2 118 ? -30.91600 47.40800 -28.73500 1.000 20.50836 ? 117 ALA   D C     1 
ATOM   3684 O  O     . ALA   C 2 118 ? -31.51000 46.78900 -29.62100 1.000 19.64403 ? 117 ALA   D O     1 
ATOM   3685 C  CB    . ALA   C 2 118 ? -30.34900 46.57300 -26.45500 1.000 23.61863 ? 117 ALA   D CB    1 
ATOM   3686 N  N     . LYS   C 2 119 ? -29.84200 48.15900 -28.96100 1.000 21.47152 ? 118 LYS   D N     1 
ATOM   3687 C  CA    . LYS   C 2 119 ? -29.21300 48.16500 -30.27400 1.000 21.73762 ? 118 LYS   D CA    1 
ATOM   3688 C  C     . LYS   C 2 119 ? -28.56800 46.80400 -30.53700 1.000 22.29509 ? 118 LYS   D C     1 
ATOM   3689 O  O     . LYS   C 2 119 ? -27.83800 46.27900 -29.69200 1.000 23.33123 ? 118 LYS   D O     1 
ATOM   3690 C  CB    . LYS   C 2 119 ? -28.17300 49.28900 -30.34700 1.000 25.22926 ? 118 LYS   D CB    1 
ATOM   3691 C  CG    . LYS   C 2 119 ? -27.52600 49.42700 -31.71500 1.000 29.78701 ? 118 LYS   D CG    1 
ATOM   3692 C  CD    . LYS   C 2 119 ? -26.68500 50.70300 -31.83400 1.000 36.25903 ? 118 LYS   D CD    1 
ATOM   3693 C  CE    . LYS   C 2 119 ? -25.32800 50.56200 -31.16800 1.000 41.00825 ? 118 LYS   D CE    1 
ATOM   3694 N  NZ    . LYS   C 2 119 ? -24.43500 51.71500 -31.50000 1.000 43.10892 ? 118 LYS   D NZ    1 
ATOM   3695 N  N     . THR   C 2 120 ? -28.87400 46.20600 -31.69000 1.000 18.65395 ? 119 THR   D N     1 
ATOM   3696 C  CA    . THR   C 2 120 ? -28.35400 44.88700 -32.05800 1.000 19.14223 ? 119 THR   D CA    1 
ATOM   3697 C  C     . THR   C 2 120 ? -27.69600 44.98300 -33.43200 1.000 19.17380 ? 119 THR   D C     1 
ATOM   3698 O  O     . THR   C 2 120 ? -28.09900 44.33800 -34.39700 1.000 18.91605 ? 119 THR   D O     1 
ATOM   3699 C  CB    . THR   C 2 120 ? -29.46000 43.82200 -32.03100 1.000 17.25734 ? 119 THR   D CB    1 
ATOM   3700 O  OG1   . THR   C 2 120 ? -30.47100 44.14400 -32.99800 1.000 18.29207 ? 119 THR   D OG1   1 
ATOM   3701 C  CG2   . THR   C 2 120 ? -30.09000 43.74800 -30.65300 1.000 17.68940 ? 119 THR   D CG2   1 
ATOM   3702 N  N     . GLU   C 2 121 ? -26.66500 45.82300 -33.52000 1.000 21.06707 ? 120 GLU   D N     1 
ATOM   3703 C  CA    . GLU   C 2 121 ? -26.12500 46.18900 -34.82300 1.000 22.72000 ? 120 GLU   D CA    1 
ATOM   3704 C  C     . GLU   C 2 121 ? -25.44900 45.01900 -35.53200 1.000 19.30691 ? 120 GLU   D C     1 
ATOM   3705 O  O     . GLU   C 2 121 ? -25.31900 45.04400 -36.76100 1.000 21.36081 ? 120 GLU   D O     1 
ATOM   3706 C  CB    . GLU   C 2 121 ? -25.17800 47.38200 -34.66600 1.000 27.88246 ? 120 GLU   D CB    1 
ATOM   3707 C  CG    . GLU   C 2 121 ? -23.80100 47.05700 -34.08100 1.000 32.95083 ? 120 GLU   D CG    1 
ATOM   3708 C  CD    . GLU   C 2 121 ? -23.79000 46.80400 -32.57300 1.000 36.40187 ? 120 GLU   D CD    1 
ATOM   3709 O  OE1   . GLU   C 2 121 ? -24.83200 46.98000 -31.89700 1.000 36.52670 ? 120 GLU   D OE1   1 
ATOM   3710 O  OE2   . GLU   C 2 121 ? -22.71600 46.42100 -32.05900 1.000 39.41177 ? 120 GLU   D OE2   1 
ATOM   3711 N  N     . TRP   C 2 122 ? -25.03200 43.99100 -34.79200 1.000 19.49645 ? 121 TRP   D N     1 
ATOM   3712 C  CA    . TRP   C 2 122 ? -24.40800 42.83600 -35.41800 1.000 21.12019 ? 121 TRP   D CA    1 
ATOM   3713 C  C     . TRP   C 2 122 ? -25.38900 42.03200 -36.26100 1.000 19.29629 ? 121 TRP   D C     1 
ATOM   3714 O  O     . TRP   C 2 122 ? -24.95600 41.17600 -37.03500 1.000 22.72985 ? 121 TRP   D O     1 
ATOM   3715 C  CB    . TRP   C 2 122 ? -23.77200 41.95700 -34.34100 1.000 21.67084 ? 121 TRP   D CB    1 
ATOM   3716 C  CG    . TRP   C 2 122 ? -24.79100 41.45100 -33.34700 1.000 21.27418 ? 121 TRP   D CG    1 
ATOM   3717 C  CD1   . TRP   C 2 122 ? -25.50700 40.29900 -33.43900 1.000 21.82155 ? 121 TRP   D CD1   1 
ATOM   3718 C  CD2   . TRP   C 2 122 ? -25.22100 42.09700 -32.13800 1.000 20.66837 ? 121 TRP   D CD2   1 
ATOM   3719 N  NE1   . TRP   C 2 122 ? -26.35600 40.17900 -32.36700 1.000 20.85588 ? 121 TRP   D NE1   1 
ATOM   3720 C  CE2   . TRP   C 2 122 ? -26.20300 41.27200 -31.55300 1.000 21.83403 ? 121 TRP   D CE2   1 
ATOM   3721 C  CE3   . TRP   C 2 122 ? -24.87200 43.29200 -31.49600 1.000 22.53562 ? 121 TRP   D CE3   1 
ATOM   3722 C  CZ2   . TRP   C 2 122 ? -26.82800 41.59100 -30.34800 1.000 22.10806 ? 121 TRP   D CZ2   1 
ATOM   3723 C  CZ3   . TRP   C 2 122 ? -25.49700 43.60700 -30.29200 1.000 22.78489 ? 121 TRP   D CZ3   1 
ATOM   3724 C  CH2   . TRP   C 2 122 ? -26.46900 42.76000 -29.73700 1.000 23.61843 ? 121 TRP   D CH2   1 
ATOM   3725 N  N     . LEU   C 2 123 ? -26.69100 42.28000 -36.12200 1.000 17.25938 ? 122 LEU   D N     1 
ATOM   3726 C  CA    . LEU   C 2 123 ? -27.69000 41.64300 -36.97200 1.000 16.67613 ? 122 LEU   D CA    1 
ATOM   3727 C  C     . LEU   C 2 123 ? -27.89300 42.37300 -38.29500 1.000 17.55130 ? 122 LEU   D C     1 
ATOM   3728 O  O     . LEU   C 2 123 ? -28.56000 41.83700 -39.18900 1.000 16.81159 ? 122 LEU   D O     1 
ATOM   3729 C  CB    . LEU   C 2 123 ? -29.01300 41.54600 -36.21100 1.000 15.80612 ? 122 LEU   D CB    1 
ATOM   3730 C  CG    . LEU   C 2 123 ? -28.92900 40.74800 -34.92000 1.000 16.95737 ? 122 LEU   D CG    1 
ATOM   3731 C  CD1   . LEU   C 2 123 ? -30.25900 40.79400 -34.19200 1.000 16.67160 ? 122 LEU   D CD1   1 
ATOM   3732 C  CD2   . LEU   C 2 123 ? -28.47200 39.29200 -35.16400 1.000 18.28391 ? 122 LEU   D CD2   1 
ATOM   3733 N  N     . ASP   C 2 124 ? -27.31000 43.56100 -38.45200 1.000 16.80034 ? 123 ASP   D N     1 
ATOM   3734 C  CA    . ASP   C 2 124 ? -27.44000 44.31600 -39.69400 1.000 17.59265 ? 123 ASP   D CA    1 
ATOM   3735 C  C     . ASP   C 2 124 ? -26.93500 43.51200 -40.88900 1.000 18.52429 ? 123 ASP   D C     1 
ATOM   3736 O  O     . ASP   C 2 124 ? -25.86500 42.89800 -40.84500 1.000 20.13962 ? 123 ASP   D O     1 
ATOM   3737 C  CB    . ASP   C 2 124 ? -26.62200 45.60500 -39.60300 1.000 18.69595 ? 123 ASP   D CB    1 
ATOM   3738 C  CG    . ASP   C 2 124 ? -27.21900 46.62300 -38.65000 1.000 19.81842 ? 123 ASP   D CG    1 
ATOM   3739 O  OD1   . ASP   C 2 124 ? -28.34700 46.41300 -38.15400 1.000 20.34360 ? 123 ASP   D OD1   1 
ATOM   3740 O  OD2   . ASP   C 2 124 ? -26.55700 47.66200 -38.42700 1.000 21.71981 ? 123 ASP   D OD2   1 
ATOM   3741 N  N     . GLY   C 2 125 ? -27.69900 43.54400 -41.97600 1.000 17.63195 ? 124 GLY   D N     1 
ATOM   3742 C  CA    . GLY   C 2 125 ? -27.33100 42.81800 -43.17800 1.000 18.56425 ? 124 GLY   D CA    1 
ATOM   3743 C  C     . GLY   C 2 125 ? -27.64900 41.33900 -43.15700 1.000 17.40287 ? 124 GLY   D C     1 
ATOM   3744 O  O     . GLY   C 2 125 ? -27.40400 40.65900 -44.16100 1.000 20.30140 ? 124 GLY   D O     1 
ATOM   3745 N  N     . LYS   C 2 126 ? -28.17000 40.81500 -42.04100 1.000 16.98527 ? 125 LYS   D N     1 
ATOM   3746 C  CA    . LYS   C 2 126 ? -28.57100 39.42200 -41.90800 1.000 18.10640 ? 125 LYS   D CA    1 
ATOM   3747 C  C     . LYS   C 2 126 ? -30.04500 39.25200 -41.58400 1.000 16.41875 ? 125 LYS   D C     1 
ATOM   3748 O  O     . LYS   C 2 126 ? -30.61100 38.22100 -41.92100 1.000 17.43320 ? 125 LYS   D O     1 
ATOM   3749 C  CB    . LYS   C 2 126 ? -27.74000 38.74200 -40.81000 1.000 21.78953 ? 125 LYS   D CB    1 
ATOM   3750 C  CG    . LYS   C 2 126 ? -26.24400 38.82700 -41.06200 1.000 26.85388 ? 125 LYS   D CG    1 
ATOM   3751 C  CD    . LYS   C 2 126 ? -25.81000 37.84600 -42.13800 1.000 34.90695 ? 125 LYS   D CD    1 
ATOM   3752 C  CE    . LYS   C 2 126 ? -24.32300 37.98700 -42.45200 1.000 39.86157 ? 125 LYS   D CE    1 
ATOM   3753 N  NZ    . LYS   C 2 126 ? -23.48500 37.87900 -41.22400 1.000 44.27459 ? 125 LYS   D NZ    1 
ATOM   3754 N  N     . HIS   C 2 127 ? -30.67000 40.22500 -40.92800 1.000 14.37975 ? 126 HIS   D N     1 
ATOM   3755 C  CA    . HIS   C 2 127 ? -32.09700 40.20200 -40.65000 1.000 14.03834 ? 126 HIS   D CA    1 
ATOM   3756 C  C     . HIS   C 2 127 ? -32.73200 41.45900 -41.23300 1.000 14.10290 ? 126 HIS   D C     1 
ATOM   3757 O  O     . HIS   C 2 127 ? -32.18400 42.56300 -41.11000 1.000 15.76747 ? 126 HIS   D O     1 
ATOM   3758 C  CB    . HIS   C 2 127 ? -32.32400 40.15700 -39.14200 1.000 15.02630 ? 126 HIS   D CB    1 
ATOM   3759 C  CG    . HIS   C 2 127 ? -31.80200 38.90300 -38.52400 1.000 13.82850 ? 126 HIS   D CG    1 
ATOM   3760 N  ND1   . HIS   C 2 127 ? -32.62100 37.84200 -38.20700 1.000 13.47143 ? 126 HIS   D ND1   1 
ATOM   3761 C  CD2   . HIS   C 2 127 ? -30.53900 38.50800 -38.23400 1.000 14.20068 ? 126 HIS   D CD2   1 
ATOM   3762 C  CE1   . HIS   C 2 127 ? -31.88300 36.85900 -37.71600 1.000 14.35139 ? 126 HIS   D CE1   1 
ATOM   3763 N  NE2   . HIS   C 2 127 ? -30.61600 37.23300 -37.73400 1.000 14.64777 ? 126 HIS   D NE2   1 
ATOM   3764 N  N     . VAL   C 2 128 ? -33.89600 41.28800 -41.85400 1.000 14.26825 ? 127 VAL   D N     1 
ATOM   3765 C  CA    . VAL   C 2 128 ? -34.57900 42.40000 -42.50600 1.000 13.42924 ? 127 VAL   D CA    1 
ATOM   3766 C  C     . VAL   C 2 128 ? -35.39800 43.18100 -41.47800 1.000 13.75490 ? 127 VAL   D C     1 
ATOM   3767 O  O     . VAL   C 2 128 ? -36.35100 42.64700 -40.89500 1.000 14.49821 ? 127 VAL   D O     1 
ATOM   3768 C  CB    . VAL   C 2 128 ? -35.46600 41.89800 -43.64800 1.000 13.48515 ? 127 VAL   D CB    1 
ATOM   3769 C  CG1   . VAL   C 2 128 ? -36.27400 43.05400 -44.23200 1.000 14.67537 ? 127 VAL   D CG1   1 
ATOM   3770 C  CG2   . VAL   C 2 128 ? -34.63100 41.17500 -44.71800 1.000 14.86099 ? 127 VAL   D CG2   1 
ATOM   3771 N  N     . VAL   C 2 129 ? -35.01900 44.44000 -41.25700 1.000 13.67153 ? 128 VAL   D N     1 
ATOM   3772 C  CA    . VAL   C 2 129 ? -35.77200 45.39200 -40.43800 1.000 15.10103 ? 128 VAL   D CA    1 
ATOM   3773 C  C     . VAL   C 2 129 ? -36.93100 45.95400 -41.25700 1.000 14.30655 ? 128 VAL   D C     1 
ATOM   3774 O  O     . VAL   C 2 129 ? -36.75000 46.40100 -42.38900 1.000 14.88760 ? 128 VAL   D O     1 
ATOM   3775 C  CB    . VAL   C 2 129 ? -34.85500 46.52600 -39.96200 1.000 14.47040 ? 128 VAL   D CB    1 
ATOM   3776 C  CG1   . VAL   C 2 129 ? -35.67900 47.62100 -39.26900 1.000 14.78098 ? 128 VAL   D CG1   1 
ATOM   3777 C  CG2   . VAL   C 2 129 ? -33.72700 46.00500 -39.08400 1.000 16.78464 ? 128 VAL   D CG2   1 
ATOM   3778 N  N     . PHE   C 2 130 ? -38.12800 45.95100 -40.68800 1.000 13.45096 ? 129 PHE   D N     1 
ATOM   3779 C  CA    . PHE   C 2 130 ? -39.29600 46.36100 -41.45400 1.000 15.11797 ? 129 PHE   D CA    1 
ATOM   3780 C  C     . PHE   C 2 130 ? -40.30300 47.16800 -40.65200 1.000 14.71903 ? 129 PHE   D C     1 
ATOM   3781 O  O     . PHE   C 2 130 ? -41.34900 47.52400 -41.20200 1.000 16.17719 ? 129 PHE   D O     1 
ATOM   3782 C  CB    . PHE   C 2 130 ? -39.99100 45.14000 -42.08800 1.000 15.50955 ? 129 PHE   D CB    1 
ATOM   3783 C  CG    . PHE   C 2 130 ? -40.57300 44.20700 -41.08200 1.000 12.97508 ? 129 PHE   D CG    1 
ATOM   3784 C  CD1   . PHE   C 2 130 ? -39.79100 43.21000 -40.50100 1.000 14.72537 ? 129 PHE   D CD1   1 
ATOM   3785 C  CD2   . PHE   C 2 130 ? -41.89900 44.31200 -40.71700 1.000 14.56924 ? 129 PHE   D CD2   1 
ATOM   3786 C  CE1   . PHE   C 2 130 ? -40.32900 42.35900 -39.55800 1.000 14.83137 ? 129 PHE   D CE1   1 
ATOM   3787 C  CE2   . PHE   C 2 130 ? -42.43500 43.45800 -39.77100 1.000 15.40696 ? 129 PHE   D CE2   1 
ATOM   3788 C  CZ    . PHE   C 2 130 ? -41.64400 42.47700 -39.18700 1.000 13.63056 ? 129 PHE   D CZ    1 
ATOM   3789 N  N     . GLY   C 2 131 ? -40.03000 47.46800 -39.38700 1.000 14.82140 ? 130 GLY   D N     1 
ATOM   3790 C  CA    . GLY   C 2 131 ? -40.97000 48.25800 -38.61400 1.000 16.18210 ? 130 GLY   D CA    1 
ATOM   3791 C  C     . GLY   C 2 131 ? -40.35500 48.72200 -37.31400 1.000 14.93772 ? 130 GLY   D C     1 
ATOM   3792 O  O     . GLY   C 2 131 ? -39.17100 48.49300 -37.04500 1.000 15.03360 ? 130 GLY   D O     1 
ATOM   3793 N  N     . LYS   C 2 132 ? -41.16900 49.41900 -36.52200 1.000 16.01969 ? 131 LYS   D N     1 
ATOM   3794 C  CA    . LYS   C 2 132 ? -40.74300 49.83600 -35.19200 1.000 16.15435 ? 131 LYS   D CA    1 
ATOM   3795 C  C     . LYS   C 2 132 ? -41.95500 49.97800 -34.29000 1.000 14.29274 ? 131 LYS   D C     1 
ATOM   3796 O  O     . LYS   C 2 132 ? -43.07900 50.24100 -34.75000 1.000 16.59137 ? 131 LYS   D O     1 
ATOM   3797 C  CB    . LYS   C 2 132 ? -39.99700 51.17500 -35.20100 1.000 19.96908 ? 131 LYS   D CB    1 
ATOM   3798 C  CG    . LYS   C 2 132 ? -40.85400 52.36400 -35.59200 1.000 23.62827 ? 131 LYS   D CG    1 
ATOM   3799 C  CD    . LYS   C 2 132 ? -40.05300 53.64300 -35.50700 1.000 28.43485 ? 131 LYS   D CD    1 
ATOM   3800 C  CE    . LYS   C 2 132 ? -40.84800 54.80700 -36.06400 1.000 32.51234 ? 131 LYS   D CE    1 
ATOM   3801 N  NZ    . LYS   C 2 132 ? -40.07000 56.06800 -35.96100 1.000 36.26207 ? 131 LYS   D NZ    1 
ATOM   3802 N  N     . VAL   C 2 133 ? -41.71300 49.81400 -32.99000 1.000 15.45273 ? 132 VAL   D N     1 
ATOM   3803 C  CA    . VAL   C 2 133 ? -42.76000 50.07500 -32.00800 1.000 15.03001 ? 132 VAL   D CA    1 
ATOM   3804 C  C     . VAL   C 2 133 ? -43.16000 51.54400 -32.07800 1.000 16.60151 ? 132 VAL   D C     1 
ATOM   3805 O  O     . VAL   C 2 133 ? -42.31000 52.44300 -32.02300 1.000 19.04371 ? 132 VAL   D O     1 
ATOM   3806 C  CB    . VAL   C 2 133 ? -42.29900 49.66000 -30.60100 1.000 16.46592 ? 132 VAL   D CB    1 
ATOM   3807 C  CG1   . VAL   C 2 133 ? -43.33300 50.04800 -29.54900 1.000 18.71259 ? 132 VAL   D CG1   1 
ATOM   3808 C  CG2   . VAL   C 2 133 ? -42.02000 48.15300 -30.52600 1.000 17.49194 ? 132 VAL   D CG2   1 
ATOM   3809 N  N     . LYS   C 2 134 ? -44.46600 51.78800 -32.21600 1.000 18.34249 ? 133 LYS   D N     1 
ATOM   3810 C  CA    . LYS   C 2 134 ? -45.06500 53.11800 -32.19700 1.000 20.81423 ? 133 LYS   D CA    1 
ATOM   3811 C  C     . LYS   C 2 134 ? -45.47700 53.48000 -30.77600 1.000 20.93956 ? 133 LYS   D C     1 
ATOM   3812 O  O     . LYS   C 2 134 ? -44.95300 54.43300 -30.19400 1.000 27.30107 ? 133 LYS   D O     1 
ATOM   3813 C  CB    . LYS   C 2 134 ? -46.27000 53.12000 -33.14600 1.000 21.33040 ? 133 LYS   D CB    1 
ATOM   3814 C  CG    . LYS   C 2 134 ? -46.97100 54.45400 -33.32300 1.000 26.34107 ? 133 LYS   D CG    1 
ATOM   3815 C  CD    . LYS   C 2 134 ? -48.12900 54.29300 -34.30400 1.000 31.02483 ? 133 LYS   D CD    1 
ATOM   3816 C  CE    . LYS   C 2 134 ? -48.59000 55.61500 -34.87900 1.000 36.99171 ? 133 LYS   D CE    1 
ATOM   3817 N  NZ    . LYS   C 2 134 ? -47.60500 56.15900 -35.86500 1.000 40.75896 ? 133 LYS   D NZ    1 
ATOM   3818 N  N     . GLU   C 2 135 ? -46.40400 52.71700 -30.20300 1.000 22.20531 ? 134 GLU   D N     1 
ATOM   3819 C  CA    . GLU   C 2 135 ? -46.81500 52.87900 -28.81900 1.000 22.51214 ? 134 GLU   D CA    1 
ATOM   3820 C  C     . GLU   C 2 135 ? -46.61700 51.56300 -28.08100 1.000 18.98945 ? 134 GLU   D C     1 
ATOM   3821 O  O     . GLU   C 2 135 ? -46.63600 50.48100 -28.68100 1.000 19.70053 ? 134 GLU   D O     1 
ATOM   3822 C  CB    . GLU   C 2 135 ? -48.28600 53.30000 -28.71000 1.000 29.91451 ? 134 GLU   D CB    1 
ATOM   3823 C  CG    . GLU   C 2 135 ? -48.53600 54.76400 -29.05900 1.000 40.73747 ? 134 GLU   D CG    1 
ATOM   3824 C  CD    . GLU   C 2 135 ? -49.89800 55.25800 -28.59800 1.000 50.98864 ? 134 GLU   D CD    1 
ATOM   3825 O  OE1   . GLU   C 2 135 ? -50.90600 54.94900 -29.26700 1.000 53.60756 ? 134 GLU   D OE1   1 
ATOM   3826 O  OE2   . GLU   C 2 135 ? -49.96200 55.94700 -27.55900 1.000 55.11753 ? 134 GLU   D OE2   1 
ATOM   3827 N  N     . GLY   C 2 136 ? -46.42400 51.65900 -26.77000 1.000 20.00100 ? 135 GLY   D N     1 
ATOM   3828 C  CA    . GLY   C 2 136 ? -46.33700 50.47700 -25.93800 1.000 17.64239 ? 135 GLY   D CA    1 
ATOM   3829 C  C     . GLY   C 2 136 ? -44.94700 49.93900 -25.69900 1.000 18.58799 ? 135 GLY   D C     1 
ATOM   3830 O  O     . GLY   C 2 136 ? -44.80800 48.76900 -25.33300 1.000 18.87716 ? 135 GLY   D O     1 
ATOM   3831 N  N     . MET   C 2 137 ? -43.89900 50.74600 -25.87500 1.000 18.52390 ? 136 MET   D N     1 
ATOM   3832 C  CA    . MET   C 2 137 ? -42.57400 50.25300 -25.51800 1.000 19.07665 ? 136 MET   D CA    1 
ATOM   3833 C  C     . MET   C 2 137 ? -42.50800 49.85500 -24.05000 1.000 18.27991 ? 136 MET   D C     1 
ATOM   3834 O  O     . MET   C 2 137 ? -41.76500 48.93400 -23.69200 1.000 20.85860 ? 136 MET   D O     1 
ATOM   3835 C  CB    . MET   C 2 137 ? -41.49700 51.28900 -25.84800 1.000 21.63409 ? 136 MET   D CB    1 
ATOM   3836 C  CG    . MET   C 2 137 ? -40.08900 50.70300 -25.94000 1.000 25.66064 ? 136 MET   D CG    1 
ATOM   3837 S  SD    . MET   C 2 137 ? -39.92900 49.43900 -27.22500 1.000 25.13495 ? 136 MET   D SD    1 
ATOM   3838 C  CE    . MET   C 2 137 ? -38.62100 48.43300 -26.53300 1.000 22.70679 ? 136 MET   D CE    1 
ATOM   3839 N  N     . ASN   C 2 138 ? -43.29500 50.51000 -23.19200 1.000 19.27392 ? 137 ASN   D N     1 
ATOM   3840 C  CA    . ASN   C 2 138 ? -43.30700 50.10300 -21.78900 1.000 20.07443 ? 137 ASN   D CA    1 
ATOM   3841 C  C     . ASN   C 2 138 ? -43.86200 48.69200 -21.62000 1.000 19.14248 ? 137 ASN   D C     1 
ATOM   3842 O  O     . ASN   C 2 138 ? -43.46900 47.97800 -20.69200 1.000 18.98006 ? 137 ASN   D O     1 
ATOM   3843 C  CB    . ASN   C 2 138 ? -44.06900 51.11800 -20.93100 1.000 23.73679 ? 137 ASN   D CB    1 
ATOM   3844 C  CG    . ASN   C 2 138 ? -45.54700 51.19000 -21.27400 1.000 28.21020 ? 137 ASN   D CG    1 
ATOM   3845 O  OD1   . ASN   C 2 138 ? -45.93300 51.08300 -22.43300 1.000 27.94415 ? 137 ASN   D OD1   1 
ATOM   3846 N  ND2   . ASN   C 2 138 ? -46.38000 51.39000 -20.25900 1.000 33.49712 ? 137 ASN   D ND2   1 
ATOM   3847 N  N     . ILE   C 2 139 ? -44.77200 48.27800 -22.50400 1.000 17.36123 ? 138 ILE   D N     1 
ATOM   3848 C  CA    . ILE   C 2 139 ? -45.24000 46.89600 -22.49800 1.000 16.77445 ? 138 ILE   D CA    1 
ATOM   3849 C  C     . ILE   C 2 139 ? -44.12100 45.93700 -22.89400 1.000 15.84615 ? 138 ILE   D C     1 
ATOM   3850 O  O     . ILE   C 2 139 ? -43.95700 44.87600 -22.29200 1.000 17.33420 ? 138 ILE   D O     1 
ATOM   3851 C  CB    . ILE   C 2 139 ? -46.47600 46.73300 -23.40100 1.000 16.26299 ? 138 ILE   D CB    1 
ATOM   3852 C  CG1   . ILE   C 2 139 ? -47.54000 47.78800 -23.05600 1.000 19.48816 ? 138 ILE   D CG1   1 
ATOM   3853 C  CG2   . ILE   C 2 139 ? -47.05700 45.31500 -23.28000 1.000 17.07946 ? 138 ILE   D CG2   1 
ATOM   3854 C  CD1   . ILE   C 2 139 ? -47.94000 47.78900 -21.61500 1.000 20.35201 ? 138 ILE   D CD1   1 
ATOM   3855 N  N     . VAL   C 2 140 ? -43.34500 46.28300 -23.92600 1.000 17.02471 ? 139 VAL   D N     1 
ATOM   3856 C  CA    . VAL   C 2 140 ? -42.22800 45.43800 -24.33800 1.000 18.46989 ? 139 VAL   D CA    1 
ATOM   3857 C  C     . VAL   C 2 140 ? -41.22300 45.31400 -23.20500 1.000 17.50254 ? 139 VAL   D C     1 
ATOM   3858 O  O     . VAL   C 2 140 ? -40.71700 44.22000 -22.91700 1.000 18.42348 ? 139 VAL   D O     1 
ATOM   3859 C  CB    . VAL   C 2 140 ? -41.58100 46.00300 -25.61600 1.000 17.84198 ? 139 VAL   D CB    1 
ATOM   3860 C  CG1   . VAL   C 2 140 ? -40.37300 45.17000 -25.98900 1.000 19.24020 ? 139 VAL   D CG1   1 
ATOM   3861 C  CG2   . VAL   C 2 140 ? -42.58300 46.01000 -26.75800 1.000 17.47776 ? 139 VAL   D CG2   1 
ATOM   3862 N  N     . GLU   C 2 141 ? -40.94200 46.43000 -22.52200 1.000 17.76573 ? 140 GLU   D N     1 
ATOM   3863 C  CA    . GLU   C 2 141 ? -40.01000 46.38900 -21.40300 1.000 18.40125 ? 140 GLU   D CA    1 
ATOM   3864 C  C     . GLU   C 2 141 ? -40.54000 45.49700 -20.28700 1.000 18.59176 ? 140 GLU   D C     1 
ATOM   3865 O  O     . GLU   C 2 141 ? -39.77900 44.74400 -19.66400 1.000 19.59871 ? 140 GLU   D O     1 
ATOM   3866 C  CB    . GLU   C 2 141 ? -39.73600 47.81000 -20.89700 1.000 21.30648 ? 140 GLU   D CB    1 
ATOM   3867 C  CG    . GLU   C 2 141 ? -38.92900 48.65900 -21.89000 1.000 26.52426 ? 140 GLU   D CG    1 
ATOM   3868 C  CD    . GLU   C 2 141 ? -39.00100 50.16100 -21.63000 1.000 30.91132 ? 140 GLU   D CD    1 
ATOM   3869 O  OE1   . GLU   C 2 141 ? -39.65300 50.59100 -20.65800 1.000 33.84534 ? 140 GLU   D OE1   1 
ATOM   3870 O  OE2   . GLU   C 2 141 ? -38.40000 50.92100 -22.41500 1.000 35.92355 ? 140 GLU   D OE2   1 
ATOM   3871 N  N     . ALA   C 2 142 ? -41.85200 45.55000 -20.04100 1.000 17.27142 ? 141 ALA   D N     1 
ATOM   3872 C  CA    . ALA   C 2 142 ? -42.47900 44.67900 -19.04800 1.000 18.84563 ? 141 ALA   D CA    1 
ATOM   3873 C  C     . ALA   C 2 142 ? -42.39500 43.20200 -19.42800 1.000 19.50486 ? 141 ALA   D C     1 
ATOM   3874 O  O     . ALA   C 2 142 ? -42.30700 42.34400 -18.54400 1.000 23.37386 ? 141 ALA   D O     1 
ATOM   3875 C  CB    . ALA   C 2 142 ? -43.93900 45.09800 -18.84400 1.000 19.76756 ? 141 ALA   D CB    1 
ATOM   3876 N  N     . MET   C 2 143 ? -42.44000 42.88100 -20.72500 1.000 16.95066 ? 142 MET   D N     1 
ATOM   3877 C  CA    . MET   C 2 143 ? -42.29900 41.49100 -21.15700 1.000 17.41003 ? 142 MET   D CA    1 
ATOM   3878 C  C     . MET   C 2 143 ? -40.93300 40.92800 -20.79300 1.000 20.73165 ? 142 MET   D C     1 
ATOM   3879 O  O     . MET   C 2 143 ? -40.79200 39.71900 -20.58700 1.000 20.40671 ? 142 MET   D O     1 
ATOM   3880 C  CB    . MET   C 2 143 ? -42.53300 41.38200 -22.66700 1.000 16.78719 ? 142 MET   D CB    1 
ATOM   3881 C  CG    . MET   C 2 143 ? -43.96700 41.69000 -23.07400 1.000 17.31457 ? 142 MET   D CG    1 
ATOM   3882 S  SD    . MET   C 2 143 ? -44.16000 42.08500 -24.82200 1.000 19.05652 ? 142 MET   D SD    1 
ATOM   3883 C  CE    . MET   C 2 143 ? -43.57600 40.57700 -25.53700 1.000 22.56892 ? 142 MET   D CE    1 
ATOM   3884 N  N     . GLU   C 2 144 ? -39.91500 41.78100 -20.70800 1.000 25.05874 ? 143 GLU   D N     1 
ATOM   3885 C  CA    . GLU   C 2 144 ? -38.57300 41.29200 -20.40000 1.000 27.93992 ? 143 GLU   D CA    1 
ATOM   3886 C  C     . GLU   C 2 144 ? -38.50200 40.62200 -19.03400 1.000 30.69482 ? 143 GLU   D C     1 
ATOM   3887 O  O     . GLU   C 2 144 ? -37.69500 39.70500 -18.84200 1.000 34.24990 ? 143 GLU   D O     1 
ATOM   3888 C  CB    . GLU   C 2 144 ? -37.57100 42.43800 -20.46800 1.000 27.57820 ? 143 GLU   D CB    1 
ATOM   3889 C  CG    . GLU   C 2 144 ? -37.12100 42.80000 -21.86400 1.000 31.50462 ? 143 GLU   D CG    1 
ATOM   3890 C  CD    . GLU   C 2 144 ? -35.94100 43.77100 -21.85200 1.000 33.36517 ? 143 GLU   D CD    1 
ATOM   3891 O  OE1   . GLU   C 2 144 ? -36.08100 44.86500 -21.28100 1.000 32.97248 ? 143 GLU   D OE1   1 
ATOM   3892 O  OE2   . GLU   C 2 144 ? -34.87600 43.45100 -22.41800 1.000 35.71094 ? 143 GLU   D OE2   1 
ATOM   3893 N  N     . ARG   C 2 145 ? -39.34400 41.05000 -18.08500 1.000 32.98682 ? 144 ARG   D N     1 
ATOM   3894 C  CA    . ARG   C 2 145 ? -39.34600 40.47900 -16.73800 1.000 35.12117 ? 144 ARG   D CA    1 
ATOM   3895 C  C     . ARG   C 2 145 ? -39.52600 38.97100 -16.77300 1.000 31.82929 ? 144 ARG   D C     1 
ATOM   3896 O  O     . ARG   C 2 145 ? -39.08400 38.26100 -15.86200 1.000 33.70540 ? 144 ARG   D O     1 
ATOM   3897 C  CB    . ARG   C 2 145 ? -40.46300 41.13500 -15.90800 1.000 40.23110 ? 144 ARG   D CB    1 
ATOM   3898 C  CG    . ARG   C 2 145 ? -40.85400 40.40000 -14.61700 1.000 41.92804 ? 144 ARG   D CG    1 
ATOM   3899 C  CD    . ARG   C 2 145 ? -41.59200 41.30900 -13.63300 1.000 43.53132 ? 144 ARG   D CD    1 
ATOM   3900 N  NE    . ARG   C 2 145 ? -43.04200 41.32600 -13.80500 1.000 43.56131 ? 144 ARG   D NE    1 
ATOM   3901 C  CZ    . ARG   C 2 145 ? -43.90100 40.69500 -13.01200 1.000 44.85810 ? 144 ARG   D CZ    1 
ATOM   3902 N  NH1   . ARG   C 2 145 ? -43.48800 39.92500 -12.01800 1.000 46.01608 ? 144 ARG   D NH1   1 
ATOM   3903 N  NH2   . ARG   C 2 145 ? -45.20700 40.84900 -13.21500 1.000 42.83880 ? 144 ARG   D NH2   1 
ATOM   3904 N  N     . PHE   C 2 146 ? -40.13000 38.46500 -17.83700 1.000 25.28975 ? 145 PHE   D N     1 
ATOM   3905 C  CA    . PHE   C 2 146 ? -40.47900 37.06300 -17.93800 1.000 23.18011 ? 145 PHE   D CA    1 
ATOM   3906 C  C     . PHE   C 2 146 ? -39.46800 36.24400 -18.72000 1.000 21.20374 ? 145 PHE   D C     1 
ATOM   3907 O  O     . PHE   C 2 146 ? -39.64400 35.03200 -18.82700 1.000 23.83704 ? 145 PHE   D O     1 
ATOM   3908 C  CB    . PHE   C 2 146 ? -41.88000 36.94000 -18.54100 1.000 22.94015 ? 145 PHE   D CB    1 
ATOM   3909 C  CG    . PHE   C 2 146 ? -42.90500 37.72300 -17.78000 1.000 20.17098 ? 145 PHE   D CG    1 
ATOM   3910 C  CD1   . PHE   C 2 146 ? -43.34500 37.27300 -16.54700 1.000 20.28709 ? 145 PHE   D CD1   1 
ATOM   3911 C  CD2   . PHE   C 2 146 ? -43.39300 38.93300 -18.26300 1.000 20.68608 ? 145 PHE   D CD2   1 
ATOM   3912 C  CE1   . PHE   C 2 146 ? -44.26200 37.99500 -15.82000 1.000 20.75717 ? 145 PHE   D CE1   1 
ATOM   3913 C  CE2   . PHE   C 2 146 ? -44.31900 39.66200 -17.53600 1.000 20.49467 ? 145 PHE   D CE2   1 
ATOM   3914 C  CZ    . PHE   C 2 146 ? -44.75900 39.19000 -16.31400 1.000 19.66183 ? 145 PHE   D CZ    1 
ATOM   3915 N  N     . GLY   C 2 147 ? -38.41100 36.86400 -19.24300 1.000 22.72369 ? 146 GLY   D N     1 
ATOM   3916 C  CA    . GLY   C 2 147 ? -37.38800 36.15200 -19.98100 1.000 19.29314 ? 146 GLY   D CA    1 
ATOM   3917 C  C     . GLY   C 2 147 ? -36.24800 35.69300 -19.09500 1.000 19.40211 ? 146 GLY   D C     1 
ATOM   3918 O  O     . GLY   C 2 147 ? -36.28700 35.80500 -17.86900 1.000 21.69086 ? 146 GLY   D O     1 
ATOM   3919 N  N     . SER   C 2 148 ? -35.19700 35.19000 -19.75000 1.000 17.86931 ? 147 SER   D N     1 
ATOM   3920 C  CA    . SER   C 2 148 ? -34.04400 34.61900 -19.06600 1.000 18.50488 ? 147 SER   D CA    1 
ATOM   3921 C  C     . SER   C 2 148 ? -32.89600 34.53300 -20.05900 1.000 19.15181 ? 147 SER   D C     1 
ATOM   3922 O  O     . SER   C 2 148 ? -33.06200 34.79500 -21.25100 1.000 19.30909 ? 147 SER   D O     1 
ATOM   3923 C  CB    . SER   C 2 148 ? -34.35400 33.23300 -18.49500 1.000 18.96115 ? 147 SER   D CB    1 
ATOM   3924 O  OG    . SER   C 2 148 ? -34.58700 32.29300 -19.54400 1.000 17.11798 ? 147 SER   D OG    1 
ATOM   3925 N  N     A ARG   C 2 149 ? -31.74200 34.10100 -19.56300 0.630 19.42524 ? 148 ARG   D N     1 
ATOM   3926 N  N     B ARG   C 2 149 ? -31.71800 34.15400 -19.54200 0.370 19.72736 ? 148 ARG   D N     1 
ATOM   3927 C  CA    A ARG   C 2 149 ? -30.53100 34.14500 -20.36700 0.630 19.31069 ? 148 ARG   D CA    1 
ATOM   3928 C  CA    B ARG   C 2 149 ? -30.51000 34.11000 -20.36700 0.370 20.23627 ? 148 ARG   D CA    1 
ATOM   3929 C  C     A ARG   C 2 149 ? -30.57400 33.17300 -21.54700 0.630 18.82633 ? 148 ARG   D C     1 
ATOM   3930 C  C     B ARG   C 2 149 ? -30.70100 33.23500 -21.60000 0.370 20.43857 ? 148 ARG   D C     1 
ATOM   3931 O  O     A ARG   C 2 149 ? -29.92900 33.42800 -22.57200 0.630 18.50666 ? 148 ARG   D O     1 
ATOM   3932 O  O     B ARG   C 2 149 ? -30.29500 33.61400 -22.70600 0.370 19.69725 ? 148 ARG   D O     1 
ATOM   3933 C  CB    A ARG   C 2 149 ? -29.32500 33.90300 -19.46800 0.630 20.78456 ? 148 ARG   D CB    1 
ATOM   3934 C  CB    B ARG   C 2 149 ? -29.30800 33.62700 -19.54500 0.370 20.89089 ? 148 ARG   D CB    1 
ATOM   3935 C  CG    A ARG   C 2 149 ? -28.01800 34.33900 -20.06000 0.630 22.04094 ? 148 ARG   D CG    1 
ATOM   3936 C  CG    B ARG   C 2 149 ? -28.03400 33.32900 -20.37400 0.370 20.89538 ? 148 ARG   D CG    1 
ATOM   3937 C  CD    A ARG   C 2 149 ? -26.89200 34.22300 -19.04900 0.630 21.87955 ? 148 ARG   D CD    1 
ATOM   3938 C  CD    B ARG   C 2 149 ? -26.81900 32.98100 -19.49900 0.370 20.39925 ? 148 ARG   D CD    1 
ATOM   3939 N  NE    A ARG   C 2 149 ? -25.61600 34.26600 -19.74700 0.630 22.02053 ? 148 ARG   D NE    1 
ATOM   3940 N  NE    B ARG   C 2 149 ? -25.61300 32.70600 -20.27900 0.370 21.47602 ? 148 ARG   D NE    1 
ATOM   3941 C  CZ    A ARG   C 2 149 ? -24.99200 33.20200 -20.23500 0.630 22.26102 ? 148 ARG   D CZ    1 
ATOM   3942 C  CZ    B ARG   C 2 149 ? -24.76600 33.62800 -20.71700 0.370 22.59226 ? 148 ARG   D CZ    1 
ATOM   3943 N  NH1   A ARG   C 2 149 ? -25.45000 31.98000 -20.03200 0.630 23.75803 ? 148 ARG   D NH1   1 
ATOM   3944 N  NH1   B ARG   C 2 149 ? -24.95600 34.91500 -20.47600 0.370 22.13773 ? 148 ARG   D NH1   1 
ATOM   3945 N  NH2   A ARG   C 2 149 ? -23.88400 33.37000 -20.95200 0.630 25.20020 ? 148 ARG   D NH2   1 
ATOM   3946 N  NH2   B ARG   C 2 149 ? -23.70400 33.25000 -21.42100 0.370 24.13953 ? 148 ARG   D NH2   1 
ATOM   3947 N  N     . ASN   C 2 150 ? -31.31800 32.06800 -21.43600 1.000 19.19183 ? 149 ASN   D N     1 
ATOM   3948 C  CA    . ASN   C 2 150 ? -31.50000 31.14000 -22.55100 1.000 20.20445 ? 149 ASN   D CA    1 
ATOM   3949 C  C     . ASN   C 2 150 ? -32.80900 31.35700 -23.29000 1.000 17.12638 ? 149 ASN   D C     1 
ATOM   3950 O  O     . ASN   C 2 150 ? -33.16100 30.54400 -24.15800 1.000 18.18915 ? 149 ASN   D O     1 
ATOM   3951 C  CB    . ASN   C 2 150 ? -31.33200 29.66800 -22.12800 1.000 20.67742 ? 149 ASN   D CB    1 
ATOM   3952 C  CG    . ASN   C 2 150 ? -32.47400 29.14000 -21.27300 1.000 20.28871 ? 149 ASN   D CG    1 
ATOM   3953 O  OD1   . ASN   C 2 150 ? -33.45500 29.83500 -21.00800 1.000 19.30257 ? 149 ASN   D OD1   1 
ATOM   3954 N  ND2   . ASN   C 2 150 ? -32.35200 27.88100 -20.84900 1.000 22.76364 ? 149 ASN   D ND2   1 
ATOM   3955 N  N     . GLY   C 2 151 ? -33.52500 32.43300 -22.97000 1.000 15.68863 ? 150 GLY   D N     1 
ATOM   3956 C  CA    . GLY   C 2 151 ? -34.74300 32.80300 -23.65100 1.000 15.70086 ? 150 GLY   D CA    1 
ATOM   3957 C  C     . GLY   C 2 151 ? -36.01300 32.18200 -23.12100 1.000 14.36342 ? 150 GLY   D C     1 
ATOM   3958 O  O     . GLY   C 2 151 ? -37.10100 32.64000 -23.48500 1.000 15.01026 ? 150 GLY   D O     1 
ATOM   3959 N  N     . LYS   C 2 152 ? -35.93100 31.15300 -22.28300 1.000 15.14872 ? 151 LYS   D N     1 
ATOM   3960 C  CA    . LYS   C 2 152 ? -37.14600 30.53900 -21.76700 1.000 16.37142 ? 151 LYS   D CA    1 
ATOM   3961 C  C     . LYS   C 2 152 ? -37.90200 31.52700 -20.89300 1.000 15.94733 ? 151 LYS   D C     1 
ATOM   3962 O  O     . LYS   C 2 152 ? -37.31600 32.26900 -20.10000 1.000 16.66492 ? 151 LYS   D O     1 
ATOM   3963 C  CB    . LYS   C 2 152 ? -36.80400 29.29900 -20.95300 1.000 18.18928 ? 151 LYS   D CB    1 
ATOM   3964 C  CG    . LYS   C 2 152 ? -36.26200 28.14000 -21.78000 1.000 21.03647 ? 151 LYS   D CG    1 
ATOM   3965 C  CD    . LYS   C 2 152 ? -37.34200 27.51200 -22.64900 1.000 23.95950 ? 151 LYS   D CD    1 
ATOM   3966 C  CE    . LYS   C 2 152 ? -36.78500 26.39800 -23.51900 1.000 28.58947 ? 151 LYS   D CE    1 
ATOM   3967 N  NZ    . LYS   C 2 152 ? -37.84800 25.76600 -24.34600 1.000 31.84769 ? 151 LYS   D NZ    1 
ATOM   3968 N  N     . THR   C 2 153 ? -39.21900 31.51700 -21.02000 1.000 17.83518 ? 152 THR   D N     1 
ATOM   3969 C  CA    . THR   C 2 153 ? -40.05800 32.45100 -20.28300 1.000 19.96903 ? 152 THR   D CA    1 
ATOM   3970 C  C     . THR   C 2 153 ? -40.67000 31.78000 -19.05600 1.000 21.26876 ? 152 THR   D C     1 
ATOM   3971 O  O     . THR   C 2 153 ? -40.95800 30.57800 -19.05100 1.000 23.85209 ? 152 THR   D O     1 
ATOM   3972 C  CB    . THR   C 2 153 ? -41.14700 33.05600 -21.17600 1.000 21.62149 ? 152 THR   D CB    1 
ATOM   3973 O  OG1   . THR   C 2 153 ? -42.00100 32.01900 -21.66900 1.000 23.77908 ? 152 THR   D OG1   1 
ATOM   3974 C  CG2   . THR   C 2 153 ? -40.51100 33.77600 -22.36500 1.000 20.14433 ? 152 THR   D CG2   1 
ATOM   3975 N  N     . SER   C 2 154 ? -40.86200 32.57400 -18.00200 1.000 22.04765 ? 153 SER   D N     1 
ATOM   3976 C  CA    . SER   C 2 154 ? -41.35600 32.04300 -16.73700 1.000 24.81107 ? 153 SER   D CA    1 
ATOM   3977 C  C     . SER   C 2 154 ? -42.87500 32.01300 -16.65900 1.000 25.13596 ? 153 SER   D C     1 
ATOM   3978 O  O     . SER   C 2 154 ? -43.42600 31.33400 -15.78500 1.000 26.57575 ? 153 SER   D O     1 
ATOM   3979 C  CB    . SER   C 2 154 ? -40.75800 32.82700 -15.56600 1.000 27.00678 ? 153 SER   D CB    1 
ATOM   3980 O  OG    . SER   C 2 154 ? -40.95400 34.21900 -15.71400 1.000 28.43414 ? 153 SER   D OG    1 
ATOM   3981 N  N     . LYS   C 2 155 ? -43.54900 32.74400 -17.54000 1.000 23.08636 ? 154 LYS   D N     1 
ATOM   3982 C  CA    . LYS   C 2 155 ? -44.98600 32.66400 -17.74200 1.000 22.60242 ? 154 LYS   D CA    1 
ATOM   3983 C  C     . LYS   C 2 155 ? -45.22700 32.69700 -19.23900 1.000 22.49771 ? 154 LYS   D C     1 
ATOM   3984 O  O     . LYS   C 2 155 ? -44.34200 33.05700 -20.02100 1.000 23.92199 ? 154 LYS   D O     1 
ATOM   3985 C  CB    . LYS   C 2 155 ? -45.71400 33.83600 -17.07700 1.000 21.42328 ? 154 LYS   D CB    1 
ATOM   3986 C  CG    . LYS   C 2 155 ? -45.56800 33.84600 -15.57200 1.000 23.60095 ? 154 LYS   D CG    1 
ATOM   3987 C  CD    . LYS   C 2 155 ? -46.41300 34.93400 -14.95200 1.000 25.75658 ? 154 LYS   D CD    1 
ATOM   3988 C  CE    . LYS   C 2 155 ? -46.12000 35.09400 -13.48700 1.000 27.28339 ? 154 LYS   D CE    1 
ATOM   3989 N  NZ    . LYS   C 2 155 ? -47.26400 35.76500 -12.81800 1.000 30.33493 ? 154 LYS   D NZ    1 
ATOM   3990 N  N     . LYS   C 2 156 ? -46.44300 32.35200 -19.64200 1.000 20.61687 ? 155 LYS   D N     1 
ATOM   3991 C  CA    . LYS   C 2 156 ? -46.75600 32.28800 -21.06000 1.000 21.16218 ? 155 LYS   D CA    1 
ATOM   3992 C  C     . LYS   C 2 156 ? -47.11800 33.67900 -21.56000 1.000 17.71621 ? 155 LYS   D C     1 
ATOM   3993 O  O     . LYS   C 2 156 ? -48.12400 34.25100 -21.13800 1.000 17.27768 ? 155 LYS   D O     1 
ATOM   3994 C  CB    . LYS   C 2 156 ? -47.89700 31.30700 -21.30600 1.000 25.22008 ? 155 LYS   D CB    1 
ATOM   3995 C  CG    . LYS   C 2 156 ? -48.04500 30.95500 -22.75400 1.000 32.21456 ? 155 LYS   D CG    1 
ATOM   3996 C  CD    . LYS   C 2 156 ? -47.77100 29.50000 -22.95600 1.000 34.13421 ? 155 LYS   D CD    1 
ATOM   3997 C  CE    . LYS   C 2 156 ? -47.49600 29.20900 -24.41100 1.000 35.99561 ? 155 LYS   D CE    1 
ATOM   3998 N  NZ    . LYS   C 2 156 ? -48.69600 29.51200 -25.19700 1.000 35.51973 ? 155 LYS   D NZ    1 
ATOM   3999 N  N     . ILE   C 2 157 ? -46.31200 34.21100 -22.47100 1.000 15.55735 ? 156 ILE   D N     1 
ATOM   4000 C  CA    . ILE   C 2 157 ? -46.49800 35.55500 -23.00300 1.000 14.06833 ? 156 ILE   D CA    1 
ATOM   4001 C  C     . ILE   C 2 157 ? -47.10200 35.40800 -24.39200 1.000 14.91881 ? 156 ILE   D C     1 
ATOM   4002 O  O     . ILE   C 2 157 ? -46.42800 34.92100 -25.29900 1.000 16.74221 ? 156 ILE   D O     1 
ATOM   4003 C  CB    . ILE   C 2 157 ? -45.16500 36.31100 -23.07000 1.000 15.80529 ? 156 ILE   D CB    1 
ATOM   4004 C  CG1   . ILE   C 2 157 ? -44.39700 36.19100 -21.74200 1.000 17.61567 ? 156 ILE   D CG1   1 
ATOM   4005 C  CG2   . ILE   C 2 157 ? -45.41100 37.75800 -23.47100 1.000 15.96816 ? 156 ILE   D CG2   1 
ATOM   4006 C  CD1   . ILE   C 2 157 ? -45.19900 36.56200 -20.47100 1.000 19.62791 ? 156 ILE   D CD1   1 
ATOM   4007 N  N     . THR   C 2 158 ? -48.36600 35.81300 -24.57400 1.000 14.58728 ? 157 THR   D N     1 
ATOM   4008 C  CA    . THR   C 2 158 ? -49.06200 35.56600 -25.82900 1.000 14.62515 ? 157 THR   D CA    1 
ATOM   4009 C  C     . THR   C 2 158 ? -49.61800 36.83800 -26.45700 1.000 13.18373 ? 157 THR   D C     1 
ATOM   4010 O  O     . THR   C 2 158 ? -49.84200 37.86600 -25.80500 1.000 14.40406 ? 157 THR   D O     1 
ATOM   4011 C  CB    . THR   C 2 158 ? -50.20700 34.58000 -25.66200 1.000 16.20010 ? 157 THR   D CB    1 
ATOM   4012 O  OG1   . THR   C 2 158 ? -51.12800 35.10500 -24.70200 1.000 17.38963 ? 157 THR   D OG1   1 
ATOM   4013 C  CG2   . THR   C 2 158 ? -49.69100 33.22500 -25.19000 1.000 17.71003 ? 157 THR   D CG2   1 
ATOM   4014 N  N     . ILE   C 2 159 ? -49.86300 36.71800 -27.75800 1.000 12.67435 ? 158 ILE   D N     1 
ATOM   4015 C  CA    . ILE   C 2 159 ? -50.58000 37.72900 -28.52700 1.000 14.48473 ? 158 ILE   D CA    1 
ATOM   4016 C  C     . ILE   C 2 159 ? -52.05300 37.33000 -28.42400 1.000 14.78025 ? 158 ILE   D C     1 
ATOM   4017 O  O     . ILE   C 2 159 ? -52.57200 36.53700 -29.20900 1.000 16.13116 ? 158 ILE   D O     1 
ATOM   4018 C  CB    . ILE   C 2 159 ? -50.08000 37.78500 -29.97100 1.000 14.57753 ? 158 ILE   D CB    1 
ATOM   4019 C  CG1   . ILE   C 2 159 ? -48.57300 38.07700 -30.00600 1.000 14.28180 ? 158 ILE   D CG1   1 
ATOM   4020 C  CG2   . ILE   C 2 159 ? -50.89700 38.78000 -30.79800 1.000 16.02912 ? 158 ILE   D CG2   1 
ATOM   4021 C  CD1   . ILE   C 2 159 ? -47.97300 37.92600 -31.38400 1.000 15.45091 ? 158 ILE   D CD1   1 
ATOM   4022 N  N     . ALA   C 2 160 ? -52.73800 37.85800 -27.40700 1.000 14.49343 ? 159 ALA   D N     1 
ATOM   4023 C  CA    . ALA   C 2 160 ? -54.12800 37.46800 -27.19400 1.000 15.95246 ? 159 ALA   D CA    1 
ATOM   4024 C  C     . ALA   C 2 160 ? -55.03400 37.99900 -28.30000 1.000 16.58392 ? 159 ALA   D C     1 
ATOM   4025 O  O     . ALA   C 2 160 ? -56.04400 37.36500 -28.63800 1.000 17.71717 ? 159 ALA   D O     1 
ATOM   4026 C  CB    . ALA   C 2 160 ? -54.61000 37.96500 -25.83000 1.000 16.50201 ? 159 ALA   D CB    1 
ATOM   4027 N  N     . ASP   C 2 161 ? -54.70500 39.16400 -28.84800 1.000 16.14182 ? 160 ASP   D N     1 
ATOM   4028 C  CA    . ASP   C 2 161 ? -55.43800 39.72700 -29.97100 1.000 17.46296 ? 160 ASP   D CA    1 
ATOM   4029 C  C     . ASP   C 2 161 ? -54.45800 40.53000 -30.81600 1.000 15.77248 ? 160 ASP   D C     1 
ATOM   4030 O  O     . ASP   C 2 161 ? -53.41500 40.98400 -30.33600 1.000 15.57855 ? 160 ASP   D O     1 
ATOM   4031 C  CB    . ASP   C 2 161 ? -56.59400 40.61700 -29.48600 1.000 19.08045 ? 160 ASP   D CB    1 
ATOM   4032 C  CG    . ASP   C 2 161 ? -57.67600 40.80600 -30.53300 1.000 24.47646 ? 160 ASP   D CG    1 
ATOM   4033 O  OD1   . ASP   C 2 161 ? -57.60500 40.16900 -31.61600 1.000 23.75675 ? 160 ASP   D OD1   1 
ATOM   4034 O  OD2   . ASP   C 2 161 ? -58.60600 41.58300 -30.25300 1.000 27.03461 ? 160 ASP   D OD2   1 
ATOM   4035 N  N     . CYS   C 2 162 ? -54.80500 40.71200 -32.08500 1.000 16.94973 ? 161 CYS   D N     1 
ATOM   4036 C  CA    . CYS   C 2 162 ? -53.97000 41.50900 -32.97400 1.000 15.95078 ? 161 CYS   D CA    1 
ATOM   4037 C  C     . CYS   C 2 162 ? -54.78900 41.92100 -34.18800 1.000 16.75529 ? 161 CYS   D C     1 
ATOM   4038 O  O     . CYS   C 2 162 ? -55.80300 41.30300 -34.51000 1.000 18.72695 ? 161 CYS   D O     1 
ATOM   4039 C  CB    . CYS   C 2 162 ? -52.67400 40.76700 -33.37400 1.000 15.78409 ? 161 CYS   D CB    1 
ATOM   4040 S  SG    . CYS   C 2 162 ? -52.87400 39.12800 -34.02200 1.000 15.94920 ? 161 CYS   D SG    1 
ATOM   4041 N  N     . GLY   C 2 163 ? -54.33900 42.97500 -34.85300 1.000 17.34347 ? 162 GLY   D N     1 
ATOM   4042 C  CA    . GLY   C 2 163 ? -55.06700 43.47900 -36.00100 1.000 17.96449 ? 162 GLY   D CA    1 
ATOM   4043 C  C     . GLY   C 2 163 ? -54.44700 44.75500 -36.51700 1.000 17.48581 ? 162 GLY   D C     1 
ATOM   4044 O  O     . GLY   C 2 163 ? -53.33900 45.13000 -36.12900 1.000 18.50736 ? 162 GLY   D O     1 
ATOM   4045 N  N     . GLN   C 2 164 ? -55.15500 45.39800 -37.44000 1.000 19.22445 ? 163 GLN   D N     1 
ATOM   4046 C  CA    . GLN   C 2 164 ? -54.68100 46.61800 -38.07800 1.000 19.81268 ? 163 GLN   D CA    1 
ATOM   4047 C  C     . GLN   C 2 164 ? -55.47800 47.80600 -37.56400 1.000 21.00452 ? 163 GLN   D C     1 
ATOM   4048 O  O     . GLN   C 2 164 ? -56.70300 47.72800 -37.42100 1.000 22.78229 ? 163 GLN   D O     1 
ATOM   4049 C  CB    . GLN   C 2 164 ? -54.79800 46.52000 -39.60200 1.000 21.60564 ? 163 GLN   D CB    1 
ATOM   4050 C  CG    . GLN   C 2 164 ? -54.19500 47.70200 -40.34700 1.000 21.08438 ? 163 GLN   D CG    1 
ATOM   4051 C  CD    . GLN   C 2 164 ? -54.12000 47.49200 -41.84900 1.000 22.03471 ? 163 GLN   D CD    1 
ATOM   4052 O  OE1   . GLN   C 2 164 ? -54.47900 46.43200 -42.36700 1.000 23.98050 ? 163 GLN   D OE1   1 
ATOM   4053 N  NE2   . GLN   C 2 164 ? -53.64400 48.50400 -42.55400 1.000 22.20223 ? 163 GLN   D NE2   1 
ATOM   4054 N  N     . LEU   C 2 165 ? -54.77500 48.89200 -37.26300 1.000 22.43875 ? 164 LEU   D N     1 
ATOM   4055 C  CA    . LEU   C 2 165 ? -55.39600 50.12700 -36.79800 1.000 25.67931 ? 164 LEU   D CA    1 
ATOM   4056 C  C     . LEU   C 2 165 ? -55.64100 51.04800 -37.97900 1.000 30.53909 ? 164 LEU   D C     1 
ATOM   4057 O  O     . LEU   C 2 165 ? -54.80500 51.15100 -38.87600 1.000 33.57704 ? 164 LEU   D O     1 
ATOM   4058 C  CB    . LEU   C 2 165 ? -54.50200 50.83000 -35.77700 1.000 26.41369 ? 164 LEU   D CB    1 
ATOM   4059 C  CG    . LEU   C 2 165 ? -54.27800 50.05800 -34.47600 1.000 28.13786 ? 164 LEU   D CG    1 
ATOM   4060 C  CD1   . LEU   C 2 165 ? -53.27800 50.77200 -33.56900 1.000 28.12260 ? 164 LEU   D CD1   1 
ATOM   4061 C  CD2   . LEU   C 2 165 ? -55.60300 49.83400 -33.76000 1.000 28.74799 ? 164 LEU   D CD2   1 
ATOM   4062 N  N     . MET   D 2 2   ? -53.31100 -5.57500 14.28500  1.000 40.76812 ? 1   MET   C N     1 
ATOM   4063 C  CA    . MET   D 2 2   ? -51.85700 -5.65200 14.23300  1.000 36.53439 ? 1   MET   C CA    1 
ATOM   4064 C  C     . MET   D 2 2   ? -51.25400 -4.59800 15.13300  1.000 32.71832 ? 1   MET   C C     1 
ATOM   4065 O  O     . MET   D 2 2   ? -51.82600 -3.51800 15.31700  1.000 30.97101 ? 1   MET   C O     1 
ATOM   4066 C  CB    . MET   D 2 2   ? -51.36300 -5.47300 12.79900  1.000 36.28316 ? 1   MET   C CB    1 
ATOM   4067 C  CG    . MET   D 2 2   ? -51.88700 -6.54800 11.86600  1.000 36.22797 ? 1   MET   C CG    1 
ATOM   4068 S  SD    . MET   D 2 2   ? -51.50100 -8.20300 12.47200  1.000 35.05517 ? 1   MET   C SD    1 
ATOM   4069 C  CE    . MET   D 2 2   ? -49.72200 -8.22200 12.22100  1.000 36.18590 ? 1   MET   C CE    1 
ATOM   4070 N  N     . VAL   D 2 3   ? -50.08900 -4.90600 15.69900  1.000 27.70156 ? 2   VAL   C N     1 
ATOM   4071 C  CA    . VAL   D 2 3   ? -49.38000 -3.89000 16.46300  1.000 25.46401 ? 2   VAL   C CA    1 
ATOM   4072 C  C     . VAL   D 2 3   ? -49.00600 -2.71400 15.56600  1.000 24.75870 ? 2   VAL   C C     1 
ATOM   4073 O  O     . VAL   D 2 3   ? -49.18300 -1.54800 15.94100  1.000 27.80075 ? 2   VAL   C O     1 
ATOM   4074 C  CB    . VAL   D 2 3   ? -48.16200 -4.50200 17.17400  1.000 25.86603 ? 2   VAL   C CB    1 
ATOM   4075 C  CG1   . VAL   D 2 3   ? -47.35800 -3.41200 17.87500  1.000 26.82879 ? 2   VAL   C CG1   1 
ATOM   4076 C  CG2   . VAL   D 2 3   ? -48.61800 -5.56100 18.16600  1.000 26.76682 ? 2   VAL   C CG2   1 
ATOM   4077 N  N     . ASN   D 2 4   ? -48.49800 -2.99300 14.36200  1.000 19.28965 ? 3   ASN   C N     1 
ATOM   4078 C  CA    . ASN   D 2 4   ? -48.04900 -1.92200 13.48700  1.000 15.01087 ? 3   ASN   C CA    1 
ATOM   4079 C  C     . ASN   D 2 4   ? -49.18600 -1.46300 12.58800  1.000 16.57376 ? 3   ASN   C C     1 
ATOM   4080 O  O     . ASN   D 2 4   ? -49.72200 -2.27700 11.81500  1.000 19.28526 ? 3   ASN   C O     1 
ATOM   4081 C  CB    . ASN   D 2 4   ? -46.86600 -2.36700 12.66000  1.000 15.19042 ? 3   ASN   C CB    1 
ATOM   4082 C  CG    . ASN   D 2 4   ? -45.60400 -2.48500 13.47400  1.000 16.34715 ? 3   ASN   C CG    1 
ATOM   4083 O  OD1   . ASN   D 2 4   ? -45.54200 -2.01300 14.60800  1.000 16.49392 ? 3   ASN   C OD1   1 
ATOM   4084 N  ND2   . ASN   D 2 4   ? -44.57800 -3.10200 12.89500  1.000 17.52825 ? 3   ASN   C ND2   1 
ATOM   4085 N  N     . PRO   D 2 5   ? -49.58900 -0.19900 12.66000  1.000 16.85044 ? 4   PRO   C N     1 
ATOM   4086 C  CA    . PRO   D 2 5   ? -50.63200 0.30900  11.76400  1.000 18.40657 ? 4   PRO   C CA    1 
ATOM   4087 C  C     . PRO   D 2 5   ? -50.14400 0.42700  10.32700  1.000 17.42647 ? 4   PRO   C C     1 
ATOM   4088 O  O     . PRO   D 2 5   ? -48.94500 0.48200  10.04000  1.000 17.38269 ? 4   PRO   C O     1 
ATOM   4089 C  CB    . PRO   D 2 5   ? -50.95600 1.68800  12.34400  1.000 20.07663 ? 4   PRO   C CB    1 
ATOM   4090 C  CG    . PRO   D 2 5   ? -49.74400 2.07600  13.10300  1.000 21.01887 ? 4   PRO   C CG    1 
ATOM   4091 C  CD    . PRO   D 2 5   ? -49.06600 0.82400  13.57700  1.000 17.82737 ? 4   PRO   C CD    1 
ATOM   4092 N  N     . THR   D 2 6   ? -51.11600 0.45700  9.42100   1.000 16.47340 ? 5   THR   C N     1 
ATOM   4093 C  CA    A THR   D 2 6   ? -50.88400 0.66800  7.99700   0.500 16.64333 ? 5   THR   C CA    1 
ATOM   4094 C  CA    B THR   D 2 6   ? -50.86800 0.67600  8.00300   0.500 19.16364 ? 5   THR   C CA    1 
ATOM   4095 C  C     . THR   D 2 6   ? -51.59100 1.94500  7.57200   1.000 16.14820 ? 5   THR   C C     1 
ATOM   4096 O  O     . THR   D 2 6   ? -52.77600 2.12500  7.87200   1.000 18.16513 ? 5   THR   C O     1 
ATOM   4097 C  CB    A THR   D 2 6   ? -51.46300 -0.48300 7.17200   0.500 16.66898 ? 5   THR   C CB    1 
ATOM   4098 C  CB    B THR   D 2 6   ? -51.37600 -0.50100 7.17300   0.500 23.41895 ? 5   THR   C CB    1 
ATOM   4099 O  OG1   A THR   D 2 6   ? -50.89100 -1.72100 7.59800   0.500 18.77552 ? 5   THR   C OG1   1 
ATOM   4100 O  OG1   B THR   D 2 6   ? -52.74900 -0.74000 7.48600   0.500 27.25896 ? 5   THR   C OG1   1 
ATOM   4101 C  CG2   A THR   D 2 6   ? -51.16100 -0.26700 5.70000   0.500 16.43966 ? 5   THR   C CG2   1 
ATOM   4102 C  CG2   B THR   D 2 6   ? -50.57500 -1.74900 7.47300   0.500 25.87899 ? 5   THR   C CG2   1 
ATOM   4103 N  N     . VAL   D 2 7   ? -50.88400 2.83000  6.87200   1.000 15.52319 ? 6   VAL   C N     1 
ATOM   4104 C  CA    . VAL   D 2 7   ? -51.53000 4.02600  6.33400   1.000 15.73445 ? 6   VAL   C CA    1 
ATOM   4105 C  C     . VAL   D 2 7   ? -51.30000 4.07100  4.82700   1.000 15.20074 ? 6   VAL   C C     1 
ATOM   4106 O  O     . VAL   D 2 7   ? -50.45800 3.35200  4.27900   1.000 15.78210 ? 6   VAL   C O     1 
ATOM   4107 C  CB    . VAL   D 2 7   ? -51.06000 5.32200  7.02000   1.000 17.08963 ? 6   VAL   C CB    1 
ATOM   4108 C  CG1   . VAL   D 2 7   ? -51.42200 5.30200  8.50400   1.000 20.25044 ? 6   VAL   C CG1   1 
ATOM   4109 C  CG2   . VAL   D 2 7   ? -49.57400 5.49800  6.80400   1.000 18.05064 ? 6   VAL   C CG2   1 
ATOM   4110 N  N     . PHE   D 2 8   ? -52.07500 4.91400  4.14400   1.000 15.68354 ? 7   PHE   C N     1 
ATOM   4111 C  CA    . PHE   D 2 8   ? -51.94700 5.04700  2.69900   1.000 16.86276 ? 7   PHE   C CA    1 
ATOM   4112 C  C     . PHE   D 2 8   ? -51.89000 6.50900  2.30500   1.000 14.04709 ? 7   PHE   C C     1 
ATOM   4113 O  O     . PHE   D 2 8   ? -52.45900 7.37100  2.98100   1.000 14.70912 ? 7   PHE   C O     1 
ATOM   4114 C  CB    . PHE   D 2 8   ? -53.10800 4.38900  1.92800   1.000 19.53401 ? 7   PHE   C CB    1 
ATOM   4115 C  CG    . PHE   D 2 8   ? -54.41600 5.11600  2.04600   1.000 20.84548 ? 7   PHE   C CG    1 
ATOM   4116 C  CD1   . PHE   D 2 8   ? -55.27300 4.83800  3.09000   1.000 20.75718 ? 7   PHE   C CD1   1 
ATOM   4117 C  CD2   . PHE   D 2 8   ? -54.79300 6.06500  1.10100   1.000 21.98182 ? 7   PHE   C CD2   1 
ATOM   4118 C  CE1   . PHE   D 2 8   ? -56.49000 5.50300  3.19500   1.000 21.02444 ? 7   PHE   C CE1   1 
ATOM   4119 C  CE2   . PHE   D 2 8   ? -55.99800 6.74200  1.21200   1.000 21.97695 ? 7   PHE   C CE2   1 
ATOM   4120 C  CZ    . PHE   D 2 8   ? -56.84800 6.45700  2.25800   1.000 21.97108 ? 7   PHE   C CZ    1 
ATOM   4121 N  N     . PHE   D 2 9   ? -51.19200 6.76800  1.19600   1.000 14.78312 ? 8   PHE   C N     1 
ATOM   4122 C  CA    . PHE   D 2 9   ? -51.27000 8.02900  0.47500   1.000 15.03463 ? 8   PHE   C CA    1 
ATOM   4123 C  C     . PHE   D 2 9   ? -51.77300 7.72400  -0.92600  1.000 14.67003 ? 8   PHE   C C     1 
ATOM   4124 O  O     . PHE   D 2 9   ? -51.23800 6.82700  -1.59400  1.000 16.35891 ? 8   PHE   C O     1 
ATOM   4125 C  CB    . PHE   D 2 9   ? -49.88800 8.64800  0.27300   1.000 14.52547 ? 8   PHE   C CB    1 
ATOM   4126 C  CG    . PHE   D 2 9   ? -49.23000 9.19800  1.50900   1.000 14.89835 ? 8   PHE   C CG    1 
ATOM   4127 C  CD1   . PHE   D 2 9   ? -49.88300 9.31500  2.71900   1.000 16.33793 ? 8   PHE   C CD1   1 
ATOM   4128 C  CD2   . PHE   D 2 9   ? -47.90000 9.60100  1.43200   1.000 14.77157 ? 8   PHE   C CD2   1 
ATOM   4129 C  CE1   . PHE   D 2 9   ? -49.20800 9.83700  3.83000   1.000 14.86525 ? 8   PHE   C CE1   1 
ATOM   4130 C  CE2   . PHE   D 2 9   ? -47.23800 10.10500 2.52700   1.000 15.32429 ? 8   PHE   C CE2   1 
ATOM   4131 C  CZ    . PHE   D 2 9   ? -47.88500 10.23400 3.72800   1.000 15.21513 ? 8   PHE   C CZ    1 
ATOM   4132 N  N     . ASP   D 2 10  ? -52.74500 8.50700  -1.39900  1.000 14.65968 ? 9   ASP   C N     1 
ATOM   4133 C  CA    . ASP   D 2 10  ? -53.08600 8.54100  -2.81700  1.000 15.14685 ? 9   ASP   C CA    1 
ATOM   4134 C  C     . ASP   D 2 10  ? -52.33300 9.72100  -3.43000  1.000 14.13798 ? 9   ASP   C C     1 
ATOM   4135 O  O     . ASP   D 2 10  ? -52.57300 10.87800 -3.06500  1.000 16.99018 ? 9   ASP   C O     1 
ATOM   4136 C  CB    . ASP   D 2 10  ? -54.59700 8.67400  -3.02700  1.000 17.11888 ? 9   ASP   C CB    1 
ATOM   4137 C  CG    . ASP   D 2 10  ? -55.34400 7.39200  -2.67100  1.000 20.44899 ? 9   ASP   C CG    1 
ATOM   4138 O  OD1   . ASP   D 2 10  ? -54.82800 6.28800  -2.95900  1.000 24.01629 ? 9   ASP   C OD1   1 
ATOM   4139 O  OD2   . ASP   D 2 10  ? -56.46100 7.48800  -2.11500  1.000 24.34849 ? 9   ASP   C OD2   1 
ATOM   4140 N  N     . ILE   D 2 11  ? -51.41900 9.42800  -4.34100  1.000 14.57973 ? 10  ILE   C N     1 
ATOM   4141 C  CA    . ILE   D 2 11  ? -50.52500 10.42000 -4.92200  1.000 15.68442 ? 10  ILE   C CA    1 
ATOM   4142 C  C     . ILE   D 2 11  ? -51.13800 10.99900 -6.18900  1.000 15.62401 ? 10  ILE   C C     1 
ATOM   4143 O  O     . ILE   D 2 11  ? -51.69100 10.26700 -7.01700  1.000 16.14129 ? 10  ILE   C O     1 
ATOM   4144 C  CB    . ILE   D 2 11  ? -49.15200 9.79200  -5.22400  1.000 15.10912 ? 10  ILE   C CB    1 
ATOM   4145 C  CG1   . ILE   D 2 11  ? -48.55400 9.14500  -3.97400  1.000 15.92452 ? 10  ILE   C CG1   1 
ATOM   4146 C  CG2   . ILE   D 2 11  ? -48.19600 10.84400 -5.78700  1.000 16.29503 ? 10  ILE   C CG2   1 
ATOM   4147 C  CD1   . ILE   D 2 11  ? -48.15700 10.13200 -2.91300  1.000 17.21773 ? 10  ILE   C CD1   1 
ATOM   4148 N  N     . ALA   D 2 12  ? -50.98500 12.31100 -6.37000  1.000 15.41574 ? 11  ALA   C N     1 
ATOM   4149 C  CA    . ALA   D 2 12  ? -51.47000 13.00400 -7.55600  1.000 16.70791 ? 11  ALA   C CA    1 
ATOM   4150 C  C     . ALA   D 2 12  ? -50.34000 13.77300 -8.22200  1.000 15.55285 ? 11  ALA   C C     1 
ATOM   4151 O  O     . ALA   D 2 12  ? -49.41100 14.25300 -7.56000  1.000 16.46365 ? 11  ALA   C O     1 
ATOM   4152 C  CB    . ALA   D 2 12  ? -52.61000 13.97500 -7.22200  1.000 16.75610 ? 11  ALA   C CB    1 
ATOM   4153 N  N     . VAL   D 2 13  ? -50.44200 13.88100 -9.54700  1.000 15.58562 ? 12  VAL   C N     1 
ATOM   4154 C  CA    . VAL   D 2 13  ? -49.51000 14.61900 -10.39400 1.000 17.03662 ? 12  VAL   C CA    1 
ATOM   4155 C  C     . VAL   D 2 13  ? -50.32500 15.72000 -11.05400 1.000 17.31954 ? 12  VAL   C C     1 
ATOM   4156 O  O     . VAL   D 2 13  ? -51.19800 15.43500 -11.88300 1.000 17.33987 ? 12  VAL   C O     1 
ATOM   4157 C  CB    . VAL   D 2 13  ? -48.87300 13.71900 -11.46500 1.000 18.54229 ? 12  VAL   C CB    1 
ATOM   4158 C  CG1   . VAL   D 2 13  ? -48.00500 14.54300 -12.39300 1.000 19.80085 ? 12  VAL   C CG1   1 
ATOM   4159 C  CG2   . VAL   D 2 13  ? -48.05800 12.60100 -10.83500 1.000 20.17585 ? 12  VAL   C CG2   1 
ATOM   4160 N  N     . ASP   D 2 14  ? -50.03900 16.97800 -10.70200 1.000 18.40796 ? 13  ASP   C N     1 
ATOM   4161 C  CA    . ASP   D 2 14  ? -50.83800 18.11900 -11.15700 1.000 18.05196 ? 13  ASP   C CA    1 
ATOM   4162 C  C     . ASP   D 2 14  ? -52.33300 17.83100 -10.99800 1.000 18.87463 ? 13  ASP   C C     1 
ATOM   4163 O  O     . ASP   D 2 14  ? -53.14900 18.12800 -11.87300 1.000 19.48403 ? 13  ASP   C O     1 
ATOM   4164 C  CB    . ASP   D 2 14  ? -50.47500 18.55400 -12.58200 1.000 21.50025 ? 13  ASP   C CB    1 
ATOM   4165 C  CG    . ASP   D 2 14  ? -49.16900 19.35100 -12.65000 1.000 25.52817 ? 13  ASP   C CG    1 
ATOM   4166 O  OD1   . ASP   D 2 14  ? -48.63300 19.77600 -11.59100 1.000 26.53395 ? 13  ASP   C OD1   1 
ATOM   4167 O  OD2   . ASP   D 2 14  ? -48.68000 19.56500 -13.78400 1.000 29.43050 ? 13  ASP   C OD2   1 
ATOM   4168 N  N     . GLY   D 2 15  ? -52.68700 17.20900 -9.87300  1.000 17.89435 ? 14  GLY   C N     1 
ATOM   4169 C  CA    . GLY   D 2 15  ? -54.06700 16.90900 -9.55700  1.000 17.15186 ? 14  GLY   C CA    1 
ATOM   4170 C  C     . GLY   D 2 15  ? -54.59600 15.59600 -10.10400 1.000 17.59040 ? 14  GLY   C C     1 
ATOM   4171 O  O     . GLY   D 2 15  ? -55.68800 15.17700 -9.69800  1.000 20.53577 ? 14  GLY   C O     1 
ATOM   4172 N  N     . GLU   D 2 16  ? -53.86600 14.92700 -11.00600 1.000 16.14349 ? 15  GLU   C N     1 
ATOM   4173 C  CA    . GLU   D 2 16  ? -54.34200 13.67500 -11.59000 1.000 15.99228 ? 15  GLU   C CA    1 
ATOM   4174 C  C     . GLU   D 2 16  ? -53.86700 12.47900 -10.77200 1.000 16.39528 ? 15  GLU   C C     1 
ATOM   4175 O  O     . GLU   D 2 16  ? -52.71800 12.45500 -10.31700 1.000 16.65750 ? 15  GLU   C O     1 
ATOM   4176 C  CB    . GLU   D 2 16  ? -53.81900 13.52600 -13.00900 1.000 16.76711 ? 15  GLU   C CB    1 
ATOM   4177 C  CG    . GLU   D 2 16  ? -54.31400 14.59700 -13.92900 1.000 17.93312 ? 15  GLU   C CG    1 
ATOM   4178 C  CD    . GLU   D 2 16  ? -55.81800 14.53200 -14.09300 1.000 19.31017 ? 15  GLU   C CD    1 
ATOM   4179 O  OE1   . GLU   D 2 16  ? -56.36600 13.40400 -14.14000 1.000 19.31806 ? 15  GLU   C OE1   1 
ATOM   4180 O  OE2   . GLU   D 2 16  ? -56.45600 15.60100 -14.17000 1.000 20.54660 ? 15  GLU   C OE2   1 
ATOM   4181 N  N     . PRO   D 2 17  ? -54.72000 11.46900 -10.59100 1.000 17.57445 ? 16  PRO   C N     1 
ATOM   4182 C  CA    . PRO   D 2 17  ? -54.31500 10.30600 -9.78800  1.000 17.49300 ? 16  PRO   C CA    1 
ATOM   4183 C  C     . PRO   D 2 17  ? -53.12700 9.60400  -10.42500 1.000 18.86291 ? 16  PRO   C C     1 
ATOM   4184 O  O     . PRO   D 2 17  ? -53.12900 9.32900  -11.62600 1.000 23.53673 ? 16  PRO   C O     1 
ATOM   4185 C  CB    . PRO   D 2 17  ? -55.55900 9.40600  -9.81000  1.000 20.22197 ? 16  PRO   C CB    1 
ATOM   4186 C  CG    . PRO   D 2 17  ? -56.66700 10.24600 -10.28400 1.000 23.34093 ? 16  PRO   C CG    1 
ATOM   4187 C  CD    . PRO   D 2 17  ? -56.08000 11.32000 -11.14200 1.000 20.38617 ? 16  PRO   C CD    1 
ATOM   4188 N  N     . LEU   D 2 18  ? -52.10300 9.33000  -9.61600  1.000 17.38509 ? 17  LEU   C N     1 
ATOM   4189 C  CA    . LEU   D 2 18  ? -50.98800 8.48700  -10.02900 1.000 17.35809 ? 17  LEU   C CA    1 
ATOM   4190 C  C     . LEU   D 2 18  ? -51.13300 7.06400  -9.49100  1.000 17.97319 ? 17  LEU   C C     1 
ATOM   4191 O  O     . LEU   D 2 18  ? -51.08400 6.08800  -10.25200 1.000 23.61084 ? 17  LEU   C O     1 
ATOM   4192 C  CB    . LEU   D 2 18  ? -49.67000 9.11800  -9.55800  1.000 18.28263 ? 17  LEU   C CB    1 
ATOM   4193 C  CG    . LEU   D 2 18  ? -48.37400 8.41400  -9.97200  1.000 19.56010 ? 17  LEU   C CG    1 
ATOM   4194 C  CD1   . LEU   D 2 18  ? -48.22300 8.38100  -11.50200 1.000 22.42349 ? 17  LEU   C CD1   1 
ATOM   4195 C  CD2   . LEU   D 2 18  ? -47.16000 9.07400  -9.30800  1.000 18.78314 ? 17  LEU   C CD2   1 
ATOM   4196 N  N     . GLY   D 2 19  ? -51.36500 6.93200  -8.19300  1.000 18.06928 ? 18  GLY   C N     1 
ATOM   4197 C  CA    . GLY   D 2 19  ? -51.59300 5.64100  -7.57700  1.000 17.59137 ? 18  GLY   C CA    1 
ATOM   4198 C  C     . GLY   D 2 19  ? -51.42600 5.74000  -6.07700  1.000 15.88297 ? 18  GLY   C C     1 
ATOM   4199 O  O     . GLY   D 2 19  ? -51.14200 6.81200  -5.52600  1.000 18.57938 ? 18  GLY   C O     1 
ATOM   4200 N  N     . ARG   D 2 20  ? -51.58500 4.59200  -5.42200  1.000 18.29312 ? 19  ARG   C N     1 
ATOM   4201 C  CA    . ARG   D 2 20  ? -51.56200 4.51600  -3.96700  1.000 17.21448 ? 19  ARG   C CA    1 
ATOM   4202 C  C     . ARG   D 2 20  ? -50.24400 3.92700  -3.46700  1.000 19.01157 ? 19  ARG   C C     1 
ATOM   4203 O  O     . ARG   D 2 20  ? -49.72400 2.95700  -4.03100  1.000 19.64581 ? 19  ARG   C O     1 
ATOM   4204 C  CB    . ARG   D 2 20  ? -52.73600 3.67200  -3.46100  1.000 18.60016 ? 19  ARG   C CB    1 
ATOM   4205 C  CG    . ARG   D 2 20  ? -52.75800 3.47900  -1.94600  1.000 20.26086 ? 19  ARG   C CG    1 
ATOM   4206 C  CD    . ARG   D 2 20  ? -54.07200 2.87500  -1.46500  1.000 20.09336 ? 19  ARG   C CD    1 
ATOM   4207 N  NE    . ARG   D 2 20  ? -55.16300 3.83400  -1.57800  1.000 20.98188 ? 19  ARG   C NE    1 
ATOM   4208 C  CZ    . ARG   D 2 20  ? -56.34400 3.70900  -0.99200  1.000 23.47569 ? 19  ARG   C CZ    1 
ATOM   4209 N  NH1   . ARG   D 2 20  ? -56.64300 2.65100  -0.26000  1.000 23.21450 ? 19  ARG   C NH1   1 
ATOM   4210 N  NH2   . ARG   D 2 20  ? -57.24100 4.67600  -1.13800  1.000 27.93572 ? 19  ARG   C NH2   1 
ATOM   4211 N  N     . VAL   D 2 21  ? -49.71400 4.51700  -2.39700  1.000 16.57102 ? 20  VAL   C N     1 
ATOM   4212 C  CA    . VAL   D 2 21  ? -48.58900 3.96300  -1.64600  1.000 16.72603 ? 20  VAL   C CA    1 
ATOM   4213 C  C     . VAL   D 2 21  ? -49.09100 3.69100  -0.23500  1.000 17.11876 ? 20  VAL   C C     1 
ATOM   4214 O  O     . VAL   D 2 21  ? -49.71200 4.56600  0.37700   1.000 18.43373 ? 20  VAL   C O     1 
ATOM   4215 C  CB    . VAL   D 2 21  ? -47.40400 4.95000  -1.60000  1.000 17.64323 ? 20  VAL   C CB    1 
ATOM   4216 C  CG1   . VAL   D 2 21  ? -46.22100 4.32100  -0.88000  1.000 17.29504 ? 20  VAL   C CG1   1 
ATOM   4217 C  CG2   . VAL   D 2 21  ? -46.99500 5.38000  -2.99500  1.000 17.82598 ? 20  VAL   C CG2   1 
ATOM   4218 N  N     . SER   D 2 22  ? -48.85100 2.48300  0.27400   1.000 15.85467 ? 21  SER   C N     1 
ATOM   4219 C  CA    . SER   D 2 22  ? -49.17600 2.16900  1.65600   1.000 16.96634 ? 21  SER   C CA    1 
ATOM   4220 C  C     . SER   D 2 22  ? -47.88900 1.92400  2.42700   1.000 15.90545 ? 21  SER   C C     1 
ATOM   4221 O  O     . SER   D 2 22  ? -46.86900 1.52600  1.85800   1.000 16.20811 ? 21  SER   C O     1 
ATOM   4222 C  CB    . SER   D 2 22  ? -50.09000 0.94900  1.78200   1.000 19.72341 ? 21  SER   C CB    1 
ATOM   4223 O  OG    . SER   D 2 22  ? -49.43100 -0.21900 1.34000   1.000 22.20616 ? 21  SER   C OG    1 
ATOM   4224 N  N     . PHE   D 2 23  ? -47.95400 2.13200  3.73500   1.000 15.30898 ? 22  PHE   C N     1 
ATOM   4225 C  CA    . PHE   D 2 23  ? -46.78800 2.05400  4.59900   1.000 15.18513 ? 22  PHE   C CA    1 
ATOM   4226 C  C     . PHE   D 2 23  ? -47.14200 1.26100  5.83800   1.000 15.56240 ? 22  PHE   C C     1 
ATOM   4227 O  O     . PHE   D 2 23  ? -48.21800 1.44600  6.40900   1.000 17.62266 ? 22  PHE   C O     1 
ATOM   4228 C  CB    . PHE   D 2 23  ? -46.35900 3.45000  5.09100   1.000 14.55463 ? 22  PHE   C CB    1 
ATOM   4229 C  CG    . PHE   D 2 23  ? -46.18500 4.46900  4.00100   1.000 14.29758 ? 22  PHE   C CG    1 
ATOM   4230 C  CD1   . PHE   D 2 23  ? -47.24000 5.28200  3.60700   1.000 15.33180 ? 22  PHE   C CD1   1 
ATOM   4231 C  CD2   . PHE   D 2 23  ? -44.95800 4.63900  3.39600   1.000 15.56607 ? 22  PHE   C CD2   1 
ATOM   4232 C  CE1   . PHE   D 2 23  ? -47.07300 6.24300  2.61600   1.000 17.48618 ? 22  PHE   C CE1   1 
ATOM   4233 C  CE2   . PHE   D 2 23  ? -44.78100 5.61700  2.40400   1.000 16.11968 ? 22  PHE   C CE2   1 
ATOM   4234 C  CZ    . PHE   D 2 23  ? -45.85500 6.39900  2.01000   1.000 16.34625 ? 22  PHE   C CZ    1 
ATOM   4235 N  N     . GLU   D 2 24  ? -46.23000 0.38700  6.25700   1.000 14.53860 ? 23  GLU   C N     1 
ATOM   4236 C  CA    . GLU   D 2 24  ? -46.26800 -0.17000 7.60600   1.000 13.38223 ? 23  GLU   C CA    1 
ATOM   4237 C  C     . GLU   D 2 24  ? -45.51500 0.79500  8.52200   1.000 12.96903 ? 23  GLU   C C     1 
ATOM   4238 O  O     . GLU   D 2 24  ? -44.38500 1.18300  8.21300   1.000 15.08687 ? 23  GLU   C O     1 
ATOM   4239 C  CB    . GLU   D 2 24  ? -45.62700 -1.55800 7.64300   1.000 15.57280 ? 23  GLU   C CB    1 
ATOM   4240 C  CG    . GLU   D 2 24  ? -45.57700 -2.14800 9.05400   1.000 16.92618 ? 23  GLU   C CG    1 
ATOM   4241 C  CD    . GLU   D 2 24  ? -44.92700 -3.52000 9.09500   1.000 20.26449 ? 23  GLU   C CD    1 
ATOM   4242 O  OE1   . GLU   D 2 24  ? -44.63000 -4.07000 8.01500   1.000 26.03957 ? 23  GLU   C OE1   1 
ATOM   4243 O  OE2   . GLU   D 2 24  ? -44.72200 -4.05700 10.20600  1.000 22.44235 ? 23  GLU   C OE2   1 
ATOM   4244 N  N     . LEU   D 2 25  ? -46.13000 1.18400  9.63700   1.000 12.96198 ? 24  LEU   C N     1 
ATOM   4245 C  CA    . LEU   D 2 25  ? -45.50600 2.07800  10.61200  1.000 13.61709 ? 24  LEU   C CA    1 
ATOM   4246 C  C     . LEU   D 2 25  ? -45.03200 1.25500  11.80600  1.000 14.81098 ? 24  LEU   C C     1 
ATOM   4247 O  O     . LEU   D 2 25  ? -45.81900 0.50800  12.41000  1.000 15.31228 ? 24  LEU   C O     1 
ATOM   4248 C  CB    . LEU   D 2 25  ? -46.48100 3.15800  11.07200  1.000 13.77648 ? 24  LEU   C CB    1 
ATOM   4249 C  CG    . LEU   D 2 25  ? -47.11000 3.96200  9.93100   1.000 13.30279 ? 24  LEU   C CG    1 
ATOM   4250 C  CD1   . LEU   D 2 25  ? -48.03900 5.03100  10.48700  1.000 15.42248 ? 24  LEU   C CD1   1 
ATOM   4251 C  CD2   . LEU   D 2 25  ? -46.03800 4.57100  9.03200   1.000 13.56704 ? 24  LEU   C CD2   1 
ATOM   4252 N  N     . PHE   D 2 26  ? -43.74600 1.38800  12.14200  1.000 14.76710 ? 25  PHE   C N     1 
ATOM   4253 C  CA    . PHE   D 2 26  ? -43.11000 0.51300  13.12600  1.000 15.21745 ? 25  PHE   C CA    1 
ATOM   4254 C  C     . PHE   D 2 26  ? -43.39500 0.98500  14.55300  1.000 15.33201 ? 25  PHE   C C     1 
ATOM   4255 O  O     . PHE   D 2 26  ? -42.50400 1.37300  15.30400  1.000 16.57229 ? 25  PHE   C O     1 
ATOM   4256 C  CB    . PHE   D 2 26  ? -41.61400 0.41400  12.85200  1.000 15.90597 ? 25  PHE   C CB    1 
ATOM   4257 C  CG    . PHE   D 2 26  ? -41.27700 -0.14400 11.49500  1.000 19.00090 ? 25  PHE   C CG    1 
ATOM   4258 C  CD1   . PHE   D 2 26  ? -41.97700 -1.22200 10.96400  1.000 19.62496 ? 25  PHE   C CD1   1 
ATOM   4259 C  CD2   . PHE   D 2 26  ? -40.24900 0.40200  10.75200  1.000 20.40424 ? 25  PHE   C CD2   1 
ATOM   4260 C  CE1   . PHE   D 2 26  ? -41.64300 -1.74500 9.71900   1.000 21.62822 ? 25  PHE   C CE1   1 
ATOM   4261 C  CE2   . PHE   D 2 26  ? -39.90900 -0.11700 9.52100   1.000 23.01298 ? 25  PHE   C CE2   1 
ATOM   4262 C  CZ    . PHE   D 2 26  ? -40.61100 -1.17900 9.00200   1.000 23.14902 ? 25  PHE   C CZ    1 
ATOM   4263 N  N     . ALA   D 2 27  ? -44.67900 0.95800  14.91600  1.000 15.41820 ? 26  ALA   C N     1 
ATOM   4264 C  CA    . ALA   D 2 27  ? -45.05400 1.31100  16.27200  1.000 15.34843 ? 26  ALA   C CA    1 
ATOM   4265 C  C     . ALA   D 2 27  ? -44.45800 0.35700  17.30200  1.000 15.78537 ? 26  ALA   C C     1 
ATOM   4266 O  O     . ALA   D 2 27  ? -44.29900 0.75000  18.46500  1.000 17.59395 ? 26  ALA   C O     1 
ATOM   4267 C  CB    . ALA   D 2 27  ? -46.57700 1.32800  16.40000  1.000 18.35878 ? 26  ALA   C CB    1 
ATOM   4268 N  N     . ASP   D 2 28  ? -44.13300 -0.88400 16.90000  1.000 15.03738 ? 27  ASP   C N     1 
ATOM   4269 C  CA    . ASP   D 2 28  ? -43.48900 -1.83600 17.79800  1.000 16.49943 ? 27  ASP   C CA    1 
ATOM   4270 C  C     . ASP   D 2 28  ? -42.14600 -1.33400 18.30600  1.000 17.19134 ? 27  ASP   C C     1 
ATOM   4271 O  O     . ASP   D 2 28  ? -41.74900 -1.67300 19.42300  1.000 22.22385 ? 27  ASP   C O     1 
ATOM   4272 C  CB    . ASP   D 2 28  ? -43.36500 -3.22000 17.14800  1.000 16.85293 ? 27  ASP   C CB    1 
ATOM   4273 C  CG    . ASP   D 2 28  ? -42.67100 -3.21100 15.78000  1.000 19.48721 ? 27  ASP   C CG    1 
ATOM   4274 O  OD1   . ASP   D 2 28  ? -42.29400 -2.14800 15.25500  1.000 21.11223 ? 27  ASP   C OD1   1 
ATOM   4275 O  OD2   . ASP   D 2 28  ? -42.50800 -4.31700 15.21500  1.000 22.82636 ? 27  ASP   C OD2   1 
ATOM   4276 N  N     . LYS   D 2 29  ? -41.42700 -0.53800 17.51900  1.000 16.99681 ? 28  LYS   C N     1 
ATOM   4277 C  CA    . LYS   D 2 29  ? -40.12000 -0.05900 17.93900  1.000 16.72493 ? 28  LYS   C CA    1 
ATOM   4278 C  C     . LYS   D 2 29  ? -39.99500 1.44600  18.07300  1.000 14.86400 ? 28  LYS   C C     1 
ATOM   4279 O  O     . LYS   D 2 29  ? -39.10300 1.89600  18.79600  1.000 15.31415 ? 28  LYS   C O     1 
ATOM   4280 C  CB    . LYS   D 2 29  ? -39.00900 -0.60000 17.02400  1.000 23.01680 ? 28  LYS   C CB    1 
ATOM   4281 C  CG    . LYS   D 2 29  ? -38.71700 -2.07900 17.29200  1.000 28.31902 ? 28  LYS   C CG    1 
ATOM   4282 C  CD    . LYS   D 2 29  ? -38.70500 -2.89800 16.03100  1.000 35.38358 ? 28  LYS   C CD    1 
ATOM   4283 C  CE    . LYS   D 2 29  ? -38.77000 -4.37900 16.37500  1.000 38.14236 ? 28  LYS   C CE    1 
ATOM   4284 N  NZ    . LYS   D 2 29  ? -38.45500 -5.21800 15.20500  1.000 40.28895 ? 28  LYS   C NZ    1 
ATOM   4285 N  N     . VAL   D 2 30  ? -40.84200 2.23000  17.41000  1.000 14.29101 ? 29  VAL   C N     1 
ATOM   4286 C  CA    . VAL   D 2 30  ? -40.75700 3.68600  17.41300  1.000 14.35079 ? 29  VAL   C CA    1 
ATOM   4287 C  C     . VAL   D 2 30  ? -42.17000 4.22500  17.63400  1.000 13.36374 ? 29  VAL   C C     1 
ATOM   4288 O  O     . VAL   D 2 30  ? -42.73200 4.87800  16.74300  1.000 14.36994 ? 29  VAL   C O     1 
ATOM   4289 C  CB    . VAL   D 2 30  ? -40.15200 4.18800  16.08700  1.000 18.40796 ? 29  VAL   C CB    1 
ATOM   4290 C  CG1   . VAL   D 2 30  ? -39.32700 5.42000  16.32500  1.000 23.51552 ? 29  VAL   C CG1   1 
ATOM   4291 C  CG2   . VAL   D 2 30  ? -39.30900 3.09500  15.40600  1.000 23.77875 ? 29  VAL   C CG2   1 
ATOM   4292 N  N     . PRO   D 2 31  ? -42.79700 3.95600  18.78600  1.000 14.71074 ? 30  PRO   C N     1 
ATOM   4293 C  CA    . PRO   D 2 31  ? -44.24100 4.22400  18.90900  1.000 13.64465 ? 30  PRO   C CA    1 
ATOM   4294 C  C     . PRO   D 2 31  ? -44.60700 5.69300  18.80600  1.000 13.75479 ? 30  PRO   C C     1 
ATOM   4295 O  O     . PRO   D 2 31  ? -45.63500 6.01500  18.21000  1.000 15.71531 ? 30  PRO   C O     1 
ATOM   4296 C  CB    . PRO   D 2 31  ? -44.60100 3.62900  20.28400  1.000 15.61522 ? 30  PRO   C CB    1 
ATOM   4297 C  CG    . PRO   D 2 31  ? -43.27700 3.58200  21.03100  1.000 16.49009 ? 30  PRO   C CG    1 
ATOM   4298 C  CD    . PRO   D 2 31  ? -42.26100 3.25900  19.97200  1.000 16.15290 ? 30  PRO   C CD    1 
ATOM   4299 N  N     . LYS   D 2 32  ? -43.81200 6.60100  19.37200  1.000 13.69420 ? 31  LYS   C N     1 
ATOM   4300 C  CA    . LYS   D 2 32  ? -44.18000 8.01400  19.34400  1.000 14.42536 ? 31  LYS   C CA    1 
ATOM   4301 C  C     . LYS   D 2 32  ? -44.08200 8.57100  17.93200  1.000 14.39704 ? 31  LYS   C C     1 
ATOM   4302 O  O     . LYS   D 2 32  ? -44.95600 9.33600  17.48900  1.000 13.72207 ? 31  LYS   C O     1 
ATOM   4303 C  CB    . LYS   D 2 32  ? -43.29000 8.81600  20.29200  1.000 15.50264 ? 31  LYS   C CB    1 
ATOM   4304 C  CG    . LYS   D 2 32  ? -43.36100 8.41100  21.74800  1.000 22.37782 ? 31  LYS   C CG    1 
ATOM   4305 C  CD    . LYS   D 2 32  ? -42.35100 9.20300  22.57300  1.000 26.99124 ? 31  LYS   C CD    1 
ATOM   4306 C  CE    . LYS   D 2 32  ? -42.36200 8.77700  24.02800  1.000 31.15591 ? 31  LYS   C CE    1 
ATOM   4307 N  NZ    . LYS   D 2 32  ? -41.26100 9.44600  24.78000  1.000 33.46148 ? 31  LYS   C NZ    1 
ATOM   4308 N  N     . THR   D 2 33  ? -43.02200 8.19300  17.21200  1.000 13.16182 ? 32  THR   C N     1 
ATOM   4309 C  CA    . THR   D 2 33  ? -42.82500 8.66200  15.84900  1.000 12.93837 ? 32  THR   C CA    1 
ATOM   4310 C  C     . THR   D 2 33  ? -43.85000 8.03900  14.91000  1.000 13.05339 ? 32  THR   C C     1 
ATOM   4311 O  O     . THR   D 2 33  ? -44.42700 8.73400  14.06500  1.000 13.00879 ? 32  THR   C O     1 
ATOM   4312 C  CB    . THR   D 2 33  ? -41.39100 8.33300  15.41900  1.000 12.04356 ? 32  THR   C CB    1 
ATOM   4313 O  OG1   . THR   D 2 33  ? -40.49300 8.85800  16.40200  1.000 13.40050 ? 32  THR   C OG1   1 
ATOM   4314 C  CG2   . THR   D 2 33  ? -41.07100 8.93700  14.07800  1.000 14.32736 ? 32  THR   C CG2   1 
ATOM   4315 N  N     . ALA   D 2 34  ? -44.13800 6.74400  15.07700  1.000 13.59866 ? 33  ALA   C N     1 
ATOM   4316 C  CA    . ALA   D 2 34  ? -45.17300 6.10900  14.26000  1.000 13.71691 ? 33  ALA   C CA    1 
ATOM   4317 C  C     . ALA   D 2 34  ? -46.53000 6.75300  14.50400  1.000 13.34905 ? 33  ALA   C C     1 
ATOM   4318 O  O     . ALA   D 2 34  ? -47.29800 6.98500  13.55600  1.000 14.55928 ? 33  ALA   C O     1 
ATOM   4319 C  CB    . ALA   D 2 34  ? -45.24400 4.61100  14.57300  1.000 14.08144 ? 33  ALA   C CB    1 
ATOM   4320 N  N     . GLU   D 2 35  ? -46.85600 7.02600  15.77700  1.000 13.58229 ? 34  GLU   C N     1 
ATOM   4321 C  CA    . GLU   D 2 35  ? -48.15600 7.60600  16.09400  1.000 14.66617 ? 34  GLU   C CA    1 
ATOM   4322 C  C     . GLU   D 2 35  ? -48.32800 8.98500  15.47300  1.000 14.47442 ? 34  GLU   C C     1 
ATOM   4323 O  O     . GLU   D 2 35  ? -49.41200 9.30100  14.97100  1.000 16.00141 ? 34  GLU   C O     1 
ATOM   4324 C  CB    . GLU   D 2 35  ? -48.36600 7.64600  17.60700  1.000 16.41275 ? 34  GLU   C CB    1 
ATOM   4325 C  CG    . GLU   D 2 35  ? -49.60300 8.41600  18.05000  1.000 17.80732 ? 34  GLU   C CG    1 
ATOM   4326 C  CD    . GLU   D 2 35  ? -50.91800 7.83000  17.54100  1.000 18.49317 ? 34  GLU   C CD    1 
ATOM   4327 O  OE1   . GLU   D 2 35  ? -50.94200 6.67200  17.06800  1.000 18.39219 ? 34  GLU   C OE1   1 
ATOM   4328 O  OE2   . GLU   D 2 35  ? -51.94200 8.53400  17.64000  1.000 21.26549 ? 34  GLU   C OE2   1 
ATOM   4329 N  N     . ASN   D 2 36  ? -47.28000 9.82100  15.49800  1.000 14.58403 ? 35  ASN   C N     1 
ATOM   4330 C  CA    . ASN   D 2 36  ? -47.35600 11.11900 14.83300  1.000 12.89060 ? 35  ASN   C CA    1 
ATOM   4331 C  C     . ASN   D 2 36  ? -47.72000 10.95600 13.35800  1.000 13.88220 ? 35  ASN   C C     1 
ATOM   4332 O  O     . ASN   D 2 36  ? -48.65500 11.59700 12.85600  1.000 13.72170 ? 35  ASN   C O     1 
ATOM   4333 C  CB    . ASN   D 2 36  ? -46.01900 11.84600 14.99500  1.000 14.07871 ? 35  ASN   C CB    1 
ATOM   4334 C  CG    . ASN   D 2 36  ? -45.98600 13.18800 14.28800  1.000 13.36798 ? 35  ASN   C CG    1 
ATOM   4335 O  OD1   . ASN   D 2 36  ? -46.78000 14.07900 14.60000  1.000 15.32996 ? 35  ASN   C OD1   1 
ATOM   4336 N  ND2   . ASN   D 2 36  ? -45.05200 13.34900 13.34200  1.000 14.15657 ? 35  ASN   C ND2   1 
ATOM   4337 N  N     . PHE   D 2 37  ? -47.00400 10.08100 12.64800  1.000 13.40880 ? 36  PHE   C N     1 
ATOM   4338 C  CA    . PHE   D 2 37  ? -47.27100 9.91800  11.22300  1.000 13.20879 ? 36  PHE   C CA    1 
ATOM   4339 C  C     . PHE   D 2 37  ? -48.67500 9.36800  10.99300  1.000 12.89282 ? 36  PHE   C C     1 
ATOM   4340 O  O     . PHE   D 2 37  ? -49.38500 9.81800  10.08600  1.000 14.09174 ? 36  PHE   C O     1 
ATOM   4341 C  CB    . PHE   D 2 37  ? -46.19200 9.03100  10.60200  1.000 13.66188 ? 36  PHE   C CB    1 
ATOM   4342 C  CG    . PHE   D 2 37  ? -46.16800 9.02500  9.09500   1.000 12.74338 ? 36  PHE   C CG    1 
ATOM   4343 C  CD1   . PHE   D 2 37  ? -45.38300 9.92300  8.39200   1.000 13.22548 ? 36  PHE   C CD1   1 
ATOM   4344 C  CD2   . PHE   D 2 37  ? -46.90200 8.09200  8.37700   1.000 13.84698 ? 36  PHE   C CD2   1 
ATOM   4345 C  CE1   . PHE   D 2 37  ? -45.32700 9.87700  7.00000   1.000 14.76130 ? 36  PHE   C CE1   1 
ATOM   4346 C  CE2   . PHE   D 2 37  ? -46.84200 8.04900  6.99000   1.000 15.55883 ? 36  PHE   C CE2   1 
ATOM   4347 C  CZ    . PHE   D 2 37  ? -46.06600 8.94000  6.30300   1.000 14.75645 ? 36  PHE   C CZ    1 
ATOM   4348 N  N     . ARG   D 2 38  ? -49.09900 8.40800  11.82300  1.000 13.65719 ? 37  ARG   C N     1 
ATOM   4349 C  CA    . ARG   D 2 38  ? -50.43600 7.83900  11.68900  1.000 13.43614 ? 37  ARG   C CA    1 
ATOM   4350 C  C     . ARG   D 2 38  ? -51.50200 8.92100  11.83600  1.000 13.42365 ? 37  ARG   C C     1 
ATOM   4351 O  O     . ARG   D 2 38  ? -52.42700 9.02300  11.01500  1.000 14.92188 ? 37  ARG   C O     1 
ATOM   4352 C  CB    . ARG   D 2 38  ? -50.63500 6.71700  12.71900  1.000 15.04679 ? 37  ARG   C CB    1 
ATOM   4353 C  CG    . ARG   D 2 38  ? -51.94400 5.94600  12.53200  1.000 16.67507 ? 37  ARG   C CG    1 
ATOM   4354 C  CD    . ARG   D 2 38  ? -52.39500 5.23100  13.80200  1.000 18.49730 ? 37  ARG   C CD    1 
ATOM   4355 N  NE    . ARG   D 2 38  ? -52.73200 6.17900  14.85900  1.000 17.74240 ? 37  ARG   C NE    1 
ATOM   4356 C  CZ    . ARG   D 2 38  ? -53.81900 6.94100  14.87200  1.000 17.89391 ? 37  ARG   C CZ    1 
ATOM   4357 N  NH1   . ARG   D 2 38  ? -54.78900 6.78300  13.98000  1.000 18.77654 ? 37  ARG   C NH1   1 
ATOM   4358 N  NH2   . ARG   D 2 38  ? -53.93600 7.88600  15.80200  1.000 19.37243 ? 37  ARG   C NH2   1 
ATOM   4359 N  N     . ALA   D 2 39  ? -51.39300 9.74900  12.87900  1.000 13.63680 ? 38  ALA   C N     1 
ATOM   4360 C  CA    . ALA   D 2 39  ? -52.41600 10.76000 13.12700  1.000 14.86881 ? 38  ALA   C CA    1 
ATOM   4361 C  C     . ALA   D 2 39  ? -52.39100 11.85300 12.06300  1.000 14.26212 ? 38  ALA   C C     1 
ATOM   4362 O  O     . ALA   D 2 39  ? -53.44500 12.38500 11.68500  1.000 16.22434 ? 38  ALA   C O     1 
ATOM   4363 C  CB    . ALA   D 2 39  ? -52.24300 11.35400 14.52500  1.000 14.83196 ? 38  ALA   C CB    1 
ATOM   4364 N  N     . LEU   D 2 40  ? -51.20200 12.20100 11.56400  1.000 13.63825 ? 39  LEU   C N     1 
ATOM   4365 C  CA    . LEU   D 2 40  ? -51.13300 13.17500 10.48400  1.000 13.68822 ? 39  LEU   C CA    1 
ATOM   4366 C  C     . LEU   D 2 40  ? -51.75400 12.62300 9.20900   1.000 13.88437 ? 39  LEU   C C     1 
ATOM   4367 O  O     . LEU   D 2 40  ? -52.28300 13.39200 8.38600   1.000 14.70226 ? 39  LEU   C O     1 
ATOM   4368 C  CB    . LEU   D 2 40  ? -49.67800 13.58800 10.26700  1.000 14.04303 ? 39  LEU   C CB    1 
ATOM   4369 C  CG    . LEU   D 2 40  ? -49.07800 14.41900 11.41000  1.000 14.55324 ? 39  LEU   C CG    1 
ATOM   4370 C  CD1   . LEU   D 2 40  ? -47.59000 14.68300 11.11800  1.000 15.68103 ? 39  LEU   C CD1   1 
ATOM   4371 C  CD2   . LEU   D 2 40  ? -49.81800 15.73800 11.66000  1.000 16.44596 ? 39  LEU   C CD2   1 
ATOM   4372 N  N     . SER   D 2 41  ? -51.71000 11.29500 9.03300   1.000 13.96637 ? 40  SER   C N     1 
ATOM   4373 C  CA    . SER   D 2 41  ? -52.28900 10.67200 7.84400   1.000 14.77273 ? 40  SER   C CA    1 
ATOM   4374 C  C     . SER   D 2 41  ? -53.80700 10.60300 7.91400   1.000 17.01492 ? 40  SER   C C     1 
ATOM   4375 O  O     . SER   D 2 41  ? -54.47300 10.72200 6.88100   1.000 16.93061 ? 40  SER   C O     1 
ATOM   4376 C  CB    . SER   D 2 41  ? -51.69300 9.27900  7.62400   1.000 15.69144 ? 40  SER   C CB    1 
ATOM   4377 O  OG    . SER   D 2 41  ? -50.29400 9.35500  7.36800   1.000 15.91148 ? 40  SER   C OG    1 
ATOM   4378 N  N     . THR   D 2 42  ? -54.36700 10.42000 9.10700   1.000 15.93232 ? 41  THR   C N     1 
ATOM   4379 C  CA    . THR   D 2 42  ? -55.82100 10.41300 9.22300   1.000 17.40168 ? 41  THR   C CA    1 
ATOM   4380 C  C     . THR   D 2 42  ? -56.40700 11.81700 9.32700   1.000 18.52956 ? 41  THR   C C     1 
ATOM   4381 O  O     . THR   D 2 42  ? -57.60000 11.99600 9.06300   1.000 20.30545 ? 41  THR   C O     1 
ATOM   4382 C  CB    . THR   D 2 42  ? -56.28000 9.62500  10.45400  1.000 18.36401 ? 41  THR   C CB    1 
ATOM   4383 O  OG1   . THR   D 2 42  ? -55.85700 10.32000 11.63200  1.000 18.45846 ? 41  THR   C OG1   1 
ATOM   4384 C  CG2   . THR   D 2 42  ? -55.74000 8.19700  10.44700  1.000 19.10721 ? 41  THR   C CG2   1 
ATOM   4385 N  N     . GLY   D 2 43  ? -55.60800 12.80200 9.72700   1.000 18.45179 ? 42  GLY   C N     1 
ATOM   4386 C  CA    . GLY   D 2 43  ? -56.10100 14.14400 9.94200   1.000 18.23421 ? 42  GLY   C CA    1 
ATOM   4387 C  C     . GLY   D 2 43  ? -56.88200 14.32700 11.21900  1.000 17.84198 ? 42  GLY   C C     1 
ATOM   4388 O  O     . GLY   D 2 43  ? -57.48900 15.38600 11.40300  1.000 19.38290 ? 42  GLY   C O     1 
ATOM   4389 N  N     . GLU   D 2 44  ? -56.85800 13.34000 12.12200  1.000 17.70429 ? 43  GLU   C N     1 
ATOM   4390 C  CA    . GLU   D 2 44  ? -57.78600 13.31200 13.24100  1.000 19.57357 ? 43  GLU   C CA    1 
ATOM   4391 C  C     . GLU   D 2 44  ? -57.54200 14.42000 14.25700  1.000 21.18982 ? 43  GLU   C C     1 
ATOM   4392 O  O     . GLU   D 2 44  ? -58.42700 14.67900 15.07400  1.000 23.29703 ? 43  GLU   C O     1 
ATOM   4393 C  CB    . GLU   D 2 44  ? -57.73800 11.94400 13.92400  1.000 20.05987 ? 43  GLU   C CB    1 
ATOM   4394 C  CG    . GLU   D 2 44  ? -56.39500 11.59200 14.53400  1.000 21.81022 ? 43  GLU   C CG    1 
ATOM   4395 C  CD    . GLU   D 2 44  ? -56.33300 10.11800 14.92600  1.000 23.11251 ? 43  GLU   C CD    1 
ATOM   4396 O  OE1   . GLU   D 2 44  ? -56.41400 9.25100  14.02500  1.000 22.64483 ? 43  GLU   C OE1   1 
ATOM   4397 O  OE2   . GLU   D 2 44  ? -56.22900 9.82500  16.14300  1.000 24.90904 ? 43  GLU   C OE2   1 
ATOM   4398 N  N     . LYS   D 2 45  ? -56.38300 15.07700 14.23700  1.000 20.58681 ? 44  LYS   C N     1 
ATOM   4399 C  CA    . LYS   D 2 45  ? -56.15500 16.21600 15.11700  1.000 21.49555 ? 44  LYS   C CA    1 
ATOM   4400 C  C     . LYS   D 2 45  ? -56.62600 17.53300 14.52300  1.000 22.00384 ? 44  LYS   C C     1 
ATOM   4401 O  O     . LYS   D 2 45  ? -56.53400 18.56100 15.19700  1.000 26.59242 ? 44  LYS   C O     1 
ATOM   4402 C  CB    . LYS   D 2 45  ? -54.67000 16.34900 15.48400  1.000 21.96060 ? 44  LYS   C CB    1 
ATOM   4403 C  CG    . LYS   D 2 45  ? -54.00800 15.07900 16.02200  1.000 22.44104 ? 44  LYS   C CG    1 
ATOM   4404 C  CD    . LYS   D 2 45  ? -54.60800 14.65200 17.34500  1.000 24.81027 ? 44  LYS   C CD    1 
ATOM   4405 C  CE    . LYS   D 2 45  ? -53.83800 13.47600 17.92900  1.000 27.65303 ? 44  LYS   C CE    1 
ATOM   4406 N  NZ    . LYS   D 2 45  ? -54.36300 13.02200 19.24700  1.000 29.81126 ? 44  LYS   C NZ    1 
ATOM   4407 N  N     . GLY   D 2 46  ? -57.10500 17.53500 13.28300  1.000 22.01967 ? 45  GLY   C N     1 
ATOM   4408 C  CA    . GLY   D 2 46  ? -57.54000 18.75000 12.62300  1.000 21.26620 ? 45  GLY   C CA    1 
ATOM   4409 C  C     . GLY   D 2 46  ? -56.56600 19.30100 11.60800  1.000 21.63959 ? 45  GLY   C C     1 
ATOM   4410 O  O     . GLY   D 2 46  ? -56.83800 20.35000 11.01600  1.000 22.84448 ? 45  GLY   C O     1 
ATOM   4411 N  N     . PHE   D 2 47  ? -55.43400 18.63100 11.40300  1.000 20.76668 ? 46  PHE   C N     1 
ATOM   4412 C  CA    . PHE   D 2 47  ? -54.41900 19.04200 10.44500  1.000 19.30802 ? 46  PHE   C CA    1 
ATOM   4413 C  C     . PHE   D 2 47  ? -53.68100 17.78200 10.02200  1.000 17.45855 ? 46  PHE   C C     1 
ATOM   4414 O  O     . PHE   D 2 47  ? -53.80600 16.73400 10.66000  1.000 17.45555 ? 46  PHE   C O     1 
ATOM   4415 C  CB    . PHE   D 2 47  ? -53.47100 20.08200 11.05300  1.000 18.01255 ? 46  PHE   C CB    1 
ATOM   4416 C  CG    . PHE   D 2 47  ? -52.90000 19.68100 12.40100  1.000 18.00955 ? 46  PHE   C CG    1 
ATOM   4417 C  CD1   . PHE   D 2 47  ? -51.78100 18.85400 12.48500  1.000 20.19160 ? 46  PHE   C CD1   1 
ATOM   4418 C  CD2   . PHE   D 2 47  ? -53.47900 20.12900 13.58200  1.000 20.58441 ? 46  PHE   C CD2   1 
ATOM   4419 C  CE1   . PHE   D 2 47  ? -51.25500 18.49300 13.73100  1.000 20.69830 ? 46  PHE   C CE1   1 
ATOM   4420 C  CE2   . PHE   D 2 47  ? -52.95200 19.76800 14.82300  1.000 21.14081 ? 46  PHE   C CE2   1 
ATOM   4421 C  CZ    . PHE   D 2 47  ? -51.85400 18.94500 14.89800  1.000 21.59562 ? 46  PHE   C CZ    1 
ATOM   4422 N  N     . GLY   D 2 48  ? -52.90400 17.87700 8.94700   1.000 15.52698 ? 47  GLY   C N     1 
ATOM   4423 C  CA    . GLY   D 2 48  ? -52.15000 16.70700 8.53300   1.000 15.15193 ? 47  GLY   C CA    1 
ATOM   4424 C  C     . GLY   D 2 48  ? -51.73500 16.78700 7.07400   1.000 14.74827 ? 47  GLY   C C     1 
ATOM   4425 O  O     . GLY   D 2 48  ? -51.74600 17.85900 6.46500   1.000 15.85760 ? 47  GLY   C O     1 
ATOM   4426 N  N     . TYR   D 2 49  ? -51.39600 15.61100 6.53500   1.000 15.12900 ? 48  TYR   C N     1 
ATOM   4427 C  CA    . TYR   D 2 49  ? -50.73500 15.49900 5.24200   1.000 14.04648 ? 48  TYR   C CA    1 
ATOM   4428 C  C     . TYR   D 2 49  ? -51.65300 15.73300 4.03900   1.000 14.73686 ? 48  TYR   C C     1 
ATOM   4429 O  O     . TYR   D 2 49  ? -51.14300 16.04400 2.95600   1.000 14.63167 ? 48  TYR   C O     1 
ATOM   4430 C  CB    . TYR   D 2 49  ? -50.11700 14.11200 5.12000   1.000 14.38815 ? 48  TYR   C CB    1 
ATOM   4431 C  CG    . TYR   D 2 49  ? -48.94000 13.87700 6.04000   1.000 13.42935 ? 48  TYR   C CG    1 
ATOM   4432 C  CD1   . TYR   D 2 49  ? -47.91300 14.81200 6.15300   1.000 13.81304 ? 48  TYR   C CD1   1 
ATOM   4433 C  CD2   . TYR   D 2 49  ? -48.82700 12.70300 6.76700   1.000 13.41958 ? 48  TYR   C CD2   1 
ATOM   4434 C  CE1   . TYR   D 2 49  ? -46.81700 14.58100 6.98800   1.000 13.54834 ? 48  TYR   C CE1   1 
ATOM   4435 C  CE2   . TYR   D 2 49  ? -47.73900 12.46500 7.59300   1.000 12.94624 ? 48  TYR   C CE2   1 
ATOM   4436 C  CZ    . TYR   D 2 49  ? -46.73500 13.40600 7.69200   1.000 12.86205 ? 48  TYR   C CZ    1 
ATOM   4437 O  OH    . TYR   D 2 49  ? -45.66400 13.16200 8.52600   1.000 13.28063 ? 48  TYR   C OH    1 
ATOM   4438 N  N     . LYS   D 2 50  ? -52.97400 15.56300 4.16700   1.000 13.87860 ? 49  LYS   C N     1 
ATOM   4439 C  CA    . LYS   D 2 50  ? -53.80200 15.59900 2.96900   1.000 15.04059 ? 49  LYS   C CA    1 
ATOM   4440 C  C     . LYS   D 2 50  ? -53.69900 16.95800 2.28300   1.000 14.37119 ? 49  LYS   C C     1 
ATOM   4441 O  O     . LYS   D 2 50  ? -53.95600 18.00300 2.89900   1.000 16.50507 ? 49  LYS   C O     1 
ATOM   4442 C  CB    . LYS   D 2 50  ? -55.26300 15.32700 3.32600   1.000 17.43961 ? 49  LYS   C CB    1 
ATOM   4443 C  CG    . LYS   D 2 50  ? -56.15600 15.23400 2.11000   1.000 20.41363 ? 49  LYS   C CG    1 
ATOM   4444 C  CD    . LYS   D 2 50  ? -57.61700 15.23000 2.52900   1.000 26.32693 ? 49  LYS   C CD    1 
ATOM   4445 C  CE    . LYS   D 2 50  ? -58.30200 13.95500 2.14500   1.000 33.72648 ? 49  LYS   C CE    1 
ATOM   4446 N  NZ    . LYS   D 2 50  ? -59.37600 13.54000 3.11600   1.000 33.79501 ? 49  LYS   C NZ    1 
ATOM   4447 N  N     . GLY   D 2 51  ? -53.33700 16.93200 0.99400   1.000 14.83406 ? 50  GLY   C N     1 
ATOM   4448 C  CA    . GLY   D 2 51  ? -53.16700 18.12700 0.18900   1.000 16.12956 ? 50  GLY   C CA    1 
ATOM   4449 C  C     . GLY   D 2 51  ? -51.72800 18.60500 0.07200   1.000 14.94774 ? 50  GLY   C C     1 
ATOM   4450 O  O     . GLY   D 2 51  ? -51.43300 19.42100 -0.80500  1.000 17.06407 ? 50  GLY   C O     1 
ATOM   4451 N  N     . SER   D 2 52  ? -50.83400 18.13600 0.94700   1.000 14.03685 ? 51  SER   C N     1 
ATOM   4452 C  CA    . SER   D 2 52  ? -49.46400 18.63500 0.96300   1.000 14.56423 ? 51  SER   C CA    1 
ATOM   4453 C  C     . SER   D 2 52  ? -48.66500 18.02100 -0.18900  1.000 15.11801 ? 51  SER   C C     1 
ATOM   4454 O  O     . SER   D 2 52  ? -49.09900 17.07900 -0.85000  1.000 15.86991 ? 51  SER   C O     1 
ATOM   4455 C  CB    . SER   D 2 52  ? -48.80900 18.37500 2.32700   1.000 15.04135 ? 51  SER   C CB    1 
ATOM   4456 O  OG    . SER   D 2 52  ? -48.63800 16.98800 2.59200   1.000 15.59273 ? 51  SER   C OG    1 
ATOM   4457 N  N     A CYS   D 2 53  ? -47.44800 18.53500 -0.37200  0.500 13.02279 ? 52  CYS   C N     1 
ATOM   4458 N  N     B CYS   D 2 53  ? -47.49200 18.57600 -0.46000  0.500 16.16240 ? 52  CYS   C N     1 
ATOM   4459 C  CA    A CYS   D 2 53  ? -46.62500 18.31200 -1.55300  0.500 12.33134 ? 52  CYS   C CA    1 
ATOM   4460 C  CA    B CYS   D 2 53  ? -46.75400 18.14200 -1.63500  0.500 18.45334 ? 52  CYS   C CA    1 
ATOM   4461 C  C     A CYS   D 2 53  ? -45.37700 17.49600 -1.21500  0.500 12.79144 ? 52  CYS   C C     1 
ATOM   4462 C  C     B CYS   D 2 53  ? -45.41200 17.52400 -1.27000  0.500 16.89026 ? 52  CYS   C C     1 
ATOM   4463 O  O     A CYS   D 2 53  ? -44.81100 17.61200 -0.12600  0.500 13.79217 ? 52  CYS   C O     1 
ATOM   4464 O  O     B CYS   D 2 53  ? -44.82200 17.81800 -0.22600  0.500 18.40753 ? 52  CYS   C O     1 
ATOM   4465 C  CB    A CYS   D 2 53  ? -46.21900 19.68700 -2.11400  0.500 12.49705 ? 52  CYS   C CB    1 
ATOM   4466 C  CB    B CYS   D 2 53  ? -46.54000 19.28500 -2.62400  0.500 21.96762 ? 52  CYS   C CB    1 
ATOM   4467 S  SG    A CYS   D 2 53  ? -45.17600 19.69500 -3.58600  0.500 12.79013 ? 52  CYS   C SG    1 
ATOM   4468 S  SG    B CYS   D 2 53  ? -45.14400 20.31500 -2.21900  0.500 24.65373 ? 52  CYS   C SG    1 
ATOM   4469 N  N     . PHE   D 2 54  ? -44.94600 16.66000 -2.16100  1.000 13.91406 ? 53  PHE   C N     1 
ATOM   4470 C  CA    . PHE   D 2 54  ? -43.57900 16.13300 -2.15200  1.000 14.45340 ? 53  PHE   C CA    1 
ATOM   4471 C  C     . PHE   D 2 54  ? -42.71800 17.17900 -2.84200  1.000 13.87836 ? 53  PHE   C C     1 
ATOM   4472 O  O     . PHE   D 2 54  ? -42.60700 17.21800 -4.06500  1.000 15.86835 ? 53  PHE   C O     1 
ATOM   4473 C  CB    . PHE   D 2 54  ? -43.51200 14.79200 -2.87100  1.000 14.68185 ? 53  PHE   C CB    1 
ATOM   4474 C  CG    . PHE   D 2 54  ? -43.91900 13.63000 -2.00600  1.000 14.16129 ? 53  PHE   C CG    1 
ATOM   4475 C  CD1   . PHE   D 2 54  ? -45.25100 13.26400 -1.88700  1.000 15.92383 ? 53  PHE   C CD1   1 
ATOM   4476 C  CD2   . PHE   D 2 54  ? -42.97100 12.92400 -1.29000  1.000 15.06392 ? 53  PHE   C CD2   1 
ATOM   4477 C  CE1   . PHE   D 2 54  ? -45.62900 12.20100 -1.07900  1.000 17.49431 ? 53  PHE   C CE1   1 
ATOM   4478 C  CE2   . PHE   D 2 54  ? -43.34100 11.84200 -0.48700  1.000 15.71891 ? 53  PHE   C CE2   1 
ATOM   4479 C  CZ    . PHE   D 2 54  ? -44.68000 11.48600 -0.38400  1.000 16.03451 ? 53  PHE   C CZ    1 
ATOM   4480 N  N     . HIS   D 2 55  ? -42.13200 18.06900 -2.04600  1.000 14.70816 ? 54  HIS   C N     1 
ATOM   4481 C  CA    . HIS   D 2 55  ? -41.49000 19.24700 -2.59600  1.000 15.40919 ? 54  HIS   C CA    1 
ATOM   4482 C  C     . HIS   D 2 55  ? -40.06300 18.97900 -3.05100  1.000 15.11745 ? 54  HIS   C C     1 
ATOM   4483 O  O     . HIS   D 2 55  ? -39.52700 19.76300 -3.83800  1.000 16.97004 ? 54  HIS   C O     1 
ATOM   4484 C  CB    . HIS   D 2 55  ? -41.49200 20.36900 -1.55800  1.000 15.84420 ? 54  HIS   C CB    1 
ATOM   4485 C  CG    . HIS   D 2 55  ? -40.71100 20.03700 -0.33000  1.000 16.39418 ? 54  HIS   C CG    1 
ATOM   4486 N  ND1   . HIS   D 2 55  ? -41.20300 19.21000 0.65700   1.000 16.60356 ? 54  HIS   C ND1   1 
ATOM   4487 C  CD2   . HIS   D 2 55  ? -39.46600 20.39800 0.06200   1.000 16.70988 ? 54  HIS   C CD2   1 
ATOM   4488 C  CE1   . HIS   D 2 55  ? -40.29800 19.08800 1.61400   1.000 17.08554 ? 54  HIS   C CE1   1 
ATOM   4489 N  NE2   . HIS   D 2 55  ? -39.23000 19.78700 1.27200   1.000 17.56550 ? 54  HIS   C NE2   1 
ATOM   4490 N  N     . ARG   D 2 56  ? -39.44200 17.89600 -2.59200  1.000 14.47495 ? 55  ARG   C N     1 
ATOM   4491 C  CA    . ARG   D 2 56  ? -38.03000 17.63900 -2.86100  1.000 14.57276 ? 55  ARG   C CA    1 
ATOM   4492 C  C     . ARG   D 2 56  ? -37.88400 16.17800 -3.25200  1.000 14.16997 ? 55  ARG   C C     1 
ATOM   4493 O  O     . ARG   D 2 56  ? -38.02800 15.28400 -2.41100  1.000 15.29537 ? 55  ARG   C O     1 
ATOM   4494 C  CB    . ARG   D 2 56  ? -37.15600 17.97400 -1.65500  1.000 14.20920 ? 55  ARG   C CB    1 
ATOM   4495 C  CG    . ARG   D 2 56  ? -35.67200 17.70200 -1.90900  1.000 15.85061 ? 55  ARG   C CG    1 
ATOM   4496 C  CD    . ARG   D 2 56  ? -34.80800 17.90000 -0.67800  1.000 14.58300 ? 55  ARG   C CD    1 
ATOM   4497 N  NE    . ARG   D 2 56  ? -34.75100 19.29500 -0.26800  1.000 16.76790 ? 55  ARG   C NE    1 
ATOM   4498 C  CZ    . ARG   D 2 56  ? -34.04200 19.70300 0.77000   1.000 18.40303 ? 55  ARG   C CZ    1 
ATOM   4499 N  NH1   . ARG   D 2 56  ? -33.36200 18.84200 1.51500   1.000 17.71098 ? 55  ARG   C NH1   1 
ATOM   4500 N  NH2   . ARG   D 2 56  ? -33.97500 21.00200 1.04300   1.000 22.72740 ? 55  ARG   C NH2   1 
ATOM   4501 N  N     . ILE   D 2 57  ? -37.63200 15.93400 -4.53500  1.000 14.63845 ? 56  ILE   C N     1 
ATOM   4502 C  CA    . ILE   D 2 57  ? -37.48700 14.58300 -5.05400  1.000 16.04167 ? 56  ILE   C CA    1 
ATOM   4503 C  C     . ILE   D 2 57  ? -36.16500 14.54200 -5.80300  1.000 16.60052 ? 56  ILE   C C     1 
ATOM   4504 O  O     . ILE   D 2 57  ? -35.98500 15.26200 -6.79600  1.000 16.97147 ? 56  ILE   C O     1 
ATOM   4505 C  CB    . ILE   D 2 57  ? -38.65500 14.19800 -5.97400  1.000 16.57728 ? 56  ILE   C CB    1 
ATOM   4506 C  CG1   . ILE   D 2 57  ? -39.98100 14.21200 -5.19600  1.000 15.24893 ? 56  ILE   C CG1   1 
ATOM   4507 C  CG2   . ILE   D 2 57  ? -38.41800 12.82100 -6.62900  1.000 17.27617 ? 56  ILE   C CG2   1 
ATOM   4508 C  CD1   . ILE   D 2 57  ? -41.17200 13.87000 -6.06000  1.000 16.45288 ? 56  ILE   C CD1   1 
ATOM   4509 N  N     . ILE   D 2 58  ? -35.22700 13.74200 -5.30700  1.000 16.43793 ? 57  ILE   C N     1 
ATOM   4510 C  CA    . ILE   D 2 58  ? -33.90800 13.64200 -5.92400  1.000 17.22065 ? 57  ILE   C CA    1 
ATOM   4511 C  C     . ILE   D 2 58  ? -33.69900 12.20600 -6.38100  1.000 18.31968 ? 57  ILE   C C     1 
ATOM   4512 O  O     . ILE   D 2 58  ? -33.53200 11.30500 -5.54400  1.000 18.71228 ? 57  ILE   C O     1 
ATOM   4513 C  CB    . ILE   D 2 58  ? -32.79500 14.12100 -4.98400  1.000 17.62548 ? 57  ILE   C CB    1 
ATOM   4514 C  CG1   . ILE   D 2 58  ? -33.04400 15.57500 -4.58200  1.000 17.50052 ? 57  ILE   C CG1   1 
ATOM   4515 C  CG2   . ILE   D 2 58  ? -31.44300 13.99100 -5.68600  1.000 17.80710 ? 57  ILE   C CG2   1 
ATOM   4516 C  CD1   . ILE   D 2 58  ? -31.98000 16.14400 -3.66700  1.000 18.34977 ? 57  ILE   C CD1   1 
ATOM   4517 N  N     . PRO   D 2 59  ? -33.70800 11.95300 -7.69000  1.000 20.02375 ? 58  PRO   C N     1 
ATOM   4518 C  CA    . PRO   D 2 59  ? -33.58700 10.57600 -8.18400  1.000 20.58694 ? 58  PRO   C CA    1 
ATOM   4519 C  C     . PRO   D 2 59  ? -32.31400 9.90900  -7.68200  1.000 21.42393 ? 58  PRO   C C     1 
ATOM   4520 O  O     . PRO   D 2 59  ? -31.24300 10.51800 -7.64000  1.000 21.97921 ? 58  PRO   C O     1 
ATOM   4521 C  CB    . PRO   D 2 59  ? -33.58600 10.74800 -9.70800  1.000 21.00920 ? 58  PRO   C CB    1 
ATOM   4522 C  CG    . PRO   D 2 59  ? -34.38300 12.01800 -9.92800  1.000 22.26273 ? 58  PRO   C CG    1 
ATOM   4523 C  CD    . PRO   D 2 59  ? -34.02200 12.91100 -8.76000  1.000 21.75165 ? 58  PRO   C CD    1 
ATOM   4524 N  N     . GLY   D 2 60  ? -32.44400 8.64000  -7.29500  1.000 22.21018 ? 59  GLY   C N     1 
ATOM   4525 C  CA    . GLY   D 2 60  ? -31.35700 7.89600  -6.70400  1.000 22.09069 ? 59  GLY   C CA    1 
ATOM   4526 C  C     . GLY   D 2 60  ? -31.22300 8.06500  -5.20900  1.000 20.65274 ? 59  GLY   C C     1 
ATOM   4527 O  O     . GLY   D 2 60  ? -30.37500 7.40000  -4.59800  1.000 23.72750 ? 59  GLY   C O     1 
ATOM   4528 N  N     . PHE   D 2 61  ? -32.04000 8.91700  -4.59400  1.000 17.82400 ? 60  PHE   C N     1 
ATOM   4529 C  CA    . PHE   D 2 61  ? -31.94100 9.15200  -3.16100  1.000 17.03915 ? 60  PHE   C CA    1 
ATOM   4530 C  C     . PHE   D 2 61  ? -33.28100 9.02400  -2.45200  1.000 16.22900 ? 60  PHE   C C     1 
ATOM   4531 O  O     . PHE   D 2 61  ? -33.48700 8.05400  -1.71100  1.000 16.18225 ? 60  PHE   C O     1 
ATOM   4532 C  CB    . PHE   D 2 61  ? -31.27500 10.49400 -2.88900  1.000 16.92883 ? 60  PHE   C CB    1 
ATOM   4533 C  CG    . PHE   D 2 61  ? -29.83900 10.53100 -3.30800  1.000 19.05147 ? 60  PHE   C CG    1 
ATOM   4534 C  CD1   . PHE   D 2 61  ? -28.84600 10.03500 -2.47300  1.000 19.87401 ? 60  PHE   C CD1   1 
ATOM   4535 C  CD2   . PHE   D 2 61  ? -29.47500 11.04000 -4.54200  1.000 20.87730 ? 60  PHE   C CD2   1 
ATOM   4536 C  CE1   . PHE   D 2 61  ? -27.51900 10.06400 -2.86000  1.000 21.72839 ? 60  PHE   C CE1   1 
ATOM   4537 C  CE2   . PHE   D 2 61  ? -28.14200 11.08200 -4.93100  1.000 22.72227 ? 60  PHE   C CE2   1 
ATOM   4538 C  CZ    . PHE   D 2 61  ? -27.17000 10.59100 -4.08900  1.000 22.40272 ? 60  PHE   C CZ    1 
ATOM   4539 N  N     . MET   D 2 62  ? -34.20000 9.97300  -2.65200  1.000 16.08796 ? 61  MET   C N     1 
ATOM   4540 C  CA    . MET   D 2 62  ? -35.41400 9.92600  -1.84400  1.000 15.80282 ? 61  MET   C CA    1 
ATOM   4541 C  C     . MET   D 2 62  ? -36.47100 10.85100 -2.41900  1.000 15.40985 ? 61  MET   C C     1 
ATOM   4542 O  O     . MET   D 2 62  ? -36.19100 11.70500 -3.26500  1.000 15.45398 ? 61  MET   C O     1 
ATOM   4543 C  CB    . MET   D 2 62  ? -35.13300 10.33600 -0.39200  1.000 16.31820 ? 61  MET   C CB    1 
ATOM   4544 C  CG    . MET   D 2 62  ? -35.11000 11.86100 -0.12100  1.000 16.42186 ? 61  MET   C CG    1 
ATOM   4545 S  SD    . MET   D 2 62  ? -33.76900 12.78500 -0.93600  1.000 17.06206 ? 61  MET   C SD    1 
ATOM   4546 C  CE    . MET   D 2 62  ? -34.56800 14.39500 -1.02500  1.000 16.76300 ? 61  MET   C CE    1 
ATOM   4547 N  N     . CYS   D 2 63  ? -37.69600 10.66800 -1.91800  1.000 13.86787 ? 62  CYS   C N     1 
ATOM   4548 C  CA    . CYS   D 2 63  ? -38.81400 11.58000 -2.11800  1.000 14.33367 ? 62  CYS   C CA    1 
ATOM   4549 C  C     . CYS   D 2 63  ? -39.19000 12.14500 -0.75100  1.000 13.80769 ? 62  CYS   C C     1 
ATOM   4550 O  O     . CYS   D 2 63  ? -39.54400 11.38300 0.16000   1.000 14.47310 ? 62  CYS   C O     1 
ATOM   4551 C  CB    . CYS   D 2 63  ? -40.02400 10.82600 -2.67900  1.000 15.93457 ? 62  CYS   C CB    1 
ATOM   4552 S  SG    . CYS   D 2 63  ? -39.79900 10.01100 -4.27500  1.000 17.64640 ? 62  CYS   C SG    1 
ATOM   4553 N  N     . GLN   D 2 64  ? -39.14600 13.47200 -0.61500  1.000 12.72996 ? 63  GLN   C N     1 
ATOM   4554 C  CA    . GLN   D 2 64  ? -39.37000 14.14200 0.66100   1.000 12.35499 ? 63  GLN   C CA    1 
ATOM   4555 C  C     . GLN   D 2 64  ? -40.60500 15.02600 0.59600   1.000 13.33385 ? 63  GLN   C C     1 
ATOM   4556 O  O     . GLN   D 2 64  ? -40.83600 15.71800 -0.39600  1.000 13.29299 ? 63  GLN   C O     1 
ATOM   4557 C  CB    . GLN   D 2 64  ? -38.13600 14.95900 1.06500   1.000 13.75842 ? 63  GLN   C CB    1 
ATOM   4558 C  CG    . GLN   D 2 64  ? -38.27800 15.76200 2.35700   1.000 12.80378 ? 63  GLN   C CG    1 
ATOM   4559 C  CD    . GLN   D 2 64  ? -37.00400 16.47900 2.71000   1.000 14.03282 ? 63  GLN   C CD    1 
ATOM   4560 O  OE1   . GLN   D 2 64  ? -35.93300 16.08300 2.27600   1.000 14.76100 ? 63  GLN   C OE1   1 
ATOM   4561 N  NE2   . GLN   D 2 64  ? -37.10900 17.53200 3.50600   1.000 13.30863 ? 63  GLN   C NE2   1 
ATOM   4562 N  N     . GLY   D 2 65  ? -41.39900 14.99500 1.66300   1.000 12.92868 ? 64  GLY   C N     1 
ATOM   4563 C  CA    . GLY   D 2 65  ? -42.60100 15.80700 1.71600   1.000 12.71711 ? 64  GLY   C CA    1 
ATOM   4564 C  C     . GLY   D 2 65  ? -43.00800 16.09800 3.14200   1.000 12.66895 ? 64  GLY   C C     1 
ATOM   4565 O  O     . GLY   D 2 65  ? -42.20000 15.96500 4.06600   1.000 13.62793 ? 64  GLY   C O     1 
ATOM   4566 N  N     . GLY   D 2 66  ? -44.24600 16.55300 3.31300   1.000 13.88828 ? 65  GLY   C N     1 
ATOM   4567 C  CA    . GLY   D 2 66  ? -44.83500 16.71400 4.63500   1.000 14.64437 ? 65  GLY   C CA    1 
ATOM   4568 C  C     . GLY   D 2 66  ? -44.96200 18.12100 5.19100   1.000 13.71707 ? 65  GLY   C C     1 
ATOM   4569 O  O     . GLY   D 2 66  ? -45.35200 18.26700 6.35500   1.000 15.23869 ? 65  GLY   C O     1 
ATOM   4570 N  N     . ASP   D 2 67  ? -44.67100 19.16500 4.41200   1.000 14.19272 ? 66  ASP   C N     1 
ATOM   4571 C  CA    . ASP   D 2 67  ? -44.80900 20.53400 4.91600   1.000 14.63180 ? 66  ASP   C CA    1 
ATOM   4572 C  C     . ASP   D 2 67  ? -46.21900 21.03300 4.62500   1.000 14.74631 ? 66  ASP   C C     1 
ATOM   4573 O  O     . ASP   D 2 67  ? -46.50000 21.57600 3.55200   1.000 17.49169 ? 66  ASP   C O     1 
ATOM   4574 C  CB    . ASP   D 2 67  ? -43.74900 21.45400 4.32300   1.000 15.21469 ? 66  ASP   C CB    1 
ATOM   4575 C  CG    . ASP   D 2 67  ? -43.92400 22.90200 4.76600   1.000 16.61584 ? 66  ASP   C CG    1 
ATOM   4576 O  OD1   . ASP   D 2 67  ? -44.82200 23.20400 5.58900   1.000 17.27579 ? 66  ASP   C OD1   1 
ATOM   4577 O  OD2   . ASP   D 2 67  ? -43.15100 23.74900 4.29400   1.000 17.43042 ? 66  ASP   C OD2   1 
ATOM   4578 N  N     . PHE   D 2 68  ? -47.10200 20.88800 5.60500   1.000 15.06731 ? 67  PHE   C N     1 
ATOM   4579 C  CA    . PHE   D 2 68  ? -48.48000 21.34300 5.47700   1.000 15.16065 ? 67  PHE   C CA    1 
ATOM   4580 C  C     . PHE   D 2 68  ? -48.74000 22.66900 6.18600   1.000 15.62884 ? 67  PHE   C C     1 
ATOM   4581 O  O     . PHE   D 2 68  ? -49.88700 23.11700 6.22500   1.000 17.79328 ? 67  PHE   C O     1 
ATOM   4582 C  CB    . PHE   D 2 68  ? -49.46800 20.25800 5.94500   1.000 18.88052 ? 67  PHE   C CB    1 
ATOM   4583 C  CG    . PHE   D 2 68  ? -49.29900 19.85400 7.38600   1.000 17.18331 ? 67  PHE   C CG    1 
ATOM   4584 C  CD1   . PHE   D 2 68  ? -49.90300 20.59000 8.40300   1.000 15.98769 ? 67  PHE   C CD1   1 
ATOM   4585 C  CD2   . PHE   D 2 68  ? -48.57500 18.72500 7.73300   1.000 18.18374 ? 67  PHE   C CD2   1 
ATOM   4586 C  CE1   . PHE   D 2 68  ? -49.76500 20.22400 9.73600   1.000 18.33216 ? 67  PHE   C CE1   1 
ATOM   4587 C  CE2   . PHE   D 2 68  ? -48.43700 18.36300 9.06500   1.000 18.18066 ? 67  PHE   C CE2   1 
ATOM   4588 C  CZ    . PHE   D 2 68  ? -49.02800 19.12100 10.06800  1.000 18.07197 ? 67  PHE   C CZ    1 
ATOM   4589 N  N     . THR   D 2 69  ? -47.71200 23.30800 6.74400   1.000 15.72332 ? 68  THR   C N     1 
ATOM   4590 C  CA    . THR   D 2 69  ? -47.91600 24.58400 7.42800   1.000 16.06261 ? 68  THR   C CA    1 
ATOM   4591 C  C     . THR   D 2 69  ? -47.41800 25.76900 6.61100   1.000 18.14293 ? 68  THR   C C     1 
ATOM   4592 O  O     . THR   D 2 69  ? -48.11300 26.77100 6.49900   1.000 20.54946 ? 68  THR   C O     1 
ATOM   4593 C  CB    . THR   D 2 69  ? -47.30200 24.61100 8.83800   1.000 17.40812 ? 68  THR   C CB    1 
ATOM   4594 O  OG1   . THR   D 2 69  ? -45.87200 24.50400 8.75000   1.000 18.10384 ? 68  THR   C OG1   1 
ATOM   4595 C  CG2   . THR   D 2 69  ? -47.88300 23.50600 9.72100   1.000 18.24399 ? 68  THR   C CG2   1 
ATOM   4596 N  N     . ARG   D 2 70  ? -46.22600 25.66900 6.02900   1.000 16.67329 ? 69  ARG   C N     1 
ATOM   4597 C  CA    . ARG   D 2 70  ? -45.68700 26.73000 5.19800   1.000 16.63959 ? 69  ARG   C CA    1 
ATOM   4598 C  C     . ARG   D 2 70  ? -45.77500 26.41100 3.71700   1.000 18.81557 ? 69  ARG   C C     1 
ATOM   4599 O  O     . ARG   D 2 70  ? -45.65200 27.32500 2.89500   1.000 21.36342 ? 69  ARG   C O     1 
ATOM   4600 C  CB    . ARG   D 2 70  ? -44.22500 26.98900 5.58300   1.000 17.44826 ? 69  ARG   C CB    1 
ATOM   4601 C  CG    . ARG   D 2 70  ? -44.00300 27.42000 7.04000   1.000 20.43309 ? 69  ARG   C CG    1 
ATOM   4602 C  CD    . ARG   D 2 70  ? -44.34700 28.88200 7.30000   1.000 31.09443 ? 69  ARG   C CD    1 
ATOM   4603 N  NE    . ARG   D 2 70  ? -45.76300 29.07900 7.58700   1.000 39.56407 ? 69  ARG   C NE    1 
ATOM   4604 C  CZ    . ARG   D 2 70  ? -46.33700 28.82000 8.75500   1.000 47.13112 ? 69  ARG   C CZ    1 
ATOM   4605 N  NH1   . ARG   D 2 70  ? -45.64600 28.32600 9.77100   1.000 49.26661 ? 69  ARG   C NH1   1 
ATOM   4606 N  NH2   . ARG   D 2 70  ? -47.63800 29.05500 8.90500   1.000 48.86362 ? 69  ARG   C NH2   1 
ATOM   4607 N  N     . HIS   D 2 71  ? -45.98500 25.14000 3.36000   1.000 17.40463 ? 70  HIS   C N     1 
ATOM   4608 C  CA    . HIS   D 2 71  ? -46.20600 24.73800 1.96900   1.000 20.47494 ? 70  HIS   C CA    1 
ATOM   4609 C  C     . HIS   D 2 71  ? -45.02800 25.10300 1.07000   1.000 22.22767 ? 70  HIS   C C     1 
ATOM   4610 O  O     . HIS   D 2 71  ? -45.19800 25.30400 -0.13300  1.000 22.53864 ? 70  HIS   C O     1 
ATOM   4611 C  CB    . HIS   D 2 71  ? -47.51000 25.31800 1.40500   1.000 20.39454 ? 70  HIS   C CB    1 
ATOM   4612 C  CG    . HIS   D 2 71  ? -48.68400 25.16400 2.31900   1.000 19.76057 ? 70  HIS   C CG    1 
ATOM   4613 N  ND1   . HIS   D 2 71  ? -49.46800 24.03200 2.33000   1.000 21.04480 ? 70  HIS   C ND1   1 
ATOM   4614 C  CD2   . HIS   D 2 71  ? -49.19500 25.98600 3.26900   1.000 21.10914 ? 70  HIS   C CD2   1 
ATOM   4615 C  CE1   . HIS   D 2 71  ? -50.41900 24.16700 3.23800   1.000 23.08910 ? 70  HIS   C CE1   1 
ATOM   4616 N  NE2   . HIS   D 2 71  ? -50.27200 25.34100 3.82500   1.000 23.03796 ? 70  HIS   C NE2   1 
ATOM   4617 N  N     . ASN   D 2 72  ? -43.82300 25.19300 1.64100   1.000 21.85386 ? 71  ASN   C N     1 
ATOM   4618 C  CA    . ASN   D 2 72  ? -42.66000 25.60900 0.87000   1.000 23.29129 ? 71  ASN   C CA    1 
ATOM   4619 C  C     . ASN   D 2 72  ? -41.38300 24.85100 1.22700   1.000 23.27771 ? 71  ASN   C C     1 
ATOM   4620 O  O     . ASN   D 2 72  ? -40.29800 25.29000 0.82100   1.000 22.65606 ? 71  ASN   C O     1 
ATOM   4621 C  CB    . ASN   D 2 72  ? -42.43700 27.13000 0.97900   1.000 26.05195 ? 71  ASN   C CB    1 
ATOM   4622 C  CG    . ASN   D 2 72  ? -42.04700 27.58200 2.38200   1.000 23.49594 ? 71  ASN   C CG    1 
ATOM   4623 O  OD1   . ASN   D 2 72  ? -41.78600 26.77300 3.26900   1.000 21.99002 ? 71  ASN   C OD1   1 
ATOM   4624 N  ND2   . ASN   D 2 72  ? -42.01000 28.89000 2.58100   1.000 28.24321 ? 71  ASN   C ND2   1 
ATOM   4625 N  N     . GLY   D 2 73  ? -41.47200 23.74500 1.97500   1.000 20.68342 ? 72  GLY   C N     1 
ATOM   4626 C  CA    . GLY   D 2 73  ? -40.30900 22.96100 2.35100   1.000 19.59649 ? 72  GLY   C CA    1 
ATOM   4627 C  C     . GLY   D 2 73  ? -39.63300 23.37900 3.64200   1.000 18.11349 ? 72  GLY   C C     1 
ATOM   4628 O  O     . GLY   D 2 73  ? -38.68200 22.71200 4.07500   1.000 17.14585 ? 72  GLY   C O     1 
ATOM   4629 N  N     . THR   D 2 74  ? -40.09700 24.44400 4.28600   1.000 16.94385 ? 73  THR   C N     1 
ATOM   4630 C  CA    . THR   D 2 74  ? -39.48000 24.89900 5.52300   1.000 15.54306 ? 73  THR   C CA    1 
ATOM   4631 C  C     . THR   D 2 74  ? -40.27700 24.53800 6.76400   1.000 16.32843 ? 73  THR   C C     1 
ATOM   4632 O  O     . THR   D 2 74  ? -39.75900 24.69100 7.87600   1.000 17.17880 ? 73  THR   C O     1 
ATOM   4633 C  CB    . THR   D 2 74  ? -39.30500 26.42800 5.49900   1.000 17.82635 ? 73  THR   C CB    1 
ATOM   4634 O  OG1   . THR   D 2 74  ? -40.58900 27.08800 5.56600   1.000 20.14523 ? 73  THR   C OG1   1 
ATOM   4635 C  CG2   . THR   D 2 74  ? -38.57600 26.84800 4.23600   1.000 22.85768 ? 73  THR   C CG2   1 
ATOM   4636 N  N     . GLY   D 2 75  ? -41.53300 24.11800 6.61900   1.000 14.92152 ? 74  GLY   C N     1 
ATOM   4637 C  CA    . GLY   D 2 75  ? -42.43700 24.03800 7.73500   1.000 15.77258 ? 74  GLY   C CA    1 
ATOM   4638 C  C     . GLY   D 2 75  ? -42.82500 22.62800 8.12300   1.000 17.16978 ? 74  GLY   C C     1 
ATOM   4639 O  O     . GLY   D 2 75  ? -42.11400 21.65100 7.85800   1.000 15.24502 ? 74  GLY   C O     1 
ATOM   4640 N  N     . GLY   D 2 76  ? -43.98700 22.52400 8.74200   1.000 19.39251 ? 75  GLY   C N     1 
ATOM   4641 C  CA    . GLY   D 2 76  ? -44.52400 21.31100 9.30300   1.000 20.45745 ? 75  GLY   C CA    1 
ATOM   4642 C  C     . GLY   D 2 76  ? -44.56400 21.36300 10.82200  1.000 17.03559 ? 75  GLY   C C     1 
ATOM   4643 O  O     . GLY   D 2 76  ? -43.92900 22.19400 11.47200  1.000 21.21771 ? 75  GLY   C O     1 
ATOM   4644 N  N     . LYS   D 2 77  ? -45.33900 20.45800 11.38300  1.000 15.81019 ? 76  LYS   C N     1 
ATOM   4645 C  CA    . LYS   D 2 77  ? -45.50200 20.37800 12.82200  1.000 16.63244 ? 76  LYS   C CA    1 
ATOM   4646 C  C     . LYS   D 2 77  ? -45.99100 18.98400 13.16600  1.000 14.27913 ? 76  LYS   C C     1 
ATOM   4647 O  O     . LYS   D 2 77  ? -46.60200 18.28800 12.33900  1.000 14.01622 ? 76  LYS   C O     1 
ATOM   4648 C  CB    . LYS   D 2 77  ? -46.44700 21.45700 13.36300  1.000 19.55134 ? 76  LYS   C CB    1 
ATOM   4649 C  CG    . LYS   D 2 77  ? -47.92500 21.27300 13.02700  1.000 20.27141 ? 76  LYS   C CG    1 
ATOM   4650 C  CD    . LYS   D 2 77  ? -48.75600 22.38300 13.67000  1.000 22.52622 ? 76  LYS   C CD    1 
ATOM   4651 C  CE    . LYS   D 2 77  ? -50.20900 22.32800 13.24200  1.000 25.03003 ? 76  LYS   C CE    1 
ATOM   4652 N  NZ    . LYS   D 2 77  ? -51.07400 23.33300 13.93400  1.000 28.67353 ? 76  LYS   C NZ    1 
ATOM   4653 N  N     . SER   D 2 78  ? -45.71400 18.58600 14.40200  1.000 14.11564 ? 77  SER   C N     1 
ATOM   4654 C  CA    . SER   D 2 78  ? -46.10900 17.27100 14.87400  1.000 14.35181 ? 77  SER   C CA    1 
ATOM   4655 C  C     . SER   D 2 78  ? -47.39200 17.37500 15.68900  1.000 14.41743 ? 77  SER   C C     1 
ATOM   4656 O  O     . SER   D 2 78  ? -47.87300 18.46300 16.00800  1.000 16.70339 ? 77  SER   C O     1 
ATOM   4657 C  CB    . SER   D 2 78  ? -45.00200 16.65400 15.73000  1.000 14.64836 ? 77  SER   C CB    1 
ATOM   4658 O  OG    . SER   D 2 78  ? -45.04900 17.11500 17.07200  1.000 15.11902 ? 77  SER   C OG    1 
ATOM   4659 N  N     . ILE   D 2 79  ? -47.93900 16.21200 16.04200  1.000 14.59895 ? 78  ILE   C N     1 
ATOM   4660 C  CA    . ILE   D 2 79  ? -49.09000 16.17300 16.93600  1.000 16.05088 ? 78  ILE   C CA    1 
ATOM   4661 C  C     . ILE   D 2 79  ? -48.72500 16.49700 18.37700  1.000 16.28131 ? 78  ILE   C C     1 
ATOM   4662 O  O     . ILE   D 2 79  ? -49.62600 16.61200 19.22600  1.000 20.06281 ? 78  ILE   C O     1 
ATOM   4663 C  CB    . ILE   D 2 79  ? -49.80700 14.81100 16.84200  1.000 15.54337 ? 78  ILE   C CB    1 
ATOM   4664 C  CG1   . ILE   D 2 79  ? -48.93500 13.67600 17.39800  1.000 15.54677 ? 78  ILE   C CG1   1 
ATOM   4665 C  CG2   . ILE   D 2 79  ? -50.25700 14.54500 15.40500  1.000 17.44378 ? 78  ILE   C CG2   1 
ATOM   4666 C  CD1   . ILE   D 2 79  ? -49.70400 12.37800 17.65800  1.000 18.41130 ? 78  ILE   C CD1   1 
ATOM   4667 N  N     . TYR   D 2 80  ? -47.43500 16.64800 18.67800  1.000 15.66267 ? 79  TYR   C N     1 
ATOM   4668 C  CA    . TYR   D 2 80  ? -46.96500 16.92800 20.03100  1.000 17.57217 ? 79  TYR   C CA    1 
ATOM   4669 C  C     . TYR   D 2 80  ? -46.54700 18.37900 20.21700  1.000 19.80693 ? 79  TYR   C C     1 
ATOM   4670 O  O     . TYR   D 2 80  ? -46.11600 18.75600 21.31000  1.000 24.91264 ? 79  TYR   C O     1 
ATOM   4671 C  CB    . TYR   D 2 80  ? -45.76800 16.02300 20.35600  1.000 17.12384 ? 79  TYR   C CB    1 
ATOM   4672 C  CG    . TYR   D 2 80  ? -45.99500 14.56600 20.03900  1.000 15.74205 ? 79  TYR   C CG    1 
ATOM   4673 C  CD1   . TYR   D 2 80  ? -46.94900 13.83200 20.73400  1.000 16.82912 ? 79  TYR   C CD1   1 
ATOM   4674 C  CD2   . TYR   D 2 80  ? -45.25600 13.91800 19.04400  1.000 16.19591 ? 79  TYR   C CD2   1 
ATOM   4675 C  CE1   . TYR   D 2 80  ? -47.16300 12.49300 20.45900  1.000 17.09900 ? 79  TYR   C CE1   1 
ATOM   4676 C  CE2   . TYR   D 2 80  ? -45.46000 12.58100 18.76200  1.000 16.79466 ? 79  TYR   C CE2   1 
ATOM   4677 C  CZ    . TYR   D 2 80  ? -46.42300 11.87700 19.46000  1.000 16.53302 ? 79  TYR   C CZ    1 
ATOM   4678 O  OH    . TYR   D 2 80  ? -46.64500 10.53700 19.19300  1.000 16.70032 ? 79  TYR   C OH    1 
ATOM   4679 N  N     . GLY   D 2 81  ? -46.66100 19.19700 19.18400  1.000 17.53975 ? 80  GLY   C N     1 
ATOM   4680 C  CA    . GLY   D 2 81  ? -46.09700 20.52400 19.15600  1.000 20.04581 ? 80  GLY   C CA    1 
ATOM   4681 C  C     . GLY   D 2 81  ? -45.26300 20.69900 17.90600  1.000 17.48187 ? 80  GLY   C C     1 
ATOM   4682 O  O     . GLY   D 2 81  ? -45.21500 19.83000 17.03000  1.000 18.75593 ? 80  GLY   C O     1 
ATOM   4683 N  N     . GLU   D 2 82  ? -44.56900 21.82900 17.81500  1.000 16.59272 ? 81  GLU   C N     1 
ATOM   4684 C  CA    . GLU   D 2 82  ? -43.83900 22.11300 16.58600  1.000 16.19115 ? 81  GLU   C CA    1 
ATOM   4685 C  C     . GLU   D 2 82  ? -42.73000 21.09700 16.33000  1.000 17.75453 ? 81  GLU   C C     1 
ATOM   4686 O  O     . GLU   D 2 82  ? -42.46800 20.73500 15.17600  1.000 20.12594 ? 81  GLU   C O     1 
ATOM   4687 C  CB    . GLU   D 2 82  ? -43.30800 23.54200 16.61400  1.000 16.31985 ? 81  GLU   C CB    1 
ATOM   4688 C  CG    . GLU   D 2 82  ? -44.42800 24.58300 16.52200  1.000 19.30502 ? 81  GLU   C CG    1 
ATOM   4689 C  CD    . GLU   D 2 82  ? -43.94600 26.00900 16.59100  1.000 20.19029 ? 81  GLU   C CD    1 
ATOM   4690 O  OE1   . GLU   D 2 82  ? -42.71900 26.23700 16.50900  1.000 22.28397 ? 81  GLU   C OE1   1 
ATOM   4691 O  OE2   . GLU   D 2 82  ? -44.80700 26.91200 16.71900  1.000 21.67775 ? 81  GLU   C OE2   1 
ATOM   4692 N  N     . LYS   D 2 83  ? -42.06900 20.62900 17.38500  1.000 16.16883 ? 82  LYS   C N     1 
ATOM   4693 C  CA    . LYS   D 2 83  ? -40.95700 19.69700 17.25400  1.000 18.41869 ? 82  LYS   C CA    1 
ATOM   4694 C  C     . LYS   D 2 83  ? -41.06300 18.63300 18.33500  1.000 16.60607 ? 82  LYS   C C     1 
ATOM   4695 O  O     . LYS   D 2 83  ? -41.63400 18.87200 19.40900  1.000 16.48901 ? 82  LYS   C O     1 
ATOM   4696 C  CB    . LYS   D 2 83  ? -39.59300 20.37600 17.48100  1.000 24.61212 ? 82  LYS   C CB    1 
ATOM   4697 C  CG    . LYS   D 2 83  ? -39.16800 21.45100 16.51000  1.000 35.83310 ? 82  LYS   C CG    1 
ATOM   4698 C  CD    . LYS   D 2 83  ? -37.92100 22.14600 17.06200  1.000 42.54262 ? 82  LYS   C CD    1 
ATOM   4699 C  CE    . LYS   D 2 83  ? -37.57500 23.41200 16.30200  1.000 48.01897 ? 82  LYS   C CE    1 
ATOM   4700 N  NZ    . LYS   D 2 83  ? -36.44200 24.14900 16.93400  1.000 51.36268 ? 82  LYS   C NZ    1 
ATOM   4701 N  N     . PHE   D 2 84  ? -40.47400 17.47100 18.06100  1.000 14.73724 ? 83  PHE   C N     1 
ATOM   4702 C  CA    . PHE   D 2 84  ? -40.30200 16.45800 19.09500  1.000 14.65863 ? 83  PHE   C CA    1 
ATOM   4703 C  C     . PHE   D 2 84  ? -38.94700 15.78500 18.95900  1.000 13.67389 ? 83  PHE   C C     1 
ATOM   4704 O  O     . PHE   D 2 84  ? -38.30600 15.81300 17.90100  1.000 14.28617 ? 83  PHE   C O     1 
ATOM   4705 C  CB    . PHE   D 2 84  ? -41.48000 15.46700 19.19700  1.000 14.68648 ? 83  PHE   C CB    1 
ATOM   4706 C  CG    . PHE   D 2 84  ? -41.66000 14.55900 17.99800  1.000 14.10492 ? 83  PHE   C CG    1 
ATOM   4707 C  CD1   . PHE   D 2 84  ? -42.23600 15.03100 16.83500  1.000 14.88923 ? 83  PHE   C CD1   1 
ATOM   4708 C  CD2   . PHE   D 2 84  ? -41.34100 13.20600 18.07900  1.000 15.10900 ? 83  PHE   C CD2   1 
ATOM   4709 C  CE1   . PHE   D 2 84  ? -42.45800 14.18400 15.75200  1.000 14.32438 ? 83  PHE   C CE1   1 
ATOM   4710 C  CE2   . PHE   D 2 84  ? -41.54800 12.34700 16.99600  1.000 16.42193 ? 83  PHE   C CE2   1 
ATOM   4711 C  CZ    . PHE   D 2 84  ? -42.10800 12.83900 15.82700  1.000 15.48606 ? 83  PHE   C CZ    1 
ATOM   4712 N  N     . GLU   D 2 85  ? -38.53500 15.13800 20.04500  1.000 14.73157 ? 84  GLU   C N     1 
ATOM   4713 C  CA    . GLU   D 2 85  ? -37.17600 14.63000 20.11400  1.000 17.55746 ? 84  GLU   C CA    1 
ATOM   4714 C  C     . GLU   D 2 85  ? -37.01000 13.37800 19.25800  1.000 15.24307 ? 84  GLU   C C     1 
ATOM   4715 O  O     . GLU   D 2 85  ? -37.97900 12.70200 18.88600  1.000 16.31435 ? 84  GLU   C O     1 
ATOM   4716 C  CB    . GLU   D 2 85  ? -36.77100 14.35600 21.56400  1.000 22.89224 ? 84  GLU   C CB    1 
ATOM   4717 C  CG    . GLU   D 2 85  ? -37.60900 13.33000 22.26700  1.000 30.25575 ? 84  GLU   C CG    1 
ATOM   4718 C  CD    . GLU   D 2 85  ? -37.32000 13.30100 23.75800  1.000 37.32770 ? 84  GLU   C CD    1 
ATOM   4719 O  OE1   . GLU   D 2 85  ? -36.76100 14.29300 24.27600  1.000 40.86603 ? 84  GLU   C OE1   1 
ATOM   4720 O  OE2   . GLU   D 2 85  ? -37.64600 12.29000 24.41000  1.000 41.02582 ? 84  GLU   C OE2   1 
ATOM   4721 N  N     . ASP   D 2 86  ? -35.75800 13.09900 18.91600  1.000 14.34803 ? 85  ASP   C N     1 
ATOM   4722 C  CA    . ASP   D 2 86  ? -35.42100 11.84200 18.25300  1.000 14.85543 ? 85  ASP   C CA    1 
ATOM   4723 C  C     . ASP   D 2 86  ? -35.69200 10.69400 19.21500  1.000 14.00279 ? 85  ASP   C C     1 
ATOM   4724 O  O     . ASP   D 2 86  ? -35.09300 10.61800 20.29900  1.000 17.26896 ? 85  ASP   C O     1 
ATOM   4725 C  CB    . ASP   D 2 86  ? -33.95600 11.85200 17.82800  1.000 15.06303 ? 85  ASP   C CB    1 
ATOM   4726 C  CG    . ASP   D 2 86  ? -33.67100 12.91400 16.78700  1.000 14.57262 ? 85  ASP   C CG    1 
ATOM   4727 O  OD1   . ASP   D 2 86  ? -34.46700 13.02800 15.82700  1.000 14.13355 ? 85  ASP   C OD1   1 
ATOM   4728 O  OD2   . ASP   D 2 86  ? -32.65600 13.63600 16.92600  1.000 14.74150 ? 85  ASP   C OD2   1 
ATOM   4729 N  N     . GLU   D 2 87  ? -36.59900 9.80800  18.82300  1.000 14.00294 ? 86  GLU   C N     1 
ATOM   4730 C  CA    . GLU   D 2 87  ? -37.09200 8.78600  19.73700  1.000 15.33501 ? 86  GLU   C CA    1 
ATOM   4731 C  C     . GLU   D 2 87  ? -36.04500 7.70200  19.97000  1.000 14.76942 ? 86  GLU   C C     1 
ATOM   4732 O  O     . GLU   D 2 87  ? -35.73500 7.35900  21.10900  1.000 15.46284 ? 86  GLU   C O     1 
ATOM   4733 C  CB    . GLU   D 2 87  ? -38.38700 8.18500  19.19200  1.000 15.76708 ? 86  GLU   C CB    1 
ATOM   4734 C  CG    . GLU   D 2 87  ? -39.03200 7.17600  20.10700  1.000 15.23875 ? 86  GLU   C CG    1 
ATOM   4735 C  CD    . GLU   D 2 87  ? -40.41800 6.80300  19.64800  1.000 15.97445 ? 86  GLU   C CD    1 
ATOM   4736 O  OE1   . GLU   D 2 87  ? -40.77400 7.14800  18.51100  1.000 15.72754 ? 86  GLU   C OE1   1 
ATOM   4737 O  OE2   . GLU   D 2 87  ? -41.15200 6.17100  20.42500  1.000 15.68365 ? 86  GLU   C OE2   1 
ATOM   4738 N  N     . ASN   D 2 88  ? -35.52300 7.12300  18.90200  1.000 15.07254 ? 87  ASN   C N     1 
ATOM   4739 C  CA    . ASN   D 2 88  ? -34.39400 6.20900  18.98400  1.000 14.07549 ? 87  ASN   C CA    1 
ATOM   4740 C  C     . ASN   D 2 88  ? -33.83100 6.07000  17.57900  1.000 13.99300 ? 87  ASN   C C     1 
ATOM   4741 O  O     . ASN   D 2 88  ? -34.39100 6.59200  16.61400  1.000 15.64403 ? 87  ASN   C O     1 
ATOM   4742 C  CB    . ASN   D 2 88  ? -34.78700 4.85500  19.60000  1.000 14.19103 ? 87  ASN   C CB    1 
ATOM   4743 C  CG    . ASN   D 2 88  ? -35.79600 4.09800  18.75400  1.000 14.53072 ? 87  ASN   C CG    1 
ATOM   4744 O  OD1   . ASN   D 2 88  ? -35.52800 3.78800  17.59000  1.000 15.62536 ? 87  ASN   C OD1   1 
ATOM   4745 N  ND2   . ASN   D 2 88  ? -36.96500 3.79400  19.32900  1.000 14.84068 ? 87  ASN   C ND2   1 
ATOM   4746 N  N     . PHE   D 2 89  ? -32.71000 5.36600  17.47300  1.000 15.08979 ? 88  PHE   C N     1 
ATOM   4747 C  CA    . PHE   D 2 89  ? -32.08300 5.07300  16.18700  1.000 15.48906 ? 88  PHE   C CA    1 
ATOM   4748 C  C     . PHE   D 2 89  ? -31.94400 3.56700  15.97600  1.000 16.80616 ? 88  PHE   C C     1 
ATOM   4749 O  O     . PHE   D 2 89  ? -30.97300 3.09300  15.38200  1.000 18.72219 ? 88  PHE   C O     1 
ATOM   4750 C  CB    . PHE   D 2 89  ? -30.74800 5.80900  16.04500  1.000 16.20116 ? 88  PHE   C CB    1 
ATOM   4751 C  CG    . PHE   D 2 89  ? -30.88000 7.30200  16.16600  1.000 16.34887 ? 88  PHE   C CG    1 
ATOM   4752 C  CD1   . PHE   D 2 89  ? -31.48700 8.03600  15.16100  1.000 18.00623 ? 88  PHE   C CD1   1 
ATOM   4753 C  CD2   . PHE   D 2 89  ? -30.42600 7.96900  17.29700  1.000 19.14465 ? 88  PHE   C CD2   1 
ATOM   4754 C  CE1   . PHE   D 2 89  ? -31.62000 9.40800  15.26200  1.000 17.05296 ? 88  PHE   C CE1   1 
ATOM   4755 C  CE2   . PHE   D 2 89  ? -30.55000 9.34400  17.40300  1.000 19.72529 ? 88  PHE   C CE2   1 
ATOM   4756 C  CZ    . PHE   D 2 89  ? -31.16000 10.06400 16.38400  1.000 19.37060 ? 88  PHE   C CZ    1 
ATOM   4757 N  N     . ILE   D 2 90  ? -32.92600 2.80700  16.46400  1.000 16.09178 ? 89  ILE   C N     1 
ATOM   4758 C  CA    . ILE   D 2 90  ? -32.86000 1.35000  16.37700  1.000 17.84734 ? 89  ILE   C CA    1 
ATOM   4759 C  C     . ILE   D 2 90  ? -32.85500 0.89800  14.92500  1.000 17.18044 ? 89  ILE   C C     1 
ATOM   4760 O  O     . ILE   D 2 90  ? -32.03900 0.05700  14.52000  1.000 20.18275 ? 89  ILE   C O     1 
ATOM   4761 C  CB    . ILE   D 2 90  ? -34.01800 0.71800  17.16300  1.000 19.52545 ? 89  ILE   C CB    1 
ATOM   4762 C  CG1   . ILE   D 2 90  ? -33.89900 1.05100  18.65800  1.000 23.33684 ? 89  ILE   C CG1   1 
ATOM   4763 C  CG2   . ILE   D 2 90  ? -34.07200 -0.80200 16.92200  1.000 22.46217 ? 89  ILE   C CG2   1 
ATOM   4764 C  CD1   . ILE   D 2 90  ? -35.09800 0.60100  19.46900  1.000 24.51407 ? 89  ILE   C CD1   1 
ATOM   4765 N  N     . LEU   D 2 91  ? -33.78500 1.41600  14.12900  1.000 15.77246 ? 90  LEU   C N     1 
ATOM   4766 C  CA    . LEU   D 2 91  ? -33.92200 0.96700  12.75500  1.000 15.45250 ? 90  LEU   C CA    1 
ATOM   4767 C  C     . LEU   D 2 91  ? -33.02800 1.77000  11.82000  1.000 15.01185 ? 90  LEU   C C     1 
ATOM   4768 O  O     . LEU   D 2 91  ? -32.76700 2.96300  12.02400  1.000 15.39462 ? 90  LEU   C O     1 
ATOM   4769 C  CB    . LEU   D 2 91  ? -35.37500 1.05700  12.30800  1.000 17.17401 ? 90  LEU   C CB    1 
ATOM   4770 C  CG    . LEU   D 2 91  ? -36.28000 0.16300  13.15300  1.000 19.63484 ? 90  LEU   C CG    1 
ATOM   4771 C  CD1   . LEU   D 2 91  ? -37.70000 0.45600  12.78000  1.000 22.44589 ? 90  LEU   C CD1   1 
ATOM   4772 C  CD2   . LEU   D 2 91  ? -35.95400 -1.31000 12.94200  1.000 22.95069 ? 90  LEU   C CD2   1 
ATOM   4773 N  N     . LYS   D 2 92  ? -32.58600 1.11600  10.75800  1.000 16.24043 ? 91  LYS   C N     1 
ATOM   4774 C  CA    . LYS   D 2 92  ? -31.57300 1.68300  9.89200   1.000 17.28729 ? 91  LYS   C CA    1 
ATOM   4775 C  C     . LYS   D 2 92  ? -32.12100 1.92200  8.48900   1.000 14.98685 ? 91  LYS   C C     1 
ATOM   4776 O  O     . LYS   D 2 92  ? -33.15700 1.37400  8.08400   1.000 15.61890 ? 91  LYS   C O     1 
ATOM   4777 C  CB    . LYS   D 2 92  ? -30.31600 0.79600  9.87300   1.000 19.41364 ? 91  LYS   C CB    1 
ATOM   4778 C  CG    . LYS   D 2 92  ? -29.61500 0.76200  11.23500  1.000 23.57959 ? 91  LYS   C CG    1 
ATOM   4779 C  CD    . LYS   D 2 92  ? -28.53000 -0.29300 11.28500  1.000 33.30439 ? 91  LYS   C CD    1 
ATOM   4780 C  CE    . LYS   D 2 92  ? -27.31400 0.07300  10.44800  1.000 40.04179 ? 91  LYS   C CE    1 
ATOM   4781 N  NZ    . LYS   D 2 92  ? -27.45900 -0.25500 8.99600   1.000 44.65147 ? 91  LYS   C NZ    1 
ATOM   4782 N  N     . HIS   D 2 93  ? -31.39700 2.76000  7.74800   1.000 16.37065 ? 92  HIS   C N     1 
ATOM   4783 C  CA    . HIS   D 2 93  ? -31.76200 3.10600  6.37600   1.000 16.66440 ? 92  HIS   C CA    1 
ATOM   4784 C  C     . HIS   D 2 93  ? -31.16800 2.03300  5.47000   1.000 17.52538 ? 92  HIS   C C     1 
ATOM   4785 O  O     . HIS   D 2 93  ? -30.08000 2.19900  4.92000   1.000 21.12683 ? 92  HIS   C O     1 
ATOM   4786 C  CB    . HIS   D 2 93  ? -31.22200 4.48400  6.01400   1.000 16.12104 ? 92  HIS   C CB    1 
ATOM   4787 C  CG    . HIS   D 2 93  ? -31.78300 5.60400  6.84300   1.000 13.28297 ? 92  HIS   C CG    1 
ATOM   4788 N  ND1   . HIS   D 2 93  ? -31.26800 5.95000  8.07400   1.000 13.72891 ? 92  HIS   C ND1   1 
ATOM   4789 C  CD2   . HIS   D 2 93  ? -32.80600 6.46400  6.61200   1.000 14.60859 ? 92  HIS   C CD2   1 
ATOM   4790 C  CE1   . HIS   D 2 93  ? -31.94600 6.97600  8.56400   1.000 13.27143 ? 92  HIS   C CE1   1 
ATOM   4791 N  NE2   . HIS   D 2 93  ? -32.89600 7.29600  7.70400   1.000 14.50151 ? 92  HIS   C NE2   1 
ATOM   4792 N  N     . THR   D 2 94  ? -31.89700 0.92600  5.29800   1.000 16.52598 ? 93  THR   C N     1 
ATOM   4793 C  CA    . THR   D 2 94  ? -31.35900 -0.30500 4.72400   1.000 20.71239 ? 93  THR   C CA    1 
ATOM   4794 C  C     . THR   D 2 94  ? -31.63500 -0.47300 3.23700   1.000 23.84076 ? 93  THR   C C     1 
ATOM   4795 O  O     . THR   D 2 94  ? -31.08100 -1.39600 2.63400   1.000 29.19983 ? 93  THR   C O     1 
ATOM   4796 C  CB    . THR   D 2 94  ? -31.90900 -1.53200 5.46000   1.000 19.86346 ? 93  THR   C CB    1 
ATOM   4797 O  OG1   . THR   D 2 94  ? -33.34000 -1.45000 5.52200   1.000 24.58508 ? 93  THR   C OG1   1 
ATOM   4798 C  CG2   . THR   D 2 94  ? -31.32900 -1.61800 6.86000   1.000 22.78568 ? 93  THR   C CG2   1 
ATOM   4799 N  N     . GLY   D 2 95  ? -32.45900 0.38200  2.62900   1.000 18.95201 ? 94  GLY   C N     1 
ATOM   4800 C  CA    . GLY   D 2 95  ? -32.75000 0.22400  1.22100   1.000 19.49473 ? 94  GLY   C CA    1 
ATOM   4801 C  C     . GLY   D 2 95  ? -33.97600 0.99400  0.77700   1.000 19.32673 ? 94  GLY   C C     1 
ATOM   4802 O  O     . GLY   D 2 95  ? -34.57000 1.76200  1.53700   1.000 19.79786 ? 94  GLY   C O     1 
ATOM   4803 N  N     . PRO   D 2 96  ? -34.38900 0.78300  -0.46900  1.000 18.78886 ? 95  PRO   C N     1 
ATOM   4804 C  CA    . PRO   D 2 96  ? -35.57200 1.48300  -0.97800  1.000 18.70205 ? 95  PRO   C CA    1 
ATOM   4805 C  C     . PRO   D 2 96  ? -36.80600 1.14700  -0.15800  1.000 18.64435 ? 95  PRO   C C     1 
ATOM   4806 O  O     . PRO   D 2 96  ? -36.95600 0.04000  0.36200   1.000 22.02463 ? 95  PRO   C O     1 
ATOM   4807 C  CB    . PRO   D 2 96  ? -35.71300 0.95800  -2.41100  1.000 19.67603 ? 95  PRO   C CB    1 
ATOM   4808 C  CG    . PRO   D 2 96  ? -34.39000 0.36900  -2.73500  1.000 21.83272 ? 95  PRO   C CG    1 
ATOM   4809 C  CD    . PRO   D 2 96  ? -33.82600 -0.15100 -1.45100  1.000 19.93306 ? 95  PRO   C CD    1 
ATOM   4810 N  N     . GLY   D 2 97  ? -37.67900 2.14000  -0.02300  1.000 17.37499 ? 96  GLY   C N     1 
ATOM   4811 C  CA    . GLY   D 2 97  ? -38.92600 1.97300  0.68100   1.000 15.98491 ? 96  GLY   C CA    1 
ATOM   4812 C  C     . GLY   D 2 97  ? -38.90000 2.39600  2.13000   1.000 15.47101 ? 96  GLY   C C     1 
ATOM   4813 O  O     . GLY   D 2 97  ? -39.96700 2.53000  2.72600   1.000 15.83777 ? 96  GLY   C O     1 
ATOM   4814 N  N     . ILE   D 2 98  ? -37.71500 2.59300  2.71300   1.000 14.40804 ? 97  ILE   C N     1 
ATOM   4815 C  CA    . ILE   D 2 98  ? -37.62100 3.02500  4.10200   1.000 14.61626 ? 97  ILE   C CA    1 
ATOM   4816 C  C     . ILE   D 2 98  ? -38.23200 4.41400  4.26700   1.000 15.36711 ? 97  ILE   C C     1 
ATOM   4817 O  O     . ILE   D 2 98  ? -38.01000 5.32700  3.45400   1.000 14.57592 ? 97  ILE   C O     1 
ATOM   4818 C  CB    . ILE   D 2 98  ? -36.15600 2.98800  4.57000   1.000 15.80513 ? 97  ILE   C CB    1 
ATOM   4819 C  CG1   . ILE   D 2 98  ? -35.66600 1.53400  4.74400   1.000 19.52932 ? 97  ILE   C CG1   1 
ATOM   4820 C  CG2   . ILE   D 2 98  ? -35.94900 3.86100  5.82600   1.000 18.57985 ? 97  ILE   C CG2   1 
ATOM   4821 C  CD1   . ILE   D 2 98  ? -36.27200 0.78400  5.92000   1.000 20.86528 ? 97  ILE   C CD1   1 
ATOM   4822 N  N     . LEU   D 2 99  ? -39.02100 4.56700  5.32600   1.000 12.45558 ? 98  LEU   C N     1 
ATOM   4823 C  CA    . LEU   D 2 99  ? -39.69200 5.80600  5.68500   1.000 12.12853 ? 98  LEU   C CA    1 
ATOM   4824 C  C     . LEU   D 2 99  ? -39.03300 6.36100  6.94600   1.000 12.65477 ? 98  LEU   C C     1 
ATOM   4825 O  O     . LEU   D 2 99  ? -38.94500 5.67100  7.97000   1.000 13.02945 ? 98  LEU   C O     1 
ATOM   4826 C  CB    . LEU   D 2 99  ? -41.16400 5.50400  5.95400   1.000 14.04071 ? 98  LEU   C CB    1 
ATOM   4827 C  CG    . LEU   D 2 99  ? -42.07700 6.66600  6.34900   1.000 14.41216 ? 98  LEU   C CG    1 
ATOM   4828 C  CD1   . LEU   D 2 99  ? -42.18000 7.74900  5.26500   1.000 15.16944 ? 98  LEU   C CD1   1 
ATOM   4829 C  CD2   . LEU   D 2 99  ? -43.47700 6.13400  6.71900   1.000 14.07183 ? 98  LEU   C CD2   1 
ATOM   4830 N  N     . SER   D 2 100 ? -38.57900 7.60400  6.86700   1.000 12.26038 ? 99  SER   C N     1 
ATOM   4831 C  CA    . SER   D 2 100 ? -37.72800 8.19700  7.89000   1.000 11.62148 ? 99  SER   C CA    1 
ATOM   4832 C  C     . SER   D 2 100 ? -38.06300 9.67600  8.05400   1.000 11.05867 ? 99  SER   C C     1 
ATOM   4833 O  O     . SER   D 2 100 ? -38.60600 10.31000 7.15600   1.000 10.99377 ? 99  SER   C O     1 
ATOM   4834 C  CB    . SER   D 2 100 ? -36.25900 7.97800  7.51300   1.000 13.51989 ? 99  SER   C CB    1 
ATOM   4835 O  OG    . SER   D 2 100 ? -35.36600 8.49600  8.48000   1.000 13.22976 ? 99  SER   C OG    1 
ATOM   4836 N  N     . MET   D 2 101 ? -37.74800 10.21900 9.23000   1.000 11.44096 ? 100 MET   C N     1 
ATOM   4837 C  CA    . MET   D 2 101 ? -38.06700 11.61100 9.52900   1.000 12.40373 ? 100 MET   C CA    1 
ATOM   4838 C  C     . MET   D 2 101 ? -37.01500 12.55900 8.97400   1.000 10.65407 ? 100 MET   C C     1 
ATOM   4839 O  O     . MET   D 2 101 ? -35.81500 12.37400 9.17800   1.000 12.41769 ? 100 MET   C O     1 
ATOM   4840 C  CB    . MET   D 2 101 ? -38.19100 11.83500 11.03100  1.000 13.61237 ? 100 MET   C CB    1 
ATOM   4841 C  CG    . MET   D 2 101 ? -39.41700 11.20200 11.66000  1.000 12.65546 ? 100 MET   C CG    1 
ATOM   4842 S  SD    . MET   D 2 101 ? -40.99400 11.72300 10.90900  1.000 13.68709 ? 100 MET   C SD    1 
ATOM   4843 C  CE    . MET   D 2 101 ? -41.23200 13.37000 11.57400  1.000 14.72188 ? 100 MET   C CE    1 
ATOM   4844 N  N     . ALA   D 2 102 ? -37.48000 13.59000 8.28800   1.000 11.74927 ? 101 ALA   C N     1 
ATOM   4845 C  CA    . ALA   D 2 102 ? -36.62200 14.71300 7.94700   1.000 12.12538 ? 101 ALA   C CA    1 
ATOM   4846 C  C     . ALA   D 2 102 ? -36.43400 15.58700 9.18000   1.000 10.93525 ? 101 ALA   C C     1 
ATOM   4847 O  O     . ALA   D 2 102 ? -37.22500 15.53800 10.11400  1.000 13.32857 ? 101 ALA   C O     1 
ATOM   4848 C  CB    . ALA   D 2 102 ? -37.25700 15.52300 6.82200   1.000 13.26841 ? 101 ALA   C CB    1 
ATOM   4849 N  N     . ASN   D 2 103 ? -35.36600 16.38100 9.20400   1.000 11.95636 ? 102 ASN   C N     1 
ATOM   4850 C  CA    . ASN   D 2 103 ? -35.15800 17.24200 10.36400  1.000 13.25166 ? 102 ASN   C CA    1 
ATOM   4851 C  C     . ASN   D 2 103 ? -34.17300 18.34900 10.00800  1.000 12.34605 ? 102 ASN   C C     1 
ATOM   4852 O  O     . ASN   D 2 103 ? -33.56000 18.34600 8.93500   1.000 14.91324 ? 102 ASN   C O     1 
ATOM   4853 C  CB    . ASN   D 2 103 ? -34.71900 16.42700 11.59100  1.000 13.22607 ? 102 ASN   C CB    1 
ATOM   4854 C  CG    . ASN   D 2 103 ? -33.36100 15.80100 11.42200  1.000 13.79700 ? 102 ASN   C CG    1 
ATOM   4855 O  OD1   . ASN   D 2 103 ? -32.39500 16.47100 11.04900  1.000 14.69211 ? 102 ASN   C OD1   1 
ATOM   4856 N  ND2   . ASN   D 2 103 ? -33.27000 14.50500 11.71400  1.000 14.14556 ? 102 ASN   C ND2   1 
ATOM   4857 N  N     . ALA   D 2 104 ? -34.01900 19.28900 10.94000  1.000 14.15204 ? 103 ALA   C N     1 
ATOM   4858 C  CA    . ALA   D 2 104 ? -33.07500 20.39500 10.83700  1.000 15.83854 ? 103 ALA   C CA    1 
ATOM   4859 C  C     . ALA   D 2 104 ? -32.01300 20.29900 11.92800  1.000 16.55830 ? 103 ALA   C C     1 
ATOM   4860 O  O     . ALA   D 2 104 ? -31.55100 21.30800 12.47000  1.000 21.39842 ? 103 ALA   C O     1 
ATOM   4861 C  CB    . ALA   D 2 104 ? -33.79200 21.74500 10.88100  1.000 17.55817 ? 103 ALA   C CB    1 
ATOM   4862 N  N     . GLY   D 2 105 ? -31.61900 19.07200 12.26600  1.000 16.11841 ? 104 GLY   C N     1 
ATOM   4863 C  CA    . GLY   D 2 105 ? -30.67400 18.84200 13.33600  1.000 16.91460 ? 104 GLY   C CA    1 
ATOM   4864 C  C     . GLY   D 2 105 ? -31.28900 18.02000 14.45700  1.000 15.91474 ? 104 GLY   C C     1 
ATOM   4865 O  O     . GLY   D 2 105 ? -32.44400 17.57900 14.38000  1.000 15.78397 ? 104 GLY   C O     1 
ATOM   4866 N  N     . PRO   D 2 106 ? -30.53200 17.81200 15.53200  1.000 17.04551 ? 105 PRO   C N     1 
ATOM   4867 C  CA    . PRO   D 2 106 ? -31.01800 16.94300 16.61800  1.000 17.24731 ? 105 PRO   C CA    1 
ATOM   4868 C  C     . PRO   D 2 106 ? -32.34200 17.43200 17.19300  1.000 14.65666 ? 105 PRO   C C     1 
ATOM   4869 O  O     . PRO   D 2 106 ? -32.52700 18.62400 17.45800  1.000 16.54457 ? 105 PRO   C O     1 
ATOM   4870 C  CB    . PRO   D 2 106 ? -29.89000 17.00800 17.65700  1.000 20.14995 ? 105 PRO   C CB    1 
ATOM   4871 C  CG    . PRO   D 2 106 ? -28.67800 17.33400 16.85100  1.000 20.05803 ? 105 PRO   C CG    1 
ATOM   4872 C  CD    . PRO   D 2 106 ? -29.13800 18.24300 15.74700  1.000 18.42812 ? 105 PRO   C CD    1 
ATOM   4873 N  N     . ASN   D 2 107 ? -33.27400 16.49800 17.37500  1.000 15.56207 ? 106 ASN   C N     1 
ATOM   4874 C  CA    . ASN   D 2 107 ? -34.49900 16.74400 18.13200  1.000 16.47219 ? 106 ASN   C CA    1 
ATOM   4875 C  C     . ASN   D 2 107 ? -35.37800 17.82000 17.50700  1.000 15.20377 ? 106 ASN   C C     1 
ATOM   4876 O  O     . ASN   D 2 107 ? -35.93500 18.66100 18.21400  1.000 16.38598 ? 106 ASN   C O     1 
ATOM   4877 C  CB    . ASN   D 2 107 ? -34.19600 17.04900 19.59500  1.000 17.10337 ? 106 ASN   C CB    1 
ATOM   4878 C  CG    . ASN   D 2 107 ? -33.36000 15.97100 20.22200  1.000 18.52358 ? 106 ASN   C CG    1 
ATOM   4879 O  OD1   . ASN   D 2 107 ? -33.71100 14.79100 20.14700  1.000 17.91359 ? 106 ASN   C OD1   1 
ATOM   4880 N  ND2   . ASN   D 2 107 ? -32.21600 16.35100 20.78500  1.000 22.00883 ? 106 ASN   C ND2   1 
ATOM   4881 N  N     . THR   D 2 108 ? -35.51600 17.78500 16.17300  1.000 13.65890 ? 107 THR   C N     1 
ATOM   4882 C  CA    . THR   D 2 108 ? -36.34800 18.75400 15.45800  1.000 13.43093 ? 107 THR   C CA    1 
ATOM   4883 C  C     . THR   D 2 108 ? -37.38400 18.06600 14.56300  1.000 14.01277 ? 107 THR   C C     1 
ATOM   4884 O  O     . THR   D 2 108 ? -37.79800 18.61600 13.54800  1.000 17.15196 ? 107 THR   C O     1 
ATOM   4885 C  CB    . THR   D 2 108 ? -35.51000 19.76700 14.67600  1.000 15.21150 ? 107 THR   C CB    1 
ATOM   4886 O  OG1   . THR   D 2 108 ? -34.71700 19.09100 13.69200  1.000 16.56471 ? 107 THR   C OG1   1 
ATOM   4887 C  CG2   . THR   D 2 108 ? -34.61600 20.58300 15.59700  1.000 16.98492 ? 107 THR   C CG2   1 
ATOM   4888 N  N     . ASN   D 2 109 ? -37.81400 16.86300 14.91600  1.000 12.89409 ? 108 ASN   C N     1 
ATOM   4889 C  CA    . ASN   D 2 109 ? -38.84200 16.18800 14.12800  1.000 12.82868 ? 108 ASN   C CA    1 
ATOM   4890 C  C     . ASN   D 2 109 ? -40.13800 16.97700 14.17100  1.000 12.63606 ? 108 ASN   C C     1 
ATOM   4891 O  O     . ASN   D 2 109 ? -40.57800 17.40000 15.23800  1.000 13.96381 ? 108 ASN   C O     1 
ATOM   4892 C  CB    . ASN   D 2 109 ? -39.08600 14.79800 14.69500  1.000 13.94560 ? 108 ASN   C CB    1 
ATOM   4893 C  CG    . ASN   D 2 109 ? -37.84400 13.96600 14.67700  1.000 13.29717 ? 108 ASN   C CG    1 
ATOM   4894 O  OD1   . ASN   D 2 109 ? -37.42200 13.51900 13.61000  1.000 14.30276 ? 108 ASN   C OD1   1 
ATOM   4895 N  ND2   . ASN   D 2 109 ? -37.23500 13.76400 15.83900  1.000 14.40550 ? 108 ASN   C ND2   1 
ATOM   4896 N  N     . GLY   D 2 110 ? -40.77100 17.12900 13.01100  1.000 12.46211 ? 109 GLY   C N     1 
ATOM   4897 C  CA    . GLY   D 2 110 ? -42.07000 17.77400 12.93400  1.000 13.25575 ? 109 GLY   C CA    1 
ATOM   4898 C  C     . GLY   D 2 110 ? -43.04000 16.89800 12.17600  1.000 12.18596 ? 109 GLY   C C     1 
ATOM   4899 O  O     . GLY   D 2 110 ? -43.54200 15.91600 12.72700  1.000 13.65682 ? 109 GLY   C O     1 
ATOM   4900 N  N     . SER   D 2 111 ? -43.26200 17.21400 10.90200  1.000 12.44622 ? 110 SER   C N     1 
ATOM   4901 C  CA    . SER   D 2 111 ? -44.05500 16.37400 10.01800  1.000 11.79080 ? 110 SER   C CA    1 
ATOM   4902 C  C     . SER   D 2 111 ? -43.31400 15.96500 8.74900   1.000 11.90685 ? 110 SER   C C     1 
ATOM   4903 O  O     . SER   D 2 111 ? -43.70800 14.98000 8.12200   1.000 13.13338 ? 110 SER   C O     1 
ATOM   4904 C  CB    . SER   D 2 111 ? -45.35900 17.07600 9.61600   1.000 13.62570 ? 110 SER   C CB    1 
ATOM   4905 O  OG    . SER   D 2 111 ? -45.07200 18.33700 9.06200   1.000 13.50568 ? 110 SER   C OG    1 
ATOM   4906 N  N     . GLN   D 2 112 ? -42.24700 16.66100 8.35800   1.000 11.81667 ? 111 GLN   C N     1 
ATOM   4907 C  CA    . GLN   D 2 112 ? -41.58300 16.28400 7.12000   1.000 12.08515 ? 111 GLN   C CA    1 
ATOM   4908 C  C     . GLN   D 2 112 ? -40.92200 14.91100 7.26400   1.000 11.26783 ? 111 GLN   C C     1 
ATOM   4909 O  O     . GLN   D 2 112 ? -40.39800 14.55800 8.32700   1.000 12.25394 ? 111 GLN   C O     1 
ATOM   4910 C  CB    . GLN   D 2 112 ? -40.56800 17.34300 6.67100   1.000 12.02629 ? 111 GLN   C CB    1 
ATOM   4911 C  CG    . GLN   D 2 112 ? -41.21300 18.61700 6.18200   1.000 13.06263 ? 111 GLN   C CG    1 
ATOM   4912 C  CD    . GLN   D 2 112 ? -40.20500 19.49500 5.47000   1.000 11.95278 ? 111 GLN   C CD    1 
ATOM   4913 O  OE1   . GLN   D 2 112 ? -39.43400 19.02100 4.62700   1.000 14.37046 ? 111 GLN   C OE1   1 
ATOM   4914 N  NE2   . GLN   D 2 112 ? -40.21700 20.78400 5.79400   1.000 13.40474 ? 111 GLN   C NE2   1 
ATOM   4915 N  N     . PHE   D 2 113 ? -40.93000 14.14900 6.16700   1.000 11.31943 ? 112 PHE   C N     1 
ATOM   4916 C  CA    . PHE   D 2 113 ? -40.48400 12.76900 6.13600   1.000 11.15446 ? 112 PHE   C CA    1 
ATOM   4917 C  C     . PHE   D 2 113 ? -39.88400 12.55400 4.76000   1.000 11.89046 ? 112 PHE   C C     1 
ATOM   4918 O  O     . PHE   D 2 113 ? -40.09400 13.34900 3.83800   1.000 11.12574 ? 112 PHE   C O     1 
ATOM   4919 C  CB    . PHE   D 2 113 ? -41.68300 11.83400 6.33100   1.000 12.56118 ? 112 PHE   C CB    1 
ATOM   4920 C  CG    . PHE   D 2 113 ? -42.70200 11.97600 5.25200   1.000 13.46466 ? 112 PHE   C CG    1 
ATOM   4921 C  CD1   . PHE   D 2 113 ? -42.61300 11.20500 4.09400   1.000 13.80496 ? 112 PHE   C CD1   1 
ATOM   4922 C  CD2   . PHE   D 2 113 ? -43.71300 12.92300 5.35200   1.000 13.62145 ? 112 PHE   C CD2   1 
ATOM   4923 C  CE1   . PHE   D 2 113 ? -43.51800 11.36600 3.06700   1.000 14.74805 ? 112 PHE   C CE1   1 
ATOM   4924 C  CE2   . PHE   D 2 113 ? -44.65000 13.07000 4.32300   1.000 14.28202 ? 112 PHE   C CE2   1 
ATOM   4925 C  CZ    . PHE   D 2 113 ? -44.54800 12.30200 3.18400   1.000 15.65981 ? 112 PHE   C CZ    1 
ATOM   4926 N  N     . PHE   D 2 114 ? -39.22400 11.41900 4.59900   1.000 11.56121 ? 113 PHE   C N     1 
ATOM   4927 C  CA    . PHE   D 2 114 ? -38.75000 11.04000 3.28100   1.000 11.91162 ? 113 PHE   C CA    1 
ATOM   4928 C  C     . PHE   D 2 114 ? -38.89200 9.54500  3.09300   1.000 10.81699 ? 113 PHE   C C     1 
ATOM   4929 O  O     . PHE   D 2 114 ? -38.82600 8.76200  4.04600   1.000 12.75966 ? 113 PHE   C O     1 
ATOM   4930 C  CB    . PHE   D 2 114 ? -37.31300 11.49300 2.96900   1.000 12.52613 ? 113 PHE   C CB    1 
ATOM   4931 C  CG    . PHE   D 2 114 ? -36.26100 10.96400 3.91800   1.000 12.83733 ? 113 PHE   C CG    1 
ATOM   4932 C  CD1   . PHE   D 2 114 ? -36.11900 11.49200 5.20900   1.000 12.28318 ? 113 PHE   C CD1   1 
ATOM   4933 C  CD2   . PHE   D 2 114 ? -35.37600 9.96800  3.50500   1.000 13.58428 ? 113 PHE   C CD2   1 
ATOM   4934 C  CE1   . PHE   D 2 114 ? -35.13300 11.01700 6.07000   1.000 12.86228 ? 113 PHE   C CE1   1 
ATOM   4935 C  CE2   . PHE   D 2 114 ? -34.37800 9.47800  4.36500   1.000 13.60606 ? 113 PHE   C CE2   1 
ATOM   4936 C  CZ    . PHE   D 2 114 ? -34.26000 10.00700 5.63800   1.000 14.33477 ? 113 PHE   C CZ    1 
ATOM   4937 N  N     . ILE   D 2 115 ? -39.08100 9.17200  1.83300   1.000 12.19806 ? 114 ILE   C N     1 
ATOM   4938 C  CA    . ILE   D 2 115 ? -39.12300 7.78300  1.40500   1.000 13.16957 ? 114 ILE   C CA    1 
ATOM   4939 C  C     . ILE   D 2 115 ? -37.85200 7.52000  0.61800   1.000 13.23894 ? 114 ILE   C C     1 
ATOM   4940 O  O     . ILE   D 2 115 ? -37.61100 8.15900  -0.41300  1.000 14.39367 ? 114 ILE   C O     1 
ATOM   4941 C  CB    . ILE   D 2 115 ? -40.35500 7.49800  0.52900   1.000 13.24042 ? 114 ILE   C CB    1 
ATOM   4942 C  CG1   . ILE   D 2 115 ? -41.65500 7.96600  1.18900   1.000 15.33048 ? 114 ILE   C CG1   1 
ATOM   4943 C  CG2   . ILE   D 2 115 ? -40.41200 6.02300  0.17400   1.000 14.63236 ? 114 ILE   C CG2   1 
ATOM   4944 C  CD1   . ILE   D 2 115 ? -42.85800 8.01900  0.22900   1.000 15.62552 ? 114 ILE   C CD1   1 
ATOM   4945 N  N     . CYS   D 2 116 ? -37.04100 6.58600  1.09700   1.000 14.17936 ? 115 CYS   C N     1 
ATOM   4946 C  CA    . CYS   D 2 116 ? -35.80700 6.25800  0.40100   1.000 15.20744 ? 115 CYS   C CA    1 
ATOM   4947 C  C     . CYS   D 2 116 ? -36.10100 5.51400  -0.88700  1.000 16.16961 ? 115 CYS   C C     1 
ATOM   4948 O  O     . CYS   D 2 116 ? -36.99000 4.66300  -0.94700  1.000 17.33974 ? 115 CYS   C O     1 
ATOM   4949 C  CB    . CYS   D 2 116 ? -34.92700 5.37100  1.27600   1.000 15.24930 ? 115 CYS   C CB    1 
ATOM   4950 S  SG    . CYS   D 2 116 ? -34.44000 6.17500  2.79200   1.000 17.38356 ? 115 CYS   C SG    1 
ATOM   4951 N  N     . THR   D 2 117 ? -35.32500 5.82400  -1.92200  1.000 16.76728 ? 116 THR   C N     1 
ATOM   4952 C  CA    . THR   D 2 117 ? -35.35500 5.05900  -3.15300  1.000 19.36265 ? 116 THR   C CA    1 
ATOM   4953 C  C     . THR   D 2 117 ? -34.06800 4.27700  -3.34300  1.000 19.21064 ? 116 THR   C C     1 
ATOM   4954 O  O     . THR   D 2 117 ? -33.90500 3.59000  -4.36100  1.000 22.55455 ? 116 THR   C O     1 
ATOM   4955 C  CB    . THR   D 2 117 ? -35.63800 5.97200  -4.35300  1.000 19.45160 ? 116 THR   C CB    1 
ATOM   4956 O  OG1   . THR   D 2 117 ? -34.66400 7.01900  -4.41700  1.000 20.52788 ? 116 THR   C OG1   1 
ATOM   4957 C  CG2   . THR   D 2 117 ? -37.03800 6.59500  -4.23000  1.000 19.98511 ? 116 THR   C CG2   1 
ATOM   4958 N  N     . ALA   D 2 118 ? -33.17800 4.33800  -2.35900  1.000 18.63395 ? 117 ALA   C N     1 
ATOM   4959 C  CA    . ALA   D 2 118 ? -31.92400 3.60600  -2.34400  1.000 19.73082 ? 117 ALA   C CA    1 
ATOM   4960 C  C     . ALA   D 2 118 ? -31.51700 3.48800  -0.88400  1.000 18.57957 ? 117 ALA   C C     1 
ATOM   4961 O  O     . ALA   D 2 118 ? -32.10900 4.12600  -0.00700  1.000 19.76087 ? 117 ALA   C O     1 
ATOM   4962 C  CB    . ALA   D 2 118 ? -30.85600 4.32900  -3.16900  1.000 21.65412 ? 117 ALA   C CB    1 
ATOM   4963 N  N     . LYS   D 2 119 ? -30.50900 2.65700  -0.62600  1.000 20.46134 ? 118 LYS   C N     1 
ATOM   4964 C  CA    . LYS   D 2 119 ? -29.92900 2.60000  0.70800   1.000 20.42931 ? 118 LYS   C CA    1 
ATOM   4965 C  C     . LYS   D 2 119 ? -29.26000 3.93700  1.01200   1.000 20.95575 ? 118 LYS   C C     1 
ATOM   4966 O  O     . LYS   D 2 119 ? -28.49500 4.46100  0.19300   1.000 24.04056 ? 118 LYS   C O     1 
ATOM   4967 C  CB    . LYS   D 2 119 ? -28.90700 1.46100  0.78800   1.000 24.57631 ? 118 LYS   C CB    1 
ATOM   4968 C  CG    . LYS   D 2 119 ? -28.30100 1.25900  2.16600   1.000 28.00902 ? 118 LYS   C CG    1 
ATOM   4969 C  CD    . LYS   D 2 119 ? -27.47200 -0.01600 2.21000   1.000 32.40621 ? 118 LYS   C CD    1 
ATOM   4970 C  CE    . LYS   D 2 119 ? -26.85400 -0.21200 3.58400   1.000 35.75623 ? 118 LYS   C CE    1 
ATOM   4971 N  NZ    . LYS   D 2 119 ? -26.07300 -1.47700 3.67500   1.000 36.87114 ? 118 LYS   C NZ    1 
ATOM   4972 N  N     . THR   D 2 120 ? -29.55400 4.50400  2.18200   1.000 19.58298 ? 119 THR   C N     1 
ATOM   4973 C  CA    . THR   D 2 120 ? -28.99900 5.80100  2.57500   1.000 18.37624 ? 119 THR   C CA    1 
ATOM   4974 C  C     . THR   D 2 120 ? -28.37300 5.67400  3.96500   1.000 17.44632 ? 119 THR   C C     1 
ATOM   4975 O  O     . THR   D 2 120 ? -28.75200 6.36700  4.91100   1.000 17.28653 ? 119 THR   C O     1 
ATOM   4976 C  CB    . THR   D 2 120 ? -30.03700 6.93600  2.52200   1.000 18.98458 ? 119 THR   C CB    1 
ATOM   4977 O  OG1   . THR   D 2 120 ? -31.07600 6.68500  3.47500   1.000 18.29728 ? 119 THR   C OG1   1 
ATOM   4978 C  CG2   . THR   D 2 120 ? -30.65500 7.05400  1.12800   1.000 19.38065 ? 119 THR   C CG2   1 
ATOM   4979 N  N     . GLU   D 2 121 ? -27.39100 4.77000  4.08500   1.000 20.16936 ? 120 GLU   C N     1 
ATOM   4980 C  CA    . GLU   D 2 121 ? -26.88700 4.39000  5.40200   1.000 21.63671 ? 120 GLU   C CA    1 
ATOM   4981 C  C     . GLU   D 2 121 ? -26.18000 5.53700  6.11200   1.000 20.21380 ? 120 GLU   C C     1 
ATOM   4982 O  O     . GLU   D 2 121 ? -26.06700 5.50700  7.34200   1.000 21.32133 ? 120 GLU   C O     1 
ATOM   4983 C  CB    . GLU   D 2 121 ? -25.94100 3.19500  5.28300   1.000 26.39610 ? 120 GLU   C CB    1 
ATOM   4984 C  CG    . GLU   D 2 121 ? -24.57000 3.54500  4.74600   1.000 31.26099 ? 120 GLU   C CG    1 
ATOM   4985 C  CD    . GLU   D 2 121 ? -24.51400 3.67500  3.22700   1.000 37.15154 ? 120 GLU   C CD    1 
ATOM   4986 O  OE1   . GLU   D 2 121 ? -25.52300 3.39000  2.54000   1.000 35.60331 ? 120 GLU   C OE1   1 
ATOM   4987 O  OE2   . GLU   D 2 121 ? -23.44400 4.06800  2.72000   1.000 39.77553 ? 120 GLU   C OE2   1 
ATOM   4988 N  N     . TRP   D 2 122 ? -25.71800 6.55300  5.37300   1.000 19.28599 ? 121 TRP   C N     1 
ATOM   4989 C  CA    . TRP   D 2 122 ? -25.06400 7.68700  6.00900   1.000 18.77813 ? 121 TRP   C CA    1 
ATOM   4990 C  C     . TRP   D 2 122 ? -26.01200 8.51000  6.87500   1.000 19.52027 ? 121 TRP   C C     1 
ATOM   4991 O  O     . TRP   D 2 122 ? -25.54200 9.33100  7.66800   1.000 20.55272 ? 121 TRP   C O     1 
ATOM   4992 C  CB    . TRP   D 2 122 ? -24.35100 8.56000  4.96500   1.000 18.95682 ? 121 TRP   C CB    1 
ATOM   4993 C  CG    . TRP   D 2 122 ? -25.29900 9.14600  3.96900   1.000 20.05103 ? 121 TRP   C CG    1 
ATOM   4994 C  CD1   . TRP   D 2 122 ? -25.93500 10.35000 4.05700   1.000 20.75080 ? 121 TRP   C CD1   1 
ATOM   4995 C  CD2   . TRP   D 2 122 ? -25.75000 8.54000  2.75100   1.000 19.74249 ? 121 TRP   C CD2   1 
ATOM   4996 N  NE1   . TRP   D 2 122 ? -26.74800 10.53600 2.96400   1.000 21.00273 ? 121 TRP   C NE1   1 
ATOM   4997 C  CE2   . TRP   D 2 122 ? -26.64400 9.44500  2.14300   1.000 20.61321 ? 121 TRP   C CE2   1 
ATOM   4998 C  CE3   . TRP   D 2 122 ? -25.46600 7.33000  2.10500   1.000 21.33492 ? 121 TRP   C CE3   1 
ATOM   4999 C  CZ2   . TRP   D 2 122 ? -27.26900 9.17600  0.92800   1.000 18.81353 ? 121 TRP   C CZ2   1 
ATOM   5000 C  CZ3   . TRP   D 2 122 ? -26.08500 7.06300  0.89900   1.000 22.06251 ? 121 TRP   C CZ3   1 
ATOM   5001 C  CH2   . TRP   D 2 122 ? -26.97900 7.98400  0.32100   1.000 20.01081 ? 121 TRP   C CH2   1 
ATOM   5002 N  N     . LEU   D 2 123 ? -27.32500 8.30900  6.75000   1.000 17.46771 ? 122 LEU   C N     1 
ATOM   5003 C  CA    . LEU   D 2 123 ? -28.30300 8.97900  7.59600   1.000 16.77581 ? 122 LEU   C CA    1 
ATOM   5004 C  C     . LEU   D 2 123 ? -28.56500 8.24300  8.91100   1.000 17.29905 ? 122 LEU   C C     1 
ATOM   5005 O  O     . LEU   D 2 123 ? -29.24700 8.79400  9.78700   1.000 16.59004 ? 122 LEU   C O     1 
ATOM   5006 C  CB    . LEU   D 2 123 ? -29.61200 9.15400  6.80600   1.000 15.74888 ? 122 LEU   C CB    1 
ATOM   5007 C  CG    . LEU   D 2 123 ? -29.45500 9.95400  5.50400   1.000 16.26136 ? 122 LEU   C CG    1 
ATOM   5008 C  CD1   . LEU   D 2 123 ? -30.77800 10.00900 4.73600   1.000 18.70079 ? 122 LEU   C CD1   1 
ATOM   5009 C  CD2   . LEU   D 2 123 ? -28.93700 11.34600 5.78500   1.000 17.61062 ? 122 LEU   C CD2   1 
ATOM   5010 N  N     . ASP   D 2 124 ? -28.04400 7.02300  9.07000   1.000 16.65972 ? 123 ASP   C N     1 
ATOM   5011 C  CA    . ASP   D 2 124 ? -28.25600 6.27400  10.30600  1.000 17.26674 ? 123 ASP   C CA    1 
ATOM   5012 C  C     . ASP   D 2 124 ? -27.72300 7.06600  11.49200  1.000 17.19684 ? 123 ASP   C C     1 
ATOM   5013 O  O     . ASP   D 2 124 ? -26.61700 7.61500  11.44600  1.000 18.76737 ? 123 ASP   C O     1 
ATOM   5014 C  CB    . ASP   D 2 124 ? -27.50100 4.94400  10.25200  1.000 18.07891 ? 123 ASP   C CB    1 
ATOM   5015 C  CG    . ASP   D 2 124 ? -28.10000 3.94300  9.27400   1.000 18.43054 ? 123 ASP   C CG    1 
ATOM   5016 O  OD1   . ASP   D 2 124 ? -29.21000 4.17500  8.73200   1.000 17.95139 ? 123 ASP   C OD1   1 
ATOM   5017 O  OD2   . ASP   D 2 124 ? -27.46300 2.88600  9.06900   1.000 21.74344 ? 123 ASP   C OD2   1 
ATOM   5018 N  N     . GLY   D 2 125 ? -28.50600 7.10800  12.57000  1.000 17.39252 ? 124 GLY   C N     1 
ATOM   5019 C  CA    . GLY   D 2 125 ? -28.11600 7.83200  13.76300  1.000 15.38550 ? 124 GLY   C CA    1 
ATOM   5020 C  C     . GLY   D 2 125 ? -28.40800 9.31300  13.73600  1.000 16.45066 ? 124 GLY   C C     1 
ATOM   5021 O  O     . GLY   D 2 125 ? -28.20700 9.98700  14.75700  1.000 19.47630 ? 124 GLY   C O     1 
ATOM   5022 N  N     . LYS   D 2 126 ? -28.91800 9.83900  12.61600  1.000 15.23013 ? 125 LYS   C N     1 
ATOM   5023 C  CA    . LYS   D 2 126 ? -29.28700 11.23800 12.48700  1.000 17.81584 ? 125 LYS   C CA    1 
ATOM   5024 C  C     . LYS   D 2 126 ? -30.75700 11.43600 12.15400  1.000 15.78061 ? 125 LYS   C C     1 
ATOM   5025 O  O     . LYS   D 2 126 ? -31.33200 12.45300 12.54400  1.000 16.83335 ? 125 LYS   C O     1 
ATOM   5026 C  CB    . LYS   D 2 126 ? -28.42600 11.91300 11.40700  1.000 20.71939 ? 125 LYS   C CB    1 
ATOM   5027 C  CG    . LYS   D 2 126 ? -26.93000 11.89900 11.71800  1.000 28.24056 ? 125 LYS   C CG    1 
ATOM   5028 C  CD    . LYS   D 2 126 ? -26.58200 12.87900 12.83300  1.000 36.54263 ? 125 LYS   C CD    1 
ATOM   5029 C  CE    . LYS   D 2 126 ? -25.08600 12.87200 13.15200  1.000 42.29727 ? 125 LYS   C CE    1 
ATOM   5030 N  NZ    . LYS   D 2 126 ? -24.24300 13.28800 11.99100  1.000 45.09180 ? 125 LYS   C NZ    1 
ATOM   5031 N  N     . HIS   D 2 127 ? -31.38200 10.47900 11.47300  1.000 13.18419 ? 126 HIS   C N     1 
ATOM   5032 C  CA    . HIS   D 2 127 ? -32.79100 10.54300 11.11800  1.000 14.00877 ? 126 HIS   C CA    1 
ATOM   5033 C  C     . HIS   D 2 127 ? -33.46600 9.29900  11.66000  1.000 13.05136 ? 126 HIS   C C     1 
ATOM   5034 O  O     . HIS   D 2 127 ? -32.93700 8.19100  11.51400  1.000 13.87813 ? 126 HIS   C O     1 
ATOM   5035 C  CB    . HIS   D 2 127 ? -32.95000 10.59600 9.59500   1.000 14.41440 ? 126 HIS   C CB    1 
ATOM   5036 C  CG    . HIS   D 2 127 ? -32.40200 11.85500 9.00600   1.000 14.05318 ? 126 HIS   C CG    1 
ATOM   5037 N  ND1   . HIS   D 2 127 ? -33.18400 12.95600 8.72400   1.000 12.74082 ? 126 HIS   C ND1   1 
ATOM   5038 C  CD2   . HIS   D 2 127 ? -31.12700 12.21900 8.72900   1.000 15.89170 ? 126 HIS   C CD2   1 
ATOM   5039 C  CE1   . HIS   D 2 127 ? -32.41300 13.93400 8.27700   1.000 14.05698 ? 126 HIS   C CE1   1 
ATOM   5040 N  NE2   . HIS   D 2 127 ? -31.16100 13.51200 8.27600   1.000 16.00683 ? 126 HIS   C NE2   1 
ATOM   5041 N  N     . VAL   D 2 128 ? -34.63100 9.47800  12.28500  1.000 13.05382 ? 127 VAL   C N     1 
ATOM   5042 C  CA    . VAL   D 2 128 ? -35.35800 8.37200  12.90300  1.000 13.17898 ? 127 VAL   C CA    1 
ATOM   5043 C  C     . VAL   D 2 128 ? -36.15600 7.62100  11.83700  1.000 11.62110 ? 127 VAL   C C     1 
ATOM   5044 O  O     . VAL   D 2 128 ? -37.08500 8.18200  11.23700  1.000 12.61620 ? 127 VAL   C O     1 
ATOM   5045 C  CB    . VAL   D 2 128 ? -36.26500 8.87100  14.03400  1.000 12.20164 ? 127 VAL   C CB    1 
ATOM   5046 C  CG1   . VAL   D 2 128 ? -37.10500 7.70900  14.57500  1.000 12.67151 ? 127 VAL   C CG1   1 
ATOM   5047 C  CG2   . VAL   D 2 128 ? -35.42000 9.50000  15.13000  1.000 13.02421 ? 127 VAL   C CG2   1 
ATOM   5048 N  N     . VAL   D 2 129 ? -35.79900 6.35200  11.61600  1.000 12.38639 ? 128 VAL   C N     1 
ATOM   5049 C  CA    . VAL   D 2 129 ? -36.54700 5.45100  10.73800  1.000 11.98743 ? 128 VAL   C CA    1 
ATOM   5050 C  C     . VAL   D 2 129 ? -37.73600 4.90200  11.50100  1.000 11.65281 ? 128 VAL   C C     1 
ATOM   5051 O  O     . VAL   D 2 129 ? -37.60200 4.44200  12.64800  1.000 13.59343 ? 128 VAL   C O     1 
ATOM   5052 C  CB    . VAL   D 2 129 ? -35.64600 4.29500  10.27000  1.000 13.15109 ? 128 VAL   C CB    1 
ATOM   5053 C  CG1   . VAL   D 2 129 ? -36.44300 3.21300  9.51400   1.000 14.09840 ? 128 VAL   C CG1   1 
ATOM   5054 C  CG2   . VAL   D 2 129 ? -34.48000 4.81300  9.42800   1.000 14.96589 ? 128 VAL   C CG2   1 
ATOM   5055 N  N     . PHE   D 2 130 ? -38.89700 4.89700  10.86200  1.000 12.40961 ? 129 PHE   C N     1 
ATOM   5056 C  CA    . PHE   D 2 130 ? -40.11700 4.52500  11.56700  1.000 13.27780 ? 129 PHE   C CA    1 
ATOM   5057 C  C     . PHE   D 2 130 ? -41.12700 3.75900  10.71900  1.000 11.99265 ? 129 PHE   C C     1 
ATOM   5058 O  O     . PHE   D 2 130 ? -42.21700 3.46200  11.21800  1.000 14.24520 ? 129 PHE   C O     1 
ATOM   5059 C  CB    . PHE   D 2 130 ? -40.78600 5.76100  12.20100  1.000 12.69753 ? 129 PHE   C CB    1 
ATOM   5060 C  CG    . PHE   D 2 130 ? -41.32500 6.73500  11.19400  1.000 11.25778 ? 129 PHE   C CG    1 
ATOM   5061 C  CD1   . PHE   D 2 130 ? -40.50600 7.70600  10.63300  1.000 12.75548 ? 129 PHE   C CD1   1 
ATOM   5062 C  CD2   . PHE   D 2 130 ? -42.64300 6.65700  10.79700  1.000 12.76553 ? 129 PHE   C CD2   1 
ATOM   5063 C  CE1   . PHE   D 2 130 ? -40.99700 8.59900  9.68200   1.000 12.42653 ? 129 PHE   C CE1   1 
ATOM   5064 C  CE2   . PHE   D 2 130 ? -43.15400 7.52500  9.84200   1.000 14.99945 ? 129 PHE   C CE2   1 
ATOM   5065 C  CZ    . PHE   D 2 130 ? -42.34000 8.51200  9.28000   1.000 15.01925 ? 129 PHE   C CZ    1 
ATOM   5066 N  N     . GLY   D 2 131 ? -40.82300 3.44200  9.46700   1.000 12.53874 ? 130 GLY   C N     1 
ATOM   5067 C  CA    . GLY   D 2 131 ? -41.75600 2.67400  8.66000   1.000 13.97034 ? 130 GLY   C CA    1 
ATOM   5068 C  C     . GLY   D 2 131 ? -41.11900 2.24900  7.35800   1.000 14.86655 ? 130 GLY   C C     1 
ATOM   5069 O  O     . GLY   D 2 131 ? -39.92700 2.45900  7.12400   1.000 13.92970 ? 130 GLY   C O     1 
ATOM   5070 N  N     . LYS   D 2 132 ? -41.93100 1.61100  6.51600   1.000 14.37360 ? 131 LYS   C N     1 
ATOM   5071 C  CA    . LYS   D 2 132 ? -41.45800 1.16000  5.21600   1.000 14.41765 ? 131 LYS   C CA    1 
ATOM   5072 C  C     . LYS   D 2 132 ? -42.65200 1.05200  4.28500   1.000 15.54102 ? 131 LYS   C C     1 
ATOM   5073 O  O     . LYS   D 2 132 ? -43.76400 0.75700  4.72200   1.000 16.49172 ? 131 LYS   C O     1 
ATOM   5074 C  CB    . LYS   D 2 132 ? -40.76800 -0.20600 5.33700   1.000 17.02352 ? 131 LYS   C CB    1 
ATOM   5075 C  CG    . LYS   D 2 132 ? -41.72400 -1.34600 5.71700   1.000 28.27949 ? 131 LYS   C CG    1 
ATOM   5076 C  CD    . LYS   D 2 132 ? -41.02100 -2.69000 5.80800   1.000 34.49058 ? 131 LYS   C CD    1 
ATOM   5077 C  CE    . LYS   D 2 132 ? -41.98200 -3.75500 6.31400   1.000 37.70995 ? 131 LYS   C CE    1 
ATOM   5078 N  NZ    . LYS   D 2 132 ? -41.30800 -5.06800 6.60600   1.000 43.30321 ? 131 LYS   C NZ    1 
ATOM   5079 N  N     . VAL   D 2 133 ? -42.40600 1.27400  2.99500   1.000 14.77056 ? 132 VAL   C N     1 
ATOM   5080 C  CA    . VAL   D 2 133 ? -43.43800 1.05600  1.98800   1.000 15.42449 ? 132 VAL   C CA    1 
ATOM   5081 C  C     . VAL   D 2 133 ? -43.86000 -0.40400 1.99100   1.000 16.18646 ? 132 VAL   C C     1 
ATOM   5082 O  O     . VAL   D 2 133 ? -43.01900 -1.31900 1.98900   1.000 17.88256 ? 132 VAL   C O     1 
ATOM   5083 C  CB    . VAL   D 2 133 ? -42.92300 1.47100  0.60300   1.000 15.13451 ? 132 VAL   C CB    1 
ATOM   5084 C  CG1   . VAL   D 2 133 ? -43.89300 1.03500  -0.50100  1.000 16.03580 ? 132 VAL   C CG1   1 
ATOM   5085 C  CG2   . VAL   D 2 133 ? -42.66700 2.97300  0.54400   1.000 16.14045 ? 132 VAL   C CG2   1 
ATOM   5086 N  N     . LYS   D 2 134 ? -45.17200 -0.62500 1.98900   1.000 18.22914 ? 133 LYS   C N     1 
ATOM   5087 C  CA    . LYS   D 2 134 ? -45.76300 -1.95500 1.93000   1.000 20.74194 ? 133 LYS   C CA    1 
ATOM   5088 C  C     . LYS   D 2 134 ? -46.14700 -2.24100 0.48600   1.000 22.18290 ? 133 LYS   C C     1 
ATOM   5089 O  O     . LYS   D 2 134 ? -45.51600 -3.06400 -0.18000  1.000 29.16166 ? 133 LYS   C O     1 
ATOM   5090 C  CB    . LYS   D 2 134 ? -47.00300 -1.97300 2.82600   1.000 26.33359 ? 133 LYS   C CB    1 
ATOM   5091 C  CG    . LYS   D 2 134 ? -47.65100 -3.32000 3.05300   1.000 34.38816 ? 133 LYS   C CG    1 
ATOM   5092 C  CD    . LYS   D 2 134 ? -48.91000 -3.14800 3.89500   1.000 38.40000 ? 133 LYS   C CD    1 
ATOM   5093 C  CE    . LYS   D 2 134 ? -49.54100 -4.47700 4.26400   1.000 43.26446 ? 133 LYS   C CE    1 
ATOM   5094 N  NZ    . LYS   D 2 134 ? -48.73600 -5.21400 5.27800   1.000 46.98306 ? 133 LYS   C NZ    1 
ATOM   5095 N  N     . GLU   D 2 135 ? -47.17600 -1.56200 -0.00500  1.000 21.50445 ? 134 GLU   C N     1 
ATOM   5096 C  CA    . GLU   D 2 135 ? -47.59800 -1.65400 -1.39200  1.000 23.01669 ? 134 GLU   C CA    1 
ATOM   5097 C  C     . GLU   D 2 135 ? -47.30500 -0.34100 -2.10800  1.000 19.43880 ? 134 GLU   C C     1 
ATOM   5098 O  O     . GLU   D 2 135 ? -47.31700 0.73600  -1.50200  1.000 18.83431 ? 134 GLU   C O     1 
ATOM   5099 C  CB    . GLU   D 2 135 ? -49.09700 -1.94700 -1.47800  1.000 32.24771 ? 134 GLU   C CB    1 
ATOM   5100 C  CG    . GLU   D 2 135 ? -49.48800 -3.30600 -0.90700  1.000 43.30343 ? 134 GLU   C CG    1 
ATOM   5101 C  CD    . GLU   D 2 135 ? -50.97700 -3.57000 -1.00100  1.000 55.18121 ? 134 GLU   C CD    1 
ATOM   5102 O  OE1   . GLU   D 2 135 ? -51.74200 -2.60500 -1.21500  1.000 59.83677 ? 134 GLU   C OE1   1 
ATOM   5103 O  OE2   . GLU   D 2 135 ? -51.38200 -4.74200 -0.85900  1.000 59.63608 ? 134 GLU   C OE2   1 
ATOM   5104 N  N     . GLY   D 2 136 ? -47.04700 -0.43400 -3.40900  1.000 18.87456 ? 135 GLY   C N     1 
ATOM   5105 C  CA    . GLY   D 2 136 ? -46.92800 0.75700  -4.22500  1.000 19.09379 ? 135 GLY   C CA    1 
ATOM   5106 C  C     . GLY   D 2 136 ? -45.53400 1.30600  -4.40400  1.000 18.61455 ? 135 GLY   C C     1 
ATOM   5107 O  O     . GLY   D 2 136 ? -45.38500 2.49400  -4.71100  1.000 18.59017 ? 135 GLY   C O     1 
ATOM   5108 N  N     . MET   D 2 137 ? -44.49500 0.48900  -4.24600  1.000 18.33339 ? 136 MET   C N     1 
ATOM   5109 C  CA    . MET   D 2 137 ? -43.15900 0.99200  -4.53600  1.000 20.73589 ? 136 MET   C CA    1 
ATOM   5110 C  C     . MET   D 2 137 ? -43.03800 1.43000  -5.99300  1.000 21.31348 ? 136 MET   C C     1 
ATOM   5111 O  O     . MET   D 2 137 ? -42.27400 2.35100  -6.30300  1.000 22.20026 ? 136 MET   C O     1 
ATOM   5112 C  CB    . MET   D 2 137 ? -42.10000 -0.04300 -4.17100  1.000 22.79211 ? 136 MET   C CB    1 
ATOM   5113 C  CG    . MET   D 2 137 ? -40.72500 0.55600  -4.05400  1.000 25.13513 ? 136 MET   C CG    1 
ATOM   5114 S  SD    . MET   D 2 137 ? -40.57900 1.76500  -2.71400  1.000 24.64366 ? 136 MET   C SD    1 
ATOM   5115 C  CE    . MET   D 2 137 ? -39.09600 2.61100  -3.26300  1.000 25.79537 ? 136 MET   C CE    1 
ATOM   5116 N  N     . ASN   D 2 138 ? -43.80700 0.80500  -6.89000  1.000 21.30229 ? 137 ASN   C N     1 
ATOM   5117 C  CA    . ASN   D 2 138 ? -43.83600 1.24800  -8.28100  1.000 20.14170 ? 137 ASN   C CA    1 
ATOM   5118 C  C     . ASN   D 2 138 ? -44.34800 2.67900  -8.40300  1.000 18.68572 ? 137 ASN   C C     1 
ATOM   5119 O  O     . ASN   D 2 138 ? -43.92600 3.41900  -9.30200  1.000 20.61534 ? 137 ASN   C O     1 
ATOM   5120 C  CB    . ASN   D 2 138 ? -44.69200 0.30000  -9.12300  1.000 23.50344 ? 137 ASN   C CB    1 
ATOM   5121 C  CG    . ASN   D 2 138 ? -46.15700 0.31800  -8.71400  1.000 25.26401 ? 137 ASN   C CG    1 
ATOM   5122 O  OD1   . ASN   D 2 138 ? -46.48200 0.15700  -7.54100  1.000 30.11418 ? 137 ASN   C OD1   1 
ATOM   5123 N  ND2   . ASN   D 2 138 ? -47.04400 0.52600  -9.67900  1.000 29.92547 ? 137 ASN   C ND2   1 
ATOM   5124 N  N     . ILE   D 2 139 ? -45.26600 3.08600  -7.52700  1.000 17.85173 ? 138 ILE   C N     1 
ATOM   5125 C  CA    . ILE   D 2 139 ? -45.72900 4.47000  -7.54100  1.000 18.32907 ? 138 ILE   C CA    1 
ATOM   5126 C  C     . ILE   D 2 139 ? -44.63100 5.40300  -7.06000  1.000 18.09601 ? 138 ILE   C C     1 
ATOM   5127 O  O     . ILE   D 2 139 ? -44.45100 6.49600  -7.60500  1.000 16.62445 ? 138 ILE   C O     1 
ATOM   5128 C  CB    . ILE   D 2 139 ? -47.01800 4.62800  -6.71700  1.000 17.32618 ? 138 ILE   C CB    1 
ATOM   5129 C  CG1   . ILE   D 2 139 ? -48.08400 3.65100  -7.22300  1.000 18.93680 ? 138 ILE   C CG1   1 
ATOM   5130 C  CG2   . ILE   D 2 139 ? -47.53100 6.07100  -6.77200  1.000 19.62790 ? 138 ILE   C CG2   1 
ATOM   5131 C  CD1   . ILE   D 2 139 ? -48.43300 3.83100  -8.69400  1.000 20.30512 ? 138 ILE   C CD1   1 
ATOM   5132 N  N     . VAL   D 2 140 ? -43.88900 4.99300  -6.02700  1.000 17.63685 ? 139 VAL   C N     1 
ATOM   5133 C  CA    . VAL   D 2 140 ? -42.75700 5.80000  -5.57600  1.000 17.54922 ? 139 VAL   C CA    1 
ATOM   5134 C  C     . VAL   D 2 140 ? -41.73900 5.95900  -6.69700  1.000 18.34677 ? 139 VAL   C C     1 
ATOM   5135 O  O     . VAL   D 2 140 ? -41.19200 7.04900  -6.91300  1.000 18.35710 ? 139 VAL   C O     1 
ATOM   5136 C  CB    . VAL   D 2 140 ? -42.12800 5.19700  -4.30600  1.000 17.39254 ? 139 VAL   C CB    1 
ATOM   5137 C  CG1   . VAL   D 2 140 ? -40.90900 6.03000  -3.85700  1.000 19.12537 ? 139 VAL   C CG1   1 
ATOM   5138 C  CG2   . VAL   D 2 140 ? -43.15600 5.13600  -3.18500  1.000 17.94256 ? 139 VAL   C CG2   1 
ATOM   5139 N  N     . GLU   D 2 141 ? -41.46700 4.87300  -7.42800  1.000 18.81236 ? 140 GLU   C N     1 
ATOM   5140 C  CA    . GLU   D 2 141 ? -40.53500 4.96300  -8.54700  1.000 20.10596 ? 140 GLU   C CA    1 
ATOM   5141 C  C     . GLU   D 2 141 ? -41.05300 5.91300  -9.62400  1.000 19.51650 ? 140 GLU   C C     1 
ATOM   5142 O  O     . GLU   D 2 141 ? -40.27100 6.64500  -10.24500 1.000 21.66269 ? 140 GLU   C O     1 
ATOM   5143 C  CB    . GLU   D 2 141 ? -40.25500 3.56500  -9.10600  1.000 23.72995 ? 140 GLU   C CB    1 
ATOM   5144 C  CG    . GLU   D 2 141 ? -39.52700 2.66900  -8.10200  1.000 28.42147 ? 140 GLU   C CG    1 
ATOM   5145 C  CD    . GLU   D 2 141 ? -39.52100 1.19300  -8.48200  1.000 31.75767 ? 140 GLU   C CD    1 
ATOM   5146 O  OE1   . GLU   D 2 141 ? -40.22400 0.80700  -9.44000  1.000 34.09094 ? 140 GLU   C OE1   1 
ATOM   5147 O  OE2   . GLU   D 2 141 ? -38.81000 0.40900  -7.81200  1.000 33.75851 ? 140 GLU   C OE2   1 
ATOM   5148 N  N     . ALA   D 2 142 ? -42.37100 5.91700  -9.85800  1.000 19.40936 ? 141 ALA   C N     1 
ATOM   5149 C  CA    . ALA   D 2 142 ? -42.95300 6.85700  -10.81200 1.000 19.56557 ? 141 ALA   C CA    1 
ATOM   5150 C  C     . ALA   D 2 142 ? -42.80300 8.29800  -10.33200 1.000 18.91481 ? 141 ALA   C C     1 
ATOM   5151 O  O     . ALA   D 2 142 ? -42.53600 9.20100  -11.13700 1.000 22.79076 ? 141 ALA   C O     1 
ATOM   5152 C  CB    . ALA   D 2 142 ? -44.41900 6.50200  -11.06700 1.000 21.02793 ? 141 ALA   C CB    1 
ATOM   5153 N  N     . MET   D 2 143 ? -42.96300 8.53100  -9.02400  1.000 17.41400 ? 142 MET   C N     1 
ATOM   5154 C  CA    . MET   D 2 143 ? -42.76600 9.86900  -8.46600  1.000 20.21927 ? 142 MET   C CA    1 
ATOM   5155 C  C     . MET   D 2 143 ? -41.33300 10.32600 -8.64000  1.000 21.56769 ? 142 MET   C C     1 
ATOM   5156 O  O     . MET   D 2 143 ? -41.07200 11.49900 -8.94700  1.000 19.94449 ? 142 MET   C O     1 
ATOM   5157 C  CB    . MET   D 2 143 ? -43.05300 9.84600  -6.96800  1.000 21.39263 ? 142 MET   C CB    1 
ATOM   5158 C  CG    . MET   D 2 143 ? -44.48400 9.61200  -6.61900  1.000 19.82884 ? 142 MET   C CG    1 
ATOM   5159 S  SD    . MET   D 2 143 ? -44.68800 9.13300  -4.89400  1.000 20.36534 ? 142 MET   C SD    1 
ATOM   5160 C  CE    . MET   D 2 143 ? -43.92500 10.54300 -4.10700  1.000 21.51300 ? 142 MET   C CE    1 
ATOM   5161 N  N     . GLU   D 2 144 ? -40.38700 9.41600  -8.39800  1.000 22.95462 ? 143 GLU   C N     1 
ATOM   5162 C  CA    . GLU   D 2 144 ? -38.97500 9.75200  -8.47500  1.000 24.40205 ? 143 GLU   C CA    1 
ATOM   5163 C  C     . GLU   D 2 144 ? -38.61700 10.30600 -9.84600  1.000 26.83908 ? 143 GLU   C C     1 
ATOM   5164 O  O     . GLU   D 2 144 ? -37.73400 11.16300 -9.95700  1.000 27.53980 ? 143 GLU   C O     1 
ATOM   5165 C  CB    . GLU   D 2 144 ? -38.15600 8.50100  -8.15000  1.000 24.38343 ? 143 GLU   C CB    1 
ATOM   5166 C  CG    . GLU   D 2 144 ? -36.67600 8.70200  -8.01800  1.000 28.34900 ? 143 GLU   C CG    1 
ATOM   5167 C  CD    . GLU   D 2 144 ? -35.95800 7.38300  -7.78800  1.000 29.85910 ? 143 GLU   C CD    1 
ATOM   5168 O  OE1   . GLU   D 2 144 ? -36.54100 6.33100  -8.12900  1.000 30.57899 ? 143 GLU   C OE1   1 
ATOM   5169 O  OE2   . GLU   D 2 144 ? -34.82500 7.39800  -7.26100  1.000 31.13782 ? 143 GLU   C OE2   1 
ATOM   5170 N  N     . ARG   D 2 145 ? -39.32400 9.86500  -10.89300 1.000 29.40834 ? 144 ARG   C N     1 
ATOM   5171 C  CA    . ARG   D 2 145 ? -39.06400 10.33200 -12.25100 1.000 31.50081 ? 144 ARG   C CA    1 
ATOM   5172 C  C     . ARG   D 2 145 ? -39.39600 11.80900 -12.45000 1.000 28.64396 ? 144 ARG   C C     1 
ATOM   5173 O  O     . ARG   D 2 145 ? -38.88200 12.42000 -13.38900 1.000 29.19769 ? 144 ARG   C O     1 
ATOM   5174 C  CB    . ARG   D 2 145 ? -39.82200 9.46300  -13.26400 1.000 39.15695 ? 144 ARG   C CB    1 
ATOM   5175 C  CG    . ARG   D 2 145 ? -39.52300 7.97500  -13.13800 1.000 46.36045 ? 144 ARG   C CG    1 
ATOM   5176 C  CD    . ARG   D 2 145 ? -40.23800 7.13100  -14.19800 1.000 51.88355 ? 144 ARG   C CD    1 
ATOM   5177 N  NE    . ARG   D 2 145 ? -39.98600 5.71200  -13.97800 1.000 56.68227 ? 144 ARG   C NE    1 
ATOM   5178 C  CZ    . ARG   D 2 145 ? -40.90700 4.82300  -13.62800 1.000 58.92022 ? 144 ARG   C CZ    1 
ATOM   5179 N  NH1   . ARG   D 2 145 ? -42.18500 5.14900  -13.53200 1.000 57.23404 ? 144 ARG   C NH1   1 
ATOM   5180 N  NH2   . ARG   D 2 145 ? -40.53600 3.57000  -13.38000 1.000 61.77363 ? 144 ARG   C NH2   1 
ATOM   5181 N  N     . PHE   D 2 146 ? -40.23200 12.40100 -11.60000 1.000 27.30202 ? 145 PHE   C N     1 
ATOM   5182 C  CA    . PHE   D 2 146 ? -40.54200 13.82000 -11.71200 1.000 24.74174 ? 145 PHE   C CA    1 
ATOM   5183 C  C     . PHE   D 2 146 ? -39.53100 14.70800 -11.00000 1.000 25.01948 ? 145 PHE   C C     1 
ATOM   5184 O  O     . PHE   D 2 146 ? -39.66200 15.93400 -11.04100 1.000 25.47308 ? 145 PHE   C O     1 
ATOM   5185 C  CB    . PHE   D 2 146 ? -41.94600 14.11000 -11.17500 1.000 21.74437 ? 145 PHE   C CB    1 
ATOM   5186 C  CG    . PHE   D 2 146 ? -43.04000 13.54900 -12.02900 1.000 21.99474 ? 145 PHE   C CG    1 
ATOM   5187 C  CD1   . PHE   D 2 146 ? -43.38500 14.16000 -13.22300 1.000 25.28854 ? 145 PHE   C CD1   1 
ATOM   5188 C  CD2   . PHE   D 2 146 ? -43.71000 12.39400 -11.65800 1.000 23.99322 ? 145 PHE   C CD2   1 
ATOM   5189 C  CE1   . PHE   D 2 146 ? -44.39200 13.63800 -14.02000 1.000 25.85318 ? 145 PHE   C CE1   1 
ATOM   5190 C  CE2   . PHE   D 2 146 ? -44.71900 11.87000 -12.45300 1.000 25.09773 ? 145 PHE   C CE2   1 
ATOM   5191 C  CZ    . PHE   D 2 146 ? -45.05300 12.49200 -13.63400 1.000 25.77095 ? 145 PHE   C CZ    1 
ATOM   5192 N  N     . GLY   D 2 147 ? -38.53400 14.12700 -10.34500 1.000 23.09864 ? 146 GLY   C N     1 
ATOM   5193 C  CA    . GLY   D 2 147 ? -37.56500 14.89300 -9.59600  1.000 21.22904 ? 146 GLY   C CA    1 
ATOM   5194 C  C     . GLY   D 2 147 ? -36.36500 15.30600 -10.43200 1.000 21.68234 ? 146 GLY   C C     1 
ATOM   5195 O  O     . GLY   D 2 147 ? -36.30500 15.10900 -11.64800 1.000 24.11063 ? 146 GLY   C O     1 
ATOM   5196 N  N     . SER   D 2 148 ? -35.38500 15.89100 -9.75100  1.000 21.33714 ? 147 SER   C N     1 
ATOM   5197 C  CA    . SER   D 2 148 ? -34.20500 16.40600 -10.42100 1.000 21.38804 ? 147 SER   C CA    1 
ATOM   5198 C  C     . SER   D 2 148 ? -33.07700 16.47900 -9.40500  1.000 21.05610 ? 147 SER   C C     1 
ATOM   5199 O  O     . SER   D 2 148 ? -33.26800 16.23100 -8.21000  1.000 20.82624 ? 147 SER   C O     1 
ATOM   5200 C  CB    . SER   D 2 148 ? -34.49000 17.76800 -11.05800 1.000 22.19591 ? 147 SER   C CB    1 
ATOM   5201 O  OG    . SER   D 2 148 ? -34.65600 18.76500 -10.07000 1.000 24.80309 ? 147 SER   C OG    1 
ATOM   5202 N  N     . ARG   D 2 149 ? -31.89900 16.85300 -9.89800  1.000 23.21948 ? 148 ARG   C N     1 
ATOM   5203 C  CA    . ARG   D 2 149 ? -30.70200 16.80400 -9.07200  1.000 23.00366 ? 148 ARG   C CA    1 
ATOM   5204 C  C     . ARG   D 2 149 ? -30.78500 17.75400 -7.88200  1.000 23.36530 ? 148 ARG   C C     1 
ATOM   5205 O  O     . ARG   D 2 149 ? -30.25200 17.44900 -6.80900  1.000 23.77697 ? 148 ARG   C O     1 
ATOM   5206 C  CB    . ARG   D 2 149 ? -29.48400 17.10200 -9.93700  1.000 23.46419 ? 148 ARG   C CB    1 
ATOM   5207 C  CG    . ARG   D 2 149 ? -28.19600 16.95300 -9.19600  1.000 21.40109 ? 148 ARG   C CG    1 
ATOM   5208 C  CD    . ARG   D 2 149 ? -27.02800 16.91000 -10.17300 1.000 23.66226 ? 148 ARG   C CD    1 
ATOM   5209 N  NE    . ARG   D 2 149 ? -25.75000 16.89200 -9.47300  1.000 24.01415 ? 148 ARG   C NE    1 
ATOM   5210 C  CZ    . ARG   D 2 149 ? -25.12500 17.98200 -9.04500  1.000 23.54537 ? 148 ARG   C CZ    1 
ATOM   5211 N  NH1   . ARG   D 2 149 ? -25.61700 19.18900 -9.26500  1.000 22.32767 ? 148 ARG   C NH1   1 
ATOM   5212 N  NH2   . ARG   D 2 149 ? -23.99000 17.85500 -8.36500  1.000 26.59521 ? 148 ARG   C NH2   1 
ATOM   5213 N  N     . ASN   D 2 150 ? -31.45400 18.89400 -8.03300  1.000 22.82355 ? 149 ASN   C N     1 
ATOM   5214 C  CA    . ASN   D 2 150 ? -31.61700 19.83700 -6.93500  1.000 22.94889 ? 149 ASN   C CA    1 
ATOM   5215 C  C     . ASN   D 2 150 ? -32.94400 19.66400 -6.21000  1.000 21.41508 ? 149 ASN   C C     1 
ATOM   5216 O  O     . ASN   D 2 150 ? -33.28500 20.48400 -5.35100  1.000 21.88837 ? 149 ASN   C O     1 
ATOM   5217 C  CB    . ASN   D 2 150 ? -31.41000 21.28700 -7.41300  1.000 26.54203 ? 149 ASN   C CB    1 
ATOM   5218 C  CG    . ASN   D 2 150 ? -32.60000 21.84000 -8.20100  1.000 28.26086 ? 149 ASN   C CG    1 
ATOM   5219 O  OD1   . ASN   D 2 150 ? -33.55500 21.12800 -8.51000  1.000 28.14236 ? 149 ASN   C OD1   1 
ATOM   5220 N  ND2   . ASN   D 2 150 ? -32.53200 23.12700 -8.53900  1.000 31.17056 ? 149 ASN   C ND2   1 
ATOM   5221 N  N     . GLY   D 2 151 ? -33.69800 18.61700 -6.54200  1.000 18.80293 ? 150 GLY   C N     1 
ATOM   5222 C  CA    . GLY   D 2 151 ? -34.92200 18.28400 -5.85200  1.000 18.25398 ? 150 GLY   C CA    1 
ATOM   5223 C  C     . GLY   D 2 151 ? -36.18400 18.90400 -6.41000  1.000 16.99769 ? 150 GLY   C C     1 
ATOM   5224 O  O     . GLY   D 2 151 ? -37.27700 18.47200 -6.02800  1.000 17.54947 ? 150 GLY   C O     1 
ATOM   5225 N  N     . LYS   D 2 152 ? -36.07600 19.91300 -7.28200  1.000 18.29303 ? 151 LYS   C N     1 
ATOM   5226 C  CA    . LYS   D 2 152 ? -37.26300 20.55100 -7.83500  1.000 18.91907 ? 151 LYS   C CA    1 
ATOM   5227 C  C     . LYS   D 2 152 ? -37.97400 19.57400 -8.75900  1.000 19.57622 ? 151 LYS   C C     1 
ATOM   5228 O  O     . LYS   D 2 152 ? -37.33800 18.84400 -9.52200  1.000 21.03304 ? 151 LYS   C O     1 
ATOM   5229 C  CB    . LYS   D 2 152 ? -36.86800 21.81300 -8.60200  1.000 23.07569 ? 151 LYS   C CB    1 
ATOM   5230 C  CG    . LYS   D 2 152 ? -36.34700 22.93200 -7.71600  1.000 26.93940 ? 151 LYS   C CG    1 
ATOM   5231 C  CD    . LYS   D 2 152 ? -37.46100 23.56300 -6.89700  1.000 31.41319 ? 151 LYS   C CD    1 
ATOM   5232 C  CE    . LYS   D 2 152 ? -36.97800 24.83100 -6.20200  1.000 34.32356 ? 151 LYS   C CE    1 
ATOM   5233 N  NZ    . LYS   D 2 152 ? -38.02500 25.40600 -5.31100  1.000 36.88115 ? 151 LYS   C NZ    1 
ATOM   5234 N  N     . THR   D 2 153 ? -39.29900 19.54200 -8.67700  1.000 21.25474 ? 152 THR   C N     1 
ATOM   5235 C  CA    . THR   D 2 153 ? -40.08200 18.60400 -9.46400  1.000 21.57299 ? 152 THR   C CA    1 
ATOM   5236 C  C     . THR   D 2 153 ? -40.63800 19.29300 -10.70800 1.000 23.09002 ? 152 THR   C C     1 
ATOM   5237 O  O     . THR   D 2 153 ? -40.91300 20.49500 -10.70300 1.000 24.34075 ? 152 THR   C O     1 
ATOM   5238 C  CB    . THR   D 2 153 ? -41.20000 18.00000 -8.61000  1.000 20.97071 ? 152 THR   C CB    1 
ATOM   5239 O  OG1   . THR   D 2 153 ? -42.09300 19.03300 -8.19800  1.000 22.38491 ? 152 THR   C OG1   1 
ATOM   5240 C  CG2   . THR   D 2 153 ? -40.61000 17.35500 -7.37100  1.000 21.71604 ? 152 THR   C CG2   1 
ATOM   5241 N  N     . SER   D 2 154 ? -40.78000 18.51900 -11.79200 1.000 23.17198 ? 153 SER   C N     1 
ATOM   5242 C  CA    . SER   D 2 154 ? -41.24500 19.07300 -13.06200 1.000 24.49947 ? 153 SER   C CA    1 
ATOM   5243 C  C     . SER   D 2 154 ? -42.75700 19.19200 -13.13300 1.000 25.72980 ? 153 SER   C C     1 
ATOM   5244 O  O     . SER   D 2 154 ? -43.27400 19.94600 -13.96500 1.000 27.73952 ? 153 SER   C O     1 
ATOM   5245 C  CB    . SER   D 2 154 ? -40.74200 18.22900 -14.23500 1.000 27.04381 ? 153 SER   C CB    1 
ATOM   5246 O  OG    . SER   D 2 154 ? -41.03900 16.85600 -14.04500 1.000 29.28988 ? 153 SER   C OG    1 
ATOM   5247 N  N     . LYS   D 2 155 ? -43.46600 18.43400 -12.30700 1.000 24.78890 ? 154 LYS   C N     1 
ATOM   5248 C  CA    . LYS   D 2 155 ? -44.89200 18.58700 -12.09500 1.000 24.45370 ? 154 LYS   C CA    1 
ATOM   5249 C  C     . LYS   D 2 155 ? -45.10300 18.49300 -10.59900 1.000 22.17354 ? 154 LYS   C C     1 
ATOM   5250 O  O     . LYS   D 2 155 ? -44.24000 17.98600 -9.87400  1.000 22.08670 ? 154 LYS   C O     1 
ATOM   5251 C  CB    . LYS   D 2 155 ? -45.69600 17.51400 -12.83900 1.000 24.45789 ? 154 LYS   C CB    1 
ATOM   5252 C  CG    . LYS   D 2 155 ? -45.68300 17.74800 -14.33400 1.000 24.84946 ? 154 LYS   C CG    1 
ATOM   5253 C  CD    . LYS   D 2 155 ? -46.59400 16.83900 -15.11100 1.000 28.15665 ? 154 LYS   C CD    1 
ATOM   5254 C  CE    . LYS   D 2 155 ? -46.44900 17.14100 -16.59100 1.000 33.57409 ? 154 LYS   C CE    1 
ATOM   5255 N  NZ    . LYS   D 2 155 ? -47.42700 16.40100 -17.42200 1.000 40.10550 ? 154 LYS   C NZ    1 
ATOM   5256 N  N     . LYS   D 2 156 ? -46.23600 19.00700 -10.13500 1.000 20.56825 ? 155 LYS   C N     1 
ATOM   5257 C  CA    . LYS   D 2 156 ? -46.49500 19.11100 -8.70700  1.000 19.78465 ? 155 LYS   C CA    1 
ATOM   5258 C  C     . LYS   D 2 156 ? -47.04100 17.78700 -8.19500  1.000 17.52188 ? 155 LYS   C C     1 
ATOM   5259 O  O     . LYS   D 2 156 ? -48.08900 17.32000 -8.65600  1.000 17.89013 ? 155 LYS   C O     1 
ATOM   5260 C  CB    . LYS   D 2 156 ? -47.45900 20.24900 -8.39700  1.000 22.28661 ? 155 LYS   C CB    1 
ATOM   5261 C  CG    . LYS   D 2 156 ? -47.45000 20.53500 -6.91500  1.000 22.14121 ? 155 LYS   C CG    1 
ATOM   5262 C  CD    . LYS   D 2 156 ? -48.27600 21.73500 -6.53200  1.000 24.27818 ? 155 LYS   C CD    1 
ATOM   5263 C  CE    . LYS   D 2 156 ? -48.22200 21.92800 -5.02000  1.000 26.32214 ? 155 LYS   C CE    1 
ATOM   5264 N  NZ    . LYS   D 2 156 ? -49.02100 23.09400 -4.58900  1.000 27.65888 ? 155 LYS   C NZ    1 
ATOM   5265 N  N     . ILE   D 2 157 ? -46.32700 17.18800 -7.24400  1.000 15.85455 ? 156 ILE   C N     1 
ATOM   5266 C  CA    . ILE   D 2 157 ? -46.62800 15.86200 -6.71700  1.000 14.95172 ? 156 ILE   C CA    1 
ATOM   5267 C  C     . ILE   D 2 157 ? -47.25000 16.07100 -5.34400  1.000 14.68405 ? 156 ILE   C C     1 
ATOM   5268 O  O     . ILE   D 2 157 ? -46.61000 16.63200 -4.44800  1.000 17.27768 ? 156 ILE   C O     1 
ATOM   5269 C  CB    . ILE   D 2 157 ? -45.34900 15.01200 -6.60700  1.000 15.75660 ? 156 ILE   C CB    1 
ATOM   5270 C  CG1   . ILE   D 2 157 ? -44.56500 15.00100 -7.93200  1.000 17.86799 ? 156 ILE   C CG1   1 
ATOM   5271 C  CG2   . ILE   D 2 157 ? -45.68000 13.59100 -6.10800  1.000 17.94031 ? 156 ILE   C CG2   1 
ATOM   5272 C  CD1   . ILE   D 2 157 ? -45.37700 14.53900 -9.13800  1.000 20.80988 ? 156 ILE   C CD1   1 
ATOM   5273 N  N     . THR   D 2 158 ? -48.50000 15.64000 -5.16800  1.000 15.43586 ? 157 THR   C N     1 
ATOM   5274 C  CA    . THR   D 2 158 ? -49.20700 15.88400 -3.91900  1.000 14.98109 ? 157 THR   C CA    1 
ATOM   5275 C  C     . THR   D 2 158 ? -49.79500 14.60400 -3.33600  1.000 13.91380 ? 157 THR   C C     1 
ATOM   5276 O  O     . THR   D 2 158 ? -49.98900 13.58800 -4.02000  1.000 15.45253 ? 157 THR   C O     1 
ATOM   5277 C  CB    . THR   D 2 158 ? -50.34300 16.90300 -4.07500  1.000 16.82155 ? 157 THR   C CB    1 
ATOM   5278 O  OG1   . THR   D 2 158 ? -51.26800 16.43500 -5.07100  1.000 17.41463 ? 157 THR   C OG1   1 
ATOM   5279 C  CG2   . THR   D 2 158 ? -49.79500 18.27200 -4.45700  1.000 19.09001 ? 157 THR   C CG2   1 
ATOM   5280 N  N     . ILE   D 2 159 ? -50.13100 14.71300 -2.05200  1.000 14.35884 ? 158 ILE   C N     1 
ATOM   5281 C  CA    . ILE   D 2 159 ? -50.88700 13.69100 -1.33200  1.000 14.46049 ? 158 ILE   C CA    1 
ATOM   5282 C  C     . ILE   D 2 159 ? -52.35000 14.10500 -1.47100  1.000 15.90836 ? 158 ILE   C C     1 
ATOM   5283 O  O     . ILE   D 2 159 ? -52.86500 14.92700 -0.71100  1.000 18.47114 ? 158 ILE   C O     1 
ATOM   5284 C  CB    . ILE   D 2 159 ? -50.44100 13.58500 0.12900   1.000 15.47566 ? 158 ILE   C CB    1 
ATOM   5285 C  CG1   . ILE   D 2 159 ? -48.96300 13.18800 0.22000   1.000 15.45572 ? 158 ILE   C CG1   1 
ATOM   5286 C  CG2   . ILE   D 2 159 ? -51.31300 12.60800 0.91400   1.000 15.53440 ? 158 ILE   C CG2   1 
ATOM   5287 C  CD1   . ILE   D 2 159 ? -48.39600 13.32400 1.63500   1.000 14.90389 ? 158 ILE   C CD1   1 
ATOM   5288 N  N     . ALA   D 2 160 ? -53.03200 13.54700 -2.47700  1.000 15.58479 ? 159 ALA   C N     1 
ATOM   5289 C  CA    . ALA   D 2 160 ? -54.40600 13.95800 -2.74500  1.000 17.59406 ? 159 ALA   C CA    1 
ATOM   5290 C  C     . ALA   D 2 160 ? -55.36100 13.40800 -1.69900  1.000 17.91363 ? 159 ALA   C C     1 
ATOM   5291 O  O     . ALA   D 2 160 ? -56.39800 14.01900 -1.42200  1.000 19.99502 ? 159 ALA   C O     1 
ATOM   5292 C  CB    . ALA   D 2 160 ? -54.81700 13.48300 -4.13000  1.000 18.86071 ? 159 ALA   C CB    1 
ATOM   5293 N  N     . ASP   D 2 161 ? -55.04400 12.24700 -1.13300  1.000 16.35519 ? 160 ASP   C N     1 
ATOM   5294 C  CA    . ASP   D 2 161 ? -55.84500 11.65900 -0.06400  1.000 15.22544 ? 160 ASP   C CA    1 
ATOM   5295 C  C     . ASP   D 2 161 ? -54.91200 10.80500 0.77500   1.000 15.62688 ? 160 ASP   C C     1 
ATOM   5296 O  O     . ASP   D 2 161 ? -53.85900 10.37300 0.31500   1.000 15.60916 ? 160 ASP   C O     1 
ATOM   5297 C  CB    . ASP   D 2 161 ? -57.01000 10.81300 -0.61300  1.000 18.19854 ? 160 ASP   C CB    1 
ATOM   5298 C  CG    . ASP   D 2 161 ? -58.18900 10.72700 0.35100   1.000 21.12489 ? 160 ASP   C CG    1 
ATOM   5299 O  OD1   . ASP   D 2 161 ? -58.05800 11.09800 1.53400   1.000 20.65325 ? 160 ASP   C OD1   1 
ATOM   5300 O  OD2   . ASP   D 2 161 ? -59.27900 10.29800 -0.08600  1.000 25.99461 ? 160 ASP   C OD2   1 
ATOM   5301 N  N     . CYS   D 2 162 ? -55.28500 10.58100 2.02600   1.000 14.99404 ? 161 CYS   C N     1 
ATOM   5302 C  CA    . CYS   D 2 162 ? -54.47700 9.74000  2.90000   1.000 15.63393 ? 161 CYS   C CA    1 
ATOM   5303 C  C     . CYS   D 2 162 ? -55.36700 9.29200  4.04500   1.000 16.21697 ? 161 CYS   C C     1 
ATOM   5304 O  O     . CYS   D 2 162 ? -56.40500 9.89800  4.32000   1.000 18.86894 ? 161 CYS   C O     1 
ATOM   5305 C  CB    . CYS   D 2 162 ? -53.20800 10.46300 3.40400   1.000 15.35831 ? 161 CYS   C CB    1 
ATOM   5306 S  SG    . CYS   D 2 162 ? -53.45300 12.10600 4.04800   1.000 16.57949 ? 161 CYS   C SG    1 
ATOM   5307 N  N     . GLY   D 2 163 ? -54.96000 8.20900  4.69400   1.000 15.89233 ? 162 GLY   C N     1 
ATOM   5308 C  CA    . GLY   D 2 163 ? -55.73800 7.69200  5.80200   1.000 17.46677 ? 162 GLY   C CA    1 
ATOM   5309 C  C     . GLY   D 2 163 ? -55.12300 6.42400  6.34600   1.000 16.84578 ? 162 GLY   C C     1 
ATOM   5310 O  O     . GLY   D 2 163 ? -54.00800 6.04600  5.98700   1.000 16.22233 ? 162 GLY   C O     1 
ATOM   5311 N  N     . GLN   D 2 164 ? -55.85400 5.78100  7.24500   1.000 17.40685 ? 163 GLN   C N     1 
ATOM   5312 C  CA    . GLN   D 2 164 ? -55.43200 4.52600  7.84500   1.000 18.04533 ? 163 GLN   C CA    1 
ATOM   5313 C  C     . GLN   D 2 164 ? -56.25100 3.36900  7.28500   1.000 21.04176 ? 163 GLN   C C     1 
ATOM   5314 O  O     . GLN   D 2 164 ? -57.47200 3.47200  7.13000   1.000 21.54391 ? 163 GLN   C O     1 
ATOM   5315 C  CB    . GLN   D 2 164 ? -55.57100 4.59100  9.36400   1.000 18.35390 ? 163 GLN   C CB    1 
ATOM   5316 C  CG    . GLN   D 2 164 ? -55.07700 3.35000  10.08400  1.000 19.88853 ? 163 GLN   C CG    1 
ATOM   5317 C  CD    . GLN   D 2 164 ? -54.99600 3.55300  11.58400  1.000 21.31031 ? 163 GLN   C CD    1 
ATOM   5318 O  OE1   . GLN   D 2 164 ? -55.33000 4.61900  12.09400  1.000 20.05366 ? 163 GLN   C OE1   1 
ATOM   5319 N  NE2   . GLN   D 2 164 ? -54.52100 2.54100  12.29400  1.000 21.25678 ? 163 GLN   C NE2   1 
ATOM   5320 N  N     . LEU   D 2 165 ? -55.57600 2.27800  6.96200   1.000 22.42763 ? 164 LEU   C N     1 
ATOM   5321 C  CA    . LEU   D 2 165 ? -56.23100 1.07100  6.48700   1.000 26.89475 ? 164 LEU   C CA    1 
ATOM   5322 C  C     . LEU   D 2 165 ? -56.40700 0.09200  7.64000   1.000 33.06402 ? 164 LEU   C C     1 
ATOM   5323 O  O     . LEU   D 2 165 ? -55.62100 0.06700  8.59000   1.000 33.20051 ? 164 LEU   C O     1 
ATOM   5324 C  CB    . LEU   D 2 165 ? -55.40200 0.41900  5.38000   1.000 28.23234 ? 164 LEU   C CB    1 
ATOM   5325 C  CG    . LEU   D 2 165 ? -55.18300 1.26800  4.12500   1.000 30.61116 ? 164 LEU   C CG    1 
ATOM   5326 C  CD1   . LEU   D 2 165 ? -54.20100 0.58100  3.18400   1.000 31.78507 ? 164 LEU   C CD1   1 
ATOM   5327 C  CD2   . LEU   D 2 165 ? -56.51300 1.53900  3.42800   1.000 30.27378 ? 164 LEU   C CD2   1 
ATOM   5328 N  N     . GLU   D 2 166 ? -57.45900 -0.71100 7.55500   1.000 41.56922 ? 165 GLU   C N     1 
ATOM   5329 C  CA    . GLU   D 2 166 ? -57.71600 -1.70300 8.58600   1.000 52.38097 ? 165 GLU   C CA    1 
ATOM   5330 C  C     . GLU   D 2 166 ? -56.54200 -2.67600 8.66700   1.000 58.07946 ? 165 GLU   C C     1 
ATOM   5331 O  O     . GLU   D 2 166 ? -56.19400 -3.17500 9.73900   1.000 60.05477 ? 165 GLU   C O     1 
ATOM   5332 C  CB    . GLU   D 2 166 ? -59.02600 -2.44200 8.30600   1.000 57.07223 ? 165 GLU   C CB    1 
ATOM   5333 C  CG    . GLU   D 2 166 ? -58.87500 -3.93700 8.09000   1.000 62.70881 ? 165 GLU   C CG    1 
ATOM   5334 C  CD    . GLU   D 2 166 ? -60.21100 -4.65300 8.05500   1.000 67.61153 ? 165 GLU   C CD    1 
ATOM   5335 O  OE1   . GLU   D 2 166 ? -61.18800 -4.11000 8.61500   1.000 68.37450 ? 165 GLU   C OE1   1 
ATOM   5336 O  OE2   . GLU   D 2 166 ? -60.28500 -5.75400 7.46800   1.000 70.41434 ? 165 GLU   C OE2   1 
ATOM   5337 O  OXT   . GLU   D 2 166 ? -55.89600 -2.96200 7.65700   1.000 59.98937 ? 165 GLU   C OXT   1 
HETATM 5338 P  PG    . GNP   E 3 .   ? -29.00600 23.05300 -31.83100 1.000 13.81389 ? 201 GNP   A PG    1 
HETATM 5339 O  O1G   . GNP   E 3 .   ? -28.90300 23.26900 -30.35300 1.000 16.28858 ? 201 GNP   A O1G   1 
HETATM 5340 O  O2G   . GNP   E 3 .   ? -27.68300 23.38800 -32.46600 1.000 15.72394 ? 201 GNP   A O2G   1 
HETATM 5341 O  O3G   . GNP   E 3 .   ? -30.11800 23.92200 -32.40300 1.000 17.67377 ? 201 GNP   A O3G   1 
HETATM 5342 N  N3B   . GNP   E 3 .   ? -29.37600 21.48800 -32.15800 1.000 14.94098 ? 201 GNP   A N3B   1 
HETATM 5343 P  PB    . GNP   E 3 .   ? -28.74900 20.14000 -31.46100 1.000 13.72823 ? 201 GNP   A PB    1 
HETATM 5344 O  O1B   . GNP   E 3 .   ? -28.78100 20.25900 -29.96600 1.000 14.05771 ? 201 GNP   A O1B   1 
HETATM 5345 O  O2B   . GNP   E 3 .   ? -27.45600 19.74200 -32.11900 1.000 13.80253 ? 201 GNP   A O2B   1 
HETATM 5346 O  O3A   . GNP   E 3 .   ? -29.79100 18.98600 -31.84200 1.000 15.61446 ? 201 GNP   A O3A   1 
HETATM 5347 P  PA    . GNP   E 3 .   ? -30.96600 18.35700 -30.96100 1.000 15.26719 ? 201 GNP   A PA    1 
HETATM 5348 O  O1A   . GNP   E 3 .   ? -31.92000 19.44800 -30.61700 1.000 16.04920 ? 201 GNP   A O1A   1 
HETATM 5349 O  O2A   . GNP   E 3 .   ? -30.37300 17.55100 -29.85500 1.000 16.79378 ? 201 GNP   A O2A   1 
HETATM 5350 O  "O5'" . GNP   E 3 .   ? -31.61900 17.36400 -32.02900 1.000 15.32732 ? 201 GNP   A "O5'" 1 
HETATM 5351 C  "C5'" . GNP   E 3 .   ? -32.22000 17.87700 -33.23700 1.000 16.95908 ? 201 GNP   A "C5'" 1 
HETATM 5352 C  "C4'" . GNP   E 3 .   ? -33.28300 16.91200 -33.70400 1.000 17.63221 ? 201 GNP   A "C4'" 1 
HETATM 5353 O  "O4'" . GNP   E 3 .   ? -32.67100 15.63400 -34.01500 1.000 17.53070 ? 201 GNP   A "O4'" 1 
HETATM 5354 C  "C3'" . GNP   E 3 .   ? -34.39900 16.60200 -32.69800 1.000 18.74496 ? 201 GNP   A "C3'" 1 
HETATM 5355 O  "O3'" . GNP   E 3 .   ? -35.64400 16.45700 -33.36900 1.000 21.05607 ? 201 GNP   A "O3'" 1 
HETATM 5356 C  "C2'" . GNP   E 3 .   ? -33.93500 15.28900 -32.06200 1.000 18.66812 ? 201 GNP   A "C2'" 1 
HETATM 5357 O  "O2'" . GNP   E 3 .   ? -35.00200 14.50400 -31.57500 1.000 20.56530 ? 201 GNP   A "O2'" 1 
HETATM 5358 C  "C1'" . GNP   E 3 .   ? -33.23100 14.61000 -33.23100 1.000 18.11508 ? 201 GNP   A "C1'" 1 
HETATM 5359 N  N9    . GNP   E 3 .   ? -32.16500 13.70300 -32.82800 1.000 18.13713 ? 201 GNP   A N9    1 
HETATM 5360 C  C8    . GNP   E 3 .   ? -31.06300 13.99800 -32.06700 1.000 17.23712 ? 201 GNP   A C8    1 
HETATM 5361 N  N7    . GNP   E 3 .   ? -30.27800 12.96700 -31.87400 1.000 15.85614 ? 201 GNP   A N7    1 
HETATM 5362 C  C5    . GNP   E 3 .   ? -30.90200 11.93000 -32.55400 1.000 16.32076 ? 201 GNP   A C5    1 
HETATM 5363 C  C6    . GNP   E 3 .   ? -30.52100 10.57500 -32.70200 1.000 16.50247 ? 201 GNP   A C6    1 
HETATM 5364 O  O6    . GNP   E 3 .   ? -29.52400 10.00000 -32.25500 1.000 16.71707 ? 201 GNP   A O6    1 
HETATM 5365 N  N1    . GNP   E 3 .   ? -31.44300 9.87100  -33.47100 1.000 18.35594 ? 201 GNP   A N1    1 
HETATM 5366 C  C2    . GNP   E 3 .   ? -32.58300 10.39600 -34.02200 1.000 19.05714 ? 201 GNP   A C2    1 
HETATM 5367 N  N2    . GNP   E 3 .   ? -33.34300 9.54800  -34.72500 1.000 22.80191 ? 201 GNP   A N2    1 
HETATM 5368 N  N3    . GNP   E 3 .   ? -32.94800 11.66800 -33.89000 1.000 19.24921 ? 201 GNP   A N3    1 
HETATM 5369 C  C4    . GNP   E 3 .   ? -32.06600 12.37200 -33.14300 1.000 18.21039 ? 201 GNP   A C4    1 
HETATM 5370 C  C1    . A1AOV F 4 .   ? -33.24100 34.46500 -34.91000 1.000 11.67120 ? 202 A1AOV A C1    1 
HETATM 5371 C  C10   . A1AOV F 4 .   ? -33.27400 28.49100 -35.96500 1.000 15.76197 ? 202 A1AOV A C10   1 
HETATM 5372 C  C11   . A1AOV F 4 .   ? -32.80500 27.19100 -35.36700 1.000 17.07297 ? 202 A1AOV A C11   1 
HETATM 5373 C  C12   . A1AOV F 4 .   ? -33.31600 25.98700 -36.14200 1.000 20.18020 ? 202 A1AOV A C12   1 
HETATM 5374 C  C13   . A1AOV F 4 .   ? -32.28600 25.69600 -37.21200 1.000 22.43099 ? 202 A1AOV A C13   1 
HETATM 5375 C  C14   . A1AOV F 4 .   ? -29.91600 26.37700 -37.30000 1.000 29.47870 ? 202 A1AOV A C14   1 
HETATM 5376 C  C15   . A1AOV F 4 .   ? -29.78400 25.80800 -38.65500 1.000 31.99537 ? 202 A1AOV A C15   1 
HETATM 5377 C  C16   . A1AOV F 4 .   ? -28.94000 24.87600 -39.13000 1.000 32.15714 ? 202 A1AOV A C16   1 
HETATM 5378 C  C17   . A1AOV F 4 .   ? -29.05800 24.53300 -40.58600 1.000 47.69557 ? 202 A1AOV A C17   1 
HETATM 5379 C  C18   . A1AOV F 4 .   ? -29.91900 25.57800 -41.28300 1.000 49.39835 ? 202 A1AOV A C18   1 
HETATM 5380 C  C19   . A1AOV F 4 .   ? -27.78700 23.89800 -42.47400 1.000 61.16897 ? 202 A1AOV A C19   1 
HETATM 5381 C  C2    . A1AOV F 4 .   ? -32.86700 33.04700 -34.58600 1.000 12.73993 ? 202 A1AOV A C2    1 
HETATM 5382 C  C20   . A1AOV F 4 .   ? -27.32300 25.96500 -41.36600 1.000 61.08653 ? 202 A1AOV A C20   1 
HETATM 5383 C  C21   . A1AOV F 4 .   ? -29.63700 23.13000 -40.71000 1.000 50.32152 ? 202 A1AOV A C21   1 
HETATM 5384 C  C22   . A1AOV F 4 .   ? -31.29500 27.08900 -35.45700 1.000 19.39993 ? 202 A1AOV A C22   1 
HETATM 5385 C  C23   . A1AOV F 4 .   ? -31.68500 35.80100 -32.27500 1.000 12.58246 ? 202 A1AOV A C23   1 
HETATM 5386 C  C24   . A1AOV F 4 .   ? -31.40600 35.46000 -30.85300 1.000 13.63350 ? 202 A1AOV A C24   1 
HETATM 5387 C  C25   . A1AOV F 4 .   ? -30.01200 35.96600 -28.90200 1.000 13.74757 ? 202 A1AOV A C25   1 
HETATM 5388 C  C26   . A1AOV F 4 .   ? -28.81000 36.83100 -28.58800 1.000 13.86885 ? 202 A1AOV A C26   1 
HETATM 5389 C  C27   . A1AOV F 4 .   ? -29.03800 38.21400 -29.19200 1.000 15.94691 ? 202 A1AOV A C27   1 
HETATM 5390 C  C28   . A1AOV F 4 .   ? -28.66900 36.98900 -27.09000 1.000 15.26160 ? 202 A1AOV A C28   1 
HETATM 5391 C  C29   . A1AOV F 4 .   ? -27.55400 36.25100 -29.21300 1.000 13.93872 ? 202 A1AOV A C29   1 
HETATM 5392 C  C3    . A1AOV F 4 .   ? -31.35200 32.84900 -34.66900 1.000 13.99407 ? 202 A1AOV A C3    1 
HETATM 5393 C  C30   . A1AOV F 4 .   ? -27.08900 34.86300 -28.81900 1.000 13.53662 ? 202 A1AOV A C30   1 
HETATM 5394 C  C31   . A1AOV F 4 .   ? -26.05000 34.56900 -27.80400 1.000 14.64043 ? 202 A1AOV A C31   1 
HETATM 5395 C  C32   . A1AOV F 4 .   ? -25.32700 35.58300 -26.98200 1.000 15.04231 ? 202 A1AOV A C32   1 
HETATM 5396 C  C33   . A1AOV F 4 .   ? -25.51100 35.73200 -25.61300 1.000 15.71625 ? 202 A1AOV A C33   1 
HETATM 5397 C  C34   . A1AOV F 4 .   ? -26.43100 34.88000 -24.83200 1.000 16.41958 ? 202 A1AOV A C34   1 
HETATM 5398 C  C35   . A1AOV F 4 .   ? -26.31100 32.84500 -23.62300 1.000 19.40664 ? 202 A1AOV A C35   1 
HETATM 5399 C  C36   . A1AOV F 4 .   ? -27.29300 35.72500 -23.91100 1.000 17.10674 ? 202 A1AOV A C36   1 
HETATM 5400 C  C37   . A1AOV F 4 .   ? -23.95400 37.47100 -25.55100 1.000 17.70567 ? 202 A1AOV A C37   1 
HETATM 5401 C  C38   . A1AOV F 4 .   ? -23.74400 37.36700 -26.91100 1.000 17.51513 ? 202 A1AOV A C38   1 
HETATM 5402 C  C39   . A1AOV F 4 .   ? -24.43400 36.41400 -27.63500 1.000 16.92177 ? 202 A1AOV A C39   1 
HETATM 5403 C  C4    . A1AOV F 4 .   ? -34.46800 31.28800 -35.09300 1.000 13.04908 ? 202 A1AOV A C4    1 
HETATM 5404 C  C40   . A1AOV F 4 .   ? -24.92200 32.52800 -26.94400 1.000 14.50842 ? 202 A1AOV A C40   1 
HETATM 5405 C  C41   . A1AOV F 4 .   ? -23.64100 32.49700 -27.75900 1.000 17.11523 ? 202 A1AOV A C41   1 
HETATM 5406 C  C42   . A1AOV F 4 .   ? -26.68200 32.65800 -28.66400 1.000 15.46037 ? 202 A1AOV A C42   1 
HETATM 5407 C  C43   . A1AOV F 4 .   ? -26.84300 31.31700 -28.97600 1.000 13.98003 ? 202 A1AOV A C43   1 
HETATM 5408 C  C44   . A1AOV F 4 .   ? -27.75700 30.93900 -29.94700 1.000 13.95888 ? 202 A1AOV A C44   1 
HETATM 5409 C  C45   . A1AOV F 4 .   ? -27.43600 33.61700 -29.32900 1.000 13.64715 ? 202 A1AOV A C45   1 
HETATM 5410 C  C46   . A1AOV F 4 .   ? -28.35300 33.24100 -30.31100 1.000 13.44483 ? 202 A1AOV A C46   1 
HETATM 5411 C  C47   . A1AOV F 4 .   ? -28.51500 31.89100 -30.62100 1.000 12.84094 ? 202 A1AOV A C47   1 
HETATM 5412 C  C48   . A1AOV F 4 .   ? -29.50100 31.43900 -31.65000 1.000 13.45522 ? 202 A1AOV A C48   1 
HETATM 5413 C  C49   . A1AOV F 4 .   ? -29.98500 30.13500 -31.62100 1.000 13.37306 ? 202 A1AOV A C49   1 
HETATM 5414 C  C5    . A1AOV F 4 .   ? -34.87400 30.22900 -36.09100 1.000 12.80396 ? 202 A1AOV A C5    1 
HETATM 5415 C  C50   . A1AOV F 4 .   ? -30.90500 29.70900 -32.57200 1.000 15.33155 ? 202 A1AOV A C50   1 
HETATM 5416 C  C51   . A1AOV F 4 .   ? -31.34400 30.58500 -33.55600 1.000 14.74950 ? 202 A1AOV A C51   1 
HETATM 5417 C  C52   . A1AOV F 4 .   ? -30.87000 31.88800 -33.59400 1.000 13.07637 ? 202 A1AOV A C52   1 
HETATM 5418 C  C53   . A1AOV F 4 .   ? -29.94900 32.30900 -32.64000 1.000 12.80998 ? 202 A1AOV A C53   1 
HETATM 5419 C  C54   . A1AOV F 4 .   ? -31.97500 37.29500 -32.35000 1.000 14.40858 ? 202 A1AOV A C54   1 
HETATM 5420 C  C55   . A1AOV F 4 .   ? -32.42800 37.64400 -33.75400 1.000 14.44278 ? 202 A1AOV A C55   1 
HETATM 5421 C  C56   . A1AOV F 4 .   ? -33.60200 36.76300 -34.14300 1.000 14.35938 ? 202 A1AOV A C56   1 
HETATM 5422 C  C6    . A1AOV F 4 .   ? -36.38600 30.25100 -36.37700 1.000 14.31400 ? 202 A1AOV A C6    1 
HETATM 5423 C  C7    . A1AOV F 4 .   ? -36.78900 31.61800 -36.92700 1.000 14.19260 ? 202 A1AOV A C7    1 
HETATM 5424 C  C8    . A1AOV F 4 .   ? -36.82800 29.17700 -37.37000 1.000 14.26079 ? 202 A1AOV A C8    1 
HETATM 5425 C  C9    . A1AOV F 4 .   ? -35.24100 28.26200 -34.51900 1.000 14.99297 ? 202 A1AOV A C9    1 
HETATM 5426 N  N1    . A1AOV F 4 .   ? -33.52100 32.12600 -35.49200 1.000 12.68348 ? 202 A1AOV A N1    1 
HETATM 5427 N  N2    . A1AOV F 4 .   ? -34.44200 28.94000 -35.54000 1.000 14.59826 ? 202 A1AOV A N2    1 
HETATM 5428 N  N3    . A1AOV F 4 .   ? -31.10200 26.37400 -36.71000 1.000 22.17637 ? 202 A1AOV A N3    1 
HETATM 5429 N  N4    . A1AOV F 4 .   ? -27.71100 24.56500 -41.16900 1.000 57.29955 ? 202 A1AOV A N4    1 
HETATM 5430 N  N5    . A1AOV F 4 .   ? -33.20800 35.37900 -33.95100 1.000 12.75628 ? 202 A1AOV A N5    1 
HETATM 5431 N  N6    . A1AOV F 4 .   ? -32.83100 35.00800 -32.73200 1.000 12.94446 ? 202 A1AOV A N6    1 
HETATM 5432 N  N7    . A1AOV F 4 .   ? -24.81400 36.66300 -24.93500 1.000 17.72634 ? 202 A1AOV A N7    1 
HETATM 5433 N  N8    . A1AOV F 4 .   ? -25.88200 33.24700 -27.77500 1.000 14.24385 ? 202 A1AOV A N8    1 
HETATM 5434 O  O1    . A1AOV F 4 .   ? -33.57800 34.75000 -36.03200 1.000 13.08916 ? 202 A1AOV A O1    1 
HETATM 5435 O  O2    . A1AOV F 4 .   ? -28.95100 26.87600 -36.76100 1.000 27.68810 ? 202 A1AOV A O2    1 
HETATM 5436 O  O3    . A1AOV F 4 .   ? -32.60600 29.10100 -36.76600 1.000 15.18964 ? 202 A1AOV A O3    1 
HETATM 5437 O  O4    . A1AOV F 4 .   ? -34.96100 31.33100 -33.98800 1.000 13.27664 ? 202 A1AOV A O4    1 
HETATM 5438 O  O5    . A1AOV F 4 .   ? -30.22600 36.04600 -30.30300 1.000 13.92668 ? 202 A1AOV A O5    1 
HETATM 5439 O  O6    . A1AOV F 4 .   ? -25.62400 34.01800 -24.04200 1.000 16.86072 ? 202 A1AOV A O6    1 
HETATM 5440 O  O7    . A1AOV F 4 .   ? -32.10400 34.75900 -30.15800 1.000 13.29409 ? 202 A1AOV A O7    1 
HETATM 5441 MG MG    . MG    G 5 .   ? -29.16300 21.93100 -28.81700 1.000 13.66757 ? 203 MG    A MG    1 
HETATM 5442 P  PG    . GNP   H 3 .   ? -29.49900 27.90600 2.58300   1.000 18.60836 ? 201 GNP   B PG    1 
HETATM 5443 O  O1G   . GNP   H 3 .   ? -30.56700 26.96300 3.08000   1.000 22.94617 ? 201 GNP   B O1G   1 
HETATM 5444 O  O2G   . GNP   H 3 .   ? -29.33400 27.73600 1.10400   1.000 19.16569 ? 201 GNP   B O2G   1 
HETATM 5445 O  O3G   . GNP   H 3 .   ? -28.22400 27.58700 3.27800   1.000 20.03459 ? 201 GNP   B O3G   1 
HETATM 5446 N  N3B   . GNP   H 3 .   ? -29.89400 29.45800 2.92900   1.000 21.12033 ? 201 GNP   B N3B   1 
HETATM 5447 P  PB    . GNP   H 3 .   ? -29.25300 30.82900 2.28200   1.000 18.79242 ? 201 GNP   B PB    1 
HETATM 5448 O  O1B   . GNP   H 3 .   ? -29.29200 30.75100 0.78200   1.000 21.45072 ? 201 GNP   B O1B   1 
HETATM 5449 O  O2B   . GNP   H 3 .   ? -27.98300 31.25200 2.95000   1.000 19.11296 ? 201 GNP   B O2B   1 
HETATM 5450 O  O3A   . GNP   H 3 .   ? -30.32200 31.96300 2.64900   1.000 21.81487 ? 201 GNP   B O3A   1 
HETATM 5451 P  PA    . GNP   H 3 .   ? -31.47600 32.59600 1.74600   1.000 22.77880 ? 201 GNP   B PA    1 
HETATM 5452 O  O1A   . GNP   H 3 .   ? -32.40500 31.52200 1.32100   1.000 21.80675 ? 201 GNP   B O1A   1 
HETATM 5453 O  O2A   . GNP   H 3 .   ? -30.85300 33.42400 0.67500   1.000 23.43631 ? 201 GNP   B O2A   1 
HETATM 5454 O  "O5'" . GNP   H 3 .   ? -32.18700 33.55100 2.81600   1.000 23.25182 ? 201 GNP   B "O5'" 1 
HETATM 5455 C  "C5'" . GNP   H 3 .   ? -32.78400 33.00000 4.01600   1.000 24.23757 ? 201 GNP   B "C5'" 1 
HETATM 5456 C  "C4'" . GNP   H 3 .   ? -33.85800 33.93700 4.51000   1.000 26.28628 ? 201 GNP   B "C4'" 1 
HETATM 5457 O  "O4'" . GNP   H 3 .   ? -33.27100 35.22200 4.84400   1.000 25.21642 ? 201 GNP   B "O4'" 1 
HETATM 5458 C  "C3'" . GNP   H 3 .   ? -34.98600 34.24300 3.51700   1.000 27.51389 ? 201 GNP   B "C3'" 1 
HETATM 5459 O  "O3'" . GNP   H 3 .   ? -36.22600 34.37400 4.20000   1.000 29.67150 ? 201 GNP   B "O3'" 1 
HETATM 5460 C  "C2'" . GNP   H 3 .   ? -34.52400 35.55800 2.88200   1.000 28.00846 ? 201 GNP   B "C2'" 1 
HETATM 5461 O  "O2'" . GNP   H 3 .   ? -35.57600 36.32100 2.33500   1.000 30.81374 ? 201 GNP   B "O2'" 1 
HETATM 5462 C  "C1'" . GNP   H 3 .   ? -33.85500 36.24200 4.06900   1.000 26.08172 ? 201 GNP   B "C1'" 1 
HETATM 5463 N  N9    . GNP   H 3 .   ? -32.80800 37.18100 3.69300   1.000 26.26699 ? 201 GNP   B N9    1 
HETATM 5464 C  C8    . GNP   H 3 .   ? -31.71900 36.93100 2.89900   1.000 24.93137 ? 201 GNP   B C8    1 
HETATM 5465 N  N7    . GNP   H 3 .   ? -30.94200 37.97200 2.74300   1.000 27.35628 ? 201 GNP   B N7    1 
HETATM 5466 C  C5    . GNP   H 3 .   ? -31.56500 38.97700 3.46800   1.000 27.50608 ? 201 GNP   B C5    1 
HETATM 5467 C  C6    . GNP   H 3 .   ? -31.19000 40.32900 3.66300   1.000 27.36041 ? 201 GNP   B C6    1 
HETATM 5468 O  O6    . GNP   H 3 .   ? -30.19700 40.92500 3.23000   1.000 25.73843 ? 201 GNP   B O6    1 
HETATM 5469 N  N1    . GNP   H 3 .   ? -32.10200 40.99300 4.48300   1.000 28.78691 ? 201 GNP   B N1    1 
HETATM 5470 C  C2    . GNP   H 3 .   ? -33.22900 40.43300 5.03100   1.000 30.07102 ? 201 GNP   B C2    1 
HETATM 5471 N  N2    . GNP   H 3 .   ? -33.99100 41.23500 5.78600   1.000 30.66189 ? 201 GNP   B N2    1 
HETATM 5472 N  N3    . GNP   H 3 .   ? -33.58700 39.16700 4.84900   1.000 28.18393 ? 201 GNP   B N3    1 
HETATM 5473 C  C4    . GNP   H 3 .   ? -32.71100 38.50000 4.06100   1.000 28.29380 ? 201 GNP   B C4    1 
HETATM 5474 C  C1    . A1AOV I 4 .   ? -33.66000 16.40900 5.49100   1.000 13.30644 ? 202 A1AOV B C1    1 
HETATM 5475 C  C10   . A1AOV I 4 .   ? -33.62100 22.42400 6.74800   1.000 17.13583 ? 202 A1AOV B C10   1 
HETATM 5476 C  C11   . A1AOV I 4 .   ? -33.16000 23.76800 6.24800   1.000 21.04366 ? 202 A1AOV B C11   1 
HETATM 5477 C  C12   . A1AOV I 4 .   ? -33.70300 24.87000 7.13900   1.000 24.91126 ? 202 A1AOV B C12   1 
HETATM 5478 C  C13   . A1AOV I 4 .   ? -32.63000 25.18600 8.16600   1.000 27.46535 ? 202 A1AOV B C13   1 
HETATM 5479 C  C14   . A1AOV I 4 .   ? -30.28000 24.46600 8.21500   1.000 41.19505 ? 202 A1AOV B C14   1 
HETATM 5480 C  C15   . A1AOV I 4 .   ? -30.10200 24.95200 9.59300   1.000 42.32103 ? 202 A1AOV B C15   1 
HETATM 5481 C  C16   . A1AOV I 4 .   ? -29.33000 25.95700 10.03400  1.000 41.91425 ? 202 A1AOV B C16   1 
HETATM 5482 C  C17   . A1AOV I 4 .   ? -29.30100 26.23800 11.50900  1.000 53.74003 ? 202 A1AOV B C17   1 
HETATM 5483 C  C18   . A1AOV I 4 .   ? -30.14600 25.23000 12.26900  1.000 54.00573 ? 202 A1AOV B C18   1 
HETATM 5484 C  C19   . A1AOV I 4 .   ? -27.30800 24.81300 11.65400  1.000 61.69227 ? 202 A1AOV B C19   1 
HETATM 5485 C  C2    . A1AOV I 4 .   ? -33.28200 17.83400 5.18900   1.000 13.97540 ? 202 A1AOV B C2    1 
HETATM 5486 C  C20   . A1AOV I 4 .   ? -27.84900 26.30000 13.41100  1.000 62.54725 ? 202 A1AOV B C20   1 
HETATM 5487 C  C21   . A1AOV I 4 .   ? -29.80100 27.66100 11.74300  1.000 56.06283 ? 202 A1AOV B C21   1 
HETATM 5488 C  C22   . A1AOV I 4 .   ? -31.65200 23.91100 6.31800   1.000 26.08759 ? 202 A1AOV B C22   1 
HETATM 5489 C  C23   . A1AOV I 4 .   ? -32.07000 15.10900 2.84900   1.000 13.86232 ? 202 A1AOV B C23   1 
HETATM 5490 C  C24   . A1AOV I 4 .   ? -31.73900 15.45600 1.43600   1.000 14.80249 ? 202 A1AOV B C24   1 
HETATM 5491 C  C25   . A1AOV I 4 .   ? -30.32300 14.97200 -0.49300  1.000 14.44811 ? 202 A1AOV B C25   1 
HETATM 5492 C  C26   . A1AOV I 4 .   ? -29.10100 14.13400 -0.79800  1.000 16.00824 ? 202 A1AOV B C26   1 
HETATM 5493 C  C27   . A1AOV I 4 .   ? -29.31100 12.74000 -0.22000  1.000 18.21954 ? 202 A1AOV B C27   1 
HETATM 5494 C  C28   . A1AOV I 4 .   ? -28.90800 14.02800 -2.29900  1.000 16.67808 ? 202 A1AOV B C28   1 
HETATM 5495 C  C29   . A1AOV I 4 .   ? -27.88200 14.72000 -0.10200  1.000 15.63764 ? 202 A1AOV B C29   1 
HETATM 5496 C  C3    . A1AOV I 4 .   ? -31.76600 17.99600 5.27400   1.000 15.06212 ? 202 A1AOV B C3    1 
HETATM 5497 C  C30   . A1AOV I 4 .   ? -27.38900 16.10300 -0.49000  1.000 15.71867 ? 202 A1AOV B C30   1 
HETATM 5498 C  C31   . A1AOV I 4 .   ? -26.32900 16.41300 -1.48500  1.000 17.31541 ? 202 A1AOV B C31   1 
HETATM 5499 C  C32   . A1AOV I 4 .   ? -25.58700 15.40700 -2.29900  1.000 16.79101 ? 202 A1AOV B C32   1 
HETATM 5500 C  C33   . A1AOV I 4 .   ? -25.73900 15.26200 -3.67300  1.000 17.89173 ? 202 A1AOV B C33   1 
HETATM 5501 C  C34   . A1AOV I 4 .   ? -26.64700 16.10700 -4.48600  1.000 18.75798 ? 202 A1AOV B C34   1 
HETATM 5502 C  C35   . A1AOV I 4 .   ? -26.48500 18.15000 -5.64300  1.000 19.37457 ? 202 A1AOV B C35   1 
HETATM 5503 C  C36   . A1AOV I 4 .   ? -27.52500 15.26000 -5.39100  1.000 20.26549 ? 202 A1AOV B C36   1 
HETATM 5504 C  C37   . A1AOV I 4 .   ? -24.18500 13.51000 -3.69400  1.000 19.63595 ? 202 A1AOV B C37   1 
HETATM 5505 C  C38   . A1AOV I 4 .   ? -24.00500 13.61700 -2.32900  1.000 20.16583 ? 202 A1AOV B C38   1 
HETATM 5506 C  C39   . A1AOV I 4 .   ? -24.71000 14.57200 -1.63000  1.000 18.95109 ? 202 A1AOV B C39   1 
HETATM 5507 C  C4    . A1AOV I 4 .   ? -34.82600 19.62300 5.69700   1.000 13.97636 ? 202 A1AOV B C4    1 
HETATM 5508 C  C40   . A1AOV I 4 .   ? -25.20700 18.47800 -2.29300  1.000 17.17401 ? 202 A1AOV B C40   1 
HETATM 5509 C  C41   . A1AOV I 4 .   ? -23.96400 18.52900 -1.42000  1.000 19.84425 ? 202 A1AOV B C41   1 
HETATM 5510 C  C42   . A1AOV I 4 .   ? -26.99400 18.31500 -0.61500  1.000 16.88751 ? 202 A1AOV B C42   1 
HETATM 5511 C  C43   . A1AOV I 4 .   ? -27.17800 19.64700 -0.29200  1.000 15.97713 ? 202 A1AOV B C43   1 
HETATM 5512 C  C44   . A1AOV I 4 .   ? -28.11300 20.01100 0.66100   1.000 15.71939 ? 202 A1AOV B C44   1 
HETATM 5513 C  C45   . A1AOV I 4 .   ? -27.75200 17.34100 0.02400   1.000 15.76926 ? 202 A1AOV B C45   1 
HETATM 5514 C  C46   . A1AOV I 4 .   ? -28.69300 17.69600 0.98400   1.000 15.65448 ? 202 A1AOV B C46   1 
HETATM 5515 C  C47   . A1AOV I 4 .   ? -28.87100 19.04000 1.30500   1.000 15.33094 ? 202 A1AOV B C47   1 
HETATM 5516 C  C48   . A1AOV I 4 .   ? -29.86900 19.47300 2.32600   1.000 15.46815 ? 202 A1AOV B C48   1 
HETATM 5517 C  C49   . A1AOV I 4 .   ? -30.33200 20.77900 2.32800   1.000 16.20908 ? 202 A1AOV B C49   1 
HETATM 5518 C  C5    . A1AOV I 4 .   ? -35.22600 20.66700 6.69700   1.000 13.97681 ? 202 A1AOV B C5    1 
HETATM 5519 C  C50   . A1AOV I 4 .   ? -31.25800 21.20300 3.27000   1.000 17.05306 ? 202 A1AOV B C50   1 
HETATM 5520 C  C51   . A1AOV I 4 .   ? -31.72700 20.30700 4.22400   1.000 15.04659 ? 202 A1AOV B C51   1 
HETATM 5521 C  C52   . A1AOV I 4 .   ? -31.27100 18.98800 4.23500   1.000 15.04189 ? 202 A1AOV B C52   1 
HETATM 5522 C  C53   . A1AOV I 4 .   ? -30.34100 18.58000 3.28600   1.000 14.68013 ? 202 A1AOV B C53   1 
HETATM 5523 C  C54   . A1AOV I 4 .   ? -32.37700 13.62000 2.89400   1.000 15.30135 ? 202 A1AOV B C54   1 
HETATM 5524 C  C55   . A1AOV I 4 .   ? -32.83200 13.25000 4.29100   1.000 14.38429 ? 202 A1AOV B C55   1 
HETATM 5525 C  C56   . A1AOV I 4 .   ? -34.00500 14.13300 4.69700   1.000 13.32411 ? 202 A1AOV B C56   1 
HETATM 5526 C  C6    . A1AOV I 4 .   ? -36.75100 20.67700 6.90800   1.000 15.04610 ? 202 A1AOV B C6    1 
HETATM 5527 C  C7    . A1AOV I 4 .   ? -37.21500 19.31000 7.41800   1.000 15.53450 ? 202 A1AOV B C7    1 
HETATM 5528 C  C8    . A1AOV I 4 .   ? -37.17300 21.73200 7.93000   1.000 15.62366 ? 202 A1AOV B C8    1 
HETATM 5529 C  C9    . A1AOV I 4 .   ? -35.45000 22.67100 5.14500   1.000 18.46694 ? 202 A1AOV B C9    1 
HETATM 5530 N  N1    . A1AOV I 4 .   ? -33.90600 18.77000 6.10000   1.000 13.12409 ? 202 A1AOV B N1    1 
HETATM 5531 N  N2    . A1AOV I 4 .   ? -34.74300 21.96900 6.21400   1.000 15.84134 ? 202 A1AOV B N2    1 
HETATM 5532 N  N3    . A1AOV I 4 .   ? -31.46000 24.52800 7.62000   1.000 29.95660 ? 202 A1AOV B N3    1 
HETATM 5533 N  N4    . A1AOV I 4 .   ? -27.89600 26.12800 11.95700  1.000 59.88872 ? 202 A1AOV B N4    1 
HETATM 5534 N  N5    . A1AOV I 4 .   ? -33.61300 15.52000 4.51400   1.000 12.59269 ? 202 A1AOV B N5    1 
HETATM 5535 N  N6    . A1AOV I 4 .   ? -33.22300 15.90500 3.30000   1.000 12.68711 ? 202 A1AOV B N6    1 
HETATM 5536 N  N7    . A1AOV I 4 .   ? -25.03000 14.32300 -4.32800  1.000 19.29493 ? 202 A1AOV B N7    1 
HETATM 5537 N  N8    . A1AOV I 4 .   ? -26.18000 17.73800 -1.49800  1.000 16.82506 ? 202 A1AOV B N8    1 
HETATM 5538 O  O1    . A1AOV I 4 .   ? -34.01600 16.10400 6.60900   1.000 14.02864 ? 202 A1AOV B O1    1 
HETATM 5539 O  O2    . A1AOV I 4 .   ? -29.32100 23.98000 7.64700   1.000 47.55930 ? 202 A1AOV B O2    1 
HETATM 5540 O  O3    . A1AOV I 4 .   ? -33.00000 21.79900 7.57500   1.000 17.35323 ? 202 A1AOV B O3    1 
HETATM 5541 O  O4    . A1AOV I 4 .   ? -35.29700 19.59600 4.58500   1.000 14.16169 ? 202 A1AOV B O4    1 
HETATM 5542 O  O5    . A1AOV I 4 .   ? -30.56300 14.86000 0.89900   1.000 14.99123 ? 202 A1AOV B O5    1 
HETATM 5543 O  O6    . A1AOV I 4 .   ? -25.83400 16.93400 -5.30700  1.000 17.90986 ? 202 A1AOV B O6    1 
HETATM 5544 O  O7    . A1AOV I 4 .   ? -32.40200 16.19200 0.74200   1.000 14.56033 ? 202 A1AOV B O7    1 
HETATM 5545 MG MG    . MG    J 5 .   ? -29.62700 29.02600 -0.43800  1.000 18.68721 ? 203 MG    B MG    1 
HETATM 5546 O  O     . HOH   K 6 .   ? -17.36600 27.25500 -33.10200 1.000 49.11270 ? 301 HOH   A O     1 
HETATM 5547 O  O     . HOH   K 6 .   ? -11.55700 31.71900 -36.34300 1.000 55.90712 ? 302 HOH   A O     1 
HETATM 5548 O  O     . HOH   K 6 .   ? -17.34800 26.70900 -36.35200 1.000 44.39008 ? 303 HOH   A O     1 
HETATM 5549 O  O     . HOH   K 6 .   ? -12.75500 1.25100  -17.76400 1.000 43.81058 ? 304 HOH   A O     1 
HETATM 5550 O  O     . HOH   K 6 .   ? -37.39000 8.98900  -34.24800 1.000 67.17913 ? 305 HOH   A O     1 
HETATM 5551 O  O     . HOH   K 6 .   ? -24.41600 25.07200 -37.70700 1.000 28.03324 ? 306 HOH   A O     1 
HETATM 5552 O  O     . HOH   K 6 .   ? -43.58500 22.41600 -27.50500 1.000 51.09504 ? 307 HOH   A O     1 
HETATM 5553 O  O     . HOH   K 6 .   ? -29.84800 21.38900 -23.41300 1.000 32.63790 ? 308 HOH   A O     1 
HETATM 5554 O  O     . HOH   K 6 .   ? -34.61700 27.06700 -26.75900 1.000 33.00854 ? 309 HOH   A O     1 
HETATM 5555 O  O     . HOH   K 6 .   ? -15.11700 30.97800 -31.99900 1.000 61.40566 ? 310 HOH   A O     1 
HETATM 5556 O  O     . HOH   K 6 .   ? -22.79500 6.43600  -46.57200 1.000 56.20910 ? 311 HOH   A O     1 
HETATM 5557 O  O     . HOH   K 6 .   ? -18.55800 37.43100 -33.93400 1.000 57.22502 ? 312 HOH   A O     1 
HETATM 5558 O  O     . HOH   K 6 .   ? -21.35800 26.04100 -17.95100 1.000 47.25010 ? 313 HOH   A O     1 
HETATM 5559 O  O     . HOH   K 6 .   ? -27.19000 22.09700 -28.26800 1.000 14.71857 ? 314 HOH   A O     1 
HETATM 5560 O  O     . HOH   K 6 .   ? -20.50300 1.44200  -38.83000 1.000 50.41126 ? 315 HOH   A O     1 
HETATM 5561 O  O     . HOH   K 6 .   ? -17.39600 24.24600 -11.34800 1.000 49.28922 ? 316 HOH   A O     1 
HETATM 5562 O  O     . HOH   K 6 .   ? -23.68800 8.41400  -17.15800 1.000 42.50181 ? 317 HOH   A O     1 
HETATM 5563 O  O     . HOH   K 6 .   ? -23.10300 13.02000 -48.96600 1.000 39.95153 ? 318 HOH   A O     1 
HETATM 5564 O  O     . HOH   K 6 .   ? -36.24600 21.67800 -23.82200 1.000 47.26640 ? 319 HOH   A O     1 
HETATM 5565 O  O     . HOH   K 6 .   ? -18.19700 22.90000 -43.92000 1.000 38.31860 ? 320 HOH   A O     1 
HETATM 5566 O  O     . HOH   K 6 .   ? -12.35900 36.09400 -28.59800 1.000 47.04240 ? 321 HOH   A O     1 
HETATM 5567 O  O     A HOH   K 6 .   ? -8.76300  5.06300  -12.54400 0.500 31.64578 ? 322 HOH   A O     1 
HETATM 5568 O  O     B HOH   K 6 .   ? -7.33200  5.27400  -11.03100 0.500 35.12133 ? 322 HOH   A O     1 
HETATM 5569 O  O     . HOH   K 6 .   ? -28.74600 1.43900  -25.90400 1.000 47.93270 ? 323 HOH   A O     1 
HETATM 5570 O  O     . HOH   K 6 .   ? -10.12200 7.34400  -16.27600 1.000 34.98637 ? 324 HOH   A O     1 
HETATM 5571 O  O     . HOH   K 6 .   ? -23.04600 29.05300 -29.69600 1.000 26.85624 ? 325 HOH   A O     1 
HETATM 5572 O  O     . HOH   K 6 .   ? -13.62300 28.72400 -38.12300 1.000 42.91309 ? 326 HOH   A O     1 
HETATM 5573 O  O     . HOH   K 6 .   ? -5.83900  19.24700 -36.62900 1.000 40.27384 ? 327 HOH   A O     1 
HETATM 5574 O  O     . HOH   K 6 .   ? -4.09700  27.41700 -23.69900 1.000 42.03607 ? 328 HOH   A O     1 
HETATM 5575 O  O     . HOH   K 6 .   ? -26.71400 27.49000 -38.02800 1.000 44.73618 ? 329 HOH   A O     1 
HETATM 5576 O  O     . HOH   K 6 .   ? -19.82900 2.93500  -27.87200 1.000 46.63794 ? 330 HOH   A O     1 
HETATM 5577 O  O     . HOH   K 6 .   ? -3.91600  8.71500  -34.95300 1.000 42.40980 ? 331 HOH   A O     1 
HETATM 5578 O  O     . HOH   K 6 .   ? -12.79800 8.67100  -6.74400  1.000 49.39860 ? 332 HOH   A O     1 
HETATM 5579 O  O     . HOH   K 6 .   ? -34.82600 5.34700  -35.53800 1.000 34.69614 ? 333 HOH   A O     1 
HETATM 5580 O  O     . HOH   K 6 .   ? -24.14600 22.89100 -41.01200 1.000 43.32232 ? 334 HOH   A O     1 
HETATM 5581 O  O     . HOH   K 6 .   ? -21.55700 24.53600 -38.03900 1.000 47.51832 ? 335 HOH   A O     1 
HETATM 5582 O  O     . HOH   K 6 .   ? -3.26000  11.46700 -30.11000 1.000 50.77077 ? 336 HOH   A O     1 
HETATM 5583 O  O     . HOH   K 6 .   ? 2.26900   27.94100 -27.47400 1.000 35.15946 ? 337 HOH   A O     1 
HETATM 5584 O  O     . HOH   K 6 .   ? -24.26200 28.65600 -27.11200 1.000 16.73481 ? 338 HOH   A O     1 
HETATM 5585 O  O     . HOH   K 6 .   ? -29.94100 11.46700 -45.63500 1.000 21.09958 ? 339 HOH   A O     1 
HETATM 5586 O  O     . HOH   K 6 .   ? -29.95700 4.14400  -46.78400 1.000 28.44742 ? 340 HOH   A O     1 
HETATM 5587 O  O     . HOH   K 6 .   ? -18.17700 3.67500  -15.62100 1.000 48.22015 ? 341 HOH   A O     1 
HETATM 5588 O  O     . HOH   K 6 .   ? -3.27600  18.47200 -34.81300 1.000 40.17846 ? 342 HOH   A O     1 
HETATM 5589 O  O     . HOH   K 6 .   ? -20.57000 3.15000  -30.38300 1.000 35.92767 ? 343 HOH   A O     1 
HETATM 5590 O  O     . HOH   K 6 .   ? -34.05700 19.36300 -28.97400 1.000 18.25916 ? 344 HOH   A O     1 
HETATM 5591 O  O     . HOH   K 6 .   ? -21.52800 25.96600 -33.73700 1.000 33.93535 ? 345 HOH   A O     1 
HETATM 5592 O  O     . HOH   K 6 .   ? -29.59500 15.03400 -39.14700 1.000 20.53245 ? 346 HOH   A O     1 
HETATM 5593 O  O     . HOH   K 6 .   ? -28.62600 14.65800 -45.75900 1.000 20.50962 ? 347 HOH   A O     1 
HETATM 5594 O  O     . HOH   K 6 .   ? -7.70500  27.42300 -39.55000 1.000 50.81507 ? 348 HOH   A O     1 
HETATM 5595 O  O     . HOH   K 6 .   ? -28.45800 35.52500 -33.88600 1.000 16.65393 ? 349 HOH   A O     1 
HETATM 5596 O  O     . HOH   K 6 .   ? -31.18200 21.64900 -29.21800 1.000 15.38969 ? 350 HOH   A O     1 
HETATM 5597 O  O     . HOH   K 6 .   ? -8.69200  4.58600  -39.95600 1.000 51.02214 ? 351 HOH   A O     1 
HETATM 5598 O  O     . HOH   K 6 .   ? -27.12300 5.15000  -46.89900 1.000 32.05247 ? 352 HOH   A O     1 
HETATM 5599 O  O     . HOH   K 6 .   ? -25.79200 10.36800 -11.08600 1.000 56.38742 ? 353 HOH   A O     1 
HETATM 5600 O  O     . HOH   K 6 .   ? -29.80500 26.57500 -31.90100 1.000 21.81562 ? 354 HOH   A O     1 
HETATM 5601 O  O     . HOH   K 6 .   ? -15.79400 5.95700  -6.78700  1.000 44.42745 ? 355 HOH   A O     1 
HETATM 5602 O  O     . HOH   K 6 .   ? -21.82100 20.25300 -48.38300 1.000 48.29983 ? 356 HOH   A O     1 
HETATM 5603 O  O     . HOH   K 6 .   ? -11.14800 10.53200 -12.61000 1.000 25.06656 ? 357 HOH   A O     1 
HETATM 5604 O  O     . HOH   K 6 .   ? -3.24500  29.79900 -31.33000 1.000 21.43420 ? 358 HOH   A O     1 
HETATM 5605 O  O     . HOH   K 6 .   ? -28.65500 2.29000  -32.06900 1.000 51.45772 ? 359 HOH   A O     1 
HETATM 5606 O  O     . HOH   K 6 .   ? -30.97200 27.14900 -24.47100 1.000 16.66771 ? 360 HOH   A O     1 
HETATM 5607 O  O     . HOH   K 6 .   ? -9.71000  14.21000 -5.69900  1.000 39.98756 ? 361 HOH   A O     1 
HETATM 5608 O  O     . HOH   K 6 .   ? -5.56900  13.43600 -24.22600 1.000 32.93115 ? 362 HOH   A O     1 
HETATM 5609 O  O     . HOH   K 6 .   ? -15.39000 23.02500 -44.98800 1.000 50.68753 ? 363 HOH   A O     1 
HETATM 5610 O  O     . HOH   K 6 .   ? -8.39700  13.64700 -27.54000 1.000 19.23675 ? 364 HOH   A O     1 
HETATM 5611 O  O     . HOH   K 6 .   ? -14.45300 -0.93600 -42.86400 1.000 54.53282 ? 365 HOH   A O     1 
HETATM 5612 O  O     . HOH   K 6 .   ? -6.39300  8.91500  -41.50300 1.000 39.50167 ? 366 HOH   A O     1 
HETATM 5613 O  O     . HOH   K 6 .   ? -8.55200  7.49500  -33.83900 1.000 32.69492 ? 367 HOH   A O     1 
HETATM 5614 O  O     . HOH   K 6 .   ? -28.91600 28.55200 -19.60400 1.000 36.91816 ? 368 HOH   A O     1 
HETATM 5615 O  O     . HOH   K 6 .   ? 1.52200   30.29700 -30.44300 1.000 14.90066 ? 369 HOH   A O     1 
HETATM 5616 O  O     . HOH   K 6 .   ? -39.19200 23.28800 -29.23600 1.000 24.21967 ? 370 HOH   A O     1 
HETATM 5617 O  O     . HOH   K 6 .   ? -21.10200 19.29600 -36.87600 1.000 15.93033 ? 371 HOH   A O     1 
HETATM 5618 O  O     . HOH   K 6 .   ? -32.38200 13.09700 -25.32100 1.000 23.89303 ? 372 HOH   A O     1 
HETATM 5619 O  O     . HOH   K 6 .   ? -12.43100 5.27400  -23.53700 1.000 38.36344 ? 373 HOH   A O     1 
HETATM 5620 O  O     . HOH   K 6 .   ? -9.75700  24.47500 -15.78900 1.000 51.29461 ? 374 HOH   A O     1 
HETATM 5621 O  O     . HOH   K 6 .   ? -15.21900 3.33900  -28.07900 1.000 31.12945 ? 375 HOH   A O     1 
HETATM 5622 O  O     . HOH   K 6 .   ? -5.43200  15.57000 -25.66500 1.000 41.20716 ? 376 HOH   A O     1 
HETATM 5623 O  O     . HOH   K 6 .   ? -24.84000 4.67400  -23.51600 1.000 24.79014 ? 377 HOH   A O     1 
HETATM 5624 O  O     . HOH   K 6 .   ? -25.68700 27.74300 -19.50000 1.000 22.33333 ? 378 HOH   A O     1 
HETATM 5625 O  O     . HOH   K 6 .   ? -9.77900  7.34700  -24.19300 1.000 49.71905 ? 379 HOH   A O     1 
HETATM 5626 O  O     . HOH   K 6 .   ? -12.06900 10.99400 -9.84200  1.000 25.26408 ? 380 HOH   A O     1 
HETATM 5627 O  O     . HOH   K 6 .   ? -6.30000  17.09700 -30.01100 1.000 28.85124 ? 381 HOH   A O     1 
HETATM 5628 O  O     . HOH   K 6 .   ? -33.89300 9.52800  -41.40400 1.000 36.25365 ? 382 HOH   A O     1 
HETATM 5629 O  O     A HOH   K 6 .   ? -32.26800 23.17100 -26.08700 0.500 27.38522 ? 383 HOH   A O     1 
HETATM 5630 O  O     B HOH   K 6 .   ? -30.64800 23.38400 -24.90800 0.500 17.88336 ? 383 HOH   A O     1 
HETATM 5631 O  O     . HOH   K 6 .   ? -19.35400 7.53900  -6.16200  1.000 52.00924 ? 384 HOH   A O     1 
HETATM 5632 O  O     . HOH   K 6 .   ? -34.63100 16.46400 -29.21100 1.000 32.65437 ? 385 HOH   A O     1 
HETATM 5633 O  O     . HOH   K 6 .   ? -4.62000  31.32700 -26.66000 1.000 19.20619 ? 386 HOH   A O     1 
HETATM 5634 O  O     . HOH   K 6 .   ? -7.81700  20.97000 -21.69600 1.000 24.29717 ? 387 HOH   A O     1 
HETATM 5635 O  O     . HOH   K 6 .   ? -13.65200 36.20000 -26.44800 1.000 26.15970 ? 388 HOH   A O     1 
HETATM 5636 O  O     . HOH   K 6 .   ? -28.08400 17.27900 -38.56100 1.000 29.95300 ? 389 HOH   A O     1 
HETATM 5637 O  O     . HOH   K 6 .   ? -27.15600 3.46100  -22.12400 1.000 58.78232 ? 390 HOH   A O     1 
HETATM 5638 O  O     . HOH   K 6 .   ? -7.86300  28.63700 -20.48000 1.000 35.64174 ? 391 HOH   A O     1 
HETATM 5639 O  O     . HOH   K 6 .   ? -7.04100  15.98200 -41.19900 1.000 52.62762 ? 392 HOH   A O     1 
HETATM 5640 O  O     . HOH   K 6 .   ? -18.94400 22.20000 -46.52000 1.000 41.63053 ? 393 HOH   A O     1 
HETATM 5641 O  O     . HOH   K 6 .   ? -22.15500 22.81800 -15.75700 1.000 25.10299 ? 394 HOH   A O     1 
HETATM 5642 O  O     . HOH   K 6 .   ? -30.13800 30.34700 -37.20100 1.000 24.48096 ? 395 HOH   A O     1 
HETATM 5643 O  O     . HOH   K 6 .   ? -15.90400 3.34300  -16.54800 1.000 31.61624 ? 396 HOH   A O     1 
HETATM 5644 O  O     . HOH   K 6 .   ? -11.98900 30.44000 -17.55700 1.000 39.17629 ? 397 HOH   A O     1 
HETATM 5645 O  O     . HOH   K 6 .   ? -38.16800 14.47900 -34.99100 1.000 55.49859 ? 398 HOH   A O     1 
HETATM 5646 O  O     . HOH   K 6 .   ? -13.40100 4.74400  -26.40400 1.000 42.31273 ? 399 HOH   A O     1 
HETATM 5647 O  O     . HOH   K 6 .   ? -11.83400 11.25700 -43.78000 1.000 32.75041 ? 400 HOH   A O     1 
HETATM 5648 O  O     . HOH   K 6 .   ? -34.36200 14.60000 -26.58700 1.000 33.88247 ? 401 HOH   A O     1 
HETATM 5649 O  O     . HOH   K 6 .   ? -9.09200  18.63700 -41.20000 1.000 51.96049 ? 402 HOH   A O     1 
HETATM 5650 O  O     . HOH   K 6 .   ? -0.01000  18.00700 -19.92300 1.000 55.62726 ? 403 HOH   A O     1 
HETATM 5651 O  O     . HOH   K 6 .   ? -23.44900 2.33800  -35.29500 1.000 60.39431 ? 404 HOH   A O     1 
HETATM 5652 O  O     . HOH   K 6 .   ? -7.87500  23.79600 -21.01700 1.000 28.23858 ? 405 HOH   A O     1 
HETATM 5653 O  O     . HOH   K 6 .   ? -1.21800  10.41900 -19.36500 1.000 54.62452 ? 406 HOH   A O     1 
HETATM 5654 O  O     . HOH   K 6 .   ? -14.43700 18.06400 -41.44500 1.000 22.98951 ? 407 HOH   A O     1 
HETATM 5655 O  O     . HOH   K 6 .   ? -16.23400 2.09700  -12.84600 1.000 35.53065 ? 408 HOH   A O     1 
HETATM 5656 O  O     . HOH   K 6 .   ? -18.32400 22.58300 -19.09300 1.000 19.61062 ? 409 HOH   A O     1 
HETATM 5657 O  O     . HOH   K 6 .   ? -4.93200  14.81300 -30.71500 1.000 51.09855 ? 410 HOH   A O     1 
HETATM 5658 O  O     . HOH   K 6 .   ? -7.58000  4.44200  -37.43400 1.000 49.76712 ? 411 HOH   A O     1 
HETATM 5659 O  O     . HOH   K 6 .   ? -32.94400 21.77600 -20.24200 1.000 55.91019 ? 412 HOH   A O     1 
HETATM 5660 O  O     . HOH   K 6 .   ? -10.34600 6.23100  -35.83700 1.000 42.74152 ? 413 HOH   A O     1 
HETATM 5661 O  O     . HOH   K 6 .   ? -16.71300 26.63700 -21.30900 1.000 20.50381 ? 414 HOH   A O     1 
HETATM 5662 O  O     A HOH   K 6 .   ? -28.08300 15.95900 -13.27200 0.500 36.82051 ? 415 HOH   A O     1 
HETATM 5663 O  O     B HOH   K 6 .   ? -28.94700 14.05800 -13.49300 0.500 35.51871 ? 415 HOH   A O     1 
HETATM 5664 O  O     . HOH   K 6 .   ? -26.61200 21.17400 -39.81300 1.000 27.42388 ? 416 HOH   A O     1 
HETATM 5665 O  O     . HOH   K 6 .   ? -17.98000 22.14200 -8.21300  1.000 22.06159 ? 417 HOH   A O     1 
HETATM 5666 O  O     . HOH   K 6 .   ? -21.38800 24.31200 -31.36400 1.000 15.64217 ? 418 HOH   A O     1 
HETATM 5667 O  O     . HOH   K 6 .   ? -16.65900 4.21100  -21.88000 1.000 42.51840 ? 419 HOH   A O     1 
HETATM 5668 O  O     . HOH   K 6 .   ? -23.90200 1.61400  -26.09000 1.000 39.76514 ? 420 HOH   A O     1 
HETATM 5669 O  O     . HOH   K 6 .   ? -17.74500 2.57200  -43.31500 1.000 40.12922 ? 421 HOH   A O     1 
HETATM 5670 O  O     . HOH   K 6 .   ? -11.54400 5.73100  -32.15800 1.000 40.16575 ? 422 HOH   A O     1 
HETATM 5671 O  O     . HOH   K 6 .   ? -12.32600 20.86100 -13.86700 1.000 25.40002 ? 423 HOH   A O     1 
HETATM 5672 O  O     A HOH   K 6 .   ? -34.13200 6.59100  -23.54200 0.500 36.28503 ? 424 HOH   A O     1 
HETATM 5673 O  O     B HOH   K 6 .   ? -33.57800 5.49800  -24.53900 0.500 43.79988 ? 424 HOH   A O     1 
HETATM 5674 O  O     . HOH   K 6 .   ? -5.46400  23.00400 -37.36800 1.000 49.84365 ? 425 HOH   A O     1 
HETATM 5675 O  O     . HOH   K 6 .   ? -40.73300 11.91100 -28.90200 1.000 49.10881 ? 426 HOH   A O     1 
HETATM 5676 O  O     . HOH   K 6 .   ? -32.62000 13.25500 -39.23800 1.000 25.08679 ? 427 HOH   A O     1 
HETATM 5677 O  O     . HOH   K 6 .   ? -7.17200  27.45200 -23.01600 1.000 28.78788 ? 428 HOH   A O     1 
HETATM 5678 O  O     . HOH   K 6 .   ? -26.09200 15.32500 -46.43300 1.000 21.35168 ? 429 HOH   A O     1 
HETATM 5679 O  O     . HOH   K 6 .   ? -17.89500 0.80500  -26.21700 1.000 33.17101 ? 430 HOH   A O     1 
HETATM 5680 O  O     . HOH   K 6 .   ? -32.06100 17.55000 -37.53500 1.000 48.45693 ? 431 HOH   A O     1 
HETATM 5681 O  O     . HOH   K 6 .   ? -28.90400 22.11700 -15.05700 1.000 50.99420 ? 432 HOH   A O     1 
HETATM 5682 O  O     . HOH   K 6 .   ? -20.51700 3.23100  -43.08400 1.000 35.37643 ? 433 HOH   A O     1 
HETATM 5683 O  O     . HOH   K 6 .   ? -35.96200 10.64400 -35.45000 1.000 42.30517 ? 434 HOH   A O     1 
HETATM 5684 O  O     . HOH   K 6 .   ? -31.91500 2.25400  -39.61900 1.000 48.66469 ? 435 HOH   A O     1 
HETATM 5685 O  O     . HOH   K 6 .   ? -25.48400 13.83300 -9.84000  1.000 32.60550 ? 436 HOH   A O     1 
HETATM 5686 O  O     . HOH   K 6 .   ? -5.93700  26.53800 -35.67300 1.000 26.78651 ? 437 HOH   A O     1 
HETATM 5687 O  O     . HOH   K 6 .   ? -16.73000 29.45200 -32.74800 1.000 48.71778 ? 438 HOH   A O     1 
HETATM 5688 O  O     . HOH   K 6 .   ? -24.09600 14.75300 -7.09600  1.000 34.01654 ? 439 HOH   A O     1 
HETATM 5689 O  O     . HOH   K 6 .   ? -33.26300 24.86700 -22.17500 1.000 41.02167 ? 440 HOH   A O     1 
HETATM 5690 O  O     . HOH   K 6 .   ? -10.90900 26.00100 -42.76100 1.000 54.16082 ? 441 HOH   A O     1 
HETATM 5691 O  O     . HOH   K 6 .   ? -31.48300 22.13000 -36.95000 1.000 31.98070 ? 442 HOH   A O     1 
HETATM 5692 O  O     . HOH   K 6 .   ? -18.26700 3.61000  -32.20100 1.000 37.00197 ? 443 HOH   A O     1 
HETATM 5693 O  O     . HOH   K 6 .   ? -12.18700 6.14300  -6.05800  1.000 57.59286 ? 444 HOH   A O     1 
HETATM 5694 O  O     . HOH   K 6 .   ? -24.42100 26.47400 -40.09000 1.000 53.92035 ? 445 HOH   A O     1 
HETATM 5695 O  O     . HOH   K 6 .   ? -28.23600 27.51500 -33.95200 1.000 28.07786 ? 446 HOH   A O     1 
HETATM 5696 O  O     . HOH   K 6 .   ? -25.41400 17.97700 -46.15000 1.000 20.46866 ? 447 HOH   A O     1 
HETATM 5697 O  O     . HOH   K 6 .   ? -27.57000 20.29400 -13.59100 1.000 37.59307 ? 448 HOH   A O     1 
HETATM 5698 O  O     . HOH   K 6 .   ? -22.07600 6.26100  -12.92600 1.000 46.42212 ? 449 HOH   A O     1 
HETATM 5699 O  O     . HOH   K 6 .   ? -22.13600 38.11300 -34.21100 1.000 63.56546 ? 450 HOH   A O     1 
HETATM 5700 O  O     . HOH   K 6 .   ? -6.85400  29.76200 -24.09900 1.000 40.35515 ? 451 HOH   A O     1 
HETATM 5701 O  O     . HOH   K 6 .   ? -35.42900 15.19800 -36.08900 1.000 34.87166 ? 452 HOH   A O     1 
HETATM 5702 O  O     . HOH   K 6 .   ? -22.29900 3.87000  -24.30600 1.000 26.05023 ? 453 HOH   A O     1 
HETATM 5703 O  O     . HOH   K 6 .   ? -33.25300 13.53300 -36.38900 1.000 26.68774 ? 454 HOH   A O     1 
HETATM 5704 O  O     . HOH   K 6 .   ? -15.98200 3.61300  -30.89200 1.000 34.97900 ? 455 HOH   A O     1 
HETATM 5705 O  O     . HOH   K 6 .   ? -28.39600 4.45900  -42.76100 1.000 44.40440 ? 456 HOH   A O     1 
HETATM 5706 O  O     . HOH   K 6 .   ? -6.09900  20.55600 -13.46200 1.000 37.37134 ? 457 HOH   A O     1 
HETATM 5707 O  O     . HOH   K 6 .   ? -10.24900 32.84500 -20.15700 1.000 37.78998 ? 458 HOH   A O     1 
HETATM 5708 O  O     . HOH   K 6 .   ? -36.67800 7.97500  -23.71100 1.000 50.03627 ? 459 HOH   A O     1 
HETATM 5709 O  O     . HOH   K 6 .   ? -24.32900 25.00400 -42.26200 1.000 50.92349 ? 460 HOH   A O     1 
HETATM 5710 O  O     . HOH   K 6 .   ? -39.96700 21.90500 -27.54100 1.000 50.67125 ? 461 HOH   A O     1 
HETATM 5711 O  O     . HOH   K 6 .   ? -39.79000 19.25500 -33.64000 1.000 51.49804 ? 462 HOH   A O     1 
HETATM 5712 O  O     . HOH   K 6 .   ? -11.72700 8.52400  -14.18800 1.000 34.01934 ? 463 HOH   A O     1 
HETATM 5713 O  O     . HOH   K 6 .   ? -27.12200 32.91700 -34.58500 1.000 30.59570 ? 464 HOH   A O     1 
HETATM 5714 O  O     . HOH   K 6 .   ? -18.46600 38.28300 -31.19000 1.000 37.29173 ? 465 HOH   A O     1 
HETATM 5715 O  O     . HOH   K 6 .   ? -21.55500 8.52200  -8.26600  1.000 52.39090 ? 466 HOH   A O     1 
HETATM 5716 O  O     . HOH   K 6 .   ? -27.75000 32.49800 -39.60600 1.000 54.42676 ? 467 HOH   A O     1 
HETATM 5717 O  O     . HOH   K 6 .   ? -7.71000  32.84700 -26.70600 1.000 25.17252 ? 468 HOH   A O     1 
HETATM 5718 O  O     . HOH   K 6 .   ? -38.98700 11.51600 -22.48000 1.000 58.15931 ? 469 HOH   A O     1 
HETATM 5719 O  O     . HOH   K 6 .   ? 0.79500   22.31000 -28.78700 1.000 44.48795 ? 470 HOH   A O     1 
HETATM 5720 O  O     . HOH   K 6 .   ? -14.59500 2.05200  -24.31500 1.000 41.33049 ? 471 HOH   A O     1 
HETATM 5721 O  O     . HOH   K 6 .   ? -29.10900 25.64300 -18.30400 1.000 50.91416 ? 472 HOH   A O     1 
HETATM 5722 O  O     . HOH   K 6 .   ? -41.75900 14.84500 -29.30800 1.000 59.85605 ? 473 HOH   A O     1 
HETATM 5723 O  O     . HOH   K 6 .   ? -30.07300 23.32700 -16.72300 1.000 54.12593 ? 474 HOH   A O     1 
HETATM 5724 O  O     . HOH   K 6 .   ? -23.00900 9.86800  -4.00600  1.000 51.08435 ? 475 HOH   A O     1 
HETATM 5725 O  O     . HOH   K 6 .   ? -20.27200 37.05300 -28.73800 1.000 31.73305 ? 476 HOH   A O     1 
HETATM 5726 O  O     . HOH   K 6 .   ? -26.59500 20.87100 -43.25200 1.000 38.39679 ? 477 HOH   A O     1 
HETATM 5727 O  O     . HOH   K 6 .   ? -3.75600  4.81200  -41.90600 1.000 65.32902 ? 478 HOH   A O     1 
HETATM 5728 O  O     . HOH   K 6 .   ? -20.87400 24.30700 -13.16900 1.000 41.33704 ? 479 HOH   A O     1 
HETATM 5729 O  O     . HOH   K 6 .   ? -30.39900 15.38900 -42.29700 1.000 45.76954 ? 480 HOH   A O     1 
HETATM 5730 O  O     . HOH   K 6 .   ? -5.07100  8.34200  -17.21100 1.000 54.03934 ? 481 HOH   A O     1 
HETATM 5731 O  O     . HOH   K 6 .   ? -9.84100  21.48400 -12.67800 1.000 43.50522 ? 482 HOH   A O     1 
HETATM 5732 O  O     . HOH   K 6 .   ? -6.93800  19.80200 -19.51300 1.000 43.31186 ? 483 HOH   A O     1 
HETATM 5733 O  O     . HOH   K 6 .   ? -27.63900 25.58800 -14.91700 1.000 51.03501 ? 484 HOH   A O     1 
HETATM 5734 O  O     . HOH   K 6 .   ? -16.02700 0.67400  -40.82600 1.000 38.71851 ? 485 HOH   A O     1 
HETATM 5735 O  O     . HOH   K 6 .   ? -6.11400  14.54500 -28.16800 1.000 36.56647 ? 486 HOH   A O     1 
HETATM 5736 O  O     . HOH   K 6 .   ? -20.70500 12.46200 -3.21700  1.000 33.14157 ? 487 HOH   A O     1 
HETATM 5737 O  O     . HOH   K 6 .   ? -9.36900  12.11600 -43.06600 1.000 44.13528 ? 488 HOH   A O     1 
HETATM 5738 O  O     A HOH   K 6 .   ? -15.88500 11.05000 -3.81400  0.500 38.50348 ? 489 HOH   A O     1 
HETATM 5739 O  O     B HOH   K 6 .   ? -15.01500 10.51200 -2.29000  0.500 55.08486 ? 489 HOH   A O     1 
HETATM 5740 O  O     . HOH   K 6 .   ? -3.99000  2.33800  -40.78200 1.000 59.02912 ? 490 HOH   A O     1 
HETATM 5741 O  O     . HOH   K 6 .   ? -12.95400 13.66300 -44.74600 1.000 67.79141 ? 491 HOH   A O     1 
HETATM 5742 O  O     . HOH   K 6 .   ? -39.35200 9.26000  -27.97000 1.000 55.72761 ? 492 HOH   A O     1 
HETATM 5743 O  O     . HOH   K 6 .   ? -22.66200 1.48900  -41.28600 1.000 64.43964 ? 493 HOH   A O     1 
HETATM 5744 O  O     . HOH   K 6 .   ? -19.15100 27.48400 -35.01200 1.000 58.92116 ? 494 HOH   A O     1 
HETATM 5745 O  O     . HOH   K 6 .   ? -36.16400 17.13200 -22.38100 1.000 50.37035 ? 495 HOH   A O     1 
HETATM 5746 O  O     . HOH   K 6 .   ? -7.90400  7.96000  -18.10000 1.000 38.37358 ? 496 HOH   A O     1 
HETATM 5747 O  O     . HOH   K 6 .   ? -4.42200  17.37100 -38.23500 1.000 43.35373 ? 497 HOH   A O     1 
HETATM 5748 O  O     . HOH   K 6 .   ? -25.51200 14.13800 -48.98600 1.000 26.72596 ? 498 HOH   A O     1 
HETATM 5749 O  O     . HOH   K 6 .   ? -27.30700 19.59400 -45.22500 1.000 35.36454 ? 499 HOH   A O     1 
HETATM 5750 O  O     . HOH   K 6 .   ? -26.28100 1.44900  -24.44600 1.000 44.81346 ? 500 HOH   A O     1 
HETATM 5751 O  O     . HOH   K 6 .   ? -3.83200  9.49800  -40.33600 1.000 44.37157 ? 501 HOH   A O     1 
HETATM 5752 O  O     . HOH   K 6 .   ? -28.25400 30.22600 -35.19300 1.000 31.79722 ? 502 HOH   A O     1 
HETATM 5753 O  O     A HOH   K 6 .   ? -15.19900 0.72200  -16.86200 0.500 23.68548 ? 503 HOH   A O     1 
HETATM 5754 O  O     B HOH   K 6 .   ? -15.01200 0.06500  -14.96100 0.500 38.57247 ? 503 HOH   A O     1 
HETATM 5755 O  O     . HOH   K 6 .   ? -20.48300 23.63900 -17.61500 1.000 42.76624 ? 504 HOH   A O     1 
HETATM 5756 O  O     . HOH   K 6 .   ? -5.91500  21.70900 -23.87800 1.000 37.44610 ? 505 HOH   A O     1 
HETATM 5757 O  O     . HOH   K 6 .   ? -6.07500  26.10300 -38.24300 1.000 48.10505 ? 506 HOH   A O     1 
HETATM 5758 O  O     . HOH   K 6 .   ? -26.12100 23.37100 -13.27500 1.000 46.87021 ? 507 HOH   A O     1 
HETATM 5759 O  O     . HOH   K 6 .   ? -8.20500  32.63300 -31.12900 1.000 47.72728 ? 508 HOH   A O     1 
HETATM 5760 O  O     . HOH   K 6 .   ? -32.23300 20.90800 -24.60800 1.000 32.02796 ? 509 HOH   A O     1 
HETATM 5761 O  O     . HOH   K 6 .   ? -8.83100  5.99500  -32.00400 1.000 67.75358 ? 510 HOH   A O     1 
HETATM 5762 O  O     . HOH   K 6 .   ? -33.05300 16.04300 -39.50400 1.000 47.10793 ? 511 HOH   A O     1 
HETATM 5763 O  O     . HOH   K 6 .   ? -7.42100  6.42500  -19.84700 1.000 54.98745 ? 512 HOH   A O     1 
HETATM 5764 O  O     . HOH   K 6 .   ? -24.52500 7.45700  -13.44900 1.000 56.05517 ? 513 HOH   A O     1 
HETATM 5765 O  O     . HOH   K 6 .   ? -33.80600 21.76800 -22.54100 1.000 52.77094 ? 514 HOH   A O     1 
HETATM 5766 O  O     . HOH   K 6 .   ? -3.70500  22.09600 -20.28700 1.000 57.19228 ? 515 HOH   A O     1 
HETATM 5767 O  O     . HOH   K 6 .   ? -12.16000 4.96000  -35.61000 1.000 44.34645 ? 516 HOH   A O     1 
HETATM 5768 O  O     . HOH   K 6 .   ? -23.61700 27.05700 -14.85800 1.000 44.13942 ? 517 HOH   A O     1 
HETATM 5769 O  O     . HOH   K 6 .   ? -16.69000 24.80400 -19.38600 1.000 29.81232 ? 518 HOH   A O     1 
HETATM 5770 O  O     . HOH   K 6 .   ? -15.42800 1.40700  -21.83700 1.000 38.83564 ? 519 HOH   A O     1 
HETATM 5771 O  O     . HOH   K 6 .   ? -32.97600 19.43100 -36.22300 1.000 37.08072 ? 520 HOH   A O     1 
HETATM 5772 O  O     . HOH   K 6 .   ? -18.57800 10.64300 -3.20300  1.000 43.98030 ? 521 HOH   A O     1 
HETATM 5773 O  O     . HOH   K 6 .   ? -9.41200  19.61500 -11.10800 1.000 31.56011 ? 522 HOH   A O     1 
HETATM 5774 O  O     . HOH   K 6 .   ? -9.22400  5.82400  -26.93400 1.000 55.84215 ? 523 HOH   A O     1 
HETATM 5775 O  O     . HOH   K 6 .   ? -36.08500 19.55000 -24.78500 1.000 62.19543 ? 524 HOH   A O     1 
HETATM 5776 O  O     . HOH   K 6 .   ? -5.08000  24.10400 -22.41400 1.000 56.61580 ? 525 HOH   A O     1 
HETATM 5777 O  O     . HOH   K 6 .   ? -33.57600 19.36700 -26.24900 1.000 30.88258 ? 526 HOH   A O     1 
HETATM 5778 O  O     . HOH   K 6 .   ? -10.70900 18.14100 -43.28500 1.000 57.89727 ? 527 HOH   A O     1 
HETATM 5779 O  O     . HOH   K 6 .   ? -8.16100  14.89600 -43.81700 1.000 60.12415 ? 528 HOH   A O     1 
HETATM 5780 O  O     . HOH   K 6 .   ? -8.19800  5.58700  -22.24100 1.000 51.50380 ? 529 HOH   A O     1 
HETATM 5781 O  O     . HOH   K 6 .   ? -25.61700 3.35400  -45.90800 1.000 41.41575 ? 530 HOH   A O     1 
HETATM 5782 O  O     . HOH   K 6 .   ? -18.87100 0.68200  -23.45600 1.000 72.11208 ? 531 HOH   A O     1 
HETATM 5783 O  O     . HOH   K 6 .   ? -4.25200  20.89100 -15.54200 1.000 34.74535 ? 532 HOH   A O     1 
HETATM 5784 O  O     . HOH   K 6 .   ? -5.88800  7.31000  -33.48000 1.000 41.44947 ? 533 HOH   A O     1 
HETATM 5785 O  O     . HOH   K 6 .   ? -12.50500 2.73300  -24.96800 1.000 48.09082 ? 534 HOH   A O     1 
HETATM 5786 O  O     . HOH   K 6 .   ? -30.25500 1.32300  -33.99900 1.000 41.99520 ? 535 HOH   A O     1 
HETATM 5787 O  O     . HOH   K 6 .   ? -21.22000 13.94000 -50.63800 1.000 50.86822 ? 536 HOH   A O     1 
HETATM 5788 O  O     . HOH   K 6 .   ? -6.36500  32.20800 -22.72900 1.000 25.44548 ? 537 HOH   A O     1 
HETATM 5789 O  O     . HOH   K 6 .   ? -5.41500  21.51000 -18.16200 1.000 57.69725 ? 538 HOH   A O     1 
HETATM 5790 O  O     A HOH   K 6 .   ? -25.68800 9.93800  -7.54900  0.500 39.52580 ? 539 HOH   A O     1 
HETATM 5791 O  O     B HOH   K 6 .   ? -26.83900 8.27600  -7.26600  0.500 38.64036 ? 539 HOH   A O     1 
HETATM 5792 O  O     . HOH   K 6 .   ? -33.35000 24.98200 -40.52900 1.000 32.04093 ? 540 HOH   A O     1 
HETATM 5793 O  O     . HOH   K 6 .   ? -19.93600 -0.23000 -27.71300 1.000 53.09139 ? 541 HOH   A O     1 
HETATM 5794 O  O     . HOH   K 6 .   ? -33.70700 22.68000 -38.55600 1.000 57.17833 ? 542 HOH   A O     1 
HETATM 5795 O  O     . HOH   K 6 .   ? -7.23100  1.85900  -40.96200 1.000 51.19803 ? 543 HOH   A O     1 
HETATM 5796 O  O     . HOH   K 6 .   ? -0.54200  20.54200 -17.99500 1.000 47.68535 ? 544 HOH   A O     1 
HETATM 5797 O  O     . HOH   K 6 .   ? -7.66700  31.55800 -20.34200 1.000 24.09815 ? 545 HOH   A O     1 
HETATM 5798 O  O     . HOH   K 6 .   ? -12.70700 17.08600 -43.23300 1.000 43.07220 ? 546 HOH   A O     1 
HETATM 5799 O  O     . HOH   K 6 .   ? -36.69200 11.13700 -38.06600 1.000 45.57289 ? 547 HOH   A O     1 
HETATM 5800 O  O     . HOH   K 6 .   ? -11.14300 5.09000  -28.29800 1.000 50.68130 ? 548 HOH   A O     1 
HETATM 5801 O  O     . HOH   K 6 .   ? -2.85900  27.51900 -21.26300 1.000 60.21622 ? 549 HOH   A O     1 
HETATM 5802 O  O     . HOH   K 6 .   ? -5.23700  21.29900 -10.70500 1.000 46.89520 ? 550 HOH   A O     1 
HETATM 5803 O  O     . HOH   K 6 .   ? -13.84200 -2.21200 -13.38400 1.000 49.34024 ? 551 HOH   A O     1 
HETATM 5804 O  O     . HOH   L 6 .   ? -19.03300 28.10600 14.79900  1.000 39.23519 ? 301 HOH   B O     1 
HETATM 5805 O  O     . HOH   L 6 .   ? -23.72300 44.19800 17.91100  1.000 61.03488 ? 302 HOH   B O     1 
HETATM 5806 O  O     . HOH   L 6 .   ? -18.94200 35.28600 18.82700  1.000 48.55466 ? 303 HOH   B O     1 
HETATM 5807 O  O     . HOH   L 6 .   ? -13.09300 15.76900 3.11200   1.000 42.49200 ? 304 HOH   B O     1 
HETATM 5808 O  O     . HOH   L 6 .   ? -30.23500 29.71700 -5.74000  1.000 34.88946 ? 305 HOH   B O     1 
HETATM 5809 O  O     . HOH   L 6 .   ? -22.05200 25.35800 4.72600   1.000 35.19362 ? 306 HOH   B O     1 
HETATM 5810 O  O     . HOH   L 6 .   ? -39.44500 27.75100 -0.12600  1.000 30.83200 ? 307 HOH   B O     1 
HETATM 5811 O  O     . HOH   L 6 .   ? -25.29700 41.84700 -17.86400 1.000 48.14194 ? 308 HOH   B O     1 
HETATM 5812 O  O     . HOH   L 6 .   ? -10.37500 32.97800 -14.45800 1.000 20.09925 ? 309 HOH   B O     1 
HETATM 5813 O  O     . HOH   L 6 .   ? -11.82500 23.61900 9.90200   1.000 48.06625 ? 310 HOH   B O     1 
HETATM 5814 O  O     . HOH   L 6 .   ? -28.92300 37.70100 -15.43300 1.000 46.32722 ? 311 HOH   B O     1 
HETATM 5815 O  O     . HOH   L 6 .   ? -21.98100 19.17800 -7.45100  1.000 51.47736 ? 312 HOH   B O     1 
HETATM 5816 O  O     . HOH   L 6 .   ? -27.61800 28.89700 -0.99600  1.000 18.68090 ? 313 HOH   B O     1 
HETATM 5817 O  O     . HOH   L 6 .   ? -13.35600 43.27500 -22.11700 1.000 32.93474 ? 314 HOH   B O     1 
HETATM 5818 O  O     . HOH   L 6 .   ? -31.89600 27.84500 -3.58400  1.000 45.01541 ? 315 HOH   B O     1 
HETATM 5819 O  O     . HOH   L 6 .   ? -9.33500  43.72700 5.30600   1.000 31.35458 ? 316 HOH   B O     1 
HETATM 5820 O  O     . HOH   L 6 .   ? -35.22100 23.93400 -2.64800  1.000 55.44829 ? 317 HOH   B O     1 
HETATM 5821 O  O     . HOH   L 6 .   ? -19.53900 48.24300 -0.84800  1.000 51.11950 ? 318 HOH   B O     1 
HETATM 5822 O  O     . HOH   L 6 .   ? 2.21400   23.17000 -1.85100  1.000 28.42479 ? 319 HOH   B O     1 
HETATM 5823 O  O     . HOH   L 6 .   ? -24.65200 27.75600 11.74100  1.000 51.97698 ? 320 HOH   B O     1 
HETATM 5824 O  O     . HOH   L 6 .   ? -27.59400 29.77600 10.45100  1.000 44.81891 ? 321 HOH   B O     1 
HETATM 5825 O  O     . HOH   L 6 .   ? -6.32300  32.01800 7.76000   1.000 47.25120 ? 322 HOH   B O     1 
HETATM 5826 O  O     . HOH   L 6 .   ? -0.38600  34.84700 -9.45300  1.000 46.82705 ? 323 HOH   B O     1 
HETATM 5827 O  O     . HOH   L 6 .   ? -21.37100 39.08100 18.33000  1.000 61.87910 ? 324 HOH   B O     1 
HETATM 5828 O  O     . HOH   L 6 .   ? -30.64800 20.75900 8.17100   1.000 32.89494 ? 325 HOH   B O     1 
HETATM 5829 O  O     . HOH   L 6 .   ? -4.57300  42.55500 6.57800   1.000 53.13212 ? 326 HOH   B O     1 
HETATM 5830 O  O     . HOH   L 6 .   ? -10.57700 44.01500 -3.85200  1.000 40.64614 ? 327 HOH   B O     1 
HETATM 5831 O  O     . HOH   L 6 .   ? -8.81000  37.75600 -1.12400  1.000 23.62231 ? 328 HOH   B O     1 
HETATM 5832 O  O     . HOH   L 6 .   ? -28.21800 45.43200 17.88700  1.000 37.55282 ? 329 HOH   B O     1 
HETATM 5833 O  O     . HOH   L 6 .   ? -29.60800 35.93500 16.44700  1.000 25.01619 ? 330 HOH   B O     1 
HETATM 5834 O  O     . HOH   L 6 .   ? -35.18800 34.47600 -0.10500  1.000 31.53309 ? 331 HOH   B O     1 
HETATM 5835 O  O     . HOH   L 6 .   ? -10.81500 18.81200 3.48300   1.000 31.85686 ? 332 HOH   B O     1 
HETATM 5836 O  O     . HOH   L 6 .   ? -32.78700 37.89100 -3.77600  1.000 33.09477 ? 333 HOH   B O     1 
HETATM 5837 O  O     . HOH   L 6 .   ? -8.17300  30.96700 -14.16500 1.000 65.89690 ? 334 HOH   B O     1 
HETATM 5838 O  O     . HOH   L 6 .   ? -17.50700 47.50200 -6.43000  1.000 40.29154 ? 335 HOH   B O     1 
HETATM 5839 O  O     . HOH   L 6 .   ? -8.88900  30.06100 11.60800  1.000 54.76972 ? 336 HOH   B O     1 
HETATM 5840 O  O     . HOH   L 6 .   ? -23.96900 42.93700 -11.94700 1.000 49.60872 ? 337 HOH   B O     1 
HETATM 5841 O  O     . HOH   L 6 .   ? -37.14500 37.93400 4.87800   1.000 57.84915 ? 338 HOH   B O     1 
HETATM 5842 O  O     . HOH   L 6 .   ? -30.09600 24.35800 2.54400   1.000 23.59757 ? 339 HOH   B O     1 
HETATM 5843 O  O     . HOH   L 6 .   ? -28.76800 22.70400 -9.71000  1.000 41.05667 ? 340 HOH   B O     1 
HETATM 5844 O  O     . HOH   L 6 .   ? -34.52100 31.61200 -0.36400  1.000 23.38468 ? 341 HOH   B O     1 
HETATM 5845 O  O     . HOH   L 6 .   ? -24.60500 22.49700 -1.95300  1.000 18.11463 ? 342 HOH   B O     1 
HETATM 5846 O  O     . HOH   L 6 .   ? -9.54900  35.32000 -21.29700 1.000 18.36356 ? 343 HOH   B O     1 
HETATM 5847 O  O     . HOH   L 6 .   ? -35.65800 45.36400 6.50600   1.000 45.44172 ? 344 HOH   B O     1 
HETATM 5848 O  O     . HOH   L 6 .   ? -10.50100 26.80900 -10.56300 1.000 49.82015 ? 345 HOH   B O     1 
HETATM 5849 O  O     . HOH   L 6 .   ? -30.90700 39.11900 16.28100  1.000 27.07786 ? 346 HOH   B O     1 
HETATM 5850 O  O     . HOH   L 6 .   ? -4.54900  30.08600 -4.25700  1.000 50.50702 ? 347 HOH   B O     1 
HETATM 5851 O  O     . HOH   L 6 .   ? -19.49500 43.64400 -22.43200 1.000 41.36483 ? 348 HOH   B O     1 
HETATM 5852 O  O     . HOH   L 6 .   ? -25.05700 25.85100 8.36000   1.000 32.09477 ? 349 HOH   B O     1 
HETATM 5853 O  O     . HOH   L 6 .   ? -28.12500 35.33100 -16.26600 1.000 37.60807 ? 350 HOH   B O     1 
HETATM 5854 O  O     . HOH   L 6 .   ? -22.83600 30.96300 19.35600  1.000 50.51840 ? 351 HOH   B O     1 
HETATM 5855 O  O     . HOH   L 6 .   ? -16.55800 24.59600 -7.73400  1.000 20.48238 ? 352 HOH   B O     1 
HETATM 5856 O  O     . HOH   L 6 .   ? -21.44600 42.56100 -21.00100 1.000 49.90035 ? 353 HOH   B O     1 
HETATM 5857 O  O     . HOH   L 6 .   ? -21.73900 31.73600 7.80300   1.000 22.33899 ? 354 HOH   B O     1 
HETATM 5858 O  O     . HOH   L 6 .   ? -10.71000 44.74000 7.40700   1.000 46.63367 ? 355 HOH   B O     1 
HETATM 5859 O  O     . HOH   L 6 .   ? -6.32400  38.43800 -3.94300  1.000 27.83458 ? 356 HOH   B O     1 
HETATM 5860 O  O     . HOH   L 6 .   ? -6.70400  34.25200 1.30000   1.000 37.16112 ? 357 HOH   B O     1 
HETATM 5861 O  O     . HOH   L 6 .   ? -5.85000  35.99900 -3.03400  1.000 46.16462 ? 358 HOH   B O     1 
HETATM 5862 O  O     . HOH   L 6 .   ? -25.77000 46.43500 -5.55200  1.000 33.16554 ? 359 HOH   B O     1 
HETATM 5863 O  O     . HOH   L 6 .   ? -31.64500 29.25600 -0.08200  1.000 19.87432 ? 360 HOH   B O     1 
HETATM 5864 O  O     . HOH   L 6 .   ? -13.78300 15.33700 -2.95400  1.000 23.59795 ? 361 HOH   B O     1 
HETATM 5865 O  O     . HOH   L 6 .   ? -8.15500  31.02900 -7.45200  1.000 26.75602 ? 362 HOH   B O     1 
HETATM 5866 O  O     . HOH   L 6 .   ? -25.68400 23.47400 -9.68200  1.000 26.70999 ? 363 HOH   B O     1 
HETATM 5867 O  O     . HOH   L 6 .   ? -30.34600 35.74300 9.90400   1.000 32.24235 ? 364 HOH   B O     1 
HETATM 5868 O  O     . HOH   L 6 .   ? -8.15700  23.09100 -8.80900  1.000 34.18547 ? 365 HOH   B O     1 
HETATM 5869 O  O     . HOH   L 6 .   ? -11.91300 40.78400 -19.43200 1.000 19.28262 ? 366 HOH   B O     1 
HETATM 5870 O  O     . HOH   L 6 .   ? -31.20600 23.86300 -4.89600  1.000 20.49109 ? 367 HOH   B O     1 
HETATM 5871 O  O     . HOH   L 6 .   ? 0.26500   29.44900 0.51400   1.000 41.43860 ? 368 HOH   B O     1 
HETATM 5872 O  O     . HOH   L 6 .   ? -10.55800 44.88600 -11.94000 1.000 23.46958 ? 369 HOH   B O     1 
HETATM 5873 O  O     . HOH   L 6 .   ? -23.45700 21.65900 0.42700   1.000 26.29691 ? 370 HOH   B O     1 
HETATM 5874 O  O     . HOH   L 6 .   ? -36.55000 29.84500 -5.15400  1.000 45.65529 ? 371 HOH   B O     1 
HETATM 5875 O  O     . HOH   L 6 .   ? -10.03000 48.60700 -10.08500 1.000 28.54650 ? 372 HOH   B O     1 
HETATM 5876 O  O     . HOH   L 6 .   ? -4.91300  39.83100 -13.38100 1.000 24.74752 ? 373 HOH   B O     1 
HETATM 5877 O  O     A HOH   L 6 .   ? -8.44000  27.69900 -8.21400  0.500 30.44656 ? 374 HOH   B O     1 
HETATM 5878 O  O     B HOH   L 6 .   ? -7.88500  29.31500 -9.35900  0.500 35.55940 ? 374 HOH   B O     1 
HETATM 5879 O  O     . HOH   L 6 .   ? -19.75400 47.93500 -13.68200 1.000 43.93386 ? 375 HOH   B O     1 
HETATM 5880 O  O     . HOH   L 6 .   ? -17.99500 29.16400 -20.74700 1.000 21.03643 ? 376 HOH   B O     1 
HETATM 5881 O  O     . HOH   L 6 .   ? -18.83700 13.93400 4.83000   1.000 45.05146 ? 377 HOH   B O     1 
HETATM 5882 O  O     . HOH   L 6 .   ? -33.30700 37.35500 10.23200  1.000 41.51736 ? 378 HOH   B O     1 
HETATM 5883 O  O     . HOH   L 6 .   ? -18.55500 28.57700 -10.03600 1.000 27.87085 ? 379 HOH   B O     1 
HETATM 5884 O  O     . HOH   L 6 .   ? -21.88800 26.80300 2.28300   1.000 20.03330 ? 380 HOH   B O     1 
HETATM 5885 O  O     . HOH   L 6 .   ? -22.15100 44.91500 -16.34500 1.000 39.01118 ? 381 HOH   B O     1 
HETATM 5886 O  O     . HOH   L 6 .   ? -19.91300 23.60900 5.63900   1.000 59.34747 ? 382 HOH   B O     1 
HETATM 5887 O  O     . HOH   L 6 .   ? -2.52800  43.16700 -15.72300 1.000 33.00851 ? 383 HOH   B O     1 
HETATM 5888 O  O     . HOH   L 6 .   ? -24.52000 38.01900 20.08900  1.000 44.11700 ? 384 HOH   B O     1 
HETATM 5889 O  O     . HOH   L 6 .   ? -3.53700  21.20100 2.41800   1.000 32.26269 ? 385 HOH   B O     1 
HETATM 5890 O  O     . HOH   L 6 .   ? -15.09600 50.73300 -10.52000 1.000 19.29855 ? 386 HOH   B O     1 
HETATM 5891 O  O     . HOH   L 6 .   ? -7.30700  24.23000 -5.99700  1.000 28.88505 ? 387 HOH   B O     1 
HETATM 5892 O  O     . HOH   L 6 .   ? -7.26700  41.97600 0.42500   1.000 49.47798 ? 388 HOH   B O     1 
HETATM 5893 O  O     . HOH   L 6 .   ? -28.78900 15.24300 4.44900   1.000 15.47758 ? 389 HOH   B O     1 
HETATM 5894 O  O     . HOH   L 6 .   ? -28.76000 33.49500 9.35100   1.000 39.92367 ? 390 HOH   B O     1 
HETATM 5895 O  O     . HOH   L 6 .   ? -31.87300 28.63800 7.80600   1.000 48.19689 ? 391 HOH   B O     1 
HETATM 5896 O  O     . HOH   L 6 .   ? -36.25500 35.78600 6.71200   1.000 57.68289 ? 392 HOH   B O     1 
HETATM 5897 O  O     . HOH   L 6 .   ? -13.79400 19.26500 4.55400   1.000 38.81266 ? 393 HOH   B O     1 
HETATM 5898 O  O     . HOH   L 6 .   ? -25.72400 37.75700 -19.01300 1.000 34.52521 ? 394 HOH   B O     1 
HETATM 5899 O  O     . HOH   L 6 .   ? -17.19500 48.41200 -15.69900 1.000 39.27391 ? 395 HOH   B O     1 
HETATM 5900 O  O     . HOH   L 6 .   ? -19.58300 28.58300 17.41900  1.000 47.42634 ? 396 HOH   B O     1 
HETATM 5901 O  O     . HOH   L 6 .   ? -22.32700 26.58300 9.18000   1.000 57.32680 ? 397 HOH   B O     1 
HETATM 5902 O  O     . HOH   L 6 .   ? -28.57300 23.66200 4.58700   1.000 56.45947 ? 398 HOH   B O     1 
HETATM 5903 O  O     . HOH   L 6 .   ? -36.50000 40.15000 6.73700   1.000 46.55677 ? 399 HOH   B O     1 
HETATM 5904 O  O     . HOH   L 6 .   ? -12.63000 15.06000 -0.46500  1.000 31.15356 ? 400 HOH   B O     1 
HETATM 5905 O  O     . HOH   L 6 .   ? -24.96200 49.46800 -3.03000  1.000 41.29160 ? 401 HOH   B O     1 
HETATM 5906 O  O     . HOH   L 6 .   ? -27.69200 30.97200 -15.57600 1.000 37.39407 ? 402 HOH   B O     1 
HETATM 5907 O  O     . HOH   L 6 .   ? -33.16000 33.60500 8.27300   1.000 46.29376 ? 403 HOH   B O     1 
HETATM 5908 O  O     . HOH   L 6 .   ? -23.08200 47.27000 -4.59800  1.000 34.43236 ? 404 HOH   B O     1 
HETATM 5909 O  O     . HOH   L 6 .   ? -17.30700 48.15000 -12.55900 1.000 25.03599 ? 405 HOH   B O     1 
HETATM 5910 O  O     . HOH   L 6 .   ? -17.40000 49.19800 -9.91700  1.000 25.06261 ? 406 HOH   B O     1 
HETATM 5911 O  O     . HOH   L 6 .   ? -11.27000 42.26300 17.43300  1.000 59.14651 ? 407 HOH   B O     1 
HETATM 5912 O  O     . HOH   L 6 .   ? -16.35700 27.85600 15.67300  1.000 43.27716 ? 408 HOH   B O     1 
HETATM 5913 O  O     . HOH   L 6 .   ? -7.68900  18.88000 -2.83700  1.000 25.02722 ? 409 HOH   B O     1 
HETATM 5914 O  O     . HOH   L 6 .   ? -13.23400 46.53500 -4.66600  1.000 49.28981 ? 410 HOH   B O     1 
HETATM 5915 O  O     . HOH   L 6 .   ? -33.90000 37.41800 7.17700   1.000 45.88286 ? 411 HOH   B O     1 
HETATM 5916 O  O     . HOH   L 6 .   ? -7.84700  21.96500 8.59700   1.000 37.64993 ? 412 HOH   B O     1 
HETATM 5917 O  O     . HOH   L 6 .   ? -27.06900 35.34400 17.27800  1.000 26.52423 ? 413 HOH   B O     1 
HETATM 5918 O  O     . HOH   L 6 .   ? -12.03200 47.46300 12.48400  1.000 47.39013 ? 414 HOH   B O     1 
HETATM 5919 O  O     . HOH   L 6 .   ? -7.23100  21.75900 -5.10900  1.000 32.73898 ? 415 HOH   B O     1 
HETATM 5920 O  O     . HOH   L 6 .   ? -10.91500 33.27200 -17.87200 1.000 35.11431 ? 416 HOH   B O     1 
HETATM 5921 O  O     . HOH   L 6 .   ? -12.19000 45.57500 3.70500   1.000 42.13651 ? 417 HOH   B O     1 
HETATM 5922 O  O     . HOH   L 6 .   ? -11.32200 18.39600 -9.63200  1.000 19.12732 ? 418 HOH   B O     1 
HETATM 5923 O  O     . HOH   L 6 .   ? -28.84900 25.34800 -11.15300 1.000 46.01165 ? 419 HOH   B O     1 
HETATM 5924 O  O     . HOH   L 6 .   ? -33.45100 26.32900 -6.67800  1.000 50.67582 ? 420 HOH   B O     1 
HETATM 5925 O  O     . HOH   L 6 .   ? -22.08300 47.44400 -12.61200 1.000 65.86371 ? 421 HOH   B O     1 
HETATM 5926 O  O     . HOH   L 6 .   ? -27.44000 17.69400 5.07200   1.000 29.44507 ? 422 HOH   B O     1 
HETATM 5927 O  O     . HOH   L 6 .   ? -15.05200 32.82500 12.46100  1.000 27.75609 ? 423 HOH   B O     1 
HETATM 5928 O  O     . HOH   L 6 .   ? -37.34400 42.69300 -5.60100  1.000 44.49924 ? 424 HOH   B O     1 
HETATM 5929 O  O     . HOH   L 6 .   ? -13.49500 23.17500 8.01100   1.000 61.14415 ? 425 HOH   B O     1 
HETATM 5930 O  O     . HOH   L 6 .   ? -22.10900 28.44700 -13.42900 1.000 35.99672 ? 426 HOH   B O     1 
HETATM 5931 O  O     . HOH   L 6 .   ? -13.03400 29.95900 -15.09600 1.000 23.60702 ? 427 HOH   B O     1 
HETATM 5932 O  O     . HOH   L 6 .   ? -34.20100 38.32500 12.53700  1.000 67.13851 ? 428 HOH   B O     1 
HETATM 5933 O  O     . HOH   L 6 .   ? -40.03700 31.91900 4.36700   1.000 47.61239 ? 429 HOH   B O     1 
HETATM 5934 O  O     . HOH   L 6 .   ? -6.29700  25.03200 6.66000   1.000 29.97134 ? 430 HOH   B O     1 
HETATM 5935 O  O     . HOH   L 6 .   ? -10.13400 15.78800 -1.48600  1.000 39.32219 ? 431 HOH   B O     1 
HETATM 5936 O  O     . HOH   L 6 .   ? -10.75900 40.57200 -16.94300 1.000 22.68501 ? 432 HOH   B O     1 
HETATM 5937 O  O     . HOH   L 6 .   ? -26.27300 32.81500 17.08900  1.000 26.86407 ? 433 HOH   B O     1 
HETATM 5938 O  O     . HOH   L 6 .   ? -41.98500 36.09800 -0.12600  1.000 48.84622 ? 434 HOH   B O     1 
HETATM 5939 O  O     . HOH   L 6 .   ? -18.70900 12.87800 1.69700   1.000 38.51571 ? 435 HOH   B O     1 
HETATM 5940 O  O     . HOH   L 6 .   ? -4.60400  27.21600 -4.88100  1.000 61.24084 ? 436 HOH   B O     1 
HETATM 5941 O  O     . HOH   L 6 .   ? -30.45100 46.90100 17.77600  1.000 47.01765 ? 437 HOH   B O     1 
HETATM 5942 O  O     . HOH   L 6 .   ? -27.30100 48.18100 -7.17900  1.000 57.44924 ? 438 HOH   B O     1 
HETATM 5943 O  O     . HOH   L 6 .   ? -18.14900 20.40600 4.78600   1.000 62.10671 ? 439 HOH   B O     1 
HETATM 5944 O  O     . HOH   L 6 .   ? -20.20800 13.92600 -0.70100  1.000 30.27919 ? 440 HOH   B O     1 
HETATM 5945 O  O     . HOH   L 6 .   ? -22.26800 40.66500 -25.62700 1.000 50.46151 ? 441 HOH   B O     1 
HETATM 5946 O  O     . HOH   L 6 .   ? -34.93900 35.81100 -2.74200  1.000 56.40962 ? 442 HOH   B O     1 
HETATM 5947 O  O     . HOH   L 6 .   ? -20.76300 27.24600 -15.86200 1.000 41.04971 ? 443 HOH   B O     1 
HETATM 5948 O  O     . HOH   L 6 .   ? -25.83900 29.63500 12.23800  1.000 46.36519 ? 444 HOH   B O     1 
HETATM 5949 O  O     . HOH   L 6 .   ? -20.07600 42.46000 -25.01900 1.000 47.95711 ? 445 HOH   B O     1 
HETATM 5950 O  O     . HOH   L 6 .   ? -21.04000 26.90100 -11.29500 1.000 47.88284 ? 446 HOH   B O     1 
HETATM 5951 O  O     . HOH   L 6 .   ? -29.06600 49.99800 -2.09000  1.000 59.56371 ? 447 HOH   B O     1 
HETATM 5952 O  O     . HOH   L 6 .   ? -15.93700 40.61900 -25.11700 1.000 53.45287 ? 448 HOH   B O     1 
HETATM 5953 O  O     . HOH   L 6 .   ? -28.87400 21.05500 6.09400   1.000 38.59770 ? 449 HOH   B O     1 
HETATM 5954 O  O     . HOH   L 6 .   ? -33.39800 33.45000 -14.96700 1.000 54.34710 ? 450 HOH   B O     1 
HETATM 5955 O  O     . HOH   L 6 .   ? -6.97800  32.55700 -9.52000  1.000 51.60836 ? 451 HOH   B O     1 
HETATM 5956 O  O     . HOH   L 6 .   ? -25.50800 12.48900 -7.25200  1.000 40.76188 ? 452 HOH   B O     1 
HETATM 5957 O  O     . HOH   L 6 .   ? -28.04000 31.27400 16.06500  1.000 50.10693 ? 453 HOH   B O     1 
HETATM 5958 O  O     . HOH   L 6 .   ? -8.52300  17.67200 -0.63000  1.000 37.11312 ? 454 HOH   B O     1 
HETATM 5959 O  O     . HOH   L 6 .   ? -20.32700 38.64600 -25.97600 1.000 30.41703 ? 455 HOH   B O     1 
HETATM 5960 O  O     . HOH   L 6 .   ? -26.61800 36.55000 19.86100  1.000 31.39014 ? 456 HOH   B O     1 
HETATM 5961 O  O     . HOH   L 6 .   ? -27.44400 29.45300 14.19400  1.000 41.56678 ? 457 HOH   B O     1 
HETATM 5962 O  O     . HOH   L 6 .   ? -24.53700 43.72600 -15.07900 1.000 44.35928 ? 458 HOH   B O     1 
HETATM 5963 O  O     . HOH   L 6 .   ? -2.69500  38.95000 -14.70400 1.000 26.15010 ? 459 HOH   B O     1 
HETATM 5964 O  O     . HOH   L 6 .   ? -7.97100  16.03500 -5.97400  1.000 40.90058 ? 460 HOH   B O     1 
HETATM 5965 O  O     . HOH   L 6 .   ? -33.68600 34.95900 10.10000  1.000 48.97220 ? 461 HOH   B O     1 
HETATM 5966 O  O     . HOH   L 6 .   ? -14.00700 38.92200 -26.79100 1.000 59.56767 ? 462 HOH   B O     1 
HETATM 5967 O  O     . HOH   L 6 .   ? -7.46000  23.84700 10.33600  1.000 50.60011 ? 463 HOH   B O     1 
HETATM 5968 O  O     . HOH   L 6 .   ? -8.53000  18.82600 2.07800   1.000 26.55505 ? 464 HOH   B O     1 
HETATM 5969 O  O     . HOH   L 6 .   ? -5.76800  27.12700 -7.16200  1.000 62.05856 ? 465 HOH   B O     1 
HETATM 5970 O  O     . HOH   L 6 .   ? -26.38600 27.90100 -15.91300 1.000 57.16649 ? 466 HOH   B O     1 
HETATM 5971 O  O     . HOH   L 6 .   ? -26.70300 44.73000 20.51800  1.000 55.60050 ? 467 HOH   B O     1 
HETATM 5972 O  O     . HOH   L 6 .   ? -33.48800 31.48500 7.06600   1.000 64.62902 ? 468 HOH   B O     1 
HETATM 5973 O  O     . HOH   L 6 .   ? -32.69600 30.07800 -4.66900  1.000 40.21586 ? 469 HOH   B O     1 
HETATM 5974 O  O     . HOH   L 6 .   ? -23.77500 24.25000 -14.20600 1.000 41.99577 ? 470 HOH   B O     1 
HETATM 5975 O  O     . HOH   L 6 .   ? -8.70200  44.43600 -10.30300 1.000 35.44631 ? 471 HOH   B O     1 
HETATM 5976 O  O     . HOH   L 6 .   ? -13.03700 16.69600 5.53100   1.000 45.91155 ? 472 HOH   B O     1 
HETATM 5977 O  O     . HOH   L 6 .   ? -6.33700  43.76900 5.28400   1.000 50.70121 ? 473 HOH   B O     1 
HETATM 5978 O  O     . HOH   L 6 .   ? -11.27400 21.40900 11.29900  1.000 45.99087 ? 474 HOH   B O     1 
HETATM 5979 O  O     . HOH   L 6 .   ? -25.13400 31.92300 19.37700  1.000 37.07461 ? 475 HOH   B O     1 
HETATM 5980 O  O     . HOH   L 6 .   ? -6.57300  18.50400 5.66500   1.000 40.69715 ? 476 HOH   B O     1 
HETATM 5981 O  O     . HOH   L 6 .   ? -6.46700  29.86300 -5.46400  1.000 43.37704 ? 477 HOH   B O     1 
HETATM 5982 O  O     . HOH   L 6 .   ? -17.40700 26.32500 -9.80400  1.000 51.96959 ? 478 HOH   B O     1 
HETATM 5983 O  O     . HOH   L 6 .   ? -8.70000  46.95200 -8.39200  1.000 65.77891 ? 479 HOH   B O     1 
HETATM 5984 O  O     . HOH   L 6 .   ? -33.92400 31.82100 -2.82700  1.000 38.69862 ? 480 HOH   B O     1 
HETATM 5985 O  O     . HOH   L 6 .   ? -34.77600 30.45300 -6.72100  1.000 62.33024 ? 481 HOH   B O     1 
HETATM 5986 O  O     . HOH   L 6 .   ? -10.98900 45.87700 -1.55200  1.000 59.66700 ? 482 HOH   B O     1 
HETATM 5987 O  O     . HOH   L 6 .   ? -34.54300 50.33100 -0.45600  1.000 53.10823 ? 483 HOH   B O     1 
HETATM 5988 O  O     . HOH   L 6 .   ? -33.86200 25.74700 11.41700  1.000 35.62304 ? 484 HOH   B O     1 
HETATM 5989 O  O     . HOH   L 6 .   ? -25.46100 34.26700 21.00200  1.000 47.32197 ? 485 HOH   B O     1 
HETATM 5990 O  O     . HOH   L 6 .   ? -13.48500 33.64000 14.42000  1.000 47.62939 ? 486 HOH   B O     1 
HETATM 5991 O  O     . HOH   L 6 .   ? -20.42800 50.21800 -15.06000 1.000 60.33925 ? 487 HOH   B O     1 
HETATM 5992 O  O     . HOH   L 6 .   ? -7.59600  20.31600 -9.07400  1.000 25.89525 ? 488 HOH   B O     1 
HETATM 5993 O  O     . HOH   L 6 .   ? -32.60200 51.77200 1.35900   1.000 52.64533 ? 489 HOH   B O     1 
HETATM 5994 O  O     . HOH   L 6 .   ? -7.63200  16.78400 7.02800   1.000 31.59675 ? 490 HOH   B O     1 
HETATM 5995 O  O     . HOH   L 6 .   ? -33.94800 28.78800 9.55000   1.000 50.90639 ? 491 HOH   B O     1 
HETATM 5996 O  O     . HOH   L 6 .   ? -29.80000 49.15100 18.15400  1.000 54.11755 ? 492 HOH   B O     1 
HETATM 5997 O  O     . HOH   L 6 .   ? -21.30600 49.28300 -10.87400 1.000 59.00578 ? 493 HOH   B O     1 
HETATM 5998 O  O     . HOH   L 6 .   ? -5.52900  20.47900 7.56000   1.000 27.89737 ? 494 HOH   B O     1 
HETATM 5999 O  O     . HOH   L 6 .   ? -2.62800  40.55800 -17.02900 1.000 23.24928 ? 495 HOH   B O     1 
HETATM 6000 O  O     . HOH   L 6 .   ? -27.03800 29.70400 20.12400  1.000 59.22249 ? 496 HOH   B O     1 
HETATM 6001 O  O     . HOH   M 6 .   ? -37.80400 40.40100 -52.58100 1.000 35.91711 ? 201 HOH   D O     1 
HETATM 6002 O  O     . HOH   M 6 .   ? -59.44200 39.30000 -33.95100 1.000 43.07307 ? 202 HOH   D O     1 
HETATM 6003 O  O     . HOH   M 6 .   ? -37.17200 45.50100 -19.13000 1.000 46.98328 ? 203 HOH   D O     1 
HETATM 6004 O  O     . HOH   M 6 .   ? -36.80500 50.83400 -24.39200 1.000 43.55211 ? 204 HOH   D O     1 
HETATM 6005 O  O     . HOH   M 6 .   ? -51.62700 40.46800 -49.32300 1.000 37.97814 ? 205 HOH   D O     1 
HETATM 6006 O  O     . HOH   M 6 .   ? -54.07700 43.31100 -16.33400 1.000 55.29642 ? 206 HOH   D O     1 
HETATM 6007 O  O     . HOH   M 6 .   ? -39.18600 45.62900 -52.41300 1.000 35.07895 ? 207 HOH   D O     1 
HETATM 6008 O  O     . HOH   M 6 .   ? -46.38500 23.92400 -46.29300 1.000 36.38295 ? 208 HOH   D O     1 
HETATM 6009 O  O     . HOH   M 6 .   ? -25.69200 46.33200 -43.02000 1.000 49.99972 ? 209 HOH   D O     1 
HETATM 6010 O  O     . HOH   M 6 .   ? -35.54500 47.42000 -21.44700 1.000 41.24661 ? 210 HOH   D O     1 
HETATM 6011 O  O     . HOH   M 6 .   ? -26.52600 46.37600 -27.42300 1.000 49.66722 ? 211 HOH   D O     1 
HETATM 6012 O  O     . HOH   M 6 .   ? -33.28000 53.44400 -37.32700 1.000 62.31523 ? 212 HOH   D O     1 
HETATM 6013 O  O     . HOH   M 6 .   ? -50.04200 50.69000 -24.99000 1.000 40.52612 ? 213 HOH   D O     1 
HETATM 6014 O  O     . HOH   M 6 .   ? -44.04100 25.24800 -39.76200 1.000 41.21898 ? 214 HOH   D O     1 
HETATM 6015 O  O     . HOH   M 6 .   ? -39.82800 30.12800 -42.94700 1.000 35.28126 ? 215 HOH   D O     1 
HETATM 6016 O  O     . HOH   M 6 .   ? -33.53800 53.61900 -33.32500 1.000 36.99710 ? 216 HOH   D O     1 
HETATM 6017 O  O     . HOH   M 6 .   ? -53.77200 32.68700 -35.51600 1.000 23.57387 ? 217 HOH   D O     1 
HETATM 6018 O  O     . HOH   M 6 .   ? -46.67000 41.59100 -51.16300 1.000 36.23993 ? 218 HOH   D O     1 
HETATM 6019 O  O     . HOH   M 6 .   ? -46.15700 53.51200 -47.24900 1.000 51.38582 ? 219 HOH   D O     1 
HETATM 6020 O  O     . HOH   M 6 .   ? -53.33000 36.15100 -42.51000 1.000 20.12181 ? 220 HOH   D O     1 
HETATM 6021 O  O     . HOH   M 6 .   ? -39.20100 34.48400 -40.00400 1.000 15.33151 ? 221 HOH   D O     1 
HETATM 6022 O  O     . HOH   M 6 .   ? -24.27400 36.82100 -22.21700 1.000 40.88801 ? 222 HOH   D O     1 
HETATM 6023 O  O     . HOH   M 6 .   ? -37.32800 51.96600 -32.40700 1.000 29.26809 ? 223 HOH   D O     1 
HETATM 6024 O  O     . HOH   M 6 .   ? -45.91400 35.19200 -31.36800 1.000 19.93180 ? 224 HOH   D O     1 
HETATM 6025 O  O     . HOH   M 6 .   ? -50.32300 23.90000 -37.08900 1.000 43.62476 ? 225 HOH   D O     1 
HETATM 6026 O  O     . HOH   M 6 .   ? -55.89600 39.47900 -48.17700 1.000 40.53247 ? 226 HOH   D O     1 
HETATM 6027 O  O     . HOH   M 6 .   ? -34.35600 38.34100 -42.46800 1.000 17.74618 ? 227 HOH   D O     1 
HETATM 6028 O  O     . HOH   M 6 .   ? -45.58000 21.11400 -32.29200 1.000 44.93581 ? 228 HOH   D O     1 
HETATM 6029 O  O     . HOH   M 6 .   ? -39.53300 24.82800 -22.47900 1.000 50.56815 ? 229 HOH   D O     1 
HETATM 6030 O  O     . HOH   M 6 .   ? -27.44700 44.50400 -25.01100 1.000 46.31786 ? 230 HOH   D O     1 
HETATM 6031 O  O     . HOH   M 6 .   ? -28.90700 35.47200 -36.63400 1.000 35.17183 ? 231 HOH   D O     1 
HETATM 6032 O  O     . HOH   M 6 .   ? -40.33900 54.88200 -43.48900 1.000 53.64468 ? 232 HOH   D O     1 
HETATM 6033 O  O     . HOH   M 6 .   ? -57.06600 45.73300 -42.62300 1.000 51.92096 ? 233 HOH   D O     1 
HETATM 6034 O  O     . HOH   M 6 .   ? -36.59900 30.75200 -40.79700 1.000 21.76515 ? 234 HOH   D O     1 
HETATM 6035 O  O     . HOH   M 6 .   ? -52.97600 50.88400 -40.83600 1.000 27.08805 ? 235 HOH   D O     1 
HETATM 6036 O  O     . HOH   M 6 .   ? -35.61200 42.28100 -53.08900 1.000 42.26368 ? 236 HOH   D O     1 
HETATM 6037 O  O     . HOH   M 6 .   ? -30.38900 29.71700 -46.56900 1.000 32.63410 ? 237 HOH   D O     1 
HETATM 6038 O  O     . HOH   M 6 .   ? -51.70600 25.02300 -35.17000 1.000 21.69994 ? 238 HOH   D O     1 
HETATM 6039 O  O     . HOH   M 6 .   ? -43.59200 31.72700 -31.10600 1.000 13.70357 ? 239 HOH   D O     1 
HETATM 6040 O  O     . HOH   M 6 .   ? -61.37800 37.88900 -30.36600 1.000 60.24623 ? 240 HOH   D O     1 
HETATM 6041 O  O     . HOH   M 6 .   ? -27.15800 49.41500 -36.42900 1.000 30.74206 ? 241 HOH   D O     1 
HETATM 6042 O  O     . HOH   M 6 .   ? -58.39100 42.80200 -27.63000 1.000 36.91317 ? 242 HOH   D O     1 
HETATM 6043 O  O     . HOH   M 6 .   ? -44.92200 55.67100 -35.88700 1.000 60.51699 ? 243 HOH   D O     1 
HETATM 6044 O  O     . HOH   M 6 .   ? -50.74600 34.42400 -22.08900 1.000 17.90643 ? 244 HOH   D O     1 
HETATM 6045 O  O     . HOH   M 6 .   ? -30.23300 53.41500 -29.86300 1.000 39.22370 ? 245 HOH   D O     1 
HETATM 6046 O  O     . HOH   M 6 .   ? -29.51400 37.50600 -47.67900 1.000 21.54219 ? 246 HOH   D O     1 
HETATM 6047 O  O     . HOH   M 6 .   ? -55.39500 31.94600 -47.71500 1.000 38.81472 ? 247 HOH   D O     1 
HETATM 6048 O  O     . HOH   M 6 .   ? -23.92300 41.44800 -42.12100 1.000 42.93406 ? 248 HOH   D O     1 
HETATM 6049 O  O     . HOH   M 6 .   ? -41.58500 32.78600 -51.39800 1.000 43.16325 ? 249 HOH   D O     1 
HETATM 6050 O  O     . HOH   M 6 .   ? -25.90100 41.94000 -46.06400 1.000 32.23134 ? 250 HOH   D O     1 
HETATM 6051 O  O     . HOH   M 6 .   ? -31.70300 49.16600 -24.05800 1.000 49.24738 ? 251 HOH   D O     1 
HETATM 6052 O  O     . HOH   M 6 .   ? -48.13800 30.14000 -46.90700 1.000 38.83499 ? 252 HOH   D O     1 
HETATM 6053 O  O     . HOH   M 6 .   ? -51.38700 48.20200 -19.91600 1.000 36.59667 ? 253 HOH   D O     1 
HETATM 6054 O  O     . HOH   M 6 .   ? -37.18800 29.75200 -25.44100 1.000 25.25007 ? 254 HOH   D O     1 
HETATM 6055 O  O     . HOH   M 6 .   ? -39.46700 27.27500 -39.67300 1.000 22.29238 ? 255 HOH   D O     1 
HETATM 6056 O  O     . HOH   M 6 .   ? -33.00300 45.58300 -43.00000 1.000 17.41583 ? 256 HOH   D O     1 
HETATM 6057 O  O     . HOH   M 6 .   ? -23.66200 43.24600 -39.23800 1.000 41.41729 ? 257 HOH   D O     1 
HETATM 6058 O  O     . HOH   M 6 .   ? -36.44800 28.01600 -41.20600 1.000 38.02494 ? 258 HOH   D O     1 
HETATM 6059 O  O     . HOH   M 6 .   ? -36.82900 30.12000 -32.11500 1.000 16.33999 ? 259 HOH   D O     1 
HETATM 6060 O  O     . HOH   M 6 .   ? -58.75700 29.74000 -40.65000 1.000 47.20718 ? 260 HOH   D O     1 
HETATM 6061 O  O     . HOH   M 6 .   ? -52.17800 28.97900 -35.19100 1.000 22.26247 ? 261 HOH   D O     1 
HETATM 6062 O  O     . HOH   M 6 .   ? -43.98900 32.80000 -23.53700 1.000 18.43998 ? 262 HOH   D O     1 
HETATM 6063 O  O     . HOH   M 6 .   ? -42.60300 35.09000 -13.67400 1.000 55.83792 ? 263 HOH   D O     1 
HETATM 6064 O  O     . HOH   M 6 .   ? -42.21500 57.42300 -37.96000 1.000 65.41142 ? 264 HOH   D O     1 
HETATM 6065 O  O     . HOH   M 6 .   ? -43.08300 50.65900 -51.17700 1.000 35.91098 ? 265 HOH   D O     1 
HETATM 6066 O  O     . HOH   M 6 .   ? -50.91000 36.22900 -15.14500 1.000 23.52373 ? 266 HOH   D O     1 
HETATM 6067 O  O     . HOH   M 6 .   ? -46.42000 56.66900 -43.79300 1.000 38.18068 ? 267 HOH   D O     1 
HETATM 6068 O  O     . HOH   M 6 .   ? -41.20500 21.91300 -46.15400 1.000 23.81006 ? 268 HOH   D O     1 
HETATM 6069 O  O     . HOH   M 6 .   ? -37.42800 50.40900 -50.82700 1.000 32.83355 ? 269 HOH   D O     1 
HETATM 6070 O  O     . HOH   M 6 .   ? -39.61100 52.42900 -31.38800 1.000 28.27881 ? 270 HOH   D O     1 
HETATM 6071 O  O     . HOH   M 6 .   ? -48.20400 52.21100 -23.56200 1.000 38.93446 ? 271 HOH   D O     1 
HETATM 6072 O  O     . HOH   M 6 .   ? -34.78700 47.11800 -44.38800 1.000 16.28761 ? 272 HOH   D O     1 
HETATM 6073 O  O     . HOH   M 6 .   ? -49.34700 25.20200 -43.70900 1.000 45.60773 ? 273 HOH   D O     1 
HETATM 6074 O  O     . HOH   M 6 .   ? -29.98800 36.70900 -44.17800 1.000 25.91991 ? 274 HOH   D O     1 
HETATM 6075 O  O     . HOH   M 6 .   ? -37.81300 26.60700 -28.97500 1.000 27.80441 ? 275 HOH   D O     1 
HETATM 6076 O  O     . HOH   M 6 .   ? -33.86300 51.45100 -38.56600 1.000 28.78902 ? 276 HOH   D O     1 
HETATM 6077 O  O     . HOH   M 6 .   ? -42.81300 39.93700 -42.41200 1.000 16.82056 ? 277 HOH   D O     1 
HETATM 6078 O  O     . HOH   M 6 .   ? -33.70600 35.11900 -44.10900 1.000 15.73597 ? 278 HOH   D O     1 
HETATM 6079 O  O     . HOH   M 6 .   ? -50.63200 45.28600 -17.07100 1.000 46.97138 ? 279 HOH   D O     1 
HETATM 6080 O  O     . HOH   M 6 .   ? -33.70900 29.90700 -18.22000 1.000 28.48380 ? 280 HOH   D O     1 
HETATM 6081 O  O     . HOH   M 6 .   ? -48.60700 46.53000 -46.47000 1.000 23.54149 ? 281 HOH   D O     1 
HETATM 6082 O  O     . HOH   M 6 .   ? -53.66300 42.86800 -23.53700 1.000 19.55584 ? 282 HOH   D O     1 
HETATM 6083 O  O     . HOH   M 6 .   ? -35.56800 48.51800 -23.93500 1.000 48.77806 ? 283 HOH   D O     1 
HETATM 6084 O  O     . HOH   M 6 .   ? -46.60800 46.78400 -48.20300 1.000 26.06866 ? 284 HOH   D O     1 
HETATM 6085 O  O     . HOH   M 6 .   ? -29.17200 35.21300 -40.22000 1.000 30.00821 ? 285 HOH   D O     1 
HETATM 6086 O  O     . HOH   M 6 .   ? -31.62000 37.67400 -51.33300 1.000 42.31926 ? 286 HOH   D O     1 
HETATM 6087 O  O     . HOH   M 6 .   ? -50.82600 53.33800 -32.04600 1.000 38.12668 ? 287 HOH   D O     1 
HETATM 6088 O  O     . HOH   M 6 .   ? -36.75800 25.62600 -37.17800 1.000 21.40872 ? 288 HOH   D O     1 
HETATM 6089 O  O     . HOH   M 6 .   ? -40.60000 22.93300 -37.38700 1.000 57.88178 ? 289 HOH   D O     1 
HETATM 6090 O  O     . HOH   M 6 .   ? -59.76900 42.89800 -32.46000 1.000 53.66173 ? 290 HOH   D O     1 
HETATM 6091 O  O     . HOH   M 6 .   ? -36.69100 46.55100 -51.57800 1.000 30.06623 ? 291 HOH   D O     1 
HETATM 6092 O  O     . HOH   M 6 .   ? -36.98700 32.13400 -49.76300 1.000 34.36359 ? 292 HOH   D O     1 
HETATM 6093 O  O     . HOH   M 6 .   ? -51.55500 31.42200 -33.47400 1.000 25.52594 ? 293 HOH   D O     1 
HETATM 6094 O  O     . HOH   M 6 .   ? -53.81800 34.39300 -25.21500 1.000 45.57507 ? 294 HOH   D O     1 
HETATM 6095 O  O     . HOH   M 6 .   ? -43.98100 42.94400 -15.93600 1.000 34.91337 ? 295 HOH   D O     1 
HETATM 6096 O  O     . HOH   M 6 .   ? -51.36100 30.11000 -24.43200 1.000 19.18209 ? 296 HOH   D O     1 
HETATM 6097 O  O     . HOH   M 6 .   ? -49.95300 36.14700 -50.70900 1.000 57.85810 ? 297 HOH   D O     1 
HETATM 6098 O  O     . HOH   M 6 .   ? -37.49700 40.03900 -46.33000 1.000 16.70365 ? 298 HOH   D O     1 
HETATM 6099 O  O     . HOH   M 6 .   ? -40.39100 30.15700 -23.38200 1.000 19.11401 ? 299 HOH   D O     1 
HETATM 6100 O  O     . HOH   M 6 .   ? -51.81200 49.30900 -23.41300 1.000 41.84945 ? 300 HOH   D O     1 
HETATM 6101 O  O     . HOH   M 6 .   ? -37.54300 32.18600 -17.26800 1.000 35.30095 ? 301 HOH   D O     1 
HETATM 6102 O  O     . HOH   M 6 .   ? -33.58600 27.73700 -24.30200 1.000 28.63926 ? 302 HOH   D O     1 
HETATM 6103 O  O     . HOH   M 6 .   ? -28.80300 49.81000 -26.87500 1.000 34.56263 ? 303 HOH   D O     1 
HETATM 6104 O  O     . HOH   M 6 .   ? -33.88800 29.70100 -48.88600 1.000 32.25473 ? 304 HOH   D O     1 
HETATM 6105 O  O     . HOH   M 6 .   ? -55.37300 41.88500 -15.02300 1.000 43.25994 ? 305 HOH   D O     1 
HETATM 6106 O  O     A HOH   M 6 .   ? -54.16300 45.77900 -24.38300 0.500 37.02318 ? 306 HOH   D O     1 
HETATM 6107 O  O     B HOH   M 6 .   ? -54.50100 45.17800 -22.81400 0.500 31.34965 ? 306 HOH   D O     1 
HETATM 6108 O  O     . HOH   M 6 .   ? -58.36400 41.40400 -37.87900 1.000 35.23070 ? 307 HOH   D O     1 
HETATM 6109 O  O     . HOH   M 6 .   ? -30.34600 44.74100 -41.45200 1.000 18.83443 ? 308 HOH   D O     1 
HETATM 6110 O  O     . HOH   M 6 .   ? -59.20300 46.29900 -30.47000 1.000 47.55090 ? 309 HOH   D O     1 
HETATM 6111 O  O     . HOH   M 6 .   ? -28.86300 51.37000 -45.99200 1.000 70.14037 ? 310 HOH   D O     1 
HETATM 6112 O  O     . HOH   M 6 .   ? -34.83000 30.08400 -26.44800 1.000 26.73469 ? 311 HOH   D O     1 
HETATM 6113 O  O     . HOH   M 6 .   ? -56.95000 33.84500 -39.20500 1.000 34.98950 ? 312 HOH   D O     1 
HETATM 6114 O  O     . HOH   M 6 .   ? -34.26400 53.01300 -30.88800 1.000 39.39881 ? 313 HOH   D O     1 
HETATM 6115 O  O     . HOH   M 6 .   ? -51.53000 33.95800 -48.40100 1.000 45.50342 ? 314 HOH   D O     1 
HETATM 6116 O  O     . HOH   M 6 .   ? -38.11800 34.69000 -15.77400 1.000 51.26703 ? 315 HOH   D O     1 
HETATM 6117 O  O     . HOH   M 6 .   ? -52.79000 27.49600 -41.85000 1.000 43.30293 ? 316 HOH   D O     1 
HETATM 6118 O  O     . HOH   M 6 .   ? -42.53700 48.52100 -18.02500 1.000 27.41676 ? 317 HOH   D O     1 
HETATM 6119 O  O     . HOH   M 6 .   ? -49.81900 34.13700 -13.82000 1.000 23.91493 ? 318 HOH   D O     1 
HETATM 6120 O  O     . HOH   M 6 .   ? -46.58900 54.10700 -25.26100 1.000 38.84355 ? 319 HOH   D O     1 
HETATM 6121 O  O     . HOH   M 6 .   ? -53.80200 36.85300 -36.62000 1.000 17.49543 ? 320 HOH   D O     1 
HETATM 6122 O  O     . HOH   M 6 .   ? -36.26900 29.46700 -28.59000 1.000 36.43835 ? 321 HOH   D O     1 
HETATM 6123 O  O     . HOH   M 6 .   ? -55.76700 29.58000 -44.82200 1.000 49.36084 ? 322 HOH   D O     1 
HETATM 6124 O  O     . HOH   M 6 .   ? -30.10000 28.40900 -44.26500 1.000 50.24167 ? 323 HOH   D O     1 
HETATM 6125 O  O     . HOH   M 6 .   ? -57.60500 44.01400 -38.14300 1.000 31.80901 ? 324 HOH   D O     1 
HETATM 6126 O  O     . HOH   M 6 .   ? -41.03600 31.70000 -39.18900 1.000 20.81193 ? 325 HOH   D O     1 
HETATM 6127 O  O     . HOH   M 6 .   ? -56.19700 34.47800 -28.97400 1.000 28.95557 ? 326 HOH   D O     1 
HETATM 6128 O  O     . HOH   M 6 .   ? -54.78200 51.44500 -30.05600 1.000 29.86450 ? 327 HOH   D O     1 
HETATM 6129 O  O     . HOH   M 6 .   ? -34.03000 54.52000 -45.58200 1.000 51.40764 ? 328 HOH   D O     1 
HETATM 6130 O  O     . HOH   M 6 .   ? -53.07500 48.50200 -45.42200 1.000 40.41489 ? 329 HOH   D O     1 
HETATM 6131 O  O     . HOH   M 6 .   ? -31.34100 34.24900 -16.63200 1.000 37.01533 ? 330 HOH   D O     1 
HETATM 6132 O  O     . HOH   M 6 .   ? -46.36500 42.77100 -15.11000 1.000 31.93280 ? 331 HOH   D O     1 
HETATM 6133 O  O     . HOH   M 6 .   ? -38.72300 27.72300 -26.36900 1.000 37.52875 ? 332 HOH   D O     1 
HETATM 6134 O  O     . HOH   M 6 .   ? -31.53500 52.44300 -40.29800 1.000 25.11917 ? 333 HOH   D O     1 
HETATM 6135 O  O     . HOH   M 6 .   ? -43.69400 53.37700 -27.21600 1.000 25.29201 ? 334 HOH   D O     1 
HETATM 6136 O  O     . HOH   M 6 .   ? -30.52100 31.42800 -50.31900 1.000 45.71221 ? 335 HOH   D O     1 
HETATM 6137 O  O     . HOH   M 6 .   ? -38.91000 39.36600 -50.40600 1.000 51.37302 ? 336 HOH   D O     1 
HETATM 6138 O  O     . HOH   M 6 .   ? -42.20800 58.08200 -35.46300 1.000 48.09988 ? 337 HOH   D O     1 
HETATM 6139 O  O     . HOH   M 6 .   ? -40.37000 27.97000 -20.37900 1.000 53.47982 ? 338 HOH   D O     1 
HETATM 6140 O  O     . HOH   M 6 .   ? -56.16500 38.86600 -22.27700 1.000 25.04006 ? 339 HOH   D O     1 
HETATM 6141 O  O     . HOH   M 6 .   ? -39.40000 35.14800 -52.06300 1.000 31.23007 ? 340 HOH   D O     1 
HETATM 6142 O  O     . HOH   M 6 .   ? -30.19100 33.12100 -38.06400 1.000 25.79497 ? 341 HOH   D O     1 
HETATM 6143 O  O     . HOH   M 6 .   ? -44.49500 56.70100 -46.02400 1.000 36.11613 ? 342 HOH   D O     1 
HETATM 6144 O  O     . HOH   M 6 .   ? -45.96300 56.81400 -41.22900 1.000 41.79070 ? 343 HOH   D O     1 
HETATM 6145 O  O     . HOH   M 6 .   ? -52.44100 45.39300 -48.47200 1.000 55.33901 ? 344 HOH   D O     1 
HETATM 6146 O  O     A HOH   M 6 .   ? -52.13900 52.01600 -44.59500 0.500 46.25224 ? 345 HOH   D O     1 
HETATM 6147 O  O     B HOH   M 6 .   ? -53.16300 51.59100 -44.97400 0.500 48.73061 ? 345 HOH   D O     1 
HETATM 6148 O  O     . HOH   M 6 .   ? -43.96700 53.43600 -23.64800 1.000 31.35019 ? 346 HOH   D O     1 
HETATM 6149 O  O     . HOH   M 6 .   ? -27.91700 38.01000 -45.58500 1.000 25.12181 ? 347 HOH   D O     1 
HETATM 6150 O  O     . HOH   M 6 .   ? -55.43300 28.07800 -42.23000 1.000 43.39549 ? 348 HOH   D O     1 
HETATM 6151 O  O     . HOH   M 6 .   ? -47.82000 38.40300 -14.26200 1.000 26.98225 ? 349 HOH   D O     1 
HETATM 6152 O  O     . HOH   M 6 .   ? -36.14700 28.05300 -30.65900 1.000 49.76952 ? 350 HOH   D O     1 
HETATM 6153 O  O     . HOH   M 6 .   ? -48.26800 56.84900 -53.39400 1.000 53.00710 ? 351 HOH   D O     1 
HETATM 6154 O  O     . HOH   M 6 .   ? -31.80000 47.30000 -32.66100 1.000 22.86007 ? 352 HOH   D O     1 
HETATM 6155 O  O     . HOH   M 6 .   ? -52.84400 30.38900 -37.65400 1.000 21.95093 ? 353 HOH   D O     1 
HETATM 6156 O  O     . HOH   M 6 .   ? -32.46200 26.96100 -42.86900 1.000 44.66087 ? 354 HOH   D O     1 
HETATM 6157 O  O     . HOH   M 6 .   ? -35.79200 38.27700 -16.06500 1.000 47.57498 ? 355 HOH   D O     1 
HETATM 6158 O  O     . HOH   M 6 .   ? -57.79500 37.95600 -47.69900 1.000 51.11320 ? 356 HOH   D O     1 
HETATM 6159 O  O     . HOH   M 6 .   ? -55.98700 38.43000 -36.01500 1.000 22.84398 ? 357 HOH   D O     1 
HETATM 6160 O  O     . HOH   M 6 .   ? -55.97400 46.93900 -25.14000 1.000 61.87817 ? 358 HOH   D O     1 
HETATM 6161 O  O     . HOH   M 6 .   ? -43.77600 29.06000 -30.17100 1.000 20.45907 ? 359 HOH   D O     1 
HETATM 6162 O  O     . HOH   M 6 .   ? -48.71800 58.73000 -51.96000 1.000 52.92611 ? 360 HOH   D O     1 
HETATM 6163 O  O     . HOH   M 6 .   ? -43.99900 29.61900 -21.03400 1.000 35.80583 ? 361 HOH   D O     1 
HETATM 6164 O  O     . HOH   M 6 .   ? -42.31200 28.42400 -15.10000 1.000 57.87604 ? 362 HOH   D O     1 
HETATM 6165 O  O     . HOH   M 6 .   ? -37.66900 53.99300 -41.78300 1.000 53.95458 ? 363 HOH   D O     1 
HETATM 6166 O  O     . HOH   M 6 .   ? -34.17200 26.93000 -18.38800 1.000 44.03424 ? 364 HOH   D O     1 
HETATM 6167 O  O     . HOH   M 6 .   ? -31.09900 30.77200 -18.50400 1.000 38.12375 ? 365 HOH   D O     1 
HETATM 6168 O  O     . HOH   M 6 .   ? -39.89900 50.50500 -51.98000 1.000 40.68741 ? 366 HOH   D O     1 
HETATM 6169 O  O     . HOH   M 6 .   ? -60.62200 34.64000 -32.90500 1.000 62.14003 ? 367 HOH   D O     1 
HETATM 6170 O  O     . HOH   M 6 .   ? -46.59100 30.19400 -14.98400 1.000 54.93580 ? 368 HOH   D O     1 
HETATM 6171 O  O     . HOH   M 6 .   ? -28.26300 34.98800 -42.91000 1.000 33.97153 ? 369 HOH   D O     1 
HETATM 6172 O  O     . HOH   M 6 .   ? -42.53300 23.30100 -39.42000 1.000 43.99330 ? 370 HOH   D O     1 
HETATM 6173 O  O     . HOH   M 6 .   ? -29.93600 37.83900 -20.20400 1.000 50.09170 ? 371 HOH   D O     1 
HETATM 6174 O  O     . HOH   M 6 .   ? -41.24000 26.47200 -41.92500 1.000 62.72182 ? 372 HOH   D O     1 
HETATM 6175 O  O     . HOH   M 6 .   ? -43.82500 30.03100 -23.62500 1.000 48.90604 ? 373 HOH   D O     1 
HETATM 6176 O  O     . HOH   M 6 .   ? -55.10000 34.38900 -37.13700 1.000 22.74228 ? 374 HOH   D O     1 
HETATM 6177 O  O     . HOH   M 6 .   ? -38.97700 55.69400 -32.71000 1.000 50.19622 ? 375 HOH   D O     1 
HETATM 6178 O  O     . HOH   M 6 .   ? -51.98200 51.66800 -29.78500 1.000 43.99772 ? 376 HOH   D O     1 
HETATM 6179 O  O     . HOH   M 6 .   ? -58.38700 37.45600 -36.41500 1.000 48.47292 ? 377 HOH   D O     1 
HETATM 6180 O  O     . HOH   M 6 .   ? -38.52500 55.07300 -49.90800 1.000 57.35608 ? 378 HOH   D O     1 
HETATM 6181 O  O     . HOH   M 6 .   ? -39.33100 30.02600 -40.38800 1.000 26.82706 ? 379 HOH   D O     1 
HETATM 6182 O  O     . HOH   M 6 .   ? -47.12100 27.72800 -46.82800 1.000 32.04449 ? 380 HOH   D O     1 
HETATM 6183 O  O     . HOH   M 6 .   ? -45.14100 54.60500 -21.30900 1.000 41.79470 ? 381 HOH   D O     1 
HETATM 6184 O  O     . HOH   M 6 .   ? -38.33100 21.14800 -35.98500 1.000 53.54888 ? 382 HOH   D O     1 
HETATM 6185 O  O     . HOH   M 6 .   ? -21.49600 44.66000 -35.35800 1.000 56.67045 ? 383 HOH   D O     1 
HETATM 6186 O  O     . HOH   M 6 .   ? -45.90900 44.28600 -51.47600 1.000 44.57508 ? 384 HOH   D O     1 
HETATM 6187 O  O     . HOH   M 6 .   ? -44.89400 29.08600 -18.86400 1.000 55.08366 ? 385 HOH   D O     1 
HETATM 6188 O  O     . HOH   M 6 .   ? -39.37400 25.40300 -48.74100 1.000 59.96642 ? 386 HOH   D O     1 
HETATM 6189 O  O     . HOH   M 6 .   ? -56.40400 36.12300 -23.66200 1.000 38.33378 ? 387 HOH   D O     1 
HETATM 6190 O  O     . HOH   M 6 .   ? -39.36800 23.36500 -39.38500 1.000 61.31991 ? 388 HOH   D O     1 
HETATM 6191 O  O     . HOH   M 6 .   ? -40.45200 47.20700 -16.95300 1.000 31.74253 ? 389 HOH   D O     1 
HETATM 6192 O  O     . HOH   M 6 .   ? -52.12200 30.72500 -19.79700 1.000 51.54190 ? 390 HOH   D O     1 
HETATM 6193 O  O     . HOH   M 6 .   ? -49.55000 33.01900 -11.65100 1.000 50.80675 ? 391 HOH   D O     1 
HETATM 6194 O  O     . HOH   M 6 .   ? -47.88900 40.45200 -15.82300 1.000 32.36657 ? 392 HOH   D O     1 
HETATM 6195 O  O     . HOH   M 6 .   ? -35.20900 30.67100 -16.14500 1.000 56.11261 ? 393 HOH   D O     1 
HETATM 6196 O  O     . HOH   M 6 .   ? -51.65600 31.70200 -22.14700 1.000 22.79844 ? 394 HOH   D O     1 
HETATM 6197 O  O     . HOH   M 6 .   ? -45.32700 25.61800 -42.49400 1.000 51.21605 ? 395 HOH   D O     1 
HETATM 6198 O  O     . HOH   M 6 .   ? -32.19600 28.17500 -47.28300 1.000 43.86942 ? 396 HOH   D O     1 
HETATM 6199 O  O     . HOH   M 6 .   ? -51.71700 51.97800 -26.85900 1.000 53.08642 ? 397 HOH   D O     1 
HETATM 6200 O  O     . HOH   M 6 .   ? -52.89200 52.86600 -42.54600 1.000 58.39580 ? 398 HOH   D O     1 
HETATM 6201 O  O     . HOH   M 6 .   ? -37.94100 24.70600 -40.81700 1.000 57.29356 ? 399 HOH   D O     1 
HETATM 6202 O  O     . HOH   M 6 .   ? -48.38700 24.26500 -41.35200 1.000 50.28136 ? 400 HOH   D O     1 
HETATM 6203 O  O     A HOH   M 6 .   ? -41.35200 27.18500 -26.62400 0.500 36.50049 ? 401 HOH   D O     1 
HETATM 6204 O  O     B HOH   M 6 .   ? -43.00000 27.92400 -27.87100 0.500 29.55985 ? 401 HOH   D O     1 
HETATM 6205 O  O     . HOH   M 6 .   ? -31.58600 37.64000 -17.43800 1.000 47.00164 ? 402 HOH   D O     1 
HETATM 6206 O  O     . HOH   M 6 .   ? -25.90500 38.72300 -21.57200 1.000 43.66192 ? 403 HOH   D O     1 
HETATM 6207 O  O     . HOH   M 6 .   ? -47.02800 25.79900 -44.76700 1.000 43.01361 ? 404 HOH   D O     1 
HETATM 6208 O  O     . HOH   M 6 .   ? -32.10400 26.66600 -16.89500 1.000 55.34722 ? 405 HOH   D O     1 
HETATM 6209 O  O     . HOH   M 6 .   ? -41.50500 27.72400 -24.08800 1.000 59.50055 ? 406 HOH   D O     1 
HETATM 6210 O  O     . HOH   M 6 .   ? -42.12100 45.17900 -15.43100 1.000 42.85433 ? 407 HOH   D O     1 
HETATM 6211 O  O     . HOH   M 6 .   ? -43.92400 53.19600 -52.25100 1.000 65.24922 ? 408 HOH   D O     1 
HETATM 6212 O  O     . HOH   M 6 .   ? -51.56800 27.94100 -39.43800 1.000 20.71705 ? 409 HOH   D O     1 
HETATM 6213 O  O     . HOH   M 6 .   ? -36.25700 53.53700 -34.46100 1.000 62.44773 ? 410 HOH   D O     1 
HETATM 6214 O  O     . HOH   M 6 .   ? -50.45700 25.25000 -39.30100 1.000 45.62784 ? 411 HOH   D O     1 
HETATM 6215 O  O     . HOH   M 6 .   ? -35.82600 49.00700 -52.64900 1.000 27.08032 ? 412 HOH   D O     1 
HETATM 6216 O  O     . HOH   M 6 .   ? -55.56200 41.04300 -23.89700 1.000 28.28069 ? 413 HOH   D O     1 
HETATM 6217 O  O     . HOH   M 6 .   ? -50.55700 48.51800 -46.70900 1.000 31.41387 ? 414 HOH   D O     1 
HETATM 6218 O  O     . HOH   M 6 .   ? -52.23200 54.45900 -34.00800 1.000 56.03293 ? 415 HOH   D O     1 
HETATM 6219 O  O     . HOH   M 6 .   ? -58.73000 27.65000 -39.06300 1.000 49.38933 ? 416 HOH   D O     1 
HETATM 6220 O  O     . HOH   M 6 .   ? -53.65200 48.60200 -20.76700 1.000 59.93003 ? 417 HOH   D O     1 
HETATM 6221 O  O     . HOH   M 6 .   ? -29.01400 52.26100 -27.38200 1.000 55.44873 ? 418 HOH   D O     1 
HETATM 6222 O  O     . HOH   M 6 .   ? -47.20700 21.61300 -44.34700 1.000 44.79769 ? 419 HOH   D O     1 
HETATM 6223 O  O     . HOH   M 6 .   ? -36.40100 52.93700 -50.29500 1.000 42.62947 ? 420 HOH   D O     1 
HETATM 6224 O  O     . HOH   M 6 .   ? -37.43900 52.98300 -26.29600 1.000 52.71675 ? 421 HOH   D O     1 
HETATM 6225 O  O     . HOH   M 6 .   ? -58.41800 33.25200 -33.25100 1.000 45.51509 ? 422 HOH   D O     1 
HETATM 6226 O  O     . HOH   M 6 .   ? -44.43400 49.44100 -52.90900 1.000 55.35753 ? 423 HOH   D O     1 
HETATM 6227 O  O     . HOH   M 6 .   ? -25.85500 34.19500 -43.11900 1.000 53.61794 ? 424 HOH   D O     1 
HETATM 6228 O  O     . HOH   M 6 .   ? -43.94200 28.33000 -25.62200 1.000 49.58968 ? 425 HOH   D O     1 
HETATM 6229 O  O     . HOH   M 6 .   ? -49.70800 39.09300 -51.23100 1.000 56.13282 ? 426 HOH   D O     1 
HETATM 6230 O  O     . HOH   M 6 .   ? -38.83200 21.30500 -44.85200 1.000 50.29114 ? 427 HOH   D O     1 
HETATM 6231 O  O     . HOH   M 6 .   ? -36.49400 22.80700 -37.51900 1.000 29.67051 ? 428 HOH   D O     1 
HETATM 6232 O  O     . HOH   M 6 .   ? -58.44800 40.13700 -21.75500 1.000 32.79833 ? 429 HOH   D O     1 
HETATM 6233 O  O     . HOH   M 6 .   ? -35.50100 26.21500 -39.53600 1.000 29.42397 ? 430 HOH   D O     1 
HETATM 6234 O  O     . HOH   M 6 .   ? -54.13900 51.49400 -25.99700 1.000 59.48563 ? 431 HOH   D O     1 
HETATM 6235 O  O     . HOH   M 6 .   ? -27.85500 29.55600 -47.75500 1.000 44.32476 ? 432 HOH   D O     1 
HETATM 6236 O  O     . HOH   M 6 .   ? -38.23600 26.68400 -18.69000 1.000 53.50103 ? 433 HOH   D O     1 
HETATM 6237 O  O     . HOH   M 6 .   ? -40.00300 48.05400 -53.51700 1.000 43.26625 ? 434 HOH   D O     1 
HETATM 6238 O  O     . HOH   M 6 .   ? -36.10000 52.74500 -38.00200 1.000 58.40931 ? 435 HOH   D O     1 
HETATM 6239 O  O     . HOH   M 6 .   ? -57.67400 34.41900 -35.89900 1.000 43.64016 ? 436 HOH   D O     1 
HETATM 6240 O  O     . HOH   M 6 .   ? -23.20300 41.54500 -28.30700 1.000 50.91783 ? 437 HOH   D O     1 
HETATM 6241 O  O     . HOH   M 6 .   ? -47.40500 45.27500 -15.29300 1.000 42.20071 ? 438 HOH   D O     1 
HETATM 6242 O  O     . HOH   M 6 .   ? -57.93400 42.36200 -23.02500 1.000 61.25347 ? 439 HOH   D O     1 
HETATM 6243 O  O     . HOH   N 6 .   ? -52.66600 -0.45400 -0.37100  1.000 49.34683 ? 201 HOH   C O     1 
HETATM 6244 O  O     . HOH   N 6 .   ? -58.78700 9.70400  5.01800   1.000 51.83067 ? 202 HOH   C O     1 
HETATM 6245 O  O     . HOH   N 6 .   ? -31.71100 -2.31500 13.80200  1.000 43.60938 ? 203 HOH   C O     1 
HETATM 6246 O  O     . HOH   N 6 .   ? -37.38800 5.84500  -10.44300 1.000 42.16837 ? 204 HOH   C O     1 
HETATM 6247 O  O     . HOH   N 6 .   ? -28.27600 -2.63800 8.96000   1.000 36.27005 ? 205 HOH   C O     1 
HETATM 6248 O  O     . HOH   N 6 .   ? -40.57000 -1.42300 1.34500   1.000 48.64515 ? 206 HOH   C O     1 
HETATM 6249 O  O     . HOH   N 6 .   ? -49.87700 19.08600 -15.97900 1.000 29.86185 ? 207 HOH   C O     1 
HETATM 6250 O  O     . HOH   N 6 .   ? -34.39000 -2.74100 3.56800   1.000 42.10958 ? 208 HOH   C O     1 
HETATM 6251 O  O     . HOH   N 6 .   ? -55.69300 5.22600  -5.14500  1.000 56.59385 ? 209 HOH   C O     1 
HETATM 6252 O  O     . HOH   N 6 .   ? -27.00200 4.37400  -1.91500  1.000 35.86734 ? 210 HOH   C O     1 
HETATM 6253 O  O     . HOH   N 6 .   ? -50.39700 -0.28900 17.85400  1.000 48.30543 ? 211 HOH   C O     1 
HETATM 6254 O  O     . HOH   N 6 .   ? -37.24000 0.30200  -5.75000  1.000 36.42385 ? 212 HOH   C O     1 
HETATM 6255 O  O     . HOH   N 6 .   ? -58.93600 8.23500  -1.81000  1.000 58.77864 ? 213 HOH   C O     1 
HETATM 6256 O  O     . HOH   N 6 .   ? -48.89000 22.30900 -11.04100 1.000 40.51718 ? 214 HOH   C O     1 
HETATM 6257 O  O     . HOH   N 6 .   ? -48.86400 -0.68200 -6.85100  1.000 41.75337 ? 215 HOH   C O     1 
HETATM 6258 O  O     . HOH   N 6 .   ? -28.28000 6.12200  -5.54200  1.000 44.40044 ? 216 HOH   C O     1 
HETATM 6259 O  O     . HOH   N 6 .   ? -55.85200 19.33200 17.62300  1.000 59.60378 ? 217 HOH   C O     1 
HETATM 6260 O  O     . HOH   N 6 .   ? -39.45600 -7.26000 13.84300  1.000 44.31806 ? 218 HOH   C O     1 
HETATM 6261 O  O     . HOH   N 6 .   ? -40.25200 5.22200  22.73300  1.000 31.46870 ? 219 HOH   C O     1 
HETATM 6262 O  O     . HOH   N 6 .   ? -44.28100 25.37200 10.68900  1.000 39.59834 ? 220 HOH   C O     1 
HETATM 6263 O  O     . HOH   N 6 .   ? -45.78000 29.96200 3.18200   1.000 35.71889 ? 221 HOH   C O     1 
HETATM 6264 O  O     . HOH   N 6 .   ? -60.19500 8.36600  1.50800   1.000 50.91537 ? 222 HOH   C O     1 
HETATM 6265 O  O     . HOH   N 6 .   ? -35.58400 -2.07200 1.24300   1.000 47.02809 ? 223 HOH   C O     1 
HETATM 6266 O  O     . HOH   N 6 .   ? -29.36700 15.20600 7.25700   1.000 36.93009 ? 224 HOH   C O     1 
HETATM 6267 O  O     . HOH   N 6 .   ? -43.82300 19.47100 1.61800   1.000 15.04104 ? 225 HOH   C O     1 
HETATM 6268 O  O     . HOH   N 6 .   ? -35.07600 12.40800 12.96900  1.000 15.42732 ? 226 HOH   C O     1 
HETATM 6269 O  O     . HOH   N 6 .   ? -57.86300 5.47200  12.28900  1.000 39.71928 ? 227 HOH   C O     1 
HETATM 6270 O  O     . HOH   N 6 .   ? -41.21100 -4.70100 12.90000  1.000 48.82278 ? 228 HOH   C O     1 
HETATM 6271 O  O     . HOH   N 6 .   ? -36.82200 8.30000  23.37300  1.000 27.35041 ? 229 HOH   C O     1 
HETATM 6272 O  O     . HOH   N 6 .   ? -50.63100 0.87400  -5.46500  1.000 32.93919 ? 230 HOH   C O     1 
HETATM 6273 O  O     . HOH   N 6 .   ? -52.39800 10.44300 19.48200  1.000 37.29395 ? 231 HOH   C O     1 
HETATM 6274 O  O     . HOH   N 6 .   ? -42.30400 28.89300 16.67000  1.000 26.18998 ? 232 HOH   C O     1 
HETATM 6275 O  O     . HOH   N 6 .   ? -30.75100 13.82700 14.78800  1.000 22.38297 ? 233 HOH   C O     1 
HETATM 6276 O  O     . HOH   N 6 .   ? -35.90800 11.46500 26.29800  1.000 40.13627 ? 234 HOH   C O     1 
HETATM 6277 O  O     . HOH   N 6 .   ? -39.77100 16.35500 10.45600  1.000 14.02014 ? 235 HOH   C O     1 
HETATM 6278 O  O     . HOH   N 6 .   ? -52.40800 22.32000 5.69900   1.000 32.33102 ? 236 HOH   C O     1 
HETATM 6279 O  O     . HOH   N 6 .   ? -42.70600 17.89700 21.68400  1.000 37.06705 ? 237 HOH   C O     1 
HETATM 6280 O  O     . HOH   N 6 .   ? -26.76500 8.96700  16.79900  1.000 47.76151 ? 238 HOH   C O     1 
HETATM 6281 O  O     . HOH   N 6 .   ? -52.81500 20.28900 -2.96000  1.000 22.36674 ? 239 HOH   C O     1 
HETATM 6282 O  O     . HOH   N 6 .   ? -33.82300 5.08100  13.33500  1.000 14.35189 ? 240 HOH   C O     1 
HETATM 6283 O  O     . HOH   N 6 .   ? -46.73800 21.01300 0.91500   1.000 16.35271 ? 241 HOH   C O     1 
HETATM 6284 O  O     . HOH   N 6 .   ? -39.78300 23.63800 10.37000  1.000 26.89719 ? 242 HOH   C O     1 
HETATM 6285 O  O     . HOH   N 6 .   ? -54.00000 14.84500 12.67000  1.000 18.87187 ? 243 HOH   C O     1 
HETATM 6286 O  O     . HOH   N 6 .   ? -52.03600 26.12500 5.72500   1.000 32.03012 ? 244 HOH   C O     1 
HETATM 6287 O  O     . HOH   N 6 .   ? -31.26900 21.02000 17.31500  1.000 26.48413 ? 245 HOH   C O     1 
HETATM 6288 O  O     . HOH   N 6 .   ? -37.50800 21.56700 -3.97100  1.000 32.04836 ? 246 HOH   C O     1 
HETATM 6289 O  O     . HOH   N 6 .   ? -30.47300 12.99200 18.40100  1.000 18.67134 ? 247 HOH   C O     1 
HETATM 6290 O  O     . HOH   N 6 .   ? -46.28000 16.03600 1.59100   1.000 19.83715 ? 248 HOH   C O     1 
HETATM 6291 O  O     . HOH   N 6 .   ? -38.21800 24.18900 -0.54200  1.000 40.48633 ? 249 HOH   C O     1 
HETATM 6292 O  O     . HOH   N 6 .   ? -47.48700 26.52600 16.99000  1.000 39.65189 ? 250 HOH   C O     1 
HETATM 6293 O  O     . HOH   N 6 .   ? -37.13200 20.18000 11.42300  1.000 21.81679 ? 251 HOH   C O     1 
HETATM 6294 O  O     . HOH   N 6 .   ? -58.67100 7.95600  13.22800  1.000 50.62785 ? 252 HOH   C O     1 
HETATM 6295 O  O     . HOH   N 6 .   ? -32.01700 2.15000  -5.69500  1.000 44.83288 ? 253 HOH   C O     1 
HETATM 6296 O  O     . HOH   N 6 .   ? -28.11800 1.19100  6.78000   1.000 32.78212 ? 254 HOH   C O     1 
HETATM 6297 O  O     . HOH   N 6 .   ? -56.63900 11.48900 18.26500  1.000 43.05744 ? 255 HOH   C O     1 
HETATM 6298 O  O     . HOH   N 6 .   ? -61.19300 12.25800 0.10100   1.000 50.12084 ? 256 HOH   C O     1 
HETATM 6299 O  O     . HOH   N 6 .   ? -44.06200 0.13400  21.13300  1.000 34.07642 ? 257 HOH   C O     1 
HETATM 6300 O  O     . HOH   N 6 .   ? -51.85800 -2.82400 10.17200  1.000 40.23034 ? 258 HOH   C O     1 
HETATM 6301 O  O     . HOH   N 6 .   ? -53.80900 0.20800  10.66000  1.000 20.67431 ? 259 HOH   C O     1 
HETATM 6302 O  O     . HOH   N 6 .   ? -47.57600 9.08500  21.34200  1.000 27.75117 ? 260 HOH   C O     1 
HETATM 6303 O  O     . HOH   N 6 .   ? -37.09400 25.37900 8.05300   1.000 23.09391 ? 261 HOH   C O     1 
HETATM 6304 O  O     . HOH   N 6 .   ? -45.47400 -4.43800 5.41500   1.000 42.85252 ? 262 HOH   C O     1 
HETATM 6305 O  O     . HOH   N 6 .   ? -51.79400 19.26800 4.06100   1.000 27.53462 ? 263 HOH   C O     1 
HETATM 6306 O  O     . HOH   N 6 .   ? -50.49400 27.14800 7.84600   1.000 46.01374 ? 264 HOH   C O     1 
HETATM 6307 O  O     . HOH   N 6 .   ? -47.60500 4.08100  18.12100  1.000 25.01056 ? 265 HOH   C O     1 
HETATM 6308 O  O     . HOH   N 6 .   ? -25.01600 2.23100  10.17800  1.000 56.76099 ? 266 HOH   C O     1 
HETATM 6309 O  O     . HOH   N 6 .   ? -49.55900 4.39100  16.32000  1.000 26.43407 ? 267 HOH   C O     1 
HETATM 6310 O  O     . HOH   N 6 .   ? -43.91600 18.43600 -6.18200  1.000 18.81356 ? 268 HOH   C O     1 
HETATM 6311 O  O     . HOH   N 6 .   ? -48.79100 20.74800 17.28200  1.000 38.65026 ? 269 HOH   C O     1 
HETATM 6312 O  O     . HOH   N 6 .   ? -35.65200 3.70500  -7.98000  1.000 38.46813 ? 270 HOH   C O     1 
HETATM 6313 O  O     . HOH   N 6 .   ? -43.55100 10.96400 12.65900  1.000 15.03259 ? 271 HOH   C O     1 
HETATM 6314 O  O     . HOH   N 6 .   ? -50.77300 17.32300 -7.65900  1.000 17.14294 ? 272 HOH   C O     1 
HETATM 6315 O  O     . HOH   N 6 .   ? -24.93800 3.52200  -0.17800  1.000 50.65971 ? 273 HOH   C O     1 
HETATM 6316 O  O     . HOH   N 6 .   ? -58.31500 17.58100 -14.79300 1.000 19.14251 ? 274 HOH   C O     1 
HETATM 6317 O  O     . HOH   N 6 .   ? -34.91600 20.85000 -3.12000  1.000 27.17604 ? 275 HOH   C O     1 
HETATM 6318 O  O     . HOH   N 6 .   ? -52.23800 17.25100 18.48700  1.000 47.36730 ? 276 HOH   C O     1 
HETATM 6319 O  O     . HOH   N 6 .   ? -55.90600 17.75400 -12.48500 1.000 25.84059 ? 277 HOH   C O     1 
HETATM 6320 O  O     . HOH   N 6 .   ? -51.42400 -2.13700 1.69900   1.000 49.01922 ? 278 HOH   C O     1 
HETATM 6321 O  O     . HOH   N 6 .   ? -56.60300 21.34900 15.04400  1.000 42.41673 ? 279 HOH   C O     1 
HETATM 6322 O  O     . HOH   N 6 .   ? -32.70000 12.81200 21.84600  1.000 42.03046 ? 280 HOH   C O     1 
HETATM 6323 O  O     . HOH   N 6 .   ? -57.17400 7.38000  17.12000  1.000 51.72554 ? 281 HOH   C O     1 
HETATM 6324 O  O     . HOH   N 6 .   ? -47.27700 -2.83800 -4.82400  1.000 50.86500 ? 282 HOH   C O     1 
HETATM 6325 O  O     . HOH   N 6 .   ? -37.07700 20.83800 2.72000   1.000 17.72896 ? 283 HOH   C O     1 
HETATM 6326 O  O     . HOH   N 6 .   ? -40.17200 20.50700 13.58200  1.000 31.62587 ? 284 HOH   C O     1 
HETATM 6327 O  O     . HOH   N 6 .   ? -38.37500 10.68100 16.67400  1.000 15.08498 ? 285 HOH   C O     1 
HETATM 6328 O  O     . HOH   N 6 .   ? -55.52500 0.07600  -0.37600  1.000 35.17160 ? 286 HOH   C O     1 
HETATM 6329 O  O     . HOH   N 6 .   ? -40.48700 20.94400 -6.20400  1.000 24.22638 ? 287 HOH   C O     1 
HETATM 6330 O  O     . HOH   N 6 .   ? -52.32400 -0.58400 -3.09400  1.000 48.14254 ? 288 HOH   C O     1 
HETATM 6331 O  O     . HOH   N 6 .   ? -44.95300 -5.70400 14.97100  1.000 41.00805 ? 289 HOH   C O     1 
HETATM 6332 O  O     . HOH   N 6 .   ? -42.00600 24.23200 11.81000  1.000 49.04316 ? 290 HOH   C O     1 
HETATM 6333 O  O     . HOH   N 6 .   ? -37.60600 18.94400 -12.33000 1.000 36.13641 ? 291 HOH   C O     1 
HETATM 6334 O  O     . HOH   N 6 .   ? -54.13200 8.91500  -6.58800  1.000 24.73406 ? 292 HOH   C O     1 
HETATM 6335 O  O     . HOH   N 6 .   ? -32.72100 23.68700 13.44800  1.000 43.47929 ? 293 HOH   C O     1 
HETATM 6336 O  O     . HOH   N 6 .   ? -34.49000 -1.10200 8.36500   1.000 27.10783 ? 294 HOH   C O     1 
HETATM 6337 O  O     . HOH   N 6 .   ? -43.73600 -6.66200 7.31700   1.000 57.04886 ? 295 HOH   C O     1 
HETATM 6338 O  O     . HOH   N 6 .   ? -34.45900 15.61300 14.67200  1.000 14.60413 ? 296 HOH   C O     1 
HETATM 6339 O  O     . HOH   N 6 .   ? -37.74200 18.46000 20.38600  1.000 45.73081 ? 297 HOH   C O     1 
HETATM 6340 O  O     . HOH   N 6 .   ? -38.58900 0.70000  21.31600  1.000 33.85003 ? 298 HOH   C O     1 
HETATM 6341 O  O     . HOH   N 6 .   ? -59.71000 4.92200  0.23900   1.000 49.93458 ? 299 HOH   C O     1 
HETATM 6342 O  O     . HOH   N 6 .   ? -43.09800 2.91400  -11.96900 1.000 39.15315 ? 300 HOH   C O     1 
HETATM 6343 O  O     . HOH   N 6 .   ? -36.27400 2.69100  -5.64100  1.000 34.97295 ? 301 HOH   C O     1 
HETATM 6344 O  O     . HOH   N 6 .   ? -33.82100 21.11900 -11.42300 1.000 36.69742 ? 302 HOH   C O     1 
HETATM 6345 O  O     . HOH   N 6 .   ? -34.68600 20.91500 19.41000  1.000 36.84111 ? 303 HOH   C O     1 
HETATM 6346 O  O     . HOH   N 6 .   ? -38.78100 10.12700 22.95600  1.000 30.17517 ? 304 HOH   C O     1 
HETATM 6347 O  O     . HOH   N 6 .   ? -35.74400 3.63900  14.74300  1.000 15.05239 ? 305 HOH   C O     1 
HETATM 6348 O  O     . HOH   N 6 .   ? -41.20400 12.29800 24.98600  1.000 65.83156 ? 306 HOH   C O     1 
HETATM 6349 O  O     . HOH   N 6 .   ? -46.56100 21.48000 -13.95500 1.000 60.06878 ? 307 HOH   C O     1 
HETATM 6350 O  O     . HOH   N 6 .   ? -42.34300 -5.44800 10.97800  1.000 46.08949 ? 308 HOH   C O     1 
HETATM 6351 O  O     . HOH   N 6 .   ? -43.24700 8.71300  -13.86800 1.000 37.12656 ? 309 HOH   C O     1 
HETATM 6352 O  O     . HOH   N 6 .   ? -57.78100 16.41200 -8.17100  1.000 26.60378 ? 310 HOH   C O     1 
HETATM 6353 O  O     . HOH   N 6 .   ? -27.82000 20.15500 -10.83100 1.000 42.86755 ? 311 HOH   C O     1 
HETATM 6354 O  O     . HOH   N 6 .   ? -53.89400 17.46100 -4.52400  1.000 34.87449 ? 312 HOH   C O     1 
HETATM 6355 O  O     . HOH   N 6 .   ? -44.82200 -1.90900 -6.43300  1.000 33.88995 ? 313 HOH   C O     1 
HETATM 6356 O  O     . HOH   N 6 .   ? -43.68800 21.17600 -10.37700 1.000 35.10589 ? 314 HOH   C O     1 
HETATM 6357 O  O     . HOH   N 6 .   ? -37.56400 4.17100  22.12000  1.000 24.64312 ? 315 HOH   C O     1 
HETATM 6358 O  O     . HOH   N 6 .   ? -29.58800 1.02200  -2.81700  1.000 41.78809 ? 316 HOH   C O     1 
HETATM 6359 O  O     . HOH   N 6 .   ? -29.74800 15.35200 10.76900  1.000 33.37527 ? 317 HOH   C O     1 
HETATM 6360 O  O     . HOH   N 6 .   ? -31.11600 6.00100  11.99900  1.000 19.41551 ? 318 HOH   C O     1 
HETATM 6361 O  O     . HOH   N 6 .   ? -58.29600 7.15400  7.95600   1.000 28.54460 ? 319 HOH   C O     1 
HETATM 6362 O  O     . HOH   N 6 .   ? -47.40900 -5.56000 13.58600  1.000 25.94722 ? 320 HOH   C O     1 
HETATM 6363 O  O     . HOH   N 6 .   ? -54.35600 14.38500 6.62400   1.000 17.93505 ? 321 HOH   C O     1 
HETATM 6364 O  O     . HOH   N 6 .   ? -41.48400 19.15500 9.63200   1.000 18.49522 ? 322 HOH   C O     1 
HETATM 6365 O  O     . HOH   N 6 .   ? -53.86100 8.60200  19.82700  1.000 53.06508 ? 323 HOH   C O     1 
HETATM 6366 O  O     . HOH   N 6 .   ? -44.41300 -2.24900 -3.25100  1.000 31.27971 ? 324 HOH   C O     1 
HETATM 6367 O  O     . HOH   N 6 .   ? -45.41800 28.23700 14.19500  1.000 45.92010 ? 325 HOH   C O     1 
HETATM 6368 O  O     . HOH   N 6 .   ? -33.81300 23.34400 -5.08400  1.000 33.75722 ? 326 HOH   C O     1 
HETATM 6369 O  O     . HOH   N 6 .   ? -40.28400 15.28000 22.38000  1.000 38.08225 ? 327 HOH   C O     1 
HETATM 6370 O  O     . HOH   N 6 .   ? -52.24000 2.32700  -7.14600  1.000 35.68584 ? 328 HOH   C O     1 
HETATM 6371 O  O     . HOH   N 6 .   ? -39.68900 11.17900 20.71300  1.000 26.66428 ? 329 HOH   C O     1 
HETATM 6372 O  O     . HOH   N 6 .   ? -38.01100 16.03500 -13.85300 1.000 40.85549 ? 330 HOH   C O     1 
HETATM 6373 O  O     . HOH   N 6 .   ? -42.20700 -6.65900 16.96500  1.000 44.66483 ? 331 HOH   C O     1 
HETATM 6374 O  O     . HOH   N 6 .   ? -30.67700 17.81100 8.72100   1.000 24.93016 ? 332 HOH   C O     1 
HETATM 6375 O  O     . HOH   N 6 .   ? -53.06900 5.55200  18.78700  1.000 36.91361 ? 333 HOH   C O     1 
HETATM 6376 O  O     . HOH   N 6 .   ? -59.03800 9.70400  7.84100   1.000 33.03541 ? 334 HOH   C O     1 
HETATM 6377 O  O     . HOH   N 6 .   ? -50.58200 14.49000 21.07600  1.000 45.87608 ? 335 HOH   C O     1 
HETATM 6378 O  O     . HOH   N 6 .   ? -36.35000 21.83700 -0.56500  1.000 46.52671 ? 336 HOH   C O     1 
HETATM 6379 O  O     . HOH   N 6 .   ? -53.47300 23.60000 12.16700  1.000 46.74392 ? 337 HOH   C O     1 
HETATM 6380 O  O     . HOH   N 6 .   ? -51.73900 6.51800  -13.14200 1.000 46.19399 ? 338 HOH   C O     1 
HETATM 6381 O  O     . HOH   N 6 .   ? -57.81200 17.42300 9.22900   1.000 47.14451 ? 339 HOH   C O     1 
HETATM 6382 O  O     . HOH   N 6 .   ? -54.09900 2.46500  15.26100  1.000 35.02388 ? 340 HOH   C O     1 
HETATM 6383 O  O     . HOH   N 6 .   ? -31.42000 19.24000 21.07400  1.000 40.34378 ? 341 HOH   C O     1 
HETATM 6384 O  O     . HOH   N 6 .   ? -51.54700 21.52600 -5.08900  1.000 21.44194 ? 342 HOH   C O     1 
HETATM 6385 O  O     . HOH   N 6 .   ? -56.48800 12.90700 -7.85700  1.000 41.45767 ? 343 HOH   C O     1 
HETATM 6386 O  O     . HOH   N 6 .   ? -42.65400 27.73700 10.00800  1.000 49.89808 ? 344 HOH   C O     1 
HETATM 6387 O  O     . HOH   N 6 .   ? -42.73500 16.18800 -16.51200 1.000 50.30878 ? 345 HOH   C O     1 
HETATM 6388 O  O     . HOH   N 6 .   ? -56.62600 12.79000 6.14500   1.000 29.34970 ? 346 HOH   C O     1 
HETATM 6389 O  O     . HOH   N 6 .   ? -30.34000 13.03100 -9.17100  1.000 39.46020 ? 347 HOH   C O     1 
HETATM 6390 O  O     . HOH   N 6 .   ? -52.33500 3.27900  -10.08600 1.000 50.94991 ? 348 HOH   C O     1 
HETATM 6391 O  O     . HOH   N 6 .   ? -29.18500 15.81900 13.60400  1.000 38.70119 ? 349 HOH   C O     1 
HETATM 6392 O  O     . HOH   N 6 .   ? -31.47500 16.51100 -12.93300 1.000 39.08379 ? 350 HOH   C O     1 
HETATM 6393 O  O     . HOH   N 6 .   ? -28.71300 12.66100 16.22400  1.000 22.00965 ? 351 HOH   C O     1 
HETATM 6394 O  O     . HOH   N 6 .   ? -32.50100 3.53900  3.08400   1.000 20.88278 ? 352 HOH   C O     1 
HETATM 6395 O  O     . HOH   N 6 .   ? -57.89900 9.31400  -4.24100  1.000 45.44053 ? 353 HOH   C O     1 
HETATM 6396 O  O     . HOH   N 6 .   ? -38.85900 23.38600 -3.00200  1.000 53.14415 ? 354 HOH   C O     1 
HETATM 6397 O  O     . HOH   N 6 .   ? -47.04300 -5.98500 11.30800  1.000 42.34942 ? 355 HOH   C O     1 
HETATM 6398 O  O     . HOH   N 6 .   ? -46.66800 -0.07300 20.48200  1.000 52.74910 ? 356 HOH   C O     1 
HETATM 6399 O  O     . HOH   N 6 .   ? -43.92700 22.05600 0.53600   1.000 23.37954 ? 357 HOH   C O     1 
HETATM 6400 O  O     . HOH   N 6 .   ? -43.34200 21.18500 -5.92900  1.000 30.03789 ? 358 HOH   C O     1 
HETATM 6401 O  O     . HOH   N 6 .   ? -43.36500 20.54500 22.15500  1.000 43.61238 ? 359 HOH   C O     1 
HETATM 6402 O  O     . HOH   N 6 .   ? -43.78200 27.16300 -2.59600  1.000 47.99913 ? 360 HOH   C O     1 
HETATM 6403 O  O     . HOH   N 6 .   ? -27.05500 4.59500  14.33800  1.000 40.79255 ? 361 HOH   C O     1 
HETATM 6404 O  O     . HOH   N 6 .   ? -56.45200 0.08000  -2.51300  1.000 47.21132 ? 362 HOH   C O     1 
HETATM 6405 O  O     . HOH   N 6 .   ? -41.45500 0.17000  22.38400  1.000 38.52299 ? 363 HOH   C O     1 
HETATM 6406 O  O     . HOH   N 6 .   ? -30.92000 20.08800 -11.31800 1.000 55.82133 ? 364 HOH   C O     1 
HETATM 6407 O  O     . HOH   N 6 .   ? -33.21400 6.66000  -10.33700 1.000 48.73600 ? 365 HOH   C O     1 
HETATM 6408 O  O     . HOH   N 6 .   ? -38.23800 -2.02900 3.00900   1.000 40.22767 ? 366 HOH   C O     1 
HETATM 6409 O  O     . HOH   N 6 .   ? -39.32100 -3.52200 12.10100  1.000 57.16237 ? 367 HOH   C O     1 
HETATM 6410 O  O     . HOH   N 6 .   ? -35.58100 8.04800  -11.22400 1.000 54.62510 ? 368 HOH   C O     1 
HETATM 6411 O  O     . HOH   N 6 .   ? -38.61100 6.86500  24.63300  1.000 54.00441 ? 369 HOH   C O     1 
HETATM 6412 O  O     . HOH   N 6 .   ? -45.85000 20.75700 -16.57700 1.000 52.96935 ? 370 HOH   C O     1 
HETATM 6413 O  O     . HOH   N 6 .   ? -47.99500 23.37400 17.37400  1.000 32.21926 ? 371 HOH   C O     1 
HETATM 6414 O  O     . HOH   N 6 .   ? -50.96600 21.77400 -9.31600  1.000 51.03437 ? 372 HOH   C O     1 
HETATM 6415 O  O     . HOH   N 6 .   ? -57.46700 1.75600  -3.90800  1.000 61.24121 ? 373 HOH   C O     1 
HETATM 6416 O  O     . HOH   N 6 .   ? -51.61500 19.94800 -7.35100  1.000 23.87858 ? 374 HOH   C O     1 
HETATM 6417 O  O     . HOH   N 6 .   ? -39.81700 20.92200 10.89200  1.000 34.65207 ? 375 HOH   C O     1 
HETATM 6418 O  O     . HOH   N 6 .   ? -44.00500 22.41700 -8.22400  1.000 47.54987 ? 376 HOH   C O     1 
HETATM 6419 O  O     . HOH   N 6 .   ? -37.43700 22.36700 20.25000  1.000 47.98683 ? 377 HOH   C O     1 
HETATM 6420 O  O     . HOH   N 6 .   ? -52.95400 -3.00500 4.32000   1.000 52.40197 ? 378 HOH   C O     1 
HETATM 6421 O  O     . HOH   N 6 .   ? -48.62700 23.42500 -14.54100 1.000 44.65898 ? 379 HOH   C O     1 
HETATM 6422 O  O     . HOH   N 6 .   ? -45.70300 -3.33700 -9.22200  1.000 62.96061 ? 380 HOH   C O     1 
HETATM 6423 O  O     . HOH   N 6 .   ? -49.06800 26.28000 12.18300  1.000 47.99290 ? 381 HOH   C O     1 
HETATM 6424 O  O     . HOH   N 6 .   ? -39.62500 23.21900 13.92200  1.000 51.00393 ? 382 HOH   C O     1 
HETATM 6425 O  O     . HOH   N 6 .   ? -43.72000 30.11600 14.56000  1.000 49.90585 ? 383 HOH   C O     1 
HETATM 6426 O  O     . HOH   N 6 .   ? -51.16400 -5.77900 8.47000   1.000 47.28148 ? 384 HOH   C O     1 
HETATM 6427 O  O     . HOH   N 6 .   ? -51.96100 23.07100 9.96300   1.000 36.18569 ? 385 HOH   C O     1 
HETATM 6428 O  O     . HOH   N 6 .   ? -36.71300 1.67300  22.80700  1.000 35.28569 ? 386 HOH   C O     1 
HETATM 6429 O  O     . HOH   N 6 .   ? -42.51800 28.39400 12.50900  1.000 55.92153 ? 387 HOH   C O     1 
HETATM 6430 O  O     . HOH   N 6 .   ? -51.55600 2.50600  16.55600  1.000 32.67737 ? 388 HOH   C O     1 
HETATM 6431 O  O     . HOH   N 6 .   ? -41.74300 12.86500 22.32900  1.000 42.49701 ? 389 HOH   C O     1 
HETATM 6432 O  O     . HOH   N 6 .   ? -48.02700 2.14500  20.02100  1.000 54.76890 ? 390 HOH   C O     1 
HETATM 6433 O  O     . HOH   N 6 .   ? -46.44300 10.37100 23.46000  1.000 49.98529 ? 391 HOH   C O     1 
HETATM 6434 O  O     . HOH   N 6 .   ? -54.38800 19.63800 -6.71500  1.000 25.90415 ? 392 HOH   C O     1 
HETATM 6435 O  O     . HOH   N 6 .   ? -51.47800 24.56200 -7.85100  1.000 53.10732 ? 393 HOH   C O     1 
HETATM 6436 O  O     . HOH   N 6 .   ? -50.61600 25.99600 9.97000   1.000 47.43808 ? 394 HOH   C O     1 
HETATM 6437 O  O     . HOH   N 6 .   ? -46.10400 -2.23300 21.07000  1.000 55.24134 ? 395 HOH   C O     1 
HETATM 6438 O  O     . HOH   N 6 .   ? -59.42300 6.12500  9.98100   1.000 48.19646 ? 396 HOH   C O     1 
HETATM 6439 O  O     . HOH   N 6 .   ? -41.39600 27.20500 -2.93700  1.000 59.77808 ? 397 HOH   C O     1 
HETATM 6440 O  O     . HOH   N 6 .   ? -36.18100 24.66700 10.39600  1.000 49.03631 ? 398 HOH   C O     1 
HETATM 6441 O  O     . HOH   N 6 .   ? -38.62600 -9.51600 16.12900  1.000 34.82198 ? 399 HOH   C O     1 
HETATM 6442 O  O     . HOH   N 6 .   ? -26.98200 5.83400  16.53000  1.000 49.98977 ? 400 HOH   C O     1 
HETATM 6443 O  O     . HOH   N 6 .   ? -50.36100 9.76600  21.61100  1.000 43.04653 ? 401 HOH   C O     1 
HETATM 6444 O  O     . HOH   N 6 .   ? -37.09900 -2.08000 7.81800   1.000 54.72399 ? 402 HOH   C O     1 
HETATM 6445 O  O     . HOH   N 6 .   ? -28.72800 20.97400 18.18600  1.000 41.38992 ? 403 HOH   C O     1 
HETATM 6446 O  O     . HOH   N 6 .   ? -37.04200 22.69100 11.76800  1.000 37.69976 ? 404 HOH   C O     1 
HETATM 6447 O  O     . HOH   N 6 .   ? -36.98200 28.22800 8.51600   1.000 37.88068 ? 405 HOH   C O     1 
HETATM 6448 O  O     . HOH   N 6 .   ? -42.93900 15.84800 22.84000  1.000 40.53089 ? 406 HOH   C O     1 
HETATM 6449 O  O     . HOH   N 6 .   ? -56.91000 -1.75400 1.00800   1.000 49.36349 ? 407 HOH   C O     1 
HETATM 6450 O  O     . HOH   N 6 .   ? -44.13500 22.99400 -3.96300  1.000 40.30382 ? 408 HOH   C O     1 
HETATM 6451 O  O     . HOH   N 6 .   ? -56.39100 10.72600 -6.37100  1.000 44.75920 ? 409 HOH   C O     1 
HETATM 6452 O  O     . HOH   N 6 .   ? -45.09500 15.11400 23.98300  1.000 56.11068 ? 410 HOH   C O     1 
HETATM 6453 O  O     . HOH   N 6 .   ? -46.52400 1.67500  22.52500  1.000 57.20402 ? 411 HOH   C O     1 
HETATM 6454 O  O     . HOH   N 6 .   ? -22.75700 7.36600  -0.59800  1.000 61.89822 ? 412 HOH   C O     1 
HETATM 6455 O  O     . HOH   N 6 .   ? -22.02600 10.90200 2.87600   1.000 55.95603 ? 413 HOH   C O     1 
HETATM 6456 O  O     . HOH   N 6 .   ? -52.71700 2.79100  19.14000  1.000 54.95499 ? 414 HOH   C O     1 
HETATM 6457 O  O     . HOH   N 6 .   ? -26.57900 20.68500 16.66200  1.000 56.99055 ? 415 HOH   C O     1 
HETATM 6458 O  O     . HOH   N 6 .   ? -42.88500 10.83400 -16.11500 1.000 38.98699 ? 416 HOH   C O     1 
HETATM 6459 O  O     . HOH   N 6 .   ? -25.42900 16.48900 15.80400  1.000 52.36667 ? 417 HOH   C O     1 
HETATM 6460 O  O     . HOH   N 6 .   ? -49.35400 7.96700  -14.87700 1.000 53.21749 ? 418 HOH   C O     1 
HETATM 6461 O  O     A HOH   N 6 .   ? -23.78600 9.48100  -1.35700  0.500 41.61132 ? 419 HOH   C O     1 
HETATM 6462 O  O     B HOH   N 6 .   ? -22.74300 10.30000 0.20600   0.500 40.08485 ? 419 HOH   C O     1 
HETATM 6463 O  O     . HOH   N 6 .   ? -25.25700 18.85200 17.80600  1.000 36.60250 ? 420 HOH   C O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N     . SER   A 1   ? 0.39894 0.38232 0.43238 0.02562  -0.11715 0.11863  0   SER   A N     
2    C  CA    . SER   A 1   ? 0.34098 0.38406 0.38682 0.00620  -0.18736 0.11265  0   SER   A CA    
3    C  C     . SER   A 1   ? 0.30900 0.37770 0.37325 0.02888  -0.14396 0.09564  0   SER   A C     
4    O  O     . SER   A 1   ? 0.40148 0.38940 0.39163 0.02840  -0.11479 0.03393  0   SER   A O     
5    C  CB    . SER   A 1   ? 0.26443 0.41633 0.45927 -0.00002 -0.16393 0.12388  0   SER   A CB    
6    O  OG    . SER   A 1   ? 0.30077 0.43987 0.45650 0.00070  -0.09896 0.13336  0   SER   A OG    
7    N  N     . MET   A 2   ? 0.25546 0.38242 0.30436 -0.01968 -0.08244 0.10356  1   MET   A N     
8    C  CA    . MET   A 2   ? 0.18952 0.32564 0.23606 0.01345  -0.06822 0.08133  1   MET   A CA    
9    C  C     . MET   A 2   ? 0.17177 0.27345 0.20269 -0.01760 -0.04546 0.01827  1   MET   A C     
10   O  O     . MET   A 2   ? 0.19236 0.26227 0.19465 0.00903  -0.04113 0.02859  1   MET   A O     
11   C  CB    . MET   A 2   ? 0.33798 0.34200 0.29675 0.00327  0.02705  0.06606  1   MET   A CB    
12   C  CG    . MET   A 2   ? 0.32018 0.31281 0.36303 -0.00978 0.00586  0.03159  1   MET   A CG    
13   S  SD    . MET   A 2   ? 0.24455 0.31168 0.35628 0.01661  -0.02876 0.01232  1   MET   A SD    
14   C  CE    . MET   A 2   ? 0.26323 0.33869 0.33873 0.03715  -0.02762 0.02064  1   MET   A CE    
15   N  N     . THR   A 3   ? 0.17843 0.26692 0.15606 0.02480  -0.04116 0.00785  2   THR   A N     
16   C  CA    . THR   A 3   ? 0.21529 0.28662 0.17492 0.02358  -0.02967 0.04833  2   THR   A CA    
17   C  C     . THR   A 3   ? 0.13466 0.26148 0.18064 0.03192  -0.01059 0.05919  2   THR   A C     
18   O  O     . THR   A 3   ? 0.18763 0.26358 0.24741 0.00548  -0.07685 0.06321  2   THR   A O     
19   C  CB    . THR   A 3   ? 0.22557 0.30779 0.17955 0.05943  -0.05951 0.04244  2   THR   A CB    
20   O  OG1   . THR   A 3   ? 0.20863 0.33664 0.21266 0.03762  -0.05973 0.01793  2   THR   A OG1   
21   C  CG2   . THR   A 3   ? 0.19760 0.32983 0.21412 0.04082  -0.02651 0.03201  2   THR   A CG2   
22   N  N     . GLU   A 4   ? 0.19912 0.23819 0.16356 0.01849  -0.04263 0.05426  3   GLU   A N     
23   C  CA    . GLU   A 4   ? 0.17128 0.22482 0.16577 0.03266  -0.03869 0.03269  3   GLU   A CA    
24   C  C     . GLU   A 4   ? 0.17537 0.21742 0.17649 0.00708  -0.02277 0.01830  3   GLU   A C     
25   O  O     . GLU   A 4   ? 0.16975 0.24024 0.16742 -0.00123 -0.02014 0.03441  3   GLU   A O     
26   C  CB    . GLU   A 4   ? 0.20059 0.24529 0.16604 0.00590  0.00167  0.01376  3   GLU   A CB    
27   C  CG    . GLU   A 4   ? 0.18878 0.25719 0.19607 0.02759  -0.02312 0.05021  3   GLU   A CG    
28   C  CD    . GLU   A 4   ? 0.30007 0.27266 0.21772 0.02944  -0.04548 0.05723  3   GLU   A CD    
29   O  OE1   . GLU   A 4   ? 0.34648 0.25908 0.21572 0.00703  -0.02432 -0.00537 3   GLU   A OE1   
30   O  OE2   . GLU   A 4   ? 0.35946 0.29930 0.24117 0.08311  -0.03616 0.02637  3   GLU   A OE2   
31   N  N     . TYR   A 5   ? 0.18292 0.20079 0.14537 0.03130  -0.02637 -0.00540 4   TYR   A N     
32   C  CA    . TYR   A 5   ? 0.16211 0.21233 0.18941 0.04450  0.00661  0.00976  4   TYR   A CA    
33   C  C     . TYR   A 5   ? 0.15987 0.19961 0.17114 0.03162  0.00584  0.03285  4   TYR   A C     
34   O  O     . TYR   A 5   ? 0.17447 0.21814 0.17734 0.02724  -0.01583 0.02765  4   TYR   A O     
35   C  CB    . TYR   A 5   ? 0.15553 0.21767 0.17732 0.05439  -0.01662 0.00263  4   TYR   A CB    
36   C  CG    . TYR   A 5   ? 0.19885 0.19957 0.12809 0.03983  -0.01436 -0.01719 4   TYR   A CG    
37   C  CD1   . TYR   A 5   ? 0.18118 0.22098 0.18286 0.04461  -0.02046 -0.01146 4   TYR   A CD1   
38   C  CD2   . TYR   A 5   ? 0.18929 0.20211 0.15676 0.02098  -0.02688 0.00168  4   TYR   A CD2   
39   C  CE1   . TYR   A 5   ? 0.19949 0.22663 0.16786 0.00777  -0.01594 -0.00122 4   TYR   A CE1   
40   C  CE2   . TYR   A 5   ? 0.18449 0.20244 0.20689 0.04054  -0.02994 0.00174  4   TYR   A CE2   
41   C  CZ    . TYR   A 5   ? 0.17357 0.22602 0.18986 0.02691  -0.05540 0.02042  4   TYR   A CZ    
42   O  OH    . TYR   A 5   ? 0.20566 0.23375 0.23715 0.03324  -0.05849 0.02255  4   TYR   A OH    
43   N  N     . LYS   A 6   ? 0.18198 0.22087 0.14977 -0.00565 -0.03524 -0.01117 5   LYS   A N     
44   C  CA    . LYS   A 6   ? 0.20898 0.19493 0.15631 0.01622  -0.02309 -0.00668 5   LYS   A CA    
45   C  C     . LYS   A 6   ? 0.13403 0.19909 0.13799 0.01014  -0.00488 0.02101  5   LYS   A C     
46   O  O     . LYS   A 6   ? 0.14592 0.20959 0.15005 -0.00568 -0.00620 0.00961  5   LYS   A O     
47   C  CB    . LYS   A 6   ? 0.27570 0.20022 0.15996 -0.00743 0.01024  -0.02181 5   LYS   A CB    
48   C  CG    . LYS   A 6   ? 0.35935 0.22828 0.20484 0.00450  -0.05038 -0.03620 5   LYS   A CG    
49   C  CD    . LYS   A 6   ? 0.49072 0.28029 0.30809 0.00338  -0.09367 -0.03489 5   LYS   A CD    
50   C  CE    . LYS   A 6   ? 0.56777 0.30540 0.43366 0.01875  -0.11341 -0.06003 5   LYS   A CE    
51   N  NZ    . LYS   A 6   ? 0.61882 0.31293 0.43512 0.05066  -0.15598 -0.12055 5   LYS   A NZ    
52   N  N     . LEU   A 7   ? 0.16928 0.18319 0.13441 -0.02410 -0.01265 0.00320  6   LEU   A N     
53   C  CA    . LEU   A 7   ? 0.16864 0.17172 0.15361 0.01862  -0.02285 0.00757  6   LEU   A CA    
54   C  C     . LEU   A 7   ? 0.13965 0.18651 0.14001 0.01978  -0.03020 0.00707  6   LEU   A C     
55   O  O     . LEU   A 7   ? 0.16296 0.23951 0.16019 0.05689  -0.00829 -0.00416 6   LEU   A O     
56   C  CB    . LEU   A 7   ? 0.19935 0.16713 0.19291 0.03006  -0.02820 0.04975  6   LEU   A CB    
57   C  CG    . LEU   A 7   ? 0.15705 0.18697 0.24057 0.00253  -0.01693 0.01440  6   LEU   A CG    
58   C  CD1   . LEU   A 7   ? 0.18679 0.20223 0.23111 -0.02679 -0.02770 0.02451  6   LEU   A CD1   
59   C  CD2   . LEU   A 7   ? 0.18939 0.20577 0.21661 0.03057  -0.04104 -0.01254 6   LEU   A CD2   
60   N  N     . VAL   A 8   ? 0.14475 0.16186 0.12684 0.00997  -0.02765 -0.00645 7   VAL   A N     
61   C  CA    . VAL   A 8   ? 0.14589 0.16371 0.13283 0.00197  -0.02302 0.01220  7   VAL   A CA    
62   C  C     . VAL   A 8   ? 0.13508 0.17518 0.12121 -0.00944 -0.04755 -0.00112 7   VAL   A C     
63   O  O     . VAL   A 8   ? 0.13293 0.18205 0.15989 0.00498  -0.01187 -0.02107 7   VAL   A O     
64   C  CB    . VAL   A 8   ? 0.15255 0.15550 0.15673 -0.02263 -0.01657 0.00152  7   VAL   A CB    
65   C  CG1   . VAL   A 8   ? 0.18162 0.14390 0.16672 -0.01194 -0.02874 0.02716  7   VAL   A CG1   
66   C  CG2   . VAL   A 8   ? 0.20611 0.16826 0.16025 -0.02234 -0.02938 -0.00848 7   VAL   A CG2   
67   N  N     . VAL   A 9   ? 0.13821 0.16159 0.14365 -0.01129 -0.03922 -0.00494 8   VAL   A N     
68   C  CA    . VAL   A 9   ? 0.11566 0.16623 0.16243 -0.01022 -0.04256 0.00791  8   VAL   A CA    
69   C  C     . VAL   A 9   ? 0.11699 0.15238 0.15874 0.00450  -0.02650 0.01151  8   VAL   A C     
70   O  O     . VAL   A 9   ? 0.16149 0.15431 0.16099 0.04296  -0.01061 0.00668  8   VAL   A O     
71   C  CB    . VAL   A 9   ? 0.16939 0.17622 0.14215 -0.02257 -0.05192 0.02301  8   VAL   A CB    
72   C  CG1   . VAL   A 9   ? 0.18553 0.16669 0.15307 -0.01483 -0.02707 0.02415  8   VAL   A CG1   
73   C  CG2   . VAL   A 9   ? 0.20735 0.19414 0.15375 -0.02821 -0.02331 0.01169  8   VAL   A CG2   
74   N  N     . VAL   A 10  ? 0.12921 0.17872 0.13625 -0.00182 -0.01238 -0.01294 9   VAL   A N     
75   C  CA    . VAL   A 10  ? 0.12410 0.17656 0.12162 -0.01413 -0.03592 0.00717  9   VAL   A CA    
76   C  C     . VAL   A 10  ? 0.13185 0.17278 0.12220 -0.02383 -0.02912 0.02366  9   VAL   A C     
77   O  O     . VAL   A 10  ? 0.17835 0.16243 0.15944 0.01108  -0.04340 -0.01175 9   VAL   A O     
78   C  CB    . VAL   A 10  ? 0.13407 0.18688 0.19086 -0.03277 -0.00836 -0.00985 9   VAL   A CB    
79   C  CG1   . VAL   A 10  ? 0.16656 0.21978 0.17196 -0.01245 -0.02875 -0.02670 9   VAL   A CG1   
80   C  CG2   . VAL   A 10  ? 0.14054 0.19390 0.22405 -0.00266 -0.01504 -0.00331 9   VAL   A CG2   
81   N  N     . GLY   A 11  ? 0.14516 0.18799 0.13702 0.01002  -0.03876 -0.01143 10  GLY   A N     
82   C  CA    . GLY   A 11  ? 0.18383 0.17706 0.13808 0.02652  -0.02609 -0.03284 10  GLY   A CA    
83   C  C     . GLY   A 11  ? 0.16435 0.17370 0.16667 0.03496  -0.00876 -0.01652 10  GLY   A C     
84   O  O     . GLY   A 11  ? 0.17989 0.17807 0.16298 0.00366  -0.02676 0.01026  10  GLY   A O     
85   N  N     . ALA   A 12  ? 0.18471 0.19325 0.13733 0.02364  -0.02370 -0.01320 11  ALA   A N     
86   C  CA    . ALA   A 12  ? 0.18544 0.21651 0.15073 0.02320  -0.03484 0.00195  11  ALA   A CA    
87   C  C     . ALA   A 12  ? 0.17658 0.22128 0.15692 0.02920  -0.06600 0.00569  11  ALA   A C     
88   O  O     . ALA   A 12  ? 0.16828 0.20043 0.17384 -0.00911 -0.04079 0.00184  11  ALA   A O     
89   C  CB    . ALA   A 12  ? 0.25779 0.22741 0.13459 0.04029  -0.03725 0.01654  11  ALA   A CB    
90   N  N     . CYS   A 13  ? 0.17964 0.23860 0.18003 0.04304  -0.06374 -0.00921 12  CYS   A N     
91   C  CA    . CYS   A 13  ? 0.15646 0.26376 0.19204 0.03659  -0.04606 0.00107  12  CYS   A CA    
92   C  C     . CYS   A 13  ? 0.16234 0.23060 0.17093 0.00992  -0.03743 -0.00874 12  CYS   A C     
93   O  O     . CYS   A 13  ? 0.22369 0.22069 0.19424 0.02289  -0.05881 -0.00897 12  CYS   A O     
94   C  CB    . CYS   A 13  ? 0.21163 0.32301 0.19690 0.09293  0.02296  0.00079  12  CYS   A CB    
95   S  SG    . CYS   A 13  ? 0.34646 0.38744 0.25531 0.13662  0.00883  0.06707  12  CYS   A SG    
96   N  N     . GLY   A 14  ? 0.15288 0.24955 0.21151 0.01139  -0.03506 0.01873  13  GLY   A N     
97   C  CA    . GLY   A 14  ? 0.16609 0.23962 0.20469 -0.01645 -0.08213 -0.00958 13  GLY   A CA    
98   C  C     . GLY   A 14  ? 0.13745 0.23453 0.22793 0.00895  -0.05583 -0.02686 13  GLY   A C     
99   O  O     . GLY   A 14  ? 0.18124 0.23245 0.27589 -0.00797 -0.09947 -0.03010 13  GLY   A O     
100  N  N     . VAL   A 15  ? 0.16937 0.19077 0.19927 0.01478  -0.06879 0.00422  14  VAL   A N     
101  C  CA    . VAL   A 15  ? 0.15998 0.18582 0.17813 0.01091  -0.04892 -0.00199 14  VAL   A CA    
102  C  C     . VAL   A 15  ? 0.14788 0.18322 0.17749 -0.01721 -0.06240 -0.01086 14  VAL   A C     
103  O  O     . VAL   A 15  ? 0.17568 0.19338 0.18421 0.00031  -0.03468 -0.02149 14  VAL   A O     
104  C  CB    . VAL   A 15  ? 0.13305 0.19327 0.15227 -0.01153 -0.06008 -0.00788 14  VAL   A CB    
105  C  CG1   . VAL   A 15  ? 0.21542 0.18597 0.15498 0.00471  -0.02648 0.02524  14  VAL   A CG1   
106  C  CG2   . VAL   A 15  ? 0.15441 0.20104 0.18012 -0.01250 -0.03804 0.01160  14  VAL   A CG2   
107  N  N     . GLY   A 16  ? 0.14980 0.20489 0.17707 -0.01530 -0.03716 -0.01710 15  GLY   A N     
108  C  CA    . GLY   A 16  ? 0.16634 0.21557 0.21281 -0.04907 -0.03881 -0.00452 15  GLY   A CA    
109  C  C     . GLY   A 16  ? 0.12687 0.17504 0.20824 0.00671  -0.05033 0.00379  15  GLY   A C     
110  O  O     . GLY   A 16  ? 0.18633 0.20348 0.20269 0.00224  -0.04952 0.00146  15  GLY   A O     
111  N  N     . LYS   A 17  ? 0.14641 0.14916 0.22113 -0.00882 -0.04575 -0.02033 16  LYS   A N     
112  C  CA    . LYS   A 17  ? 0.14058 0.16123 0.19582 -0.01293 0.00735  -0.02348 16  LYS   A CA    
113  C  C     . LYS   A 17  ? 0.13849 0.17740 0.19654 -0.00952 -0.04232 0.01075  16  LYS   A C     
114  O  O     . LYS   A 17  ? 0.14481 0.19098 0.18938 0.00937  -0.04032 0.02043  16  LYS   A O     
115  C  CB    . LYS   A 17  ? 0.14928 0.17537 0.15757 -0.00317 -0.00340 0.01977  16  LYS   A CB    
116  C  CG    . LYS   A 17  ? 0.14619 0.17380 0.17271 0.01512  -0.00574 0.01615  16  LYS   A CG    
117  C  CD    . LYS   A 17  ? 0.17662 0.17236 0.18273 -0.02654 -0.01735 0.03165  16  LYS   A CD    
118  C  CE    . LYS   A 17  ? 0.19443 0.19727 0.17488 0.01172  -0.05130 0.01302  16  LYS   A CE    
119  N  NZ    . LYS   A 17  ? 0.14460 0.20960 0.12978 -0.00598 -0.02880 0.00732  16  LYS   A NZ    
120  N  N     . SER   A 18  ? 0.13442 0.19032 0.20756 -0.00158 -0.04727 -0.00395 17  SER   A N     
121  C  CA    . SER   A 18  ? 0.16049 0.20887 0.20685 -0.00925 -0.00267 -0.00127 17  SER   A CA    
122  C  C     . SER   A 18  ? 0.16538 0.19951 0.20921 0.00843  -0.01874 -0.00709 17  SER   A C     
123  O  O     . SER   A 18  ? 0.18825 0.19262 0.21045 -0.03112 -0.00685 0.02649  17  SER   A O     
124  C  CB    . SER   A 18  ? 0.13673 0.19263 0.28690 0.02599  -0.03230 0.01544  17  SER   A CB    
125  O  OG    . SER   A 18  ? 0.16344 0.19080 0.23725 0.00616  -0.01596 0.04107  17  SER   A OG    
126  N  N     . ALA   A 19  ? 0.17161 0.21700 0.22644 -0.01594 -0.01549 -0.03315 18  ALA   A N     
127  C  CA    . ALA   A 19  ? 0.19037 0.22225 0.24301 -0.01852 -0.02065 -0.01321 18  ALA   A CA    
128  C  C     . ALA   A 19  ? 0.19486 0.20420 0.21768 -0.03198 -0.01317 0.00013  18  ALA   A C     
129  O  O     . ALA   A 19  ? 0.18361 0.20827 0.20583 -0.04982 0.00234  -0.00334 18  ALA   A O     
130  C  CB    . ALA   A 19  ? 0.18078 0.24603 0.25464 -0.03940 -0.01384 -0.02177 18  ALA   A CB    
131  N  N     . LEU   A 20  ? 0.13732 0.22264 0.22963 -0.03496 -0.00653 0.01326  19  LEU   A N     
132  C  CA    . LEU   A 20  ? 0.17357 0.21594 0.20389 -0.02935 -0.02663 0.02469  19  LEU   A CA    
133  C  C     . LEU   A 20  ? 0.19324 0.21713 0.18434 -0.04823 0.00170  0.00951  19  LEU   A C     
134  O  O     . LEU   A 20  ? 0.24032 0.24154 0.20104 -0.06411 -0.00407 0.02968  19  LEU   A O     
135  C  CB    . LEU   A 20  ? 0.20677 0.21740 0.18171 -0.02614 -0.01592 0.01597  19  LEU   A CB    
136  C  CG    . LEU   A 20  ? 0.22978 0.19510 0.18055 -0.03814 -0.03362 0.00777  19  LEU   A CG    
137  C  CD1   . LEU   A 20  ? 0.21693 0.21394 0.20982 -0.00404 0.03662  -0.00705 19  LEU   A CD1   
138  C  CD2   . LEU   A 20  ? 0.31658 0.17799 0.21280 -0.00564 -0.02654 0.00347  19  LEU   A CD2   
139  N  N     . THR   A 21  ? 0.20586 0.22757 0.19523 -0.01895 0.01143  0.01038  20  THR   A N     
140  C  CA    . THR   A 21  ? 0.17206 0.23302 0.19021 -0.03035 0.00304  -0.01344 20  THR   A CA    
141  C  C     . THR   A 21  ? 0.20688 0.24880 0.20321 -0.05839 0.02865  -0.01794 20  THR   A C     
142  O  O     . THR   A 21  ? 0.28438 0.25741 0.20033 -0.09003 0.02153  -0.00148 20  THR   A O     
143  C  CB    . THR   A 21  ? 0.18649 0.25118 0.19504 -0.06292 -0.00424 0.01725  20  THR   A CB    
144  O  OG1   . THR   A 21  ? 0.18865 0.24990 0.19146 -0.05417 -0.01770 0.00734  20  THR   A OG1   
145  C  CG2   . THR   A 21  ? 0.26008 0.27306 0.17813 -0.09290 -0.00445 -0.01928 20  THR   A CG2   
146  N  N     . ILE   A 22  ? 0.22011 0.24163 0.24832 -0.05495 0.03741  0.00855  21  ILE   A N     
147  C  CA    A ILE   A 22  ? 0.21227 0.26718 0.27429 -0.04672 0.05734  0.01276  21  ILE   A CA    
148  C  CA    B ILE   A 22  ? 0.23431 0.26948 0.27455 -0.05208 0.05034  0.00752  21  ILE   A CA    
149  C  C     . ILE   A 22  ? 0.21543 0.28178 0.24232 -0.06324 0.04434  0.01410  21  ILE   A C     
150  O  O     . ILE   A 22  ? 0.32370 0.29979 0.27147 -0.06571 0.07271  0.02984  21  ILE   A O     
151  C  CB    A ILE   A 22  ? 0.18745 0.25157 0.30039 -0.05249 0.03704  0.00878  21  ILE   A CB    
152  C  CB    B ILE   A 22  ? 0.24563 0.25986 0.30580 -0.06371 0.01874  -0.00753 21  ILE   A CB    
153  C  CG1   A ILE   A 22  ? 0.19396 0.25022 0.34249 -0.05355 0.03022  0.00210  21  ILE   A CG1   
154  C  CG1   B ILE   A 22  ? 0.28089 0.26575 0.34665 -0.07344 -0.00043 -0.02292 21  ILE   A CG1   
155  C  CG2   A ILE   A 22  ? 0.18339 0.27614 0.33234 -0.05329 0.04901  0.03069  21  ILE   A CG2   
156  C  CG2   B ILE   A 22  ? 0.23607 0.27794 0.34797 -0.04933 0.01720  0.01718  21  ILE   A CG2   
157  C  CD1   A ILE   A 22  ? 0.17365 0.27122 0.34936 -0.02192 0.00853  0.04157  21  ILE   A CD1   
158  C  CD1   B ILE   A 22  ? 0.25779 0.28281 0.36950 -0.06805 -0.05108 -0.00326 21  ILE   A CD1   
159  N  N     . GLN   A 23  ? 0.23266 0.26397 0.21908 -0.02978 0.00624  0.03180  22  GLN   A N     
160  C  CA    . GLN   A 23  ? 0.27528 0.26858 0.22456 -0.04970 0.01953  0.01473  22  GLN   A CA    
161  C  C     . GLN   A 23  ? 0.29531 0.29279 0.22398 -0.08409 0.01624  0.04508  22  GLN   A C     
162  O  O     . GLN   A 23  ? 0.32904 0.30006 0.23793 -0.10078 -0.04445 0.05270  22  GLN   A O     
163  C  CB    . GLN   A 23  ? 0.34383 0.27816 0.24296 -0.06251 -0.01192 0.00465  22  GLN   A CB    
164  C  CG    . GLN   A 23  ? 0.40405 0.28689 0.27610 -0.06805 -0.02517 0.02838  22  GLN   A CG    
165  C  CD    . GLN   A 23  ? 0.40169 0.27620 0.24067 -0.04105 0.03812  0.05317  22  GLN   A CD    
166  O  OE1   . GLN   A 23  ? 0.34293 0.30489 0.30665 -0.09113 -0.01762 0.02257  22  GLN   A OE1   
167  N  NE2   . GLN   A 23  ? 0.41933 0.27699 0.27352 -0.04453 -0.01709 0.05047  22  GLN   A NE2   
168  N  N     . LEU   A 24  ? 0.24808 0.28710 0.22738 -0.07896 -0.01121 0.07339  23  LEU   A N     
169  C  CA    . LEU   A 24  ? 0.26283 0.32957 0.24816 -0.09667 -0.05884 0.09643  23  LEU   A CA    
170  C  C     . LEU   A 24  ? 0.38460 0.36232 0.23565 -0.13561 -0.03402 0.12614  23  LEU   A C     
171  O  O     . LEU   A 24  ? 0.44879 0.39181 0.28609 -0.14142 -0.01918 0.11474  23  LEU   A O     
172  C  CB    . LEU   A 24  ? 0.26235 0.35444 0.24536 -0.07382 -0.05789 0.08966  23  LEU   A CB    
173  C  CG    . LEU   A 24  ? 0.32236 0.38688 0.29305 -0.08237 -0.05604 0.06236  23  LEU   A CG    
174  C  CD1   . LEU   A 24  ? 0.37010 0.40392 0.31451 -0.03299 -0.06330 0.07887  23  LEU   A CD1   
175  C  CD2   . LEU   A 24  ? 0.32175 0.41340 0.26242 -0.05796 -0.06334 0.03693  23  LEU   A CD2   
176  N  N     . ILE   A 25  ? 0.41222 0.42370 0.21346 -0.14549 0.01056  0.07572  24  ILE   A N     
177  C  CA    . ILE   A 25  ? 0.50346 0.46540 0.21651 -0.17865 0.07525  0.03874  24  ILE   A CA    
178  C  C     . ILE   A 25  ? 0.48740 0.50988 0.25345 -0.18862 0.11232  0.02589  24  ILE   A C     
179  O  O     . ILE   A 25  ? 0.51205 0.52658 0.32951 -0.21210 0.10782  0.04980  24  ILE   A O     
180  C  CB    . ILE   A 25  ? 0.52343 0.44017 0.21119 -0.17740 0.09766  0.00384  24  ILE   A CB    
181  C  CG1   . ILE   A 25  ? 0.54766 0.43863 0.23210 -0.21962 -0.00587 0.01017  24  ILE   A CG1   
182  C  CG2   . ILE   A 25  ? 0.58229 0.44889 0.23968 -0.14164 0.11145  -0.03570 24  ILE   A CG2   
183  C  CD1   . ILE   A 25  ? 0.51734 0.44590 0.24924 -0.19291 -0.07448 0.04375  24  ILE   A CD1   
184  N  N     . GLN   A 26  ? 0.46687 0.53332 0.35201 -0.21713 0.09066  0.02061  25  GLN   A N     
185  C  CA    . GLN   A 26  ? 0.46690 0.55683 0.37478 -0.17724 0.13565  0.02432  25  GLN   A CA    
186  C  C     . GLN   A 26  ? 0.42710 0.52408 0.36969 -0.18950 0.08979  0.07771  25  GLN   A C     
187  O  O     . GLN   A 26  ? 0.43523 0.53048 0.38660 -0.18078 0.09861  0.05690  25  GLN   A O     
188  C  CB    . GLN   A 26  ? 0.51919 0.59293 0.41588 -0.15514 0.18223  0.00494  25  GLN   A CB    
189  C  CG    . GLN   A 26  ? 0.54227 0.63592 0.49169 -0.13396 0.20370  -0.01519 25  GLN   A CG    
190  C  CD    . GLN   A 26  ? 0.60436 0.66400 0.54023 -0.11675 0.20786  -0.05486 25  GLN   A CD    
191  O  OE1   . GLN   A 26  ? 0.66074 0.67835 0.57254 -0.09534 0.20877  -0.06819 25  GLN   A OE1   
192  N  NE2   . GLN   A 26  ? 0.60982 0.67802 0.55812 -0.11444 0.22087  -0.06497 25  GLN   A NE2   
193  N  N     . ASN   A 27  ? 0.46161 0.50753 0.35806 -0.16388 0.09111  0.12913  26  ASN   A N     
194  C  CA    . ASN   A 27  ? 0.53320 0.50240 0.37388 -0.09115 0.10845  0.19481  26  ASN   A CA    
195  C  C     . ASN   A 27  ? 0.46552 0.48491 0.41897 -0.12249 0.10224  0.16240  26  ASN   A C     
196  O  O     . ASN   A 27  ? 0.43942 0.48004 0.46915 -0.14958 0.09444  0.17725  26  ASN   A O     
197  C  CB    . ASN   A 27  ? 0.70660 0.52922 0.37613 0.02041  0.08235  0.23001  26  ASN   A CB    
198  C  CG    . ASN   A 27  ? 0.88071 0.55545 0.43081 0.08394  0.11333  0.21366  26  ASN   A CG    
199  O  OD1   . ASN   A 27  ? 0.97038 0.57587 0.45750 0.12249  0.10320  0.20749  26  ASN   A OD1   
200  N  ND2   . ASN   A 27  ? 0.93729 0.55433 0.46369 0.10127  0.12588  0.21131  26  ASN   A ND2   
201  N  N     . HIS   A 28  ? 0.43637 0.48689 0.40627 -0.10332 0.12309  0.10025  27  HIS   A N     
202  C  CA    . HIS   A 28  ? 0.36732 0.48034 0.42114 -0.04089 0.11782  0.08320  27  HIS   A CA    
203  C  C     . HIS   A 28  ? 0.24154 0.42318 0.41623 -0.06171 0.07619  0.10303  27  HIS   A C     
204  O  O     . HIS   A 28  ? 0.29329 0.39702 0.39410 -0.08325 0.07582  0.12372  27  HIS   A O     
205  C  CB    . HIS   A 28  ? 0.46701 0.52411 0.46653 -0.00877 0.13498  0.04934  27  HIS   A CB    
206  C  CG    . HIS   A 28  ? 0.56154 0.56528 0.54028 0.02479  0.11081  0.02067  27  HIS   A CG    
207  N  ND1   . HIS   A 28  ? 0.58773 0.58982 0.57624 0.04215  0.09259  -0.00855 27  HIS   A ND1   
208  C  CD2   . HIS   A 28  ? 0.61180 0.58026 0.59412 0.04023  0.08121  0.01212  27  HIS   A CD2   
209  C  CE1   . HIS   A 28  ? 0.56831 0.59602 0.58234 0.06262  0.09696  -0.02124 27  HIS   A CE1   
210  N  NE2   . HIS   A 28  ? 0.60957 0.59407 0.60988 0.06940  0.09260  -0.00275 27  HIS   A NE2   
211  N  N     . PHE   A 29  ? 0.24703 0.39769 0.41229 -0.03085 0.04579  0.09603  28  PHE   A N     
212  C  CA    . PHE   A 29  ? 0.23843 0.37526 0.39202 -0.05966 0.03566  0.07522  28  PHE   A CA    
213  C  C     . PHE   A 29  ? 0.42611 0.40460 0.41330 0.01413  0.04935  0.05488  28  PHE   A C     
214  O  O     . PHE   A 29  ? 0.42762 0.43451 0.44537 0.04937  0.03234  0.04045  28  PHE   A O     
215  C  CB    . PHE   A 29  ? 0.27035 0.34184 0.35851 -0.04298 0.03713  0.05585  28  PHE   A CB    
216  C  CG    . PHE   A 29  ? 0.26670 0.29242 0.36557 -0.07308 0.00882  0.04418  28  PHE   A CG    
217  C  CD1   . PHE   A 29  ? 0.26700 0.27605 0.38382 -0.08339 0.02362  0.02192  28  PHE   A CD1   
218  C  CD2   . PHE   A 29  ? 0.25809 0.28781 0.38868 -0.08092 0.01271  0.03735  28  PHE   A CD2   
219  C  CE1   . PHE   A 29  ? 0.25792 0.27157 0.36710 -0.09781 0.01715  0.00572  28  PHE   A CE1   
220  C  CE2   . PHE   A 29  ? 0.22140 0.28018 0.35209 -0.05376 -0.00595 0.03954  28  PHE   A CE2   
221  C  CZ    . PHE   A 29  ? 0.25836 0.26682 0.38798 -0.06590 0.00278  0.00038  28  PHE   A CZ    
222  N  N     . VAL   A 30  ? 0.55698 0.41382 0.44733 0.06206  0.05207  0.02086  29  VAL   A N     
223  C  CA    . VAL   A 30  ? 0.61221 0.42004 0.45776 0.09400  0.03014  0.00139  29  VAL   A CA    
224  C  C     . VAL   A 30  ? 0.56769 0.39008 0.45876 0.06860  -0.00120 0.00311  29  VAL   A C     
225  O  O     . VAL   A 30  ? 0.61722 0.39037 0.49894 0.10333  0.01681  -0.00488 29  VAL   A O     
226  C  CB    . VAL   A 30  ? 0.69835 0.44003 0.45489 0.14825  0.04083  0.00264  29  VAL   A CB    
227  C  CG1   . VAL   A 30  ? 0.71412 0.44839 0.45692 0.15482  0.03888  0.00283  29  VAL   A CG1   
228  C  CG2   . VAL   A 30  ? 0.71333 0.45449 0.47776 0.13921  0.06263  0.01706  29  VAL   A CG2   
229  N  N     . ASP   A 31  ? 0.50074 0.37685 0.44008 0.00276  -0.01064 -0.01488 30  ASP   A N     
230  C  CA    A ASP   A 31  ? 0.46997 0.36938 0.48711 -0.01973 -0.07072 -0.03243 30  ASP   A CA    
231  C  CA    B ASP   A 31  ? 0.45451 0.37096 0.45314 -0.06339 -0.05317 -0.02706 30  ASP   A CA    
232  C  C     . ASP   A 31  ? 0.36288 0.35843 0.47109 -0.04809 -0.03629 -0.02610 30  ASP   A C     
233  O  O     . ASP   A 31  ? 0.24669 0.36484 0.48864 -0.05616 -0.09377 -0.03577 30  ASP   A O     
234  C  CB    A ASP   A 31  ? 0.56775 0.36699 0.53950 0.00353  -0.10995 -0.06421 30  ASP   A CB    
235  C  CB    B ASP   A 31  ? 0.52210 0.37443 0.44334 -0.12642 -0.05345 -0.04587 30  ASP   A CB    
236  C  CG    A ASP   A 31  ? 0.59543 0.36047 0.57095 0.01576  -0.16742 -0.07454 30  ASP   A CG    
237  C  CG    B ASP   A 31  ? 0.58610 0.38548 0.43142 -0.16674 -0.07147 -0.04268 30  ASP   A CG    
238  O  OD1   A ASP   A 31  ? 0.52497 0.33048 0.56320 -0.00953 -0.25117 -0.08833 30  ASP   A OD1   
239  O  OD1   B ASP   A 31  ? 0.62069 0.38771 0.41343 -0.19192 -0.10021 -0.05058 30  ASP   A OD1   
240  O  OD2   A ASP   A 31  ? 0.64231 0.38659 0.59658 0.00963  -0.15917 -0.06292 30  ASP   A OD2   
241  O  OD2   B ASP   A 31  ? 0.63024 0.39570 0.44212 -0.16317 -0.02894 -0.01444 30  ASP   A OD2   
242  N  N     . GLU   A 32  ? 0.37796 0.34461 0.47047 -0.07500 0.02791  0.02236  31  GLU   A N     
243  C  CA    . GLU   A 32  ? 0.28356 0.32971 0.42350 -0.07523 0.05868  0.07302  31  GLU   A CA    
244  C  C     . GLU   A 32  ? 0.28053 0.30684 0.35653 -0.04151 -0.01366 0.05866  31  GLU   A C     
245  O  O     . GLU   A 32  ? 0.36098 0.34339 0.35649 -0.05468 -0.05104 0.10230  31  GLU   A O     
246  C  CB    . GLU   A 32  ? 0.32768 0.36496 0.47213 -0.03623 0.10585  0.09141  31  GLU   A CB    
247  C  CG    . GLU   A 32  ? 0.40948 0.40458 0.53150 -0.00897 0.09557  0.11914  31  GLU   A CG    
248  C  CD    . GLU   A 32  ? 0.46461 0.43284 0.59288 -0.01015 0.08194  0.14530  31  GLU   A CD    
249  O  OE1   . GLU   A 32  ? 0.51104 0.44223 0.59706 -0.01642 0.09109  0.18620  31  GLU   A OE1   
250  O  OE2   . GLU   A 32  ? 0.46303 0.43097 0.61084 -0.03099 0.11917  0.14937  31  GLU   A OE2   
251  N  N     . TYR   A 33  ? 0.17708 0.26353 0.32109 -0.03079 -0.01985 0.01085  32  TYR   A N     
252  C  CA    . TYR   A 33  ? 0.19189 0.23404 0.24832 -0.01426 -0.05922 0.04322  32  TYR   A CA    
253  C  C     . TYR   A 33  ? 0.21715 0.21655 0.24892 0.01586  -0.04647 0.01078  32  TYR   A C     
254  O  O     . TYR   A 33  ? 0.18053 0.23949 0.30791 0.03689  -0.03868 -0.00952 32  TYR   A O     
255  C  CB    . TYR   A 33  ? 0.17543 0.25892 0.23766 0.00949  -0.04221 0.04301  32  TYR   A CB    
256  C  CG    . TYR   A 33  ? 0.15262 0.25678 0.26473 -0.01003 -0.02474 0.01438  32  TYR   A CG    
257  C  CD1   . TYR   A 33  ? 0.15663 0.27013 0.29218 0.00976  -0.03705 -0.02686 32  TYR   A CD1   
258  C  CD2   . TYR   A 33  ? 0.26705 0.26928 0.26046 -0.07079 -0.08054 0.03750  32  TYR   A CD2   
259  C  CE1   . TYR   A 33  ? 0.15895 0.25496 0.27635 0.02313  -0.07096 0.00462  32  TYR   A CE1   
260  C  CE2   . TYR   A 33  ? 0.30649 0.27351 0.31325 -0.08363 -0.09510 0.04747  32  TYR   A CE2   
261  C  CZ    . TYR   A 33  ? 0.20643 0.26380 0.28749 -0.02800 -0.09656 0.04019  32  TYR   A CZ    
262  O  OH    . TYR   A 33  ? 0.21799 0.28264 0.24885 -0.02765 -0.05050 0.04982  32  TYR   A OH    
263  N  N     . ASP   A 34  ? 0.15342 0.17565 0.22647 -0.01936 -0.00885 0.01091  33  ASP   A N     
264  C  CA    . ASP   A 34  ? 0.14589 0.22030 0.23592 -0.00221 0.00540  0.03007  33  ASP   A CA    
265  C  C     . ASP   A 34  ? 0.14483 0.22785 0.20683 0.02001  -0.02336 0.02421  33  ASP   A C     
266  O  O     . ASP   A 34  ? 0.17295 0.22317 0.20086 0.04145  -0.01570 0.03128  33  ASP   A O     
267  C  CB    . ASP   A 34  ? 0.18889 0.24831 0.26476 0.03115  0.04927  0.02866  33  ASP   A CB    
268  C  CG    . ASP   A 34  ? 0.24734 0.29356 0.27229 0.00118  0.05876  0.03180  33  ASP   A CG    
269  O  OD1   . ASP   A 34  ? 0.20493 0.29801 0.31542 0.02311  0.00168  -0.00387 33  ASP   A OD1   
270  O  OD2   . ASP   A 34  ? 0.33656 0.33607 0.28342 0.04275  0.05039  0.01118  33  ASP   A OD2   
271  N  N     . PRO   A 35  ? 0.14929 0.21713 0.22663 -0.01145 -0.06777 0.04826  34  PRO   A N     
272  C  CA    . PRO   A 35  ? 0.18767 0.20883 0.25699 -0.04401 -0.04066 0.05428  34  PRO   A CA    
273  C  C     . PRO   A 35  ? 0.13839 0.24164 0.22884 -0.01268 0.00028  0.02211  34  PRO   A C     
274  O  O     . PRO   A 35  ? 0.14860 0.26674 0.26563 0.02580  -0.02251 -0.02609 34  PRO   A O     
275  C  CB    . PRO   A 35  ? 0.18855 0.22740 0.26321 -0.03760 -0.09246 0.07651  34  PRO   A CB    
276  C  CG    . PRO   A 35  ? 0.22980 0.26017 0.24953 -0.03981 -0.08519 0.06371  34  PRO   A CG    
277  C  CD    . PRO   A 35  ? 0.24252 0.23641 0.25309 -0.00178 -0.10680 0.06517  34  PRO   A CD    
278  N  N     . THR   A 36  ? 0.14789 0.22661 0.20482 -0.02336 -0.03159 0.04534  35  THR   A N     
279  C  CA    . THR   A 36  ? 0.12374 0.19387 0.22277 0.00598  -0.02820 0.01966  35  THR   A CA    
280  C  C     . THR   A 36  ? 0.13993 0.18409 0.19029 0.00621  -0.02318 0.00136  35  THR   A C     
281  O  O     . THR   A 36  ? 0.17271 0.21165 0.19657 0.00275  -0.01211 0.02727  35  THR   A O     
282  C  CB    . THR   A 36  ? 0.16334 0.18188 0.22049 0.00600  -0.04803 -0.00182 35  THR   A CB    
283  O  OG1   . THR   A 36  ? 0.17955 0.19885 0.17459 0.01044  -0.00705 0.01681  35  THR   A OG1   
284  C  CG2   . THR   A 36  ? 0.17852 0.20689 0.19807 0.00688  -0.01580 0.01736  35  THR   A CG2   
285  N  N     . ILE   A 37  ? 0.14974 0.18526 0.18139 0.02637  -0.04390 -0.00847 36  ILE   A N     
286  C  CA    . ILE   A 37  ? 0.14236 0.20896 0.18363 0.03243  -0.01593 -0.00342 36  ILE   A CA    
287  C  C     . ILE   A 37  ? 0.14910 0.21317 0.18256 0.00113  0.00092  0.02844  36  ILE   A C     
288  O  O     . ILE   A 37  ? 0.13143 0.21992 0.19230 0.01156  -0.00665 0.03622  36  ILE   A O     
289  C  CB    . ILE   A 37  ? 0.12098 0.20142 0.22315 0.03170  0.00078  0.01248  36  ILE   A CB    
290  C  CG1   . ILE   A 37  ? 0.14442 0.25614 0.24990 0.05719  -0.02688 0.03065  36  ILE   A CG1   
291  C  CG2   . ILE   A 37  ? 0.18654 0.17022 0.27779 -0.00130 0.01092  -0.01579 36  ILE   A CG2   
292  C  CD1   . ILE   A 37  ? 0.20831 0.29903 0.25642 0.05643  0.01402  0.04698  36  ILE   A CD1   
293  N  N     . GLU   A 38  ? 0.12600 0.21072 0.15618 0.01577  -0.00257 0.02300  37  GLU   A N     
294  C  CA    . GLU   A 38  ? 0.15048 0.18571 0.17540 0.00112  -0.00873 0.01230  37  GLU   A CA    
295  C  C     . GLU   A 38  ? 0.15379 0.19738 0.18338 0.02214  -0.00995 0.01708  37  GLU   A C     
296  O  O     . GLU   A 38  ? 0.14477 0.21491 0.20951 0.03538  0.00492  0.01416  37  GLU   A O     
297  C  CB    . GLU   A 38  ? 0.12683 0.19245 0.16784 0.01121  -0.00735 0.00656  37  GLU   A CB    
298  C  CG    . GLU   A 38  ? 0.14648 0.22846 0.17120 0.01670  -0.00191 -0.00925 37  GLU   A CG    
299  C  CD    . GLU   A 38  ? 0.19766 0.23900 0.16733 0.00785  -0.03477 0.00413  37  GLU   A CD    
300  O  OE1   . GLU   A 38  ? 0.15683 0.26822 0.23158 -0.01127 -0.00095 -0.01816 37  GLU   A OE1   
301  O  OE2   . GLU   A 38  ? 0.26463 0.28990 0.19152 -0.03906 -0.03359 -0.01431 37  GLU   A OE2   
302  N  N     . ASP   A 39  ? 0.15217 0.20893 0.16660 0.00556  -0.00690 0.03081  38  ASP   A N     
303  C  CA    . ASP   A 39  ? 0.15381 0.22842 0.17195 0.02393  0.00609  0.02565  38  ASP   A CA    
304  C  C     . ASP   A 39  ? 0.18038 0.21714 0.18830 0.03801  -0.00383 0.05504  38  ASP   A C     
305  O  O     . ASP   A 39  ? 0.16369 0.21893 0.20754 0.03362  0.00365  0.00659  38  ASP   A O     
306  C  CB    . ASP   A 39  ? 0.14127 0.25202 0.26718 0.01356  -0.01695 0.05442  38  ASP   A CB    
307  C  CG    . ASP   A 39  ? 0.14982 0.30124 0.27199 0.03869  0.05394  0.07780  38  ASP   A CG    
308  O  OD1   . ASP   A 39  ? 0.17295 0.32788 0.33690 0.06264  0.03029  0.09220  38  ASP   A OD1   
309  O  OD2   . ASP   A 39  ? 0.24291 0.32286 0.29668 -0.00753 -0.04842 0.09342  38  ASP   A OD2   
310  N  N     . SER   A 40  ? 0.19735 0.23806 0.16171 0.05535  0.01911  0.05747  39  SER   A N     
311  C  CA    . SER   A 40  ? 0.18657 0.24961 0.15557 0.05295  0.01259  0.02116  39  SER   A CA    
312  C  C     . SER   A 40  ? 0.18163 0.27272 0.17039 0.04158  0.02566  0.05506  39  SER   A C     
313  O  O     . SER   A 40  ? 0.23442 0.31758 0.21862 0.08022  0.07059  0.06630  39  SER   A O     
314  C  CB    . SER   A 40  ? 0.28027 0.27592 0.22608 -0.00155 -0.05412 0.01444  39  SER   A CB    
315  O  OG    . SER   A 40  ? 0.35464 0.31225 0.30869 -0.03641 -0.08355 0.01823  39  SER   A OG    
316  N  N     . TYR   A 41  ? 0.23934 0.25239 0.17090 0.06313  -0.02525 0.06536  40  TYR   A N     
317  C  CA    . TYR   A 41  ? 0.21109 0.27941 0.16580 0.04782  -0.02274 0.07875  40  TYR   A CA    
318  C  C     . TYR   A 41  ? 0.21329 0.27970 0.15470 0.09010  0.02205  0.04504  40  TYR   A C     
319  O  O     . TYR   A 41  ? 0.22063 0.28318 0.17025 0.06707  0.03305  0.02896  40  TYR   A O     
320  C  CB    . TYR   A 41  ? 0.16393 0.28832 0.23736 0.00892  -0.02374 0.06500  40  TYR   A CB    
321  C  CG    . TYR   A 41  ? 0.17608 0.31910 0.21181 0.01092  -0.01441 0.02336  40  TYR   A CG    
322  C  CD1   . TYR   A 41  ? 0.24108 0.36143 0.28097 -0.01800 -0.01749 0.08283  40  TYR   A CD1   
323  C  CD2   . TYR   A 41  ? 0.19210 0.28916 0.18369 0.00314  -0.01879 0.01277  40  TYR   A CD2   
324  C  CE1   . TYR   A 41  ? 0.26147 0.37939 0.29182 -0.01988 -0.06659 0.09396  40  TYR   A CE1   
325  C  CE2   . TYR   A 41  ? 0.17177 0.29712 0.21934 0.01366  -0.02192 0.03084  40  TYR   A CE2   
326  C  CZ    . TYR   A 41  ? 0.18172 0.35751 0.25437 0.01590  -0.06954 0.11099  40  TYR   A CZ    
327  O  OH    . TYR   A 41  ? 0.22346 0.39984 0.27149 0.01474  0.00277  0.09768  40  TYR   A OH    
328  N  N     . ARG   A 42  ? 0.23804 0.31260 0.18135 0.08624  0.03861  0.07728  41  ARG   A N     
329  C  CA    . ARG   A 42  ? 0.23559 0.32087 0.17632 0.09100  0.03102  0.09255  41  ARG   A CA    
330  C  C     . ARG   A 42  ? 0.18431 0.33083 0.19528 0.08062  -0.01008 0.07143  41  ARG   A C     
331  O  O     . ARG   A 42  ? 0.18446 0.35495 0.23323 0.08035  0.04316  0.09121  41  ARG   A O     
332  C  CB    . ARG   A 42  ? 0.21639 0.33343 0.18816 0.04802  0.06847  0.06527  41  ARG   A CB    
333  C  CG    . ARG   A 42  ? 0.29118 0.34570 0.20484 0.04391  0.07855  0.06602  41  ARG   A CG    
334  C  CD    . ARG   A 42  ? 0.35376 0.35382 0.22493 0.03904  0.05994  0.03561  41  ARG   A CD    
335  N  NE    . ARG   A 42  ? 0.34084 0.34764 0.26167 -0.03643 -0.00046 0.02101  41  ARG   A NE    
336  C  CZ    . ARG   A 42  ? 0.27704 0.35897 0.26026 -0.05812 0.04710  0.04349  41  ARG   A CZ    
337  N  NH1   . ARG   A 42  ? 0.31708 0.40715 0.30566 -0.06308 0.06920  0.02195  41  ARG   A NH1   
338  N  NH2   . ARG   A 42  ? 0.31947 0.34364 0.21577 -0.06421 0.02101  0.03334  41  ARG   A NH2   
339  N  N     . LYS   A 43  ? 0.19048 0.29302 0.17042 0.02675  0.00460  0.05704  42  LYS   A N     
340  C  CA    . LYS   A 43  ? 0.15991 0.29514 0.24369 -0.00826 -0.05304 0.04866  42  LYS   A CA    
341  C  C     . LYS   A 43  ? 0.16024 0.24991 0.23199 0.01191  -0.01191 0.03208  42  LYS   A C     
342  O  O     . LYS   A 43  ? 0.16795 0.22813 0.22568 -0.00207 -0.02215 0.02088  42  LYS   A O     
343  C  CB    . LYS   A 43  ? 0.20630 0.34777 0.31870 -0.01539 -0.09535 0.05678  42  LYS   A CB    
344  C  CG    . LYS   A 43  ? 0.37591 0.37883 0.36450 -0.04252 -0.16699 0.05938  42  LYS   A CG    
345  C  CD    . LYS   A 43  ? 0.44657 0.39643 0.37694 -0.07316 -0.19944 0.09865  42  LYS   A CD    
346  C  CE    . LYS   A 43  ? 0.56816 0.41724 0.42361 -0.08577 -0.13670 0.10856  42  LYS   A CE    
347  N  NZ    . LYS   A 43  ? 0.60558 0.43875 0.40144 -0.09088 -0.13705 0.11589  42  LYS   A NZ    
348  N  N     . GLN   A 44  ? 0.20970 0.24042 0.20526 0.02055  -0.01900 0.04243  43  GLN   A N     
349  C  CA    . GLN   A 44  ? 0.17949 0.24087 0.21452 0.01939  0.00060  0.02590  43  GLN   A CA    
350  C  C     . GLN   A 44  ? 0.17778 0.22531 0.26320 -0.00914 -0.00753 0.00959  43  GLN   A C     
351  O  O     . GLN   A 44  ? 0.19805 0.25693 0.27512 0.00010  -0.01218 0.00221  43  GLN   A O     
352  C  CB    . GLN   A 44  ? 0.27590 0.28091 0.17213 0.02351  -0.01817 0.01942  43  GLN   A CB    
353  C  CG    . GLN   A 44  ? 0.41390 0.30641 0.20014 0.07462  0.01678  0.00189  43  GLN   A CG    
354  C  CD    . GLN   A 44  ? 0.50753 0.33359 0.24199 0.06134  0.03782  0.00862  43  GLN   A CD    
355  O  OE1   . GLN   A 44  ? 0.52384 0.34224 0.23372 0.02760  0.04874  0.02155  43  GLN   A OE1   
356  N  NE2   . GLN   A 44  ? 0.56327 0.36394 0.25645 0.04199  0.05006  0.01936  43  GLN   A NE2   
357  N  N     . VAL   A 45  ? 0.22503 0.17773 0.28328 0.00540  -0.01085 0.01001  44  VAL   A N     
358  C  CA    . VAL   A 45  ? 0.20857 0.20486 0.22907 0.00950  -0.00729 -0.00401 44  VAL   A CA    
359  C  C     . VAL   A 45  ? 0.25054 0.18287 0.22853 -0.02409 0.01070  -0.01168 44  VAL   A C     
360  O  O     . VAL   A 45  ? 0.21994 0.20024 0.34259 -0.00885 -0.10108 -0.03410 44  VAL   A O     
361  C  CB    . VAL   A 45  ? 0.23636 0.22047 0.20464 -0.00893 -0.03799 -0.01872 44  VAL   A CB    
362  C  CG1   . VAL   A 45  ? 0.32137 0.26154 0.24223 0.01027  -0.06208 -0.05216 44  VAL   A CG1   
363  C  CG2   . VAL   A 45  ? 0.32556 0.25712 0.22231 -0.00359 -0.01325 0.02649  44  VAL   A CG2   
364  N  N     . VAL   A 46  ? 0.32651 0.19572 0.23601 -0.01253 -0.00432 -0.00851 45  VAL   A N     
365  C  CA    . VAL   A 46  ? 0.27359 0.21316 0.22672 0.03839  -0.03468 0.00986  45  VAL   A CA    
366  C  C     . VAL   A 46  ? 0.26246 0.22107 0.24443 0.00831  -0.06866 0.00225  45  VAL   A C     
367  O  O     . VAL   A 46  ? 0.27341 0.23610 0.28203 0.00128  -0.06650 -0.01527 45  VAL   A O     
368  C  CB    . VAL   A 46  ? 0.32640 0.23583 0.27085 0.03083  -0.02677 0.04177  45  VAL   A CB    
369  C  CG1   . VAL   A 46  ? 0.36819 0.23089 0.29998 0.03196  -0.03515 0.04111  45  VAL   A CG1   
370  C  CG2   . VAL   A 46  ? 0.42097 0.26043 0.27353 0.01965  0.00348  0.05249  45  VAL   A CG2   
371  N  N     . ILE   A 47  ? 0.25914 0.18467 0.27648 0.01538  -0.07339 -0.01232 46  ILE   A N     
372  C  CA    . ILE   A 47  ? 0.26563 0.18409 0.28657 0.04551  -0.04103 0.00764  46  ILE   A CA    
373  C  C     . ILE   A 47  ? 0.26359 0.19720 0.31886 0.04082  -0.05597 -0.00503 46  ILE   A C     
374  O  O     . ILE   A 47  ? 0.28168 0.18468 0.34347 0.04220  -0.09033 -0.00247 46  ILE   A O     
375  C  CB    . ILE   A 47  ? 0.25846 0.18759 0.24883 0.04685  -0.04646 0.00724  46  ILE   A CB    
376  C  CG1   . ILE   A 47  ? 0.23696 0.20487 0.22764 0.03560  -0.04111 0.00672  46  ILE   A CG1   
377  C  CG2   . ILE   A 47  ? 0.27869 0.21947 0.25364 0.04837  0.03094  -0.00388 46  ILE   A CG2   
378  C  CD1   . ILE   A 47  ? 0.27749 0.20066 0.19885 0.05179  -0.05680 0.04247  46  ILE   A CD1   
379  N  N     . ASP   A 48  ? 0.30324 0.21006 0.30739 0.06561  -0.04392 0.01861  47  ASP   A N     
380  C  CA    . ASP   A 48  ? 0.32472 0.25493 0.33586 0.07759  -0.04111 0.01555  47  ASP   A CA    
381  C  C     . ASP   A 48  ? 0.37354 0.24953 0.34983 0.08388  -0.06506 0.02585  47  ASP   A C     
382  O  O     . ASP   A 48  ? 0.36510 0.28323 0.38209 0.07844  -0.11733 0.03890  47  ASP   A O     
383  C  CB    . ASP   A 48  ? 0.28058 0.29465 0.40873 0.09781  -0.00958 0.05090  47  ASP   A CB    
384  C  CG    . ASP   A 48  ? 0.40272 0.30210 0.46221 0.10286  0.05364  0.08188  47  ASP   A CG    
385  O  OD1   . ASP   A 48  ? 0.41451 0.32459 0.46183 0.13343  0.00595  0.10777  47  ASP   A OD1   
386  O  OD2   . ASP   A 48  ? 0.48759 0.29732 0.51332 0.08633  0.07783  0.06342  47  ASP   A OD2   
387  N  N     . GLY   A 49  ? 0.40635 0.22374 0.34378 0.04720  -0.07520 0.03997  48  GLY   A N     
388  C  CA    . GLY   A 49  ? 0.39446 0.21900 0.33339 0.00841  -0.08716 0.02909  48  GLY   A CA    
389  C  C     . GLY   A 49  ? 0.49443 0.21334 0.34554 0.01819  -0.10837 0.06610  48  GLY   A C     
390  O  O     . GLY   A 49  ? 0.58466 0.23510 0.36428 0.00487  -0.12476 0.07205  48  GLY   A O     
391  N  N     . GLU   A 50  ? 0.39358 0.21849 0.36191 0.04654  -0.15461 0.07193  49  GLU   A N     
392  C  CA    . GLU   A 50  ? 0.33000 0.22195 0.35662 0.02401  -0.07764 0.06330  49  GLU   A CA    
393  C  C     . GLU   A 50  ? 0.27417 0.23037 0.27041 0.02589  -0.08666 0.04842  49  GLU   A C     
394  O  O     . GLU   A 50  ? 0.29522 0.25280 0.23795 0.04461  -0.08469 -0.00129 49  GLU   A O     
395  C  CB    . GLU   A 50  ? 0.29198 0.24165 0.47089 0.04551  -0.08147 0.04870  49  GLU   A CB    
396  C  CG    . GLU   A 50  ? 0.32927 0.28113 0.58692 0.01628  -0.13573 0.07703  49  GLU   A CG    
397  C  CD    . GLU   A 50  ? 0.37474 0.33176 0.69397 0.04057  -0.18172 0.07829  49  GLU   A CD    
398  O  OE1   . GLU   A 50  ? 0.41984 0.36122 0.70018 0.01615  -0.21677 0.08247  49  GLU   A OE1   
399  O  OE2   . GLU   A 50  ? 0.46808 0.37444 0.78096 0.04079  -0.16871 0.06110  49  GLU   A OE2   
400  N  N     . THR   A 51  ? 0.27842 0.24895 0.24213 0.00954  -0.06997 0.03133  50  THR   A N     
401  C  CA    . THR   A 51  ? 0.25189 0.24478 0.20725 0.01674  -0.03092 0.00933  50  THR   A CA    
402  C  C     . THR   A 51  ? 0.25904 0.21813 0.23429 -0.00822 -0.05050 0.03970  50  THR   A C     
403  O  O     . THR   A 51  ? 0.23463 0.23188 0.22648 0.01520  -0.05288 0.04829  50  THR   A O     
404  C  CB    . THR   A 51  ? 0.33011 0.24731 0.25066 0.03924  0.02566  0.03950  50  THR   A CB    
405  O  OG1   . THR   A 51  ? 0.43804 0.25540 0.24926 0.00998  -0.00032 0.04420  50  THR   A OG1   
406  C  CG2   . THR   A 51  ? 0.27273 0.29884 0.30701 0.06528  0.02357  0.00375  50  THR   A CG2   
407  N  N     . CYS   A 52  ? 0.22145 0.22200 0.24462 -0.01542 -0.02409 0.07282  51  CYS   A N     
408  C  CA    . CYS   A 52  ? 0.16518 0.19753 0.24361 -0.00989 -0.01016 0.00592  51  CYS   A CA    
409  C  C     . CYS   A 52  ? 0.18704 0.21098 0.26792 -0.00328 -0.01727 0.03405  51  CYS   A C     
410  O  O     . CYS   A 52  ? 0.24679 0.21242 0.34155 0.01690  -0.04877 0.02919  51  CYS   A O     
411  C  CB    . CYS   A 52  ? 0.20703 0.21629 0.22854 0.00825  -0.03742 -0.01160 51  CYS   A CB    
412  S  SG    . CYS   A 52  ? 0.25303 0.23416 0.23819 0.02603  -0.02630 0.01208  51  CYS   A SG    
413  N  N     . LEU   A 53  ? 0.17844 0.21175 0.17354 0.01459  -0.02314 0.02053  52  LEU   A N     
414  C  CA    . LEU   A 53  ? 0.18226 0.19439 0.16413 0.01695  -0.02886 0.00624  52  LEU   A CA    
415  C  C     . LEU   A 53  ? 0.16905 0.20444 0.16557 0.01229  0.00204  0.03511  52  LEU   A C     
416  O  O     . LEU   A 53  ? 0.18003 0.23994 0.15944 -0.00616 -0.00585 0.02862  52  LEU   A O     
417  C  CB    . LEU   A 53  ? 0.22676 0.19808 0.24628 -0.00254 -0.01047 -0.00784 52  LEU   A CB    
418  C  CG    . LEU   A 53  ? 0.19795 0.24609 0.30982 0.00904  -0.02079 -0.05829 52  LEU   A CG    
419  C  CD1   . LEU   A 53  ? 0.24723 0.28514 0.35377 0.00436  -0.01455 -0.07025 52  LEU   A CD1   
420  C  CD2   . LEU   A 53  ? 0.20680 0.27534 0.29355 0.03927  0.00654  -0.04415 52  LEU   A CD2   
421  N  N     . LEU   A 54  ? 0.15085 0.22707 0.17412 0.01291  -0.02492 0.03833  53  LEU   A N     
422  C  CA    . LEU   A 54  ? 0.23253 0.24549 0.16252 0.02654  -0.01637 0.02464  53  LEU   A CA    
423  C  C     . LEU   A 54  ? 0.15046 0.24702 0.19468 -0.00187 -0.00538 0.05275  53  LEU   A C     
424  O  O     . LEU   A 54  ? 0.15731 0.26104 0.23333 0.01564  0.01963  0.04244  53  LEU   A O     
425  C  CB    . LEU   A 54  ? 0.21041 0.24747 0.15978 -0.01106 0.02274  0.00365  53  LEU   A CB    
426  C  CG    . LEU   A 54  ? 0.23587 0.26510 0.24810 0.01852  -0.00458 -0.01452 53  LEU   A CG    
427  C  CD1   . LEU   A 54  ? 0.30325 0.26319 0.22594 0.02777  -0.08906 -0.02345 53  LEU   A CD1   
428  C  CD2   . LEU   A 54  ? 0.22769 0.27894 0.25675 0.00409  -0.01542 -0.06070 53  LEU   A CD2   
429  N  N     . ASP   A 55  ? 0.18414 0.21610 0.12870 0.02320  -0.00325 0.01733  54  ASP   A N     
430  C  CA    . ASP   A 55  ? 0.20540 0.26534 0.19319 0.05667  -0.01418 0.03957  54  ASP   A CA    
431  C  C     . ASP   A 55  ? 0.18438 0.29398 0.14635 0.04818  0.01991  0.04275  54  ASP   A C     
432  O  O     . ASP   A 55  ? 0.20787 0.38500 0.16255 0.05369  0.02724  0.05905  54  ASP   A O     
433  C  CB    . ASP   A 55  ? 0.21098 0.29581 0.22309 0.02796  0.01487  -0.00411 54  ASP   A CB    
434  C  CG    . ASP   A 55  ? 0.45997 0.39417 0.26262 0.00540  0.02438  0.00589  54  ASP   A CG    
435  O  OD1   . ASP   A 55  ? 0.59319 0.45224 0.26744 -0.03624 0.00882  -0.00147 54  ASP   A OD1   
436  O  OD2   . ASP   A 55  ? 0.51310 0.43856 0.30744 0.00441  -0.04490 0.02312  54  ASP   A OD2   
437  N  N     . ILE   A 56  ? 0.18418 0.24662 0.14225 0.04200  0.00826  0.02701  55  ILE   A N     
438  C  CA    . ILE   A 56  ? 0.16845 0.23047 0.15139 0.00758  0.00569  0.03855  55  ILE   A CA    
439  C  C     . ILE   A 56  ? 0.13966 0.22237 0.15482 0.00550  0.02736  0.01609  55  ILE   A C     
440  O  O     . ILE   A 56  ? 0.15982 0.25196 0.17925 0.04228  0.02857  0.03801  55  ILE   A O     
441  C  CB    . ILE   A 56  ? 0.26107 0.22784 0.16034 -0.01119 -0.03177 0.02574  55  ILE   A CB    
442  C  CG1   . ILE   A 56  ? 0.35308 0.26837 0.18823 -0.04970 0.00270  0.05244  55  ILE   A CG1   
443  C  CG2   . ILE   A 56  ? 0.30790 0.22773 0.15754 -0.01505 -0.02281 0.04325  55  ILE   A CG2   
444  C  CD1   . ILE   A 56  ? 0.44156 0.30213 0.25325 -0.01781 0.03023  0.06371  55  ILE   A CD1   
445  N  N     . LEU   A 57  ? 0.12667 0.17386 0.17679 0.01737  -0.00651 0.00730  56  LEU   A N     
446  C  CA    . LEU   A 57  ? 0.14639 0.16222 0.13507 0.02266  -0.01882 -0.00555 56  LEU   A CA    
447  C  C     . LEU   A 57  ? 0.12906 0.18800 0.12518 0.01512  0.02604  0.01134  56  LEU   A C     
448  O  O     . LEU   A 57  ? 0.14601 0.20927 0.13956 0.01209  0.00138  0.01177  56  LEU   A O     
449  C  CB    . LEU   A 57  ? 0.13050 0.17846 0.20442 0.02497  -0.01591 -0.01084 56  LEU   A CB    
450  C  CG    . LEU   A 57  ? 0.14635 0.20448 0.25636 0.01451  -0.01456 -0.01418 56  LEU   A CG    
451  C  CD1   . LEU   A 57  ? 0.22195 0.22541 0.23556 0.07007  -0.01808 0.01486  56  LEU   A CD1   
452  C  CD2   . LEU   A 57  ? 0.19670 0.22879 0.33507 -0.00401 0.02326  0.00215  56  LEU   A CD2   
453  N  N     . ASP   A 58  ? 0.13585 0.17901 0.14808 0.01352  -0.02202 0.01399  57  ASP   A N     
454  C  CA    . ASP   A 58  ? 0.13598 0.20670 0.16555 0.00118  -0.03668 0.01942  57  ASP   A CA    
455  C  C     . ASP   A 58  ? 0.14976 0.19492 0.15905 0.03267  -0.04825 -0.00648 57  ASP   A C     
456  O  O     . ASP   A 58  ? 0.14833 0.21207 0.18363 0.02874  -0.01430 0.01022  57  ASP   A O     
457  C  CB    . ASP   A 58  ? 0.17436 0.24623 0.22131 -0.03863 -0.03149 0.01772  57  ASP   A CB    
458  C  CG    . ASP   A 58  ? 0.18481 0.23789 0.20221 -0.05681 -0.06061 0.01902  57  ASP   A CG    
459  O  OD1   . ASP   A 58  ? 0.18827 0.25537 0.18156 -0.02030 -0.05732 0.00216  57  ASP   A OD1   
460  O  OD2   . ASP   A 58  ? 0.23349 0.25592 0.21507 -0.05988 -0.06250 -0.00776 57  ASP   A OD2   
461  N  N     . THR   A 59  ? 0.17316 0.19032 0.13059 0.00297  0.00781  0.01192  58  THR   A N     
462  C  CA    . THR   A 59  ? 0.14855 0.18698 0.17095 -0.00795 -0.00219 0.01739  58  THR   A CA    
463  C  C     . THR   A 59  ? 0.12573 0.17570 0.16558 0.02345  0.02328  0.01283  58  THR   A C     
464  O  O     . THR   A 59  ? 0.17053 0.19502 0.16715 0.01373  -0.03331 -0.00723 58  THR   A O     
465  C  CB    . THR   A 59  ? 0.15537 0.20036 0.17534 -0.00561 -0.00881 0.01998  58  THR   A CB    
466  O  OG1   . THR   A 59  ? 0.13868 0.21151 0.21356 0.01528  0.00811  0.04652  58  THR   A OG1   
467  C  CG2   . THR   A 59  ? 0.14464 0.21420 0.21728 0.00012  -0.02902 0.03726  58  THR   A CG2   
468  N  N     . ALA   A 60  ? 0.14329 0.18895 0.18526 0.02508  -0.03105 0.01457  59  ALA   A N     
469  C  CA    . ALA   A 60  ? 0.20051 0.17165 0.16953 0.02586  -0.03395 0.03846  59  ALA   A CA    
470  C  C     . ALA   A 60  ? 0.19377 0.22647 0.17054 0.01429  -0.00296 0.04409  59  ALA   A C     
471  O  O     . ALA   A 60  ? 0.16154 0.29295 0.20293 0.03636  0.00542  0.05022  59  ALA   A O     
472  C  CB    . ALA   A 60  ? 0.17999 0.19483 0.22137 0.04149  -0.02825 0.03935  59  ALA   A CB    
473  N  N     . GLY   A 61  ? 0.20222 0.24943 0.16241 -0.00035 0.00516  0.02859  60  GLY   A N     
474  C  CA    . GLY   A 61  ? 0.25764 0.27856 0.22460 0.03871  -0.01106 0.04099  60  GLY   A CA    
475  C  C     . GLY   A 61  ? 0.52771 0.32752 0.28724 0.03102  0.05802  0.05448  60  GLY   A C     
476  O  O     . GLY   A 61  ? 0.79057 0.37450 0.33563 0.03394  0.12433  0.03198  60  GLY   A O     
477  N  N     . GLN   A 62  ? 0.54892 0.32276 0.31530 0.00140  0.01382  0.13020  61  GLN   A N     
478  C  CA    . GLN   A 62  ? 0.63139 0.34681 0.38765 -0.04226 0.06970  0.10517  61  GLN   A CA    
479  C  C     . GLN   A 62  ? 0.61245 0.38442 0.43545 -0.07830 0.13145  0.06673  61  GLN   A C     
480  O  O     . GLN   A 62  ? 0.60870 0.38973 0.47125 -0.09620 0.08458  0.05226  61  GLN   A O     
481  C  CB    . GLN   A 62  ? 0.75060 0.33442 0.42563 -0.02800 0.02108  0.11420  61  GLN   A CB    
482  C  CG    . GLN   A 62  ? 0.89604 0.33576 0.42281 -0.03736 0.05154  0.10524  61  GLN   A CG    
483  C  CD    . GLN   A 62  ? 1.05418 0.33798 0.43537 -0.05227 0.07766  0.09956  61  GLN   A CD    
484  O  OE1   . GLN   A 62  ? 1.15043 0.35000 0.44956 -0.03403 0.01805  0.09812  61  GLN   A OE1   
485  N  NE2   . GLN   A 62  ? 1.09640 0.32914 0.43889 -0.05274 0.07628  0.08208  61  GLN   A NE2   
486  N  N     . GLU   A 63  ? 0.67210 0.46308 0.49436 -0.04320 0.20878  0.02642  62  GLU   A N     
487  C  CA    . GLU   A 63  ? 0.75944 0.55170 0.60385 -0.02457 0.26048  0.01432  62  GLU   A CA    
488  C  C     . GLU   A 63  ? 0.65344 0.56661 0.63103 -0.01105 0.23672  0.03068  62  GLU   A C     
489  O  O     . GLU   A 63  ? 0.64369 0.57640 0.67038 -0.00178 0.23467  0.03290  62  GLU   A O     
490  C  CB    . GLU   A 63  ? 0.97821 0.61414 0.68245 -0.03208 0.29063  0.00774  62  GLU   A CB    
491  C  CG    . GLU   A 63  ? 1.18114 0.66391 0.76881 -0.03576 0.30036  0.00470  62  GLU   A CG    
492  C  CD    . GLU   A 63  ? 1.34638 0.70034 0.83530 -0.04356 0.32021  0.00584  62  GLU   A CD    
493  O  OE1   . GLU   A 63  ? 1.41940 0.71920 0.86190 -0.04452 0.32006  0.01740  62  GLU   A OE1   
494  O  OE2   . GLU   A 63  ? 1.38641 0.72069 0.85597 -0.04331 0.33429  -0.01170 62  GLU   A OE2   
495  N  N     . GLU   A 64  ? 0.52508 0.58085 0.63309 0.00087  0.19491  0.04136  63  GLU   A N     
496  C  CA    . GLU   A 64  ? 0.52668 0.60671 0.67380 0.01443  0.12558  0.05124  63  GLU   A CA    
497  C  C     . GLU   A 64  ? 0.45598 0.58476 0.60583 0.04591  0.09601  0.06572  63  GLU   A C     
498  O  O     . GLU   A 64  ? 0.59862 0.59326 0.64593 0.02984  0.03557  0.04908  63  GLU   A O     
499  C  CB    . GLU   A 64  ? 0.63576 0.65612 0.75272 0.00798  0.04846  0.05625  63  GLU   A CB    
500  C  CG    . GLU   A 64  ? 0.72891 0.70076 0.81864 0.02021  0.01123  0.06197  63  GLU   A CG    
501  C  CD    . GLU   A 64  ? 0.82995 0.73343 0.86786 -0.00086 -0.01370 0.06235  63  GLU   A CD    
502  O  OE1   . GLU   A 64  ? 0.84696 0.73803 0.88005 -0.00086 -0.01581 0.06211  63  GLU   A OE1   
503  O  OE2   . GLU   A 64  ? 0.86133 0.74363 0.88783 -0.02481 -0.02032 0.05903  63  GLU   A OE2   
504  N  N     . TYR   A 65  ? 0.24982 0.55489 0.48626 0.10798  0.08824  0.10099  64  TYR   A N     
505  C  CA    . TYR   A 65  ? 0.20205 0.49604 0.42129 0.11726  0.05630  0.14302  64  TYR   A CA    
506  C  C     . TYR   A 65  ? 0.19702 0.43934 0.37874 0.10455  0.04817  0.18085  64  TYR   A C     
507  O  O     . TYR   A 65  ? 0.21527 0.43296 0.37107 0.11621  0.06929  0.19970  64  TYR   A O     
508  C  CB    . TYR   A 65  ? 0.18947 0.47076 0.34900 0.10486  0.04585  0.16570  64  TYR   A CB    
509  C  CG    . TYR   A 65  ? 0.17857 0.45815 0.28273 0.08022  0.02905  0.18142  64  TYR   A CG    
510  C  CD1   . TYR   A 65  ? 0.23296 0.45489 0.28751 0.12747  0.04710  0.17708  64  TYR   A CD1   
511  C  CD2   . TYR   A 65  ? 0.21170 0.47061 0.31015 0.09134  0.02636  0.15945  64  TYR   A CD2   
512  C  CE1   . TYR   A 65  ? 0.21522 0.43484 0.34558 0.13144  0.05358  0.15797  64  TYR   A CE1   
513  C  CE2   . TYR   A 65  ? 0.18409 0.44552 0.26363 0.09958  0.06595  0.17526  64  TYR   A CE2   
514  C  CZ    . TYR   A 65  ? 0.18333 0.41998 0.29809 0.09154  0.08302  0.13974  64  TYR   A CZ    
515  O  OH    . TYR   A 65  ? 0.21959 0.43772 0.25703 0.10758  0.04042  0.11670  64  TYR   A OH    
516  N  N     . SER   A 66  ? 0.18952 0.42069 0.39236 0.07155  0.07896  0.19148  65  SER   A N     
517  C  CA    . SER   A 66  ? 0.19713 0.40238 0.42669 0.05356  0.09632  0.19660  65  SER   A CA    
518  C  C     . SER   A 66  ? 0.17166 0.35570 0.42126 0.04256  0.07514  0.18991  65  SER   A C     
519  O  O     . SER   A 66  ? 0.18606 0.35813 0.43989 0.04558  0.05943  0.21016  65  SER   A O     
520  C  CB    . SER   A 66  ? 0.27424 0.42147 0.47859 0.05514  0.13762  0.19840  65  SER   A CB    
521  O  OG    . SER   A 66  ? 0.36692 0.47604 0.51948 0.05125  0.14042  0.17945  65  SER   A OG    
522  N  N     . ALA   A 67  ? 0.22794 0.34141 0.42843 0.01886  0.08418  0.19357  66  ALA   A N     
523  C  CA    . ALA   A 67  ? 0.23870 0.31777 0.44866 0.00111  0.04555  0.15882  66  ALA   A CA    
524  C  C     . ALA   A 67  ? 0.17735 0.30512 0.41216 -0.00039 0.02007  0.12940  66  ALA   A C     
525  O  O     . ALA   A 67  ? 0.15747 0.32991 0.43371 0.01345  -0.00541 0.16297  66  ALA   A O     
526  C  CB    . ALA   A 67  ? 0.28346 0.31845 0.51233 -0.02016 0.03868  0.12966  66  ALA   A CB    
527  N  N     A MET   A 68  ? 0.13517 0.28840 0.39565 0.02518  0.02195  0.11028  67  MET   A N     
528  N  N     B MET   A 68  ? 0.15590 0.29843 0.36201 -0.00327 0.02306  0.12519  67  MET   A N     
529  C  CA    A MET   A 68  ? 0.12318 0.26094 0.37843 0.04648  0.01706  0.09241  67  MET   A CA    
530  C  CA    B MET   A 68  ? 0.15487 0.28372 0.31891 0.00232  0.02112  0.12799  67  MET   A CA    
531  C  C     A MET   A 68  ? 0.11855 0.26134 0.33313 0.05030  0.03996  0.09038  67  MET   A C     
532  C  C     B MET   A 68  ? 0.14981 0.26606 0.28248 0.02338  0.05053  0.10917  67  MET   A C     
533  O  O     A MET   A 68  ? 0.11872 0.26366 0.33331 0.05642  0.03304  0.07832  67  MET   A O     
534  O  O     B MET   A 68  ? 0.20350 0.26368 0.28990 0.02038  0.02538  0.12320  67  MET   A O     
535  C  CB    A MET   A 68  ? 0.13653 0.27216 0.43293 0.05130  0.02245  0.08767  67  MET   A CB    
536  C  CB    B MET   A 68  ? 0.18411 0.32305 0.31853 -0.00949 0.04092  0.10039  67  MET   A CB    
537  C  CG    A MET   A 68  ? 0.13108 0.26198 0.42691 0.05127  -0.00518 0.05843  67  MET   A CG    
538  C  CG    B MET   A 68  ? 0.16826 0.33541 0.24799 -0.01571 -0.01046 0.06679  67  MET   A CG    
539  S  SD    A MET   A 68  ? 0.21294 0.23608 0.46701 0.02031  -0.01110 0.04733  67  MET   A SD    
540  S  SD    B MET   A 68  ? 0.18622 0.34332 0.26334 -0.00622 -0.05212 0.02065  67  MET   A SD    
541  C  CE    A MET   A 68  ? 0.24202 0.22706 0.49495 -0.03765 -0.03349 0.05717  67  MET   A CE    
542  C  CE    B MET   A 68  ? 0.19649 0.33409 0.29437 -0.00650 -0.00853 0.01499  67  MET   A CE    
543  N  N     . ARG   A 69  ? 0.13672 0.26025 0.30246 0.04156  0.01894  0.08328  68  ARG   A N     
544  C  CA    . ARG   A 69  ? 0.19531 0.23018 0.30607 0.02548  -0.03061 0.02892  68  ARG   A CA    
545  C  C     . ARG   A 69  ? 0.16522 0.22827 0.23711 0.02727  -0.02519 0.04547  68  ARG   A C     
546  O  O     . ARG   A 69  ? 0.19468 0.22603 0.21572 0.04562  0.01523  0.03562  68  ARG   A O     
547  C  CB    . ARG   A 69  ? 0.23850 0.26725 0.39434 0.03712  -0.05144 -0.00348 68  ARG   A CB    
548  C  CG    . ARG   A 69  ? 0.34961 0.27680 0.47875 0.02481  -0.04749 -0.05293 68  ARG   A CG    
549  C  CD    . ARG   A 69  ? 0.42752 0.27572 0.51110 -0.00091 -0.08411 -0.06086 68  ARG   A CD    
550  N  NE    . ARG   A 69  ? 0.44454 0.24399 0.54737 -0.02770 -0.09505 -0.06777 68  ARG   A NE    
551  C  CZ    . ARG   A 69  ? 0.48475 0.25021 0.57755 -0.02171 -0.03054 -0.06880 68  ARG   A CZ    
552  N  NH1   . ARG   A 69  ? 0.52785 0.25745 0.59251 -0.03288 0.01169  -0.07340 68  ARG   A NH1   
553  N  NH2   . ARG   A 69  ? 0.47299 0.25679 0.55320 0.01682  0.00434  -0.09249 68  ARG   A NH2   
554  N  N     . ASP   A 70  ? 0.17295 0.26055 0.22791 0.00349  0.00517  0.02570  69  ASP   A N     
555  C  CA    . ASP   A 70  ? 0.12687 0.26355 0.21767 0.01118  0.01722  0.03043  69  ASP   A CA    
556  C  C     . ASP   A 70  ? 0.20980 0.22143 0.19676 0.03649  0.03914  0.02639  69  ASP   A C     
557  O  O     . ASP   A 70  ? 0.16175 0.23083 0.19864 0.03932  -0.00711 0.01372  69  ASP   A O     
558  C  CB    . ASP   A 70  ? 0.14315 0.29775 0.23382 -0.00656 0.03187  0.07908  69  ASP   A CB    
559  C  CG    . ASP   A 70  ? 0.20639 0.36165 0.28305 0.04673  0.02214  0.08482  69  ASP   A CG    
560  O  OD1   . ASP   A 70  ? 0.26122 0.39860 0.26246 0.07591  0.03530  0.10855  69  ASP   A OD1   
561  O  OD2   . ASP   A 70  ? 0.26809 0.37960 0.30162 0.04128  0.02276  0.13333  69  ASP   A OD2   
562  N  N     . GLN   A 71  ? 0.16646 0.20948 0.22642 -0.00888 0.02937  0.02438  70  GLN   A N     
563  C  CA    . GLN   A 71  ? 0.16174 0.18679 0.22296 0.00848  0.02986  0.02155  70  GLN   A CA    
564  C  C     . GLN   A 71  ? 0.12588 0.18481 0.20674 0.00371  0.00220  -0.00066 70  GLN   A C     
565  O  O     . GLN   A 71  ? 0.16828 0.17633 0.18108 0.00609  0.00193  -0.00090 70  GLN   A O     
566  C  CB    . GLN   A 71  ? 0.18894 0.19768 0.26703 0.05062  0.05805  -0.02003 70  GLN   A CB    
567  C  CG    . GLN   A 71  ? 0.25947 0.20554 0.24278 0.00372  0.05904  0.00257  70  GLN   A CG    
568  C  CD    . GLN   A 71  ? 0.25021 0.19244 0.21000 -0.02822 0.03619  -0.01047 70  GLN   A CD    
569  O  OE1   . GLN   A 71  ? 0.24244 0.21360 0.27569 -0.04874 0.03134  0.02449  70  GLN   A OE1   
570  N  NE2   . GLN   A 71  ? 0.34502 0.17676 0.18834 -0.02450 0.01982  -0.01535 70  GLN   A NE2   
571  N  N     . TYR   A 72  ? 0.15544 0.18049 0.18377 0.00986  0.00739  0.01153  71  TYR   A N     
572  C  CA    . TYR   A 72  ? 0.12818 0.18396 0.24219 0.00334  -0.00539 -0.00582 71  TYR   A CA    
573  C  C     . TYR   A 72  ? 0.13422 0.19107 0.19114 0.01224  -0.02371 0.00940  71  TYR   A C     
574  O  O     . TYR   A 72  ? 0.15348 0.17909 0.19178 0.00707  0.00065  0.02770  71  TYR   A O     
575  C  CB    . TYR   A 72  ? 0.12508 0.21174 0.24748 -0.00100 -0.03596 -0.02234 71  TYR   A CB    
576  C  CG    . TYR   A 72  ? 0.16570 0.19630 0.21681 -0.01311 -0.00160 0.02490  71  TYR   A CG    
577  C  CD1   . TYR   A 72  ? 0.17724 0.22534 0.19541 0.02604  -0.00408 0.04104  71  TYR   A CD1   
578  C  CD2   . TYR   A 72  ? 0.17116 0.21896 0.19089 -0.01563 -0.03158 0.01881  71  TYR   A CD2   
579  C  CE1   . TYR   A 72  ? 0.14302 0.24119 0.19743 0.01246  -0.01491 0.02631  71  TYR   A CE1   
580  C  CE2   . TYR   A 72  ? 0.13097 0.23942 0.19589 -0.01075 -0.01212 0.01366  71  TYR   A CE2   
581  C  CZ    . TYR   A 72  ? 0.12757 0.22711 0.20042 -0.01653 -0.02829 0.02386  71  TYR   A CZ    
582  O  OH    . TYR   A 72  ? 0.12150 0.23229 0.23630 0.01004  -0.01676 0.00896  71  TYR   A OH    
583  N  N     . MET   A 73  ? 0.11492 0.24024 0.19436 0.01161  0.00472  0.00770  72  MET   A N     
584  C  CA    . MET   A 73  ? 0.10800 0.22410 0.15537 0.01521  0.00207  -0.00308 72  MET   A CA    
585  C  C     . MET   A 73  ? 0.13761 0.17581 0.17673 0.01581  0.00604  -0.00953 72  MET   A C     
586  O  O     . MET   A 73  ? 0.15860 0.19144 0.20155 0.02209  -0.03258 -0.00371 72  MET   A O     
587  C  CB    . MET   A 73  ? 0.12816 0.24705 0.19520 0.00675  -0.02233 0.00795  72  MET   A CB    
588  C  CG    . MET   A 73  ? 0.22204 0.27686 0.14181 0.01948  -0.01733 0.01322  72  MET   A CG    
589  S  SD    . MET   A 73  ? 0.20391 0.31010 0.20938 0.00142  -0.02209 0.00199  72  MET   A SD    
590  C  CE    . MET   A 73  ? 0.19941 0.37413 0.26846 0.01457  -0.06294 0.01697  72  MET   A CE    
591  N  N     . ARG   A 74  ? 0.13913 0.18799 0.17983 -0.00068 -0.02396 -0.00210 73  ARG   A N     
592  C  CA    . ARG   A 74  ? 0.17065 0.17946 0.22067 0.02118  -0.04399 -0.01334 73  ARG   A CA    
593  C  C     . ARG   A 74  ? 0.19546 0.19887 0.20939 0.02338  -0.04392 -0.02056 73  ARG   A C     
594  O  O     . ARG   A 74  ? 0.19212 0.21797 0.22398 0.00548  -0.03204 -0.02333 73  ARG   A O     
595  C  CB    . ARG   A 74  ? 0.22964 0.19072 0.26924 0.00082  0.03408  -0.00120 73  ARG   A CB    
596  C  CG    . ARG   A 74  ? 0.26306 0.21387 0.33265 -0.08039 0.03454  0.00286  73  ARG   A CG    
597  C  CD    . ARG   A 74  ? 0.31133 0.23819 0.33855 -0.05937 -0.03849 -0.01062 73  ARG   A CD    
598  N  NE    . ARG   A 74  ? 0.37997 0.23066 0.31227 -0.12092 -0.01553 -0.00137 73  ARG   A NE    
599  C  CZ    . ARG   A 74  ? 0.51685 0.25589 0.27501 -0.08158 -0.02968 0.01346  73  ARG   A CZ    
600  N  NH1   . ARG   A 74  ? 0.41176 0.27462 0.25268 -0.07779 0.00147  -0.01643 73  ARG   A NH1   
601  N  NH2   . ARG   A 74  ? 0.50293 0.26657 0.27927 -0.10560 -0.08966 0.01354  73  ARG   A NH2   
602  N  N     . THR   A 75  ? 0.19845 0.18298 0.17181 0.00183  -0.01809 0.02032  74  THR   A N     
603  C  CA    . THR   A 75  ? 0.22847 0.17971 0.19852 -0.00858 -0.03152 0.03760  74  THR   A CA    
604  C  C     . THR   A 75  ? 0.19121 0.18321 0.18475 0.00568  -0.03006 0.04304  74  THR   A C     
605  O  O     . THR   A 75  ? 0.24192 0.19404 0.17958 0.00904  -0.01793 0.01754  74  THR   A O     
606  C  CB    . THR   A 75  ? 0.24129 0.16675 0.21302 -0.00627 0.05517  -0.02222 74  THR   A CB    
607  O  OG1   . THR   A 75  ? 0.28294 0.20842 0.24559 0.00657  0.01704  -0.02005 74  THR   A OG1   
608  C  CG2   . THR   A 75  ? 0.30851 0.23359 0.24550 0.00020  0.06120  -0.03865 74  THR   A CG2   
609  N  N     . GLY   A 76  ? 0.15744 0.18781 0.18240 -0.00781 -0.03970 0.01219  75  GLY   A N     
610  C  CA    . GLY   A 76  ? 0.13983 0.17105 0.20784 0.00530  -0.03456 0.01325  75  GLY   A CA    
611  C  C     . GLY   A 76  ? 0.15700 0.15239 0.21730 -0.01253 -0.02701 -0.00158 75  GLY   A C     
612  O  O     . GLY   A 76  ? 0.15363 0.19698 0.21481 -0.00072 -0.01278 0.02631  75  GLY   A O     
613  N  N     . GLU   A 77  ? 0.15242 0.14580 0.16142 -0.00800 -0.02410 -0.00210 76  GLU   A N     
614  C  CA    . GLU   A 77  ? 0.16825 0.17017 0.15879 0.02763  -0.05099 -0.01482 76  GLU   A CA    
615  C  C     . GLU   A 77  ? 0.17112 0.17625 0.15946 0.02215  -0.03633 -0.02600 76  GLU   A C     
616  O  O     . GLU   A 77  ? 0.15743 0.21177 0.22649 0.00940  -0.04140 -0.06355 76  GLU   A O     
617  C  CB    . GLU   A 77  ? 0.21564 0.21357 0.15370 0.04971  -0.06823 -0.01388 76  GLU   A CB    
618  C  CG    . GLU   A 77  ? 0.28994 0.26292 0.19984 0.04411  -0.10479 -0.03585 76  GLU   A CG    
619  C  CD    . GLU   A 77  ? 0.32078 0.31820 0.23581 0.02357  -0.06348 -0.01410 76  GLU   A CD    
620  O  OE1   . GLU   A 77  ? 0.26345 0.38880 0.19909 -0.00385 -0.09238 0.02614  76  GLU   A OE1   
621  O  OE2   . GLU   A 77  ? 0.34410 0.31746 0.26701 0.03331  -0.05875 -0.00419 76  GLU   A OE2   
622  N  N     . GLY   A 78  ? 0.14691 0.16738 0.13985 0.00583  -0.03121 -0.02541 77  GLY   A N     
623  C  CA    . GLY   A 78  ? 0.15945 0.17151 0.16103 0.01960  -0.02302 -0.00696 77  GLY   A CA    
624  C  C     . GLY   A 78  ? 0.13624 0.16236 0.16362 0.00117  -0.02589 0.00685  77  GLY   A C     
625  O  O     . GLY   A 78  ? 0.13133 0.17454 0.15406 0.01142  -0.01324 -0.00765 77  GLY   A O     
626  N  N     . PHE   A 79  ? 0.12927 0.15677 0.14340 -0.01401 -0.01828 -0.01587 78  PHE   A N     
627  C  CA    . PHE   A 79  ? 0.12130 0.16916 0.15528 -0.00990 -0.04126 0.00468  78  PHE   A CA    
628  C  C     . PHE   A 79  ? 0.11184 0.17258 0.17878 -0.00608 -0.04727 0.00559  78  PHE   A C     
629  O  O     . PHE   A 79  ? 0.14660 0.17494 0.18725 0.01432  -0.01798 -0.02407 78  PHE   A O     
630  C  CB    . PHE   A 79  ? 0.14730 0.16553 0.16043 -0.00761 0.01169  0.00764  78  PHE   A CB    
631  C  CG    . PHE   A 79  ? 0.13130 0.20024 0.13903 -0.00936 -0.00373 0.00264  78  PHE   A CG    
632  C  CD1   . PHE   A 79  ? 0.12376 0.19200 0.19817 0.01517  0.01025  0.00668  78  PHE   A CD1   
633  C  CD2   . PHE   A 79  ? 0.14431 0.16782 0.16803 0.01793  0.02980  0.00832  78  PHE   A CD2   
634  C  CE1   . PHE   A 79  ? 0.15714 0.16426 0.17732 -0.00298 0.01493  -0.02206 78  PHE   A CE1   
635  C  CE2   . PHE   A 79  ? 0.16635 0.18041 0.15858 -0.03579 -0.00997 -0.01282 78  PHE   A CE2   
636  C  CZ    . PHE   A 79  ? 0.15701 0.16319 0.18324 -0.01383 0.02109  -0.00184 78  PHE   A CZ    
637  N  N     . LEU   A 80  ? 0.14271 0.15027 0.16062 0.00416  -0.03386 0.01168  79  LEU   A N     
638  C  CA    . LEU   A 80  ? 0.12108 0.16844 0.20436 0.01670  -0.03611 -0.00254 79  LEU   A CA    
639  C  C     . LEU   A 80  ? 0.15876 0.16857 0.15947 0.01907  -0.05340 -0.00610 79  LEU   A C     
640  O  O     . LEU   A 80  ? 0.17806 0.19615 0.17397 0.03974  -0.05345 -0.02956 79  LEU   A O     
641  C  CB    . LEU   A 80  ? 0.12880 0.20344 0.29827 0.02966  0.01974  -0.00034 79  LEU   A CB    
642  C  CG    . LEU   A 80  ? 0.24318 0.19215 0.38545 0.03629  0.02560  -0.00390 79  LEU   A CG    
643  C  CD1   . LEU   A 80  ? 0.32752 0.16848 0.30091 0.08147  -0.03959 -0.00749 79  LEU   A CD1   
644  C  CD2   . LEU   A 80  ? 0.25548 0.18778 0.41639 -0.01073 0.06597  -0.01804 79  LEU   A CD2   
645  N  N     . CYS   A 81  ? 0.17092 0.18089 0.14645 0.00547  -0.06801 -0.00566 80  CYS   A N     
646  C  CA    . CYS   A 81  ? 0.14588 0.19784 0.16809 -0.01289 -0.03297 -0.02370 80  CYS   A CA    
647  C  C     . CYS   A 81  ? 0.14929 0.15946 0.17755 -0.01908 -0.03686 -0.03845 80  CYS   A C     
648  O  O     . CYS   A 81  ? 0.16558 0.15716 0.17831 0.02052  -0.03498 -0.01090 80  CYS   A O     
649  C  CB    . CYS   A 81  ? 0.15559 0.21543 0.19841 0.00748  -0.01681 -0.05397 80  CYS   A CB    
650  S  SG    . CYS   A 81  ? 0.17774 0.25905 0.23465 -0.01408 -0.03796 -0.04496 80  CYS   A SG    
651  N  N     . VAL   A 82  ? 0.14280 0.18629 0.16917 0.00666  -0.05031 -0.01070 81  VAL   A N     
652  C  CA    . VAL   A 82  ? 0.14364 0.19431 0.14915 0.00734  -0.05232 -0.00880 81  VAL   A CA    
653  C  C     . VAL   A 82  ? 0.15265 0.18462 0.17359 -0.03316 -0.04794 -0.02303 81  VAL   A C     
654  O  O     . VAL   A 82  ? 0.16161 0.18630 0.19453 -0.00681 -0.02407 -0.01364 81  VAL   A O     
655  C  CB    . VAL   A 82  ? 0.13531 0.18159 0.16878 0.00268  -0.03445 0.00016  81  VAL   A CB    
656  C  CG1   . VAL   A 82  ? 0.15358 0.19360 0.20259 -0.00197 -0.02655 -0.01487 81  VAL   A CG1   
657  C  CG2   . VAL   A 82  ? 0.19723 0.22070 0.12314 0.02678  -0.01520 0.00813  81  VAL   A CG2   
658  N  N     . PHE   A 83  ? 0.16905 0.20310 0.12160 -0.01085 -0.05100 -0.02656 82  PHE   A N     
659  C  CA    . PHE   A 83  ? 0.15776 0.19104 0.15381 0.01201  -0.06290 -0.02284 82  PHE   A CA    
660  C  C     . PHE   A 83  ? 0.15059 0.18722 0.17222 -0.00650 -0.03088 -0.04435 82  PHE   A C     
661  O  O     . PHE   A 83  ? 0.17241 0.19749 0.18455 -0.03145 -0.01896 0.02720  82  PHE   A O     
662  C  CB    . PHE   A 83  ? 0.17923 0.18967 0.16206 0.01577  -0.06464 0.01064  82  PHE   A CB    
663  C  CG    . PHE   A 83  ? 0.19862 0.19820 0.16464 0.02236  -0.05203 0.00241  82  PHE   A CG    
664  C  CD1   . PHE   A 83  ? 0.24386 0.19237 0.15722 0.04423  -0.05071 -0.02456 82  PHE   A CD1   
665  C  CD2   . PHE   A 83  ? 0.18966 0.19446 0.16344 0.01437  -0.04480 -0.02094 82  PHE   A CD2   
666  C  CE1   . PHE   A 83  ? 0.23360 0.18739 0.17474 0.03114  -0.01837 -0.02670 82  PHE   A CE1   
667  C  CE2   . PHE   A 83  ? 0.24431 0.21479 0.15808 0.03131  -0.02126 0.01601  82  PHE   A CE2   
668  C  CZ    . PHE   A 83  ? 0.22754 0.19967 0.13812 0.02551  -0.00443 -0.02254 82  PHE   A CZ    
669  N  N     . ALA   A 84  ? 0.15466 0.19086 0.18046 0.00247  -0.06609 -0.04192 83  ALA   A N     
670  C  CA    . ALA   A 84  ? 0.19997 0.17209 0.19022 0.01178  -0.05154 -0.04697 83  ALA   A CA    
671  C  C     . ALA   A 84  ? 0.18250 0.18206 0.17592 0.01224  -0.05188 -0.01196 83  ALA   A C     
672  O  O     . ALA   A 84  ? 0.19457 0.19621 0.16726 -0.02042 -0.04766 -0.00951 83  ALA   A O     
673  C  CB    . ALA   A 84  ? 0.18774 0.18855 0.21078 0.00614  -0.04737 -0.02386 83  ALA   A CB    
674  N  N     . ILE   A 85  ? 0.21305 0.18431 0.17240 -0.00290 -0.04848 -0.02995 84  ILE   A N     
675  C  CA    . ILE   A 85  ? 0.24127 0.21777 0.17561 0.01070  -0.06772 -0.00644 84  ILE   A CA    
676  C  C     . ILE   A 85  ? 0.27395 0.22579 0.17983 -0.01061 -0.07497 -0.01318 84  ILE   A C     
677  O  O     . ILE   A 85  ? 0.30624 0.23390 0.18109 -0.00333 -0.10029 -0.02398 84  ILE   A O     
678  C  CB    . ILE   A 85  ? 0.25621 0.23501 0.22237 0.02023  -0.07377 0.01152  84  ILE   A CB    
679  C  CG1   . ILE   A 85  ? 0.31438 0.23285 0.27514 -0.01814 -0.06430 0.00078  84  ILE   A CG1   
680  C  CG2   . ILE   A 85  ? 0.25915 0.24908 0.23939 0.04957  -0.09819 -0.01296 84  ILE   A CG2   
681  C  CD1   . ILE   A 85  ? 0.35900 0.27750 0.31095 -0.05436 -0.05214 -0.01226 84  ILE   A CD1   
682  N  N     . ASN   A 86  ? 0.22321 0.22260 0.18710 -0.01711 -0.08170 -0.02131 85  ASN   A N     
683  C  CA    . ASN   A 86  ? 0.19225 0.24005 0.20186 -0.02177 -0.06488 -0.01438 85  ASN   A CA    
684  C  C     . ASN   A 86  ? 0.19744 0.23605 0.16941 -0.01670 -0.06476 -0.02028 85  ASN   A C     
685  O  O     . ASN   A 86  ? 0.22378 0.24480 0.18800 0.01139  -0.09213 -0.03446 85  ASN   A O     
686  C  CB    . ASN   A 86  ? 0.19708 0.26543 0.24142 -0.01400 -0.05007 -0.00847 85  ASN   A CB    
687  C  CG    . ASN   A 86  ? 0.17510 0.26688 0.23681 -0.02440 -0.07734 -0.00093 85  ASN   A CG    
688  O  OD1   . ASN   A 86  ? 0.20832 0.24307 0.21473 0.00864  -0.06617 -0.01401 85  ASN   A OD1   
689  N  ND2   . ASN   A 86  ? 0.21573 0.28943 0.24310 -0.02104 -0.04194 -0.01668 85  ASN   A ND2   
690  N  N     . ASN   A 87  ? 0.17582 0.21180 0.16461 -0.02266 -0.03356 -0.02047 86  ASN   A N     
691  C  CA    . ASN   A 87  ? 0.22030 0.20731 0.19471 -0.02088 -0.01226 0.01466  86  ASN   A CA    
692  C  C     . ASN   A 87  ? 0.21248 0.20954 0.19123 0.00999  -0.02328 -0.00602 86  ASN   A C     
693  O  O     . ASN   A 87  ? 0.21321 0.19023 0.20343 0.02071  -0.08401 -0.03229 86  ASN   A O     
694  C  CB    . ASN   A 87  ? 0.23008 0.23701 0.22855 0.03009  -0.01949 0.00105  86  ASN   A CB    
695  C  CG    . ASN   A 87  ? 0.21387 0.24902 0.24388 0.03891  -0.01077 -0.00209 86  ASN   A CG    
696  O  OD1   . ASN   A 87  ? 0.22267 0.26271 0.24882 0.01507  -0.02986 0.04665  86  ASN   A OD1   
697  N  ND2   . ASN   A 87  ? 0.23458 0.24937 0.31102 0.05269  -0.03710 -0.03804 86  ASN   A ND2   
698  N  N     . THR   A 88  ? 0.21379 0.22868 0.18962 -0.00832 -0.04202 0.00590  87  THR   A N     
699  C  CA    . THR   A 88  ? 0.17301 0.22949 0.16601 -0.01106 -0.02596 0.00294  87  THR   A CA    
700  C  C     . THR   A 88  ? 0.19726 0.24224 0.18007 0.01006  -0.05514 -0.01211 87  THR   A C     
701  O  O     . THR   A 88  ? 0.20505 0.27693 0.17530 0.01005  -0.05771 -0.02826 87  THR   A O     
702  C  CB    . THR   A 88  ? 0.23450 0.28389 0.20327 0.00162  0.00014  -0.02990 87  THR   A CB    
703  O  OG1   . THR   A 88  ? 0.32094 0.27801 0.22325 0.00098  -0.07088 -0.05600 87  THR   A OG1   
704  C  CG2   . THR   A 88  ? 0.23070 0.30950 0.21434 -0.02864 0.00636  -0.01705 87  THR   A CG2   
705  N  N     . LYS   A 89  ? 0.20946 0.26008 0.21310 0.00951  -0.04889 0.00541  88  LYS   A N     
706  C  CA    . LYS   A 89  ? 0.16308 0.26594 0.21771 0.01649  -0.00980 0.01688  88  LYS   A CA    
707  C  C     . LYS   A 89  ? 0.15560 0.25791 0.21879 0.00305  -0.06060 0.00058  88  LYS   A C     
708  O  O     . LYS   A 89  ? 0.20481 0.23370 0.22095 -0.02024 -0.06477 0.03217  88  LYS   A O     
709  C  CB    . LYS   A 89  ? 0.24988 0.27017 0.26875 0.01278  -0.06263 0.01841  88  LYS   A CB    
710  C  CG    . LYS   A 89  ? 0.33271 0.30002 0.33789 0.01343  -0.07051 0.03885  88  LYS   A CG    
711  C  CD    . LYS   A 89  ? 0.35944 0.33391 0.38571 0.03324  -0.04157 0.01158  88  LYS   A CD    
712  C  CE    . LYS   A 89  ? 0.40910 0.34803 0.40794 0.01312  -0.00955 0.01238  88  LYS   A CE    
713  N  NZ    . LYS   A 89  ? 0.36323 0.36213 0.43690 0.00049  -0.04226 0.02253  88  LYS   A NZ    
714  N  N     . SER   A 90  ? 0.21022 0.23561 0.17802 0.01974  -0.05355 -0.00049 89  SER   A N     
715  C  CA    . SER   A 90  ? 0.19314 0.23571 0.16395 0.04606  -0.05672 -0.02224 89  SER   A CA    
716  C  C     . SER   A 90  ? 0.18106 0.19689 0.19299 -0.01049 -0.05595 -0.03538 89  SER   A C     
717  O  O     . SER   A 90  ? 0.23493 0.17850 0.22067 0.01018  -0.05844 -0.01677 89  SER   A O     
718  C  CB    . SER   A 90  ? 0.23628 0.22829 0.15843 0.02621  -0.01736 -0.01926 89  SER   A CB    
719  O  OG    . SER   A 90  ? 0.23084 0.17819 0.18804 0.01203  -0.03415 -0.02006 89  SER   A OG    
720  N  N     . PHE   A 91  ? 0.15391 0.19368 0.18694 0.02745  -0.04353 0.00439  90  PHE   A N     
721  C  CA    . PHE   A 91  ? 0.18561 0.19986 0.17627 -0.02497 -0.05413 -0.00449 90  PHE   A CA    
722  C  C     . PHE   A 91  ? 0.17283 0.24067 0.18677 -0.01542 -0.06044 0.00670  90  PHE   A C     
723  O  O     . PHE   A 91  ? 0.19477 0.24925 0.21322 0.00671  -0.04715 -0.02346 90  PHE   A O     
724  C  CB    . PHE   A 91  ? 0.19455 0.22499 0.19857 -0.02253 -0.03938 -0.02478 90  PHE   A CB    
725  C  CG    . PHE   A 91  ? 0.14322 0.24449 0.18186 0.03388  -0.02238 -0.00070 90  PHE   A CG    
726  C  CD1   . PHE   A 91  ? 0.16288 0.27481 0.21246 0.03717  -0.04594 -0.01312 90  PHE   A CD1   
727  C  CD2   . PHE   A 91  ? 0.23158 0.29420 0.22563 0.06416  -0.00486 -0.01424 90  PHE   A CD2   
728  C  CE1   . PHE   A 91  ? 0.16994 0.30815 0.24832 0.04844  -0.04236 0.01056  90  PHE   A CE1   
729  C  CE2   . PHE   A 91  ? 0.29228 0.29689 0.24320 0.07368  -0.01075 0.00917  90  PHE   A CE2   
730  C  CZ    . PHE   A 91  ? 0.27323 0.31408 0.26096 0.04220  -0.02595 0.01382  90  PHE   A CZ    
731  N  N     . GLU   A 92  ? 0.21588 0.26972 0.20319 -0.00983 -0.03247 0.03006  91  GLU   A N     
732  C  CA    . GLU   A 92  ? 0.26230 0.31027 0.27363 -0.03849 -0.06996 0.07823  91  GLU   A CA    
733  C  C     . GLU   A 92  ? 0.25915 0.27975 0.32707 -0.09004 -0.05515 0.06806  91  GLU   A C     
734  O  O     . GLU   A 92  ? 0.39726 0.30138 0.40017 -0.11407 -0.01770 0.06187  91  GLU   A O     
735  C  CB    . GLU   A 92  ? 0.25446 0.37745 0.28132 -0.05895 -0.06028 0.07478  91  GLU   A CB    
736  C  CG    . GLU   A 92  ? 0.36277 0.43467 0.28462 -0.07203 -0.01694 0.07012  91  GLU   A CG    
737  C  CD    . GLU   A 92  ? 0.53618 0.48333 0.38268 -0.09170 0.06909  0.03474  91  GLU   A CD    
738  O  OE1   . GLU   A 92  ? 0.56629 0.49710 0.37941 -0.08248 0.05481  0.04706  91  GLU   A OE1   
739  O  OE2   . GLU   A 92  ? 0.58475 0.51586 0.42585 -0.10285 0.10484  0.00944  91  GLU   A OE2   
740  N  N     . ASP   A 93  ? 0.22108 0.25338 0.33406 -0.00049 -0.09058 0.02732  92  ASP   A N     
741  C  CA    . ASP   A 93  ? 0.26274 0.24278 0.34467 -0.01595 -0.04754 -0.00384 92  ASP   A CA    
742  C  C     . ASP   A 93  ? 0.26180 0.21570 0.34269 -0.03786 -0.04579 0.01803  92  ASP   A C     
743  O  O     . ASP   A 93  ? 0.22741 0.23097 0.36693 -0.03471 -0.06247 0.00727  92  ASP   A O     
744  C  CB    . ASP   A 93  ? 0.25210 0.25003 0.35554 0.06395  0.00625  0.00615  92  ASP   A CB    
745  C  CG    . ASP   A 93  ? 0.27581 0.28853 0.40748 0.03760  0.15917  0.00092  92  ASP   A CG    
746  O  OD1   . ASP   A 93  ? 0.30141 0.28529 0.41916 -0.03001 0.04885  0.01919  92  ASP   A OD1   
747  O  OD2   . ASP   A 93  ? 0.37986 0.31730 0.40593 0.08650  0.15900  0.01491  92  ASP   A OD2   
748  N  N     . ILE   A 94  ? 0.22136 0.20029 0.29035 -0.02307 -0.05498 0.01499  93  ILE   A N     
749  C  CA    . ILE   A 94  ? 0.18471 0.23506 0.22606 -0.00765 0.01217  0.01089  93  ILE   A CA    
750  C  C     . ILE   A 94  ? 0.23561 0.24460 0.16855 -0.00031 -0.00761 0.00512  93  ILE   A C     
751  O  O     . ILE   A 94  ? 0.30446 0.20121 0.13821 -0.02008 -0.04176 -0.03146 93  ILE   A O     
752  C  CB    . ILE   A 94  ? 0.20052 0.23692 0.19718 -0.01655 -0.04289 0.01612  93  ILE   A CB    
753  C  CG1   . ILE   A 94  ? 0.20777 0.24201 0.18112 -0.01290 -0.01915 -0.00932 93  ILE   A CG1   
754  C  CG2   . ILE   A 94  ? 0.26111 0.24916 0.20038 0.01086  -0.05332 -0.03212 93  ILE   A CG2   
755  C  CD1   . ILE   A 94  ? 0.21939 0.27312 0.19122 -0.01911 0.01570  0.00160  93  ILE   A CD1   
756  N  N     . HIS   A 95  ? 0.22369 0.28667 0.15859 -0.02733 -0.01091 0.00059  94  HIS   A N     
757  C  CA    . HIS   A 95  ? 0.22631 0.33709 0.16894 -0.05378 -0.04987 0.01639  94  HIS   A CA    
758  C  C     . HIS   A 95  ? 0.22851 0.33057 0.18062 -0.05647 -0.06674 0.01494  94  HIS   A C     
759  O  O     . HIS   A 95  ? 0.25070 0.36484 0.18674 -0.04698 -0.06328 0.00400  94  HIS   A O     
760  C  CB    . HIS   A 95  ? 0.28850 0.40581 0.23652 -0.07585 -0.01848 0.05322  94  HIS   A CB    
761  C  CG    . HIS   A 95  ? 0.41171 0.45641 0.24813 -0.11683 0.00800  0.08091  94  HIS   A CG    
762  N  ND1   . HIS   A 95  ? 0.44024 0.49179 0.28511 -0.14010 0.01594  0.06727  94  HIS   A ND1   
763  C  CD2   . HIS   A 95  ? 0.44364 0.48295 0.27153 -0.12685 -0.03952 0.09345  94  HIS   A CD2   
764  C  CE1   . HIS   A 95  ? 0.48774 0.50265 0.28165 -0.14257 0.04881  0.10415  94  HIS   A CE1   
765  N  NE2   . HIS   A 95  ? 0.50936 0.49526 0.28426 -0.11620 -0.03351 0.10385  94  HIS   A NE2   
766  N  N     . HIS   A 96  ? 0.23824 0.28527 0.17603 -0.04329 -0.01724 0.01545  95  HIS   A N     
767  C  CA    . HIS   A 96  ? 0.27643 0.29963 0.17605 -0.06237 -0.03398 0.01975  95  HIS   A CA    
768  C  C     . HIS   A 96  ? 0.23665 0.27010 0.18031 -0.04897 -0.02366 0.01515  95  HIS   A C     
769  O  O     . HIS   A 96  ? 0.26261 0.26205 0.21726 -0.05750 -0.01473 -0.01004 95  HIS   A O     
770  C  CB    . HIS   A 96  ? 0.45752 0.34885 0.21376 -0.04654 -0.06581 0.05784  95  HIS   A CB    
771  C  CG    . HIS   A 96  ? 0.69166 0.43874 0.37615 -0.05703 -0.04642 0.10818  95  HIS   A CG    
772  N  ND1   . HIS   A 96  ? 0.79018 0.47884 0.46494 -0.06969 -0.03572 0.09635  95  HIS   A ND1   
773  C  CD2   . HIS   A 96  ? 0.77357 0.47162 0.40856 -0.07030 -0.01041 0.14410  95  HIS   A CD2   
774  C  CE1   . HIS   A 96  ? 0.83446 0.49250 0.46217 -0.07973 0.00194  0.12075  95  HIS   A CE1   
775  N  NE2   . HIS   A 96  ? 0.83028 0.49777 0.44358 -0.07922 -0.00789 0.13124  95  HIS   A NE2   
776  N  N     . TYR   A 97  ? 0.23794 0.25265 0.19189 -0.03965 0.00433  -0.02303 96  TYR   A N     
777  C  CA    . TYR   A 97  ? 0.23494 0.25296 0.19782 -0.05899 -0.01582 0.00320  96  TYR   A CA    
778  C  C     . TYR   A 97  ? 0.27823 0.24071 0.20132 -0.06361 -0.02723 -0.00105 96  TYR   A C     
779  O  O     . TYR   A 97  ? 0.27127 0.26219 0.19751 -0.07282 -0.03232 -0.00650 96  TYR   A O     
780  C  CB    . TYR   A 97  ? 0.23700 0.28387 0.22298 -0.06393 0.04473  -0.02748 96  TYR   A CB    
781  C  CG    . TYR   A 97  ? 0.22680 0.29493 0.24813 -0.09100 0.05927  -0.06011 96  TYR   A CG    
782  C  CD1   . TYR   A 97  ? 0.29094 0.27802 0.28230 -0.09190 0.06294  -0.05652 96  TYR   A CD1   
783  C  CD2   . TYR   A 97  ? 0.25117 0.34991 0.27646 -0.07168 0.04192  -0.07123 96  TYR   A CD2   
784  C  CE1   . TYR   A 97  ? 0.25982 0.31366 0.28487 -0.09058 0.04743  -0.06090 96  TYR   A CE1   
785  C  CE2   . TYR   A 97  ? 0.30058 0.37431 0.32681 -0.06586 0.06565  -0.08000 96  TYR   A CE2   
786  C  CZ    . TYR   A 97  ? 0.22539 0.36027 0.34550 -0.08138 0.06930  -0.07422 96  TYR   A CZ    
787  O  OH    . TYR   A 97  ? 0.24647 0.40677 0.38529 -0.04609 0.07510  -0.06776 96  TYR   A OH    
788  N  N     . ARG   A 98  ? 0.25964 0.23207 0.23559 -0.05038 -0.01829 0.01916  97  ARG   A N     
789  C  CA    . ARG   A 98  ? 0.23359 0.21953 0.24226 -0.02905 -0.04717 0.01477  97  ARG   A CA    
790  C  C     . ARG   A 98  ? 0.21191 0.20244 0.22129 -0.03224 -0.01903 -0.00844 97  ARG   A C     
791  O  O     . ARG   A 98  ? 0.28995 0.20924 0.20833 -0.02198 -0.07191 -0.01273 97  ARG   A O     
792  C  CB    . ARG   A 98  ? 0.26897 0.24142 0.29576 -0.04561 -0.05889 -0.02442 97  ARG   A CB    
793  C  CG    . ARG   A 98  ? 0.26409 0.26784 0.32709 -0.01985 -0.03878 -0.04000 97  ARG   A CG    
794  C  CD    . ARG   A 98  ? 0.28912 0.31767 0.33480 0.01094  -0.02956 -0.02093 97  ARG   A CD    
795  N  NE    . ARG   A 98  ? 0.27845 0.35750 0.37023 0.04282  -0.08192 -0.00916 97  ARG   A NE    
796  C  CZ    . ARG   A 98  ? 0.29219 0.40326 0.43584 0.05580  -0.01868 -0.01163 97  ARG   A CZ    
797  N  NH1   . ARG   A 98  ? 0.34525 0.42354 0.46505 0.06096  -0.05430 -0.00368 97  ARG   A NH1   
798  N  NH2   . ARG   A 98  ? 0.28619 0.43151 0.46604 0.07904  0.00487  -0.00597 97  ARG   A NH2   
799  N  N     . GLU   A 99  ? 0.19590 0.22473 0.21560 -0.03954 -0.02289 0.01103  98  GLU   A N     
800  C  CA    . GLU   A 99  ? 0.23267 0.26363 0.18722 -0.04591 -0.03001 0.00898  98  GLU   A CA    
801  C  C     . GLU   A 99  ? 0.23149 0.25722 0.16028 -0.03973 -0.05989 -0.00290 98  GLU   A C     
802  O  O     . GLU   A 99  ? 0.17979 0.26043 0.20928 -0.05703 -0.04209 -0.00961 98  GLU   A O     
803  C  CB    . GLU   A 99  ? 0.28083 0.31702 0.16957 -0.08011 -0.02495 -0.00310 98  GLU   A CB    
804  C  CG    . GLU   A 99  ? 0.33647 0.38655 0.19202 -0.06125 0.01476  -0.03598 98  GLU   A CG    
805  C  CD    . GLU   A 99  ? 0.56522 0.45553 0.24784 -0.09829 0.02569  -0.03532 98  GLU   A CD    
806  O  OE1   . GLU   A 99  ? 0.72318 0.49424 0.23322 -0.10510 -0.00738 -0.02745 98  GLU   A OE1   
807  O  OE2   . GLU   A 99  ? 0.60472 0.48623 0.26919 -0.09471 0.03076  -0.02486 98  GLU   A OE2   
808  N  N     . GLN   A 100 ? 0.19749 0.25279 0.17918 -0.02204 -0.02192 0.00977  99  GLN   A N     
809  C  CA    A GLN   A 100 ? 0.21676 0.24767 0.21313 -0.01764 -0.05839 0.00609  99  GLN   A CA    
810  C  CA    B GLN   A 100 ? 0.19281 0.24609 0.16754 -0.03619 -0.02152 0.00754  99  GLN   A CA    
811  C  C     . GLN   A 100 ? 0.18306 0.23509 0.18539 -0.01846 -0.04042 0.01519  99  GLN   A C     
812  O  O     . GLN   A 100 ? 0.15357 0.23160 0.18841 -0.03060 -0.02328 -0.02294 99  GLN   A O     
813  C  CB    A GLN   A 100 ? 0.25185 0.25863 0.29718 -0.01661 -0.08056 -0.00748 99  GLN   A CB    
814  C  CB    B GLN   A 100 ? 0.17199 0.25738 0.18688 -0.05670 -0.01425 -0.01343 99  GLN   A CB    
815  C  CG    A GLN   A 100 ? 0.30735 0.28319 0.36925 0.01058  -0.08581 0.01914  99  GLN   A CG    
816  C  CG    B GLN   A 100 ? 0.15543 0.27296 0.20989 -0.01461 -0.01380 -0.01646 99  GLN   A CG    
817  C  CD    A GLN   A 100 ? 0.36978 0.32247 0.44257 0.03357  -0.04434 0.06816  99  GLN   A CD    
818  C  CD    B GLN   A 100 ? 0.21071 0.29452 0.24454 -0.01244 -0.03976 0.00966  99  GLN   A CD    
819  O  OE1   A GLN   A 100 ? 0.42315 0.32077 0.45404 0.04814  -0.00529 0.06173  99  GLN   A OE1   
820  O  OE1   B GLN   A 100 ? 0.19965 0.31375 0.24531 -0.03146 0.00402  0.02057  99  GLN   A OE1   
821  N  NE2   A GLN   A 100 ? 0.28816 0.35291 0.47328 0.06280  -0.09139 0.09898  99  GLN   A NE2   
822  N  NE2   B GLN   A 100 ? 0.24180 0.28828 0.26890 -0.02971 -0.04201 0.04313  99  GLN   A NE2   
823  N  N     . ILE   A 101 ? 0.19715 0.22560 0.18284 -0.02223 -0.02639 0.00546  100 ILE   A N     
824  C  CA    . ILE   A 101 ? 0.19373 0.22335 0.15753 -0.03379 0.00447  -0.00997 100 ILE   A CA    
825  C  C     . ILE   A 101 ? 0.14285 0.22372 0.14465 -0.01659 -0.00087 -0.00695 100 ILE   A C     
826  O  O     . ILE   A 101 ? 0.17493 0.24154 0.18693 -0.03452 0.00789  -0.03041 100 ILE   A O     
827  C  CB    . ILE   A 101 ? 0.18910 0.21571 0.18808 -0.05050 -0.03337 0.00922  100 ILE   A CB    
828  C  CG1   . ILE   A 101 ? 0.24680 0.21005 0.18494 -0.07193 0.01362  -0.01388 100 ILE   A CG1   
829  C  CG2   . ILE   A 101 ? 0.28928 0.23898 0.18707 -0.05112 -0.06016 0.02368  100 ILE   A CG2   
830  C  CD1   . ILE   A 101 ? 0.22144 0.22524 0.18192 -0.05026 0.01154  -0.00570 100 ILE   A CD1   
831  N  N     . LYS   A 102 ? 0.18044 0.20593 0.18620 -0.01543 -0.00369 -0.01268 101 LYS   A N     
832  C  CA    . LYS   A 102 ? 0.15026 0.20365 0.21097 -0.01338 0.00325  -0.00939 101 LYS   A CA    
833  C  C     . LYS   A 102 ? 0.13869 0.18044 0.21033 -0.00191 -0.00465 -0.00834 101 LYS   A C     
834  O  O     . LYS   A 102 ? 0.15571 0.19354 0.19385 -0.01353 -0.00902 -0.00766 101 LYS   A O     
835  C  CB    . LYS   A 102 ? 0.21820 0.22212 0.21975 0.01676  0.02174  -0.08347 101 LYS   A CB    
836  C  CG    . LYS   A 102 ? 0.26264 0.24406 0.29962 0.00274  0.00406  -0.09724 101 LYS   A CG    
837  C  CD    . LYS   A 102 ? 0.29860 0.28186 0.39983 0.03176  0.02756  -0.07083 101 LYS   A CD    
838  C  CE    . LYS   A 102 ? 0.39023 0.29163 0.45383 0.01845  0.11284  -0.09140 101 LYS   A CE    
839  N  NZ    . LYS   A 102 ? 0.48311 0.29108 0.47346 0.01670  0.13148  -0.10650 101 LYS   A NZ    
840  N  N     . ARG   A 103 ? 0.14441 0.18711 0.20709 -0.00950 -0.00598 -0.00177 102 ARG   A N     
841  C  CA    . ARG   A 103 ? 0.21263 0.18827 0.23931 0.00960  -0.00770 -0.01175 102 ARG   A CA    
842  C  C     . ARG   A 103 ? 0.12851 0.20784 0.24462 -0.01862 -0.00559 -0.00846 102 ARG   A C     
843  O  O     . ARG   A 103 ? 0.15483 0.21777 0.23203 -0.01146 0.00689  -0.02196 102 ARG   A O     
844  C  CB    . ARG   A 103 ? 0.29937 0.19426 0.23123 -0.00034 -0.05098 -0.00821 102 ARG   A CB    
845  C  CG    . ARG   A 103 ? 0.40280 0.23776 0.24787 -0.01882 -0.06924 0.01897  102 ARG   A CG    
846  C  CD    . ARG   A 103 ? 0.41519 0.27097 0.25573 -0.02995 -0.10547 0.04359  102 ARG   A CD    
847  N  NE    . ARG   A 103 ? 0.38958 0.31537 0.27651 -0.07644 -0.07530 0.03245  102 ARG   A NE    
848  C  CZ    . ARG   A 103 ? 0.34748 0.34491 0.30701 -0.09472 -0.02285 0.04151  102 ARG   A CZ    
849  N  NH1   . ARG   A 103 ? 0.40369 0.36817 0.28916 -0.03836 -0.02917 0.07670  102 ARG   A NH1   
850  N  NH2   . ARG   A 103 ? 0.24624 0.33819 0.30387 -0.04036 -0.01336 0.02024  102 ARG   A NH2   
851  N  N     . VAL   A 104 ? 0.15925 0.24155 0.26043 0.00510  -0.00201 -0.03478 103 VAL   A N     
852  C  CA    . VAL   A 104 ? 0.11477 0.29559 0.26843 -0.02387 0.01589  -0.07059 103 VAL   A CA    
853  C  C     . VAL   A 104 ? 0.14909 0.30954 0.24654 -0.02485 0.06480  -0.10904 103 VAL   A C     
854  O  O     . VAL   A 104 ? 0.16160 0.35973 0.27316 -0.06009 0.05173  -0.12650 103 VAL   A O     
855  C  CB    . VAL   A 104 ? 0.13899 0.28386 0.30400 -0.03718 0.05318  -0.10231 103 VAL   A CB    
856  C  CG1   . VAL   A 104 ? 0.17125 0.28899 0.37599 -0.04194 0.10422  -0.11736 103 VAL   A CG1   
857  C  CG2   . VAL   A 104 ? 0.18456 0.29925 0.31994 -0.00334 -0.01317 -0.07644 103 VAL   A CG2   
858  N  N     . LYS   A 105 ? 0.14475 0.31624 0.21749 -0.03686 0.00605  -0.07059 104 LYS   A N     
859  C  CA    . LYS   A 105 ? 0.18380 0.29733 0.18681 -0.05195 0.04343  -0.03767 104 LYS   A CA    
860  C  C     . LYS   A 105 ? 0.16699 0.30206 0.18434 -0.02806 0.01886  -0.03245 104 LYS   A C     
861  O  O     . LYS   A 105 ? 0.19040 0.30739 0.23479 -0.03116 0.01076  -0.00706 104 LYS   A O     
862  C  CB    . LYS   A 105 ? 0.21689 0.28589 0.25828 -0.04863 0.00112  0.00062  104 LYS   A CB    
863  C  CG    . LYS   A 105 ? 0.19864 0.25152 0.26724 -0.04082 0.04311  -0.04584 104 LYS   A CG    
864  C  CD    . LYS   A 105 ? 0.21716 0.22151 0.24092 -0.03641 0.01013  -0.01449 104 LYS   A CD    
865  C  CE    . LYS   A 105 ? 0.20829 0.21875 0.18233 -0.02934 -0.01276 -0.01410 104 LYS   A CE    
866  N  NZ    . LYS   A 105 ? 0.16977 0.23814 0.20535 -0.00189 -0.03598 -0.02023 104 LYS   A NZ    
867  N  N     . ASP   A 106 ? 0.15262 0.27304 0.17654 -0.04674 0.02214  -0.04203 105 ASP   A N     
868  C  CA    . ASP   A 106 ? 0.13669 0.24420 0.16764 -0.03698 -0.00744 -0.06226 105 ASP   A CA    
869  C  C     . ASP   A 106 ? 0.17923 0.21926 0.21070 -0.03198 0.01498  -0.03099 105 ASP   A C     
870  O  O     . ASP   A 106 ? 0.20209 0.22339 0.25677 -0.04070 -0.00348 0.02153  105 ASP   A O     
871  C  CB    . ASP   A 106 ? 0.16569 0.25448 0.20586 -0.02945 0.01329  -0.03415 105 ASP   A CB    
872  C  CG    . ASP   A 106 ? 0.18363 0.24598 0.19223 -0.03790 -0.01800 -0.00101 105 ASP   A CG    
873  O  OD1   . ASP   A 106 ? 0.18769 0.23397 0.19760 -0.02981 0.01566  -0.03506 105 ASP   A OD1   
874  O  OD2   . ASP   A 106 ? 0.20103 0.27488 0.19255 -0.05067 -0.02277 -0.01906 105 ASP   A OD2   
875  N  N     . SER   A 107 ? 0.18107 0.21120 0.20180 -0.03157 0.02631  -0.00817 106 SER   A N     
876  C  CA    . SER   A 107 ? 0.26245 0.19770 0.28470 -0.03684 0.00064  -0.01469 106 SER   A CA    
877  C  C     . SER   A 107 ? 0.23681 0.19701 0.31558 0.01210  0.04906  -0.04640 106 SER   A C     
878  O  O     . SER   A 107 ? 0.27757 0.20432 0.30609 -0.00800 -0.03335 -0.01259 106 SER   A O     
879  C  CB    . SER   A 107 ? 0.44242 0.20469 0.33807 -0.05911 -0.02641 0.02050  106 SER   A CB    
880  O  OG    . SER   A 107 ? 0.55217 0.23809 0.37822 -0.05133 -0.06329 0.02160  106 SER   A OG    
881  N  N     . GLU   A 108 ? 0.26964 0.22455 0.39632 -0.00545 0.10291  -0.03416 107 GLU   A N     
882  C  CA    . GLU   A 108 ? 0.36713 0.26541 0.46766 0.01107  0.16184  -0.07137 107 GLU   A CA    
883  C  C     . GLU   A 108 ? 0.28425 0.23487 0.49166 0.01395  0.11654  -0.08904 107 GLU   A C     
884  O  O     . GLU   A 108 ? 0.37360 0.25974 0.51629 -0.01093 0.06628  -0.09900 107 GLU   A O     
885  C  CB    . GLU   A 108 ? 0.43163 0.31060 0.53169 -0.02595 0.18940  -0.07423 107 GLU   A CB    
886  C  CG    . GLU   A 108 ? 0.46536 0.32787 0.58358 -0.07058 0.18078  -0.07169 107 GLU   A CG    
887  C  CD    . GLU   A 108 ? 0.57421 0.36738 0.65009 -0.06480 0.12354  -0.06893 107 GLU   A CD    
888  O  OE1   . GLU   A 108 ? 0.55918 0.36827 0.65911 -0.05220 0.07166  -0.09349 107 GLU   A OE1   
889  O  OE2   . GLU   A 108 ? 0.61093 0.38906 0.67458 -0.06121 0.10879  -0.04993 107 GLU   A OE2   
890  N  N     . ASP   A 109 ? 0.21065 0.23336 0.50312 -0.00296 0.13889  -0.02385 108 ASP   A N     
891  C  CA    . ASP   A 109 ? 0.18703 0.28966 0.56167 0.03145  0.05829  0.00003  108 ASP   A CA    
892  C  C     . ASP   A 109 ? 0.19947 0.31879 0.49296 0.01651  0.03327  -0.01133 108 ASP   A C     
893  O  O     . ASP   A 109 ? 0.20405 0.37912 0.59618 -0.01043 -0.03530 -0.03302 108 ASP   A O     
894  C  CB    . ASP   A 109 ? 0.35943 0.34782 0.67369 0.11041  0.03114  0.04206  108 ASP   A CB    
895  C  CG    . ASP   A 109 ? 0.53668 0.40976 0.78228 0.10793  -0.02707 0.04282  108 ASP   A CG    
896  O  OD1   . ASP   A 109 ? 0.61991 0.42578 0.84904 0.11883  -0.01533 0.05029  108 ASP   A OD1   
897  O  OD2   . ASP   A 109 ? 0.59984 0.43989 0.80047 0.08001  -0.05076 0.03133  108 ASP   A OD2   
898  N  N     . VAL   A 110 ? 0.18222 0.27746 0.34510 -0.02158 0.01185  0.01003  109 VAL   A N     
899  C  CA    . VAL   A 110 ? 0.16335 0.21823 0.26286 -0.01086 0.02197  0.01371  109 VAL   A CA    
900  C  C     . VAL   A 110 ? 0.11157 0.20312 0.19466 -0.00297 -0.02144 -0.01087 109 VAL   A C     
901  O  O     . VAL   A 110 ? 0.15290 0.23448 0.17580 -0.01636 -0.01132 -0.01723 109 VAL   A O     
902  C  CB    . VAL   A 110 ? 0.17153 0.21099 0.25942 -0.02430 0.01639  0.04125  109 VAL   A CB    
903  C  CG1   . VAL   A 110 ? 0.17239 0.20407 0.26734 -0.02080 0.02761  0.02538  109 VAL   A CG1   
904  C  CG2   . VAL   A 110 ? 0.19772 0.24388 0.32279 -0.04256 0.05912  0.03161  109 VAL   A CG2   
905  N  N     . PRO   A 111 ? 0.14200 0.20698 0.19746 -0.00335 -0.00902 -0.02901 110 PRO   A N     
906  C  CA    . PRO   A 111 ? 0.12613 0.22392 0.18949 -0.01444 -0.04397 -0.00167 110 PRO   A CA    
907  C  C     . PRO   A 111 ? 0.11535 0.18396 0.15903 0.02035  -0.00699 -0.00551 110 PRO   A C     
908  O  O     . PRO   A 111 ? 0.13450 0.18194 0.16747 0.02066  -0.01120 -0.03063 110 PRO   A O     
909  C  CB    . PRO   A 111 ? 0.13847 0.25270 0.15826 0.02138  -0.05266 0.01514  110 PRO   A CB    
910  C  CG    . PRO   A 111 ? 0.16803 0.23987 0.17221 -0.00354 -0.03841 0.01270  110 PRO   A CG    
911  C  CD    . PRO   A 111 ? 0.14612 0.23508 0.17587 -0.01944 -0.03722 -0.00167 110 PRO   A CD    
912  N  N     . MET   A 112 ? 0.12208 0.21291 0.17074 -0.00445 -0.01968 -0.03035 111 MET   A N     
913  C  CA    . MET   A 112 ? 0.14847 0.18390 0.19204 -0.02118 -0.04737 -0.00143 111 MET   A CA    
914  C  C     . MET   A 112 ? 0.17586 0.16801 0.17233 0.02164  -0.04717 -0.00908 111 MET   A C     
915  O  O     . MET   A 112 ? 0.16958 0.17016 0.21763 0.01184  -0.04456 -0.02855 111 MET   A O     
916  C  CB    . MET   A 112 ? 0.34070 0.24102 0.32040 -0.09437 0.00744  0.04731  111 MET   A CB    
917  C  CG    . MET   A 112 ? 0.40470 0.30317 0.34153 -0.03576 -0.04963 0.03378  111 MET   A CG    
918  S  SD    . MET   A 112 ? 0.39298 0.34880 0.24075 0.01429  0.06791  0.06538  111 MET   A SD    
919  C  CE    . MET   A 112 ? 0.43031 0.33285 0.26709 0.03436  -0.00229 0.09186  111 MET   A CE    
920  N  N     . VAL   A 113 ? 0.15977 0.15801 0.16603 0.00881  -0.04975 -0.01604 112 VAL   A N     
921  C  CA    . VAL   A 113 ? 0.16522 0.14781 0.13234 0.00935  -0.03128 -0.00229 112 VAL   A CA    
922  C  C     . VAL   A 113 ? 0.17768 0.14980 0.16581 0.03306  -0.04345 -0.02306 112 VAL   A C     
923  O  O     . VAL   A 113 ? 0.17046 0.16161 0.17117 0.02791  -0.03192 -0.02323 112 VAL   A O     
924  C  CB    . VAL   A 113 ? 0.20930 0.17104 0.15754 -0.01157 -0.03816 0.01530  112 VAL   A CB    
925  C  CG1   . VAL   A 113 ? 0.21935 0.18953 0.24987 -0.00094 -0.01779 0.01821  112 VAL   A CG1   
926  C  CG2   . VAL   A 113 ? 0.23450 0.19527 0.15677 0.00006  -0.05183 -0.00096 112 VAL   A CG2   
927  N  N     . LEU   A 114 ? 0.15713 0.18181 0.17010 0.02369  -0.06435 -0.02582 113 LEU   A N     
928  C  CA    . LEU   A 114 ? 0.19338 0.19836 0.14610 0.02448  -0.03118 -0.02489 113 LEU   A CA    
929  C  C     . LEU   A 114 ? 0.18805 0.18400 0.15766 0.03437  -0.04501 -0.03088 113 LEU   A C     
930  O  O     . LEU   A 114 ? 0.17769 0.17258 0.19891 0.02165  -0.05418 -0.04094 113 LEU   A O     
931  C  CB    . LEU   A 114 ? 0.19714 0.23424 0.13745 0.03355  -0.02841 -0.02878 113 LEU   A CB    
932  C  CG    . LEU   A 114 ? 0.22823 0.20137 0.15852 0.01888  -0.04882 -0.03425 113 LEU   A CG    
933  C  CD1   . LEU   A 114 ? 0.24514 0.20665 0.22182 0.02138  -0.06444 0.00075  113 LEU   A CD1   
934  C  CD2   . LEU   A 114 ? 0.29913 0.21730 0.13822 0.04850  0.00330  -0.02200 113 LEU   A CD2   
935  N  N     . VAL   A 115 ? 0.17333 0.15762 0.16484 0.00467  -0.04850 -0.00395 114 VAL   A N     
936  C  CA    . VAL   A 115 ? 0.18050 0.14355 0.15539 0.00401  -0.04482 -0.03102 114 VAL   A CA    
937  C  C     . VAL   A 115 ? 0.19341 0.15545 0.17833 0.01319  -0.04484 -0.02192 114 VAL   A C     
938  O  O     . VAL   A 115 ? 0.19770 0.17665 0.21682 0.02127  -0.08338 -0.01262 114 VAL   A O     
939  C  CB    . VAL   A 115 ? 0.16346 0.20482 0.15354 -0.01147 -0.02226 -0.00684 114 VAL   A CB    
940  C  CG1   . VAL   A 115 ? 0.16115 0.23283 0.23205 -0.02188 -0.00518 -0.00567 114 VAL   A CG1   
941  C  CG2   . VAL   A 115 ? 0.19271 0.25892 0.15598 0.02955  -0.05948 -0.02886 114 VAL   A CG2   
942  N  N     . GLY   A 116 ? 0.17267 0.20028 0.18474 0.01500  -0.06345 -0.02271 115 GLY   A N     
943  C  CA    . GLY   A 116 ? 0.15465 0.20308 0.20122 -0.00061 -0.04173 -0.03470 115 GLY   A CA    
944  C  C     . GLY   A 116 ? 0.17562 0.19626 0.18425 -0.00924 -0.04235 -0.02673 115 GLY   A C     
945  O  O     . GLY   A 116 ? 0.22494 0.19992 0.23762 -0.01922 -0.04346 -0.02421 115 GLY   A O     
946  N  N     . ASN   A 117 ? 0.17974 0.19931 0.21831 -0.00143 -0.08108 -0.00517 116 ASN   A N     
947  C  CA    . ASN   A 117 ? 0.19269 0.18906 0.23604 -0.01122 -0.06314 -0.03859 116 ASN   A CA    
948  C  C     . ASN   A 117 ? 0.18827 0.19390 0.24266 -0.00460 -0.07604 -0.02516 116 ASN   A C     
949  O  O     . ASN   A 117 ? 0.20730 0.21507 0.20850 -0.01326 -0.04808 -0.02182 116 ASN   A O     
950  C  CB    . ASN   A 117 ? 0.18857 0.18981 0.16722 -0.01476 -0.04295 -0.01010 116 ASN   A CB    
951  C  CG    . ASN   A 117 ? 0.16877 0.19346 0.18078 -0.03452 -0.01814 -0.02132 116 ASN   A CG    
952  O  OD1   . ASN   A 117 ? 0.21146 0.19284 0.18349 -0.03375 -0.04831 -0.01427 116 ASN   A OD1   
953  N  ND2   . ASN   A 117 ? 0.22244 0.19519 0.20213 -0.02708 -0.03018 -0.02745 116 ASN   A ND2   
954  N  N     . LYS   A 118 ? 0.20202 0.18891 0.25215 -0.02168 -0.07215 -0.02773 117 LYS   A N     
955  C  CA    . LYS   A 118 ? 0.22451 0.19345 0.25989 -0.01338 -0.08861 -0.02408 117 LYS   A CA    
956  C  C     . LYS   A 118 ? 0.24303 0.21000 0.22592 -0.01595 -0.08813 -0.02692 117 LYS   A C     
957  O  O     . LYS   A 118 ? 0.26757 0.20274 0.22890 -0.02384 -0.08939 -0.02306 117 LYS   A O     
958  C  CB    . LYS   A 118 ? 0.22879 0.19223 0.25613 -0.00085 -0.06908 -0.03092 117 LYS   A CB    
959  C  CG    . LYS   A 118 ? 0.22495 0.15901 0.25114 0.01437  -0.07143 -0.00402 117 LYS   A CG    
960  C  CD    . LYS   A 118 ? 0.18513 0.16653 0.28512 -0.00453 -0.07836 0.00935  117 LYS   A CD    
961  C  CE    . LYS   A 118 ? 0.17024 0.17017 0.26227 0.02103  -0.06145 -0.00298 117 LYS   A CE    
962  N  NZ    . LYS   A 118 ? 0.16284 0.21654 0.29539 0.00084  -0.05842 -0.00642 117 LYS   A NZ    
963  N  N     . CYS   A 119 ? 0.25209 0.22422 0.20948 -0.00632 -0.07222 -0.02349 118 CYS   A N     
964  C  CA    A CYS   A 119 ? 0.26190 0.21351 0.23436 0.00681  -0.07882 -0.01251 118 CYS   A CA    
965  C  CA    B CYS   A 119 ? 0.24851 0.22966 0.23700 -0.00666 -0.07786 -0.01487 118 CYS   A CA    
966  C  C     . CYS   A 119 ? 0.30145 0.21537 0.22521 -0.02254 -0.07475 -0.00713 118 CYS   A C     
967  O  O     . CYS   A 119 ? 0.37602 0.21184 0.23548 -0.04464 -0.05417 -0.03919 118 CYS   A O     
968  C  CB    A CYS   A 119 ? 0.32526 0.22265 0.25911 0.02578  -0.10381 -0.02154 118 CYS   A CB    
969  C  CB    B CYS   A 119 ? 0.28770 0.26203 0.26645 -0.00295 -0.10684 -0.03298 118 CYS   A CB    
970  S  SG    A CYS   A 119 ? 0.38876 0.22798 0.27020 0.05077  -0.11188 -0.02308 118 CYS   A SG    
971  S  SG    B CYS   A 119 ? 0.31232 0.27543 0.28963 -0.00204 -0.09255 -0.04190 118 CYS   A SG    
972  N  N     . ASP   A 120 ? 0.33578 0.20219 0.25863 -0.04613 -0.08101 -0.00480 119 ASP   A N     
973  C  CA    . ASP   A 120 ? 0.31558 0.19957 0.28760 -0.03954 -0.05328 -0.01214 119 ASP   A CA    
974  C  C     . ASP   A 120 ? 0.34595 0.20079 0.29756 -0.03259 -0.09468 -0.03433 119 ASP   A C     
975  O  O     . ASP   A 120 ? 0.35246 0.21575 0.30859 -0.03510 -0.13528 -0.01133 119 ASP   A O     
976  C  CB    . ASP   A 120 ? 0.28020 0.20807 0.33271 -0.04186 -0.03530 -0.01842 119 ASP   A CB    
977  C  CG    . ASP   A 120 ? 0.20466 0.22736 0.31773 -0.04989 -0.06512 0.01016  119 ASP   A CG    
978  O  OD1   . ASP   A 120 ? 0.24266 0.22159 0.30456 -0.03524 -0.09978 -0.00987 119 ASP   A OD1   
979  O  OD2   . ASP   A 120 ? 0.20280 0.27087 0.36446 -0.04203 -0.04714 -0.02382 119 ASP   A OD2   
980  N  N     . LEU   A 121 ? 0.30013 0.22198 0.31198 -0.02620 -0.15119 -0.04115 120 LEU   A N     
981  C  CA    . LEU   A 121 ? 0.30230 0.22067 0.31296 -0.02068 -0.10682 -0.01188 120 LEU   A CA    
982  C  C     . LEU   A 121 ? 0.31852 0.23973 0.31350 -0.00867 -0.09816 -0.02110 120 LEU   A C     
983  O  O     . LEU   A 121 ? 0.36598 0.27306 0.34814 -0.00685 -0.11526 -0.01440 120 LEU   A O     
984  C  CB    . LEU   A 121 ? 0.31360 0.21176 0.30587 -0.04715 -0.11663 -0.00286 120 LEU   A CB    
985  C  CG    . LEU   A 121 ? 0.30206 0.24467 0.35058 0.00148  -0.13608 -0.00802 120 LEU   A CG    
986  C  CD1   . LEU   A 121 ? 0.34177 0.23995 0.35855 -0.00385 -0.16174 -0.01546 120 LEU   A CD1   
987  C  CD2   . LEU   A 121 ? 0.27520 0.26549 0.38776 -0.05553 -0.09186 -0.02113 120 LEU   A CD2   
988  N  N     . PRO   A 122 ? 0.29752 0.26053 0.28813 -0.01091 -0.13506 -0.03675 121 PRO   A N     
989  C  CA    . PRO   A 122 ? 0.35947 0.26698 0.28617 -0.02238 -0.11605 -0.04855 121 PRO   A CA    
990  C  C     . PRO   A 122 ? 0.31349 0.28384 0.30539 -0.02498 -0.12919 -0.02119 121 PRO   A C     
991  O  O     . PRO   A 122 ? 0.33293 0.32091 0.30859 -0.00866 -0.11537 0.00845  121 PRO   A O     
992  C  CB    . PRO   A 122 ? 0.36593 0.26905 0.27874 -0.01981 -0.07134 -0.02108 121 PRO   A CB    
993  C  CG    . PRO   A 122 ? 0.29233 0.29654 0.26326 -0.03366 -0.15022 -0.02726 121 PRO   A CG    
994  C  CD    . PRO   A 122 ? 0.23847 0.27638 0.27877 -0.04145 -0.10987 -0.02317 121 PRO   A CD    
995  N  N     . SER   A 123 ? 0.28783 0.25470 0.28996 -0.01371 -0.11985 0.00619  122 SER   A N     
996  C  CA    . SER   A 123 ? 0.29133 0.26438 0.29862 -0.01107 -0.09230 0.02003  122 SER   A CA    
997  C  C     . SER   A 123 ? 0.27472 0.23398 0.27579 -0.01954 -0.15403 -0.00904 122 SER   A C     
998  O  O     . SER   A 123 ? 0.29205 0.21597 0.25485 -0.02000 -0.09599 -0.01384 122 SER   A O     
999  C  CB    . SER   A 123 ? 0.25717 0.28667 0.33115 -0.01239 -0.12750 -0.00413 122 SER   A CB    
1000 O  OG    . SER   A 123 ? 0.24802 0.29013 0.34119 -0.01448 -0.11566 -0.00674 122 SER   A OG    
1001 N  N     . ARG   A 124 ? 0.24472 0.24252 0.27035 -0.02350 -0.10109 -0.00738 123 ARG   A N     
1002 C  CA    . ARG   A 124 ? 0.27667 0.25802 0.25509 -0.01583 -0.09531 -0.00858 123 ARG   A CA    
1003 C  C     . ARG   A 124 ? 0.28008 0.25793 0.23135 -0.04394 -0.09306 -0.03099 123 ARG   A C     
1004 O  O     . ARG   A 124 ? 0.32770 0.29026 0.23732 -0.06099 -0.10569 -0.04986 123 ARG   A O     
1005 C  CB    . ARG   A 124 ? 0.29443 0.24365 0.30232 0.02955  -0.14415 -0.01211 123 ARG   A CB    
1006 C  CG    . ARG   A 124 ? 0.32809 0.22870 0.35970 0.03811  -0.16946 -0.01015 123 ARG   A CG    
1007 C  CD    . ARG   A 124 ? 0.37607 0.24133 0.35435 0.04152  -0.16700 -0.01680 123 ARG   A CD    
1008 N  NE    . ARG   A 124 ? 0.37877 0.27796 0.36102 -0.00049 -0.17115 -0.02178 123 ARG   A NE    
1009 C  CZ    . ARG   A 124 ? 0.39318 0.28351 0.34025 0.02949  -0.14172 -0.00829 123 ARG   A CZ    
1010 N  NH1   . ARG   A 124 ? 0.37399 0.27034 0.33480 0.03535  -0.10249 -0.05719 123 ARG   A NH1   
1011 N  NH2   . ARG   A 124 ? 0.43506 0.29776 0.34715 0.04587  -0.14244 0.03012  123 ARG   A NH2   
1012 N  N     . THR   A 125 ? 0.20088 0.22126 0.23137 -0.01963 -0.06560 -0.01260 124 THR   A N     
1013 C  CA    . THR   A 125 ? 0.22251 0.25356 0.20828 -0.02858 -0.03958 -0.05074 124 THR   A CA    
1014 C  C     . THR   A 125 ? 0.26567 0.30947 0.17716 0.02859  -0.03836 -0.03962 124 THR   A C     
1015 O  O     . THR   A 125 ? 0.26958 0.33824 0.23307 0.03620  -0.04766 -0.05822 124 THR   A O     
1016 C  CB    . THR   A 125 ? 0.24513 0.27142 0.21729 0.02160  -0.06512 -0.04646 124 THR   A CB    
1017 O  OG1   . THR   A 125 ? 0.26168 0.27129 0.20236 0.02395  -0.06655 -0.03434 124 THR   A OG1   
1018 C  CG2   . THR   A 125 ? 0.18773 0.27357 0.26468 -0.00029 -0.06910 -0.00126 124 THR   A CG2   
1019 N  N     . VAL   A 126 ? 0.27888 0.29520 0.17422 0.05959  -0.09511 -0.04836 125 VAL   A N     
1020 C  CA    . VAL   A 126 ? 0.25374 0.27530 0.19698 0.07653  -0.06308 -0.05799 125 VAL   A CA    
1021 C  C     . VAL   A 126 ? 0.29829 0.27768 0.24372 0.07393  -0.10135 -0.09859 125 VAL   A C     
1022 O  O     . VAL   A 126 ? 0.29673 0.25628 0.28300 0.02707  -0.11505 -0.04770 125 VAL   A O     
1023 C  CB    . VAL   A 126 ? 0.24120 0.24276 0.20311 0.03337  -0.09454 -0.05247 125 VAL   A CB    
1024 C  CG1   . VAL   A 126 ? 0.28133 0.25536 0.25450 0.06013  -0.12276 -0.04363 125 VAL   A CG1   
1025 C  CG2   . VAL   A 126 ? 0.26693 0.26041 0.25076 0.01486  -0.08486 -0.04052 125 VAL   A CG2   
1026 N  N     . ASP   A 127 ? 0.37324 0.33242 0.27865 0.12890  -0.15648 -0.13148 126 ASP   A N     
1027 C  CA    . ASP   A 127 ? 0.43997 0.36638 0.31371 0.15794  -0.14842 -0.16403 126 ASP   A CA    
1028 C  C     . ASP   A 127 ? 0.46400 0.31754 0.31076 0.15635  -0.13563 -0.14591 126 ASP   A C     
1029 O  O     . ASP   A 127 ? 0.41934 0.28082 0.32572 0.13200  -0.16169 -0.14086 126 ASP   A O     
1030 C  CB    . ASP   A 127 ? 0.62129 0.45981 0.39158 0.16642  -0.11336 -0.21342 126 ASP   A CB    
1031 C  CG    . ASP   A 127 ? 0.83415 0.55687 0.54369 0.14881  -0.07364 -0.20697 126 ASP   A CG    
1032 O  OD1   . ASP   A 127 ? 0.99300 0.59849 0.63143 0.13731  -0.05976 -0.20976 126 ASP   A OD1   
1033 O  OD2   . ASP   A 127 ? 0.84596 0.60787 0.56654 0.13109  -0.07298 -0.20455 126 ASP   A OD2   
1034 N  N     . THR   A 128 ? 0.44774 0.29844 0.30508 0.15869  -0.07875 -0.12952 127 THR   A N     
1035 C  CA    . THR   A 128 ? 0.37255 0.29712 0.30523 0.09655  -0.13675 -0.06688 127 THR   A CA    
1036 C  C     . THR   A 128 ? 0.40931 0.27947 0.29173 0.11237  -0.11832 -0.06022 127 THR   A C     
1037 O  O     . THR   A 128 ? 0.34120 0.26252 0.27902 0.08154  -0.13156 -0.04816 127 THR   A O     
1038 C  CB    . THR   A 128 ? 0.36265 0.31937 0.34080 0.07217  -0.11288 -0.05666 127 THR   A CB    
1039 O  OG1   . THR   A 128 ? 0.41449 0.35215 0.38203 0.06424  -0.10872 -0.06349 127 THR   A OG1   
1040 C  CG2   . THR   A 128 ? 0.43512 0.31725 0.34570 0.04177  -0.09077 -0.03411 127 THR   A CG2   
1041 N  N     . LYS   A 129 ? 0.37653 0.29585 0.31049 0.16241  -0.09352 -0.07357 128 LYS   A N     
1042 C  CA    . LYS   A 129 ? 0.41988 0.30733 0.31175 0.16419  -0.09050 -0.09368 128 LYS   A CA    
1043 C  C     . LYS   A 129 ? 0.42767 0.31477 0.24007 0.14079  -0.13569 -0.08947 128 LYS   A C     
1044 O  O     . LYS   A 129 ? 0.43841 0.32173 0.23837 0.13545  -0.11618 -0.09991 128 LYS   A O     
1045 C  CB    . LYS   A 129 ? 0.53802 0.34991 0.39898 0.13015  -0.06502 -0.08276 128 LYS   A CB    
1046 C  CG    . LYS   A 129 ? 0.61044 0.41012 0.53789 0.12487  -0.04071 -0.02653 128 LYS   A CG    
1047 C  CD    . LYS   A 129 ? 0.64590 0.43079 0.64256 0.11635  0.02202  0.01983  128 LYS   A CD    
1048 C  CE    . LYS   A 129 ? 0.63675 0.42403 0.69972 0.14996  0.05912  0.04684  128 LYS   A CE    
1049 N  NZ    . LYS   A 129 ? 0.64810 0.42935 0.72408 0.13639  0.10494  0.04374  128 LYS   A NZ    
1050 N  N     . GLN   A 130 ? 0.48863 0.31485 0.23470 0.15829  -0.12057 -0.07050 129 GLN   A N     
1051 C  CA    A GLN   A 130 ? 0.48126 0.32356 0.24466 0.13247  -0.11933 -0.06097 129 GLN   A CA    
1052 C  CA    B GLN   A 130 ? 0.48191 0.31114 0.25336 0.12736  -0.12649 -0.06422 129 GLN   A CA    
1053 C  C     . GLN   A 130 ? 0.42836 0.31643 0.22977 0.10868  -0.11537 -0.03424 129 GLN   A C     
1054 O  O     . GLN   A 130 ? 0.33853 0.33584 0.22153 0.11045  -0.03741 -0.02738 129 GLN   A O     
1055 C  CB    A GLN   A 130 ? 0.58257 0.34875 0.25496 0.13065  -0.12454 -0.04627 129 GLN   A CB    
1056 C  CB    B GLN   A 130 ? 0.57480 0.31143 0.27761 0.11651  -0.14108 -0.05583 129 GLN   A CB    
1057 C  CG    A GLN   A 130 ? 0.63780 0.37222 0.26677 0.12946  -0.13060 -0.03181 129 GLN   A CG    
1058 C  CG    B GLN   A 130 ? 0.62286 0.30550 0.30921 0.10441  -0.16793 -0.05864 129 GLN   A CG    
1059 C  CD    A GLN   A 130 ? 0.69778 0.39683 0.26031 0.13043  -0.12372 -0.02379 129 GLN   A CD    
1060 C  CD    B GLN   A 130 ? 0.67723 0.32462 0.35568 0.07942  -0.19961 -0.04527 129 GLN   A CD    
1061 O  OE1   A GLN   A 130 ? 0.68570 0.42101 0.24002 0.13183  -0.14406 -0.01136 129 GLN   A OE1   
1062 O  OE1   B GLN   A 130 ? 0.62495 0.33884 0.39955 0.07731  -0.22762 -0.01639 129 GLN   A OE1   
1063 N  NE2   A GLN   A 130 ? 0.71923 0.38884 0.29511 0.16776  -0.09780 -0.03702 129 GLN   A NE2   
1064 N  NE2   B GLN   A 130 ? 0.70903 0.33235 0.36253 0.06689  -0.17655 -0.06165 129 GLN   A NE2   
1065 N  N     . ALA   A 131 ? 0.34796 0.28949 0.20647 0.11344  -0.06654 -0.01043 130 ALA   A N     
1066 C  CA    . ALA   A 131 ? 0.31267 0.27724 0.20357 0.10117  -0.01944 -0.01970 130 ALA   A CA    
1067 C  C     . ALA   A 131 ? 0.23622 0.26884 0.22012 0.09426  -0.06678 -0.02017 130 ALA   A C     
1068 O  O     . ALA   A 131 ? 0.25001 0.27978 0.20413 0.05590  -0.04684 -0.05185 130 ALA   A O     
1069 C  CB    . ALA   A 131 ? 0.27000 0.26617 0.26694 0.08304  -0.02263 0.02095  130 ALA   A CB    
1070 N  N     . GLN   A 132 ? 0.24107 0.28815 0.24733 0.10068  -0.05804 -0.01027 131 GLN   A N     
1071 C  CA    . GLN   A 132 ? 0.18743 0.29909 0.28181 0.10921  -0.05818 -0.03398 131 GLN   A CA    
1072 C  C     . GLN   A 132 ? 0.18656 0.29967 0.24621 0.08130  -0.04688 -0.05554 131 GLN   A C     
1073 O  O     . GLN   A 132 ? 0.27134 0.29164 0.24418 0.09511  -0.04938 -0.05477 131 GLN   A O     
1074 C  CB    . GLN   A 132 ? 0.32879 0.32584 0.34385 0.10271  -0.07657 -0.02988 131 GLN   A CB    
1075 C  CG    . GLN   A 132 ? 0.46192 0.38231 0.44939 0.08839  -0.04685 -0.04157 131 GLN   A CG    
1076 C  CD    . GLN   A 132 ? 0.61036 0.43773 0.53246 0.07557  -0.00421 -0.01380 131 GLN   A CD    
1077 O  OE1   . GLN   A 132 ? 0.66619 0.47502 0.53459 0.08699  0.01020  -0.00762 131 GLN   A OE1   
1078 N  NE2   . GLN   A 132 ? 0.63832 0.44743 0.57305 0.03854  -0.01166 0.00163  131 GLN   A NE2   
1079 N  N     . ASP   A 133 ? 0.26545 0.33109 0.21391 0.09108  -0.01493 -0.04817 132 ASP   A N     
1080 C  CA    . ASP   A 133 ? 0.30764 0.35685 0.19694 0.09865  -0.03463 -0.07046 132 ASP   A CA    
1081 C  C     . ASP   A 133 ? 0.26992 0.35304 0.20818 0.10892  -0.01529 -0.04746 132 ASP   A C     
1082 O  O     . ASP   A 133 ? 0.25835 0.36702 0.21550 0.06773  -0.02171 -0.04060 132 ASP   A O     
1083 C  CB    . ASP   A 133 ? 0.40105 0.39211 0.20164 0.13717  -0.03981 -0.09416 132 ASP   A CB    
1084 C  CG    . ASP   A 133 ? 0.45819 0.44670 0.25902 0.11372  -0.03272 -0.10853 132 ASP   A CG    
1085 O  OD1   . ASP   A 133 ? 0.43230 0.46581 0.34207 0.16657  -0.05755 -0.09565 132 ASP   A OD1   
1086 O  OD2   . ASP   A 133 ? 0.47897 0.48149 0.27974 0.09500  -0.00190 -0.10946 132 ASP   A OD2   
1087 N  N     . LEU   A 134 ? 0.30172 0.33793 0.18690 0.10865  -0.00155 -0.04944 133 LEU   A N     
1088 C  CA    . LEU   A 134 ? 0.25415 0.32248 0.19225 0.08962  -0.02809 -0.02431 133 LEU   A CA    
1089 C  C     . LEU   A 134 ? 0.20328 0.31259 0.14710 0.03185  0.01889  -0.02939 133 LEU   A C     
1090 O  O     . LEU   A 134 ? 0.22153 0.31062 0.23929 0.01516  -0.01507 -0.01743 133 LEU   A O     
1091 C  CB    . LEU   A 134 ? 0.23515 0.30915 0.24350 0.12953  -0.01319 -0.02708 133 LEU   A CB    
1092 C  CG    . LEU   A 134 ? 0.25632 0.30379 0.21436 0.08369  0.03718  -0.00449 133 LEU   A CG    
1093 C  CD1   . LEU   A 134 ? 0.29960 0.31700 0.23313 -0.00604 0.02584  0.03950  133 LEU   A CD1   
1094 C  CD2   . LEU   A 134 ? 0.27866 0.31545 0.22888 0.11487  -0.00142 0.00167  133 LEU   A CD2   
1095 N  N     . ALA   A 135 ? 0.20936 0.32134 0.18555 0.06947  0.00100  -0.02200 134 ALA   A N     
1096 C  CA    . ALA   A 135 ? 0.22007 0.32452 0.16451 0.07388  0.00304  -0.00108 134 ALA   A CA    
1097 C  C     . ALA   A 135 ? 0.19728 0.32522 0.18588 0.05661  0.02509  -0.03064 134 ALA   A C     
1098 O  O     . ALA   A 135 ? 0.17714 0.34721 0.21851 0.02520  -0.01654 -0.01231 134 ALA   A O     
1099 C  CB    . ALA   A 135 ? 0.18614 0.31046 0.18029 0.06012  0.01306  -0.00373 134 ALA   A CB    
1100 N  N     . ARG   A 136 ? 0.23359 0.32468 0.24102 0.09984  -0.00148 0.00270  135 ARG   A N     
1101 C  CA    . ARG   A 136 ? 0.19598 0.33756 0.27654 0.09308  0.00708  -0.04482 135 ARG   A CA    
1102 C  C     . ARG   A 136 ? 0.20736 0.34637 0.25036 0.06952  -0.01937 -0.04715 135 ARG   A C     
1103 O  O     . ARG   A 136 ? 0.20648 0.34476 0.29543 0.04631  -0.01507 -0.04245 135 ARG   A O     
1104 C  CB    . ARG   A 136 ? 0.29472 0.35383 0.31843 0.08243  0.04118  -0.07705 135 ARG   A CB    
1105 C  CG    . ARG   A 136 ? 0.39285 0.34840 0.42403 0.14660  0.07176  -0.10776 135 ARG   A CG    
1106 C  CD    . ARG   A 136 ? 0.51002 0.35812 0.56789 0.21218  0.05085  -0.11379 135 ARG   A CD    
1107 N  NE    . ARG   A 136 ? 0.65311 0.37084 0.69850 0.21984  0.04793  -0.10498 135 ARG   A NE    
1108 C  CZ    . ARG   A 136 ? 0.77992 0.37590 0.80727 0.21493  0.03102  -0.08846 135 ARG   A CZ    
1109 N  NH1   . ARG   A 136 ? 0.84778 0.37081 0.83677 0.19721  0.04121  -0.09580 135 ARG   A NH1   
1110 N  NH2   . ARG   A 136 ? 0.77911 0.38173 0.85052 0.21509  0.02379  -0.05576 135 ARG   A NH2   
1111 N  N     . SER   A 137 ? 0.24089 0.35246 0.21572 0.08262  0.00046  -0.04464 136 SER   A N     
1112 C  CA    . SER   A 137 ? 0.24737 0.37995 0.21342 0.04389  0.03629  -0.01144 136 SER   A CA    
1113 C  C     . SER   A 137 ? 0.21972 0.38200 0.26890 0.02332  0.00951  0.00843  136 SER   A C     
1114 O  O     . SER   A 137 ? 0.22194 0.41022 0.30519 -0.03192 0.01215  -0.00097 136 SER   A O     
1115 C  CB    . SER   A 137 ? 0.18855 0.40489 0.24260 0.03290  0.05527  -0.00131 136 SER   A CB    
1116 O  OG    . SER   A 137 ? 0.25779 0.41990 0.23551 0.01937  0.00840  0.00267  136 SER   A OG    
1117 N  N     . TYR   A 138 ? 0.25980 0.33454 0.23389 0.07243  0.03155  0.03180  137 TYR   A N     
1118 C  CA    . TYR   A 138 ? 0.23834 0.32294 0.24504 0.06119  -0.00461 -0.00174 137 TYR   A CA    
1119 C  C     . TYR   A 138 ? 0.21668 0.33162 0.25564 0.01883  -0.01128 -0.01529 137 TYR   A C     
1120 O  O     . TYR   A 138 ? 0.20761 0.35123 0.27606 -0.00201 0.01276  0.00762  137 TYR   A O     
1121 C  CB    . TYR   A 138 ? 0.20960 0.31840 0.26859 0.07534  0.01167  0.00379  137 TYR   A CB    
1122 C  CG    . TYR   A 138 ? 0.30411 0.31184 0.27881 0.06457  0.00355  -0.02288 137 TYR   A CG    
1123 C  CD1   . TYR   A 138 ? 0.28404 0.31133 0.27949 0.05745  -0.00868 -0.03450 137 TYR   A CD1   
1124 C  CD2   . TYR   A 138 ? 0.27915 0.32843 0.25279 0.04992  0.00575  -0.00087 137 TYR   A CD2   
1125 C  CE1   . TYR   A 138 ? 0.29591 0.31229 0.26503 0.09427  -0.01521 -0.03600 137 TYR   A CE1   
1126 C  CE2   . TYR   A 138 ? 0.31310 0.30971 0.21588 0.07981  -0.00645 0.00754  137 TYR   A CE2   
1127 C  CZ    . TYR   A 138 ? 0.35024 0.30481 0.24565 0.08672  -0.03747 -0.01268 137 TYR   A CZ    
1128 O  OH    . TYR   A 138 ? 0.42911 0.29404 0.24544 0.07190  -0.01613 -0.01168 137 TYR   A OH    
1129 N  N     . GLY   A 139 ? 0.17454 0.33077 0.24620 0.05235  0.00753  0.01807  138 GLY   A N     
1130 C  CA    . GLY   A 139 ? 0.21585 0.33964 0.25295 0.06617  0.04048  0.00105  138 GLY   A CA    
1131 C  C     . GLY   A 139 ? 0.19556 0.33724 0.22828 0.06578  0.02437  -0.04691 138 GLY   A C     
1132 O  O     . GLY   A 139 ? 0.25825 0.37731 0.21087 0.05632  -0.01330 -0.03016 138 GLY   A O     
1133 N  N     . ILE   A 140 ? 0.15082 0.30182 0.22772 0.06154  -0.01311 -0.05374 139 ILE   A N     
1134 C  CA    . ILE   A 140 ? 0.18100 0.28117 0.18642 0.05477  0.01113  -0.04200 139 ILE   A CA    
1135 C  C     . ILE   A 140 ? 0.23026 0.27371 0.15824 0.06621  -0.03775 -0.04635 139 ILE   A C     
1136 O  O     . ILE   A 140 ? 0.24045 0.26491 0.19692 0.05869  -0.05770 -0.03392 139 ILE   A O     
1137 C  CB    . ILE   A 140 ? 0.18372 0.24935 0.21523 0.03349  -0.04232 -0.04547 139 ILE   A CB    
1138 C  CG1   . ILE   A 140 ? 0.22789 0.22407 0.22210 0.04440  -0.04664 -0.02432 139 ILE   A CG1   
1139 C  CG2   . ILE   A 140 ? 0.20088 0.27347 0.22188 -0.01245 -0.02754 -0.05615 139 ILE   A CG2   
1140 C  CD1   . ILE   A 140 ? 0.24936 0.22117 0.25972 0.05114  -0.03235 -0.01560 139 ILE   A CD1   
1141 N  N     . PRO   A 141 ? 0.19385 0.25791 0.17479 0.05139  -0.03550 -0.02285 140 PRO   A N     
1142 C  CA    . PRO   A 141 ? 0.18770 0.23390 0.19251 0.00422  -0.04074 -0.01930 140 PRO   A CA    
1143 C  C     . PRO   A 141 ? 0.18783 0.21262 0.20802 0.04414  -0.04244 -0.03104 140 PRO   A C     
1144 O  O     . PRO   A 141 ? 0.20098 0.20998 0.21032 0.04836  -0.03346 -0.02565 140 PRO   A O     
1145 C  CB    . PRO   A 141 ? 0.22368 0.25197 0.20718 0.06560  -0.01186 -0.01838 140 PRO   A CB    
1146 C  CG    . PRO   A 141 ? 0.20596 0.26091 0.20093 0.01890  -0.04956 -0.02732 140 PRO   A CG    
1147 C  CD    . PRO   A 141 ? 0.24013 0.22060 0.14131 0.03482  -0.03667 -0.00885 140 PRO   A CD    
1148 N  N     . PHE   A 142 ? 0.18408 0.24241 0.22878 0.04034  -0.05744 -0.03609 141 PHE   A N     
1149 C  CA    . PHE   A 142 ? 0.19843 0.22542 0.25970 0.01542  -0.05180 -0.04559 141 PHE   A CA    
1150 C  C     . PHE   A 142 ? 0.19347 0.17861 0.26337 0.03131  -0.07262 -0.04406 141 PHE   A C     
1151 O  O     . PHE   A 142 ? 0.27007 0.14809 0.29973 0.04316  -0.04621 -0.01421 141 PHE   A O     
1152 C  CB    . PHE   A 142 ? 0.24340 0.25200 0.23923 0.04239  -0.06251 -0.04208 141 PHE   A CB    
1153 C  CG    . PHE   A 142 ? 0.24867 0.21064 0.21662 0.04421  -0.06306 -0.02160 141 PHE   A CG    
1154 C  CD1   . PHE   A 142 ? 0.28013 0.23872 0.22691 0.05846  -0.09553 -0.03156 141 PHE   A CD1   
1155 C  CD2   . PHE   A 142 ? 0.40342 0.24637 0.25512 0.01465  -0.10638 -0.05439 141 PHE   A CD2   
1156 C  CE1   . PHE   A 142 ? 0.31125 0.24855 0.20866 0.01769  -0.02574 -0.04721 141 PHE   A CE1   
1157 C  CE2   . PHE   A 142 ? 0.38282 0.24147 0.27326 0.02484  -0.12668 -0.07852 141 PHE   A CE2   
1158 C  CZ    . PHE   A 142 ? 0.34025 0.23963 0.25589 0.01720  -0.07267 -0.03683 141 PHE   A CZ    
1159 N  N     . ILE   A 143 ? 0.15354 0.23356 0.23522 0.00276  -0.05426 -0.01396 142 ILE   A N     
1160 C  CA    . ILE   A 143 ? 0.19673 0.25394 0.27091 0.00562  -0.04146 -0.02444 142 ILE   A CA    
1161 C  C     . ILE   A 143 ? 0.20114 0.22993 0.26806 0.03633  -0.06451 -0.03587 142 ILE   A C     
1162 O  O     . ILE   A 143 ? 0.23791 0.17380 0.24180 0.02796  -0.08514 -0.03444 142 ILE   A O     
1163 C  CB    . ILE   A 143 ? 0.24041 0.30043 0.26673 -0.03494 -0.04947 0.02583  142 ILE   A CB    
1164 C  CG1   . ILE   A 143 ? 0.31316 0.34989 0.31106 0.00056  -0.07132 0.01421  142 ILE   A CG1   
1165 C  CG2   . ILE   A 143 ? 0.22127 0.30925 0.29420 -0.05106 -0.04688 0.05632  142 ILE   A CG2   
1166 C  CD1   . ILE   A 143 ? 0.34514 0.36131 0.32225 -0.01957 -0.02702 -0.00348 142 ILE   A CD1   
1167 N  N     . GLU   A 144 ? 0.22989 0.24589 0.26496 0.00278  -0.08394 -0.02719 143 GLU   A N     
1168 C  CA    . GLU   A 144 ? 0.24425 0.24479 0.26753 0.00320  -0.05230 -0.05532 143 GLU   A CA    
1169 C  C     . GLU   A 144 ? 0.28049 0.21448 0.30069 -0.00737 -0.11640 -0.02098 143 GLU   A C     
1170 O  O     . GLU   A 144 ? 0.30312 0.20379 0.34756 0.00916  -0.10915 0.01277  143 GLU   A O     
1171 C  CB    . GLU   A 144 ? 0.40006 0.30597 0.29647 -0.03268 -0.04963 -0.08935 143 GLU   A CB    
1172 C  CG    . GLU   A 144 ? 0.57991 0.34992 0.31429 -0.05950 -0.07537 -0.09856 143 GLU   A CG    
1173 C  CD    . GLU   A 144 ? 0.72769 0.36001 0.33966 -0.04391 -0.10357 -0.07342 143 GLU   A CD    
1174 O  OE1   . GLU   A 144 ? 0.80135 0.37129 0.35879 -0.07562 -0.09776 -0.07891 143 GLU   A OE1   
1175 O  OE2   . GLU   A 144 ? 0.72985 0.34280 0.32708 0.01416  -0.14963 -0.03875 143 GLU   A OE2   
1176 N  N     . THR   A 145 ? 0.24651 0.19449 0.25104 0.00475  -0.05687 -0.03818 144 THR   A N     
1177 C  CA    . THR   A 145 ? 0.24408 0.19725 0.21924 -0.00641 -0.07140 -0.03785 144 THR   A CA    
1178 C  C     . THR   A 145 ? 0.27258 0.17966 0.22523 -0.02974 -0.04846 -0.00478 144 THR   A C     
1179 O  O     . THR   A 145 ? 0.24262 0.21936 0.25214 -0.03661 -0.07027 -0.00929 144 THR   A O     
1180 C  CB    . THR   A 145 ? 0.23114 0.17156 0.21895 0.00001  -0.08762 -0.00061 144 THR   A CB    
1181 O  OG1   . THR   A 145 ? 0.19878 0.17475 0.22602 -0.00547 -0.06180 0.00740  144 THR   A OG1   
1182 C  CG2   . THR   A 145 ? 0.23451 0.18790 0.25160 -0.00707 -0.08545 -0.01620 144 THR   A CG2   
1183 N  N     . SER   A 146 ? 0.20332 0.19520 0.25502 -0.03697 -0.04642 -0.00098 145 SER   A N     
1184 C  CA    . SER   A 146 ? 0.23560 0.19460 0.24585 -0.04184 -0.05955 -0.02184 145 SER   A CA    
1185 C  C     . SER   A 146 ? 0.23678 0.20635 0.23754 -0.07627 -0.06161 -0.01716 145 SER   A C     
1186 O  O     . SER   A 146 ? 0.27504 0.21755 0.23720 -0.05843 -0.05475 0.02342  145 SER   A O     
1187 C  CB    . SER   A 146 ? 0.26672 0.21271 0.29502 -0.02644 -0.09051 0.01025  145 SER   A CB    
1188 O  OG    . SER   A 146 ? 0.22196 0.22183 0.31787 -0.02691 -0.08180 -0.01016 145 SER   A OG    
1189 N  N     . ALA   A 147 ? 0.25012 0.20336 0.24547 -0.07389 -0.04680 -0.01932 146 ALA   A N     
1190 C  CA    . ALA   A 147 ? 0.22750 0.19979 0.23232 -0.07394 -0.00674 -0.00582 146 ALA   A CA    
1191 C  C     . ALA   A 147 ? 0.20276 0.23670 0.24394 -0.04561 -0.00729 0.02613  146 ALA   A C     
1192 O  O     . ALA   A 147 ? 0.33095 0.29402 0.25820 -0.06817 0.02847  0.04246  146 ALA   A O     
1193 C  CB    . ALA   A 147 ? 0.26943 0.19650 0.26026 -0.07173 -0.04279 0.02468  146 ALA   A CB    
1194 N  N     . LYS   A 148 ? 0.25638 0.22876 0.27218 -0.05668 -0.06934 -0.00092 147 LYS   A N     
1195 C  CA    . LYS   A 148 ? 0.23592 0.28476 0.32805 -0.06703 -0.02519 0.01582  147 LYS   A CA    
1196 C  C     . LYS   A 148 ? 0.27822 0.28657 0.35575 -0.07770 -0.02364 0.03986  147 LYS   A C     
1197 O  O     . LYS   A 148 ? 0.27450 0.30315 0.41708 -0.06810 0.00918  0.03856  147 LYS   A O     
1198 C  CB    . LYS   A 148 ? 0.19373 0.29589 0.38236 -0.05158 -0.06015 0.01862  147 LYS   A CB    
1199 C  CG    . LYS   A 148 ? 0.22279 0.31773 0.44505 -0.08839 -0.05203 0.00608  147 LYS   A CG    
1200 C  CD    . LYS   A 148 ? 0.24938 0.35607 0.49714 -0.08947 -0.10507 -0.02413 147 LYS   A CD    
1201 C  CE    . LYS   A 148 ? 0.29626 0.38053 0.54393 -0.08100 -0.09738 -0.03532 147 LYS   A CE    
1202 N  NZ    . LYS   A 148 ? 0.40263 0.40476 0.59435 -0.09294 -0.08788 -0.01560 147 LYS   A NZ    
1203 N  N     . THR   A 149 ? 0.28435 0.26238 0.33088 -0.10446 -0.11370 0.04724  148 THR   A N     
1204 C  CA    . THR   A 149 ? 0.32246 0.28054 0.33104 -0.09238 -0.11682 0.05959  148 THR   A CA    
1205 C  C     . THR   A 149 ? 0.26949 0.29292 0.34410 -0.13468 -0.08823 0.07651  148 THR   A C     
1206 O  O     . THR   A 149 ? 0.35683 0.28841 0.38014 -0.14458 -0.06387 0.04568  148 THR   A O     
1207 C  CB    . THR   A 149 ? 0.30602 0.26567 0.37161 -0.07517 -0.11356 0.03199  148 THR   A CB    
1208 O  OG1   . THR   A 149 ? 0.29446 0.25977 0.41085 -0.07535 -0.12301 0.01377  148 THR   A OG1   
1209 C  CG2   . THR   A 149 ? 0.33255 0.26567 0.37667 -0.07484 -0.09184 0.02833  148 THR   A CG2   
1210 N  N     . ARG   A 150 ? 0.28982 0.28810 0.30437 -0.13000 -0.10115 0.08623  149 ARG   A N     
1211 C  CA    . ARG   A 150 ? 0.37788 0.30460 0.27150 -0.11083 -0.10915 0.07400  149 ARG   A CA    
1212 C  C     . ARG   A 150 ? 0.39125 0.27423 0.27523 -0.07581 -0.11413 0.08790  149 ARG   A C     
1213 O  O     . ARG   A 150 ? 0.33803 0.23936 0.31389 -0.08453 -0.15082 0.07355  149 ARG   A O     
1214 C  CB    . ARG   A 150 ? 0.52336 0.31381 0.23824 -0.14013 -0.07859 0.05235  149 ARG   A CB    
1215 C  CG    . ARG   A 150 ? 0.65152 0.34216 0.29687 -0.07140 -0.06234 0.04090  149 ARG   A CG    
1216 C  CD    . ARG   A 150 ? 0.71711 0.34687 0.33011 -0.02215 -0.03025 0.06829  149 ARG   A CD    
1217 N  NE    . ARG   A 150 ? 0.75402 0.34193 0.38562 0.01450  -0.00693 0.08882  149 ARG   A NE    
1218 C  CZ    . ARG   A 150 ? 0.81482 0.33794 0.42040 0.05091  0.01988  0.10687  149 ARG   A CZ    
1219 N  NH1   . ARG   A 150 ? 0.77737 0.33005 0.43523 0.06021  0.03649  0.11990  149 ARG   A NH1   
1220 N  NH2   . ARG   A 150 ? 0.84931 0.33172 0.44364 0.06193  0.02475  0.10632  149 ARG   A NH2   
1221 N  N     . GLN   A 151 ? 0.33105 0.25866 0.29761 -0.11252 -0.04566 0.04785  150 GLN   A N     
1222 C  CA    . GLN   A 151 ? 0.33174 0.24706 0.31840 -0.09919 -0.08634 0.03998  150 GLN   A CA    
1223 C  C     . GLN   A 151 ? 0.32772 0.22161 0.26949 -0.06237 -0.10458 0.05331  150 GLN   A C     
1224 O  O     . GLN   A 151 ? 0.30899 0.23767 0.22177 -0.04731 -0.07166 0.04780  150 GLN   A O     
1225 C  CB    . GLN   A 151 ? 0.36140 0.30009 0.37416 -0.08308 -0.08172 -0.04460 150 GLN   A CB    
1226 C  CG    . GLN   A 151 ? 0.43820 0.36068 0.46067 -0.08248 -0.09848 -0.08418 150 GLN   A CG    
1227 C  CD    . GLN   A 151 ? 0.49938 0.41041 0.57808 -0.07609 -0.05646 -0.08567 150 GLN   A CD    
1228 O  OE1   . GLN   A 151 ? 0.52167 0.45118 0.61131 -0.05602 -0.06947 -0.07631 150 GLN   A OE1   
1229 N  NE2   . GLN   A 151 ? 0.50876 0.41389 0.59526 -0.10383 -0.08241 -0.10843 150 GLN   A NE2   
1230 N  N     . GLY   A 152 ? 0.30313 0.21873 0.29130 -0.04548 -0.09791 0.03156  151 GLY   A N     
1231 C  CA    . GLY   A 152 ? 0.31385 0.20388 0.25729 -0.05509 -0.10244 0.01850  151 GLY   A CA    
1232 C  C     . GLY   A 152 ? 0.32705 0.18113 0.23933 -0.09294 -0.08388 0.02989  151 GLY   A C     
1233 O  O     . GLY   A 152 ? 0.28168 0.19860 0.24142 -0.06426 -0.09160 0.02998  151 GLY   A O     
1234 N  N     . VAL   A 153 ? 0.32114 0.20671 0.23872 -0.06987 -0.07660 0.01852  152 VAL   A N     
1235 C  CA    . VAL   A 153 ? 0.29016 0.20564 0.24797 -0.05097 -0.10377 0.02665  152 VAL   A CA    
1236 C  C     . VAL   A 153 ? 0.28387 0.18952 0.24157 -0.07362 -0.09438 0.05318  152 VAL   A C     
1237 O  O     . VAL   A 153 ? 0.26277 0.17243 0.24982 -0.07329 -0.07512 0.02238  152 VAL   A O     
1238 C  CB    . VAL   A 153 ? 0.21485 0.22050 0.29459 -0.05134 -0.05842 0.00795  152 VAL   A CB    
1239 C  CG1   . VAL   A 153 ? 0.26195 0.22697 0.33778 0.00012  -0.04305 -0.00248 152 VAL   A CG1   
1240 C  CG2   . VAL   A 153 ? 0.27309 0.24125 0.28074 -0.06499 -0.11342 0.04190  152 VAL   A CG2   
1241 N  N     . ASP   A 154 ? 0.27367 0.21302 0.24684 -0.04749 -0.06092 0.06525  153 ASP   A N     
1242 C  CA    . ASP   A 154 ? 0.24844 0.25556 0.23101 -0.03183 -0.04756 0.08099  153 ASP   A CA    
1243 C  C     . ASP   A 154 ? 0.29240 0.24475 0.18433 -0.05235 -0.04890 0.04285  153 ASP   A C     
1244 O  O     . ASP   A 154 ? 0.27853 0.25609 0.18358 -0.08311 -0.04941 0.04723  153 ASP   A O     
1245 C  CB    . ASP   A 154 ? 0.30242 0.29288 0.27243 -0.03227 -0.03371 0.09807  153 ASP   A CB    
1246 C  CG    . ASP   A 154 ? 0.38025 0.30922 0.29878 -0.03004 0.00744  0.10059  153 ASP   A CG    
1247 O  OD1   . ASP   A 154 ? 0.42208 0.34198 0.35385 -0.02646 0.06073  0.08213  153 ASP   A OD1   
1248 O  OD2   . ASP   A 154 ? 0.47930 0.33992 0.33443 -0.01843 0.01399  0.08248  153 ASP   A OD2   
1249 N  N     . ASP   A 155 ? 0.29340 0.21884 0.19051 -0.00395 -0.06837 0.02654  154 ASP   A N     
1250 C  CA    . ASP   A 155 ? 0.29800 0.19754 0.22071 -0.00111 -0.03850 0.02111  154 ASP   A CA    
1251 C  C     . ASP   A 155 ? 0.26379 0.18273 0.24851 0.01224  -0.05339 0.02589  154 ASP   A C     
1252 O  O     . ASP   A 155 ? 0.21414 0.17171 0.22213 -0.00901 -0.05401 0.01764  154 ASP   A O     
1253 C  CB    . ASP   A 155 ? 0.37252 0.20403 0.29213 -0.01955 -0.09006 0.00416  154 ASP   A CB    
1254 C  CG    . ASP   A 155 ? 0.43857 0.22282 0.29968 -0.01015 -0.11674 -0.03085 154 ASP   A CG    
1255 O  OD1   . ASP   A 155 ? 0.44780 0.22047 0.35011 0.01370  -0.08929 -0.01647 154 ASP   A OD1   
1256 O  OD2   . ASP   A 155 ? 0.48695 0.26377 0.30080 0.01018  -0.10028 0.00108  154 ASP   A OD2   
1257 N  N     . ALA   A 156 ? 0.23287 0.16441 0.20563 -0.02959 -0.09700 0.02045  155 ALA   A N     
1258 C  CA    . ALA   A 156 ? 0.25717 0.16864 0.20309 -0.01266 -0.07213 0.02888  155 ALA   A CA    
1259 C  C     . ALA   A 156 ? 0.19229 0.17532 0.21783 0.00030  -0.03354 0.01701  155 ALA   A C     
1260 O  O     . ALA   A 156 ? 0.19823 0.17064 0.18035 -0.00536 -0.03881 0.01785  155 ALA   A O     
1261 C  CB    . ALA   A 156 ? 0.28906 0.17062 0.21343 -0.05144 -0.07393 0.04782  155 ALA   A CB    
1262 N  N     . PHE   A 157 ? 0.22655 0.18560 0.16539 -0.00789 -0.05936 0.00421  156 PHE   A N     
1263 C  CA    . PHE   A 157 ? 0.20439 0.18840 0.19169 0.03521  -0.04594 -0.01097 156 PHE   A CA    
1264 C  C     . PHE   A 157 ? 0.23356 0.19660 0.17230 0.02353  -0.05748 -0.00485 156 PHE   A C     
1265 O  O     . PHE   A 157 ? 0.20331 0.20724 0.19248 -0.00051 -0.05660 0.02304  156 PHE   A O     
1266 C  CB    . PHE   A 157 ? 0.18219 0.22669 0.21251 0.02159  -0.03321 0.01440  156 PHE   A CB    
1267 C  CG    . PHE   A 157 ? 0.16074 0.17808 0.23341 0.02248  -0.04559 -0.00221 156 PHE   A CG    
1268 C  CD1   . PHE   A 157 ? 0.21699 0.17904 0.22196 0.01841  0.00458  0.02464  156 PHE   A CD1   
1269 C  CD2   . PHE   A 157 ? 0.19337 0.18557 0.25074 -0.03461 -0.04362 0.02881  156 PHE   A CD2   
1270 C  CE1   . PHE   A 157 ? 0.18652 0.21481 0.21898 -0.00904 0.03338  0.00932  156 PHE   A CE1   
1271 C  CE2   . PHE   A 157 ? 0.22684 0.19694 0.22147 -0.00793 -0.03917 0.02388  156 PHE   A CE2   
1272 C  CZ    . PHE   A 157 ? 0.19404 0.21920 0.21272 0.01560  0.00620  0.01321  156 PHE   A CZ    
1273 N  N     . TYR   A 158 ? 0.20805 0.18534 0.18310 0.00542  -0.04235 0.02964  157 TYR   A N     
1274 C  CA    . TYR   A 158 ? 0.20335 0.18659 0.20091 0.01606  -0.03883 0.02713  157 TYR   A CA    
1275 C  C     . TYR   A 158 ? 0.22101 0.17293 0.18194 0.02006  -0.05185 0.02610  157 TYR   A C     
1276 O  O     . TYR   A 158 ? 0.24269 0.19423 0.18261 -0.00522 -0.05793 0.03470  157 TYR   A O     
1277 C  CB    . TYR   A 158 ? 0.22081 0.22304 0.22431 -0.00328 -0.02454 0.00852  157 TYR   A CB    
1278 C  CG    . TYR   A 158 ? 0.29489 0.26941 0.21006 -0.03952 -0.01488 0.01043  157 TYR   A CG    
1279 C  CD1   . TYR   A 158 ? 0.24267 0.32293 0.21938 -0.03710 -0.04989 0.00919  157 TYR   A CD1   
1280 C  CD2   . TYR   A 158 ? 0.32460 0.29900 0.23130 -0.07484 -0.01842 0.07233  157 TYR   A CD2   
1281 C  CE1   . TYR   A 158 ? 0.36087 0.35505 0.21059 -0.06091 -0.04229 0.02227  157 TYR   A CE1   
1282 C  CE2   . TYR   A 158 ? 0.35255 0.35390 0.23888 -0.07084 0.02331  0.03507  157 TYR   A CE2   
1283 C  CZ    . TYR   A 158 ? 0.34235 0.38261 0.21800 -0.07354 -0.00936 0.02804  157 TYR   A CZ    
1284 O  OH    . TYR   A 158 ? 0.36255 0.43360 0.26151 -0.07764 0.03604  0.05150  157 TYR   A OH    
1285 N  N     . THR   A 159 ? 0.20971 0.16641 0.18311 0.01745  -0.02289 0.01687  158 THR   A N     
1286 C  CA    . THR   A 159 ? 0.22799 0.17056 0.18357 0.02549  -0.04189 -0.00545 158 THR   A CA    
1287 C  C     . THR   A 159 ? 0.16891 0.16228 0.19085 0.04216  -0.04217 -0.01248 158 THR   A C     
1288 O  O     . THR   A 159 ? 0.16581 0.20591 0.22352 0.01336  -0.02946 -0.02951 158 THR   A O     
1289 C  CB    . THR   A 159 ? 0.24339 0.15019 0.20383 -0.01296 -0.04687 0.00631  158 THR   A CB    
1290 O  OG1   . THR   A 159 ? 0.26377 0.16048 0.22478 -0.01686 -0.04684 0.00097  158 THR   A OG1   
1291 C  CG2   . THR   A 159 ? 0.24504 0.18998 0.26399 -0.03234 -0.01180 0.01209  158 THR   A CG2   
1292 N  N     . LEU   A 160 ? 0.17035 0.15503 0.17322 0.01343  -0.03274 -0.00692 159 LEU   A N     
1293 C  CA    . LEU   A 160 ? 0.18216 0.16772 0.15639 -0.00046 -0.04952 -0.00027 159 LEU   A CA    
1294 C  C     . LEU   A 160 ? 0.22772 0.17435 0.14743 0.00815  -0.03755 0.01612  159 LEU   A C     
1295 O  O     . LEU   A 160 ? 0.17104 0.17622 0.18266 0.01273  -0.04423 0.00471  159 LEU   A O     
1296 C  CB    . LEU   A 160 ? 0.19129 0.16490 0.18884 0.03346  -0.03732 0.02861  159 LEU   A CB    
1297 C  CG    . LEU   A 160 ? 0.14680 0.15138 0.18759 0.02713  -0.01137 0.00296  159 LEU   A CG    
1298 C  CD1   . LEU   A 160 ? 0.20654 0.13673 0.24211 -0.00627 0.02653  -0.00218 159 LEU   A CD1   
1299 C  CD2   . LEU   A 160 ? 0.19629 0.17399 0.21129 0.02143  -0.03042 0.01441  159 LEU   A CD2   
1300 N  N     . VAL   A 161 ? 0.21515 0.17398 0.14502 0.04201  -0.04855 0.02190  160 VAL   A N     
1301 C  CA    . VAL   A 161 ? 0.22186 0.22151 0.13965 0.04228  -0.03890 0.00833  160 VAL   A CA    
1302 C  C     . VAL   A 161 ? 0.21502 0.18436 0.16803 0.02179  -0.08061 0.00044  160 VAL   A C     
1303 O  O     . VAL   A 161 ? 0.21452 0.19600 0.18708 -0.00386 -0.05731 -0.01251 160 VAL   A O     
1304 C  CB    . VAL   A 161 ? 0.22804 0.21573 0.13293 0.01849  -0.04269 0.02746  160 VAL   A CB    
1305 C  CG1   . VAL   A 161 ? 0.18434 0.22266 0.17595 -0.01328 -0.02565 0.03443  160 VAL   A CG1   
1306 C  CG2   . VAL   A 161 ? 0.21497 0.22128 0.19162 0.02347  -0.02322 -0.00726 160 VAL   A CG2   
1307 N  N     . ARG   A 162 ? 0.22438 0.17092 0.19464 0.03232  -0.05141 -0.01352 161 ARG   A N     
1308 C  CA    . ARG   A 162 ? 0.23103 0.17610 0.27275 0.02665  -0.05835 -0.02210 161 ARG   A CA    
1309 C  C     . ARG   A 162 ? 0.20354 0.18311 0.23517 0.03893  -0.07676 -0.01457 161 ARG   A C     
1310 O  O     . ARG   A 162 ? 0.21565 0.21710 0.25292 0.02086  -0.06146 -0.01220 161 ARG   A O     
1311 C  CB    . ARG   A 162 ? 0.22688 0.16087 0.33878 0.02398  -0.02523 0.00190  161 ARG   A CB    
1312 C  CG    . ARG   A 162 ? 0.25455 0.15892 0.29389 -0.01696 -0.07186 -0.00935 161 ARG   A CG    
1313 C  CD    . ARG   A 162 ? 0.30361 0.16824 0.34236 -0.03176 0.02121  0.01036  161 ARG   A CD    
1314 N  NE    . ARG   A 162 ? 0.35697 0.15566 0.34844 0.00546  0.00153  -0.00543 161 ARG   A NE    
1315 C  CZ    . ARG   A 162 ? 0.41785 0.18688 0.37068 0.00296  -0.05570 -0.02515 161 ARG   A CZ    
1316 N  NH1   . ARG   A 162 ? 0.43631 0.19365 0.35759 0.01558  -0.04371 -0.00048 161 ARG   A NH1   
1317 N  NH2   . ARG   A 162 ? 0.41850 0.22361 0.39263 0.04147  -0.06324 -0.05843 161 ARG   A NH2   
1318 N  N     . GLU   A 163 ? 0.19589 0.19359 0.20181 0.02225  -0.04165 0.00384  162 GLU   A N     
1319 C  CA    . GLU   A 163 ? 0.21627 0.19999 0.20704 0.03282  -0.03656 0.00032  162 GLU   A CA    
1320 C  C     . GLU   A 163 ? 0.18289 0.23060 0.18240 0.03108  -0.02716 -0.01442 162 GLU   A C     
1321 O  O     . GLU   A 163 ? 0.13196 0.26805 0.25583 0.00315  -0.01642 -0.04633 162 GLU   A O     
1322 C  CB    . GLU   A 163 ? 0.20903 0.19948 0.19676 0.03477  -0.03367 -0.04494 162 GLU   A CB    
1323 C  CG    . GLU   A 163 ? 0.21068 0.22093 0.23830 0.04930  -0.02034 -0.05049 162 GLU   A CG    
1324 C  CD    . GLU   A 163 ? 0.20120 0.23232 0.30763 0.03400  -0.06593 -0.02893 162 GLU   A CD    
1325 O  OE1   . GLU   A 163 ? 0.22604 0.25366 0.38285 0.05586  0.01576  -0.00175 162 GLU   A OE1   
1326 O  OE2   . GLU   A 163 ? 0.28397 0.26771 0.40457 0.04335  -0.02704 -0.03619 162 GLU   A OE2   
1327 N  N     . ILE   A 164 ? 0.19676 0.19272 0.16487 0.04435  -0.02968 -0.01976 163 ILE   A N     
1328 C  CA    . ILE   A 164 ? 0.20139 0.21864 0.17151 0.02432  -0.03849 -0.03320 163 ILE   A CA    
1329 C  C     . ILE   A 164 ? 0.17067 0.22946 0.19366 0.01895  -0.05887 -0.03560 163 ILE   A C     
1330 O  O     . ILE   A 164 ? 0.19730 0.22794 0.20571 0.02244  -0.04585 -0.00340 163 ILE   A O     
1331 C  CB    . ILE   A 164 ? 0.23062 0.21722 0.14380 0.01444  -0.03020 -0.03178 163 ILE   A CB    
1332 C  CG1   . ILE   A 164 ? 0.19319 0.20916 0.15240 0.04945  -0.02780 -0.00254 163 ILE   A CG1   
1333 C  CG2   . ILE   A 164 ? 0.21698 0.21143 0.16490 -0.01041 -0.03968 0.00091  163 ILE   A CG2   
1334 C  CD1   . ILE   A 164 ? 0.23295 0.18994 0.16433 0.03441  -0.00656 0.01566  163 ILE   A CD1   
1335 N  N     . ARG   A 165 ? 0.23212 0.21020 0.21439 -0.00038 -0.09547 -0.00374 164 ARG   A N     
1336 C  CA    . ARG   A 165 ? 0.29205 0.22278 0.24967 0.03344  -0.12724 0.00170  164 ARG   A CA    
1337 C  C     . ARG   A 165 ? 0.29602 0.24998 0.27475 0.04850  -0.13122 -0.00281 164 ARG   A C     
1338 O  O     . ARG   A 165 ? 0.24846 0.29662 0.26692 0.00615  -0.10295 0.01432  164 ARG   A O     
1339 C  CB    . ARG   A 165 ? 0.31566 0.22079 0.29329 0.01444  -0.15961 0.03043  164 ARG   A CB    
1340 C  CG    . ARG   A 165 ? 0.35022 0.24156 0.32570 0.02260  -0.11482 0.07891  164 ARG   A CG    
1341 C  CD    . ARG   A 165 ? 0.41556 0.29790 0.40686 0.01850  -0.04478 0.17073  164 ARG   A CD    
1342 N  NE    . ARG   A 165 ? 0.50519 0.33593 0.46722 0.02248  -0.07563 0.21842  164 ARG   A NE    
1343 C  CZ    . ARG   A 165 ? 0.49038 0.43440 0.54030 0.00061  -0.13719 0.21792  164 ARG   A CZ    
1344 N  NH1   . ARG   A 165 ? 0.49729 0.48401 0.57076 -0.04864 -0.11984 0.19310  164 ARG   A NH1   
1345 N  NH2   . ARG   A 165 ? 0.41671 0.46613 0.53744 0.00045  -0.22498 0.17661  164 ARG   A NH2   
1346 N  N     . LYS   A 166 ? 0.28853 0.25515 0.30885 0.06148  -0.14210 -0.01065 165 LYS   A N     
1347 C  CA    . LYS   A 166 ? 0.27159 0.29714 0.35449 0.08587  -0.08465 -0.05444 165 LYS   A CA    
1348 C  C     . LYS   A 166 ? 0.19764 0.30098 0.35706 0.06826  -0.06062 -0.06245 165 LYS   A C     
1349 O  O     . LYS   A 166 ? 0.20512 0.35447 0.34754 0.02948  -0.05718 -0.07971 165 LYS   A O     
1350 C  CB    . LYS   A 166 ? 0.37844 0.31152 0.37434 0.12180  -0.09700 -0.11922 165 LYS   A CB    
1351 C  CG    . LYS   A 166 ? 0.61685 0.37637 0.48108 0.12560  -0.06719 -0.14941 165 LYS   A CG    
1352 C  CD    . LYS   A 166 ? 0.76476 0.42140 0.57904 0.11119  -0.05973 -0.15496 165 LYS   A CD    
1353 C  CE    . LYS   A 166 ? 0.86767 0.45808 0.65823 0.10975  -0.04438 -0.13212 165 LYS   A CE    
1354 N  NZ    . LYS   A 166 ? 0.92644 0.47388 0.68728 0.10020  -0.04161 -0.11344 165 LYS   A NZ    
1355 N  N     . HIS   A 167 ? 0.22703 0.28505 0.29168 0.02917  -0.04663 -0.07818 166 HIS   A N     
1356 C  CA    . HIS   A 167 ? 0.22007 0.29216 0.25492 0.02237  -0.07325 -0.05843 166 HIS   A CA    
1357 C  C     . HIS   A 167 ? 0.21898 0.31692 0.24976 0.02558  -0.03336 -0.02667 166 HIS   A C     
1358 O  O     . HIS   A 167 ? 0.18258 0.34305 0.31205 -0.00370 -0.02018 -0.02251 166 HIS   A O     
1359 C  CB    . HIS   A 167 ? 0.25123 0.31916 0.29034 0.02158  -0.05675 -0.04113 166 HIS   A CB    
1360 C  CG    . HIS   A 167 ? 0.23775 0.34084 0.42226 -0.01963 -0.09442 -0.00017 166 HIS   A CG    
1361 N  ND1   . HIS   A 167 ? 0.35361 0.35006 0.47406 -0.04739 -0.04916 0.01667  166 HIS   A ND1   
1362 C  CD2   . HIS   A 167 ? 0.31929 0.35578 0.49048 -0.01829 -0.05699 0.02950  166 HIS   A CD2   
1363 C  CE1   . HIS   A 167 ? 0.34544 0.35918 0.50683 -0.02282 -0.02148 0.04008  166 HIS   A CE1   
1364 N  NE2   . HIS   A 167 ? 0.38294 0.36928 0.53262 -0.00502 -0.02548 0.04747  166 HIS   A NE2   
1365 N  N     . LYS   A 168 ? 0.17948 0.32239 0.25206 0.00920  -0.02630 -0.05470 167 LYS   A N     
1366 C  CA    . LYS   A 168 ? 0.19348 0.33117 0.23509 0.02669  -0.04810 -0.04535 167 LYS   A CA    
1367 C  C     . LYS   A 168 ? 0.28007 0.39947 0.27720 0.03770  -0.07878 -0.06882 167 LYS   A C     
1368 O  O     . LYS   A 168 ? 0.23711 0.41762 0.30610 -0.00173 -0.10672 -0.07377 167 LYS   A O     
1369 C  CB    . LYS   A 168 ? 0.23090 0.29421 0.20553 0.04449  -0.04784 -0.02638 167 LYS   A CB    
1370 C  CG    . LYS   A 168 ? 0.20604 0.27031 0.18279 0.01944  -0.07307 -0.01582 167 LYS   A CG    
1371 C  CD    . LYS   A 168 ? 0.22723 0.28089 0.20279 0.04111  -0.00667 0.00121  167 LYS   A CD    
1372 C  CE    . LYS   A 168 ? 0.34354 0.29682 0.18480 0.01772  0.02165  0.01249  167 LYS   A CE    
1373 N  NZ    . LYS   A 168 ? 0.35962 0.28098 0.20730 0.02147  0.04964  -0.01480 167 LYS   A NZ    
1374 N  N     . GLU   A 169 ? 0.30640 0.43780 0.41104 0.04913  -0.19247 -0.04787 168 GLU   A N     
1375 C  CA    . GLU   A 169 ? 0.39103 0.48258 0.52898 0.08588  -0.25373 -0.01368 168 GLU   A CA    
1376 C  C     . GLU   A 169 ? 0.40452 0.53236 0.63307 0.09296  -0.27567 -0.03575 168 GLU   A C     
1377 O  O     . GLU   A 169 ? 0.48595 0.54257 0.68460 0.14507  -0.30750 -0.06196 168 GLU   A O     
1378 C  CB    . GLU   A 169 ? 0.46676 0.48552 0.56852 0.13820  -0.25498 0.03654  168 GLU   A CB    
1379 C  CG    . GLU   A 169 ? 0.54356 0.48136 0.59993 0.15632  -0.23536 0.05816  168 GLU   A CG    
1380 C  CD    . GLU   A 169 ? 0.58223 0.46586 0.64034 0.17400  -0.19635 0.06998  168 GLU   A CD    
1381 O  OE1   . GLU   A 169 ? 0.56548 0.46755 0.64267 0.18286  -0.20653 0.06990  168 GLU   A OE1   
1382 O  OE2   . GLU   A 169 ? 0.62639 0.47349 0.66447 0.12007  -0.16778 0.06189  168 GLU   A OE2   
1383 N  N     . LYS   A 170 ? 0.42235 0.57865 0.73742 0.04547  -0.26114 -0.06030 169 LYS   A N     
1384 C  CA    . LYS   A 170 ? 0.54073 0.61811 0.84686 0.00258  -0.11597 -0.07467 169 LYS   A CA    
1385 C  C     . LYS   A 170 ? 0.67369 0.63898 0.95311 -0.00669 -0.01641 -0.10037 169 LYS   A C     
1386 O  O     . LYS   A 170 ? 0.73391 0.66286 0.98662 -0.02594 -0.01000 -0.10152 169 LYS   A O     
1387 C  CB    . LYS   A 170 ? 0.58450 0.63003 0.83328 -0.03343 -0.06423 -0.07036 169 LYS   A CB    
1388 C  CG    . LYS   A 170 ? 0.63496 0.63158 0.82913 -0.06335 -0.01691 -0.06919 169 LYS   A CG    
1389 C  CD    . LYS   A 170 ? 0.67504 0.63308 0.82294 -0.08170 0.01338  -0.05597 169 LYS   A CD    
1390 C  CE    . LYS   A 170 ? 0.70710 0.63926 0.83283 -0.09805 0.04452  -0.03906 169 LYS   A CE    
1391 N  NZ    . LYS   A 170 ? 0.71215 0.64739 0.83325 -0.09404 0.06133  -0.03601 169 LYS   A NZ    
1392 O  OXT   . LYS   A 170 ? 0.70085 0.62474 0.99088 0.00649  0.06570  -0.12603 169 LYS   A OXT   
1393 N  N     . SER   B 1   ? 0.82920 0.46403 0.57472 0.01575  0.04393  0.18724  0   SER   B N     
1394 C  CA    . SER   B 1   ? 0.67556 0.43880 0.50613 0.01459  0.10235  0.22496  0   SER   B CA    
1395 C  C     . SER   B 1   ? 0.52417 0.41158 0.46320 0.00485  0.08761  0.18084  0   SER   B C     
1396 O  O     . SER   B 1   ? 0.51926 0.43186 0.46840 -0.00708 0.02963  0.20300  0   SER   B O     
1397 C  CB    . SER   B 1   ? 0.69476 0.46364 0.54257 0.01024  0.13969  0.18970  0   SER   B CB    
1398 O  OG    . SER   B 1   ? 0.67363 0.46707 0.55794 0.01877  0.14673  0.11594  0   SER   B OG    
1399 N  N     . MET   B 2   ? 0.34828 0.37561 0.36417 0.03700  0.13186  0.12825  1   MET   B N     
1400 C  CA    . MET   B 2   ? 0.23566 0.30259 0.29436 0.05833  0.08495  0.09831  1   MET   B CA    
1401 C  C     . MET   B 2   ? 0.25342 0.22876 0.16827 0.03588  0.05039  0.02362  1   MET   B C     
1402 O  O     . MET   B 2   ? 0.24247 0.23512 0.15456 -0.02441 0.01064  0.00655  1   MET   B O     
1403 C  CB    . MET   B 2   ? 0.36899 0.33641 0.37532 0.11321  -0.00072 0.10520  1   MET   B CB    
1404 C  CG    . MET   B 2   ? 0.31162 0.35392 0.38594 0.15083  -0.00577 0.12934  1   MET   B CG    
1405 S  SD    . MET   B 2   ? 0.36417 0.41487 0.41931 0.11428  0.07838  0.13606  1   MET   B SD    
1406 C  CE    . MET   B 2   ? 0.42482 0.45476 0.50525 0.10337  0.08224  0.12676  1   MET   B CE    
1407 N  N     . THR   B 3   ? 0.20927 0.18105 0.16650 -0.03616 -0.00983 0.03081  2   THR   B N     
1408 C  CA    . THR   B 3   ? 0.15076 0.19962 0.17843 -0.01648 0.02806  0.03004  2   THR   B CA    
1409 C  C     . THR   B 3   ? 0.13861 0.19177 0.16152 -0.00991 0.02454  0.00580  2   THR   B C     
1410 O  O     . THR   B 3   ? 0.16575 0.22404 0.24105 0.02030  0.02945  0.03552  2   THR   B O     
1411 C  CB    . THR   B 3   ? 0.20539 0.24180 0.21623 -0.03215 0.06362  -0.00515 2   THR   B CB    
1412 O  OG1   . THR   B 3   ? 0.26469 0.27906 0.23530 -0.01605 0.03835  -0.03912 2   THR   B OG1   
1413 C  CG2   . THR   B 3   ? 0.19573 0.27056 0.24130 -0.04579 0.03627  -0.00920 2   THR   B CG2   
1414 N  N     . GLU   B 4   ? 0.17829 0.17485 0.14464 -0.01533 0.00297  0.03942  3   GLU   B N     
1415 C  CA    . GLU   B 4   ? 0.16949 0.15900 0.16161 -0.00887 0.02106  0.02934  3   GLU   B CA    
1416 C  C     . GLU   B 4   ? 0.15202 0.18588 0.14910 0.00016  -0.00195 0.01693  3   GLU   B C     
1417 O  O     . GLU   B 4   ? 0.15666 0.22029 0.16284 0.01060  0.01194  0.01681  3   GLU   B O     
1418 C  CB    . GLU   B 4   ? 0.16831 0.17159 0.22337 -0.01215 0.01467  -0.03357 3   GLU   B CB    
1419 C  CG    . GLU   B 4   ? 0.20634 0.18392 0.20510 -0.02791 -0.01383 -0.03884 3   GLU   B CG    
1420 C  CD    . GLU   B 4   ? 0.22500 0.22609 0.25219 -0.06581 -0.04059 -0.02545 3   GLU   B CD    
1421 O  OE1   . GLU   B 4   ? 0.31698 0.23554 0.21857 -0.03923 -0.01345 -0.02789 3   GLU   B OE1   
1422 O  OE2   . GLU   B 4   ? 0.33179 0.25263 0.28588 -0.09333 -0.06879 0.00039  3   GLU   B OE2   
1423 N  N     . TYR   B 5   ? 0.15012 0.16545 0.13909 -0.01636 0.01393  -0.00893 4   TYR   B N     
1424 C  CA    . TYR   B 5   ? 0.21394 0.19839 0.12567 -0.02137 0.00126  0.02316  4   TYR   B CA    
1425 C  C     . TYR   B 5   ? 0.13962 0.20726 0.15259 0.01785  -0.01098 0.00538  4   TYR   B C     
1426 O  O     . TYR   B 5   ? 0.15143 0.20857 0.17289 -0.00245 -0.01848 0.03983  4   TYR   B O     
1427 C  CB    . TYR   B 5   ? 0.22890 0.21804 0.13580 -0.03925 -0.01731 -0.00204 4   TYR   B CB    
1428 C  CG    . TYR   B 5   ? 0.15795 0.24591 0.10471 -0.04213 -0.00122 -0.01213 4   TYR   B CG    
1429 C  CD1   . TYR   B 5   ? 0.17702 0.27511 0.16168 -0.02963 -0.00740 0.01189  4   TYR   B CD1   
1430 C  CD2   . TYR   B 5   ? 0.16878 0.23792 0.18941 -0.01921 0.02132  0.01082  4   TYR   B CD2   
1431 C  CE1   . TYR   B 5   ? 0.18242 0.26800 0.17415 -0.03856 0.01443  0.01598  4   TYR   B CE1   
1432 C  CE2   . TYR   B 5   ? 0.16639 0.23864 0.25049 0.02122  0.01556  -0.00591 4   TYR   B CE2   
1433 C  CZ    . TYR   B 5   ? 0.19210 0.24169 0.17707 -0.00101 0.03009  0.00905  4   TYR   B CZ    
1434 O  OH    . TYR   B 5   ? 0.17254 0.21772 0.20095 -0.00922 -0.00218 0.01880  4   TYR   B OH    
1435 N  N     A LYS   B 6   ? 0.10975 0.23177 0.13782 0.01261  0.05156  0.01245  5   LYS   B N     
1436 N  N     B LYS   B 6   ? 0.18914 0.21161 0.17390 0.00508  -0.04604 0.02977  5   LYS   B N     
1437 C  CA    A LYS   B 6   ? 0.14228 0.23530 0.14281 -0.00650 0.03353  0.05449  5   LYS   B CA    
1438 C  CA    B LYS   B 6   ? 0.19749 0.19591 0.18400 0.01802  -0.06011 0.03224  5   LYS   B CA    
1439 C  C     A LYS   B 6   ? 0.17000 0.22639 0.13534 0.01046  0.01277  0.03110  5   LYS   B C     
1440 C  C     B LYS   B 6   ? 0.19598 0.19803 0.15380 0.00140  -0.04038 0.03641  5   LYS   B C     
1441 O  O     A LYS   B 6   ? 0.16382 0.24778 0.13945 0.03317  0.02327  0.01753  5   LYS   B O     
1442 O  O     B LYS   B 6   ? 0.18311 0.21414 0.17000 -0.01900 -0.02877 0.02935  5   LYS   B O     
1443 C  CB    A LYS   B 6   ? 0.16376 0.26425 0.14410 -0.01938 0.03191  0.04202  5   LYS   B CB    
1444 C  CB    B LYS   B 6   ? 0.25439 0.18927 0.20570 0.03004  -0.06254 -0.02159 5   LYS   B CB    
1445 C  CG    A LYS   B 6   ? 0.23559 0.32222 0.21482 0.01130  -0.00821 0.00472  5   LYS   B CG    
1446 C  CG    B LYS   B 6   ? 0.31682 0.22394 0.26202 0.00731  -0.12316 -0.02365 5   LYS   B CG    
1447 C  CD    A LYS   B 6   ? 0.31449 0.34795 0.24199 0.04655  0.00548  0.03209  5   LYS   B CD    
1448 C  CD    B LYS   B 6   ? 0.44322 0.23542 0.31358 0.02223  -0.11851 -0.00968 5   LYS   B CD    
1449 C  CE    A LYS   B 6   ? 0.32737 0.35955 0.25054 0.07325  -0.00212 0.02731  5   LYS   B CE    
1450 C  CE    B LYS   B 6   ? 0.50337 0.23369 0.38345 0.02676  -0.10576 -0.02916 5   LYS   B CE    
1451 N  NZ    A LYS   B 6   ? 0.32707 0.37176 0.25114 0.10104  0.08465  -0.01290 5   LYS   B NZ    
1452 N  NZ    B LYS   B 6   ? 0.55365 0.24469 0.42122 -0.00220 -0.10811 -0.03499 5   LYS   B NZ    
1453 N  N     . LEU   B 7   ? 0.16559 0.21119 0.14101 0.00029  -0.01400 0.00746  6   LEU   B N     
1454 C  CA    . LEU   B 7   ? 0.18661 0.19303 0.13568 -0.00822 0.00870  0.02500  6   LEU   B CA    
1455 C  C     . LEU   B 7   ? 0.14887 0.20902 0.15437 -0.02826 0.01660  0.02541  6   LEU   B C     
1456 O  O     . LEU   B 7   ? 0.19070 0.26241 0.17901 -0.07571 -0.02280 0.04450  6   LEU   B O     
1457 C  CB    . LEU   B 7   ? 0.21880 0.18190 0.15948 -0.01964 0.03318  0.04432  6   LEU   B CB    
1458 C  CG    . LEU   B 7   ? 0.17370 0.16678 0.16670 -0.02000 0.01958  0.00509  6   LEU   B CG    
1459 C  CD1   . LEU   B 7   ? 0.18918 0.17388 0.23393 0.00204  0.05234  -0.01358 6   LEU   B CD1   
1460 C  CD2   . LEU   B 7   ? 0.23728 0.21424 0.17973 -0.07487 0.01178  -0.00922 6   LEU   B CD2   
1461 N  N     . VAL   B 8   ? 0.17311 0.19504 0.12047 0.03307  0.04157  0.01612  7   VAL   B N     
1462 C  CA    . VAL   B 8   ? 0.19977 0.20460 0.14625 0.00319  0.05723  0.03029  7   VAL   B CA    
1463 C  C     . VAL   B 8   ? 0.17469 0.18848 0.14362 -0.00436 0.06849  0.02664  7   VAL   B C     
1464 O  O     . VAL   B 8   ? 0.18609 0.20810 0.16926 -0.01332 0.02234  0.00552  7   VAL   B O     
1465 C  CB    . VAL   B 8   ? 0.18452 0.20423 0.16908 0.00618  -0.00194 0.03417  7   VAL   B CB    
1466 C  CG1   . VAL   B 8   ? 0.18297 0.18679 0.18589 -0.01272 0.01005  0.04942  7   VAL   B CG1   
1467 C  CG2   . VAL   B 8   ? 0.17883 0.20475 0.15178 0.03139  -0.00195 0.01719  7   VAL   B CG2   
1468 N  N     . VAL   B 9   ? 0.16365 0.19557 0.16556 0.01701  0.06669  0.04745  8   VAL   B N     
1469 C  CA    . VAL   B 9   ? 0.17765 0.21064 0.14325 0.00522  0.05703  0.03132  8   VAL   B CA    
1470 C  C     . VAL   B 9   ? 0.22826 0.19005 0.14607 -0.00471 0.06485  0.01049  8   VAL   B C     
1471 O  O     . VAL   B 9   ? 0.24821 0.18162 0.17727 -0.01884 0.04961  0.01735  8   VAL   B O     
1472 C  CB    . VAL   B 9   ? 0.18558 0.21074 0.17914 0.03055  0.03402  0.03589  8   VAL   B CB    
1473 C  CG1   . VAL   B 9   ? 0.20462 0.23764 0.18765 0.00706  0.05692  0.00521  8   VAL   B CG1   
1474 C  CG2   . VAL   B 9   ? 0.24988 0.23053 0.19793 0.04180  0.04297  0.05930  8   VAL   B CG2   
1475 N  N     . VAL   B 10  ? 0.23355 0.19936 0.14502 -0.01717 0.04138  -0.00040 9   VAL   B N     
1476 C  CA    . VAL   B 10  ? 0.22620 0.21615 0.15205 0.00889  0.04372  0.00555  9   VAL   B CA    
1477 C  C     . VAL   B 10  ? 0.21506 0.20981 0.15801 0.00923  0.03848  0.02971  9   VAL   B C     
1478 O  O     . VAL   B 10  ? 0.23814 0.20051 0.18149 -0.00190 0.05926  -0.00764 9   VAL   B O     
1479 C  CB    . VAL   B 10  ? 0.19153 0.25941 0.16711 -0.00963 0.04082  0.00521  9   VAL   B CB    
1480 C  CG1   . VAL   B 10  ? 0.24569 0.25098 0.14510 0.05919  0.05212  -0.01423 9   VAL   B CG1   
1481 C  CG2   . VAL   B 10  ? 0.22953 0.28424 0.19315 -0.03945 0.02673  0.04298  9   VAL   B CG2   
1482 N  N     . GLY   B 11  ? 0.24774 0.23020 0.15918 -0.00962 0.05063  0.00882  10  GLY   B N     
1483 C  CA    . GLY   B 11  ? 0.23490 0.23566 0.14160 -0.04304 0.05151  -0.01040 10  GLY   B CA    
1484 C  C     . GLY   B 11  ? 0.25099 0.22672 0.12893 0.00011  0.03346  0.00251  10  GLY   B C     
1485 O  O     . GLY   B 11  ? 0.28843 0.22580 0.15951 -0.02482 0.05710  -0.01125 10  GLY   B O     
1486 N  N     . ALA   B 12  ? 0.27502 0.24151 0.16617 -0.02082 0.05417  0.00660  11  ALA   B N     
1487 C  CA    . ALA   B 12  ? 0.24715 0.24227 0.16893 -0.02823 0.05137  0.00220  11  ALA   B CA    
1488 C  C     . ALA   B 12  ? 0.28372 0.23900 0.18440 -0.01588 0.08790  0.04424  11  ALA   B C     
1489 O  O     . ALA   B 12  ? 0.31415 0.24103 0.17258 -0.00820 0.07318  0.05998  11  ALA   B O     
1490 C  CB    . ALA   B 12  ? 0.33838 0.26552 0.15081 -0.02977 0.09811  0.00914  11  ALA   B CB    
1491 N  N     . CYS   B 13  ? 0.26415 0.25657 0.18833 -0.01627 0.07879  0.03972  12  CYS   B N     
1492 C  CA    . CYS   B 13  ? 0.23787 0.28365 0.22558 0.00617  0.06781  0.04722  12  CYS   B CA    
1493 C  C     . CYS   B 13  ? 0.29142 0.27416 0.26476 0.01141  0.12505  0.04535  12  CYS   B C     
1494 O  O     . CYS   B 13  ? 0.30416 0.26922 0.26884 0.01268  0.11530  0.03629  12  CYS   B O     
1495 C  CB    . CYS   B 13  ? 0.29651 0.33262 0.23180 -0.05102 0.04571  0.05239  12  CYS   B CB    
1496 S  SG    . CYS   B 13  ? 0.53630 0.39652 0.31626 -0.14378 0.06111  0.07426  12  CYS   B SG    
1497 N  N     . GLY   B 14  ? 0.30181 0.28451 0.26192 0.03349  0.11534  0.05933  13  GLY   B N     
1498 C  CA    . GLY   B 14  ? 0.24154 0.29338 0.31870 0.06608  0.15359  0.06472  13  GLY   B CA    
1499 C  C     . GLY   B 14  ? 0.24707 0.26529 0.33825 0.01773  0.16361  0.05847  13  GLY   B C     
1500 O  O     . GLY   B 14  ? 0.31877 0.27824 0.39712 0.02926  0.18356  0.04797  13  GLY   B O     
1501 N  N     . VAL   B 15  ? 0.27227 0.25615 0.24681 0.00612  0.10723  0.04951  14  VAL   B N     
1502 C  CA    . VAL   B 15  ? 0.32018 0.23979 0.22408 -0.00125 0.08476  0.03506  14  VAL   B CA    
1503 C  C     . VAL   B 15  ? 0.29349 0.23578 0.26545 0.02198  0.13186  0.02212  14  VAL   B C     
1504 O  O     . VAL   B 15  ? 0.37655 0.24049 0.30165 0.05245  0.14623  0.01175  14  VAL   B O     
1505 C  CB    . VAL   B 15  ? 0.27027 0.23617 0.18522 0.01572  0.09115  0.02361  14  VAL   B CB    
1506 C  CG1   . VAL   B 15  ? 0.29886 0.27013 0.24939 -0.00120 0.10017  0.02564  14  VAL   B CG1   
1507 C  CG2   . VAL   B 15  ? 0.25862 0.26073 0.17885 -0.01333 0.05009  0.02898  14  VAL   B CG2   
1508 N  N     . GLY   B 16  ? 0.25867 0.25241 0.25223 0.01394  0.12033  0.01641  15  GLY   B N     
1509 C  CA    . GLY   B 16  ? 0.30026 0.26047 0.22268 0.08977  0.13787  0.03593  15  GLY   B CA    
1510 C  C     . GLY   B 16  ? 0.27687 0.23688 0.24668 0.07051  0.10874  0.06111  15  GLY   B C     
1511 O  O     . GLY   B 16  ? 0.28865 0.26843 0.25946 0.08013  0.09135  0.07151  15  GLY   B O     
1512 N  N     . LYS   B 17  ? 0.24600 0.21522 0.23156 0.06184  0.10652  0.06454  16  LYS   B N     
1513 C  CA    . LYS   B 17  ? 0.26304 0.22153 0.23451 0.06311  0.09561  0.03733  16  LYS   B CA    
1514 C  C     . LYS   B 17  ? 0.22345 0.25621 0.22610 0.04194  0.09402  0.01688  16  LYS   B C     
1515 O  O     . LYS   B 17  ? 0.26287 0.25298 0.21869 0.02383  0.06459  0.03439  16  LYS   B O     
1516 C  CB    . LYS   B 17  ? 0.19126 0.20005 0.21915 0.03948  0.08991  0.03066  16  LYS   B CB    
1517 C  CG    . LYS   B 17  ? 0.22991 0.23317 0.20371 -0.03327 0.04399  0.04390  16  LYS   B CG    
1518 C  CD    . LYS   B 17  ? 0.26499 0.22945 0.23783 0.00074  0.05066  0.05628  16  LYS   B CD    
1519 C  CE    . LYS   B 17  ? 0.24982 0.24443 0.23922 0.00434  0.09365  0.05160  16  LYS   B CE    
1520 N  NZ    . LYS   B 17  ? 0.23160 0.22632 0.18302 0.01138  0.07317  0.03853  16  LYS   B NZ    
1521 N  N     . SER   B 18  ? 0.18167 0.25207 0.26323 0.01518  0.05401  0.03442  17  SER   B N     
1522 C  CA    . SER   B 18  ? 0.18361 0.24364 0.26180 0.00817  0.05417  0.04301  17  SER   B CA    
1523 C  C     . SER   B 18  ? 0.21277 0.25256 0.27325 0.05547  0.10426  0.05534  17  SER   B C     
1524 O  O     . SER   B 18  ? 0.25839 0.26995 0.26460 0.08357  0.07477  0.07538  17  SER   B O     
1525 C  CB    . SER   B 18  ? 0.19249 0.22634 0.25671 -0.00651 0.05200  0.03840  17  SER   B CB    
1526 O  OG    . SER   B 18  ? 0.22303 0.21760 0.23694 0.00983  0.02417  0.04073  17  SER   B OG    
1527 N  N     . ALA   B 19  ? 0.23821 0.24122 0.28939 0.08190  0.10540  0.04360  18  ALA   B N     
1528 C  CA    . ALA   B 19  ? 0.28846 0.24998 0.32809 0.09418  0.13289  0.06575  18  ALA   B CA    
1529 C  C     . ALA   B 19  ? 0.30408 0.25855 0.28916 0.09872  0.16323  0.08942  18  ALA   B C     
1530 O  O     . ALA   B 19  ? 0.29364 0.27356 0.32990 0.09501  0.09796  0.09546  18  ALA   B O     
1531 C  CB    . ALA   B 19  ? 0.37769 0.23719 0.34539 0.09910  0.15898  0.05924  18  ALA   B CB    
1532 N  N     . LEU   B 20  ? 0.27622 0.27641 0.28000 0.09394  0.13374  0.07590  19  LEU   B N     
1533 C  CA    . LEU   B 20  ? 0.31605 0.26048 0.26999 0.07792  0.11931  0.07494  19  LEU   B CA    
1534 C  C     . LEU   B 20  ? 0.28502 0.27291 0.28548 0.06999  0.12570  0.05778  19  LEU   B C     
1535 O  O     . LEU   B 20  ? 0.31327 0.28056 0.30229 0.08377  0.13406  0.06031  19  LEU   B O     
1536 C  CB    . LEU   B 20  ? 0.35435 0.23432 0.25699 0.08470  0.10668  0.02310  19  LEU   B CB    
1537 C  CG    . LEU   B 20  ? 0.34132 0.22177 0.25704 0.06876  0.09820  0.05013  19  LEU   B CG    
1538 C  CD1   . LEU   B 20  ? 0.35191 0.25912 0.27689 0.04466  0.12284  0.05569  19  LEU   B CD1   
1539 C  CD2   . LEU   B 20  ? 0.42472 0.21342 0.28007 0.09381  0.11593  0.05917  19  LEU   B CD2   
1540 N  N     . THR   B 21  ? 0.27641 0.27524 0.24723 0.07827  0.09099  0.04701  20  THR   B N     
1541 C  CA    . THR   B 21  ? 0.25905 0.30438 0.24002 0.07170  0.05738  0.05236  20  THR   B CA    
1542 C  C     . THR   B 21  ? 0.27830 0.29068 0.25198 0.12197  0.05916  0.06466  20  THR   B C     
1543 O  O     . THR   B 21  ? 0.30842 0.32142 0.24356 0.10325  0.06517  0.07993  20  THR   B O     
1544 C  CB    . THR   B 21  ? 0.24293 0.29735 0.21543 0.11048  0.02222  0.05112  20  THR   B CB    
1545 O  OG1   . THR   B 21  ? 0.24868 0.31018 0.25379 0.08113  0.06626  0.03073  20  THR   B OG1   
1546 C  CG2   . THR   B 21  ? 0.29434 0.29329 0.24118 0.08946  0.03416  0.05012  20  THR   B CG2   
1547 N  N     . ILE   B 22  ? 0.27864 0.31016 0.32052 0.11546  0.07530  0.08860  21  ILE   B N     
1548 C  CA    . ILE   B 22  ? 0.31335 0.34323 0.35902 0.10945  0.06478  0.10566  21  ILE   B CA    
1549 C  C     . ILE   B 22  ? 0.32847 0.37453 0.34416 0.12168  0.07367  0.12057  21  ILE   B C     
1550 O  O     . ILE   B 22  ? 0.36184 0.39321 0.32728 0.13565  0.00960  0.09889  21  ILE   B O     
1551 C  CB    . ILE   B 22  ? 0.28460 0.34774 0.40581 0.11139  0.06509  0.10810  21  ILE   B CB    
1552 C  CG1   . ILE   B 22  ? 0.29430 0.34737 0.46849 0.08216  0.06712  0.09942  21  ILE   B CG1   
1553 C  CG2   . ILE   B 22  ? 0.28052 0.36560 0.41918 0.10806  0.02326  0.10973  21  ILE   B CG2   
1554 C  CD1   . ILE   B 22  ? 0.39896 0.35707 0.53090 0.05329  0.05047  0.08865  21  ILE   B CD1   
1555 N  N     . GLN   B 23  ? 0.26625 0.37105 0.36456 0.13966  0.10659  0.14983  22  GLN   B N     
1556 C  CA    . GLN   B 23  ? 0.31525 0.37353 0.38000 0.14232  0.12076  0.16046  22  GLN   B CA    
1557 C  C     . GLN   B 23  ? 0.34516 0.38220 0.37089 0.17871  0.13727  0.16034  22  GLN   B C     
1558 O  O     . GLN   B 23  ? 0.40255 0.37924 0.40221 0.19977  0.11284  0.16262  22  GLN   B O     
1559 C  CB    . GLN   B 23  ? 0.30506 0.38927 0.39757 0.11428  0.11592  0.12198  22  GLN   B CB    
1560 C  CG    . GLN   B 23  ? 0.32298 0.40224 0.42229 0.13439  0.13224  0.11631  22  GLN   B CG    
1561 C  CD    . GLN   B 23  ? 0.38781 0.40848 0.42585 0.14383  0.10895  0.13974  22  GLN   B CD    
1562 O  OE1   . GLN   B 23  ? 0.38039 0.42363 0.43720 0.21482  0.10766  0.12225  22  GLN   B OE1   
1563 N  NE2   . GLN   B 23  ? 0.39116 0.40692 0.42966 0.11870  0.12306  0.16284  22  GLN   B NE2   
1564 N  N     . LEU   B 24  ? 0.32442 0.38893 0.37424 0.17433  0.15888  0.17218  23  LEU   B N     
1565 C  CA    . LEU   B 24  ? 0.32956 0.42685 0.39039 0.16920  0.16204  0.18726  23  LEU   B CA    
1566 C  C     . LEU   B 24  ? 0.34711 0.43473 0.35591 0.16197  0.13570  0.19671  23  LEU   B C     
1567 O  O     . LEU   B 24  ? 0.36796 0.46238 0.40368 0.17833  0.14855  0.18907  23  LEU   B O     
1568 C  CB    . LEU   B 24  ? 0.31924 0.43073 0.40375 0.12877  0.18239  0.14940  23  LEU   B CB    
1569 C  CG    . LEU   B 24  ? 0.34110 0.46315 0.40304 0.16809  0.17283  0.13296  23  LEU   B CG    
1570 C  CD1   . LEU   B 24  ? 0.39461 0.46330 0.42349 0.15679  0.11308  0.13647  23  LEU   B CD1   
1571 C  CD2   . LEU   B 24  ? 0.34885 0.48213 0.42634 0.16467  0.17992  0.06651  23  LEU   B CD2   
1572 N  N     . ILE   B 25  ? 0.43340 0.44938 0.35615 0.15469  0.04448  0.16802  24  ILE   B N     
1573 C  CA    . ILE   B 25  ? 0.46651 0.44710 0.37970 0.13402  0.04742  0.15377  24  ILE   B CA    
1574 C  C     . ILE   B 25  ? 0.49885 0.46942 0.39124 0.15238  0.00440  0.17778  24  ILE   B C     
1575 O  O     . ILE   B 25  ? 0.58830 0.48781 0.38568 0.16730  -0.01636 0.14608  24  ILE   B O     
1576 C  CB    . ILE   B 25  ? 0.41802 0.42286 0.35073 0.13848  0.04985  0.11232  24  ILE   B CB    
1577 C  CG1   . ILE   B 25  ? 0.35387 0.39435 0.36008 0.11311  0.07443  0.12191  24  ILE   B CG1   
1578 C  CG2   . ILE   B 25  ? 0.44933 0.43533 0.34146 0.11162  -0.01150 0.10597  24  ILE   B CG2   
1579 C  CD1   . ILE   B 25  ? 0.32513 0.36920 0.32983 0.08473  0.11264  0.13829  24  ILE   B CD1   
1580 N  N     . GLN   B 26  ? 0.48127 0.49513 0.40349 0.15319  -0.01452 0.19033  25  GLN   B N     
1581 C  CA    . GLN   B 26  ? 0.46525 0.51775 0.48574 0.14882  -0.02762 0.19124  25  GLN   B CA    
1582 C  C     . GLN   B 26  ? 0.42492 0.52529 0.51360 0.14737  -0.03522 0.21975  25  GLN   B C     
1583 O  O     . GLN   B 26  ? 0.41186 0.53927 0.54238 0.11369  -0.10243 0.18688  25  GLN   B O     
1584 C  CB    . GLN   B 26  ? 0.48034 0.53335 0.51521 0.13963  -0.00744 0.17849  25  GLN   B CB    
1585 C  CG    . GLN   B 26  ? 0.55570 0.54476 0.55323 0.13328  0.01006  0.16311  25  GLN   B CG    
1586 C  CD    . GLN   B 26  ? 0.63355 0.55435 0.59438 0.13329  0.03056  0.13380  25  GLN   B CD    
1587 O  OE1   . GLN   B 26  ? 0.69774 0.55389 0.61589 0.12460  0.04033  0.12247  25  GLN   B OE1   
1588 N  NE2   . GLN   B 26  ? 0.64332 0.56945 0.61081 0.14367  0.01691  0.13413  25  GLN   B NE2   
1589 N  N     . ASN   B 27  ? 0.40213 0.53414 0.48757 0.15996  0.02485  0.23475  26  ASN   B N     
1590 C  CA    . ASN   B 27  ? 0.38616 0.54520 0.48580 0.17406  0.07924  0.22175  26  ASN   B CA    
1591 C  C     . ASN   B 27  ? 0.34388 0.53140 0.48848 0.15128  0.10564  0.22251  26  ASN   B C     
1592 O  O     . ASN   B 27  ? 0.32276 0.52041 0.52210 0.16645  0.11857  0.26051  26  ASN   B O     
1593 C  CB    . ASN   B 27  ? 0.50591 0.57956 0.54540 0.14899  0.04330  0.20594  26  ASN   B CB    
1594 C  CG    . ASN   B 27  ? 0.71120 0.60543 0.61938 0.10968  0.00824  0.18262  26  ASN   B CG    
1595 O  OD1   . ASN   B 27  ? 0.79347 0.62393 0.63122 0.09673  0.03808  0.15858  26  ASN   B OD1   
1596 N  ND2   . ASN   B 27  ? 0.76185 0.60455 0.64483 0.11229  -0.02657 0.17779  26  ASN   B ND2   
1597 N  N     . HIS   B 28  ? 0.30626 0.51135 0.47784 0.11658  0.13916  0.20614  27  HIS   B N     
1598 C  CA    . HIS   B 28  ? 0.41137 0.51122 0.46992 0.12639  0.06209  0.18355  27  HIS   B CA    
1599 C  C     . HIS   B 28  ? 0.37768 0.47131 0.45312 0.15621  0.09226  0.17424  27  HIS   B C     
1600 O  O     . HIS   B 28  ? 0.38830 0.45732 0.43941 0.19569  0.09870  0.14954  27  HIS   B O     
1601 C  CB    . HIS   B 28  ? 0.55071 0.55745 0.51807 0.10239  -0.00993 0.13288  27  HIS   B CB    
1602 C  CG    . HIS   B 28  ? 0.69531 0.60160 0.55685 0.09416  -0.08123 0.08900  27  HIS   B CG    
1603 N  ND1   . HIS   B 28  ? 0.78225 0.62687 0.58067 0.08022  -0.09045 0.05405  27  HIS   B ND1   
1604 C  CD2   . HIS   B 28  ? 0.74756 0.61922 0.57333 0.09207  -0.09565 0.07327  27  HIS   B CD2   
1605 C  CE1   . HIS   B 28  ? 0.79744 0.63838 0.59274 0.08833  -0.10152 0.04594  27  HIS   B CE1   
1606 N  NE2   . HIS   B 28  ? 0.78980 0.63920 0.59658 0.08591  -0.10108 0.04947  27  HIS   B NE2   
1607 N  N     . PHE   B 29  ? 0.37629 0.47550 0.46326 0.10955  0.07628  0.15661  28  PHE   B N     
1608 C  CA    . PHE   B 29  ? 0.37455 0.45495 0.47535 0.09826  0.08833  0.15516  28  PHE   B CA    
1609 C  C     . PHE   B 29  ? 0.44408 0.46083 0.52352 0.03637  0.11447  0.17981  28  PHE   B C     
1610 O  O     . PHE   B 29  ? 0.43899 0.47147 0.56146 0.04030  0.09043  0.17790  28  PHE   B O     
1611 C  CB    . PHE   B 29  ? 0.41330 0.43124 0.45728 0.10647  0.12311  0.13254  28  PHE   B CB    
1612 C  CG    . PHE   B 29  ? 0.39911 0.41554 0.47351 0.10310  0.17114  0.08262  28  PHE   B CG    
1613 C  CD1   . PHE   B 29  ? 0.43344 0.39690 0.49493 0.13461  0.12268  0.03874  28  PHE   B CD1   
1614 C  CD2   . PHE   B 29  ? 0.36415 0.41264 0.47637 0.10629  0.22925  0.07362  28  PHE   B CD2   
1615 C  CE1   . PHE   B 29  ? 0.42538 0.40017 0.49529 0.13933  0.17274  0.04611  28  PHE   B CE1   
1616 C  CE2   . PHE   B 29  ? 0.38014 0.40827 0.47876 0.13459  0.19862  0.04073  28  PHE   B CE2   
1617 C  CZ    . PHE   B 29  ? 0.43655 0.40727 0.47602 0.11998  0.19444  0.04744  28  PHE   B CZ    
1618 N  N     . VAL   B 30  ? 0.44444 0.46716 0.52448 0.01832  0.15152  0.17747  29  VAL   B N     
1619 C  CA    . VAL   B 30  ? 0.56270 0.47526 0.56316 0.02092  0.13087  0.16527  29  VAL   B CA    
1620 C  C     . VAL   B 30  ? 0.58353 0.45493 0.59318 0.02260  0.18505  0.16450  29  VAL   B C     
1621 O  O     . VAL   B 30  ? 0.65174 0.43345 0.59206 -0.01557 0.18507  0.15391  29  VAL   B O     
1622 C  CB    . VAL   B 30  ? 0.58884 0.48559 0.56641 0.00555  0.08322  0.18523  29  VAL   B CB    
1623 C  CG1   . VAL   B 30  ? 0.59286 0.48924 0.55810 0.00420  0.04240  0.19050  29  VAL   B CG1   
1624 C  CG2   . VAL   B 30  ? 0.61543 0.49499 0.56228 -0.00324 0.02839  0.18366  29  VAL   B CG2   
1625 N  N     . ASP   B 31  ? 0.51594 0.46689 0.62848 0.08521  0.24547  0.15069  30  ASP   B N     
1626 C  CA    . ASP   B 31  ? 0.41164 0.47787 0.66579 0.12306  0.27606  0.11182  30  ASP   B CA    
1627 C  C     . ASP   B 31  ? 0.45339 0.45567 0.65645 0.06662  0.25594  0.13589  30  ASP   B C     
1628 O  O     . ASP   B 31  ? 0.46068 0.45317 0.64524 0.04303  0.30618  0.12000  30  ASP   B O     
1629 C  CB    . ASP   B 31  ? 0.45694 0.53118 0.72142 0.18410  0.26771  0.08113  30  ASP   B CB    
1630 C  CG    . ASP   B 31  ? 0.52791 0.56778 0.78013 0.21505  0.30047  0.10389  30  ASP   B CG    
1631 O  OD1   . ASP   B 31  ? 0.53940 0.59726 0.77325 0.19657  0.32777  0.10741  30  ASP   B OD1   
1632 O  OD2   . ASP   B 31  ? 0.56652 0.59172 0.83170 0.24126  0.27306  0.11041  30  ASP   B OD2   
1633 N  N     . GLU   B 32  ? 0.44821 0.42501 0.65924 0.02459  0.13098  0.14233  31  GLU   B N     
1634 C  CA    . GLU   B 32  ? 0.46025 0.40533 0.60708 0.00913  0.05261  0.14672  31  GLU   B CA    
1635 C  C     . GLU   B 32  ? 0.33643 0.36846 0.48055 0.03707  0.02254  0.16207  31  GLU   B C     
1636 O  O     . GLU   B 32  ? 0.38676 0.35903 0.42816 0.01974  0.04101  0.17644  31  GLU   B O     
1637 C  CB    . GLU   B 32  ? 0.58560 0.42661 0.66540 -0.03283 0.00918  0.14983  31  GLU   B CB    
1638 C  CG    . GLU   B 32  ? 0.66214 0.43727 0.71241 -0.07952 -0.01831 0.14905  31  GLU   B CG    
1639 C  CD    . GLU   B 32  ? 0.71977 0.44390 0.75869 -0.10060 -0.04483 0.14872  31  GLU   B CD    
1640 O  OE1   . GLU   B 32  ? 0.75867 0.45640 0.76975 -0.07116 -0.06969 0.15435  31  GLU   B OE1   
1641 O  OE2   . GLU   B 32  ? 0.69023 0.41979 0.75862 -0.14662 -0.06401 0.15727  31  GLU   B OE2   
1642 N  N     . TYR   B 33  ? 0.26172 0.35186 0.42167 0.04271  -0.00083 0.15519  32  TYR   B N     
1643 C  CA    . TYR   B 33  ? 0.22514 0.35493 0.33491 0.03841  0.04170  0.13538  32  TYR   B CA    
1644 C  C     . TYR   B 33  ? 0.22763 0.38395 0.29752 0.02184  0.06302  0.11497  32  TYR   B C     
1645 O  O     . TYR   B 33  ? 0.22705 0.39124 0.28701 -0.00771 0.04804  0.10678  32  TYR   B O     
1646 C  CB    . TYR   B 33  ? 0.23604 0.35467 0.30952 0.00717  0.03471  0.13571  32  TYR   B CB    
1647 C  CG    . TYR   B 33  ? 0.20928 0.36811 0.30930 -0.01642 0.02371  0.12697  32  TYR   B CG    
1648 C  CD1   . TYR   B 33  ? 0.17545 0.38641 0.33180 0.02243  0.01576  0.08829  32  TYR   B CD1   
1649 C  CD2   . TYR   B 33  ? 0.23166 0.38412 0.30428 0.05296  0.06778  0.08847  32  TYR   B CD2   
1650 C  CE1   . TYR   B 33  ? 0.24601 0.35920 0.28978 0.03898  0.00398  0.10353  32  TYR   B CE1   
1651 C  CE2   . TYR   B 33  ? 0.21835 0.38256 0.34312 0.09672  0.05716  0.07252  32  TYR   B CE2   
1652 C  CZ    . TYR   B 33  ? 0.22575 0.36146 0.29879 0.04187  0.04077  0.12790  32  TYR   B CZ    
1653 O  OH    . TYR   B 33  ? 0.28624 0.37162 0.24476 0.02483  0.04101  0.09186  32  TYR   B OH    
1654 N  N     . ASP   B 34  ? 0.16796 0.38022 0.28666 0.06469  0.05555  0.11815  33  ASP   B N     
1655 C  CA    . ASP   B 34  ? 0.22707 0.38654 0.24223 0.07680  0.01683  0.10653  33  ASP   B CA    
1656 C  C     . ASP   B 34  ? 0.19139 0.36065 0.23144 0.07064  0.05194  0.12133  33  ASP   B C     
1657 O  O     . ASP   B 34  ? 0.17630 0.36303 0.22176 0.02141  0.02448  0.13054  33  ASP   B O     
1658 C  CB    . ASP   B 34  ? 0.20265 0.42758 0.26264 0.06156  0.00305  0.09189  33  ASP   B CB    
1659 C  CG    . ASP   B 34  ? 0.24544 0.46731 0.30142 0.03360  -0.03085 0.08482  33  ASP   B CG    
1660 O  OD1   . ASP   B 34  ? 0.24669 0.48682 0.32032 0.01055  -0.02952 0.04985  33  ASP   B OD1   
1661 O  OD2   . ASP   B 34  ? 0.40151 0.49011 0.33335 0.02246  -0.01243 0.10547  33  ASP   B OD2   
1662 N  N     . PRO   B 35  ? 0.17637 0.34953 0.25500 0.04438  0.04891  0.13508  34  PRO   B N     
1663 C  CA    . PRO   B 35  ? 0.16643 0.33389 0.24589 0.06841  0.05024  0.11805  34  PRO   B CA    
1664 C  C     . PRO   B 35  ? 0.16744 0.33264 0.23199 0.02282  -0.01249 0.08176  34  PRO   B C     
1665 O  O     . PRO   B 35  ? 0.19133 0.37111 0.27937 -0.01506 0.03251  0.06753  34  PRO   B O     
1666 C  CB    . PRO   B 35  ? 0.19616 0.33555 0.26670 0.07379  0.04819  0.13016  34  PRO   B CB    
1667 C  CG    . PRO   B 35  ? 0.20960 0.34967 0.29413 0.05493  0.05522  0.13734  34  PRO   B CG    
1668 C  CD    . PRO   B 35  ? 0.22047 0.35464 0.28760 0.04235  0.07365  0.13037  34  PRO   B CD    
1669 N  N     . THR   B 36  ? 0.13605 0.26820 0.23321 0.01514  0.02831  0.07391  35  THR   B N     
1670 C  CA    . THR   B 36  ? 0.18639 0.27154 0.22687 0.00670  0.07187  0.06383  35  THR   B CA    
1671 C  C     . THR   B 36  ? 0.14510 0.28259 0.16034 0.02682  0.01456  0.07353  35  THR   B C     
1672 O  O     . THR   B 36  ? 0.13087 0.31193 0.21022 0.00803  0.00605  0.07250  35  THR   B O     
1673 C  CB    . THR   B 36  ? 0.16483 0.25223 0.24314 0.00436  0.06276  0.02542  35  THR   B CB    
1674 O  OG1   . THR   B 36  ? 0.18240 0.25057 0.24696 -0.00141 0.00440  0.04080  35  THR   B OG1   
1675 C  CG2   . THR   B 36  ? 0.16467 0.23960 0.23433 0.00317  0.03874  0.03495  35  THR   B CG2   
1676 N  N     . ILE   B 37  ? 0.16586 0.26922 0.17702 0.02495  0.01871  0.05743  36  ILE   B N     
1677 C  CA    . ILE   B 37  ? 0.14681 0.25671 0.17734 -0.01213 0.03446  0.05390  36  ILE   B CA    
1678 C  C     . ILE   B 37  ? 0.15493 0.23971 0.15307 -0.03689 -0.00472 0.06440  36  ILE   B C     
1679 O  O     . ILE   B 37  ? 0.13061 0.28615 0.19816 -0.01285 -0.00987 0.05316  36  ILE   B O     
1680 C  CB    . ILE   B 37  ? 0.17882 0.26226 0.22297 -0.05624 0.02777  0.03915  36  ILE   B CB    
1681 C  CG1   . ILE   B 37  ? 0.18400 0.31700 0.26429 -0.06735 -0.00416 0.07895  36  ILE   B CG1   
1682 C  CG2   . ILE   B 37  ? 0.23359 0.24454 0.23759 -0.03582 0.02862  0.01299  36  ILE   B CG2   
1683 C  CD1   . ILE   B 37  ? 0.19350 0.33616 0.29910 -0.06523 -0.01452 0.09055  36  ILE   B CD1   
1684 N  N     . GLU   B 38  ? 0.15621 0.25046 0.18726 -0.01241 0.03292  0.08570  37  GLU   B N     
1685 C  CA    . GLU   B 38  ? 0.15026 0.24962 0.16482 0.01340  0.03036  0.05835  37  GLU   B CA    
1686 C  C     . GLU   B 38  ? 0.15122 0.24806 0.17757 -0.03039 0.01809  0.08375  37  GLU   B C     
1687 O  O     . GLU   B 38  ? 0.17366 0.28383 0.20220 -0.05339 -0.01029 0.04781  37  GLU   B O     
1688 C  CB    . GLU   B 38  ? 0.13885 0.25309 0.20277 0.01217  0.01193  0.04572  37  GLU   B CB    
1689 C  CG    . GLU   B 38  ? 0.13623 0.26529 0.21156 -0.02319 0.02753  0.03298  37  GLU   B CG    
1690 C  CD    . GLU   B 38  ? 0.14689 0.27048 0.23278 -0.01344 0.04777  0.01258  37  GLU   B CD    
1691 O  OE1   . GLU   B 38  ? 0.19361 0.26850 0.24855 0.00191  -0.02054 -0.00856 37  GLU   B OE1   
1692 O  OE2   . GLU   B 38  ? 0.20125 0.26791 0.19126 -0.01201 0.03783  0.00854  37  GLU   B OE2   
1693 N  N     . ASP   B 39  ? 0.19464 0.24357 0.19239 -0.00756 0.01351  0.07573  38  ASP   B N     
1694 C  CA    . ASP   B 39  ? 0.16591 0.26828 0.23487 -0.00425 0.00048  0.08934  38  ASP   B CA    
1695 C  C     . ASP   B 39  ? 0.14946 0.24828 0.21130 -0.02378 0.02265  0.04662  38  ASP   B C     
1696 O  O     . ASP   B 39  ? 0.16228 0.23585 0.19130 -0.02992 0.02643  0.03304  38  ASP   B O     
1697 C  CB    . ASP   B 39  ? 0.14195 0.29088 0.30495 -0.00726 -0.00609 0.08927  38  ASP   B CB    
1698 C  CG    . ASP   B 39  ? 0.16826 0.33811 0.32470 0.00131  0.00860  0.08005  38  ASP   B CG    
1699 O  OD1   . ASP   B 39  ? 0.23504 0.33656 0.36749 -0.04839 -0.01404 0.11739  38  ASP   B OD1   
1700 O  OD2   . ASP   B 39  ? 0.25293 0.38595 0.33019 0.01473  0.08154  0.09269  38  ASP   B OD2   
1701 N  N     . SER   B 40  ? 0.18907 0.25444 0.19842 -0.01348 -0.00874 0.06641  39  SER   B N     
1702 C  CA    . SER   B 40  ? 0.18484 0.25735 0.23312 0.00035  0.03453  0.10657  39  SER   B CA    
1703 C  C     . SER   B 40  ? 0.19512 0.26903 0.21664 -0.01168 0.01898  0.10645  39  SER   B C     
1704 O  O     . SER   B 40  ? 0.21701 0.31382 0.25929 -0.04073 -0.02692 0.09073  39  SER   B O     
1705 C  CB    . SER   B 40  ? 0.26954 0.25451 0.25086 0.06168  0.05515  0.10245  39  SER   B CB    
1706 O  OG    . SER   B 40  ? 0.30609 0.27019 0.32578 0.04209  0.05447  0.08208  39  SER   B OG    
1707 N  N     . TYR   B 41  ? 0.21667 0.28322 0.20767 -0.01360 0.02232  0.12843  40  TYR   B N     
1708 C  CA    . TYR   B 41  ? 0.24127 0.28021 0.27032 -0.00790 0.01377  0.14457  40  TYR   B CA    
1709 C  C     . TYR   B 41  ? 0.20111 0.28070 0.24685 -0.03276 -0.03412 0.11907  40  TYR   B C     
1710 O  O     . TYR   B 41  ? 0.14942 0.33385 0.21826 -0.03692 -0.02438 0.10551  40  TYR   B O     
1711 C  CB    . TYR   B 41  ? 0.18705 0.29726 0.34390 0.01620  0.03389  0.13450  40  TYR   B CB    
1712 C  CG    . TYR   B 41  ? 0.17973 0.33187 0.34802 0.05027  0.02663  0.13462  40  TYR   B CG    
1713 C  CD1   . TYR   B 41  ? 0.21568 0.35520 0.33587 0.01659  0.07202  0.11601  40  TYR   B CD1   
1714 C  CD2   . TYR   B 41  ? 0.24303 0.39705 0.34807 0.01686  -0.02208 0.16074  40  TYR   B CD2   
1715 C  CE1   . TYR   B 41  ? 0.16659 0.39357 0.38528 0.01333  0.05757  0.13024  40  TYR   B CE1   
1716 C  CE2   . TYR   B 41  ? 0.24072 0.42880 0.40717 0.00125  -0.00384 0.17140  40  TYR   B CE2   
1717 C  CZ    . TYR   B 41  ? 0.19393 0.43675 0.39737 -0.00092 0.03092  0.17966  40  TYR   B CZ    
1718 O  OH    . TYR   B 41  ? 0.21855 0.48778 0.42347 -0.01651 0.03792  0.18840  40  TYR   B OH    
1719 N  N     . ARG   B 42  ? 0.17406 0.26758 0.24468 -0.04422 -0.03116 0.11152  41  ARG   B N     
1720 C  CA    . ARG   B 42  ? 0.22152 0.26093 0.22367 -0.07228 -0.01973 0.07282  41  ARG   B CA    
1721 C  C     . ARG   B 42  ? 0.19893 0.26245 0.20637 -0.05234 -0.00587 0.07292  41  ARG   B C     
1722 O  O     . ARG   B 42  ? 0.20857 0.27263 0.21782 -0.04528 -0.04612 0.09064  41  ARG   B O     
1723 C  CB    . ARG   B 42  ? 0.27436 0.26610 0.23477 -0.05259 -0.04535 0.04416  41  ARG   B CB    
1724 C  CG    . ARG   B 42  ? 0.28959 0.27019 0.22890 -0.07325 -0.02278 0.02679  41  ARG   B CG    
1725 C  CD    . ARG   B 42  ? 0.30265 0.29637 0.24881 -0.08716 -0.03351 0.02288  41  ARG   B CD    
1726 N  NE    . ARG   B 42  ? 0.25948 0.32204 0.28661 -0.09332 -0.01147 0.01495  41  ARG   B NE    
1727 C  CZ    . ARG   B 42  ? 0.24962 0.32188 0.29887 -0.06321 0.00318  0.02956  41  ARG   B CZ    
1728 N  NH1   . ARG   B 42  ? 0.28776 0.32035 0.34701 -0.02897 -0.06620 -0.02521 41  ARG   B NH1   
1729 N  NH2   . ARG   B 42  ? 0.23162 0.32056 0.32798 0.00523  0.00468  0.02690  41  ARG   B NH2   
1730 N  N     . LYS   B 43  ? 0.17297 0.23472 0.20571 -0.02304 0.03627  0.06615  42  LYS   B N     
1731 C  CA    . LYS   B 43  ? 0.15354 0.24152 0.21845 -0.01577 0.04673  0.08174  42  LYS   B CA    
1732 C  C     . LYS   B 43  ? 0.14780 0.24671 0.20467 -0.01300 0.01966  0.05101  42  LYS   B C     
1733 O  O     . LYS   B 43  ? 0.14113 0.28155 0.22677 0.01288  0.01298  0.07108  42  LYS   B O     
1734 C  CB    . LYS   B 43  ? 0.21061 0.25066 0.29912 -0.00946 0.09256  0.02565  42  LYS   B CB    
1735 C  CG    . LYS   B 43  ? 0.34321 0.27683 0.34810 0.01802  0.12013  0.04999  42  LYS   B CG    
1736 C  CD    . LYS   B 43  ? 0.40489 0.29457 0.39007 0.01545  0.15046  0.06895  42  LYS   B CD    
1737 C  CE    . LYS   B 43  ? 0.57508 0.31359 0.41164 0.02785  0.14445  0.09422  42  LYS   B CE    
1738 N  NZ    . LYS   B 43  ? 0.62855 0.33932 0.47681 0.02687  0.14551  0.11553  42  LYS   B NZ    
1739 N  N     . GLN   B 44  ? 0.15597 0.23628 0.18821 -0.04154 -0.00105 0.03937  43  GLN   B N     
1740 C  CA    . GLN   B 44  ? 0.18794 0.22191 0.16402 -0.04890 -0.01163 0.00824  43  GLN   B CA    
1741 C  C     . GLN   B 44  ? 0.18144 0.21621 0.19221 -0.00843 0.01017  0.00492  43  GLN   B C     
1742 O  O     . GLN   B 44  ? 0.18661 0.24436 0.28625 0.00576  -0.00159 -0.00229 43  GLN   B O     
1743 C  CB    . GLN   B 44  ? 0.18042 0.26585 0.16109 -0.04981 -0.00594 0.03417  43  GLN   B CB    
1744 C  CG    . GLN   B 44  ? 0.24799 0.30016 0.18538 -0.06007 -0.00378 0.03816  43  GLN   B CG    
1745 C  CD    . GLN   B 44  ? 0.43156 0.33975 0.21253 -0.08411 0.03946  0.05658  43  GLN   B CD    
1746 O  OE1   . GLN   B 44  ? 0.50926 0.37427 0.24699 -0.07136 -0.00336 0.04766  43  GLN   B OE1   
1747 N  NE2   . GLN   B 44  ? 0.52268 0.37981 0.24514 -0.10121 0.06903  0.04005  43  GLN   B NE2   
1748 N  N     . VAL   B 45  ? 0.17821 0.20603 0.21546 -0.03040 -0.01397 0.02206  44  VAL   B N     
1749 C  CA    . VAL   B 45  ? 0.16954 0.22166 0.23143 -0.01661 0.01198  0.00605  44  VAL   B CA    
1750 C  C     . VAL   B 45  ? 0.18052 0.19395 0.23832 -0.02286 0.01558  0.01631  44  VAL   B C     
1751 O  O     . VAL   B 45  ? 0.16895 0.18733 0.28819 -0.01119 0.02626  -0.00187 44  VAL   B O     
1752 C  CB    . VAL   B 45  ? 0.18558 0.27237 0.22448 -0.02208 0.06747  -0.00497 44  VAL   B CB    
1753 C  CG1   . VAL   B 45  ? 0.21413 0.32413 0.22264 -0.04559 0.02555  0.00861  44  VAL   B CG1   
1754 C  CG2   . VAL   B 45  ? 0.23817 0.28030 0.21323 0.03511  0.02866  -0.00096 44  VAL   B CG2   
1755 N  N     . VAL   B 46  ? 0.25582 0.17990 0.24283 -0.01950 0.01112  0.00542  45  VAL   B N     
1756 C  CA    . VAL   B 46  ? 0.21758 0.19628 0.24247 -0.02971 -0.03946 0.00500  45  VAL   B CA    
1757 C  C     . VAL   B 46  ? 0.17533 0.20824 0.22371 -0.00139 -0.01250 -0.00550 45  VAL   B C     
1758 O  O     . VAL   B 46  ? 0.20973 0.27047 0.26760 0.04458  -0.00219 -0.02395 45  VAL   B O     
1759 C  CB    . VAL   B 46  ? 0.21116 0.25786 0.29153 -0.02495 -0.10074 0.04445  45  VAL   B CB    
1760 C  CG1   . VAL   B 46  ? 0.24909 0.27375 0.30830 -0.04243 -0.05301 0.06953  45  VAL   B CG1   
1761 C  CG2   . VAL   B 46  ? 0.23319 0.26127 0.24299 0.00494  -0.02476 0.05225  45  VAL   B CG2   
1762 N  N     . ILE   B 47  ? 0.18922 0.18192 0.17527 -0.02109 0.03822  -0.00702 46  ILE   B N     
1763 C  CA    . ILE   B 47  ? 0.20452 0.19221 0.20195 -0.03443 0.03854  -0.01556 46  ILE   B CA    
1764 C  C     . ILE   B 47  ? 0.19784 0.15000 0.22883 -0.01290 0.05194  -0.02681 46  ILE   B C     
1765 O  O     . ILE   B 47  ? 0.19929 0.15754 0.23284 -0.01811 0.05644  -0.03109 46  ILE   B O     
1766 C  CB    . ILE   B 47  ? 0.19938 0.19863 0.21904 -0.04165 0.00065  -0.01020 46  ILE   B CB    
1767 C  CG1   . ILE   B 47  ? 0.18621 0.17744 0.22576 -0.02436 0.01708  0.02010  46  ILE   B CG1   
1768 C  CG2   . ILE   B 47  ? 0.19871 0.25510 0.19376 -0.06654 0.00727  -0.05753 46  ILE   B CG2   
1769 C  CD1   . ILE   B 47  ? 0.22026 0.20282 0.22664 -0.01953 -0.01666 0.02243  46  ILE   B CD1   
1770 N  N     . ASP   B 48  ? 0.24538 0.15174 0.24605 -0.01747 0.05273  -0.04003 47  ASP   B N     
1771 C  CA    . ASP   B 48  ? 0.19324 0.18519 0.28007 -0.03483 0.06478  -0.03462 47  ASP   B CA    
1772 C  C     . ASP   B 48  ? 0.22503 0.17048 0.30913 -0.07112 0.05520  -0.01323 47  ASP   B C     
1773 O  O     . ASP   B 48  ? 0.25839 0.19889 0.30184 -0.06606 0.03307  -0.02108 47  ASP   B O     
1774 C  CB    . ASP   B 48  ? 0.20638 0.19914 0.25567 0.00365  0.00285  -0.03060 47  ASP   B CB    
1775 C  CG    . ASP   B 48  ? 0.20889 0.19543 0.24904 0.00570  0.00308  -0.02725 47  ASP   B CG    
1776 O  OD1   . ASP   B 48  ? 0.27229 0.18205 0.29217 0.01231  0.02620  -0.02277 47  ASP   B OD1   
1777 O  OD2   . ASP   B 48  ? 0.30934 0.23948 0.21753 -0.01476 0.01836  -0.04410 47  ASP   B OD2   
1778 N  N     . GLY   B 49  ? 0.26320 0.15534 0.25166 -0.03237 0.00229  -0.01307 48  GLY   B N     
1779 C  CA    . GLY   B 49  ? 0.29603 0.17490 0.25616 -0.01570 -0.02117 0.00633  48  GLY   B CA    
1780 C  C     . GLY   B 49  ? 0.33630 0.18586 0.22476 -0.02460 0.04145  0.00737  48  GLY   B C     
1781 O  O     . GLY   B 49  ? 0.38880 0.23527 0.25493 -0.00470 0.05588  0.01127  48  GLY   B O     
1782 N  N     . GLU   B 50  ? 0.22532 0.15968 0.24264 0.00623  -0.00033 -0.01244 49  GLU   B N     
1783 C  CA    . GLU   B 50  ? 0.20536 0.17759 0.26532 -0.00687 0.03730  -0.02683 49  GLU   B CA    
1784 C  C     . GLU   B 50  ? 0.22008 0.19234 0.21178 -0.02505 0.05114  0.00520  49  GLU   B C     
1785 O  O     . GLU   B 50  ? 0.22168 0.23576 0.22885 -0.05262 0.03446  0.00403  49  GLU   B O     
1786 C  CB    . GLU   B 50  ? 0.22624 0.20665 0.42336 0.01044  0.09426  0.00916  49  GLU   B CB    
1787 C  CG    . GLU   B 50  ? 0.32366 0.27108 0.55587 0.01130  0.16010  0.05631  49  GLU   B CG    
1788 C  CD    . GLU   B 50  ? 0.53765 0.34326 0.67624 0.04540  0.17865  0.14604  49  GLU   B CD    
1789 O  OE1   . GLU   B 50  ? 0.61894 0.37447 0.68676 0.08910  0.14405  0.13713  49  GLU   B OE1   
1790 O  OE2   . GLU   B 50  ? 0.61637 0.34593 0.73127 0.05671  0.14860  0.16246  49  GLU   B OE2   
1791 N  N     . THR   B 51  ? 0.21625 0.17747 0.19152 -0.01910 0.04527  -0.00013 50  THR   B N     
1792 C  CA    . THR   B 51  ? 0.22700 0.17958 0.17738 -0.04119 0.00916  0.04492  50  THR   B CA    
1793 C  C     . THR   B 51  ? 0.17846 0.18262 0.18153 -0.02430 0.04519  -0.00151 50  THR   B C     
1794 O  O     . THR   B 51  ? 0.17683 0.21570 0.20626 -0.00582 0.04053  -0.00859 50  THR   B O     
1795 C  CB    . THR   B 51  ? 0.28609 0.22096 0.20659 -0.03043 -0.01489 0.04801  50  THR   B CB    
1796 O  OG1   . THR   B 51  ? 0.36477 0.21575 0.25396 -0.01244 -0.04930 0.06903  50  THR   B OG1   
1797 C  CG2   . THR   B 51  ? 0.29839 0.28415 0.22497 -0.05179 -0.05350 0.03810  50  THR   B CG2   
1798 N  N     . CYS   B 52  ? 0.19915 0.19345 0.16887 -0.03848 0.03120  0.02641  51  CYS   B N     
1799 C  CA    . CYS   B 52  ? 0.18648 0.20998 0.19061 -0.03776 0.02437  0.03580  51  CYS   B CA    
1800 C  C     . CYS   B 52  ? 0.16995 0.19882 0.20771 -0.02103 0.02727  0.02418  51  CYS   B C     
1801 O  O     . CYS   B 52  ? 0.16510 0.18967 0.25254 -0.00712 0.00213  0.00676  51  CYS   B O     
1802 C  CB    . CYS   B 52  ? 0.18556 0.26347 0.21697 -0.00977 0.02640  -0.00798 51  CYS   B CB    
1803 S  SG    . CYS   B 52  ? 0.22492 0.27313 0.22894 0.00267  0.00058  -0.00170 51  CYS   B SG    
1804 N  N     . LEU   B 53  ? 0.17999 0.18337 0.17350 -0.01018 0.02732  0.01593  52  LEU   B N     
1805 C  CA    . LEU   B 53  ? 0.16151 0.22170 0.17467 -0.01928 0.01217  0.02591  52  LEU   B CA    
1806 C  C     . LEU   B 53  ? 0.14528 0.20390 0.21615 -0.01864 -0.00155 0.02510  52  LEU   B C     
1807 O  O     . LEU   B 53  ? 0.15778 0.23118 0.21582 -0.00623 -0.00635 0.02313  52  LEU   B O     
1808 C  CB    . LEU   B 53  ? 0.27342 0.27092 0.18850 0.03689  -0.01241 -0.03130 52  LEU   B CB    
1809 C  CG    . LEU   B 53  ? 0.36790 0.32092 0.33740 0.05105  -0.01074 -0.09251 52  LEU   B CG    
1810 C  CD1   . LEU   B 53  ? 0.34380 0.29813 0.33506 0.02462  -0.00177 -0.11808 52  LEU   B CD1   
1811 C  CD2   . LEU   B 53  ? 0.28368 0.36930 0.39830 0.06228  -0.02908 -0.10558 52  LEU   B CD2   
1812 N  N     . LEU   B 54  ? 0.13918 0.21661 0.18450 -0.03305 -0.00894 0.03154  53  LEU   B N     
1813 C  CA    . LEU   B 54  ? 0.17058 0.23738 0.17701 -0.03002 0.02121  0.03277  53  LEU   B CA    
1814 C  C     . LEU   B 54  ? 0.17318 0.23819 0.18933 -0.02608 0.02282  0.05115  53  LEU   B C     
1815 O  O     . LEU   B 54  ? 0.15711 0.26315 0.22474 -0.02432 -0.02024 0.05638  53  LEU   B O     
1816 C  CB    . LEU   B 54  ? 0.16561 0.25565 0.20975 -0.01546 -0.00450 -0.00596 53  LEU   B CB    
1817 C  CG    . LEU   B 54  ? 0.21483 0.26648 0.21231 -0.02040 0.00704  0.01225  53  LEU   B CG    
1818 C  CD1   . LEU   B 54  ? 0.26054 0.26360 0.20873 -0.01941 0.03521  -0.00679 53  LEU   B CD1   
1819 C  CD2   . LEU   B 54  ? 0.17918 0.29906 0.19922 -0.03665 -0.01014 0.02212  53  LEU   B CD2   
1820 N  N     . ASP   B 55  ? 0.15110 0.23972 0.16372 -0.03385 -0.02272 0.03743  54  ASP   B N     
1821 C  CA    . ASP   B 55  ? 0.14705 0.24723 0.18521 -0.02256 -0.02356 0.06447  54  ASP   B CA    
1822 C  C     . ASP   B 55  ? 0.18686 0.26586 0.12048 -0.03705 -0.01844 0.05152  54  ASP   B C     
1823 O  O     . ASP   B 55  ? 0.19347 0.39711 0.13786 -0.04391 -0.02351 0.04027  54  ASP   B O     
1824 C  CB    . ASP   B 55  ? 0.22251 0.32510 0.18465 0.03880  -0.02432 0.03633  54  ASP   B CB    
1825 C  CG    . ASP   B 55  ? 0.45187 0.44599 0.25946 0.08155  -0.02616 0.00406  54  ASP   B CG    
1826 O  OD1   . ASP   B 55  ? 0.57518 0.51818 0.36739 0.12652  0.00125  -0.02404 54  ASP   B OD1   
1827 O  OD2   . ASP   B 55  ? 0.49695 0.46725 0.27026 0.07415  0.04755  0.01105  54  ASP   B OD2   
1828 N  N     . ILE   B 56  ? 0.20352 0.20265 0.15591 -0.02100 0.02235  0.02399  55  ILE   B N     
1829 C  CA    . ILE   B 56  ? 0.22439 0.19560 0.17613 -0.00908 0.01320  0.04436  55  ILE   B CA    
1830 C  C     . ILE   B 56  ? 0.15755 0.19823 0.17702 -0.01281 0.01544  0.04780  55  ILE   B C     
1831 O  O     . ILE   B 56  ? 0.17840 0.25115 0.21605 -0.02932 0.00111  0.08236  55  ILE   B O     
1832 C  CB    . ILE   B 56  ? 0.28571 0.22396 0.19975 0.02158  0.07137  0.04743  55  ILE   B CB    
1833 C  CG1   . ILE   B 56  ? 0.39530 0.26962 0.22462 0.06560  0.02973  0.02509  55  ILE   B CG1   
1834 C  CG2   . ILE   B 56  ? 0.31436 0.23694 0.19746 0.02669  0.04318  0.02559  55  ILE   B CG2   
1835 C  CD1   . ILE   B 56  ? 0.38043 0.31067 0.27032 0.03890  -0.00663 0.02475  55  ILE   B CD1   
1836 N  N     . LEU   B 57  ? 0.18179 0.19395 0.15357 -0.00117 -0.00102 0.03193  56  LEU   B N     
1837 C  CA    . LEU   B 57  ? 0.17327 0.18597 0.15041 0.00105  0.00997  0.04311  56  LEU   B CA    
1838 C  C     . LEU   B 57  ? 0.13407 0.20144 0.14653 -0.00138 0.00143  0.04553  56  LEU   B C     
1839 O  O     . LEU   B 57  ? 0.16934 0.22775 0.16864 -0.02303 0.00500  0.02273  56  LEU   B O     
1840 C  CB    . LEU   B 57  ? 0.14958 0.16139 0.21337 0.00275  -0.02410 0.03569  56  LEU   B CB    
1841 C  CG    . LEU   B 57  ? 0.23311 0.14802 0.27137 -0.00145 -0.04303 0.02792  56  LEU   B CG    
1842 C  CD1   . LEU   B 57  ? 0.20650 0.15556 0.30258 -0.04351 -0.02480 0.01006  56  LEU   B CD1   
1843 C  CD2   . LEU   B 57  ? 0.23717 0.20231 0.28389 0.01297  -0.08279 0.04169  56  LEU   B CD2   
1844 N  N     . ASP   B 58  ? 0.14116 0.20328 0.17635 0.01142  0.03240  0.03453  57  ASP   B N     
1845 C  CA    . ASP   B 58  ? 0.16848 0.23038 0.23700 -0.01460 0.05263  0.04495  57  ASP   B CA    
1846 C  C     . ASP   B 58  ? 0.15572 0.21770 0.17710 -0.00697 0.03100  0.04496  57  ASP   B C     
1847 O  O     . ASP   B 58  ? 0.16311 0.25001 0.20730 -0.02178 0.01760  0.03021  57  ASP   B O     
1848 C  CB    . ASP   B 58  ? 0.14718 0.25862 0.29442 0.06328  0.05342  0.07332  57  ASP   B CB    
1849 C  CG    . ASP   B 58  ? 0.17157 0.29467 0.26047 0.02939  0.00517  0.07047  57  ASP   B CG    
1850 O  OD1   . ASP   B 58  ? 0.21788 0.31644 0.23578 0.00300  0.07175  0.04739  57  ASP   B OD1   
1851 O  OD2   . ASP   B 58  ? 0.20120 0.31973 0.26603 0.02655  0.03987  0.08240  57  ASP   B OD2   
1852 N  N     . THR   B 59  ? 0.16389 0.22752 0.20837 0.00602  -0.00085 0.04823  58  THR   B N     
1853 C  CA    . THR   B 59  ? 0.14801 0.21952 0.17718 -0.00120 0.00975  0.04663  58  THR   B CA    
1854 C  C     . THR   B 59  ? 0.15326 0.22777 0.17893 0.00390  0.00432  0.02619  58  THR   B C     
1855 O  O     . THR   B 59  ? 0.21766 0.22701 0.21074 0.00128  0.07061  0.04201  58  THR   B O     
1856 C  CB    . THR   B 59  ? 0.18540 0.22213 0.17034 -0.03350 0.03811  0.00675  58  THR   B CB    
1857 O  OG1   . THR   B 59  ? 0.18586 0.24386 0.19721 -0.03456 0.00966  0.05603  58  THR   B OG1   
1858 C  CG2   . THR   B 59  ? 0.16954 0.22931 0.21723 -0.01926 0.01563  0.04091  58  THR   B CG2   
1859 N  N     . ALA   B 60  ? 0.17020 0.25263 0.18813 -0.01311 0.03030  0.05295  59  ALA   B N     
1860 C  CA    . ALA   B 60  ? 0.20029 0.22397 0.19213 -0.00024 0.03181  0.04823  59  ALA   B CA    
1861 C  C     . ALA   B 60  ? 0.27274 0.24753 0.20048 -0.02832 0.05441  0.03841  59  ALA   B C     
1862 O  O     . ALA   B 60  ? 0.23410 0.27732 0.21725 -0.03425 0.01720  0.02125  59  ALA   B O     
1863 C  CB    . ALA   B 60  ? 0.25278 0.21256 0.21644 -0.03681 0.00362  0.06623  59  ALA   B CB    
1864 N  N     . GLY   B 61  ? 0.32905 0.24700 0.16043 -0.00457 0.07722  0.03339  60  GLY   B N     
1865 C  CA    . GLY   B 61  ? 0.47566 0.31508 0.18561 0.01116  0.07851  0.03538  60  GLY   B CA    
1866 C  C     . GLY   B 61  ? 0.54944 0.35282 0.19772 0.00931  0.05675  0.04400  60  GLY   B C     
1867 O  O     . GLY   B 61  ? 0.69714 0.38750 0.22031 -0.02348 0.00420  0.07998  60  GLY   B O     
1868 N  N     . GLN   B 62  ? 0.49198 0.33595 0.21359 0.03528  0.05075  0.08418  61  GLN   B N     
1869 C  CA    . GLN   B 62  ? 0.54003 0.33679 0.30495 0.04742  0.04574  0.08292  61  GLN   B CA    
1870 C  C     . GLN   B 62  ? 0.51606 0.32103 0.32342 0.03012  0.01797  0.08344  61  GLN   B C     
1871 O  O     . GLN   B 62  ? 0.51291 0.30546 0.32699 0.01318  0.09071  0.08213  61  GLN   B O     
1872 C  CB    . GLN   B 62  ? 0.58854 0.35198 0.34682 0.08708  0.02941  0.09493  61  GLN   B CB    
1873 C  CG    . GLN   B 62  ? 0.58091 0.36961 0.34100 0.13168  0.00232  0.12121  61  GLN   B CG    
1874 C  CD    . GLN   B 62  ? 0.59660 0.40298 0.32262 0.10942  0.02143  0.14287  61  GLN   B CD    
1875 O  OE1   . GLN   B 62  ? 0.72141 0.40906 0.35531 0.12983  0.07733  0.13664  61  GLN   B OE1   
1876 N  NE2   . GLN   B 62  ? 0.42464 0.42643 0.25956 0.03246  0.08626  0.14663  61  GLN   B NE2   
1877 N  N     . GLU   B 63  ? 0.52610 0.37332 0.38829 -0.00810 -0.05743 0.05038  62  GLU   B N     
1878 C  CA    . GLU   B 63  ? 0.57236 0.42172 0.49299 -0.01936 -0.10412 -0.00441 62  GLU   B CA    
1879 C  C     . GLU   B 63  ? 0.42981 0.40893 0.52574 -0.04531 -0.06162 0.00159  62  GLU   B C     
1880 O  O     . GLU   B 63  ? 0.46616 0.40784 0.59254 -0.04594 -0.07486 -0.00609 62  GLU   B O     
1881 C  CB    . GLU   B 63  ? 0.75753 0.48365 0.54845 0.01459  -0.14797 -0.06157 62  GLU   B CB    
1882 C  CG    . GLU   B 63  ? 0.90524 0.53415 0.57874 0.03392  -0.17678 -0.09867 62  GLU   B CG    
1883 C  CD    . GLU   B 63  ? 1.02331 0.57484 0.61999 0.00765  -0.20109 -0.12729 62  GLU   B CD    
1884 O  OE1   . GLU   B 63  ? 1.06469 0.58714 0.60817 -0.01479 -0.21438 -0.15735 62  GLU   B OE1   
1885 O  OE2   . GLU   B 63  ? 1.07922 0.59995 0.64499 0.00435  -0.18831 -0.11407 62  GLU   B OE2   
1886 N  N     . GLU   B 64  ? 0.34130 0.39337 0.44166 -0.09931 0.00531  0.00479  63  GLU   B N     
1887 C  CA    . GLU   B 64  ? 0.35467 0.39571 0.40276 -0.08923 0.04447  0.00597  63  GLU   B CA    
1888 C  C     . GLU   B 64  ? 0.27969 0.37974 0.33973 -0.08389 -0.00739 0.03701  63  GLU   B C     
1889 O  O     . GLU   B 64  ? 0.27674 0.37752 0.39330 -0.04393 0.04473  0.06872  63  GLU   B O     
1890 C  CB    . GLU   B 64  ? 0.57996 0.42603 0.46325 -0.10001 0.12877  -0.00228 63  GLU   B CB    
1891 C  CG    . GLU   B 64  ? 0.80406 0.46008 0.56321 -0.13022 0.13070  -0.00819 63  GLU   B CG    
1892 C  CD    . GLU   B 64  ? 1.00872 0.49141 0.66383 -0.14761 0.16008  -0.01036 63  GLU   B CD    
1893 O  OE1   . GLU   B 64  ? 1.07599 0.50729 0.72817 -0.15308 0.14929  -0.00729 63  GLU   B OE1   
1894 O  OE2   . GLU   B 64  ? 1.08654 0.50580 0.68527 -0.14157 0.16162  -0.02573 63  GLU   B OE2   
1895 N  N     . TYR   B 65  ? 0.24179 0.35574 0.25231 -0.02493 -0.02885 0.02270  64  TYR   B N     
1896 C  CA    . TYR   B 65  ? 0.20439 0.34563 0.21185 -0.04354 0.01290  0.05514  64  TYR   B CA    
1897 C  C     . TYR   B 65  ? 0.18620 0.32746 0.21577 -0.04489 -0.01895 0.06634  64  TYR   B C     
1898 O  O     . TYR   B 65  ? 0.20517 0.28707 0.25300 -0.04025 -0.03911 0.08124  64  TYR   B O     
1899 C  CB    . TYR   B 65  ? 0.15887 0.34894 0.21664 -0.03036 -0.03431 0.07894  64  TYR   B CB    
1900 C  CG    . TYR   B 65  ? 0.13675 0.36064 0.21141 -0.07622 -0.02844 0.08605  64  TYR   B CG    
1901 C  CD1   . TYR   B 65  ? 0.19586 0.36799 0.22478 -0.07542 -0.03868 0.09333  64  TYR   B CD1   
1902 C  CD2   . TYR   B 65  ? 0.14443 0.35825 0.22800 -0.06312 -0.01347 0.10338  64  TYR   B CD2   
1903 C  CE1   . TYR   B 65  ? 0.18007 0.36803 0.27833 -0.08233 -0.02263 0.10069  64  TYR   B CE1   
1904 C  CE2   . TYR   B 65  ? 0.18502 0.36096 0.25526 -0.05672 0.00117  0.09092  64  TYR   B CE2   
1905 C  CZ    . TYR   B 65  ? 0.19422 0.34536 0.26735 -0.06878 0.01155  0.09654  64  TYR   B CZ    
1906 O  OH    . TYR   B 65  ? 0.21541 0.30594 0.28439 -0.07294 -0.00915 0.10346  64  TYR   B OH    
1907 N  N     . SER   B 66  ? 0.20781 0.33260 0.24725 -0.04921 -0.05634 0.09624  65  SER   B N     
1908 C  CA    . SER   B 66  ? 0.20988 0.34342 0.27810 -0.07466 -0.08534 0.08923  65  SER   B CA    
1909 C  C     . SER   B 66  ? 0.19664 0.31197 0.28738 -0.03959 -0.05232 0.08204  65  SER   B C     
1910 O  O     . SER   B 66  ? 0.16962 0.31461 0.31094 -0.03164 -0.04083 0.10151  65  SER   B O     
1911 C  CB    . SER   B 66  ? 0.27901 0.37452 0.32995 -0.03320 -0.08417 0.08284  65  SER   B CB    
1912 O  OG    . SER   B 66  ? 0.33385 0.40857 0.39044 0.02125  -0.09523 0.08300  65  SER   B OG    
1913 N  N     . ALA   B 67  ? 0.19059 0.28826 0.28134 0.01067  -0.01817 0.11468  66  ALA   B N     
1914 C  CA    . ALA   B 67  ? 0.21626 0.26670 0.29858 0.00666  0.00690  0.11557  66  ALA   B CA    
1915 C  C     . ALA   B 67  ? 0.16463 0.25864 0.29559 0.00160  -0.00257 0.08527  66  ALA   B C     
1916 O  O     . ALA   B 67  ? 0.17489 0.25801 0.32149 0.00447  -0.02742 0.08213  66  ALA   B O     
1917 C  CB    . ALA   B 67  ? 0.31336 0.26219 0.36384 0.03800  -0.03022 0.11954  66  ALA   B CB    
1918 N  N     . MET   B 68  ? 0.15846 0.23335 0.23490 0.00019  -0.01515 0.06751  67  MET   B N     
1919 C  CA    . MET   B 68  ? 0.20360 0.22719 0.19131 0.01308  -0.02120 0.05807  67  MET   B CA    
1920 C  C     . MET   B 68  ? 0.21776 0.21324 0.18490 0.02635  -0.01543 0.04437  67  MET   B C     
1921 O  O     . MET   B 68  ? 0.16958 0.23729 0.21857 0.00827  -0.01532 0.03435  67  MET   B O     
1922 C  CB    . MET   B 68  ? 0.16136 0.27871 0.20683 0.03795  -0.00969 0.08229  67  MET   B CB    
1923 C  CG    . MET   B 68  ? 0.25254 0.35405 0.23055 -0.01569 0.02781  0.06627  67  MET   B CG    
1924 S  SD    . MET   B 68  ? 0.26212 0.47907 0.28869 0.04778  0.00403  0.04691  67  MET   B SD    
1925 C  CE    . MET   B 68  ? 0.39890 0.45547 0.28591 0.02063  0.10355  0.04368  67  MET   B CE    
1926 N  N     . ARG   B 69  ? 0.20215 0.20755 0.22833 0.00444  0.01666  0.03620  68  ARG   B N     
1927 C  CA    . ARG   B 69  ? 0.23854 0.20842 0.21416 -0.03082 0.02275  0.02524  68  ARG   B CA    
1928 C  C     . ARG   B 69  ? 0.25724 0.21236 0.21009 -0.03355 -0.03700 0.05198  68  ARG   B C     
1929 O  O     . ARG   B 69  ? 0.29174 0.21923 0.20243 -0.03911 -0.03714 0.05035  68  ARG   B O     
1930 C  CB    . ARG   B 69  ? 0.29464 0.27545 0.26939 -0.09408 0.04922  0.00274  68  ARG   B CB    
1931 C  CG    . ARG   B 69  ? 0.36243 0.27645 0.37495 -0.12768 0.03569  -0.03148 68  ARG   B CG    
1932 C  CD    . ARG   B 69  ? 0.52763 0.29964 0.49996 -0.06964 -0.03362 -0.04663 68  ARG   B CD    
1933 N  NE    . ARG   B 69  ? 0.63934 0.28903 0.59423 -0.11545 -0.07162 -0.08539 68  ARG   B NE    
1934 C  CZ    . ARG   B 69  ? 0.74822 0.28071 0.64067 -0.01658 -0.08556 -0.07319 68  ARG   B CZ    
1935 N  NH1   . ARG   B 69  ? 0.74377 0.29034 0.66556 0.00959  -0.12977 -0.06931 68  ARG   B NH1   
1936 N  NH2   . ARG   B 69  ? 0.75267 0.25413 0.64343 0.05689  -0.09882 -0.07000 68  ARG   B NH2   
1937 N  N     . ASP   B 70  ? 0.21018 0.25249 0.21661 -0.07463 -0.05227 0.04332  69  ASP   B N     
1938 C  CA    . ASP   B 70  ? 0.19401 0.27834 0.22074 -0.05770 -0.04303 0.08967  69  ASP   B CA    
1939 C  C     . ASP   B 70  ? 0.21910 0.27038 0.21626 -0.01652 -0.07518 0.06843  69  ASP   B C     
1940 O  O     . ASP   B 70  ? 0.16941 0.27196 0.26205 -0.05982 -0.05621 0.08582  69  ASP   B O     
1941 C  CB    . ASP   B 70  ? 0.20983 0.33509 0.22127 -0.04237 -0.06975 0.12465  69  ASP   B CB    
1942 C  CG    . ASP   B 70  ? 0.19838 0.38760 0.28118 -0.06444 -0.02747 0.12014  69  ASP   B CG    
1943 O  OD1   . ASP   B 70  ? 0.28355 0.39175 0.26790 -0.10585 -0.08654 0.09962  69  ASP   B OD1   
1944 O  OD2   . ASP   B 70  ? 0.17611 0.44527 0.30999 -0.02741 -0.03785 0.14132  69  ASP   B OD2   
1945 N  N     . GLN   B 71  ? 0.19274 0.22894 0.20465 -0.01884 -0.01828 0.02631  70  GLN   B N     
1946 C  CA    . GLN   B 71  ? 0.15775 0.19917 0.22731 -0.03143 -0.02630 0.03819  70  GLN   B CA    
1947 C  C     . GLN   B 71  ? 0.15093 0.20005 0.17811 -0.02069 -0.00191 0.01822  70  GLN   B C     
1948 O  O     . GLN   B 71  ? 0.16665 0.21009 0.17609 -0.02744 -0.00719 0.02799  70  GLN   B O     
1949 C  CB    . GLN   B 71  ? 0.22424 0.20358 0.22586 -0.03349 -0.02853 0.01653  70  GLN   B CB    
1950 C  CG    . GLN   B 71  ? 0.20108 0.23022 0.20715 -0.02404 -0.02239 0.02032  70  GLN   B CG    
1951 C  CD    . GLN   B 71  ? 0.22371 0.22057 0.20325 -0.00167 -0.04297 0.02496  70  GLN   B CD    
1952 O  OE1   . GLN   B 71  ? 0.27849 0.22924 0.24562 0.00671  -0.04051 0.06159  70  GLN   B OE1   
1953 N  NE2   . GLN   B 71  ? 0.21270 0.23254 0.16745 -0.01751 0.01057  -0.00106 70  GLN   B NE2   
1954 N  N     . TYR   B 72  ? 0.16869 0.19524 0.18972 0.00481  -0.02234 0.03896  71  TYR   B N     
1955 C  CA    . TYR   B 72  ? 0.16129 0.19947 0.17786 -0.01240 0.00173  0.02042  71  TYR   B CA    
1956 C  C     . TYR   B 72  ? 0.17911 0.22600 0.18412 -0.03252 -0.00919 0.01960  71  TYR   B C     
1957 O  O     . TYR   B 72  ? 0.17098 0.20154 0.24890 -0.01724 -0.00120 0.00899  71  TYR   B O     
1958 C  CB    . TYR   B 72  ? 0.16406 0.21379 0.20163 -0.00881 0.02606  0.00797  71  TYR   B CB    
1959 C  CG    . TYR   B 72  ? 0.17598 0.20949 0.16023 -0.00653 -0.00708 0.02573  71  TYR   B CG    
1960 C  CD1   . TYR   B 72  ? 0.13975 0.21397 0.16873 0.01092  -0.01754 0.01077  71  TYR   B CD1   
1961 C  CD2   . TYR   B 72  ? 0.19730 0.22798 0.14941 0.00569  -0.00662 0.03357  71  TYR   B CD2   
1962 C  CE1   . TYR   B 72  ? 0.15777 0.23310 0.20761 0.00797  -0.00170 0.01272  71  TYR   B CE1   
1963 C  CE2   . TYR   B 72  ? 0.14325 0.24300 0.19311 -0.02247 -0.01103 0.02994  71  TYR   B CE2   
1964 C  CZ    . TYR   B 72  ? 0.16297 0.24314 0.20298 -0.01579 -0.00394 0.03270  71  TYR   B CZ    
1965 O  OH    . TYR   B 72  ? 0.16565 0.25700 0.22972 -0.00370 -0.01583 0.05455  71  TYR   B OH    
1966 N  N     . MET   B 73  ? 0.14116 0.25669 0.19079 -0.01645 -0.01132 0.00269  72  MET   B N     
1967 C  CA    A MET   B 73  ? 0.15377 0.25166 0.16312 -0.01418 -0.00532 -0.01165 72  MET   B CA    
1968 C  CA    B MET   B 73  ? 0.13429 0.26348 0.17767 -0.02532 -0.00883 -0.02284 72  MET   B CA    
1969 C  C     . MET   B 73  ? 0.15652 0.22712 0.16449 -0.02199 -0.02825 -0.00765 72  MET   B C     
1970 O  O     . MET   B 73  ? 0.16532 0.24311 0.18905 -0.04417 0.01850  -0.01701 72  MET   B O     
1971 C  CB    A MET   B 73  ? 0.18616 0.25708 0.15800 0.01504  0.01933  -0.01505 72  MET   B CB    
1972 C  CB    B MET   B 73  ? 0.10439 0.29095 0.19345 -0.03297 -0.00825 -0.04238 72  MET   B CB    
1973 C  CG    A MET   B 73  ? 0.23144 0.25709 0.18011 0.02742  0.02905  -0.00194 72  MET   B CG    
1974 C  CG    B MET   B 73  ? 0.15712 0.31618 0.21987 -0.03210 -0.00488 -0.02912 72  MET   B CG    
1975 S  SD    A MET   B 73  ? 0.22169 0.24632 0.20044 0.02706  0.02888  0.01319  72  MET   B SD    
1976 S  SD    B MET   B 73  ? 0.18332 0.36796 0.22956 -0.02165 0.00513  0.00750  72  MET   B SD    
1977 C  CE    A MET   B 73  ? 0.20271 0.25000 0.21002 0.01501  0.10284  0.00962  72  MET   B CE    
1978 C  CE    B MET   B 73  ? 0.18953 0.38278 0.27151 -0.02657 0.05374  -0.02133 72  MET   B CE    
1979 N  N     . ARG   B 74  ? 0.16419 0.22082 0.17945 0.00939  -0.00636 -0.00320 73  ARG   B N     
1980 C  CA    . ARG   B 74  ? 0.19563 0.20739 0.20293 0.01408  -0.02211 0.01213  73  ARG   B CA    
1981 C  C     . ARG   B 74  ? 0.17975 0.23817 0.21396 0.00587  0.02486  0.00608  73  ARG   B C     
1982 O  O     . ARG   B 74  ? 0.20975 0.25838 0.23359 -0.00970 0.05891  -0.00129 73  ARG   B O     
1983 C  CB    . ARG   B 74  ? 0.22775 0.19459 0.28142 0.04619  -0.01722 0.00852  73  ARG   B CB    
1984 C  CG    . ARG   B 74  ? 0.21915 0.19919 0.33405 0.01601  0.03711  -0.01526 73  ARG   B CG    
1985 C  CD    . ARG   B 74  ? 0.28910 0.22806 0.35756 0.04944  0.02461  -0.02126 73  ARG   B CD    
1986 N  NE    . ARG   B 74  ? 0.35186 0.28377 0.31940 0.08425  0.05443  -0.01850 73  ARG   B NE    
1987 C  CZ    . ARG   B 74  ? 0.38780 0.30982 0.30443 0.08850  -0.04068 -0.04567 73  ARG   B CZ    
1988 N  NH1   . ARG   B 74  ? 0.31571 0.32143 0.36642 0.11612  -0.05347 -0.10899 73  ARG   B NH1   
1989 N  NH2   . ARG   B 74  ? 0.39889 0.33767 0.29764 0.09131  -0.12682 -0.01318 73  ARG   B NH2   
1990 N  N     . THR   B 75  ? 0.19912 0.22256 0.15676 0.01203  0.01328  0.02183  74  THR   B N     
1991 C  CA    . THR   B 75  ? 0.25844 0.23128 0.19773 0.01371  -0.01132 0.01883  74  THR   B CA    
1992 C  C     . THR   B 75  ? 0.23629 0.21332 0.16399 0.03285  0.00262  0.00870  74  THR   B C     
1993 O  O     . THR   B 75  ? 0.25816 0.23479 0.17520 0.00702  -0.02075 0.01953  74  THR   B O     
1994 C  CB    . THR   B 75  ? 0.27072 0.25008 0.23726 -0.01841 -0.03216 0.03364  74  THR   B CB    
1995 O  OG1   . THR   B 75  ? 0.20830 0.31573 0.21012 -0.04676 -0.00731 0.01869  74  THR   B OG1   
1996 C  CG2   . THR   B 75  ? 0.36255 0.24489 0.30376 0.01799  -0.03563 0.02683  74  THR   B CG2   
1997 N  N     . GLY   B 76  ? 0.18721 0.20231 0.18330 0.00680  0.00814  0.01309  75  GLY   B N     
1998 C  CA    . GLY   B 76  ? 0.15462 0.19875 0.17810 -0.03266 0.00980  0.01009  75  GLY   B CA    
1999 C  C     . GLY   B 76  ? 0.12996 0.20216 0.18001 0.02217  0.00719  0.02558  75  GLY   B C     
2000 O  O     . GLY   B 76  ? 0.14556 0.21106 0.20433 0.00792  0.01832  0.02867  75  GLY   B O     
2001 N  N     . GLU   B 77  ? 0.16822 0.19981 0.15097 -0.01312 0.00240  0.00612  76  GLU   B N     
2002 C  CA    . GLU   B 77  ? 0.16805 0.21084 0.14051 -0.03805 0.03009  0.01470  76  GLU   B CA    
2003 C  C     . GLU   B 77  ? 0.16187 0.24011 0.14541 -0.03202 -0.00502 -0.02647 76  GLU   B C     
2004 O  O     . GLU   B 77  ? 0.18381 0.26466 0.16947 -0.04240 0.01502  -0.01689 76  GLU   B O     
2005 C  CB    . GLU   B 77  ? 0.19230 0.24237 0.14743 -0.01609 0.05549  -0.02214 76  GLU   B CB    
2006 C  CG    . GLU   B 77  ? 0.23571 0.30498 0.20200 -0.01809 0.05014  -0.00292 76  GLU   B CG    
2007 C  CD    . GLU   B 77  ? 0.23607 0.36357 0.22129 -0.00012 0.03986  0.07906  76  GLU   B CD    
2008 O  OE1   . GLU   B 77  ? 0.17572 0.37928 0.21588 0.03237  0.03502  0.03073  76  GLU   B OE1   
2009 O  OE2   . GLU   B 77  ? 0.35439 0.42458 0.28458 -0.00380 0.01145  0.12481  76  GLU   B OE2   
2010 N  N     . GLY   B 78  ? 0.16350 0.21542 0.14665 -0.02108 0.02085  0.00237  77  GLY   B N     
2011 C  CA    . GLY   B 78  ? 0.19727 0.23005 0.13889 -0.00198 0.05266  -0.00249 77  GLY   B CA    
2012 C  C     . GLY   B 78  ? 0.15404 0.19805 0.15140 -0.01056 0.03680  0.03384  77  GLY   B C     
2013 O  O     . GLY   B 78  ? 0.17553 0.23646 0.15061 -0.04130 0.00919  0.01053  77  GLY   B O     
2014 N  N     . PHE   B 79  ? 0.20974 0.18369 0.13807 -0.01167 0.02827  0.00319  78  PHE   B N     
2015 C  CA    . PHE   B 79  ? 0.21301 0.19905 0.15995 -0.00594 0.03788  0.03094  78  PHE   B CA    
2016 C  C     . PHE   B 79  ? 0.21805 0.18225 0.14544 -0.04307 0.04332  0.01300  78  PHE   B C     
2017 O  O     . PHE   B 79  ? 0.21622 0.18256 0.17408 -0.03035 0.02101  -0.01179 78  PHE   B O     
2018 C  CB    . PHE   B 79  ? 0.22319 0.20284 0.14719 -0.01801 0.01871  0.03192  78  PHE   B CB    
2019 C  CG    . PHE   B 79  ? 0.16779 0.19278 0.13375 0.00575  0.00152  -0.00571 78  PHE   B CG    
2020 C  CD1   . PHE   B 79  ? 0.19124 0.19889 0.16160 -0.00952 -0.01602 0.00414  78  PHE   B CD1   
2021 C  CD2   . PHE   B 79  ? 0.16701 0.18766 0.16362 -0.01888 -0.00389 0.00656  78  PHE   B CD2   
2022 C  CE1   . PHE   B 79  ? 0.18673 0.19985 0.15512 0.01960  -0.01372 -0.01562 78  PHE   B CE1   
2023 C  CE2   . PHE   B 79  ? 0.18988 0.21051 0.14825 0.03958  0.00127  0.01653  78  PHE   B CE2   
2024 C  CZ    . PHE   B 79  ? 0.15775 0.20468 0.17279 0.02576  -0.01727 -0.01607 78  PHE   B CZ    
2025 N  N     . LEU   B 80  ? 0.21887 0.18964 0.16552 -0.01008 0.05726  0.01577  79  LEU   B N     
2026 C  CA    . LEU   B 80  ? 0.22452 0.24106 0.17751 -0.02770 0.05392  0.01581  79  LEU   B CA    
2027 C  C     . LEU   B 80  ? 0.23339 0.23250 0.18184 -0.01798 0.06190  0.00512  79  LEU   B C     
2028 O  O     . LEU   B 80  ? 0.30647 0.22784 0.19149 -0.07038 0.07747  -0.01472 79  LEU   B O     
2029 C  CB    . LEU   B 80  ? 0.29008 0.24209 0.31679 -0.01572 -0.02326 0.02688  79  LEU   B CB    
2030 C  CG    . LEU   B 80  ? 0.32844 0.24544 0.36700 -0.02354 -0.06458 0.04132  79  LEU   B CG    
2031 C  CD1   . LEU   B 80  ? 0.37858 0.22394 0.27611 -0.09338 0.03992  0.02855  79  LEU   B CD1   
2032 C  CD2   . LEU   B 80  ? 0.28912 0.28467 0.39118 0.01414  -0.08116 0.02337  79  LEU   B CD2   
2033 N  N     . CYS   B 81  ? 0.22424 0.22256 0.17189 -0.01531 0.06746  -0.00710 80  CYS   B N     
2034 C  CA    . CYS   B 81  ? 0.20189 0.24071 0.18504 -0.02329 0.06695  -0.01534 80  CYS   B CA    
2035 C  C     . CYS   B 81  ? 0.20842 0.23083 0.18953 -0.03450 0.10520  0.00747  80  CYS   B C     
2036 O  O     . CYS   B 81  ? 0.28205 0.20077 0.20517 -0.05464 0.06355  -0.00365 80  CYS   B O     
2037 C  CB    . CYS   B 81  ? 0.24503 0.27118 0.23231 -0.05105 0.05087  -0.03993 80  CYS   B CB    
2038 S  SG    . CYS   B 81  ? 0.27442 0.32299 0.27912 -0.01216 0.05168  -0.06146 80  CYS   B SG    
2039 N  N     . VAL   B 82  ? 0.25704 0.23140 0.19463 -0.01277 0.09593  0.00809  81  VAL   B N     
2040 C  CA    . VAL   B 82  ? 0.24324 0.22369 0.21456 -0.02786 0.10987  0.01522  81  VAL   B CA    
2041 C  C     . VAL   B 82  ? 0.26710 0.20266 0.23046 -0.01663 0.06883  -0.01898 81  VAL   B C     
2042 O  O     . VAL   B 82  ? 0.26879 0.19070 0.23246 -0.03594 0.08707  -0.00592 81  VAL   B O     
2043 C  CB    . VAL   B 82  ? 0.30140 0.20991 0.21733 -0.01639 0.08587  0.00938  81  VAL   B CB    
2044 C  CG1   . VAL   B 82  ? 0.28964 0.21409 0.23400 0.00299  0.14563  -0.00892 81  VAL   B CG1   
2045 C  CG2   . VAL   B 82  ? 0.34374 0.22723 0.20156 0.01413  0.10783  -0.00870 81  VAL   B CG2   
2046 N  N     . PHE   B 83  ? 0.27803 0.21789 0.20976 -0.01692 0.11161  -0.01591 82  PHE   B N     
2047 C  CA    . PHE   B 83  ? 0.33414 0.22988 0.17992 -0.02468 0.12024  -0.00076 82  PHE   B CA    
2048 C  C     . PHE   B 83  ? 0.36867 0.24656 0.17991 -0.02756 0.13367  -0.01168 82  PHE   B C     
2049 O  O     . PHE   B 83  ? 0.37540 0.25817 0.21520 -0.04076 0.14874  -0.00717 82  PHE   B O     
2050 C  CB    . PHE   B 83  ? 0.35163 0.24429 0.17868 -0.02474 0.11848  -0.00727 82  PHE   B CB    
2051 C  CG    . PHE   B 83  ? 0.34334 0.25371 0.20284 -0.04679 0.12452  -0.03128 82  PHE   B CG    
2052 C  CD1   . PHE   B 83  ? 0.39666 0.25960 0.19753 -0.07849 0.13307  -0.02456 82  PHE   B CD1   
2053 C  CD2   . PHE   B 83  ? 0.39533 0.26330 0.19897 -0.07019 0.10244  -0.05974 82  PHE   B CD2   
2054 C  CE1   . PHE   B 83  ? 0.41931 0.27635 0.18235 -0.05363 0.10841  -0.02260 82  PHE   B CE1   
2055 C  CE2   . PHE   B 83  ? 0.41542 0.25820 0.21609 -0.06506 0.13282  -0.04688 82  PHE   B CE2   
2056 C  CZ    . PHE   B 83  ? 0.45227 0.27275 0.19223 -0.06940 0.13153  -0.03356 82  PHE   B CZ    
2057 N  N     . ALA   B 84  ? 0.36763 0.23473 0.18818 0.00405  0.12812  -0.00909 83  ALA   B N     
2058 C  CA    . ALA   B 84  ? 0.37835 0.25544 0.22078 0.00038  0.14589  0.00703  83  ALA   B CA    
2059 C  C     . ALA   B 84  ? 0.39686 0.24208 0.22552 0.02276  0.16499  0.01910  83  ALA   B C     
2060 O  O     . ALA   B 84  ? 0.35227 0.25491 0.20964 0.02560  0.12473  0.02156  83  ALA   B O     
2061 C  CB    . ALA   B 84  ? 0.36467 0.27455 0.23194 -0.01730 0.08922  -0.03812 83  ALA   B CB    
2062 N  N     . ILE   B 85  ? 0.44830 0.22308 0.24905 0.00909  0.18187  -0.00181 84  ILE   B N     
2063 C  CA    . ILE   B 85  ? 0.43796 0.24463 0.27910 -0.00861 0.18587  0.02710  84  ILE   B CA    
2064 C  C     . ILE   B 85  ? 0.45670 0.26498 0.30733 0.00185  0.20813  0.04152  84  ILE   B C     
2065 O  O     . ILE   B 85  ? 0.50605 0.24232 0.40107 0.02279  0.26552  0.02940  84  ILE   B O     
2066 C  CB    . ILE   B 85  ? 0.48627 0.25641 0.31834 -0.01234 0.17147  0.03321  84  ILE   B CB    
2067 C  CG1   . ILE   B 85  ? 0.46381 0.26131 0.37078 0.05173  0.18854  0.02422  84  ILE   B CG1   
2068 C  CG2   . ILE   B 85  ? 0.49745 0.28303 0.27986 -0.06647 0.17696  0.03460  84  ILE   B CG2   
2069 C  CD1   . ILE   B 85  ? 0.53390 0.30151 0.38373 0.05287  0.21355  0.01909  84  ILE   B CD1   
2070 N  N     . ASN   B 86  ? 0.39798 0.29100 0.29135 0.00811  0.19731  0.03034  85  ASN   B N     
2071 C  CA    . ASN   B 86  ? 0.35977 0.30487 0.29632 -0.00987 0.17764  0.00192  85  ASN   B CA    
2072 C  C     . ASN   B 86  ? 0.27963 0.28800 0.27182 -0.01058 0.13960  -0.01216 85  ASN   B C     
2073 O  O     . ASN   B 86  ? 0.33337 0.27843 0.26788 0.00701  0.15434  0.01592  85  ASN   B O     
2074 C  CB    . ASN   B 86  ? 0.34575 0.33828 0.34062 0.01420  0.20457  0.02898  85  ASN   B CB    
2075 C  CG    . ASN   B 86  ? 0.35237 0.36184 0.32066 0.02247  0.19478  0.05948  85  ASN   B CG    
2076 O  OD1   . ASN   B 86  ? 0.38447 0.36460 0.27562 0.05124  0.18495  0.04584  85  ASN   B OD1   
2077 N  ND2   . ASN   B 86  ? 0.30833 0.37029 0.35636 0.00114  0.15872  0.06406  85  ASN   B ND2   
2078 N  N     . ASN   B 87  ? 0.30692 0.28218 0.28436 -0.01646 0.13856  -0.01353 86  ASN   B N     
2079 C  CA    . ASN   B 87  ? 0.29056 0.27254 0.22129 -0.04380 0.09862  -0.00458 86  ASN   B CA    
2080 C  C     . ASN   B 87  ? 0.35137 0.30386 0.24870 -0.04506 0.10492  -0.01134 86  ASN   B C     
2081 O  O     . ASN   B 87  ? 0.32108 0.29554 0.25949 -0.04950 0.12370  -0.03585 86  ASN   B O     
2082 C  CB    . ASN   B 87  ? 0.36899 0.26473 0.18790 -0.04947 0.03103  -0.03597 86  ASN   B CB    
2083 C  CG    . ASN   B 87  ? 0.37619 0.28857 0.23413 -0.05530 0.02833  -0.03602 86  ASN   B CG    
2084 O  OD1   . ASN   B 87  ? 0.36643 0.29074 0.22782 -0.06940 0.06171  0.00668  86  ASN   B OD1   
2085 N  ND2   . ASN   B 87  ? 0.37902 0.31296 0.28076 -0.08356 0.07518  -0.05507 86  ASN   B ND2   
2086 N  N     . THR   B 88  ? 0.35266 0.31874 0.24313 -0.06039 0.10934  -0.01301 87  THR   B N     
2087 C  CA    . THR   B 88  ? 0.36456 0.32987 0.20593 -0.05248 0.11525  -0.03459 87  THR   B CA    
2088 C  C     . THR   B 88  ? 0.31948 0.31682 0.20661 -0.06422 0.09421  -0.02679 87  THR   B C     
2089 O  O     . THR   B 88  ? 0.34597 0.33400 0.24564 -0.06680 0.11693  0.00720  87  THR   B O     
2090 C  CB    . THR   B 88  ? 0.43805 0.35397 0.27005 -0.01656 0.07063  -0.04029 87  THR   B CB    
2091 O  OG1   . THR   B 88  ? 0.44728 0.32836 0.31993 -0.00845 0.09156  -0.07301 87  THR   B OG1   
2092 C  CG2   . THR   B 88  ? 0.41843 0.37486 0.27533 0.01825  0.06015  -0.04404 87  THR   B CG2   
2093 N  N     . LYS   B 89  ? 0.35634 0.32600 0.19526 -0.09072 0.10221  -0.04681 88  LYS   B N     
2094 C  CA    . LYS   B 89  ? 0.36648 0.31236 0.20238 -0.09993 0.10230  -0.02838 88  LYS   B CA    
2095 C  C     . LYS   B 89  ? 0.41148 0.28579 0.21275 -0.05324 0.08775  -0.02947 88  LYS   B C     
2096 O  O     . LYS   B 89  ? 0.41197 0.29380 0.21778 -0.02320 0.06826  -0.03223 88  LYS   B O     
2097 C  CB    . LYS   B 89  ? 0.41150 0.33597 0.25531 -0.12310 0.10805  -0.00281 88  LYS   B CB    
2098 C  CG    . LYS   B 89  ? 0.49591 0.36827 0.29226 -0.11369 0.08785  0.02716  88  LYS   B CG    
2099 C  CD    . LYS   B 89  ? 0.59291 0.38305 0.32991 -0.07001 0.02209  0.00730  88  LYS   B CD    
2100 C  CE    . LYS   B 89  ? 0.66989 0.38631 0.36183 -0.05065 0.01184  -0.00473 88  LYS   B CE    
2101 N  NZ    . LYS   B 89  ? 0.69584 0.39057 0.38996 -0.05082 -0.01121 -0.00502 88  LYS   B NZ    
2102 N  N     . SER   B 90  ? 0.40832 0.24781 0.21179 -0.06181 0.10302  0.00597  89  SER   B N     
2103 C  CA    . SER   B 90  ? 0.35127 0.25732 0.18576 -0.04271 0.09152  0.00673  89  SER   B CA    
2104 C  C     . SER   B 90  ? 0.38489 0.25356 0.21080 -0.06808 0.07990  0.01308  89  SER   B C     
2105 O  O     . SER   B 90  ? 0.37389 0.24756 0.23270 -0.03864 0.09501  -0.02385 89  SER   B O     
2106 C  CB    . SER   B 90  ? 0.39599 0.22822 0.19332 -0.02521 0.10404  0.02319  89  SER   B CB    
2107 O  OG    . SER   B 90  ? 0.43951 0.23506 0.18784 -0.05362 0.11373  -0.00827 89  SER   B OG    
2108 N  N     . PHE   B 91  ? 0.33620 0.27807 0.20884 -0.07006 0.10000  -0.02128 90  PHE   B N     
2109 C  CA    . PHE   B 91  ? 0.34493 0.30700 0.25196 -0.06027 0.12968  -0.05165 90  PHE   B CA    
2110 C  C     . PHE   B 91  ? 0.29674 0.33522 0.24647 -0.02513 0.14593  -0.06341 90  PHE   B C     
2111 O  O     . PHE   B 91  ? 0.32423 0.33843 0.25560 -0.03894 0.09606  -0.03289 90  PHE   B O     
2112 C  CB    . PHE   B 91  ? 0.41161 0.31794 0.25285 -0.08760 0.15549  -0.04995 90  PHE   B CB    
2113 C  CG    . PHE   B 91  ? 0.45356 0.33575 0.22443 -0.09819 0.15129  -0.06724 90  PHE   B CG    
2114 C  CD1   . PHE   B 91  ? 0.42644 0.34350 0.25912 -0.12689 0.16772  -0.05262 90  PHE   B CD1   
2115 C  CD2   . PHE   B 91  ? 0.48242 0.37810 0.28770 -0.11772 0.15361  -0.04354 90  PHE   B CD2   
2116 C  CE1   . PHE   B 91  ? 0.48257 0.38426 0.31385 -0.12534 0.10909  -0.06115 90  PHE   B CE1   
2117 C  CE2   . PHE   B 91  ? 0.49161 0.40293 0.32059 -0.13428 0.13484  -0.02735 90  PHE   B CE2   
2118 C  CZ    . PHE   B 91  ? 0.50612 0.41028 0.33757 -0.13355 0.09949  -0.04730 90  PHE   B CZ    
2119 N  N     . GLU   B 92  ? 0.33281 0.35976 0.24541 -0.04853 0.12050  -0.00885 91  GLU   B N     
2120 C  CA    . GLU   B 92  ? 0.33108 0.38860 0.33546 -0.06184 0.10605  0.02848  91  GLU   B CA    
2121 C  C     . GLU   B 92  ? 0.29359 0.33436 0.41183 -0.06381 0.07690  0.04229  91  GLU   B C     
2122 O  O     . GLU   B 92  ? 0.36344 0.36098 0.50348 -0.07495 0.09400  0.04856  91  GLU   B O     
2123 C  CB    . GLU   B 92  ? 0.36857 0.44439 0.31891 -0.05915 0.05818  0.03828  91  GLU   B CB    
2124 C  CG    . GLU   B 92  ? 0.44996 0.49460 0.30506 -0.04673 0.07740  0.02206  91  GLU   B CG    
2125 C  CD    . GLU   B 92  ? 0.56589 0.52732 0.31278 0.00523  0.01560  0.01659  91  GLU   B CD    
2126 O  OE1   . GLU   B 92  ? 0.56090 0.52201 0.32834 0.00873  -0.04427 0.05542  91  GLU   B OE1   
2127 O  OE2   . GLU   B 92  ? 0.60521 0.55950 0.30476 0.03756  0.07957  -0.01292 91  GLU   B OE2   
2128 N  N     . ASP   B 93  ? 0.31645 0.28033 0.39069 -0.09191 0.00941  0.03990  92  ASP   B N     
2129 C  CA    . ASP   B 93  ? 0.36242 0.31011 0.39229 -0.04981 0.03790  0.00392  92  ASP   B CA    
2130 C  C     . ASP   B 93  ? 0.34963 0.28673 0.30868 -0.05653 0.02712  -0.01437 92  ASP   B C     
2131 O  O     . ASP   B 93  ? 0.36401 0.28972 0.29049 -0.03389 0.04952  -0.00153 92  ASP   B O     
2132 C  CB    . ASP   B 93  ? 0.43884 0.34143 0.50103 -0.05584 0.01987  -0.01528 92  ASP   B CB    
2133 C  CG    . ASP   B 93  ? 0.50749 0.37656 0.58806 -0.03115 -0.00561 -0.01728 92  ASP   B CG    
2134 O  OD1   . ASP   B 93  ? 0.42618 0.35309 0.52431 0.02103  -0.05388 0.02400  92  ASP   B OD1   
2135 O  OD2   . ASP   B 93  ? 0.61780 0.41047 0.67897 -0.08600 -0.00446 -0.01507 92  ASP   B OD2   
2136 N  N     . ILE   B 94  ? 0.31754 0.25889 0.25177 -0.06136 0.07649  -0.00369 93  ILE   B N     
2137 C  CA    . ILE   B 94  ? 0.36844 0.29177 0.22938 -0.05690 0.07404  -0.00042 93  ILE   B CA    
2138 C  C     . ILE   B 94  ? 0.33552 0.29850 0.20031 -0.02935 0.03168  -0.00102 93  ILE   B C     
2139 O  O     . ILE   B 94  ? 0.35195 0.27967 0.16405 0.03239  0.03697  0.01604  93  ILE   B O     
2140 C  CB    . ILE   B 94  ? 0.40108 0.31467 0.23423 -0.06316 0.07653  0.00208  93  ILE   B CB    
2141 C  CG1   . ILE   B 94  ? 0.38521 0.32856 0.20223 -0.04587 0.01492  -0.01241 93  ILE   B CG1   
2142 C  CG2   . ILE   B 94  ? 0.41401 0.32691 0.23865 -0.07455 0.06500  0.01404  93  ILE   B CG2   
2143 C  CD1   . ILE   B 94  ? 0.38933 0.31356 0.19299 -0.02692 0.04825  0.01467  93  ILE   B CD1   
2144 N  N     . HIS   B 95  ? 0.35148 0.32217 0.17848 -0.01304 0.00710  -0.02695 94  HIS   B N     
2145 C  CA    . HIS   B 95  ? 0.38332 0.34927 0.18832 0.00831  0.00488  -0.00258 94  HIS   B CA    
2146 C  C     . HIS   B 95  ? 0.37679 0.34471 0.21066 0.04226  -0.00050 -0.00224 94  HIS   B C     
2147 O  O     . HIS   B 95  ? 0.30350 0.37202 0.20309 0.06279  -0.00043 -0.00991 94  HIS   B O     
2148 C  CB    . HIS   B 95  ? 0.45304 0.37749 0.23164 0.00881  0.02775  0.01751  94  HIS   B CB    
2149 C  CG    . HIS   B 95  ? 0.57361 0.39957 0.28897 0.05087  -0.01134 0.01916  94  HIS   B CG    
2150 N  ND1   . HIS   B 95  ? 0.57618 0.40475 0.30321 0.08034  -0.02584 0.07763  94  HIS   B ND1   
2151 C  CD2   . HIS   B 95  ? 0.60712 0.41543 0.33080 0.07455  0.00435  0.00693  94  HIS   B CD2   
2152 C  CE1   . HIS   B 95  ? 0.61947 0.42345 0.34185 0.09330  -0.06459 0.07296  94  HIS   B CE1   
2153 N  NE2   . HIS   B 95  ? 0.64074 0.42469 0.32963 0.07404  0.00594  0.05808  94  HIS   B NE2   
2154 N  N     . HIS   B 96  ? 0.43359 0.31232 0.18598 0.03158  0.04506  -0.01234 95  HIS   B N     
2155 C  CA    . HIS   B 96  ? 0.59135 0.34432 0.22433 0.04961  0.05039  0.01304  95  HIS   B CA    
2156 C  C     . HIS   B 96  ? 0.45201 0.31562 0.17469 0.06578  0.03375  0.01155  95  HIS   B C     
2157 O  O     . HIS   B 96  ? 0.41993 0.30342 0.18936 0.06406  0.02258  0.03449  95  HIS   B O     
2158 C  CB    . HIS   B 96  ? 0.83915 0.39111 0.31178 0.01751  0.09742  0.02661  95  HIS   B CB    
2159 C  CG    . HIS   B 96  ? 1.09154 0.44683 0.44892 -0.01261 0.08729  0.02679  95  HIS   B CG    
2160 N  ND1   . HIS   B 96  ? 1.19736 0.48205 0.48621 -0.02772 0.09650  0.01952  95  HIS   B ND1   
2161 C  CD2   . HIS   B 96  ? 1.19345 0.47447 0.50389 -0.01684 0.08448  0.03810  95  HIS   B CD2   
2162 C  CE1   . HIS   B 96  ? 1.25527 0.49357 0.50740 -0.02302 0.09225  0.05284  95  HIS   B CE1   
2163 N  NE2   . HIS   B 96  ? 1.25329 0.49409 0.50456 -0.02275 0.11913  0.05387  95  HIS   B NE2   
2164 N  N     . TYR   B 97  ? 0.38489 0.30918 0.21425 0.04983  0.03873  0.02141  96  TYR   B N     
2165 C  CA    . TYR   B 97  ? 0.30589 0.29736 0.20308 0.03761  0.03019  0.02228  96  TYR   B CA    
2166 C  C     . TYR   B 97  ? 0.33562 0.28877 0.18083 0.03232  0.01182  0.00039  96  TYR   B C     
2167 O  O     . TYR   B 97  ? 0.34208 0.30215 0.16522 0.02705  -0.00304 -0.01453 96  TYR   B O     
2168 C  CB    . TYR   B 97  ? 0.35898 0.30259 0.21983 0.04557  0.04462  0.00419  96  TYR   B CB    
2169 C  CG    . TYR   B 97  ? 0.38448 0.29463 0.22981 0.02170  0.01069  -0.00081 96  TYR   B CG    
2170 C  CD1   . TYR   B 97  ? 0.36673 0.27737 0.24611 0.02640  -0.04663 -0.01476 96  TYR   B CD1   
2171 C  CD2   . TYR   B 97  ? 0.43452 0.31016 0.27948 -0.00641 0.00078  -0.03079 96  TYR   B CD2   
2172 C  CE1   . TYR   B 97  ? 0.40571 0.30172 0.26592 0.01294  -0.02262 -0.00684 96  TYR   B CE1   
2173 C  CE2   . TYR   B 97  ? 0.46855 0.33092 0.30462 -0.01740 -0.04533 -0.04328 96  TYR   B CE2   
2174 C  CZ    . TYR   B 97  ? 0.44735 0.33137 0.32539 -0.00774 -0.01437 -0.00950 96  TYR   B CZ    
2175 O  OH    . TYR   B 97  ? 0.46227 0.37625 0.36583 0.00317  0.01364  -0.00064 96  TYR   B OH    
2176 N  N     . ARG   B 98  ? 0.41014 0.26550 0.18582 0.00604  0.03329  -0.01837 97  ARG   B N     
2177 C  CA    . ARG   B 98  ? 0.44121 0.27798 0.23541 -0.00810 0.02889  -0.00906 97  ARG   B CA    
2178 C  C     . ARG   B 98  ? 0.39131 0.25764 0.15407 -0.03111 0.04039  -0.01046 97  ARG   B C     
2179 O  O     . ARG   B 98  ? 0.34700 0.25741 0.18485 -0.04099 0.04618  -0.00227 97  ARG   B O     
2180 C  CB    . ARG   B 98  ? 0.42238 0.30677 0.30425 -0.01397 -0.00071 -0.03414 97  ARG   B CB    
2181 C  CG    . ARG   B 98  ? 0.41687 0.34973 0.30882 -0.04534 0.01119  -0.01406 97  ARG   B CG    
2182 C  CD    . ARG   B 98  ? 0.45163 0.39297 0.32092 -0.07783 0.02517  0.01373  97  ARG   B CD    
2183 N  NE    . ARG   B 98  ? 0.51767 0.43786 0.37299 -0.10908 0.00539  0.05788  97  ARG   B NE    
2184 C  CZ    . ARG   B 98  ? 0.57023 0.48147 0.37104 -0.10955 -0.10459 0.10814  97  ARG   B CZ    
2185 N  NH1   . ARG   B 98  ? 0.57720 0.51595 0.43341 -0.09001 -0.10231 0.12062  97  ARG   B NH1   
2186 N  NH2   . ARG   B 98  ? 0.57098 0.49555 0.34933 -0.13384 -0.11200 0.13820  97  ARG   B NH2   
2187 N  N     . GLU   B 99  ? 0.37021 0.25855 0.16115 -0.01255 0.02637  -0.01812 98  GLU   B N     
2188 C  CA    . GLU   B 99  ? 0.34823 0.25983 0.15475 0.03933  0.01161  0.00120  98  GLU   B CA    
2189 C  C     . GLU   B 99  ? 0.33301 0.23656 0.13652 0.00907  -0.01209 0.00121  98  GLU   B C     
2190 O  O     . GLU   B 99  ? 0.34545 0.26322 0.19356 0.01763  0.00724  -0.01806 98  GLU   B O     
2191 C  CB    . GLU   B 99  ? 0.38879 0.32734 0.13467 0.07106  0.01357  0.01704  98  GLU   B CB    
2192 C  CG    . GLU   B 99  ? 0.49616 0.36754 0.18014 0.06543  -0.08304 0.01852  98  GLU   B CG    
2193 C  CD    . GLU   B 99  ? 0.60895 0.39792 0.28993 0.04874  -0.09157 0.01768  98  GLU   B CD    
2194 O  OE1   . GLU   B 99  ? 0.58940 0.40482 0.33351 0.05782  -0.02658 0.02245  98  GLU   B OE1   
2195 O  OE2   . GLU   B 99  ? 0.67246 0.42464 0.37751 0.02906  -0.08859 0.04728  98  GLU   B OE2   
2196 N  N     . GLN   B 100 ? 0.27572 0.25301 0.13064 -0.01907 -0.03318 0.02167  99  GLN   B N     
2197 C  CA    . GLN   B 100 ? 0.24949 0.26387 0.14323 -0.00516 0.00631  -0.00315 99  GLN   B CA    
2198 C  C     . GLN   B 100 ? 0.28239 0.23693 0.13534 0.02078  -0.02961 -0.01001 99  GLN   B C     
2199 O  O     . GLN   B 100 ? 0.26276 0.22550 0.16919 0.00666  -0.03076 -0.01419 99  GLN   B O     
2200 C  CB    . GLN   B 100 ? 0.25690 0.31158 0.21564 -0.05129 0.02863  -0.04790 99  GLN   B CB    
2201 C  CG    . GLN   B 100 ? 0.36570 0.38349 0.49904 -0.04023 -0.05165 -0.07517 99  GLN   B CG    
2202 C  CD    . GLN   B 100 ? 0.45707 0.41882 0.67260 -0.03425 -0.12667 -0.11372 99  GLN   B CD    
2203 O  OE1   . GLN   B 100 ? 0.45627 0.46149 0.74370 -0.01304 -0.16071 -0.12824 99  GLN   B OE1   
2204 N  NE2   . GLN   B 100 ? 0.49808 0.42538 0.70137 -0.04700 -0.19395 -0.12074 99  GLN   B NE2   
2205 N  N     . ILE   B 101 ? 0.23935 0.24049 0.14842 -0.00360 -0.01959 0.02375  100 ILE   B N     
2206 C  CA    . ILE   B 101 ? 0.23182 0.23864 0.15816 0.02510  -0.02479 0.04358  100 ILE   B CA    
2207 C  C     . ILE   B 101 ? 0.25721 0.24285 0.11075 -0.00959 -0.01755 0.02160  100 ILE   B C     
2208 O  O     . ILE   B 101 ? 0.22623 0.27745 0.13762 -0.01587 0.00033  0.03538  100 ILE   B O     
2209 C  CB    . ILE   B 101 ? 0.26266 0.25035 0.16458 0.02438  -0.01693 0.03410  100 ILE   B CB    
2210 C  CG1   . ILE   B 101 ? 0.27122 0.25868 0.18654 0.05711  0.00730  0.02381  100 ILE   B CG1   
2211 C  CG2   . ILE   B 101 ? 0.31012 0.27504 0.14999 0.02719  0.01326  0.01225  100 ILE   B CG2   
2212 C  CD1   . ILE   B 101 ? 0.36392 0.27315 0.16619 0.06467  0.04828  0.01595  100 ILE   B CD1   
2213 N  N     . LYS   B 102 ? 0.25698 0.22303 0.15284 -0.02037 -0.01234 -0.00549 101 LYS   B N     
2214 C  CA    . LYS   B 102 ? 0.25593 0.21717 0.16608 -0.03303 -0.01923 -0.02043 101 LYS   B CA    
2215 C  C     . LYS   B 102 ? 0.27452 0.22859 0.18858 -0.01744 0.00321  -0.01936 101 LYS   B C     
2216 O  O     . LYS   B 102 ? 0.27372 0.20027 0.19454 0.00230  0.00440  0.00749  101 LYS   B O     
2217 C  CB    . LYS   B 102 ? 0.35292 0.21356 0.18783 -0.04372 -0.02941 -0.03607 101 LYS   B CB    
2218 C  CG    . LYS   B 102 ? 0.41402 0.21126 0.22696 -0.02636 -0.06783 -0.06683 101 LYS   B CG    
2219 C  CD    . LYS   B 102 ? 0.57278 0.26245 0.32631 -0.01362 -0.04954 -0.06446 101 LYS   B CD    
2220 C  CE    . LYS   B 102 ? 0.72262 0.28961 0.36349 -0.02173 -0.03240 -0.08179 101 LYS   B CE    
2221 N  NZ    . LYS   B 102 ? 0.82837 0.31650 0.37958 -0.01404 -0.01775 -0.05555 101 LYS   B NZ    
2222 N  N     . ARG   B 103 ? 0.22614 0.23292 0.16181 0.00685  -0.02667 0.00136  102 ARG   B N     
2223 C  CA    . ARG   B 103 ? 0.26298 0.26562 0.17737 0.01793  -0.03798 0.00957  102 ARG   B CA    
2224 C  C     . ARG   B 103 ? 0.18585 0.22927 0.17080 0.02794  -0.04456 0.00437  102 ARG   B C     
2225 O  O     . ARG   B 103 ? 0.19806 0.21387 0.18438 0.01586  -0.03838 0.02833  102 ARG   B O     
2226 C  CB    . ARG   B 103 ? 0.33464 0.34811 0.21383 -0.01180 -0.01595 0.05166  102 ARG   B CB    
2227 C  CG    . ARG   B 103 ? 0.37973 0.41341 0.25846 -0.00211 0.03360  0.06468  102 ARG   B CG    
2228 C  CD    . ARG   B 103 ? 0.42730 0.47626 0.25032 0.00993  0.09074  0.11464  102 ARG   B CD    
2229 N  NE    . ARG   B 103 ? 0.41933 0.50747 0.24454 0.01675  0.11405  0.13905  102 ARG   B NE    
2230 C  CZ    . ARG   B 103 ? 0.46190 0.54171 0.32674 0.03411  0.13251  0.11914  102 ARG   B CZ    
2231 N  NH1   . ARG   B 103 ? 0.41968 0.53729 0.35163 0.07608  0.08277  0.13773  102 ARG   B NH1   
2232 N  NH2   . ARG   B 103 ? 0.47534 0.55869 0.36064 0.02211  0.09724  0.11405  102 ARG   B NH2   
2233 N  N     . VAL   B 104 ? 0.21138 0.22771 0.16656 -0.01235 -0.05467 0.03272  103 VAL   B N     
2234 C  CA    . VAL   B 104 ? 0.15355 0.25309 0.17270 0.01692  -0.04999 0.02900  103 VAL   B CA    
2235 C  C     . VAL   B 104 ? 0.14245 0.26794 0.18989 -0.02377 -0.01870 0.00880  103 VAL   B C     
2236 O  O     . VAL   B 104 ? 0.17415 0.27853 0.21353 -0.00745 -0.03526 0.00141  103 VAL   B O     
2237 C  CB    . VAL   B 104 ? 0.16978 0.25805 0.17957 -0.01288 -0.04003 0.00840  103 VAL   B CB    
2238 C  CG1   . VAL   B 104 ? 0.14900 0.25435 0.19345 0.00363  -0.05143 0.00976  103 VAL   B CG1   
2239 C  CG2   . VAL   B 104 ? 0.16593 0.26023 0.20866 -0.02658 -0.00215 0.01844  103 VAL   B CG2   
2240 N  N     . LYS   B 105 ? 0.18724 0.27324 0.15014 -0.03657 -0.04138 0.01654  104 LYS   B N     
2241 C  CA    . LYS   B 105 ? 0.18446 0.26904 0.16728 0.01985  -0.03368 0.04630  104 LYS   B CA    
2242 C  C     . LYS   B 105 ? 0.20550 0.28126 0.19544 0.00093  -0.04862 0.06126  104 LYS   B C     
2243 O  O     . LYS   B 105 ? 0.17376 0.31900 0.21192 -0.00915 -0.03815 0.06035  104 LYS   B O     
2244 C  CB    . LYS   B 105 ? 0.23521 0.26213 0.18735 0.02470  -0.03604 0.03076  104 LYS   B CB    
2245 C  CG    . LYS   B 105 ? 0.20506 0.27177 0.23024 0.04015  -0.05015 0.01299  104 LYS   B CG    
2246 C  CD    . LYS   B 105 ? 0.23035 0.27144 0.22236 0.00993  0.01671  0.03317  104 LYS   B CD    
2247 C  CE    . LYS   B 105 ? 0.22069 0.29488 0.19229 -0.01667 -0.01237 0.01783  104 LYS   B CE    
2248 N  NZ    . LYS   B 105 ? 0.17997 0.33091 0.19001 -0.00086 -0.05630 0.01191  104 LYS   B NZ    
2249 N  N     . ASP   B 106 ? 0.20873 0.25570 0.17752 0.04120  -0.05284 0.00596  105 ASP   B N     
2250 C  CA    . ASP   B 106 ? 0.19156 0.26404 0.20652 -0.00113 -0.06739 0.01334  105 ASP   B CA    
2251 C  C     . ASP   B 106 ? 0.22985 0.25101 0.21418 0.01195  -0.03657 0.03240  105 ASP   B C     
2252 O  O     . ASP   B 106 ? 0.19635 0.26352 0.25387 0.01599  -0.00614 0.02537  105 ASP   B O     
2253 C  CB    . ASP   B 106 ? 0.21205 0.27291 0.22459 -0.02264 -0.03774 -0.00796 105 ASP   B CB    
2254 C  CG    . ASP   B 106 ? 0.22328 0.29198 0.26152 0.01420  -0.02106 0.00158  105 ASP   B CG    
2255 O  OD1   . ASP   B 106 ? 0.22153 0.30324 0.22089 0.03029  -0.05989 -0.00007 105 ASP   B OD1   
2256 O  OD2   . ASP   B 106 ? 0.25201 0.29037 0.25347 0.00683  -0.05075 0.01150  105 ASP   B OD2   
2257 N  N     . SER   B 107 ? 0.25063 0.25025 0.20525 0.01267  -0.05613 0.04758  106 SER   B N     
2258 C  CA    . SER   B 107 ? 0.25459 0.22911 0.23964 -0.00033 -0.03129 0.03854  106 SER   B CA    
2259 C  C     . SER   B 107 ? 0.32096 0.22990 0.23492 -0.00486 -0.07079 -0.02558 106 SER   B C     
2260 O  O     . SER   B 107 ? 0.40277 0.23869 0.27554 -0.01488 -0.02909 -0.03253 106 SER   B O     
2261 C  CB    . SER   B 107 ? 0.32998 0.24020 0.29830 -0.01773 -0.03323 0.08751  106 SER   B CB    
2262 O  OG    . SER   B 107 ? 0.33883 0.27707 0.35820 -0.02360 -0.03526 0.09638  106 SER   B OG    
2263 N  N     . GLU   B 108 ? 0.42548 0.28420 0.28585 0.00388  -0.16561 0.00458  107 GLU   B N     
2264 C  CA    . GLU   B 108 ? 0.45371 0.29198 0.39339 0.00469  -0.19596 -0.02647 107 GLU   B CA    
2265 C  C     . GLU   B 108 ? 0.43546 0.29082 0.41898 -0.04260 -0.18580 -0.02869 107 GLU   B C     
2266 O  O     . GLU   B 108 ? 0.49128 0.32219 0.43045 -0.05379 -0.17932 -0.05195 107 GLU   B O     
2267 C  CB    . GLU   B 108 ? 0.55235 0.30505 0.46990 0.00171  -0.20248 -0.07041 107 GLU   B CB    
2268 C  CG    . GLU   B 108 ? 0.69886 0.33330 0.52035 0.03829  -0.21305 -0.06733 107 GLU   B CG    
2269 C  CD    . GLU   B 108 ? 0.86792 0.36303 0.57629 0.07681  -0.23123 -0.03658 107 GLU   B CD    
2270 O  OE1   . GLU   B 108 ? 0.98238 0.36984 0.59000 0.07790  -0.24841 -0.03475 107 GLU   B OE1   
2271 O  OE2   . GLU   B 108 ? 0.89558 0.37686 0.61299 0.08949  -0.19363 -0.02991 107 GLU   B OE2   
2272 N  N     . ASP   B 109 ? 0.37449 0.28315 0.43198 -0.09106 -0.16304 0.00983  108 ASP   B N     
2273 C  CA    . ASP   B 109 ? 0.37699 0.31454 0.39680 -0.05784 -0.14714 0.04089  108 ASP   B CA    
2274 C  C     . ASP   B 109 ? 0.29130 0.31692 0.29463 -0.04286 -0.13357 -0.00148 108 ASP   B C     
2275 O  O     . ASP   B 109 ? 0.32849 0.39985 0.34225 -0.02856 -0.08125 0.00022  108 ASP   B O     
2276 C  CB    . ASP   B 109 ? 0.50355 0.34960 0.53367 -0.09368 -0.14123 0.09078  108 ASP   B CB    
2277 C  CG    . ASP   B 109 ? 0.65521 0.39213 0.64575 -0.11303 -0.10428 0.12095  108 ASP   B CG    
2278 O  OD1   . ASP   B 109 ? 0.71615 0.39993 0.70503 -0.14183 -0.11676 0.15137  108 ASP   B OD1   
2279 O  OD2   . ASP   B 109 ? 0.69482 0.45933 0.67867 -0.08624 -0.06535 0.12328  108 ASP   B OD2   
2280 N  N     . VAL   B 110 ? 0.22585 0.26306 0.25961 -0.04064 -0.08438 0.00656  109 VAL   B N     
2281 C  CA    . VAL   B 110 ? 0.20317 0.24370 0.23072 -0.02486 -0.03549 0.01438  109 VAL   B CA    
2282 C  C     . VAL   B 110 ? 0.19461 0.25147 0.20488 -0.04786 0.01993  -0.00146 109 VAL   B C     
2283 O  O     . VAL   B 110 ? 0.21332 0.27290 0.17651 -0.04253 -0.00946 -0.02374 109 VAL   B O     
2284 C  CB    . VAL   B 110 ? 0.19062 0.22161 0.24379 -0.01122 -0.01667 0.01605  109 VAL   B CB    
2285 C  CG1   . VAL   B 110 ? 0.21343 0.23106 0.26999 -0.00597 -0.05664 0.02020  109 VAL   B CG1   
2286 C  CG2   . VAL   B 110 ? 0.24739 0.24570 0.27425 0.00083  -0.00597 0.01048  109 VAL   B CG2   
2287 N  N     . PRO   B 111 ? 0.20536 0.23194 0.18533 -0.01999 0.02007  0.00604  110 PRO   B N     
2288 C  CA    . PRO   B 111 ? 0.18746 0.25802 0.16734 -0.04458 0.02440  0.02654  110 PRO   B CA    
2289 C  C     . PRO   B 111 ? 0.19784 0.23634 0.15686 -0.06053 -0.01019 -0.01351 110 PRO   B C     
2290 O  O     . PRO   B 111 ? 0.19206 0.22185 0.15856 -0.02149 -0.01216 -0.00613 110 PRO   B O     
2291 C  CB    . PRO   B 111 ? 0.17189 0.28888 0.17951 -0.03277 0.04408  0.03372  110 PRO   B CB    
2292 C  CG    . PRO   B 111 ? 0.17226 0.27284 0.17653 -0.01502 -0.01449 0.00666  110 PRO   B CG    
2293 C  CD    . PRO   B 111 ? 0.21648 0.24900 0.16788 0.01210  0.03971  0.02565  110 PRO   B CD    
2294 N  N     . MET   B 112 ? 0.19065 0.21707 0.15257 -0.04746 0.01951  -0.01441 111 MET   B N     
2295 C  CA    . MET   B 112 ? 0.22513 0.21277 0.14481 -0.03782 0.02151  -0.01407 111 MET   B CA    
2296 C  C     . MET   B 112 ? 0.19954 0.22908 0.17112 -0.06660 0.00499  -0.00836 111 MET   B C     
2297 O  O     . MET   B 112 ? 0.25742 0.25187 0.14766 -0.06347 0.02979  -0.00964 111 MET   B O     
2298 C  CB    . MET   B 112 ? 0.32471 0.28798 0.20897 0.04525  0.00066  0.03250  111 MET   B CB    
2299 C  CG    . MET   B 112 ? 0.43261 0.34039 0.23559 0.00425  -0.00999 0.01538  111 MET   B CG    
2300 S  SD    . MET   B 112 ? 0.47533 0.37146 0.22309 -0.00602 -0.02360 0.06779  111 MET   B SD    
2301 C  CE    . MET   B 112 ? 0.60330 0.38493 0.26961 -0.00102 -0.05254 0.05332  111 MET   B CE    
2302 N  N     . VAL   B 113 ? 0.23416 0.21411 0.14838 -0.03851 0.04067  0.00935  112 VAL   B N     
2303 C  CA    . VAL   B 113 ? 0.25572 0.20989 0.18377 -0.05885 0.06640  -0.01822 112 VAL   B CA    
2304 C  C     . VAL   B 113 ? 0.26507 0.22624 0.17856 -0.07775 0.05266  -0.02272 112 VAL   B C     
2305 O  O     . VAL   B 113 ? 0.27068 0.23484 0.18551 -0.06244 0.06307  -0.01399 112 VAL   B O     
2306 C  CB    . VAL   B 113 ? 0.30657 0.20595 0.18996 -0.00484 0.07186  -0.02881 112 VAL   B CB    
2307 C  CG1   . VAL   B 113 ? 0.31759 0.17992 0.23142 -0.00163 0.08726  -0.02442 112 VAL   B CG1   
2308 C  CG2   . VAL   B 113 ? 0.31980 0.22631 0.22742 -0.04153 0.10179  0.00249  112 VAL   B CG2   
2309 N  N     . LEU   B 114 ? 0.31359 0.24014 0.16045 -0.06937 0.05537  -0.03177 113 LEU   B N     
2310 C  CA    . LEU   B 114 ? 0.37345 0.23685 0.17200 -0.04822 0.12407  -0.03358 113 LEU   B CA    
2311 C  C     . LEU   B 114 ? 0.33873 0.21076 0.16017 -0.03440 0.11275  -0.03982 113 LEU   B C     
2312 O  O     . LEU   B 114 ? 0.35496 0.21465 0.21821 -0.06337 0.07583  -0.00842 113 LEU   B O     
2313 C  CB    . LEU   B 114 ? 0.40093 0.26623 0.16676 -0.05715 0.11752  -0.00740 113 LEU   B CB    
2314 C  CG    . LEU   B 114 ? 0.36910 0.28641 0.15701 -0.09691 0.08652  -0.03403 113 LEU   B CG    
2315 C  CD1   . LEU   B 114 ? 0.33325 0.27842 0.15934 -0.08487 0.06815  0.00682  113 LEU   B CD1   
2316 C  CD2   . LEU   B 114 ? 0.37176 0.33684 0.17343 -0.10587 0.05602  -0.06027 113 LEU   B CD2   
2317 N  N     . VAL   B 115 ? 0.26718 0.22551 0.20840 -0.02320 0.12158  -0.04275 114 VAL   B N     
2318 C  CA    . VAL   B 115 ? 0.31468 0.21540 0.21866 -0.01919 0.14608  0.00881  114 VAL   B CA    
2319 C  C     . VAL   B 115 ? 0.38822 0.21546 0.22972 -0.01095 0.12830  -0.00535 114 VAL   B C     
2320 O  O     . VAL   B 115 ? 0.38647 0.20217 0.23577 -0.05058 0.14669  -0.02460 114 VAL   B O     
2321 C  CB    . VAL   B 115 ? 0.33677 0.22732 0.22619 0.01828  0.13255  0.00655  114 VAL   B CB    
2322 C  CG1   . VAL   B 115 ? 0.34827 0.25033 0.27512 0.01309  0.10077  0.02755  114 VAL   B CG1   
2323 C  CG2   . VAL   B 115 ? 0.28909 0.24627 0.20192 -0.03436 0.12661  0.01216  114 VAL   B CG2   
2324 N  N     . GLY   B 116 ? 0.35750 0.26309 0.27376 -0.01001 0.16818  -0.01308 115 GLY   B N     
2325 C  CA    . GLY   B 116 ? 0.40798 0.25429 0.29358 -0.01045 0.18007  -0.02258 115 GLY   B CA    
2326 C  C     . GLY   B 116 ? 0.43557 0.21769 0.28804 -0.01741 0.20379  -0.00755 115 GLY   B C     
2327 O  O     . GLY   B 116 ? 0.55161 0.17042 0.32578 -0.01242 0.19419  0.00984  115 GLY   B O     
2328 N  N     . ASN   B 117 ? 0.39423 0.25861 0.24696 -0.04762 0.17464  -0.01681 116 ASN   B N     
2329 C  CA    . ASN   B 117 ? 0.33566 0.24516 0.26791 0.02809  0.16357  0.00776  116 ASN   B CA    
2330 C  C     . ASN   B 117 ? 0.41383 0.24749 0.28204 0.03116  0.18192  0.02741  116 ASN   B C     
2331 O  O     . ASN   B 117 ? 0.42002 0.23344 0.26907 0.05302  0.18708  0.04777  116 ASN   B O     
2332 C  CB    . ASN   B 117 ? 0.35640 0.26318 0.25217 0.04044  0.14858  0.03244  116 ASN   B CB    
2333 C  CG    . ASN   B 117 ? 0.34353 0.25109 0.28131 0.07395  0.17249  0.04554  116 ASN   B CG    
2334 O  OD1   . ASN   B 117 ? 0.35573 0.22987 0.33386 0.05766  0.18435  0.01892  116 ASN   B OD1   
2335 N  ND2   . ASN   B 117 ? 0.38980 0.27329 0.27704 0.06417  0.15480  0.02402  116 ASN   B ND2   
2336 N  N     . LYS   B 118 ? 0.41855 0.24534 0.28587 0.05141  0.19811  0.03073  117 LYS   B N     
2337 C  CA    . LYS   B 118 ? 0.42371 0.27537 0.31905 0.02660  0.21357  0.04077  117 LYS   B CA    
2338 C  C     . LYS   B 118 ? 0.49617 0.27710 0.35851 0.03755  0.24436  0.04257  117 LYS   B C     
2339 O  O     . LYS   B 118 ? 0.55424 0.28894 0.35686 0.05197  0.25172  0.01779  117 LYS   B O     
2340 C  CB    . LYS   B 118 ? 0.42182 0.27792 0.29985 -0.00953 0.19535  0.04783  117 LYS   B CB    
2341 C  CG    . LYS   B 118 ? 0.39053 0.26742 0.32371 -0.01429 0.14585  0.02711  117 LYS   B CG    
2342 C  CD    . LYS   B 118 ? 0.36945 0.26506 0.31608 -0.00474 0.15701  0.00403  117 LYS   B CD    
2343 C  CE    . LYS   B 118 ? 0.36206 0.24091 0.28535 0.00931  0.14956  0.05743  117 LYS   B CE    
2344 N  NZ    . LYS   B 118 ? 0.32783 0.25140 0.31040 -0.01021 0.08862  0.05045  117 LYS   B NZ    
2345 N  N     . CYS   B 119 ? 0.55453 0.26160 0.37699 0.05954  0.25983  0.02189  118 CYS   B N     
2346 C  CA    A CYS   B 119 ? 0.58001 0.26057 0.39304 0.04864  0.27391  0.02198  118 CYS   B CA    
2347 C  CA    B CYS   B 119 ? 0.58776 0.28254 0.39761 0.05014  0.27454  0.01021  118 CYS   B CA    
2348 C  C     . CYS   B 119 ? 0.60917 0.28468 0.42353 0.05940  0.28772  0.01531  118 CYS   B C     
2349 O  O     . CYS   B 119 ? 0.63756 0.28587 0.47091 0.07859  0.27256  -0.01963 118 CYS   B O     
2350 C  CB    A CYS   B 119 ? 0.57899 0.21966 0.39772 0.03166  0.27687  0.01570  118 CYS   B CB    
2351 C  CB    B CYS   B 119 ? 0.60114 0.28667 0.40981 0.02771  0.27915  -0.01657 118 CYS   B CB    
2352 S  SG    A CYS   B 119 ? 0.62561 0.21369 0.38782 0.02053  0.27489  0.02234  118 CYS   B SG    
2353 S  SG    B CYS   B 119 ? 0.66736 0.30851 0.40470 0.00663  0.26104  -0.04107 118 CYS   B SG    
2354 N  N     . ASP   B 120 ? 0.59426 0.29758 0.43660 0.07130  0.28807  0.02976  119 ASP   B N     
2355 C  CA    . ASP   B 120 ? 0.59765 0.31535 0.46837 0.06926  0.30980  0.04309  119 ASP   B CA    
2356 C  C     . ASP   B 120 ? 0.56950 0.32861 0.46741 0.05420  0.30481  0.04687  119 ASP   B C     
2357 O  O     . ASP   B 120 ? 0.61250 0.32605 0.47376 0.05323  0.31672  0.03950  119 ASP   B O     
2358 C  CB    . ASP   B 120 ? 0.59132 0.30345 0.48963 0.05524  0.27148  0.06129  119 ASP   B CB    
2359 C  CG    . ASP   B 120 ? 0.58446 0.29773 0.50674 0.07925  0.28204  0.04766  119 ASP   B CG    
2360 O  OD1   . ASP   B 120 ? 0.55932 0.28238 0.48106 0.07116  0.29483  0.01756  119 ASP   B OD1   
2361 O  OD2   . ASP   B 120 ? 0.55358 0.29572 0.52254 0.08494  0.31328  0.05083  119 ASP   B OD2   
2362 N  N     . LEU   B 121 ? 0.60338 0.32468 0.44452 0.05008  0.29747  0.06701  120 LEU   B N     
2363 C  CA    . LEU   B 121 ? 0.62728 0.33249 0.42858 0.05496  0.29885  0.04127  120 LEU   B CA    
2364 C  C     . LEU   B 121 ? 0.62659 0.35494 0.46241 0.03895  0.31470  0.03921  120 LEU   B C     
2365 O  O     . LEU   B 121 ? 0.63528 0.38270 0.48561 0.00735  0.32780  0.00486  120 LEU   B O     
2366 C  CB    . LEU   B 121 ? 0.56888 0.32568 0.42278 0.08418  0.27332  0.01086  120 LEU   B CB    
2367 C  CG    . LEU   B 121 ? 0.53533 0.32792 0.42788 0.07800  0.26841  0.00359  120 LEU   B CG    
2368 C  CD1   . LEU   B 121 ? 0.58016 0.32751 0.45570 0.02980  0.23283  -0.00755 120 LEU   B CD1   
2369 C  CD2   . LEU   B 121 ? 0.43141 0.32622 0.45668 0.10706  0.24184  0.03128  120 LEU   B CD2   
2370 N  N     . PRO   B 122 ? 0.60008 0.34292 0.44265 0.07140  0.29935  0.05640  121 PRO   B N     
2371 C  CA    . PRO   B 122 ? 0.62069 0.33911 0.43228 0.06996  0.29788  0.03527  121 PRO   B CA    
2372 C  C     . PRO   B 122 ? 0.59962 0.31493 0.45620 0.04745  0.30703  0.03027  121 PRO   B C     
2373 O  O     . PRO   B 122 ? 0.58540 0.33168 0.51489 0.01812  0.32531  -0.01065 121 PRO   B O     
2374 C  CB    . PRO   B 122 ? 0.57503 0.33245 0.39319 0.07384  0.27151  0.05988  121 PRO   B CB    
2375 C  CG    . PRO   B 122 ? 0.57713 0.33634 0.38414 0.10914  0.26335  0.07953  121 PRO   B CG    
2376 C  CD    . PRO   B 122 ? 0.54380 0.33681 0.41851 0.10827  0.27352  0.07406  121 PRO   B CD    
2377 N  N     . SER   B 123 ? 0.58813 0.29554 0.45641 0.05440  0.30023  0.01458  122 SER   B N     
2378 C  CA    . SER   B 123 ? 0.59075 0.27190 0.46612 0.04159  0.26538  -0.01883 122 SER   B CA    
2379 C  C     . SER   B 123 ? 0.55066 0.26981 0.43692 0.02473  0.26771  -0.04028 122 SER   B C     
2380 O  O     . SER   B 123 ? 0.52177 0.25815 0.40548 0.04833  0.24487  -0.02642 122 SER   B O     
2381 C  CB    . SER   B 123 ? 0.57973 0.26734 0.49720 0.04634  0.21993  -0.04083 122 SER   B CB    
2382 O  OG    . SER   B 123 ? 0.55991 0.26251 0.48236 0.06047  0.18875  -0.04505 122 SER   B OG    
2383 N  N     . ARG   B 124 ? 0.50837 0.26408 0.41914 -0.02985 0.26897  -0.04783 123 ARG   B N     
2384 C  CA    . ARG   B 124 ? 0.55685 0.28555 0.35337 -0.03780 0.23967  -0.06746 123 ARG   B CA    
2385 C  C     . ARG   B 124 ? 0.50817 0.30915 0.34692 -0.01588 0.23687  -0.04851 123 ARG   B C     
2386 O  O     . ARG   B 124 ? 0.58927 0.31793 0.36204 -0.04219 0.24656  -0.07533 123 ARG   B O     
2387 C  CB    . ARG   B 124 ? 0.53709 0.29853 0.37032 -0.08058 0.21898  -0.04881 123 ARG   B CB    
2388 C  CG    . ARG   B 124 ? 0.58338 0.31876 0.37937 -0.10594 0.21728  -0.04235 123 ARG   B CG    
2389 C  CD    . ARG   B 124 ? 0.63875 0.33553 0.39256 -0.10720 0.20511  -0.02903 123 ARG   B CD    
2390 N  NE    . ARG   B 124 ? 0.63887 0.35603 0.40066 -0.06477 0.24397  -0.00351 123 ARG   B NE    
2391 C  CZ    . ARG   B 124 ? 0.64904 0.36739 0.39174 -0.04290 0.23410  -0.00297 123 ARG   B CZ    
2392 N  NH1   . ARG   B 124 ? 0.55934 0.35205 0.39264 -0.05881 0.24445  -0.00538 123 ARG   B NH1   
2393 N  NH2   . ARG   B 124 ? 0.66647 0.39060 0.41632 -0.03009 0.23546  0.03854  123 ARG   B NH2   
2394 N  N     . THR   B 125 ? 0.47921 0.29883 0.32870 -0.01611 0.22406  -0.04741 124 THR   B N     
2395 C  CA    . THR   B 125 ? 0.47127 0.32093 0.32182 -0.06190 0.21310  -0.08366 124 THR   B CA    
2396 C  C     . THR   B 125 ? 0.46076 0.36313 0.30510 -0.08602 0.19524  -0.07899 124 THR   B C     
2397 O  O     . THR   B 125 ? 0.48078 0.38186 0.31809 -0.08698 0.17658  -0.05180 124 THR   B O     
2398 C  CB    . THR   B 125 ? 0.42061 0.31894 0.32252 -0.07170 0.20903  -0.07532 124 THR   B CB    
2399 O  OG1   . THR   B 125 ? 0.45328 0.32888 0.28689 -0.09073 0.19195  -0.05585 124 THR   B OG1   
2400 C  CG2   . THR   B 125 ? 0.40200 0.33622 0.32097 -0.09219 0.18009  -0.07310 124 THR   B CG2   
2401 N  N     . VAL   B 126 ? 0.46243 0.35824 0.27905 -0.10770 0.18635  -0.08712 125 VAL   B N     
2402 C  CA    . VAL   B 126 ? 0.47536 0.38192 0.29731 -0.10517 0.18725  -0.11572 125 VAL   B CA    
2403 C  C     . VAL   B 126 ? 0.52425 0.43334 0.35230 -0.13464 0.17985  -0.17852 125 VAL   B C     
2404 O  O     . VAL   B 126 ? 0.55326 0.43290 0.32688 -0.10572 0.21363  -0.11283 125 VAL   B O     
2405 C  CB    . VAL   B 126 ? 0.40014 0.37023 0.31003 -0.09560 0.19526  -0.08074 125 VAL   B CB    
2406 C  CG1   . VAL   B 126 ? 0.40183 0.36365 0.32936 -0.09067 0.20532  -0.07833 125 VAL   B CG1   
2407 C  CG2   . VAL   B 126 ? 0.40676 0.37079 0.32590 -0.08289 0.20714  -0.05924 125 VAL   B CG2   
2408 N  N     . ASP   B 127 ? 0.55103 0.46686 0.43817 -0.15679 0.17725  -0.23381 126 ASP   B N     
2409 C  CA    . ASP   B 127 ? 0.56954 0.50913 0.46585 -0.15625 0.18674  -0.25392 126 ASP   B CA    
2410 C  C     . ASP   B 127 ? 0.49996 0.53059 0.46815 -0.17001 0.21264  -0.24998 126 ASP   B C     
2411 O  O     . ASP   B 127 ? 0.50073 0.53831 0.48219 -0.18220 0.22193  -0.25129 126 ASP   B O     
2412 C  CB    . ASP   B 127 ? 0.69464 0.54250 0.51242 -0.16387 0.15958  -0.28027 126 ASP   B CB    
2413 C  CG    . ASP   B 127 ? 0.84649 0.58173 0.60423 -0.17886 0.14955  -0.31379 126 ASP   B CG    
2414 O  OD1   . ASP   B 127 ? 0.90448 0.58743 0.63908 -0.19261 0.15277  -0.30655 126 ASP   B OD1   
2415 O  OD2   . ASP   B 127 ? 0.89446 0.60455 0.61759 -0.18058 0.12948  -0.32312 126 ASP   B OD2   
2416 N  N     . THR   B 128 ? 0.51760 0.55690 0.44949 -0.15096 0.18670  -0.22231 127 THR   B N     
2417 C  CA    . THR   B 128 ? 0.52735 0.57091 0.44386 -0.16030 0.15506  -0.19769 127 THR   B CA    
2418 C  C     . THR   B 128 ? 0.55419 0.56065 0.38479 -0.21925 0.18273  -0.17598 127 THR   B C     
2419 O  O     . THR   B 128 ? 0.55232 0.55478 0.37473 -0.23567 0.14503  -0.17803 127 THR   B O     
2420 C  CB    . THR   B 128 ? 0.51785 0.60438 0.49710 -0.10546 0.16010  -0.16551 127 THR   B CB    
2421 O  OG1   . THR   B 128 ? 0.53641 0.61322 0.51047 -0.06025 0.10402  -0.17518 127 THR   B OG1   
2422 C  CG2   . THR   B 128 ? 0.54711 0.61151 0.51239 -0.08245 0.15027  -0.16308 127 THR   B CG2   
2423 N  N     . LYS   B 129 ? 0.56565 0.55922 0.36153 -0.25558 0.19928  -0.16576 128 LYS   B N     
2424 C  CA    . LYS   B 129 ? 0.64033 0.56206 0.35642 -0.25405 0.17919  -0.16322 128 LYS   B CA    
2425 C  C     . LYS   B 129 ? 0.64055 0.53809 0.32439 -0.25796 0.18683  -0.13982 128 LYS   B C     
2426 O  O     . LYS   B 129 ? 0.62105 0.51208 0.32324 -0.26307 0.18125  -0.14961 128 LYS   B O     
2427 C  CB    . LYS   B 129 ? 0.64255 0.58977 0.36247 -0.25725 0.17622  -0.18764 128 LYS   B CB    
2428 C  CG    . LYS   B 129 ? 0.69444 0.62921 0.36680 -0.28105 0.13882  -0.18939 128 LYS   B CG    
2429 C  CD    . LYS   B 129 ? 0.74956 0.66943 0.41339 -0.29766 0.11847  -0.17171 128 LYS   B CD    
2430 C  CE    . LYS   B 129 ? 0.81800 0.69760 0.44062 -0.29561 0.12307  -0.17467 128 LYS   B CE    
2431 N  NZ    . LYS   B 129 ? 0.86237 0.70389 0.46089 -0.29575 0.10323  -0.19108 128 LYS   B NZ    
2432 N  N     . GLN   B 130 ? 0.66161 0.52240 0.29816 -0.24074 0.16792  -0.12153 129 GLN   B N     
2433 C  CA    . GLN   B 130 ? 0.69788 0.54539 0.29556 -0.26115 0.15492  -0.08596 129 GLN   B CA    
2434 C  C     . GLN   B 130 ? 0.59174 0.51248 0.25613 -0.23587 0.12630  -0.09002 129 GLN   B C     
2435 O  O     . GLN   B 130 ? 0.55676 0.51588 0.22653 -0.20105 0.09883  -0.09229 129 GLN   B O     
2436 C  CB    . GLN   B 130 ? 0.85312 0.58177 0.34961 -0.25898 0.16447  -0.06676 129 GLN   B CB    
2437 C  CG    . GLN   B 130 ? 1.01824 0.62405 0.38030 -0.26785 0.15230  -0.07965 129 GLN   B CG    
2438 C  CD    . GLN   B 130 ? 1.19270 0.66010 0.36593 -0.26501 0.16394  -0.06652 129 GLN   B CD    
2439 O  OE1   . GLN   B 130 ? 1.24728 0.67790 0.38892 -0.26741 0.17107  -0.05053 129 GLN   B OE1   
2440 N  NE2   . GLN   B 130 ? 1.25462 0.66805 0.37068 -0.25657 0.13268  -0.08164 129 GLN   B NE2   
2441 N  N     . ALA   B 131 ? 0.52721 0.47203 0.24845 -0.24108 0.12308  -0.11056 130 ALA   B N     
2442 C  CA    . ALA   B 131 ? 0.53197 0.43394 0.25891 -0.22410 0.14188  -0.11559 130 ALA   B CA    
2443 C  C     . ALA   B 131 ? 0.52320 0.40350 0.25904 -0.21908 0.14072  -0.11900 130 ALA   B C     
2444 O  O     . ALA   B 131 ? 0.53678 0.38565 0.25967 -0.22566 0.10550  -0.09142 130 ALA   B O     
2445 C  CB    . ALA   B 131 ? 0.56382 0.45811 0.27224 -0.23989 0.13308  -0.09607 130 ALA   B CB    
2446 N  N     . GLN   B 132 ? 0.48760 0.39893 0.29282 -0.21658 0.13794  -0.11858 131 GLN   B N     
2447 C  CA    . GLN   B 132 ? 0.51315 0.38113 0.35106 -0.21504 0.17986  -0.13355 131 GLN   B CA    
2448 C  C     . GLN   B 132 ? 0.55911 0.38345 0.31558 -0.19833 0.15459  -0.12962 131 GLN   B C     
2449 O  O     . GLN   B 132 ? 0.53903 0.39211 0.32002 -0.16654 0.16294  -0.09633 131 GLN   B O     
2450 C  CB    . GLN   B 132 ? 0.61221 0.37671 0.44761 -0.18201 0.24850  -0.13454 131 GLN   B CB    
2451 C  CG    . GLN   B 132 ? 0.69209 0.39023 0.53819 -0.17435 0.28135  -0.11455 131 GLN   B CG    
2452 C  CD    . GLN   B 132 ? 0.81743 0.40951 0.62409 -0.14089 0.32600  -0.09651 131 GLN   B CD    
2453 O  OE1   . GLN   B 132 ? 0.86136 0.42523 0.63935 -0.10009 0.36462  -0.11609 131 GLN   B OE1   
2454 N  NE2   . GLN   B 132 ? 0.84328 0.40137 0.66636 -0.14614 0.33037  -0.07099 131 GLN   B NE2   
2455 N  N     . ASP   B 133 ? 0.56284 0.39416 0.25545 -0.19425 0.13028  -0.10077 132 ASP   B N     
2456 C  CA    . ASP   B 133 ? 0.66955 0.40678 0.28317 -0.18216 0.11985  -0.11378 132 ASP   B CA    
2457 C  C     . ASP   B 133 ? 0.63896 0.37718 0.24224 -0.19498 0.13426  -0.07996 132 ASP   B C     
2458 O  O     . ASP   B 133 ? 0.70567 0.36718 0.27245 -0.19863 0.12777  -0.06723 132 ASP   B O     
2459 C  CB    . ASP   B 133 ? 0.72882 0.44458 0.30303 -0.16264 0.09911  -0.14607 132 ASP   B CB    
2460 C  CG    . ASP   B 133 ? 0.80428 0.47828 0.35715 -0.14626 0.08674  -0.14734 132 ASP   B CG    
2461 O  OD1   . ASP   B 133 ? 0.82768 0.48884 0.40328 -0.15711 0.06715  -0.11853 132 ASP   B OD1   
2462 O  OD2   . ASP   B 133 ? 0.82040 0.49315 0.37897 -0.10258 0.09409  -0.17060 132 ASP   B OD2   
2463 N  N     . LEU   B 134 ? 0.63296 0.38210 0.21970 -0.18036 0.11012  -0.06382 133 LEU   B N     
2464 C  CA    . LEU   B 134 ? 0.56131 0.36889 0.23756 -0.16644 0.08579  -0.04542 133 LEU   B CA    
2465 C  C     . LEU   B 134 ? 0.51720 0.36614 0.23029 -0.14328 0.07180  -0.03493 133 LEU   B C     
2466 O  O     . LEU   B 134 ? 0.50221 0.39776 0.25259 -0.09820 0.05166  -0.01058 133 LEU   B O     
2467 C  CB    . LEU   B 134 ? 0.57247 0.36407 0.26098 -0.16994 0.13421  -0.03074 133 LEU   B CB    
2468 C  CG    . LEU   B 134 ? 0.64542 0.38098 0.29076 -0.16618 0.11408  0.00119  133 LEU   B CG    
2469 C  CD1   . LEU   B 134 ? 0.68690 0.39056 0.31825 -0.14707 0.07220  0.01847  133 LEU   B CD1   
2470 C  CD2   . LEU   B 134 ? 0.61498 0.38746 0.28212 -0.17549 0.15587  0.00551  133 LEU   B CD2   
2471 N  N     . ALA   B 135 ? 0.48616 0.35135 0.21939 -0.15365 0.09221  -0.02661 134 ALA   B N     
2472 C  CA    . ALA   B 135 ? 0.47882 0.36723 0.22017 -0.13263 0.06771  -0.04155 134 ALA   B CA    
2473 C  C     . ALA   B 135 ? 0.48704 0.39486 0.24651 -0.15840 0.04866  -0.05918 134 ALA   B C     
2474 O  O     . ALA   B 135 ? 0.47851 0.41815 0.24539 -0.13601 0.03109  -0.05919 134 ALA   B O     
2475 C  CB    . ALA   B 135 ? 0.46505 0.34804 0.23484 -0.10085 0.02192  -0.03913 134 ALA   B CB    
2476 N  N     . ARG   B 136 ? 0.48372 0.41525 0.26411 -0.17357 0.08361  -0.06719 135 ARG   B N     
2477 C  CA    . ARG   B 136 ? 0.50329 0.42456 0.33445 -0.18882 0.03392  -0.10010 135 ARG   B CA    
2478 C  C     . ARG   B 136 ? 0.48330 0.42585 0.30601 -0.14902 0.01999  -0.07056 135 ARG   B C     
2479 O  O     . ARG   B 136 ? 0.51749 0.42572 0.31244 -0.07591 -0.00705 -0.04789 135 ARG   B O     
2480 C  CB    . ARG   B 136 ? 0.52047 0.43095 0.40541 -0.23538 0.06051  -0.15940 135 ARG   B CB    
2481 C  CG    . ARG   B 136 ? 0.58903 0.44735 0.48377 -0.23582 0.08253  -0.19702 135 ARG   B CG    
2482 C  CD    . ARG   B 136 ? 0.72812 0.47206 0.59521 -0.23935 0.13037  -0.23735 135 ARG   B CD    
2483 N  NE    . ARG   B 136 ? 0.84021 0.49830 0.68800 -0.24390 0.17076  -0.25175 135 ARG   B NE    
2484 C  CZ    . ARG   B 136 ? 0.89989 0.51498 0.76678 -0.26852 0.19286  -0.23986 135 ARG   B CZ    
2485 N  NH1   . ARG   B 136 ? 0.93164 0.51575 0.77406 -0.28348 0.19879  -0.24240 135 ARG   B NH1   
2486 N  NH2   . ARG   B 136 ? 0.91988 0.52689 0.80965 -0.25699 0.20116  -0.22555 135 ARG   B NH2   
2487 N  N     . SER   B 137 ? 0.55981 0.43810 0.25346 -0.13678 0.02766  -0.06580 136 SER   B N     
2488 C  CA    . SER   B 137 ? 0.61388 0.45706 0.26690 -0.11375 0.01835  -0.04496 136 SER   B CA    
2489 C  C     . SER   B 137 ? 0.59335 0.46215 0.29063 -0.09488 0.00921  -0.05370 136 SER   B C     
2490 O  O     . SER   B 137 ? 0.61691 0.49983 0.34267 -0.09514 0.00476  -0.04806 136 SER   B O     
2491 C  CB    . SER   B 137 ? 0.68892 0.48029 0.27093 -0.12330 0.02575  -0.03748 136 SER   B CB    
2492 O  OG    . SER   B 137 ? 0.73451 0.49749 0.25580 -0.12308 0.02905  -0.00715 136 SER   B OG    
2493 N  N     . TYR   B 138 ? 0.53352 0.42317 0.27784 -0.13810 0.02198  -0.04753 137 TYR   B N     
2494 C  CA    . TYR   B 138 ? 0.53812 0.42131 0.28536 -0.08602 0.06734  -0.04266 137 TYR   B CA    
2495 C  C     . TYR   B 138 ? 0.52973 0.42540 0.26490 -0.07329 0.05749  -0.04001 137 TYR   B C     
2496 O  O     . TYR   B 138 ? 0.52627 0.42945 0.30343 -0.06683 0.03961  -0.03274 137 TYR   B O     
2497 C  CB    . TYR   B 138 ? 0.51716 0.41607 0.26836 -0.07073 0.04349  -0.04689 137 TYR   B CB    
2498 C  CG    . TYR   B 138 ? 0.50929 0.41700 0.26337 -0.07616 0.08638  -0.04791 137 TYR   B CG    
2499 C  CD1   . TYR   B 138 ? 0.53741 0.41695 0.27239 -0.10586 0.08151  -0.05405 137 TYR   B CD1   
2500 C  CD2   . TYR   B 138 ? 0.51036 0.41860 0.27585 -0.03640 0.12849  -0.04430 137 TYR   B CD2   
2501 C  CE1   . TYR   B 138 ? 0.55850 0.41446 0.24465 -0.08034 0.08290  -0.05371 137 TYR   B CE1   
2502 C  CE2   . TYR   B 138 ? 0.53246 0.41071 0.25304 -0.07889 0.15163  -0.02670 137 TYR   B CE2   
2503 C  CZ    . TYR   B 138 ? 0.58124 0.40353 0.23231 -0.09421 0.15026  -0.03211 137 TYR   B CZ    
2504 O  OH    . TYR   B 138 ? 0.68786 0.39099 0.29891 -0.09782 0.14322  -0.02016 137 TYR   B OH    
2505 N  N     . GLY   B 139 ? 0.47320 0.42071 0.25803 -0.09990 0.04232  -0.04444 138 GLY   B N     
2506 C  CA    . GLY   B 139 ? 0.43434 0.42034 0.22486 -0.11557 -0.00949 -0.00562 138 GLY   B CA    
2507 C  C     . GLY   B 139 ? 0.43767 0.39925 0.21957 -0.11561 -0.01029 -0.04214 138 GLY   B C     
2508 O  O     . GLY   B 139 ? 0.41204 0.39248 0.25186 -0.12404 0.00404  -0.04285 138 GLY   B O     
2509 N  N     . ILE   B 140 ? 0.34397 0.38273 0.20011 -0.11704 0.01934  -0.05548 139 ILE   B N     
2510 C  CA    . ILE   B 140 ? 0.36561 0.36734 0.20731 -0.11184 0.02036  -0.04694 139 ILE   B CA    
2511 C  C     . ILE   B 140 ? 0.37594 0.34825 0.18437 -0.11423 0.06086  -0.05028 139 ILE   B C     
2512 O  O     . ILE   B 140 ? 0.38235 0.34792 0.20053 -0.12496 0.06648  -0.06266 139 ILE   B O     
2513 C  CB    . ILE   B 140 ? 0.38581 0.33449 0.20837 -0.11558 0.05260  -0.06489 139 ILE   B CB    
2514 C  CG1   . ILE   B 140 ? 0.39388 0.33289 0.20596 -0.15173 0.07435  -0.04672 139 ILE   B CG1   
2515 C  CG2   . ILE   B 140 ? 0.37190 0.32719 0.21516 -0.09515 0.02172  -0.06147 139 ILE   B CG2   
2516 C  CD1   . ILE   B 140 ? 0.42946 0.35179 0.27385 -0.13883 0.05946  -0.02852 139 ILE   B CD1   
2517 N  N     . PRO   B 141 ? 0.39455 0.32599 0.20311 -0.14844 0.07938  -0.01092 140 PRO   B N     
2518 C  CA    . PRO   B 141 ? 0.37379 0.31986 0.22593 -0.14698 0.09063  -0.02691 140 PRO   B CA    
2519 C  C     . PRO   B 141 ? 0.41729 0.29725 0.21551 -0.17009 0.11519  -0.03851 140 PRO   B C     
2520 O  O     . PRO   B 141 ? 0.42986 0.31960 0.20869 -0.15343 0.12685  -0.04450 140 PRO   B O     
2521 C  CB    . PRO   B 141 ? 0.41769 0.33862 0.19938 -0.11685 0.06283  -0.03816 140 PRO   B CB    
2522 C  CG    . PRO   B 141 ? 0.39833 0.33854 0.18544 -0.11189 0.06757  -0.02671 140 PRO   B CG    
2523 C  CD    . PRO   B 141 ? 0.43508 0.33559 0.14730 -0.12905 0.06368  -0.02153 140 PRO   B CD    
2524 N  N     . PHE   B 142 ? 0.44830 0.28276 0.23986 -0.12101 0.11886  -0.04713 141 PHE   B N     
2525 C  CA    . PHE   B 142 ? 0.46942 0.25674 0.23640 -0.12380 0.12131  -0.05222 141 PHE   B CA    
2526 C  C     . PHE   B 142 ? 0.49026 0.23169 0.31842 -0.08293 0.15942  -0.02077 141 PHE   B C     
2527 O  O     . PHE   B 142 ? 0.57611 0.21184 0.31915 -0.10322 0.15645  -0.01806 141 PHE   B O     
2528 C  CB    . PHE   B 142 ? 0.52933 0.27850 0.21481 -0.11876 0.10252  -0.07314 141 PHE   B CB    
2529 C  CG    . PHE   B 142 ? 0.59354 0.28925 0.27823 -0.12157 0.15283  -0.08095 141 PHE   B CG    
2530 C  CD1   . PHE   B 142 ? 0.58745 0.27601 0.26957 -0.16593 0.18360  -0.07588 141 PHE   B CD1   
2531 C  CD2   . PHE   B 142 ? 0.60930 0.31180 0.30630 -0.12536 0.19795  -0.06674 141 PHE   B CD2   
2532 C  CE1   . PHE   B 142 ? 0.57069 0.30081 0.30920 -0.19151 0.20257  -0.09576 141 PHE   B CE1   
2533 C  CE2   . PHE   B 142 ? 0.58934 0.32801 0.33759 -0.12835 0.23343  -0.09320 141 PHE   B CE2   
2534 C  CZ    . PHE   B 142 ? 0.59664 0.32342 0.34926 -0.16542 0.21724  -0.09024 141 PHE   B CZ    
2535 N  N     . ILE   B 143 ? 0.41009 0.22972 0.34405 -0.02622 0.15123  -0.01796 142 ILE   B N     
2536 C  CA    . ILE   B 143 ? 0.35861 0.26567 0.38945 -0.00052 0.16300  -0.01525 142 ILE   B CA    
2537 C  C     . ILE   B 143 ? 0.36247 0.23582 0.39216 -0.03264 0.19182  -0.03835 142 ILE   B C     
2538 O  O     . ILE   B 143 ? 0.38191 0.20784 0.34356 -0.04153 0.16432  -0.01156 142 ILE   B O     
2539 C  CB    . ILE   B 143 ? 0.40283 0.35139 0.46961 0.00879  0.11516  -0.00860 142 ILE   B CB    
2540 C  CG1   . ILE   B 143 ? 0.39194 0.39542 0.52426 0.00151  0.06681  -0.01334 142 ILE   B CG1   
2541 C  CG2   . ILE   B 143 ? 0.46200 0.38122 0.46544 -0.01446 0.08174  -0.00511 142 ILE   B CG2   
2542 C  CD1   . ILE   B 143 ? 0.36613 0.40949 0.55716 0.02047  0.06012  -0.02567 142 ILE   B CD1   
2543 N  N     . GLU   B 144 ? 0.46220 0.25524 0.43109 -0.01845 0.21169  -0.04541 143 GLU   B N     
2544 C  CA    . GLU   B 144 ? 0.56550 0.29154 0.43556 -0.03506 0.22482  -0.05939 143 GLU   B CA    
2545 C  C     . GLU   B 144 ? 0.53172 0.25872 0.41937 -0.03128 0.24089  -0.00640 143 GLU   B C     
2546 O  O     . GLU   B 144 ? 0.55804 0.27346 0.43571 -0.04259 0.27008  0.00310  143 GLU   B O     
2547 C  CB    . GLU   B 144 ? 0.66785 0.35359 0.44993 -0.03198 0.24063  -0.09884 143 GLU   B CB    
2548 C  CG    . GLU   B 144 ? 0.75928 0.40661 0.47008 -0.06400 0.26935  -0.11645 143 GLU   B CG    
2549 C  CD    . GLU   B 144 ? 0.83403 0.45902 0.48946 -0.10067 0.29502  -0.11165 143 GLU   B CD    
2550 O  OE1   . GLU   B 144 ? 0.91497 0.48929 0.55624 -0.08791 0.22473  -0.11072 143 GLU   B OE1   
2551 O  OE2   . GLU   B 144 ? 0.78356 0.48561 0.48806 -0.13614 0.34175  -0.08615 143 GLU   B OE2   
2552 N  N     . THR   B 145 ? 0.49232 0.22591 0.39460 0.02378  0.25525  -0.00555 144 THR   B N     
2553 C  CA    . THR   B 145 ? 0.48148 0.23448 0.39648 0.04694  0.21920  0.00684  144 THR   B CA    
2554 C  C     . THR   B 145 ? 0.47936 0.25529 0.40083 0.07096  0.23767  0.02964  144 THR   B C     
2555 O  O     . THR   B 145 ? 0.44525 0.25194 0.41080 0.07869  0.24742  0.04567  144 THR   B O     
2556 C  CB    . THR   B 145 ? 0.47862 0.22229 0.32472 0.02372  0.22701  0.02608  144 THR   B CB    
2557 O  OG1   . THR   B 145 ? 0.51288 0.22460 0.29543 0.03157  0.21233  0.03646  144 THR   B OG1   
2558 C  CG2   . THR   B 145 ? 0.44434 0.24339 0.33147 0.01556  0.22548  0.01530  144 THR   B CG2   
2559 N  N     . SER   B 146 ? 0.45826 0.25531 0.35709 0.07735  0.21388  0.05303  145 SER   B N     
2560 C  CA    . SER   B 146 ? 0.44477 0.27912 0.37133 0.10217  0.22370  0.04386  145 SER   B CA    
2561 C  C     . SER   B 146 ? 0.41121 0.29354 0.34579 0.08209  0.21403  0.09121  145 SER   B C     
2562 O  O     . SER   B 146 ? 0.45981 0.31355 0.36928 0.11370  0.23370  0.08459  145 SER   B O     
2563 C  CB    . SER   B 146 ? 0.41466 0.28256 0.39095 0.11571  0.21032  0.03516  145 SER   B CB    
2564 O  OG    . SER   B 146 ? 0.41492 0.29575 0.44347 0.09674  0.23455  0.02951  145 SER   B OG    
2565 N  N     . ALA   B 147 ? 0.37084 0.30397 0.36386 0.11803  0.20337  0.09474  146 ALA   B N     
2566 C  CA    . ALA   B 147 ? 0.43062 0.32567 0.34806 0.14058  0.17034  0.07798  146 ALA   B CA    
2567 C  C     . ALA   B 147 ? 0.42284 0.35934 0.35598 0.14201  0.20211  0.07901  146 ALA   B C     
2568 O  O     . ALA   B 147 ? 0.43340 0.37266 0.38929 0.14748  0.15147  0.07492  146 ALA   B O     
2569 C  CB    . ALA   B 147 ? 0.43090 0.31806 0.32340 0.17005  0.18303  0.08268  146 ALA   B CB    
2570 N  N     . LYS   B 148 ? 0.45035 0.36209 0.36984 0.16815  0.19510  0.07439  147 LYS   B N     
2571 C  CA    . LYS   B 148 ? 0.48149 0.38601 0.42815 0.16072  0.16974  0.09668  147 LYS   B CA    
2572 C  C     . LYS   B 148 ? 0.55070 0.37556 0.46510 0.18630  0.17196  0.11542  147 LYS   B C     
2573 O  O     . LYS   B 148 ? 0.54783 0.38680 0.50550 0.18283  0.16577  0.10513  147 LYS   B O     
2574 C  CB    . LYS   B 148 ? 0.46321 0.40095 0.44071 0.14488  0.21090  0.07742  147 LYS   B CB    
2575 C  CG    . LYS   B 148 ? 0.43656 0.42228 0.47646 0.15261  0.23302  0.07991  147 LYS   B CG    
2576 C  CD    . LYS   B 148 ? 0.46749 0.44658 0.46894 0.15414  0.25281  0.07448  147 LYS   B CD    
2577 C  CE    . LYS   B 148 ? 0.52714 0.48919 0.46657 0.14021  0.26056  0.07313  147 LYS   B CE    
2578 N  NZ    . LYS   B 148 ? 0.59593 0.52247 0.49819 0.11033  0.16469  0.06416  147 LYS   B NZ    
2579 N  N     . THR   B 149 ? 0.53373 0.37988 0.44501 0.18759  0.23490  0.11646  148 THR   B N     
2580 C  CA    . THR   B 149 ? 0.52265 0.38309 0.47412 0.17051  0.27420  0.12181  148 THR   B CA    
2581 C  C     . THR   B 149 ? 0.53122 0.38846 0.46652 0.18360  0.27320  0.14452  148 THR   B C     
2582 O  O     . THR   B 149 ? 0.58424 0.40597 0.46974 0.21902  0.24119  0.15472  148 THR   B O     
2583 C  CB    . THR   B 149 ? 0.45970 0.38553 0.53356 0.13423  0.27688  0.10642  148 THR   B CB    
2584 O  OG1   . THR   B 149 ? 0.50051 0.36009 0.54728 0.12371  0.29991  0.10228  148 THR   B OG1   
2585 C  CG2   . THR   B 149 ? 0.47631 0.40575 0.53026 0.11023  0.28968  0.10269  148 THR   B CG2   
2586 N  N     . ARG   B 150 ? 0.51450 0.38436 0.46987 0.19392  0.26705  0.16667  149 ARG   B N     
2587 C  CA    . ARG   B 150 ? 0.51208 0.38666 0.47910 0.17572  0.27315  0.16834  149 ARG   B CA    
2588 C  C     . ARG   B 150 ? 0.52763 0.37232 0.47337 0.16703  0.27724  0.16098  149 ARG   B C     
2589 O  O     . ARG   B 150 ? 0.49561 0.34720 0.48648 0.18062  0.27059  0.17485  149 ARG   B O     
2590 C  CB    . ARG   B 150 ? 0.53443 0.39989 0.49568 0.18141  0.28478  0.16797  149 ARG   B CB    
2591 C  CG    . ARG   B 150 ? 0.63693 0.42624 0.54053 0.10781  0.24187  0.15175  149 ARG   B CG    
2592 C  CD    . ARG   B 150 ? 0.63466 0.44841 0.55131 0.05633  0.25078  0.16322  149 ARG   B CD    
2593 N  NE    . ARG   B 150 ? 0.64825 0.45807 0.60085 0.02403  0.19966  0.19013  149 ARG   B NE    
2594 C  CZ    . ARG   B 150 ? 0.65984 0.47143 0.63714 -0.00205 0.19096  0.18221  149 ARG   B CZ    
2595 N  NH1   . ARG   B 150 ? 0.63448 0.49206 0.66338 0.01047  0.19409  0.15921  149 ARG   B NH1   
2596 N  NH2   . ARG   B 150 ? 0.68148 0.46590 0.64443 -0.02658 0.16859  0.20021  149 ARG   B NH2   
2597 N  N     . GLN   B 151 ? 0.52563 0.35579 0.45662 0.17153  0.27218  0.14148  150 GLN   B N     
2598 C  CA    . GLN   B 151 ? 0.59694 0.34692 0.47847 0.16601  0.29654  0.10887  150 GLN   B CA    
2599 C  C     . GLN   B 151 ? 0.53119 0.29045 0.45761 0.14259  0.27493  0.10211  150 GLN   B C     
2600 O  O     . GLN   B 151 ? 0.48064 0.28058 0.47027 0.10599  0.27444  0.11501  150 GLN   B O     
2601 C  CB    . GLN   B 151 ? 0.66616 0.40904 0.54770 0.16364  0.33799  0.08971  150 GLN   B CB    
2602 C  CG    . GLN   B 151 ? 0.82508 0.47458 0.65606 0.18660  0.37445  0.07204  150 GLN   B CG    
2603 C  CD    . GLN   B 151 ? 0.94945 0.53055 0.76977 0.16232  0.36403  0.06342  150 GLN   B CD    
2604 O  OE1   . GLN   B 151 ? 0.95335 0.54458 0.79487 0.17425  0.41073  0.04824  150 GLN   B OE1   
2605 N  NE2   . GLN   B 151 ? 0.98496 0.55068 0.80856 0.15311  0.35605  0.06377  150 GLN   B NE2   
2606 N  N     . GLY   B 152 ? 0.52398 0.26084 0.41729 0.11001  0.26202  0.06270  151 GLY   B N     
2607 C  CA    . GLY   B 152 ? 0.46143 0.25795 0.39396 0.10490  0.23914  0.05851  151 GLY   B CA    
2608 C  C     . GLY   B 152 ? 0.47992 0.25911 0.36429 0.07577  0.19699  0.06364  151 GLY   B C     
2609 O  O     . GLY   B 152 ? 0.49566 0.26178 0.33305 0.04479  0.22707  0.03291  151 GLY   B O     
2610 N  N     . VAL   B 153 ? 0.38360 0.24293 0.39383 0.07398  0.18724  0.07681  152 VAL   B N     
2611 C  CA    . VAL   B 153 ? 0.33976 0.26900 0.39204 0.09255  0.18157  0.07174  152 VAL   B CA    
2612 C  C     . VAL   B 153 ? 0.28432 0.26333 0.33509 0.11491  0.15518  0.07502  152 VAL   B C     
2613 O  O     . VAL   B 153 ? 0.27956 0.27165 0.31663 0.09046  0.12178  0.05740  152 VAL   B O     
2614 C  CB    . VAL   B 153 ? 0.36153 0.27789 0.43467 0.06709  0.23075  0.07112  152 VAL   B CB    
2615 C  CG1   . VAL   B 153 ? 0.36406 0.30673 0.47771 0.06953  0.21437  0.04653  152 VAL   B CG1   
2616 C  CG2   . VAL   B 153 ? 0.35039 0.24845 0.49357 0.07962  0.20474  0.07989  152 VAL   B CG2   
2617 N  N     . ASP   B 154 ? 0.35852 0.28138 0.35923 0.10036  0.15316  0.08427  153 ASP   B N     
2618 C  CA    . ASP   B 154 ? 0.37886 0.27012 0.34769 0.06247  0.14423  0.10172  153 ASP   B CA    
2619 C  C     . ASP   B 154 ? 0.41896 0.24678 0.32319 0.06142  0.19944  0.07141  153 ASP   B C     
2620 O  O     . ASP   B 154 ? 0.38834 0.26887 0.30042 0.05288  0.16396  0.09146  153 ASP   B O     
2621 C  CB    . ASP   B 154 ? 0.36612 0.30389 0.36639 0.07501  0.12575  0.12256  153 ASP   B CB    
2622 C  CG    . ASP   B 154 ? 0.35911 0.35793 0.42851 0.06199  0.08102  0.14855  153 ASP   B CG    
2623 O  OD1   . ASP   B 154 ? 0.37418 0.39715 0.48503 0.06707  0.04803  0.16483  153 ASP   B OD1   
2624 O  OD2   . ASP   B 154 ? 0.46316 0.40236 0.47817 0.06340  0.03770  0.13131  153 ASP   B OD2   
2625 N  N     . ASP   B 155 ? 0.41466 0.22821 0.33342 0.03047  0.21774  0.04099  154 ASP   B N     
2626 C  CA    . ASP   B 155 ? 0.45657 0.26643 0.32492 0.06511  0.21175  0.01323  154 ASP   B CA    
2627 C  C     . ASP   B 155 ? 0.40061 0.23364 0.25185 0.01151  0.17854  0.02646  154 ASP   B C     
2628 O  O     . ASP   B 155 ? 0.35655 0.23426 0.26029 -0.00549 0.17135  0.00459  154 ASP   B O     
2629 C  CB    . ASP   B 155 ? 0.57061 0.32105 0.40659 0.08799  0.27315  0.03501  154 ASP   B CB    
2630 C  CG    . ASP   B 155 ? 0.80075 0.45570 0.55510 0.08571  0.25223  0.00762  154 ASP   B CG    
2631 O  OD1   . ASP   B 155 ? 0.89828 0.49747 0.61347 0.07033  0.20917  0.01194  154 ASP   B OD1   
2632 O  OD2   . ASP   B 155 ? 0.86847 0.51666 0.60548 0.06278  0.23560  0.01070  154 ASP   B OD2   
2633 N  N     . ALA   B 156 ? 0.37287 0.23860 0.23228 0.02750  0.16068  0.00386  155 ALA   B N     
2634 C  CA    . ALA   B 156 ? 0.36131 0.23448 0.28189 0.02657  0.13772  0.02744  155 ALA   B CA    
2635 C  C     . ALA   B 156 ? 0.29899 0.22483 0.24637 0.00816  0.12581  0.01002  155 ALA   B C     
2636 O  O     . ALA   B 156 ? 0.31631 0.24162 0.19120 -0.01104 0.11549  0.00337  155 ALA   B O     
2637 C  CB    . ALA   B 156 ? 0.31278 0.22790 0.31581 0.03458  0.15515  0.07156  155 ALA   B CB    
2638 N  N     . PHE   B 157 ? 0.28304 0.22794 0.27374 -0.02584 0.11376  0.00500  156 PHE   B N     
2639 C  CA    . PHE   B 157 ? 0.30870 0.21800 0.21507 -0.03339 0.09553  0.00316  156 PHE   B CA    
2640 C  C     . PHE   B 157 ? 0.24389 0.23141 0.21526 -0.01581 0.04947  0.01102  156 PHE   B C     
2641 O  O     . PHE   B 157 ? 0.22623 0.22894 0.19048 -0.01473 0.04411  0.01166  156 PHE   B O     
2642 C  CB    . PHE   B 157 ? 0.26629 0.23728 0.23035 -0.03633 0.06264  0.02044  156 PHE   B CB    
2643 C  CG    . PHE   B 157 ? 0.20836 0.22915 0.24742 -0.02601 0.05909  0.04187  156 PHE   B CG    
2644 C  CD1   . PHE   B 157 ? 0.23449 0.24681 0.26769 -0.00790 0.02755  0.05701  156 PHE   B CD1   
2645 C  CD2   . PHE   B 157 ? 0.23253 0.22655 0.28093 0.00423  0.06716  0.04577  156 PHE   B CD2   
2646 C  CE1   . PHE   B 157 ? 0.21178 0.24896 0.28432 0.01750  0.01376  0.04836  156 PHE   B CE1   
2647 C  CE2   . PHE   B 157 ? 0.26909 0.22619 0.30521 0.02997  0.05804  0.06072  156 PHE   B CE2   
2648 C  CZ    . PHE   B 157 ? 0.22491 0.21972 0.28335 0.04056  0.04209  0.04989  156 PHE   B CZ    
2649 N  N     . TYR   B 158 ? 0.21280 0.24576 0.23612 0.01143  0.08413  0.01112  157 TYR   B N     
2650 C  CA    . TYR   B 158 ? 0.23250 0.22890 0.24950 0.00316  0.12117  0.03436  157 TYR   B CA    
2651 C  C     . TYR   B 158 ? 0.26697 0.20027 0.19523 -0.04463 0.11386  0.03045  157 TYR   B C     
2652 O  O     . TYR   B 158 ? 0.24556 0.17982 0.19714 -0.00687 0.06743  0.02854  157 TYR   B O     
2653 C  CB    . TYR   B 158 ? 0.25473 0.26226 0.21295 0.00166  0.05318  0.04823  157 TYR   B CB    
2654 C  CG    . TYR   B 158 ? 0.28091 0.30458 0.23373 -0.00327 0.04379  0.05341  157 TYR   B CG    
2655 C  CD1   . TYR   B 158 ? 0.28180 0.34276 0.23294 -0.00490 0.06422  0.06635  157 TYR   B CD1   
2656 C  CD2   . TYR   B 158 ? 0.34950 0.34094 0.26152 0.04151  0.00053  0.06368  157 TYR   B CD2   
2657 C  CE1   . TYR   B 158 ? 0.25816 0.38672 0.27642 0.02268  0.11483  0.07288  157 TYR   B CE1   
2658 C  CE2   . TYR   B 158 ? 0.32209 0.37694 0.27668 0.03967  -0.01065 0.07661  157 TYR   B CE2   
2659 C  CZ    . TYR   B 158 ? 0.25883 0.42340 0.31225 0.01287  0.04948  0.09498  157 TYR   B CZ    
2660 O  OH    . TYR   B 158 ? 0.24625 0.47903 0.39248 -0.01393 -0.00446 0.10981  157 TYR   B OH    
2661 N  N     . THR   B 159 ? 0.27011 0.20163 0.19492 -0.00642 0.04718  0.03543  158 THR   B N     
2662 C  CA    . THR   B 159 ? 0.27949 0.20399 0.19779 -0.04030 0.06261  0.01909  158 THR   B CA    
2663 C  C     . THR   B 159 ? 0.22386 0.21134 0.16701 -0.03890 0.08488  0.00055  158 THR   B C     
2664 O  O     . THR   B 159 ? 0.23779 0.24770 0.19645 -0.03246 0.04500  0.01242  158 THR   B O     
2665 C  CB    . THR   B 159 ? 0.36142 0.20804 0.22434 -0.02306 0.03271  -0.01748 158 THR   B CB    
2666 O  OG1   . THR   B 159 ? 0.39042 0.20898 0.27521 -0.01270 0.08171  -0.01954 158 THR   B OG1   
2667 C  CG2   . THR   B 159 ? 0.42248 0.23846 0.23793 -0.03673 0.01195  -0.02755 158 THR   B CG2   
2668 N  N     . LEU   B 160 ? 0.20827 0.24020 0.15608 -0.01036 0.05813  0.01970  159 LEU   B N     
2669 C  CA    . LEU   B 160 ? 0.23303 0.20939 0.14018 -0.02661 0.06406  0.00488  159 LEU   B CA    
2670 C  C     . LEU   B 160 ? 0.23431 0.22028 0.16432 -0.05176 0.05216  0.02795  159 LEU   B C     
2671 O  O     . LEU   B 160 ? 0.17451 0.23319 0.19242 -0.03152 0.02023  0.03014  159 LEU   B O     
2672 C  CB    . LEU   B 160 ? 0.25335 0.19887 0.16180 -0.06011 0.02669  0.03385  159 LEU   B CB    
2673 C  CG    . LEU   B 160 ? 0.19224 0.22984 0.13593 -0.03857 0.00589  -0.00125 159 LEU   B CG    
2674 C  CD1   . LEU   B 160 ? 0.22799 0.22638 0.16264 -0.02862 -0.00022 -0.00265 159 LEU   B CD1   
2675 C  CD2   . LEU   B 160 ? 0.22621 0.23442 0.15739 -0.08721 0.02310  0.01188  159 LEU   B CD2   
2676 N  N     . VAL   B 161 ? 0.21763 0.21572 0.15400 -0.01951 0.01893  0.07119  160 VAL   B N     
2677 C  CA    . VAL   B 161 ? 0.20503 0.23307 0.15816 -0.03223 0.04127  0.03949  160 VAL   B CA    
2678 C  C     . VAL   B 161 ? 0.23741 0.20694 0.15735 -0.00593 0.00761  0.00613  160 VAL   B C     
2679 O  O     . VAL   B 161 ? 0.22065 0.21424 0.15390 -0.05364 0.02372  -0.00594 160 VAL   B O     
2680 C  CB    . VAL   B 161 ? 0.21309 0.23590 0.17000 -0.01863 0.02422  0.04718  160 VAL   B CB    
2681 C  CG1   . VAL   B 161 ? 0.19112 0.23489 0.18101 -0.02533 0.03791  0.01538  160 VAL   B CG1   
2682 C  CG2   . VAL   B 161 ? 0.20811 0.23741 0.17374 -0.02131 -0.00546 0.03906  160 VAL   B CG2   
2683 N  N     . ARG   B 162 ? 0.18550 0.22242 0.14844 -0.01096 0.03873  0.01760  161 ARG   B N     
2684 C  CA    . ARG   B 162 ? 0.21611 0.22564 0.19056 -0.03057 0.02208  0.00362  161 ARG   B CA    
2685 C  C     . ARG   B 162 ? 0.19155 0.22447 0.17260 -0.03582 0.05518  0.01465  161 ARG   B C     
2686 O  O     . ARG   B 162 ? 0.21905 0.25660 0.16475 -0.01805 0.02630  0.01118  161 ARG   B O     
2687 C  CB    . ARG   B 162 ? 0.24331 0.21492 0.19809 -0.03297 0.02505  0.00627  161 ARG   B CB    
2688 C  CG    . ARG   B 162 ? 0.25709 0.19471 0.20517 -0.01097 0.04673  0.02838  161 ARG   B CG    
2689 C  CD    . ARG   B 162 ? 0.39362 0.23163 0.29603 0.00031  -0.01934 0.00426  161 ARG   B CD    
2690 N  NE    . ARG   B 162 ? 0.35726 0.24774 0.28916 0.02677  0.02478  -0.00882 161 ARG   B NE    
2691 C  CZ    . ARG   B 162 ? 0.42209 0.25929 0.29439 -0.00530 0.06973  0.00068  161 ARG   B CZ    
2692 N  NH1   . ARG   B 162 ? 0.46517 0.28993 0.30329 -0.01343 0.12038  0.01489  161 ARG   B NH1   
2693 N  NH2   . ARG   B 162 ? 0.37305 0.24164 0.26139 -0.01677 0.01994  0.01282  161 ARG   B NH2   
2694 N  N     . GLU   B 163 ? 0.19331 0.23255 0.18376 -0.04296 0.03605  0.01109  162 GLU   B N     
2695 C  CA    . GLU   B 163 ? 0.22920 0.22378 0.17100 -0.03349 0.02521  0.01090  162 GLU   B CA    
2696 C  C     . GLU   B 163 ? 0.20910 0.22222 0.17247 -0.03191 0.02080  -0.01098 162 GLU   B C     
2697 O  O     . GLU   B 163 ? 0.21991 0.26064 0.15909 -0.03093 0.02286  -0.00019 162 GLU   B O     
2698 C  CB    . GLU   B 163 ? 0.28159 0.24498 0.16201 -0.06936 0.03410  -0.02494 162 GLU   B CB    
2699 C  CG    . GLU   B 163 ? 0.31075 0.26813 0.19338 -0.06067 0.02750  -0.05764 162 GLU   B CG    
2700 C  CD    . GLU   B 163 ? 0.34898 0.27596 0.20249 -0.03223 0.00687  -0.05335 162 GLU   B CD    
2701 O  OE1   . GLU   B 163 ? 0.31880 0.29656 0.24970 -0.07943 -0.00668 0.00656  162 GLU   B OE1   
2702 O  OE2   . GLU   B 163 ? 0.45049 0.27525 0.23081 -0.04687 0.02203  -0.05328 162 GLU   B OE2   
2703 N  N     . ILE   B 164 ? 0.20852 0.22789 0.15095 -0.04879 0.04183  0.00550  163 ILE   B N     
2704 C  CA    . ILE   B 164 ? 0.21335 0.23293 0.14400 -0.03099 0.02993  0.01528  163 ILE   B CA    
2705 C  C     . ILE   B 164 ? 0.16941 0.24386 0.15034 -0.03734 0.00695  0.01009  163 ILE   B C     
2706 O  O     . ILE   B 164 ? 0.17852 0.24984 0.18906 -0.03426 0.00709  -0.00494 163 ILE   B O     
2707 C  CB    . ILE   B 164 ? 0.19408 0.21973 0.15445 -0.03579 0.01431  -0.01609 163 ILE   B CB    
2708 C  CG1   . ILE   B 164 ? 0.18674 0.21694 0.18471 -0.05044 0.01519  0.00120  163 ILE   B CG1   
2709 C  CG2   . ILE   B 164 ? 0.17220 0.25473 0.16068 -0.02494 0.01715  -0.02929 163 ILE   B CG2   
2710 C  CD1   . ILE   B 164 ? 0.15597 0.22101 0.22523 -0.03813 -0.00634 0.03529  163 ILE   B CD1   
2711 N  N     . ARG   B 165 ? 0.20296 0.24711 0.14086 -0.04045 0.03790  0.01367  164 ARG   B N     
2712 C  CA    . ARG   B 165 ? 0.21104 0.25771 0.16854 -0.04018 0.04554  0.01564  164 ARG   B CA    
2713 C  C     . ARG   B 165 ? 0.17129 0.27073 0.19095 -0.04321 0.03940  -0.00740 164 ARG   B C     
2714 O  O     . ARG   B 165 ? 0.19722 0.28433 0.20617 -0.02187 0.02510  0.01356  164 ARG   B O     
2715 C  CB    . ARG   B 165 ? 0.22438 0.22871 0.16142 -0.01563 0.00575  0.02103  164 ARG   B CB    
2716 C  CG    . ARG   B 165 ? 0.23210 0.23943 0.13494 0.01012  -0.00394 0.02422  164 ARG   B CG    
2717 C  CD    . ARG   B 165 ? 0.19214 0.23272 0.19875 0.02329  0.00969  0.02462  164 ARG   B CD    
2718 N  NE    . ARG   B 165 ? 0.19625 0.25872 0.18313 0.01857  -0.01601 0.02899  164 ARG   B NE    
2719 C  CZ    . ARG   B 165 ? 0.17339 0.25786 0.21487 -0.01793 0.02247  0.02383  164 ARG   B CZ    
2720 N  NH1   . ARG   B 165 ? 0.21124 0.26974 0.23309 0.00691  0.07670  -0.00486 164 ARG   B NH1   
2721 N  NH2   . ARG   B 165 ? 0.16358 0.27291 0.22568 0.00053  0.00537  0.03347  164 ARG   B NH2   
2722 N  N     . LYS   B 166 ? 0.19290 0.30892 0.17198 -0.02976 0.01101  0.00170  165 LYS   B N     
2723 C  CA    . LYS   B 166 ? 0.18412 0.33467 0.19658 -0.01511 -0.02105 -0.02070 165 LYS   B CA    
2724 C  C     . LYS   B 166 ? 0.15353 0.31133 0.20621 -0.03794 -0.00186 -0.00782 165 LYS   B C     
2725 O  O     . LYS   B 166 ? 0.19435 0.33155 0.22738 -0.04557 0.03174  -0.01041 165 LYS   B O     
2726 C  CB    . LYS   B 166 ? 0.26053 0.38767 0.18207 -0.05337 -0.05496 -0.06249 165 LYS   B CB    
2727 C  CG    . LYS   B 166 ? 0.41304 0.43319 0.29243 -0.04439 0.01519  -0.08953 165 LYS   B CG    
2728 C  CD    . LYS   B 166 ? 0.57039 0.46501 0.37710 -0.06181 -0.01561 -0.13085 165 LYS   B CD    
2729 C  CE    . LYS   B 166 ? 0.64109 0.49481 0.42311 -0.05633 0.03892  -0.15113 165 LYS   B CE    
2730 N  NZ    . LYS   B 166 ? 0.70833 0.50932 0.45953 -0.07652 0.03714  -0.14461 165 LYS   B NZ    
2731 N  N     . HIS   B 167 ? 0.18359 0.27358 0.18732 -0.00852 -0.00241 0.00997  166 HIS   B N     
2732 C  CA    . HIS   B 167 ? 0.21629 0.29352 0.18824 -0.02029 -0.00250 0.02839  166 HIS   B CA    
2733 C  C     . HIS   B 167 ? 0.24460 0.30814 0.19288 -0.00261 0.01055  -0.00546 166 HIS   B C     
2734 O  O     . HIS   B 167 ? 0.32712 0.34086 0.21016 0.03104  -0.02251 -0.02979 166 HIS   B O     
2735 C  CB    . HIS   B 167 ? 0.22981 0.30543 0.25852 -0.04355 0.01512  0.02482  166 HIS   B CB    
2736 C  CG    . HIS   B 167 ? 0.26455 0.32693 0.33595 -0.03167 0.06509  0.00315  166 HIS   B CG    
2737 N  ND1   . HIS   B 167 ? 0.38021 0.34019 0.40197 0.00105  0.01623  -0.00583 166 HIS   B ND1   
2738 C  CD2   . HIS   B 167 ? 0.37007 0.34877 0.40181 0.00438  0.02898  -0.00727 166 HIS   B CD2   
2739 C  CE1   . HIS   B 167 ? 0.43471 0.35535 0.41444 -0.00663 0.02078  -0.00175 166 HIS   B CE1   
2740 N  NE2   . HIS   B 167 ? 0.43734 0.36301 0.44837 -0.00730 0.03500  0.00776  166 HIS   B NE2   
2741 N  N     . LYS   B 168 ? 0.20067 0.30673 0.18745 -0.02857 0.01077  -0.01010 167 LYS   B N     
2742 C  CA    A LYS   B 168 ? 0.19129 0.31511 0.22157 -0.00818 0.03014  -0.02071 167 LYS   B CA    
2743 C  CA    B LYS   B 168 ? 0.21300 0.31885 0.25404 -0.03212 0.06689  -0.04196 167 LYS   B CA    
2744 C  C     . LYS   B 168 ? 0.22625 0.32270 0.26335 0.00314  0.05671  -0.06251 167 LYS   B C     
2745 O  O     . LYS   B 168 ? 0.22923 0.35043 0.25153 -0.00762 0.04361  -0.05423 167 LYS   B O     
2746 C  CB    A LYS   B 168 ? 0.16283 0.29078 0.19135 0.00318  -0.04347 0.00950  167 LYS   B CB    
2747 C  CB    B LYS   B 168 ? 0.22894 0.30365 0.28887 -0.06313 0.08353  -0.06330 167 LYS   B CB    
2748 C  CG    A LYS   B 168 ? 0.21933 0.28771 0.16052 -0.04339 -0.08039 0.00505  167 LYS   B CG    
2749 C  CG    B LYS   B 168 ? 0.25672 0.30875 0.33571 -0.07090 0.13674  -0.09543 167 LYS   B CG    
2750 C  CD    A LYS   B 168 ? 0.26295 0.31217 0.16002 -0.06098 -0.01876 -0.01341 167 LYS   B CD    
2751 C  CD    B LYS   B 168 ? 0.28395 0.32079 0.39889 -0.06993 0.12797  -0.11708 167 LYS   B CD    
2752 C  CE    A LYS   B 168 ? 0.27390 0.33840 0.18424 -0.07016 0.01954  -0.01632 167 LYS   B CE    
2753 C  CE    B LYS   B 168 ? 0.30811 0.32511 0.45082 -0.05182 0.11850  -0.14359 167 LYS   B CE    
2754 N  NZ    A LYS   B 168 ? 0.25843 0.35916 0.21392 -0.06745 0.06558  0.01074  167 LYS   B NZ    
2755 N  NZ    B LYS   B 168 ? 0.31858 0.32228 0.48159 -0.00213 0.12704  -0.16823 167 LYS   B NZ    
2756 N  N     . GLU   B 169 ? 0.23032 0.38661 0.30608 -0.03078 0.07479  -0.06837 168 GLU   B N     
2757 C  CA    . GLU   B 169 ? 0.27015 0.45416 0.45380 -0.09907 0.11103  -0.07543 168 GLU   B CA    
2758 C  C     . GLU   B 169 ? 0.26215 0.51197 0.55682 -0.13104 0.02190  -0.09417 168 GLU   B C     
2759 O  O     . GLU   B 169 ? 0.32422 0.50968 0.63894 -0.14642 0.08569  -0.07764 168 GLU   B O     
2760 C  CB    . GLU   B 169 ? 0.40504 0.48487 0.53662 -0.10133 0.13234  -0.02932 168 GLU   B CB    
2761 C  CG    . GLU   B 169 ? 0.63598 0.52302 0.63220 -0.04077 0.04331  -0.01188 168 GLU   B CG    
2762 C  CD    . GLU   B 169 ? 0.81018 0.54991 0.68628 -0.02588 0.00978  -0.02512 168 GLU   B CD    
2763 O  OE1   . GLU   B 169 ? 0.84940 0.57132 0.67902 -0.00636 -0.00138 -0.04730 168 GLU   B OE1   
2764 O  OE2   . GLU   B 169 ? 0.88055 0.57820 0.70629 -0.03234 -0.01168 -0.02597 168 GLU   B OE2   
2765 N  N     . LYS   B 170 ? 0.25092 0.57813 0.59426 -0.11276 -0.10426 -0.10761 169 LYS   B N     
2766 C  CA    . LYS   B 170 ? 0.31315 0.65942 0.67529 -0.05207 -0.06455 -0.12111 169 LYS   B CA    
2767 C  C     . LYS   B 170 ? 0.28026 0.70077 0.71285 -0.03550 -0.04808 -0.10767 169 LYS   B C     
2768 O  O     . LYS   B 170 ? 0.30658 0.71439 0.68133 0.01858  -0.04013 -0.10991 169 LYS   B O     
2769 C  CB    . LYS   B 170 ? 0.44697 0.68664 0.70435 -0.02706 -0.05012 -0.11893 169 LYS   B CB    
2770 C  CG    . LYS   B 170 ? 0.58401 0.70764 0.73896 0.00935  0.00765  -0.12688 169 LYS   B CG    
2771 C  CD    . LYS   B 170 ? 0.65584 0.72148 0.77674 0.03510  0.04058  -0.13602 169 LYS   B CD    
2772 C  CE    . LYS   B 170 ? 0.71114 0.73112 0.79675 0.04916  0.04830  -0.14503 169 LYS   B CE    
2773 N  NZ    . LYS   B 170 ? 0.73318 0.73687 0.80745 0.04918  0.04834  -0.14876 169 LYS   B NZ    
2774 O  OXT   . LYS   B 170 ? 0.24554 0.71796 0.73509 -0.07194 -0.06288 -0.10115 169 LYS   B OXT   
2775 N  N     . MET   C 2   ? 0.89123 0.65182 0.80125 0.05779  -0.03923 0.09283  1   MET   D N     
2776 C  CA    . MET   C 2   ? 0.89441 0.64835 0.80862 0.05626  -0.04542 0.09711  1   MET   D CA    
2777 C  C     . MET   C 2   ? 0.86309 0.61344 0.76901 0.05302  -0.05204 0.10570  1   MET   D C     
2778 O  O     . MET   C 2   ? 0.86673 0.61259 0.76436 0.05409  -0.04906 0.10431  1   MET   D O     
2779 C  CB    . MET   C 2   ? 0.91772 0.67782 0.84950 0.05309  -0.05059 0.09142  1   MET   D CB    
2780 C  CG    . MET   C 2   ? 0.94168 0.70186 0.89466 0.05176  -0.05147 0.09389  1   MET   D CG    
2781 S  SD    . MET   C 2   ? 1.00512 0.72492 0.93571 0.03950  -0.02137 0.08774  1   MET   D SD    
2782 C  CE    . MET   C 2   ? 1.01789 0.72637 0.93944 0.02922  -0.01972 0.07558  1   MET   D CE    
2783 N  N     . VAL   C 3   ? 0.79139 0.57018 0.70813 0.05174  -0.06470 0.12826  2   VAL   D N     
2784 C  CA    . VAL   C 3   ? 0.70986 0.51167 0.65586 0.06046  -0.10567 0.15134  2   VAL   D CA    
2785 C  C     . VAL   C 3   ? 0.58523 0.44348 0.57805 0.03656  -0.11555 0.18984  2   VAL   D C     
2786 O  O     . VAL   C 3   ? 0.56042 0.47184 0.54953 0.04929  -0.14645 0.19093  2   VAL   D O     
2787 C  CB    . VAL   C 3   ? 0.75943 0.51316 0.68117 0.09771  -0.12206 0.12932  2   VAL   D CB    
2788 C  CG1   . VAL   C 3   ? 0.76267 0.51119 0.69734 0.10205  -0.09573 0.12562  2   VAL   D CG1   
2789 C  CG2   . VAL   C 3   ? 0.79247 0.51356 0.68201 0.11400  -0.13850 0.12702  2   VAL   D CG2   
2790 N  N     . ASN   C 4   ? 0.46479 0.36777 0.52757 0.02008  -0.11119 0.20156  3   ASN   D N     
2791 C  CA    . ASN   C 4   ? 0.43738 0.29906 0.45739 0.03411  -0.02556 0.16847  3   ASN   D CA    
2792 C  C     . ASN   C 4   ? 0.40990 0.29032 0.43676 0.05874  -0.02620 0.13345  3   ASN   D C     
2793 O  O     . ASN   C 4   ? 0.43866 0.30792 0.43731 0.05783  -0.04520 0.14288  3   ASN   D O     
2794 C  CB    . ASN   C 4   ? 0.37749 0.25007 0.39607 0.06171  -0.00586 0.14527  3   ASN   D CB    
2795 C  CG    . ASN   C 4   ? 0.44608 0.23670 0.41516 0.05856  0.01996  0.11411  3   ASN   D CG    
2796 O  OD1   . ASN   C 4   ? 0.40163 0.24096 0.39649 0.06160  -0.00185 0.10536  3   ASN   D OD1   
2797 N  ND2   . ASN   C 4   ? 0.41897 0.21292 0.39200 0.07435  0.06225  0.11553  3   ASN   D ND2   
2798 N  N     . PRO   C 5   ? 0.33389 0.26302 0.40128 0.06759  -0.03991 0.10454  4   PRO   D N     
2799 C  CA    . PRO   C 5   ? 0.30804 0.23567 0.37275 0.06435  0.01040  0.07470  4   PRO   D CA    
2800 C  C     . PRO   C 5   ? 0.22517 0.21132 0.33313 0.07644  -0.03963 0.06295  4   PRO   D C     
2801 O  O     . PRO   C 5   ? 0.22830 0.22824 0.33110 0.05682  -0.02190 0.06170  4   PRO   D O     
2802 C  CB    . PRO   C 5   ? 0.34645 0.24085 0.40437 0.03067  0.04428  0.04005  4   PRO   D CB    
2803 C  CG    . PRO   C 5   ? 0.29248 0.25499 0.42651 -0.02623 -0.00196 0.05899  4   PRO   D CG    
2804 C  CD    . PRO   C 5   ? 0.32148 0.23900 0.39525 0.02168  -0.04394 0.09934  4   PRO   D CD    
2805 N  N     . THR   C 6   ? 0.27232 0.20450 0.30701 0.02072  -0.03825 0.06527  5   THR   D N     
2806 C  CA    A THR   C 6   ? 0.30751 0.19604 0.28176 0.01866  -0.04170 0.06770  5   THR   D CA    
2807 C  CA    B THR   C 6   ? 0.32840 0.21275 0.30665 0.02337  -0.00663 0.05735  5   THR   D CA    
2808 C  C     . THR   C 6   ? 0.24787 0.20521 0.27211 0.05350  -0.02258 0.04927  5   THR   D C     
2809 O  O     . THR   C 6   ? 0.21448 0.23500 0.29571 0.04033  0.00012  0.03440  5   THR   D O     
2810 C  CB    A THR   C 6   ? 0.36341 0.16518 0.28872 -0.01304 -0.05302 0.06041  5   THR   D CB    
2811 C  CB    B THR   C 6   ? 0.42354 0.22141 0.35749 0.01253  0.04864  0.02750  5   THR   D CB    
2812 O  OG1   A THR   C 6   ? 0.47089 0.17084 0.33512 -0.00013 -0.03275 0.06269  5   THR   D OG1   
2813 O  OG1   B THR   C 6   ? 0.43555 0.22917 0.40993 0.06278  0.08536  -0.01854 5   THR   D OG1   
2814 C  CG2   A THR   C 6   ? 0.33603 0.14504 0.29088 -0.01287 -0.08304 0.02398  5   THR   D CG2   
2815 C  CG2   B THR   C 6   ? 0.50202 0.23498 0.39122 -0.00760 0.04126  0.01839  5   THR   D CG2   
2816 N  N     . VAL   C 7   ? 0.27094 0.17342 0.23404 0.03343  -0.00209 0.03999  6   VAL   D N     
2817 C  CA    . VAL   C 7   ? 0.27415 0.20097 0.20020 0.06887  0.01212  0.02713  6   VAL   D CA    
2818 C  C     . VAL   C 7   ? 0.18342 0.21383 0.22612 0.05575  0.01592  0.02071  6   VAL   D C     
2819 O  O     . VAL   C 7   ? 0.19538 0.23145 0.24841 0.00636  -0.02111 0.00683  6   VAL   D O     
2820 C  CB    . VAL   C 7   ? 0.27319 0.25929 0.22438 0.03455  0.01201  0.00523  6   VAL   D CB    
2821 C  CG1   . VAL   C 7   ? 0.27448 0.29343 0.21273 0.00854  -0.02273 -0.00010 6   VAL   D CG1   
2822 C  CG2   . VAL   C 7   ? 0.21445 0.26070 0.24679 0.06481  -0.00383 0.03144  6   VAL   D CG2   
2823 N  N     . PHE   C 8   ? 0.22495 0.20504 0.24386 0.03089  0.04782  0.00230  7   PHE   D N     
2824 C  CA    . PHE   C 8   ? 0.23242 0.21683 0.23924 -0.00935 0.02187  -0.01509 7   PHE   D CA    
2825 C  C     . PHE   C 8   ? 0.16006 0.19242 0.23264 -0.00711 0.01926  -0.02804 7   PHE   D C     
2826 O  O     . PHE   C 8   ? 0.18058 0.17817 0.21490 0.02725  -0.01581 -0.03163 7   PHE   D O     
2827 C  CB    . PHE   C 8   ? 0.26241 0.21918 0.25914 0.04272  -0.02706 -0.04484 7   PHE   D CB    
2828 C  CG    . PHE   C 8   ? 0.19751 0.23609 0.30099 0.05688  0.00907  -0.04555 7   PHE   D CG    
2829 C  CD1   . PHE   C 8   ? 0.19440 0.27787 0.33425 0.03074  0.01607  -0.03406 7   PHE   D CD1   
2830 C  CD2   . PHE   C 8   ? 0.22324 0.26378 0.31718 0.04196  0.05740  -0.02985 7   PHE   D CD2   
2831 C  CE1   . PHE   C 8   ? 0.20058 0.29007 0.36275 0.03116  0.04449  -0.01828 7   PHE   D CE1   
2832 C  CE2   . PHE   C 8   ? 0.19209 0.27935 0.36043 0.06079  0.02249  0.01826  7   PHE   D CE2   
2833 C  CZ    . PHE   C 8   ? 0.15747 0.29639 0.37258 0.04548  0.05686  0.00487  7   PHE   D CZ    
2834 N  N     . PHE   C 9   ? 0.17708 0.19466 0.20996 0.01475  -0.01654 0.01035  8   PHE   D N     
2835 C  CA    . PHE   C 9   ? 0.14068 0.21132 0.17996 0.00574  0.00760  -0.01568 8   PHE   D CA    
2836 C  C     . PHE   C 9   ? 0.14862 0.20630 0.21921 0.00523  0.00238  -0.03764 8   PHE   D C     
2837 O  O     . PHE   C 9   ? 0.18683 0.20616 0.23620 -0.01646 0.01523  -0.03705 8   PHE   D O     
2838 C  CB    . PHE   C 9   ? 0.13522 0.23045 0.17153 0.04502  0.00394  -0.00451 8   PHE   D CB    
2839 C  CG    . PHE   C 9   ? 0.17416 0.18633 0.18833 -0.00390 0.02055  -0.00837 8   PHE   D CG    
2840 C  CD1   . PHE   C 9   ? 0.19800 0.20983 0.18130 0.04493  0.02883  -0.00705 8   PHE   D CD1   
2841 C  CD2   . PHE   C 9   ? 0.18002 0.17999 0.20663 0.00626  0.05852  0.00335  8   PHE   D CD2   
2842 C  CE1   . PHE   C 9   ? 0.16304 0.20312 0.22318 -0.00152 -0.00162 -0.01425 8   PHE   D CE1   
2843 C  CE2   . PHE   C 9   ? 0.18782 0.16991 0.21219 0.02791  0.03586  0.00681  8   PHE   D CE2   
2844 C  CZ    . PHE   C 9   ? 0.22117 0.17033 0.19837 -0.00582 0.02747  -0.01589 8   PHE   D CZ    
2845 N  N     . ASP   C 10  ? 0.14981 0.20799 0.21182 0.02752  0.03910  -0.03131 9   ASP   D N     
2846 C  CA    . ASP   C 10  ? 0.18245 0.23028 0.24178 0.04125  0.06875  -0.02248 9   ASP   D CA    
2847 C  C     . ASP   C 10  ? 0.17835 0.19120 0.21929 -0.00156 0.01084  -0.03332 9   ASP   D C     
2848 O  O     . ASP   C 10  ? 0.18211 0.19196 0.23397 -0.01730 0.00778  -0.02807 9   ASP   D O     
2849 C  CB    . ASP   C 10  ? 0.12370 0.25787 0.28518 0.03307  0.04361  -0.02637 9   ASP   D CB    
2850 C  CG    . ASP   C 10  ? 0.15435 0.30676 0.35809 0.00853  -0.00671 -0.01905 9   ASP   D CG    
2851 O  OD1   . ASP   C 10  ? 0.24938 0.31053 0.34823 0.03757  -0.00582 -0.01120 9   ASP   D OD1   
2852 O  OD2   . ASP   C 10  ? 0.22872 0.33050 0.42044 0.06336  -0.04906 -0.01952 9   ASP   D OD2   
2853 N  N     . ILE   C 11  ? 0.16169 0.17953 0.20205 0.03126  0.02094  -0.05004 10  ILE   D N     
2854 C  CA    . ILE   C 11  ? 0.15504 0.18876 0.20248 0.00564  0.01214  -0.01551 10  ILE   D CA    
2855 C  C     . ILE   C 11  ? 0.15934 0.18310 0.19388 -0.01022 0.02590  -0.05890 10  ILE   D C     
2856 O  O     . ILE   C 11  ? 0.20504 0.20169 0.21399 0.02058  0.01130  -0.04237 10  ILE   D O     
2857 C  CB    . ILE   C 11  ? 0.17314 0.19398 0.19929 0.01973  -0.00284 -0.01353 10  ILE   D CB    
2858 C  CG1   . ILE   C 11  ? 0.20066 0.21553 0.16872 0.01427  0.03160  -0.00298 10  ILE   D CG1   
2859 C  CG2   . ILE   C 11  ? 0.22494 0.18987 0.20247 -0.01309 -0.00934 -0.03063 10  ILE   D CG2   
2860 C  CD1   . ILE   C 11  ? 0.20348 0.24231 0.16078 -0.00673 0.04199  -0.01392 10  ILE   D CD1   
2861 N  N     . ALA   C 12  ? 0.16397 0.19816 0.16307 0.00421  0.04285  -0.01780 11  ALA   D N     
2862 C  CA    . ALA   C 12  ? 0.13788 0.20601 0.17562 -0.01927 0.02255  -0.01340 11  ALA   D CA    
2863 C  C     . ALA   C 12  ? 0.18528 0.20663 0.15915 0.00242  0.06448  -0.02693 11  ALA   D C     
2864 O  O     . ALA   C 12  ? 0.19687 0.20334 0.17791 -0.00220 0.03359  -0.02400 11  ALA   D O     
2865 C  CB    . ALA   C 12  ? 0.18061 0.22247 0.23411 -0.02903 0.02909  -0.01321 11  ALA   D CB    
2866 N  N     . VAL   C 13  ? 0.18193 0.21378 0.18040 -0.03274 0.04585  -0.01264 12  VAL   D N     
2867 C  CA    . VAL   C 13  ? 0.19356 0.20498 0.18736 -0.01282 0.03461  0.01491  12  VAL   D CA    
2868 C  C     . VAL   C 13  ? 0.24272 0.19148 0.18182 0.04957  0.04572  -0.00430 12  VAL   D C     
2869 O  O     . VAL   C 13  ? 0.20066 0.23831 0.17085 0.00131  0.03423  -0.02689 12  VAL   D O     
2870 C  CB    . VAL   C 13  ? 0.20187 0.23396 0.19990 -0.00068 0.01600  -0.02549 12  VAL   D CB    
2871 C  CG1   . VAL   C 13  ? 0.17044 0.23989 0.21298 -0.00453 0.00838  -0.03309 12  VAL   D CG1   
2872 C  CG2   . VAL   C 13  ? 0.18457 0.26026 0.23781 -0.00258 0.01164  -0.04715 12  VAL   D CG2   
2873 N  N     . ASP   C 14  ? 0.20618 0.21223 0.20974 -0.00623 0.05208  0.00459  13  ASP   D N     
2874 C  CA    . ASP   C 14  ? 0.24219 0.22580 0.20811 -0.01956 0.03525  0.02185  13  ASP   D CA    
2875 C  C     . ASP   C 14  ? 0.21589 0.20668 0.21626 0.00742  -0.02973 0.00878  13  ASP   D C     
2876 O  O     . ASP   C 14  ? 0.26411 0.24664 0.26871 -0.04496 0.07832  0.00344  13  ASP   D O     
2877 C  CB    . ASP   C 14  ? 0.26641 0.25871 0.23994 -0.00252 0.06518  0.05002  13  ASP   D CB    
2878 C  CG    . ASP   C 14  ? 0.29241 0.31279 0.23426 -0.00625 0.04277  0.02841  13  ASP   D CG    
2879 O  OD1   . ASP   C 14  ? 0.31572 0.31242 0.26613 0.01212  0.02618  0.01523  13  ASP   D OD1   
2880 O  OD2   . ASP   C 14  ? 0.30758 0.35294 0.22127 0.02147  0.04833  0.02303  13  ASP   D OD2   
2881 N  N     . GLY   C 15  ? 0.17491 0.21361 0.22886 -0.00183 -0.00293 -0.02008 14  GLY   D N     
2882 C  CA    . GLY   C 15  ? 0.19249 0.22903 0.24594 -0.03322 0.02333  -0.03540 14  GLY   D CA    
2883 C  C     . GLY   C 15  ? 0.19054 0.23505 0.24701 -0.03373 0.04040  -0.04339 14  GLY   D C     
2884 O  O     . GLY   C 15  ? 0.16135 0.26722 0.32018 -0.03753 -0.02007 -0.05966 14  GLY   D O     
2885 N  N     . GLU   C 16  ? 0.20207 0.21026 0.20709 -0.04164 0.04371  -0.04306 15  GLU   D N     
2886 C  CA    . GLU   C 16  ? 0.17870 0.24001 0.18913 -0.01059 0.01534  -0.04118 15  GLU   D CA    
2887 C  C     . GLU   C 16  ? 0.14978 0.26700 0.19380 -0.00475 0.03399  -0.01915 15  GLU   D C     
2888 O  O     . GLU   C 16  ? 0.15300 0.22297 0.21799 -0.00009 0.04743  -0.02034 15  GLU   D O     
2889 C  CB    . GLU   C 16  ? 0.18595 0.24943 0.14631 -0.03751 0.01975  -0.01450 15  GLU   D CB    
2890 C  CG    . GLU   C 16  ? 0.21827 0.25552 0.19859 -0.01920 0.06406  -0.00987 15  GLU   D CG    
2891 C  CD    . GLU   C 16  ? 0.19122 0.26956 0.25006 0.00623  0.07323  0.04310  15  GLU   D CD    
2892 O  OE1   . GLU   C 16  ? 0.26513 0.28317 0.27692 -0.03483 0.08501  0.04296  15  GLU   D OE1   
2893 O  OE2   . GLU   C 16  ? 0.20302 0.27572 0.24353 0.00921  0.00875  0.03975  15  GLU   D OE2   
2894 N  N     . PRO   C 17  ? 0.13538 0.29241 0.19673 -0.00180 0.03853  -0.01138 16  PRO   D N     
2895 C  CA    A PRO   C 17  ? 0.18329 0.28014 0.22269 -0.01121 0.01543  -0.02291 16  PRO   D CA    
2896 C  CA    B PRO   C 17  ? 0.17411 0.27667 0.20852 0.00461  0.03590  -0.02913 16  PRO   D CA    
2897 C  C     . PRO   C 17  ? 0.19677 0.26248 0.19075 0.00566  0.05116  -0.03608 16  PRO   D C     
2898 O  O     . PRO   C 17  ? 0.23825 0.31300 0.20614 0.01058  0.05461  -0.06611 16  PRO   D O     
2899 C  CB    A PRO   C 17  ? 0.22886 0.29436 0.26436 -0.01649 0.02832  -0.00893 16  PRO   D CB    
2900 C  CB    B PRO   C 17  ? 0.18529 0.28345 0.22709 0.02645  0.07239  -0.02670 16  PRO   D CB    
2901 C  CG    A PRO   C 17  ? 0.24973 0.30640 0.26160 -0.01143 0.00721  0.00488  16  PRO   D CG    
2902 C  CG    B PRO   C 17  ? 0.14092 0.29111 0.20896 0.06552  0.06518  -0.01170 16  PRO   D CG    
2903 C  CD    A PRO   C 17  ? 0.18822 0.31486 0.24954 0.01468  0.00319  0.00037  16  PRO   D CD    
2904 C  CD    B PRO   C 17  ? 0.16629 0.30874 0.22762 0.04644  0.02803  -0.01267 16  PRO   D CD    
2905 N  N     . LEU   C 18  ? 0.18184 0.22480 0.19876 -0.00428 0.04495  -0.05096 17  LEU   D N     
2906 C  CA    . LEU   C 18  ? 0.15750 0.23136 0.24245 -0.00446 0.02554  -0.04203 17  LEU   D CA    
2907 C  C     . LEU   C 18  ? 0.21655 0.20067 0.19524 -0.01096 0.07569  -0.05736 17  LEU   D C     
2908 O  O     . LEU   C 18  ? 0.25064 0.20703 0.23033 0.01143  0.03318  -0.06533 17  LEU   D O     
2909 C  CB    . LEU   C 18  ? 0.17166 0.25305 0.21277 0.00776  0.01848  -0.02476 17  LEU   D CB    
2910 C  CG    . LEU   C 18  ? 0.16560 0.25981 0.24365 -0.02709 0.00038  -0.06885 17  LEU   D CG    
2911 C  CD1   . LEU   C 18  ? 0.18977 0.30833 0.26222 -0.02491 -0.05088 -0.05323 17  LEU   D CD1   
2912 C  CD2   . LEU   C 18  ? 0.14796 0.25988 0.26693 0.01102  0.01072  -0.07614 17  LEU   D CD2   
2913 N  N     . GLY   C 19  ? 0.22060 0.21316 0.21330 0.01337  0.04196  -0.04684 18  GLY   D N     
2914 C  CA    . GLY   C 19  ? 0.25053 0.18843 0.22504 0.02459  0.07304  -0.03322 18  GLY   D CA    
2915 C  C     . GLY   C 19  ? 0.20641 0.18579 0.22709 0.02837  0.02827  -0.03375 18  GLY   D C     
2916 O  O     . GLY   C 19  ? 0.24082 0.19592 0.21050 0.01545  0.03961  -0.05608 18  GLY   D O     
2917 N  N     . ARG   C 20  ? 0.25559 0.18075 0.20060 0.03764  0.03361  -0.03159 19  ARG   D N     
2918 C  CA    . ARG   C 20  ? 0.20790 0.18152 0.21413 0.03491  0.05921  -0.00070 19  ARG   D CA    
2919 C  C     . ARG   C 20  ? 0.23874 0.19249 0.23743 -0.01842 0.05204  -0.02463 19  ARG   D C     
2920 O  O     . ARG   C 20  ? 0.30172 0.17969 0.27370 -0.03797 0.06631  -0.04338 19  ARG   D O     
2921 C  CB    . ARG   C 20  ? 0.29234 0.19034 0.22311 0.06723  0.02106  -0.01310 19  ARG   D CB    
2922 C  CG    . ARG   C 20  ? 0.26366 0.21043 0.24130 0.06889  -0.00265 -0.05567 19  ARG   D CG    
2923 C  CD    . ARG   C 20  ? 0.22213 0.23326 0.29381 0.02557  -0.04152 -0.04087 19  ARG   D CD    
2924 N  NE    . ARG   C 20  ? 0.22509 0.25365 0.32574 0.05664  -0.05828 -0.04352 19  ARG   D NE    
2925 C  CZ    . ARG   C 20  ? 0.23311 0.27408 0.36022 0.06580  -0.03408 -0.02350 19  ARG   D CZ    
2926 N  NH1   . ARG   C 20  ? 0.28307 0.27886 0.37892 0.07428  0.03407  0.00310  19  ARG   D NH1   
2927 N  NH2   . ARG   C 20  ? 0.23752 0.26863 0.37464 0.05778  0.00795  -0.03218 19  ARG   D NH2   
2928 N  N     . VAL   C 21  ? 0.18794 0.19224 0.21687 0.00456  0.03186  -0.00978 20  VAL   D N     
2929 C  CA    . VAL   C 21  ? 0.21415 0.18798 0.22688 -0.00110 0.02241  0.01399  20  VAL   D CA    
2930 C  C     . VAL   C 21  ? 0.20661 0.19130 0.22251 0.00979  0.04142  0.00732  20  VAL   D C     
2931 O  O     . VAL   C 21  ? 0.20635 0.20217 0.23683 -0.01463 0.00725  -0.02834 20  VAL   D O     
2932 C  CB    . VAL   C 21  ? 0.18636 0.22399 0.21630 0.01097  0.01152  0.00530  20  VAL   D CB    
2933 C  CG1   . VAL   C 21  ? 0.20434 0.21922 0.24573 -0.02055 -0.01447 0.03183  20  VAL   D CG1   
2934 C  CG2   . VAL   C 21  ? 0.20210 0.24374 0.25600 0.02509  -0.01867 0.00134  20  VAL   D CG2   
2935 N  N     . SER   C 22  ? 0.22713 0.17214 0.25233 0.02918  0.03404  -0.00216 21  SER   D N     
2936 C  CA    . SER   C 22  ? 0.24417 0.19798 0.24911 0.02445  0.06287  0.00440  21  SER   D CA    
2937 C  C     . SER   C 22  ? 0.23284 0.17996 0.22449 0.03566  0.03143  0.00694  21  SER   D C     
2938 O  O     . SER   C 22  ? 0.25624 0.20999 0.24165 0.01431  -0.00064 -0.01185 21  SER   D O     
2939 C  CB    . SER   C 22  ? 0.18665 0.22764 0.35846 0.01225  0.00611  -0.01504 21  SER   D CB    
2940 O  OG    . SER   C 22  ? 0.27407 0.21197 0.40073 0.04506  0.00695  0.02437  21  SER   D OG    
2941 N  N     . PHE   C 23  ? 0.23659 0.16139 0.21174 0.03853  0.01397  0.01148  22  PHE   D N     
2942 C  CA    . PHE   C 23  ? 0.19533 0.15632 0.24915 0.04235  0.00696  0.01363  22  PHE   D CA    
2943 C  C     . PHE   C 23  ? 0.18270 0.17872 0.27455 0.04666  -0.00369 0.02109  22  PHE   D C     
2944 O  O     . PHE   C 23  ? 0.20226 0.21696 0.27105 0.03415  -0.01465 0.01786  22  PHE   D O     
2945 C  CB    . PHE   C 23  ? 0.21873 0.15858 0.27506 0.03672  -0.00443 0.00744  22  PHE   D CB    
2946 C  CG    . PHE   C 23  ? 0.21660 0.16227 0.24094 0.03987  -0.00668 0.00490  22  PHE   D CG    
2947 C  CD1   . PHE   C 23  ? 0.22924 0.17293 0.20259 0.01180  0.01531  0.02433  22  PHE   D CD1   
2948 C  CD2   . PHE   C 23  ? 0.25317 0.16474 0.26648 0.00067  -0.02732 0.02714  22  PHE   D CD2   
2949 C  CE1   . PHE   C 23  ? 0.21457 0.15912 0.23876 -0.01165 0.04171  -0.00109 22  PHE   D CE1   
2950 C  CE2   . PHE   C 23  ? 0.19733 0.17293 0.30158 0.01995  -0.01837 0.01159  22  PHE   D CE2   
2951 C  CZ    . PHE   C 23  ? 0.19972 0.16944 0.26826 0.00099  0.01547  -0.01132 22  PHE   D CZ    
2952 N  N     . GLU   C 24  ? 0.25298 0.15822 0.25363 0.02394  0.04311  0.03033  23  GLU   D N     
2953 C  CA    . GLU   C 24  ? 0.30109 0.12643 0.24188 0.03947  0.02239  0.01181  23  GLU   D CA    
2954 C  C     . GLU   C 24  ? 0.24874 0.14306 0.23058 0.04226  0.03183  0.01958  23  GLU   D C     
2955 O  O     . GLU   C 24  ? 0.23596 0.16065 0.24219 0.05081  -0.00456 0.01617  23  GLU   D O     
2956 C  CB    . GLU   C 24  ? 0.30237 0.13723 0.27702 0.05669  0.00197  0.01667  23  GLU   D CB    
2957 C  CG    . GLU   C 24  ? 0.34886 0.13461 0.30805 0.03175  0.04466  0.04610  23  GLU   D CG    
2958 C  CD    . GLU   C 24  ? 0.40623 0.17815 0.33561 0.01228  0.03159  0.03224  23  GLU   D CD    
2959 O  OE1   . GLU   C 24  ? 0.48802 0.16535 0.33896 -0.04292 0.03682  -0.00339 23  GLU   D OE1   
2960 O  OE2   . GLU   C 24  ? 0.39925 0.20606 0.35444 0.00202  0.07947  0.04849  23  GLU   D OE2   
2961 N  N     . LEU   C 25  ? 0.26032 0.12529 0.24015 0.01864  0.00123  0.00249  24  LEU   D N     
2962 C  CA    . LEU   C 25  ? 0.25255 0.16290 0.23603 -0.00296 -0.01133 0.01288  24  LEU   D CA    
2963 C  C     . LEU   C 25  ? 0.22147 0.17393 0.24115 0.01279  0.01332  0.05795  24  LEU   D C     
2964 O  O     . LEU   C 25  ? 0.24825 0.18751 0.27124 0.04242  -0.00788 0.04063  24  LEU   D O     
2965 C  CB    . LEU   C 25  ? 0.23223 0.16621 0.25303 0.01055  -0.01548 0.02367  24  LEU   D CB    
2966 C  CG    . LEU   C 25  ? 0.20724 0.16487 0.26656 0.00770  -0.02518 0.00153  24  LEU   D CG    
2967 C  CD1   . LEU   C 25  ? 0.25524 0.19059 0.26707 0.02566  0.02429  0.00051  24  LEU   D CD1   
2968 C  CD2   . LEU   C 25  ? 0.16631 0.16136 0.29416 0.04019  -0.04857 -0.01035 24  LEU   D CD2   
2969 N  N     . PHE   C 26  ? 0.23444 0.17968 0.26793 0.00135  0.00469  0.04731  25  PHE   D N     
2970 C  CA    . PHE   C 26  ? 0.31030 0.18387 0.26376 0.01936  0.01567  0.05070  25  PHE   D CA    
2971 C  C     . PHE   C 26  ? 0.31958 0.19384 0.24761 0.07052  0.02179  0.09063  25  PHE   D C     
2972 O  O     . PHE   C 26  ? 0.33141 0.23421 0.29839 0.07133  0.05193  0.08278  25  PHE   D O     
2973 C  CB    . PHE   C 26  ? 0.26322 0.20946 0.27509 0.01292  0.02829  0.02355  25  PHE   D CB    
2974 C  CG    . PHE   C 26  ? 0.31504 0.24275 0.30935 0.02024  0.04137  0.01571  25  PHE   D CG    
2975 C  CD1   . PHE   C 26  ? 0.35657 0.28127 0.30537 0.02093  0.05030  -0.01629 25  PHE   D CD1   
2976 C  CD2   . PHE   C 26  ? 0.31801 0.24173 0.31257 -0.00192 0.05212  0.07162  25  PHE   D CD2   
2977 C  CE1   . PHE   C 26  ? 0.36647 0.29674 0.34579 0.00641  0.04679  0.00742  25  PHE   D CE1   
2978 C  CE2   . PHE   C 26  ? 0.36392 0.24749 0.31405 -0.01608 0.04527  0.05147  25  PHE   D CE2   
2979 C  CZ    . PHE   C 26  ? 0.35151 0.27561 0.31854 0.00423  0.08501  0.04781  25  PHE   D CZ    
2980 N  N     . ALA   C 27  ? 0.36637 0.18754 0.26873 0.02890  -0.05187 0.04399  26  ALA   D N     
2981 C  CA    . ALA   C 27  ? 0.32207 0.20665 0.27357 0.01279  -0.03798 0.04127  26  ALA   D CA    
2982 C  C     . ALA   C 27  ? 0.35816 0.23254 0.28389 0.02843  -0.00139 0.06766  26  ALA   D C     
2983 O  O     . ALA   C 27  ? 0.37659 0.25255 0.28711 0.05886  0.01177  0.09957  26  ALA   D O     
2984 C  CB    . ALA   C 27  ? 0.34631 0.22917 0.27036 -0.03134 -0.05752 -0.00020 26  ALA   D CB    
2985 N  N     . ASP   C 28  ? 0.32703 0.22636 0.30734 0.03297  0.02837  0.08845  27  ASP   D N     
2986 C  CA    . ASP   C 28  ? 0.34562 0.23495 0.30471 0.05048  0.05724  0.11247  27  ASP   D CA    
2987 C  C     . ASP   C 28  ? 0.37022 0.27322 0.33314 0.03359  0.05649  0.13423  27  ASP   D C     
2988 O  O     . ASP   C 28  ? 0.42441 0.34056 0.35198 0.05385  0.06322  0.12722  27  ASP   D O     
2989 C  CB    . ASP   C 28  ? 0.45084 0.21048 0.32327 0.07680  0.01302  0.09194  27  ASP   D CB    
2990 C  CG    . ASP   C 28  ? 0.55504 0.20513 0.37162 0.00870  0.02831  0.03834  27  ASP   D CG    
2991 O  OD1   . ASP   C 28  ? 0.54237 0.22659 0.38971 -0.01850 -0.01419 0.03405  27  ASP   D OD1   
2992 O  OD2   . ASP   C 28  ? 0.74023 0.24122 0.45388 -0.01232 0.05723  -0.00568 27  ASP   D OD2   
2993 N  N     . LYS   C 29  ? 0.35142 0.24760 0.35173 0.02805  0.00828  0.09426  28  LYS   D N     
2994 C  CA    . LYS   C 29  ? 0.32061 0.22951 0.33617 0.01001  -0.00717 0.07751  28  LYS   D CA    
2995 C  C     . LYS   C 29  ? 0.29423 0.23048 0.27176 0.00694  0.02999  0.08219  28  LYS   D C     
2996 O  O     . LYS   C 29  ? 0.31432 0.21887 0.26604 0.03013  0.04972  0.09916  28  LYS   D O     
2997 C  CB    . LYS   C 29  ? 0.35519 0.23028 0.43325 -0.01688 -0.03166 0.01141  28  LYS   D CB    
2998 C  CG    . LYS   C 29  ? 0.40896 0.22819 0.53067 -0.03443 -0.03145 0.00016  28  LYS   D CG    
2999 C  CD    . LYS   C 29  ? 0.47840 0.25145 0.61067 -0.06916 -0.01885 -0.00922 28  LYS   D CD    
3000 C  CE    . LYS   C 29  ? 0.45495 0.24851 0.63582 -0.10115 -0.02033 -0.02657 28  LYS   D CE    
3001 N  NZ    . LYS   C 29  ? 0.43627 0.25751 0.66435 -0.09816 0.01110  -0.02754 28  LYS   D NZ    
3002 N  N     . VAL   C 30  ? 0.23615 0.20892 0.24308 0.00670  0.00892  0.06768  29  VAL   D N     
3003 C  CA    . VAL   C 30  ? 0.26277 0.20181 0.26942 0.02823  -0.02150 0.06227  29  VAL   D CA    
3004 C  C     . VAL   C 30  ? 0.25303 0.18953 0.24497 0.03667  -0.00400 0.04055  29  VAL   D C     
3005 O  O     . VAL   C 30  ? 0.25902 0.18431 0.25965 0.01401  -0.00077 0.04441  29  VAL   D O     
3006 C  CB    . VAL   C 30  ? 0.26215 0.19803 0.26399 -0.01511 -0.03473 0.05942  29  VAL   D CB    
3007 C  CG1   . VAL   C 30  ? 0.31214 0.20776 0.29834 0.02712  0.02853  0.07816  29  VAL   D CG1   
3008 C  CG2   . VAL   C 30  ? 0.29961 0.24464 0.26953 0.01599  -0.00865 0.04470  29  VAL   D CG2   
3009 N  N     . PRO   C 31  ? 0.27730 0.22226 0.21002 0.01882  0.00036  0.05401  30  PRO   D N     
3010 C  CA    . PRO   C 31  ? 0.21732 0.19606 0.21301 0.04510  -0.00435 0.07943  30  PRO   D CA    
3011 C  C     . PRO   C 31  ? 0.25721 0.19645 0.22726 0.04269  -0.01319 0.05525  30  PRO   D C     
3012 O  O     . PRO   C 31  ? 0.26855 0.19553 0.23919 0.02779  0.01453  0.04911  30  PRO   D O     
3013 C  CB    . PRO   C 31  ? 0.34259 0.22380 0.20297 0.00632  -0.00527 0.06529  30  PRO   D CB    
3014 C  CG    . PRO   C 31  ? 0.37569 0.23356 0.18871 0.01064  -0.00598 0.04476  30  PRO   D CG    
3015 C  CD    . PRO   C 31  ? 0.36468 0.22485 0.19226 0.00311  -0.02474 0.05415  30  PRO   D CD    
3016 N  N     . LYS   C 32  ? 0.29387 0.21429 0.20962 0.03744  -0.00994 0.02259  31  LYS   D N     
3017 C  CA    A LYS   C 32  ? 0.31715 0.21226 0.19461 0.03376  0.01679  0.05274  31  LYS   D CA    
3018 C  CA    B LYS   C 32  ? 0.32876 0.22289 0.19155 0.03684  0.01181  0.03627  31  LYS   D CA    
3019 C  C     . LYS   C 32  ? 0.28078 0.18173 0.18983 0.02851  0.03452  0.05542  31  LYS   D C     
3020 O  O     . LYS   C 32  ? 0.26511 0.20588 0.15532 0.00062  -0.00494 0.02148  31  LYS   D O     
3021 C  CB    A LYS   C 32  ? 0.36399 0.24163 0.16756 0.04070  0.01812  0.04897  31  LYS   D CB    
3022 C  CB    B LYS   C 32  ? 0.39250 0.26879 0.15862 0.04970  -0.00652 0.01287  31  LYS   D CB    
3023 C  CG    A LYS   C 32  ? 0.33892 0.25890 0.17937 0.02506  0.07220  0.07292  31  LYS   D CG    
3024 C  CG    B LYS   C 32  ? 0.43501 0.30518 0.17010 0.04789  0.01877  0.00974  31  LYS   D CG    
3025 C  CD    A LYS   C 32  ? 0.38576 0.26993 0.19290 0.01050  0.10735  0.07158  31  LYS   D CD    
3026 C  CD    B LYS   C 32  ? 0.45772 0.32761 0.17331 0.04128  0.02977  -0.00938 31  LYS   D CD    
3027 C  CE    A LYS   C 32  ? 0.35689 0.27541 0.22010 0.03528  0.13372  0.06349  31  LYS   D CE    
3028 C  CE    B LYS   C 32  ? 0.44615 0.33873 0.18544 0.02911  0.04509  0.00845  31  LYS   D CE    
3029 N  NZ    A LYS   C 32  ? 0.40961 0.28492 0.21208 0.05993  0.12426  0.06202  31  LYS   D NZ    
3030 N  NZ    B LYS   C 32  ? 0.41974 0.34992 0.20655 -0.00997 0.03774  0.00231  31  LYS   D NZ    
3031 N  N     . THR   C 33  ? 0.25173 0.19972 0.16699 0.03244  -0.00134 0.02917  32  THR   D N     
3032 C  CA    . THR   C 33  ? 0.22965 0.20903 0.15727 0.01184  -0.01181 0.02477  32  THR   D CA    
3033 C  C     . THR   C 33  ? 0.20575 0.19860 0.14334 0.02062  0.02848  0.04401  32  THR   D C     
3034 O  O     . THR   C 33  ? 0.22493 0.19677 0.17296 0.04710  -0.00094 0.04038  32  THR   D O     
3035 C  CB    . THR   C 33  ? 0.19963 0.20795 0.18209 0.02568  0.04264  0.03176  32  THR   D CB    
3036 O  OG1   . THR   C 33  ? 0.23740 0.20668 0.18812 0.02195  0.01556  0.01571  32  THR   D OG1   
3037 C  CG2   . THR   C 33  ? 0.20834 0.21641 0.19396 0.03836  0.02425  0.05339  32  THR   D CG2   
3038 N  N     . ALA   C 34  ? 0.22230 0.17358 0.19246 0.03121  -0.00509 0.04635  33  ALA   D N     
3039 C  CA    . ALA   C 34  ? 0.21664 0.17736 0.21545 0.04791  -0.03056 0.02235  33  ALA   D CA    
3040 C  C     . ALA   C 34  ? 0.18239 0.16671 0.19173 0.04030  0.01152  0.03501  33  ALA   D C     
3041 O  O     . ALA   C 34  ? 0.19075 0.18653 0.21316 0.02218  -0.00721 0.03482  33  ALA   D O     
3042 C  CB    . ALA   C 34  ? 0.30470 0.16464 0.23223 0.04009  -0.02557 0.00309  33  ALA   D CB    
3043 N  N     . GLU   C 35  ? 0.23059 0.19836 0.18245 0.01624  -0.03406 0.02813  34  GLU   D N     
3044 C  CA    . GLU   C 35  ? 0.26902 0.19789 0.16674 0.01969  -0.04596 0.03147  34  GLU   D CA    
3045 C  C     . GLU   C 35  ? 0.25199 0.17345 0.21255 0.01681  -0.02751 0.02527  34  GLU   D C     
3046 O  O     . GLU   C 35  ? 0.22620 0.18471 0.21618 0.01170  -0.04182 0.04111  34  GLU   D O     
3047 C  CB    . GLU   C 35  ? 0.27652 0.22385 0.20757 0.01435  -0.06807 0.00252  34  GLU   D CB    
3048 C  CG    . GLU   C 35  ? 0.31307 0.26370 0.22813 0.03120  -0.06791 0.00010  34  GLU   D CG    
3049 C  CD    . GLU   C 35  ? 0.36533 0.29580 0.26247 0.03881  -0.02669 0.01083  34  GLU   D CD    
3050 O  OE1   . GLU   C 35  ? 0.35105 0.28359 0.23457 0.08135  -0.03865 0.03101  34  GLU   D OE1   
3051 O  OE2   . GLU   C 35  ? 0.39141 0.32003 0.29780 0.02635  -0.03631 -0.00807 34  GLU   D OE2   
3052 N  N     . ASN   C 36  ? 0.23957 0.16926 0.16683 0.01752  -0.02391 0.01793  35  ASN   D N     
3053 C  CA    . ASN   C 36  ? 0.23400 0.16928 0.17498 0.04242  -0.02244 0.00223  35  ASN   D CA    
3054 C  C     . ASN   C 36  ? 0.19165 0.18473 0.19174 0.03909  -0.02208 0.01815  35  ASN   D C     
3055 O  O     . ASN   C 36  ? 0.18356 0.18861 0.18636 0.01340  -0.00058 -0.00325 35  ASN   D O     
3056 C  CB    . ASN   C 36  ? 0.23396 0.16865 0.16329 0.05761  0.01060  0.02019  35  ASN   D CB    
3057 C  CG    . ASN   C 36  ? 0.22561 0.17141 0.17529 0.05566  -0.01430 -0.00172 35  ASN   D CG    
3058 O  OD1   . ASN   C 36  ? 0.28104 0.16517 0.17936 -0.00688 -0.05336 -0.01300 35  ASN   D OD1   
3059 N  ND2   . ASN   C 36  ? 0.19892 0.18499 0.19110 0.02911  -0.02196 0.00373  35  ASN   D ND2   
3060 N  N     . PHE   C 37  ? 0.21517 0.18536 0.15258 0.00944  -0.03186 -0.00181 36  PHE   D N     
3061 C  CA    . PHE   C 37  ? 0.20188 0.16571 0.19431 0.01704  -0.01777 0.00285  36  PHE   D CA    
3062 C  C     . PHE   C 37  ? 0.17357 0.16080 0.20616 0.01213  -0.01574 0.01332  36  PHE   D C     
3063 O  O     . PHE   C 37  ? 0.14309 0.22029 0.19487 0.01985  -0.01824 0.01319  36  PHE   D O     
3064 C  CB    . PHE   C 37  ? 0.18247 0.14334 0.20833 0.02209  -0.00943 -0.02911 36  PHE   D CB    
3065 C  CG    . PHE   C 37  ? 0.20153 0.16752 0.18545 0.02540  -0.00777 -0.01159 36  PHE   D CG    
3066 C  CD1   . PHE   C 37  ? 0.18844 0.14247 0.18094 0.00319  -0.02466 0.01275  36  PHE   D CD1   
3067 C  CD2   . PHE   C 37  ? 0.21435 0.17390 0.19480 0.00637  0.00388  -0.00379 36  PHE   D CD2   
3068 C  CE1   . PHE   C 37  ? 0.16803 0.16812 0.21615 -0.02483 -0.01163 0.02746  36  PHE   D CE1   
3069 C  CE2   . PHE   C 37  ? 0.20213 0.20288 0.20708 -0.01068 -0.00105 0.00807  36  PHE   D CE2   
3070 C  CZ    . PHE   C 37  ? 0.19891 0.19743 0.21760 -0.03524 -0.01759 -0.01501 36  PHE   D CZ    
3071 N  N     . ARG   C 38  ? 0.16982 0.16721 0.21238 0.01148  -0.04170 0.00391  37  ARG   D N     
3072 C  CA    . ARG   C 38  ? 0.19008 0.16326 0.21412 0.02242  -0.02962 0.03692  37  ARG   D CA    
3073 C  C     . ARG   C 38  ? 0.17301 0.18613 0.18533 0.01804  0.00031  0.01871  37  ARG   D C     
3074 O  O     . ARG   C 38  ? 0.19049 0.18265 0.18833 0.01769  0.00370  0.00914  37  ARG   D O     
3075 C  CB    . ARG   C 38  ? 0.24217 0.17190 0.25507 0.04983  -0.03608 0.03469  37  ARG   D CB    
3076 C  CG    . ARG   C 38  ? 0.20758 0.18925 0.25109 0.05618  -0.02814 0.01817  37  ARG   D CG    
3077 C  CD    . ARG   C 38  ? 0.27503 0.21724 0.23802 0.02409  -0.07299 0.02273  37  ARG   D CD    
3078 N  NE    . ARG   C 38  ? 0.24618 0.22616 0.23150 0.00127  -0.06253 0.05733  37  ARG   D NE    
3079 C  CZ    . ARG   C 38  ? 0.26548 0.25805 0.27005 0.02802  -0.03848 0.04029  37  ARG   D CZ    
3080 N  NH1   . ARG   C 38  ? 0.25578 0.26045 0.27022 0.05861  -0.07560 0.04184  37  ARG   D NH1   
3081 N  NH2   . ARG   C 38  ? 0.25082 0.27254 0.24061 0.00881  -0.05197 0.05842  37  ARG   D NH2   
3082 N  N     . ALA   C 39  ? 0.21441 0.18205 0.20600 0.00028  -0.04690 0.01487  38  ALA   D N     
3083 C  CA    . ALA   C 39  ? 0.22857 0.21180 0.16920 0.02159  -0.03013 -0.00572 38  ALA   D CA    
3084 C  C     . ALA   C 39  ? 0.21020 0.19771 0.20555 0.01246  -0.05412 0.01081  38  ALA   D C     
3085 O  O     . ALA   C 39  ? 0.21113 0.21845 0.22803 0.01409  -0.02159 0.01525  38  ALA   D O     
3086 C  CB    . ALA   C 39  ? 0.24042 0.23048 0.16012 0.03021  -0.04019 -0.01750 38  ALA   D CB    
3087 N  N     . LEU   C 40  ? 0.17330 0.18121 0.21120 0.04801  -0.04197 0.01503  39  LEU   D N     
3088 C  CA    . LEU   C 40  ? 0.15618 0.20374 0.19798 0.03628  -0.02950 0.00916  39  LEU   D CA    
3089 C  C     . LEU   C 40  ? 0.15057 0.19428 0.22079 0.00289  -0.00876 0.00800  39  LEU   D C     
3090 O  O     . LEU   C 40  ? 0.15384 0.19264 0.24931 0.02144  0.00464  0.02995  39  LEU   D O     
3091 C  CB    . LEU   C 40  ? 0.13270 0.20835 0.19323 0.03021  0.00897  0.00842  39  LEU   D CB    
3092 C  CG    . LEU   C 40  ? 0.17375 0.19100 0.18225 0.01790  -0.00123 -0.00502 39  LEU   D CG    
3093 C  CD1   . LEU   C 40  ? 0.20240 0.18995 0.20227 0.02658  -0.03060 0.01015  39  LEU   D CD1   
3094 C  CD2   . LEU   C 40  ? 0.19889 0.18022 0.23418 -0.00124 -0.00866 -0.02032 39  LEU   D CD2   
3095 N  N     . SER   C 41  ? 0.20388 0.19563 0.21910 0.01729  -0.02915 -0.02930 40  SER   D N     
3096 C  CA    . SER   C 41  ? 0.12932 0.22615 0.22606 0.02481  -0.03937 -0.05069 40  SER   D CA    
3097 C  C     . SER   C 41  ? 0.18981 0.22258 0.20115 0.02116  -0.04718 -0.03343 40  SER   D C     
3098 O  O     . SER   C 41  ? 0.19361 0.27309 0.23795 0.05015  -0.01069 -0.00146 40  SER   D O     
3099 C  CB    . SER   C 41  ? 0.22282 0.20344 0.24143 0.03204  -0.04344 -0.04331 40  SER   D CB    
3100 O  OG    . SER   C 41  ? 0.17806 0.20470 0.22741 0.00232  -0.03598 -0.00640 40  SER   D OG    
3101 N  N     . THR   C 42  ? 0.17115 0.23572 0.22287 0.03678  -0.01926 -0.01532 41  THR   D N     
3102 C  CA    . THR   C 42  ? 0.17049 0.26177 0.25136 0.04890  -0.06051 -0.00298 41  THR   D CA    
3103 C  C     . THR   C 42  ? 0.15160 0.25246 0.26496 0.05036  -0.04945 0.00142  41  THR   D C     
3104 O  O     . THR   C 42  ? 0.17995 0.28858 0.27854 0.04256  -0.01809 0.00124  41  THR   D O     
3105 C  CB    . THR   C 42  ? 0.15943 0.26876 0.24933 0.01997  -0.02987 -0.00321 41  THR   D CB    
3106 O  OG1   . THR   C 42  ? 0.19436 0.26994 0.22632 0.02533  -0.03850 0.00620  41  THR   D OG1   
3107 C  CG2   . THR   C 42  ? 0.22795 0.27889 0.28717 0.00878  -0.05553 0.00900  41  THR   D CG2   
3108 N  N     . GLY   C 43  ? 0.21769 0.23157 0.24352 0.03855  -0.05507 -0.03091 42  GLY   D N     
3109 C  CA    . GLY   C 43  ? 0.18789 0.26653 0.28912 0.02146  -0.07957 -0.01725 42  GLY   D CA    
3110 C  C     . GLY   C 43  ? 0.23724 0.29618 0.29375 0.01535  -0.06931 0.00069  42  GLY   D C     
3111 O  O     . GLY   C 43  ? 0.23853 0.30349 0.27836 0.01108  -0.04790 0.02576  42  GLY   D O     
3112 N  N     . GLU   C 44  ? 0.19072 0.29402 0.28316 0.03664  -0.06931 -0.00605 43  GLU   D N     
3113 C  CA    . GLU   C 44  ? 0.20496 0.28996 0.27385 0.01117  -0.09869 -0.01035 43  GLU   D CA    
3114 C  C     . GLU   C 44  ? 0.20550 0.29658 0.31354 -0.02552 -0.06434 -0.01983 43  GLU   D C     
3115 O  O     . GLU   C 44  ? 0.25420 0.31030 0.31484 -0.02144 -0.09537 -0.03316 43  GLU   D O     
3116 C  CB    . GLU   C 44  ? 0.25067 0.26911 0.26889 -0.00750 -0.07495 0.05368  43  GLU   D CB    
3117 C  CG    . GLU   C 44  ? 0.28410 0.24927 0.24969 -0.00607 -0.05930 0.03629  43  GLU   D CG    
3118 C  CD    . GLU   C 44  ? 0.30945 0.28399 0.24006 0.03242  -0.08677 0.03737  43  GLU   D CD    
3119 O  OE1   . GLU   C 44  ? 0.32851 0.29492 0.27200 0.05743  -0.02640 -0.00429 43  GLU   D OE1   
3120 O  OE2   . GLU   C 44  ? 0.38561 0.29653 0.23519 0.02083  -0.04658 0.03314  43  GLU   D OE2   
3121 N  N     . LYS   C 45  ? 0.22649 0.25727 0.27770 0.00714  -0.04788 0.00389  44  LYS   D N     
3122 C  CA    . LYS   C 45  ? 0.21459 0.27129 0.28537 -0.00586 -0.03974 0.02460  44  LYS   D CA    
3123 C  C     . LYS   C 45  ? 0.24489 0.28770 0.30115 -0.03134 -0.07793 0.02189  44  LYS   D C     
3124 O  O     . LYS   C 45  ? 0.23400 0.30059 0.36490 -0.04303 -0.04240 0.01564  44  LYS   D O     
3125 C  CB    . LYS   C 45  ? 0.21860 0.28950 0.30666 0.01091  -0.05562 0.02675  44  LYS   D CB    
3126 C  CG    . LYS   C 45  ? 0.21203 0.30903 0.30884 -0.00108 -0.04178 0.07312  44  LYS   D CG    
3127 C  CD    . LYS   C 45  ? 0.32507 0.31947 0.28859 0.00135  -0.05284 0.05930  44  LYS   D CD    
3128 C  CE    . LYS   C 45  ? 0.46326 0.34063 0.30001 0.01981  -0.07553 0.05886  44  LYS   D CE    
3129 N  NZ    . LYS   C 45  ? 0.51657 0.36069 0.31012 0.01279  -0.06478 0.03449  44  LYS   D NZ    
3130 N  N     . GLY   C 46  ? 0.23971 0.29467 0.27342 -0.05581 -0.07651 0.04744  45  GLY   D N     
3131 C  CA    . GLY   C 46  ? 0.22172 0.29424 0.30601 -0.02929 -0.09198 0.03568  45  GLY   D CA    
3132 C  C     . GLY   C 46  ? 0.27131 0.28763 0.29352 -0.02831 -0.10649 0.05681  45  GLY   D C     
3133 O  O     . GLY   C 46  ? 0.27192 0.27190 0.34224 -0.04391 -0.11257 0.07540  45  GLY   D O     
3134 N  N     . PHE   C 47  ? 0.22778 0.25670 0.26671 -0.03447 -0.09716 0.00836  46  PHE   D N     
3135 C  CA    . PHE   C 47  ? 0.21480 0.23640 0.24381 -0.00306 -0.08004 -0.00141 46  PHE   D CA    
3136 C  C     . PHE   C 47  ? 0.21052 0.22224 0.20619 -0.03231 -0.05752 0.01949  46  PHE   D C     
3137 O  O     . PHE   C 47  ? 0.22316 0.21849 0.24531 -0.00670 -0.08759 0.03908  46  PHE   D O     
3138 C  CB    . PHE   C 47  ? 0.20284 0.24050 0.23904 0.00283  -0.05082 -0.01602 46  PHE   D CB    
3139 C  CG    . PHE   C 47  ? 0.23268 0.25165 0.22996 0.02851  -0.03501 -0.03017 46  PHE   D CG    
3140 C  CD1   . PHE   C 47  ? 0.27053 0.24755 0.21928 -0.01081 -0.02781 -0.03186 46  PHE   D CD1   
3141 C  CD2   . PHE   C 47  ? 0.28677 0.26073 0.21397 0.00447  -0.04687 -0.01065 46  PHE   D CD2   
3142 C  CE1   . PHE   C 47  ? 0.27798 0.27233 0.22350 -0.01265 -0.07588 -0.04190 46  PHE   D CE1   
3143 C  CE2   . PHE   C 47  ? 0.32160 0.26864 0.25667 -0.01693 -0.08098 -0.01410 46  PHE   D CE2   
3144 C  CZ    . PHE   C 47  ? 0.27872 0.28607 0.26804 -0.00836 -0.04059 -0.03285 46  PHE   D CZ    
3145 N  N     . GLY   C 48  ? 0.22748 0.19838 0.20553 -0.01560 -0.05768 -0.01181 47  GLY   D N     
3146 C  CA    . GLY   C 48  ? 0.22436 0.18181 0.21265 -0.00624 -0.07060 -0.00993 47  GLY   D CA    
3147 C  C     . GLY   C 48  ? 0.15055 0.17501 0.23214 -0.02966 -0.02392 -0.00043 47  GLY   D C     
3148 O  O     . GLY   C 48  ? 0.17379 0.18861 0.20039 -0.00761 -0.01129 -0.00790 47  GLY   D O     
3149 N  N     . TYR   C 49  ? 0.14048 0.19309 0.18744 0.00697  -0.01830 0.00219  48  TYR   D N     
3150 C  CA    . TYR   C 49  ? 0.17119 0.18703 0.15166 -0.01303 -0.02513 -0.01447 48  TYR   D CA    
3151 C  C     . TYR   C 49  ? 0.13440 0.19252 0.16100 -0.00440 -0.01601 -0.00279 48  TYR   D C     
3152 O  O     . TYR   C 49  ? 0.18331 0.21817 0.14884 0.02127  0.01035  0.02199  48  TYR   D O     
3153 C  CB    . TYR   C 49  ? 0.15558 0.16674 0.18324 -0.00615 -0.00604 0.00144  48  TYR   D CB    
3154 C  CG    . TYR   C 49  ? 0.18539 0.16641 0.16852 0.01197  -0.02532 -0.00681 48  TYR   D CG    
3155 C  CD1   . TYR   C 49  ? 0.17621 0.16709 0.17146 0.02158  -0.04184 -0.00120 48  TYR   D CD1   
3156 C  CD2   . TYR   C 49  ? 0.15856 0.17270 0.20263 0.00434  -0.01406 -0.01847 48  TYR   D CD2   
3157 C  CE1   . TYR   C 49  ? 0.15178 0.17541 0.15863 0.01731  -0.01835 -0.01291 48  TYR   D CE1   
3158 C  CE2   . TYR   C 49  ? 0.17378 0.17922 0.18426 0.02490  -0.02193 -0.03089 48  TYR   D CE2   
3159 C  CZ    . TYR   C 49  ? 0.19659 0.16246 0.16290 0.01375  -0.02361 0.01040  48  TYR   D CZ    
3160 O  OH    . TYR   C 49  ? 0.16999 0.15476 0.16802 0.00597  0.00198  0.01942  48  TYR   D OH    
3161 N  N     . LYS   C 50  ? 0.13906 0.16116 0.17453 -0.00265 -0.00350 -0.00599 49  LYS   D N     
3162 C  CA    . LYS   C 50  ? 0.14125 0.21273 0.18949 0.02410  -0.00099 0.03364  49  LYS   D CA    
3163 C  C     . LYS   C 50  ? 0.15062 0.19214 0.16990 0.00409  -0.02182 -0.01720 49  LYS   D C     
3164 O  O     . LYS   C 50  ? 0.20961 0.19562 0.20768 -0.02453 -0.01989 -0.02067 49  LYS   D O     
3165 C  CB    . LYS   C 50  ? 0.13875 0.24574 0.22815 0.00204  -0.01060 0.00803  49  LYS   D CB    
3166 C  CG    . LYS   C 50  ? 0.11990 0.28018 0.22788 0.00307  0.00297  -0.02560 49  LYS   D CG    
3167 C  CD    . LYS   C 50  ? 0.16674 0.31959 0.25861 -0.00633 0.01328  0.02434  49  LYS   D CD    
3168 C  CE    . LYS   C 50  ? 0.14030 0.35880 0.29523 0.00761  0.02497  0.08573  49  LYS   D CE    
3169 N  NZ    . LYS   C 50  ? 0.19525 0.40436 0.43108 0.07466  -0.01267 0.07339  49  LYS   D NZ    
3170 N  N     . GLY   C 51  ? 0.13409 0.21304 0.16629 0.01350  -0.00842 0.01597  50  GLY   D N     
3171 C  CA    . GLY   C 51  ? 0.15674 0.19901 0.18901 0.00964  0.02191  0.00612  50  GLY   D CA    
3172 C  C     . GLY   C 51  ? 0.20458 0.18772 0.14904 -0.00399 0.01281  0.01350  50  GLY   D C     
3173 O  O     . GLY   C 51  ? 0.17103 0.19872 0.16763 -0.02532 0.01534  -0.00471 50  GLY   D O     
3174 N  N     . SER   C 52  ? 0.16973 0.19782 0.14752 0.00572  -0.00739 -0.00902 51  SER   D N     
3175 C  CA    . SER   C 52  ? 0.16495 0.19529 0.15269 0.02017  -0.01734 -0.02204 51  SER   D CA    
3176 C  C     . SER   C 52  ? 0.14757 0.18731 0.18047 -0.00668 -0.00376 -0.01099 51  SER   D C     
3177 O  O     . SER   C 52  ? 0.17947 0.18745 0.20097 0.00337  0.01495  -0.01588 51  SER   D O     
3178 C  CB    . SER   C 52  ? 0.20655 0.20793 0.14793 -0.00063 -0.00125 -0.01470 51  SER   D CB    
3179 O  OG    . SER   C 52  ? 0.16256 0.22927 0.18010 -0.00254 0.01706  0.01888  51  SER   D OG    
3180 N  N     A CYS   C 53  ? 0.16856 0.20582 0.19588 -0.01933 -0.01230 -0.04279 52  CYS   D N     
3181 N  N     B CYS   C 53  ? 0.14325 0.18865 0.20811 -0.03510 -0.01931 -0.02536 52  CYS   D N     
3182 C  CA    A CYS   C 53  ? 0.15827 0.21036 0.14851 -0.01162 -0.01479 -0.01659 52  CYS   D CA    
3183 C  CA    B CYS   C 53  ? 0.16787 0.17955 0.15898 -0.01158 -0.01482 -0.02147 52  CYS   D CA    
3184 C  C     A CYS   C 53  ? 0.13435 0.19967 0.15248 -0.03241 -0.00018 -0.01627 52  CYS   D C     
3185 C  C     B CYS   C 53  ? 0.16370 0.18556 0.14741 -0.00851 0.00912  -0.03772 52  CYS   D C     
3186 O  O     A CYS   C 53  ? 0.12127 0.20352 0.16183 -0.03793 0.01519  -0.00689 52  CYS   D O     
3187 O  O     B CYS   C 53  ? 0.23597 0.20209 0.16204 -0.00042 0.01082  -0.06002 52  CYS   D O     
3188 C  CB    A CYS   C 53  ? 0.19572 0.22406 0.15640 0.01603  -0.03602 -0.02848 52  CYS   D CB    
3189 C  CB    B CYS   C 53  ? 0.17478 0.18530 0.17033 0.00269  -0.03904 -0.01634 52  CYS   D CB    
3190 S  SG    A CYS   C 53  ? 0.19081 0.23874 0.20303 0.00395  0.00225  -0.00005 52  CYS   D SG    
3191 S  SG    B CYS   C 53  ? 0.17352 0.18407 0.18150 0.00996  -0.00877 -0.00543 52  CYS   D SG    
3192 N  N     . PHE   C 54  ? 0.12135 0.18777 0.16798 0.00184  0.00005  -0.02886 53  PHE   D N     
3193 C  CA    . PHE   C 54  ? 0.13633 0.18526 0.17655 0.01071  0.00449  -0.01222 53  PHE   D CA    
3194 C  C     . PHE   C 54  ? 0.12274 0.19551 0.16529 -0.00612 0.03707  0.03376  53  PHE   D C     
3195 O  O     . PHE   C 54  ? 0.18040 0.22974 0.15492 0.01155  0.03195  0.02554  53  PHE   D O     
3196 C  CB    . PHE   C 54  ? 0.17045 0.18344 0.17598 0.01373  -0.00896 0.00477  53  PHE   D CB    
3197 C  CG    . PHE   C 54  ? 0.13260 0.18146 0.17436 0.01036  -0.01792 -0.01812 53  PHE   D CG    
3198 C  CD1   . PHE   C 54  ? 0.15262 0.19181 0.17553 0.01569  -0.00031 -0.04236 53  PHE   D CD1   
3199 C  CD2   . PHE   C 54  ? 0.19080 0.19738 0.15897 -0.04280 0.03262  -0.02858 53  PHE   D CD2   
3200 C  CE1   . PHE   C 54  ? 0.15858 0.21151 0.20386 0.01453  -0.03581 -0.01007 53  PHE   D CE1   
3201 C  CE2   . PHE   C 54  ? 0.19092 0.20135 0.20321 -0.01709 0.01421  -0.03469 53  PHE   D CE2   
3202 C  CZ    . PHE   C 54  ? 0.19256 0.20507 0.22239 -0.03237 -0.01051 -0.03305 53  PHE   D CZ    
3203 N  N     . HIS   C 55  ? 0.09586 0.19303 0.18419 0.00538  0.00831  0.00081  54  HIS   D N     
3204 C  CA    . HIS   C 55  ? 0.13335 0.19062 0.18930 0.00397  -0.02930 -0.01171 54  HIS   D CA    
3205 C  C     . HIS   C 55  ? 0.15513 0.19634 0.16269 0.00458  0.00285  0.01209  54  HIS   D C     
3206 O  O     . HIS   C 55  ? 0.16045 0.19374 0.19778 0.01882  -0.00772 0.03534  54  HIS   D O     
3207 C  CB    . HIS   C 55  ? 0.15830 0.18925 0.18781 -0.00675 0.01414  0.00576  54  HIS   D CB    
3208 C  CG    . HIS   C 55  ? 0.13286 0.20041 0.19066 0.00080  -0.01362 -0.00897 54  HIS   D CG    
3209 N  ND1   . HIS   C 55  ? 0.15771 0.23175 0.18907 -0.01917 0.00300  -0.00245 54  HIS   D ND1   
3210 C  CD2   . HIS   C 55  ? 0.17379 0.20030 0.19690 -0.01214 0.01327  -0.03573 54  HIS   D CD2   
3211 C  CE1   . HIS   C 55  ? 0.17340 0.22204 0.18494 -0.01001 0.01825  -0.00561 54  HIS   D CE1   
3212 N  NE2   . HIS   C 55  ? 0.16830 0.20948 0.19630 -0.00917 0.00429  -0.03303 54  HIS   D NE2   
3213 N  N     . ARG   C 56  ? 0.12653 0.19849 0.15849 0.00915  0.00052  -0.01477 55  ARG   D N     
3214 C  CA    . ARG   C 56  ? 0.14460 0.21086 0.15667 -0.01084 0.00432  -0.00590 55  ARG   D CA    
3215 C  C     . ARG   C 56  ? 0.14620 0.18860 0.14456 0.00719  -0.01103 0.01424  55  ARG   D C     
3216 O  O     . ARG   C 56  ? 0.17514 0.17960 0.17345 -0.01079 -0.02616 0.02275  55  ARG   D O     
3217 C  CB    . ARG   C 56  ? 0.16969 0.22714 0.14698 -0.01170 0.00407  0.02093  55  ARG   D CB    
3218 C  CG    . ARG   C 56  ? 0.13041 0.23742 0.19512 -0.00671 -0.00045 0.01931  55  ARG   D CG    
3219 C  CD    . ARG   C 56  ? 0.11638 0.18499 0.22780 0.02052  0.02616  -0.00593 55  ARG   D CD    
3220 N  NE    . ARG   C 56  ? 0.14626 0.17922 0.27645 0.00829  0.04492  0.00948  55  ARG   D NE    
3221 C  CZ    . ARG   C 56  ? 0.15126 0.18299 0.27844 0.00395  0.05881  -0.00394 55  ARG   D CZ    
3222 N  NH1   . ARG   C 56  ? 0.17712 0.21721 0.21335 -0.02579 0.01096  0.01397  55  ARG   D NH1   
3223 N  NH2   . ARG   C 56  ? 0.27000 0.20695 0.39719 0.00855  0.09875  -0.03871 55  ARG   D NH2   
3224 N  N     . ILE   C 57  ? 0.16228 0.17562 0.15771 0.01383  0.00313  0.00151  56  ILE   D N     
3225 C  CA    . ILE   C 57  ? 0.15633 0.18865 0.17238 -0.00333 -0.01685 -0.01414 56  ILE   D CA    
3226 C  C     . ILE   C 57  ? 0.16121 0.22636 0.16105 0.00917  -0.01896 0.00505  56  ILE   D C     
3227 O  O     . ILE   C 57  ? 0.16873 0.21781 0.17828 -0.00433 -0.02369 0.02852  56  ILE   D O     
3228 C  CB    . ILE   C 57  ? 0.17691 0.20938 0.17936 0.02244  -0.04975 -0.02607 56  ILE   D CB    
3229 C  CG1   . ILE   C 57  ? 0.13640 0.24050 0.20184 0.01478  -0.02100 -0.03528 56  ILE   D CG1   
3230 C  CG2   . ILE   C 57  ? 0.20224 0.21921 0.20540 -0.00042 -0.01524 -0.05863 56  ILE   D CG2   
3231 C  CD1   . ILE   C 57  ? 0.19211 0.27058 0.21957 0.01631  -0.04103 -0.02548 56  ILE   D CD1   
3232 N  N     . ILE   C 58  ? 0.14785 0.23646 0.17678 -0.01804 -0.02122 -0.02698 57  ILE   D N     
3233 C  CA    . ILE   C 58  ? 0.19306 0.23754 0.17219 -0.03567 -0.01070 -0.01362 57  ILE   D CA    
3234 C  C     . ILE   C 58  ? 0.20993 0.23639 0.18108 -0.04151 -0.04343 -0.00369 57  ILE   D C     
3235 O  O     . ILE   C 58  ? 0.22313 0.23439 0.21223 -0.04139 -0.05739 -0.01173 57  ILE   D O     
3236 C  CB    . ILE   C 58  ? 0.16804 0.24205 0.19457 -0.05107 -0.02536 -0.00454 57  ILE   D CB    
3237 C  CG1   . ILE   C 58  ? 0.17448 0.25112 0.20227 -0.02377 0.02055  0.00337  57  ILE   D CG1   
3238 C  CG2   . ILE   C 58  ? 0.16856 0.25720 0.22300 -0.02480 -0.04436 0.02031  57  ILE   D CG2   
3239 C  CD1   . ILE   C 58  ? 0.22276 0.26991 0.21044 -0.02883 -0.00307 0.01937  57  ILE   D CD1   
3240 N  N     . PRO   C 59  ? 0.22947 0.24765 0.18053 -0.03057 -0.07156 -0.00467 58  PRO   D N     
3241 C  CA    . PRO   C 59  ? 0.30955 0.27646 0.20427 -0.08944 -0.06135 -0.01766 58  PRO   D CA    
3242 C  C     . PRO   C 59  ? 0.35315 0.27906 0.22765 -0.08319 -0.07044 -0.03531 58  PRO   D C     
3243 O  O     . PRO   C 59  ? 0.38508 0.30278 0.26148 -0.06500 -0.09102 -0.04235 58  PRO   D O     
3244 C  CB    . PRO   C 59  ? 0.36956 0.28655 0.19108 -0.06678 -0.07795 -0.00125 58  PRO   D CB    
3245 C  CG    . PRO   C 59  ? 0.38137 0.28898 0.15560 -0.02112 -0.07419 -0.02239 58  PRO   D CG    
3246 C  CD    . PRO   C 59  ? 0.32784 0.28752 0.14859 -0.01141 -0.02776 -0.00558 58  PRO   D CD    
3247 N  N     . GLY   C 60  ? 0.36850 0.25493 0.23331 -0.08871 -0.03254 -0.03175 59  GLY   D N     
3248 C  CA    . GLY   C 60  ? 0.38023 0.26570 0.27832 -0.08260 -0.04840 0.00997  59  GLY   D CA    
3249 C  C     . GLY   C 60  ? 0.30922 0.24556 0.26300 -0.07686 -0.03988 -0.01620 59  GLY   D C     
3250 O  O     . GLY   C 60  ? 0.29925 0.25826 0.29297 -0.09373 -0.07035 -0.01036 59  GLY   D O     
3251 N  N     . PHE   C 61  ? 0.21130 0.22456 0.23524 -0.01609 -0.05996 -0.02931 60  PHE   D N     
3252 C  CA    . PHE   C 61  ? 0.18877 0.20877 0.24548 -0.00862 -0.04398 0.01082  60  PHE   D CA    
3253 C  C     . PHE   C 61  ? 0.13918 0.19303 0.24296 -0.02115 -0.02341 -0.02916 60  PHE   D C     
3254 O  O     . PHE   C 61  ? 0.20435 0.19718 0.22905 -0.01811 -0.01065 0.01131  60  PHE   D O     
3255 C  CB    . PHE   C 61  ? 0.17029 0.22289 0.25291 -0.04692 -0.04737 0.02005  60  PHE   D CB    
3256 C  CG    . PHE   C 61  ? 0.16412 0.24977 0.25387 -0.05348 -0.03918 0.01737  60  PHE   D CG    
3257 C  CD1   . PHE   C 61  ? 0.17146 0.27380 0.26653 -0.06645 -0.02634 0.01587  60  PHE   D CD1   
3258 C  CD2   . PHE   C 61  ? 0.20977 0.25270 0.25861 -0.05137 -0.06815 0.00126  60  PHE   D CD2   
3259 C  CE1   . PHE   C 61  ? 0.17952 0.27613 0.26729 -0.01496 -0.00516 -0.00025 60  PHE   D CE1   
3260 C  CE2   . PHE   C 61  ? 0.23989 0.24951 0.29138 -0.03931 -0.02617 -0.02214 60  PHE   D CE2   
3261 C  CZ    . PHE   C 61  ? 0.20091 0.26248 0.29846 -0.00732 -0.03464 -0.02225 60  PHE   D CZ    
3262 N  N     . MET   C 62  ? 0.14747 0.21084 0.22970 -0.02701 -0.00762 -0.04717 61  MET   D N     
3263 C  CA    . MET   C 62  ? 0.11787 0.21349 0.18744 0.00311  -0.02124 -0.01542 61  MET   D CA    
3264 C  C     . MET   C 62  ? 0.16997 0.20910 0.16973 0.00509  -0.03034 0.00756  61  MET   D C     
3265 O  O     . MET   C 62  ? 0.16423 0.19622 0.18882 0.00957  -0.00712 0.00027  61  MET   D O     
3266 C  CB    . MET   C 62  ? 0.18108 0.20170 0.19220 0.00955  0.00044  -0.02468 61  MET   D CB    
3267 C  CG    . MET   C 62  ? 0.19188 0.22031 0.20250 0.03948  -0.03283 -0.00559 61  MET   D CG    
3268 S  SD    . MET   C 62  ? 0.17600 0.20576 0.21315 0.00248  -0.02113 -0.01247 61  MET   D SD    
3269 C  CE    . MET   C 62  ? 0.23035 0.18082 0.23796 0.00549  0.02125  -0.00144 61  MET   D CE    
3270 N  N     . CYS   C 63  ? 0.15265 0.20281 0.16841 0.00766  -0.01447 -0.02255 62  CYS   D N     
3271 C  CA    . CYS   C 63  ? 0.15558 0.19725 0.15615 -0.02487 0.01436  -0.03141 62  CYS   D CA    
3272 C  C     . CYS   C 63  ? 0.13212 0.17427 0.12581 -0.01621 -0.01767 -0.01239 62  CYS   D C     
3273 O  O     . CYS   C 63  ? 0.20878 0.18137 0.13812 -0.00051 -0.01662 -0.01761 62  CYS   D O     
3274 C  CB    . CYS   C 63  ? 0.17635 0.21037 0.17744 0.00174  0.00769  -0.04125 62  CYS   D CB    
3275 S  SG    . CYS   C 63  ? 0.21553 0.22604 0.19468 0.00953  -0.00622 -0.03357 62  CYS   D SG    
3276 N  N     . GLN   C 64  ? 0.12926 0.16696 0.14720 0.00053  0.00588  -0.01628 63  GLN   D N     
3277 C  CA    . GLN   C 64  ? 0.11611 0.19147 0.16387 -0.00024 0.01237  -0.01965 63  GLN   D CA    
3278 C  C     . GLN   C 64  ? 0.15195 0.19093 0.12831 0.01384  -0.01010 0.00190  63  GLN   D C     
3279 O  O     . GLN   C 64  ? 0.13718 0.19583 0.14701 0.00078  -0.00166 0.00416  63  GLN   D O     
3280 C  CB    . GLN   C 64  ? 0.13083 0.19091 0.16207 0.00661  0.00161  -0.02895 63  GLN   D CB    
3281 C  CG    . GLN   C 64  ? 0.13531 0.16171 0.17310 -0.00516 0.03016  0.02102  63  GLN   D CG    
3282 C  CD    . GLN   C 64  ? 0.12967 0.18105 0.17500 0.02487  0.00269  0.01559  63  GLN   D CD    
3283 O  OE1   . GLN   C 64  ? 0.13853 0.20493 0.19793 -0.00706 0.01449  -0.00170 63  GLN   D OE1   
3284 N  NE2   . GLN   C 64  ? 0.15407 0.18808 0.16424 0.00530  -0.00827 -0.00422 63  GLN   D NE2   
3285 N  N     . GLY   C 65  ? 0.12319 0.17855 0.14211 -0.00689 0.00710  -0.01428 64  GLY   D N     
3286 C  CA    . GLY   C 65  ? 0.14547 0.17755 0.15702 0.00146  0.00624  -0.01793 64  GLY   D CA    
3287 C  C     . GLY   C 65  ? 0.09750 0.17442 0.17541 0.02873  -0.01645 -0.01119 64  GLY   D C     
3288 O  O     . GLY   C 65  ? 0.17380 0.16508 0.16762 -0.00594 0.01216  0.00408  64  GLY   D O     
3289 N  N     . GLY   C 66  ? 0.16493 0.17049 0.19517 0.01402  -0.03693 -0.02270 65  GLY   D N     
3290 C  CA    . GLY   C 66  ? 0.18773 0.16588 0.18905 0.02636  -0.05436 0.01110  65  GLY   D CA    
3291 C  C     . GLY   C 66  ? 0.19852 0.16198 0.17189 0.00619  -0.03965 0.00158  65  GLY   D C     
3292 O  O     . GLY   C 66  ? 0.20845 0.19938 0.18491 0.00709  -0.06802 0.01159  65  GLY   D O     
3293 N  N     . ASP   C 67  ? 0.14810 0.16298 0.18055 -0.00775 -0.00247 -0.02096 66  ASP   D N     
3294 C  CA    . ASP   C 67  ? 0.14815 0.17176 0.16601 -0.01146 -0.02499 -0.01683 66  ASP   D CA    
3295 C  C     . ASP   C 67  ? 0.13766 0.19584 0.16217 -0.00945 0.00348  0.00583  66  ASP   D C     
3296 O  O     . ASP   C 67  ? 0.15343 0.24702 0.16918 -0.03485 0.00357  0.00003  66  ASP   D O     
3297 C  CB    . ASP   C 67  ? 0.16999 0.17126 0.18030 0.03551  -0.05043 -0.00364 66  ASP   D CB    
3298 C  CG    . ASP   C 67  ? 0.16775 0.19565 0.18077 -0.00552 0.01510  -0.00274 66  ASP   D CG    
3299 O  OD1   . ASP   C 67  ? 0.19347 0.19319 0.18436 0.00014  -0.00325 -0.01552 66  ASP   D OD1   
3300 O  OD2   . ASP   C 67  ? 0.18716 0.18822 0.17668 0.03563  0.00172  0.00445  66  ASP   D OD2   
3301 N  N     . PHE   C 68  ? 0.13031 0.17847 0.17946 0.00324  0.01653  -0.01763 67  PHE   D N     
3302 C  CA    . PHE   C 68  ? 0.14693 0.19717 0.17360 0.00969  0.01240  -0.02377 67  PHE   D CA    
3303 C  C     . PHE   C 68  ? 0.14542 0.21436 0.15883 -0.02562 0.00018  -0.01291 67  PHE   D C     
3304 O  O     . PHE   C 68  ? 0.15199 0.20964 0.19642 0.00006  -0.00465 -0.00010 67  PHE   D O     
3305 C  CB    . PHE   C 68  ? 0.20511 0.21250 0.13984 0.03280  -0.02699 -0.02518 67  PHE   D CB    
3306 C  CG    . PHE   C 68  ? 0.15559 0.22114 0.17454 0.01931  -0.02371 -0.00926 67  PHE   D CG    
3307 C  CD1   . PHE   C 68  ? 0.19689 0.21935 0.19205 0.01782  -0.01789 -0.00675 67  PHE   D CD1   
3308 C  CD2   . PHE   C 68  ? 0.15715 0.24005 0.22111 0.02776  -0.06547 -0.00208 67  PHE   D CD2   
3309 C  CE1   . PHE   C 68  ? 0.25198 0.21630 0.18859 0.02026  -0.03214 -0.00257 67  PHE   D CE1   
3310 C  CE2   . PHE   C 68  ? 0.18174 0.24764 0.22951 0.02927  -0.04843 0.00577  67  PHE   D CE2   
3311 C  CZ    . PHE   C 68  ? 0.21197 0.23647 0.22450 0.03554  -0.04929 0.01684  67  PHE   D CZ    
3312 N  N     . THR   C 69  ? 0.17490 0.17613 0.18681 -0.00601 0.01170  -0.04022 68  THR   D N     
3313 C  CA    . THR   C 69  ? 0.20758 0.21420 0.17681 -0.01252 -0.01394 -0.03166 68  THR   D CA    
3314 C  C     . THR   C 69  ? 0.21950 0.19845 0.20172 0.01430  -0.00202 -0.01213 68  THR   D C     
3315 O  O     . THR   C 69  ? 0.27447 0.19893 0.30700 -0.01378 -0.06565 0.01046  68  THR   D O     
3316 C  CB    . THR   C 69  ? 0.20389 0.24921 0.17399 0.00137  -0.02611 -0.02045 68  THR   D CB    
3317 O  OG1   . THR   C 69  ? 0.20319 0.27462 0.22270 -0.02054 -0.02039 -0.02799 68  THR   D OG1   
3318 C  CG2   . THR   C 69  ? 0.25733 0.27465 0.18149 0.04497  -0.03196 0.00367  68  THR   D CG2   
3319 N  N     . ARG   C 70  ? 0.22572 0.17854 0.17912 0.01750  -0.00908 -0.00745 69  ARG   D N     
3320 C  CA    . ARG   C 70  ? 0.17553 0.18366 0.19727 0.02021  0.01491  -0.01879 69  ARG   D CA    
3321 C  C     . ARG   C 70  ? 0.17330 0.19638 0.17218 -0.00046 -0.01212 0.00511  69  ARG   D C     
3322 O  O     . ARG   C 70  ? 0.21668 0.23151 0.20501 0.01451  0.00350  0.01240  69  ARG   D O     
3323 C  CB    . ARG   C 70  ? 0.22934 0.21019 0.17501 0.01744  0.02201  -0.02059 69  ARG   D CB    
3324 C  CG    . ARG   C 70  ? 0.37036 0.24571 0.21913 -0.03863 0.01937  -0.05231 69  ARG   D CG    
3325 C  CD    . ARG   C 70  ? 0.48933 0.33479 0.27747 -0.05993 0.03231  -0.09556 69  ARG   D CD    
3326 N  NE    . ARG   C 70  ? 0.69213 0.39976 0.39673 -0.09690 -0.00037 -0.11124 69  ARG   D NE    
3327 C  CZ    . ARG   C 70  ? 0.84984 0.43034 0.45164 -0.11170 0.03399  -0.15028 69  ARG   D CZ    
3328 N  NH1   . ARG   C 70  ? 0.94269 0.45690 0.47028 -0.11410 0.06592  -0.12976 69  ARG   D NH1   
3329 N  NH2   . ARG   C 70  ? 0.85939 0.45426 0.48306 -0.13329 0.02610  -0.16620 69  ARG   D NH2   
3330 N  N     . HIS   C 71  ? 0.15934 0.20013 0.19378 -0.01005 -0.01533 -0.00167 70  HIS   D N     
3331 C  CA    . HIS   C 71  ? 0.15666 0.23037 0.19993 0.02779  -0.01363 0.00648  70  HIS   D CA    
3332 C  C     . HIS   C 71  ? 0.18101 0.23537 0.21393 0.02738  0.01536  0.01165  70  HIS   D C     
3333 O  O     . HIS   C 71  ? 0.22315 0.27073 0.22544 0.01205  0.01813  0.01693  70  HIS   D O     
3334 C  CB    . HIS   C 71  ? 0.15829 0.24643 0.19714 -0.00935 0.01988  -0.02070 70  HIS   D CB    
3335 C  CG    . HIS   C 71  ? 0.18988 0.24057 0.21838 -0.02288 0.01894  -0.02117 70  HIS   D CG    
3336 N  ND1   . HIS   C 71  ? 0.17681 0.24347 0.21481 0.01818  0.03357  0.00145  70  HIS   D ND1   
3337 C  CD2   . HIS   C 71  ? 0.15722 0.27661 0.26163 -0.01195 0.01871  -0.01252 70  HIS   D CD2   
3338 C  CE1   . HIS   C 71  ? 0.19314 0.28807 0.22858 0.01338  0.02521  -0.00318 70  HIS   D CE1   
3339 N  NE2   . HIS   C 71  ? 0.14326 0.29591 0.26137 0.00428  0.02641  -0.00598 70  HIS   D NE2   
3340 N  N     . ASN   C 72  ? 0.18677 0.20444 0.17621 0.01644  -0.00803 -0.00426 71  ASN   D N     
3341 C  CA    . ASN   C 72  ? 0.18114 0.22780 0.20465 -0.00915 -0.03924 0.04153  71  ASN   D CA    
3342 C  C     . ASN   C 72  ? 0.19838 0.22851 0.18783 0.04190  -0.03249 0.01344  71  ASN   D C     
3343 O  O     . ASN   C 72  ? 0.22384 0.21425 0.20176 0.01354  -0.02690 0.02163  71  ASN   D O     
3344 C  CB    . ASN   C 72  ? 0.22810 0.22858 0.26238 0.00359  -0.03695 0.02893  71  ASN   D CB    
3345 C  CG    . ASN   C 72  ? 0.23065 0.20225 0.31086 0.00974  -0.02237 0.02163  71  ASN   D CG    
3346 O  OD1   . ASN   C 72  ? 0.19367 0.18299 0.29494 -0.00714 -0.01715 0.01469  71  ASN   D OD1   
3347 N  ND2   . ASN   C 72  ? 0.30203 0.19682 0.37146 -0.01642 -0.00831 0.00750  71  ASN   D ND2   
3348 N  N     . GLY   C 73  ? 0.15054 0.23553 0.17384 0.01042  0.00708  0.00022  72  GLY   D N     
3349 C  CA    . GLY   C 73  ? 0.15319 0.22986 0.18119 -0.00341 -0.02391 -0.02172 72  GLY   D CA    
3350 C  C     . GLY   C 73  ? 0.18439 0.21812 0.16652 0.00123  -0.02865 0.00365  72  GLY   D C     
3351 O  O     . GLY   C 73  ? 0.15199 0.21227 0.20217 0.00413  -0.00767 -0.00458 72  GLY   D O     
3352 N  N     . THR   C 74  ? 0.18346 0.20192 0.14194 0.00197  -0.02795 0.00107  73  THR   D N     
3353 C  CA    . THR   C 74  ? 0.24464 0.20786 0.15094 -0.00181 -0.05911 0.01896  73  THR   D CA    
3354 C  C     . THR   C 74  ? 0.21466 0.20952 0.15326 -0.00090 -0.00714 0.02361  73  THR   D C     
3355 O  O     . THR   C 74  ? 0.18635 0.22398 0.17211 0.01094  -0.00632 0.01239  73  THR   D O     
3356 C  CB    . THR   C 74  ? 0.16398 0.22162 0.18632 0.01053  -0.02025 0.02298  73  THR   D CB    
3357 O  OG1   . THR   C 74  ? 0.18294 0.20571 0.23506 0.00504  -0.03592 0.00661  73  THR   D OG1   
3358 C  CG2   . THR   C 74  ? 0.27500 0.26335 0.19718 0.02248  -0.06893 0.04227  73  THR   D CG2   
3359 N  N     . GLY   C 75  ? 0.17134 0.18149 0.19496 -0.00155 -0.02767 0.02184  74  GLY   D N     
3360 C  CA    . GLY   C 75  ? 0.21492 0.19658 0.20417 -0.01437 -0.05834 0.02673  74  GLY   D CA    
3361 C  C     . GLY   C 75  ? 0.22682 0.19424 0.21445 -0.04877 -0.07285 -0.01608 74  GLY   D C     
3362 O  O     . GLY   C 75  ? 0.18313 0.22496 0.18650 0.01952  -0.03834 -0.01923 74  GLY   D O     
3363 N  N     . GLY   C 76  ? 0.36880 0.18529 0.26847 -0.04577 -0.14319 0.00960  75  GLY   D N     
3364 C  CA    . GLY   C 76  ? 0.36926 0.17686 0.28837 -0.00151 -0.15970 0.01504  75  GLY   D CA    
3365 C  C     . GLY   C 76  ? 0.30431 0.18237 0.27596 -0.00033 -0.11122 0.01478  75  GLY   D C     
3366 O  O     . GLY   C 76  ? 0.29941 0.23883 0.31605 0.06988  -0.03461 0.03773  75  GLY   D O     
3367 N  N     . LYS   C 77  ? 0.25764 0.16070 0.24639 0.01652  -0.05769 0.02268  76  LYS   D N     
3368 C  CA    . LYS   C 77  ? 0.28218 0.17373 0.19953 0.00649  -0.05085 0.01307  76  LYS   D CA    
3369 C  C     . LYS   C 77  ? 0.27413 0.19312 0.16560 0.01244  -0.03294 0.01768  76  LYS   D C     
3370 O  O     . LYS   C 77  ? 0.23284 0.19843 0.17439 0.02118  -0.04312 -0.00459 76  LYS   D O     
3371 C  CB    . LYS   C 77  ? 0.28131 0.21736 0.30331 -0.00736 -0.05657 0.01616  76  LYS   D CB    
3372 C  CG    . LYS   C 77  ? 0.24527 0.21085 0.34323 0.01214  -0.01439 -0.00163 76  LYS   D CG    
3373 C  CD    . LYS   C 77  ? 0.28690 0.23492 0.31987 -0.00170 -0.07990 -0.01197 76  LYS   D CD    
3374 C  CE    . LYS   C 77  ? 0.36144 0.24179 0.35267 -0.02280 -0.05975 -0.07019 76  LYS   D CE    
3375 N  NZ    . LYS   C 77  ? 0.39423 0.25830 0.36525 -0.02968 -0.07054 -0.07342 76  LYS   D NZ    
3376 N  N     . SER   C 78  ? 0.23660 0.18217 0.17170 0.01976  -0.02730 0.00978  77  SER   D N     
3377 C  CA    . SER   C 78  ? 0.19961 0.16490 0.16604 0.01912  -0.02948 0.01820  77  SER   D CA    
3378 C  C     . SER   C 78  ? 0.24567 0.16886 0.18631 0.00552  -0.00898 0.01823  77  SER   D C     
3379 O  O     . SER   C 78  ? 0.23418 0.19476 0.23459 -0.01511 -0.03342 -0.00269 77  SER   D O     
3380 C  CB    . SER   C 78  ? 0.23803 0.21768 0.13698 -0.00194 0.00085  -0.02860 77  SER   D CB    
3381 O  OG    . SER   C 78  ? 0.27627 0.21238 0.17527 0.02517  -0.02045 -0.01034 77  SER   D OG    
3382 N  N     . ILE   C 79  ? 0.25123 0.18691 0.20464 0.01374  -0.05633 -0.00410 78  ILE   D N     
3383 C  CA    . ILE   C 79  ? 0.24696 0.20761 0.22139 0.01721  -0.06900 0.00767  78  ILE   D CA    
3384 C  C     . ILE   C 79  ? 0.28401 0.23828 0.21240 -0.00036 -0.07215 -0.00062 78  ILE   D C     
3385 O  O     . ILE   C 79  ? 0.30753 0.28156 0.22373 0.04457  -0.07312 -0.04990 78  ILE   D O     
3386 C  CB    . ILE   C 79  ? 0.23512 0.22314 0.20596 0.03100  -0.04882 0.00685  78  ILE   D CB    
3387 C  CG1   . ILE   C 79  ? 0.26597 0.21452 0.23347 0.04996  -0.03596 0.00636  78  ILE   D CG1   
3388 C  CG2   . ILE   C 79  ? 0.23373 0.24238 0.19264 0.03163  -0.03300 0.00196  78  ILE   D CG2   
3389 C  CD1   . ILE   C 79  ? 0.24904 0.22193 0.22320 0.01177  -0.01183 0.01481  78  ILE   D CD1   
3390 N  N     . TYR   C 80  ? 0.30364 0.20457 0.17543 0.01079  -0.02736 0.00881  79  TYR   D N     
3391 C  CA    . TYR   C 80  ? 0.38351 0.20566 0.16050 0.01090  -0.01978 -0.01049 79  TYR   D CA    
3392 C  C     . TYR   C 80  ? 0.45441 0.21290 0.15110 0.02498  -0.01491 0.02988  79  TYR   D C     
3393 O  O     . TYR   C 80  ? 0.56327 0.23764 0.18191 0.01886  0.00630  0.00171  79  TYR   D O     
3394 C  CB    . TYR   C 80  ? 0.34494 0.22380 0.21303 -0.03535 0.00418  -0.00523 79  TYR   D CB    
3395 C  CG    . TYR   C 80  ? 0.31157 0.21319 0.18448 -0.00430 -0.01272 0.01358  79  TYR   D CG    
3396 C  CD1   . TYR   C 80  ? 0.31158 0.20491 0.23125 -0.01321 -0.02641 0.03835  79  TYR   D CD1   
3397 C  CD2   . TYR   C 80  ? 0.30341 0.21545 0.17358 0.02263  0.02277  0.02134  79  TYR   D CD2   
3398 C  CE1   . TYR   C 80  ? 0.29786 0.21292 0.19431 -0.01747 -0.05978 0.00950  79  TYR   D CE1   
3399 C  CE2   . TYR   C 80  ? 0.30999 0.19337 0.18236 0.04666  -0.00724 0.02843  79  TYR   D CE2   
3400 C  CZ    . TYR   C 80  ? 0.31104 0.19486 0.19839 0.02987  -0.06800 0.02208  79  TYR   D CZ    
3401 O  OH    . TYR   C 80  ? 0.27391 0.20217 0.22807 0.00967  -0.04118 0.02335  79  TYR   D OH    
3402 N  N     . GLY   C 81  ? 0.37897 0.19332 0.18816 0.06563  -0.00655 0.00744  80  GLY   D N     
3403 C  CA    . GLY   C 81  ? 0.41120 0.17862 0.20865 0.02265  -0.05321 0.02790  80  GLY   D CA    
3404 C  C     . GLY   C 81  ? 0.29089 0.18818 0.17344 0.01208  -0.04674 -0.02026 80  GLY   D C     
3405 O  O     . GLY   C 81  ? 0.32098 0.19962 0.20542 0.02501  -0.00271 -0.00262 80  GLY   D O     
3406 N  N     . GLU   C 82  ? 0.28473 0.17253 0.21124 0.00569  -0.00645 0.01231  81  GLU   D N     
3407 C  CA    . GLU   C 82  ? 0.25753 0.15791 0.20443 -0.01306 -0.00093 0.02232  81  GLU   D CA    
3408 C  C     . GLU   C 82  ? 0.29987 0.16911 0.18375 -0.04521 -0.00858 0.00290  81  GLU   D C     
3409 O  O     . GLU   C 82  ? 0.37486 0.23143 0.17125 -0.00597 -0.00939 -0.01606 81  GLU   D O     
3410 C  CB    . GLU   C 82  ? 0.31497 0.14148 0.23440 0.00960  -0.03343 0.00188  81  GLU   D CB    
3411 C  CG    . GLU   C 82  ? 0.29065 0.15972 0.23776 -0.03163 0.02103  -0.02323 81  GLU   D CG    
3412 C  CD    . GLU   C 82  ? 0.30520 0.17859 0.23748 -0.01184 -0.00425 -0.03890 81  GLU   D CD    
3413 O  OE1   . GLU   C 82  ? 0.30017 0.21960 0.29544 0.02083  -0.02892 -0.01382 81  GLU   D OE1   
3414 O  OE2   . GLU   C 82  ? 0.36386 0.18496 0.23234 -0.02609 0.01277  -0.03293 81  GLU   D OE2   
3415 N  N     . LYS   C 83  ? 0.27944 0.16333 0.17201 -0.02377 -0.00274 -0.01633 82  LYS   D N     
3416 C  CA    . LYS   C 83  ? 0.28506 0.19632 0.21515 -0.02532 -0.02617 0.00873  82  LYS   D CA    
3417 C  C     . LYS   C 83  ? 0.31064 0.19464 0.17718 -0.00615 -0.01261 -0.00501 82  LYS   D C     
3418 O  O     . LYS   C 83  ? 0.35049 0.19949 0.18093 -0.04935 -0.00888 -0.01528 82  LYS   D O     
3419 C  CB    . LYS   C 83  ? 0.37317 0.24338 0.33084 -0.02834 -0.05053 0.08292  82  LYS   D CB    
3420 C  CG    . LYS   C 83  ? 0.58681 0.32424 0.45675 -0.04088 -0.09185 0.08891  82  LYS   D CG    
3421 C  CD    . LYS   C 83  ? 0.72479 0.40603 0.50585 -0.01180 -0.14010 0.09352  82  LYS   D CD    
3422 C  CE    . LYS   C 83  ? 0.79566 0.45318 0.53543 0.01700  -0.19941 0.11237  82  LYS   D CE    
3423 N  NZ    . LYS   C 83  ? 0.78223 0.47409 0.51760 0.06724  -0.26063 0.12863  82  LYS   D NZ    
3424 N  N     . PHE   C 84  ? 0.30831 0.17850 0.13468 0.02184  0.02149  0.00360  83  PHE   D N     
3425 C  CA    . PHE   C 84  ? 0.24769 0.21007 0.15877 0.00612  -0.02549 0.00213  83  PHE   D CA    
3426 C  C     . PHE   C 84  ? 0.29704 0.20404 0.13551 0.00693  -0.02219 -0.02012 83  PHE   D C     
3427 O  O     . PHE   C 84  ? 0.25020 0.18228 0.15673 -0.01039 0.01008  -0.01562 83  PHE   D O     
3428 C  CB    . PHE   C 84  ? 0.29476 0.18141 0.16953 0.01522  -0.01942 -0.00998 83  PHE   D CB    
3429 C  CG    . PHE   C 84  ? 0.30470 0.18937 0.14382 0.00966  -0.04183 -0.00027 83  PHE   D CG    
3430 C  CD1   . PHE   C 84  ? 0.32372 0.19099 0.17390 -0.00337 -0.00661 -0.00274 83  PHE   D CD1   
3431 C  CD2   . PHE   C 84  ? 0.32317 0.18821 0.16669 -0.01796 -0.01896 -0.00969 83  PHE   D CD2   
3432 C  CE1   . PHE   C 84  ? 0.23553 0.16509 0.20707 0.00736  0.04867  -0.00075 83  PHE   D CE1   
3433 C  CE2   . PHE   C 84  ? 0.24855 0.19108 0.20299 -0.02854 -0.00477 0.00167  83  PHE   D CE2   
3434 C  CZ    . PHE   C 84  ? 0.23047 0.19373 0.21662 -0.01099 -0.00433 -0.01027 83  PHE   D CZ    
3435 N  N     . GLU   C 85  ? 0.31799 0.20814 0.15571 0.00105  0.01268  -0.01735 84  GLU   D N     
3436 C  CA    . GLU   C 85  ? 0.33918 0.22340 0.14870 -0.04017 0.01702  0.01564  84  GLU   D CA    
3437 C  C     . GLU   C 85  ? 0.30700 0.18684 0.14548 -0.00543 -0.00422 0.00030  84  GLU   D C     
3438 O  O     . GLU   C 85  ? 0.32326 0.18329 0.20060 -0.01887 0.00537  -0.01374 84  GLU   D O     
3439 C  CB    . GLU   C 85  ? 0.46960 0.28210 0.17978 0.00026  0.00855  0.02041  84  GLU   D CB    
3440 C  CG    . GLU   C 85  ? 0.68651 0.35592 0.29169 -0.00543 0.11482  0.07236  84  GLU   D CG    
3441 C  CD    . GLU   C 85  ? 0.83663 0.45058 0.39318 0.02483  0.16281  0.10114  84  GLU   D CD    
3442 O  OE1   . GLU   C 85  ? 0.87620 0.49051 0.40339 0.03871  0.15840  0.09955  84  GLU   D OE1   
3443 O  OE2   . GLU   C 85  ? 0.90874 0.45684 0.45505 0.01820  0.21434  0.12400  84  GLU   D OE2   
3444 N  N     . ASP   C 86  ? 0.28976 0.18168 0.17143 -0.02476 -0.00046 0.01896  85  ASP   D N     
3445 C  CA    . ASP   C 86  ? 0.20884 0.18897 0.19935 -0.01518 0.01514  0.02747  85  ASP   D CA    
3446 C  C     . ASP   C 86  ? 0.27681 0.23252 0.15710 0.00452  0.03501  0.03195  85  ASP   D C     
3447 O  O     . ASP   C 86  ? 0.33421 0.22097 0.17027 -0.00313 0.07020  0.01103  85  ASP   D O     
3448 C  CB    . ASP   C 86  ? 0.24918 0.19474 0.20819 0.00253  0.03670  0.03776  85  ASP   D CB    
3449 C  CG    . ASP   C 86  ? 0.19943 0.19752 0.18308 0.01867  0.03442  0.05289  85  ASP   D CG    
3450 O  OD1   . ASP   C 86  ? 0.25057 0.20237 0.17339 -0.00002 0.04835  0.03318  85  ASP   D OD1   
3451 O  OD2   . ASP   C 86  ? 0.25508 0.19144 0.18514 0.01284  0.03852  0.00730  85  ASP   D OD2   
3452 N  N     . GLU   C 87  ? 0.25625 0.21401 0.17612 0.01605  0.01621  0.03654  86  GLU   D N     
3453 C  CA    . GLU   C 87  ? 0.29060 0.21151 0.22331 -0.00886 0.00633  0.02544  86  GLU   D CA    
3454 C  C     . GLU   C 87  ? 0.28997 0.21018 0.18364 0.00933  0.02963  0.02681  86  GLU   D C     
3455 O  O     . GLU   C 87  ? 0.28442 0.22222 0.20372 0.01237  0.03640  0.02472  86  GLU   D O     
3456 C  CB    . GLU   C 87  ? 0.25941 0.21370 0.24953 -0.01120 0.01169  0.05154  86  GLU   D CB    
3457 C  CG    . GLU   C 87  ? 0.31127 0.21510 0.21121 0.00459  0.03369  0.06511  86  GLU   D CG    
3458 C  CD    . GLU   C 87  ? 0.25919 0.21618 0.20086 0.00716  0.04998  0.06738  86  GLU   D CD    
3459 O  OE1   . GLU   C 87  ? 0.30960 0.20270 0.20893 -0.00736 0.01719  0.01686  86  GLU   D OE1   
3460 O  OE2   . GLU   C 87  ? 0.32179 0.25014 0.21845 0.06225  0.01896  0.07256  86  GLU   D OE2   
3461 N  N     . ASN   C 88  ? 0.21237 0.20062 0.20632 -0.02009 -0.00007 0.05534  87  ASN   D N     
3462 C  CA    . ASN   C 88  ? 0.27051 0.18839 0.17107 -0.00680 0.02981  0.03066  87  ASN   D CA    
3463 C  C     . ASN   C 88  ? 0.25188 0.19649 0.20692 0.00124  0.01195  0.04784  87  ASN   D C     
3464 O  O     . ASN   C 88  ? 0.27259 0.19531 0.21497 -0.00394 0.02195  0.03218  87  ASN   D O     
3465 C  CB    . ASN   C 88  ? 0.29094 0.20999 0.17215 -0.00794 0.05903  0.04859  87  ASN   D CB    
3466 C  CG    . ASN   C 88  ? 0.26549 0.20937 0.21248 0.04161  0.04528  0.04043  87  ASN   D CG    
3467 O  OD1   . ASN   C 88  ? 0.26716 0.20424 0.22925 0.01938  0.06166  0.02654  87  ASN   D OD1   
3468 N  ND2   . ASN   C 88  ? 0.24846 0.22283 0.23287 0.03573  0.03125  0.04582  87  ASN   D ND2   
3469 N  N     . PHE   C 89  ? 0.28061 0.20568 0.20050 -0.00802 0.03231  0.03066  88  PHE   D N     
3470 C  CA    . PHE   C 89  ? 0.27592 0.20912 0.21006 0.01027  0.02273  0.00463  88  PHE   D CA    
3471 C  C     . PHE   C 89  ? 0.31683 0.20269 0.22411 -0.00256 0.05336  0.01941  88  PHE   D C     
3472 O  O     . PHE   C 89  ? 0.28988 0.23161 0.24484 -0.02123 0.02077  0.00979  88  PHE   D O     
3473 C  CB    . PHE   C 89  ? 0.23508 0.23625 0.24712 0.00101  0.02126  -0.00115 88  PHE   D CB    
3474 C  CG    . PHE   C 89  ? 0.21051 0.25743 0.21209 -0.01255 0.01569  0.01481  88  PHE   D CG    
3475 C  CD1   . PHE   C 89  ? 0.22597 0.24687 0.22996 0.02511  -0.01420 0.03565  88  PHE   D CD1   
3476 C  CD2   . PHE   C 89  ? 0.32701 0.27166 0.22256 0.00986  0.04243  0.02514  88  PHE   D CD2   
3477 C  CE1   . PHE   C 89  ? 0.21751 0.22407 0.22590 0.03801  0.03847  0.03704  88  PHE   D CE1   
3478 C  CE2   . PHE   C 89  ? 0.29970 0.25840 0.25306 0.04690  0.03632  -0.00152 88  PHE   D CE2   
3479 C  CZ    . PHE   C 89  ? 0.28723 0.25013 0.23867 0.04777  0.03160  0.00556  88  PHE   D CZ    
3480 N  N     . ILE   C 90  ? 0.30535 0.18312 0.22379 -0.00017 0.08852  0.02257  89  ILE   D N     
3481 C  CA    . ILE   C 90  ? 0.32723 0.17536 0.22517 -0.02859 0.07753  0.02279  89  ILE   D CA    
3482 C  C     . ILE   C 90  ? 0.33716 0.18250 0.24775 -0.06175 0.06028  0.02710  89  ILE   D C     
3483 O  O     . ILE   C 90  ? 0.38516 0.19920 0.31950 -0.07231 0.02608  0.00320  89  ILE   D O     
3484 C  CB    . ILE   C 90  ? 0.31697 0.17820 0.23243 0.01461  0.01347  0.02742  89  ILE   D CB    
3485 C  CG1   . ILE   C 90  ? 0.35827 0.20241 0.24354 0.03145  0.01121  0.07913  89  ILE   D CG1   
3486 C  CG2   . ILE   C 90  ? 0.37716 0.16498 0.27435 0.00341  -0.02400 0.00813  89  ILE   D CG2   
3487 C  CD1   . ILE   C 90  ? 0.38740 0.21816 0.30382 0.04587  -0.02378 0.08092  89  ILE   D CD1   
3488 N  N     . LEU   C 91  ? 0.30943 0.16935 0.25218 -0.02059 0.02123  0.02485  90  LEU   D N     
3489 C  CA    . LEU   C 91  ? 0.25108 0.17658 0.24970 0.00885  0.01208  0.04286  90  LEU   D CA    
3490 C  C     . LEU   C 91  ? 0.28387 0.18151 0.24791 0.00115  0.00174  0.03843  90  LEU   D C     
3491 O  O     . LEU   C 91  ? 0.27536 0.19445 0.22932 -0.00912 0.02971  0.02625  90  LEU   D O     
3492 C  CB    . LEU   C 91  ? 0.18673 0.20567 0.29531 0.02273  0.02429  0.04173  90  LEU   D CB    
3493 C  CG    . LEU   C 91  ? 0.23113 0.18804 0.31739 0.02085  0.01170  0.03314  90  LEU   D CG    
3494 C  CD1   . LEU   C 91  ? 0.26889 0.22073 0.29194 0.00104  -0.00981 0.02818  90  LEU   D CD1   
3495 C  CD2   . LEU   C 91  ? 0.28046 0.19404 0.32939 0.05967  0.05652  0.03590  90  LEU   D CD2   
3496 N  N     . LYS   C 92  ? 0.31600 0.18521 0.22312 -0.02171 0.01936  0.02639  91  LYS   D N     
3497 C  CA    . LYS   C 92  ? 0.30945 0.19441 0.24060 -0.03430 0.03521  0.01203  91  LYS   D CA    
3498 C  C     . LYS   C 92  ? 0.21580 0.17290 0.25277 -0.03201 0.02893  -0.00149 91  LYS   D C     
3499 O  O     . LYS   C 92  ? 0.23044 0.19881 0.24862 0.00473  0.03596  0.01384  91  LYS   D O     
3500 C  CB    . LYS   C 92  ? 0.33267 0.23287 0.25394 -0.04855 0.04808  0.00964  91  LYS   D CB    
3501 C  CG    . LYS   C 92  ? 0.46151 0.28378 0.27630 -0.04447 0.04729  0.00620  91  LYS   D CG    
3502 C  CD    . LYS   C 92  ? 0.54019 0.35365 0.28175 -0.00755 0.10975  0.03560  91  LYS   D CD    
3503 C  CE    . LYS   C 92  ? 0.57982 0.40389 0.27298 0.02401  0.13424  0.05504  91  LYS   D CE    
3504 N  NZ    . LYS   C 92  ? 0.59327 0.44687 0.31918 0.03226  0.17861  0.06382  91  LYS   D NZ    
3505 N  N     . HIS   C 93  ? 0.22937 0.17481 0.24348 -0.03457 0.00647  0.01086  92  HIS   D N     
3506 C  CA    . HIS   C 93  ? 0.26366 0.17170 0.19989 -0.01710 0.03434  -0.01060 92  HIS   D CA    
3507 C  C     . HIS   C 93  ? 0.30277 0.19982 0.23928 -0.01027 -0.03106 -0.02708 92  HIS   D C     
3508 O  O     . HIS   C 93  ? 0.42749 0.22070 0.30285 0.01317  -0.13209 -0.05328 92  HIS   D O     
3509 C  CB    . HIS   C 93  ? 0.23795 0.17577 0.21775 -0.00907 0.00089  -0.02318 92  HIS   D CB    
3510 C  CG    . HIS   C 93  ? 0.21355 0.17343 0.19278 -0.00940 -0.01328 -0.00634 92  HIS   D CG    
3511 N  ND1   . HIS   C 93  ? 0.23509 0.14734 0.20261 0.00773  0.01087  0.00258  92  HIS   D ND1   
3512 C  CD2   . HIS   C 93  ? 0.21987 0.14645 0.23107 0.01192  -0.04260 -0.01093 92  HIS   D CD2   
3513 C  CE1   . HIS   C 93  ? 0.22734 0.15061 0.20750 -0.02388 0.00436  -0.00060 92  HIS   D CE1   
3514 N  NE2   . HIS   C 93  ? 0.16755 0.18302 0.21368 -0.00788 0.02671  0.00523  92  HIS   D NE2   
3515 N  N     . THR   C 94  ? 0.24720 0.18419 0.26870 -0.05039 -0.00012 -0.00581 93  THR   D N     
3516 C  CA    . THR   C 94  ? 0.29114 0.20331 0.28882 -0.05352 -0.00409 -0.00747 93  THR   D CA    
3517 C  C     . THR   C 94  ? 0.29251 0.22919 0.28163 -0.06895 -0.00157 -0.01756 93  THR   D C     
3518 O  O     . THR   C 94  ? 0.33381 0.26992 0.32105 -0.07515 -0.00995 -0.01046 93  THR   D O     
3519 C  CB    . THR   C 94  ? 0.28607 0.21641 0.26961 -0.05446 -0.02922 -0.01716 93  THR   D CB    
3520 O  OG1   . THR   C 94  ? 0.31903 0.24792 0.28846 -0.00675 -0.03022 -0.02469 93  THR   D OG1   
3521 C  CG2   . THR   C 94  ? 0.35434 0.20637 0.31697 -0.05415 -0.03035 -0.02413 93  THR   D CG2   
3522 N  N     . GLY   C 95  ? 0.27467 0.22122 0.24982 -0.03008 0.03515  -0.05613 94  GLY   D N     
3523 C  CA    . GLY   C 95  ? 0.23592 0.24386 0.27665 -0.05300 -0.00778 -0.02818 94  GLY   D CA    
3524 C  C     . GLY   C 95  ? 0.21373 0.21456 0.24870 -0.03596 -0.00916 -0.03095 94  GLY   D C     
3525 O  O     . GLY   C 95  ? 0.23962 0.19379 0.21275 -0.01872 -0.01562 -0.02905 94  GLY   D O     
3526 N  N     . PRO   C 96  ? 0.24838 0.21056 0.26057 -0.04861 0.02866  -0.06483 95  PRO   D N     
3527 C  CA    . PRO   C 96  ? 0.27739 0.20893 0.23511 -0.01556 0.00837  -0.03951 95  PRO   D CA    
3528 C  C     . PRO   C 96  ? 0.24950 0.20319 0.24942 -0.00044 -0.02361 -0.04395 95  PRO   D C     
3529 O  O     . PRO   C 96  ? 0.28709 0.22034 0.30427 -0.00693 -0.00967 -0.01151 95  PRO   D O     
3530 C  CB    . PRO   C 96  ? 0.32366 0.24609 0.24480 -0.06768 0.02583  -0.04874 95  PRO   D CB    
3531 C  CG    . PRO   C 96  ? 0.30542 0.28964 0.26699 -0.07937 0.04008  -0.08172 95  PRO   D CG    
3532 C  CD    . PRO   C 96  ? 0.27787 0.24423 0.27374 -0.06651 0.02517  -0.08442 95  PRO   D CD    
3533 N  N     . GLY   C 97  ? 0.21975 0.20482 0.20177 0.00169  0.00035  -0.04543 96  GLY   D N     
3534 C  CA    . GLY   C 97  ? 0.21618 0.19881 0.20602 -0.00170 0.00897  -0.03971 96  GLY   D CA    
3535 C  C     . GLY   C 97  ? 0.21689 0.15463 0.21467 -0.00047 0.00928  -0.00960 96  GLY   D C     
3536 O  O     . GLY   C 97  ? 0.20089 0.19759 0.22862 0.00079  0.00959  -0.04348 96  GLY   D O     
3537 N  N     . ILE   C 98  ? 0.20378 0.16498 0.22109 -0.00376 0.01851  -0.01975 97  ILE   D N     
3538 C  CA    . ILE   C 98  ? 0.18634 0.17219 0.23964 0.00141  0.02261  -0.04773 97  ILE   D CA    
3539 C  C     . ILE   C 98  ? 0.16897 0.17828 0.23693 0.00789  0.01460  -0.01025 97  ILE   D C     
3540 O  O     . ILE   C 98  ? 0.21775 0.18297 0.20358 0.02131  0.01281  -0.00340 97  ILE   D O     
3541 C  CB    . ILE   C 98  ? 0.19765 0.17860 0.25094 -0.02723 0.00816  -0.03129 97  ILE   D CB    
3542 C  CG1   . ILE   C 98  ? 0.19981 0.18891 0.31490 -0.02766 -0.01508 0.02605  97  ILE   D CG1   
3543 C  CG2   . ILE   C 98  ? 0.23806 0.19499 0.22869 0.00266  0.04616  -0.04503 97  ILE   D CG2   
3544 C  CD1   . ILE   C 98  ? 0.31581 0.20627 0.32724 -0.01867 0.01264  0.00632  97  ILE   D CD1   
3545 N  N     . LEU   C 99  ? 0.16743 0.14418 0.18346 -0.01612 -0.00186 -0.00925 98  LEU   D N     
3546 C  CA    . LEU   C 99  ? 0.18764 0.17169 0.17829 0.02413  -0.00303 -0.01618 98  LEU   D CA    
3547 C  C     . LEU   C 99  ? 0.16185 0.17276 0.14735 -0.00624 -0.00047 0.02788  98  LEU   D C     
3548 O  O     . LEU   C 99  ? 0.21324 0.16011 0.15432 0.03616  -0.00479 0.00554  98  LEU   D O     
3549 C  CB    . LEU   C 99  ? 0.14610 0.19210 0.21191 0.00346  -0.00843 -0.01157 98  LEU   D CB    
3550 C  CG    . LEU   C 99  ? 0.15797 0.18924 0.18496 0.01643  0.01715  0.00602  98  LEU   D CG    
3551 C  CD1   . LEU   C 99  ? 0.20307 0.20471 0.22533 -0.01524 -0.00196 0.01836  98  LEU   D CD1   
3552 C  CD2   . LEU   C 99  ? 0.14316 0.20556 0.23023 0.01141  -0.02476 0.00426  98  LEU   D CD2   
3553 N  N     . SER   C 100 ? 0.14967 0.15841 0.17173 0.01181  0.01930  -0.00179 99  SER   D N     
3554 C  CA    . SER   C 100 ? 0.16143 0.15580 0.17124 0.02324  0.03294  -0.02115 99  SER   D CA    
3555 C  C     . SER   C 100 ? 0.20734 0.16508 0.14992 -0.00345 0.02083  -0.01877 99  SER   D C     
3556 O  O     . SER   C 100 ? 0.15850 0.18702 0.13887 -0.00667 0.00893  0.00337  99  SER   D O     
3557 C  CB    . SER   C 100 ? 0.15669 0.17392 0.21265 -0.00676 0.02855  -0.01078 99  SER   D CB    
3558 O  OG    . SER   C 100 ? 0.18978 0.18811 0.15905 0.02101  0.02614  0.01232  99  SER   D OG    
3559 N  N     . MET   C 101 ? 0.15807 0.14785 0.15253 0.00275  0.00990  -0.00268 100 MET   D N     
3560 C  CA    . MET   C 101 ? 0.17720 0.14926 0.15336 0.00561  0.02130  -0.02919 100 MET   D CA    
3561 C  C     . MET   C 101 ? 0.18532 0.14945 0.16504 0.02034  0.03388  0.00895  100 MET   D C     
3562 O  O     . MET   C 101 ? 0.18995 0.17461 0.17017 0.00927  0.02865  0.03022  100 MET   D O     
3563 C  CB    . MET   C 101 ? 0.21404 0.17362 0.13130 0.01625  0.01359  -0.01958 100 MET   D CB    
3564 C  CG    . MET   C 101 ? 0.21849 0.15965 0.20216 -0.00167 0.00229  0.02345  100 MET   D CG    
3565 S  SD    . MET   C 101 ? 0.20587 0.16343 0.19416 0.01098  -0.02508 0.00662  100 MET   D SD    
3566 C  CE    . MET   C 101 ? 0.23659 0.16452 0.22120 0.02660  0.00304  -0.00626 100 MET   D CE    
3567 N  N     . ALA   C 102 ? 0.18264 0.14688 0.12935 0.00374  0.01012  0.01407  101 ALA   D N     
3568 C  CA    . ALA   C 102 ? 0.13356 0.13575 0.15126 0.02070  -0.00559 0.01075  101 ALA   D CA    
3569 C  C     . ALA   C 102 ? 0.14234 0.14996 0.16837 0.02189  -0.00068 -0.00187 101 ALA   D C     
3570 O  O     . ALA   C 102 ? 0.16657 0.17916 0.18244 0.01410  -0.02243 0.00588  101 ALA   D O     
3571 C  CB    . ALA   C 102 ? 0.17297 0.15536 0.14247 -0.00557 -0.01520 0.02726  101 ALA   D CB    
3572 N  N     . ASN   C 103 ? 0.16876 0.16362 0.15851 0.00905  0.01852  0.00068  102 ASN   D N     
3573 C  CA    . ASN   C 103 ? 0.19836 0.17863 0.13463 0.04909  0.03975  0.02621  102 ASN   D CA    
3574 C  C     . ASN   C 103 ? 0.19589 0.17805 0.13643 0.03438  0.03049  0.03002  102 ASN   D C     
3575 O  O     . ASN   C 103 ? 0.18304 0.20245 0.16651 0.02730  0.03253  0.03587  102 ASN   D O     
3576 C  CB    . ASN   C 103 ? 0.16627 0.18317 0.16476 0.03736  0.04065  0.04021  102 ASN   D CB    
3577 C  CG    . ASN   C 103 ? 0.19561 0.17223 0.19750 0.04111  0.03231  0.02678  102 ASN   D CG    
3578 O  OD1   . ASN   C 103 ? 0.17203 0.18733 0.19418 0.02670  0.02713  0.02217  102 ASN   D OD1   
3579 N  ND2   . ASN   C 103 ? 0.25819 0.17355 0.14315 0.02181  0.02999  0.00339  102 ASN   D ND2   
3580 N  N     . ALA   C 104 ? 0.19980 0.17038 0.17656 0.04354  0.02654  0.01857  103 ALA   D N     
3581 C  CA    . ALA   C 104 ? 0.20451 0.15999 0.20285 0.02620  0.04706  0.01009  103 ALA   D CA    
3582 C  C     . ALA   C 104 ? 0.22539 0.20456 0.23670 0.03341  0.03653  0.01251  103 ALA   D C     
3583 O  O     . ALA   C 104 ? 0.27013 0.22187 0.31949 0.06639  0.09130  -0.00229 103 ALA   D O     
3584 C  CB    . ALA   C 104 ? 0.20543 0.15964 0.24004 0.00869  -0.00438 -0.00577 103 ALA   D CB    
3585 N  N     . GLY   C 105 ? 0.21208 0.21764 0.17639 0.00336  0.04297  0.01497  104 GLY   D N     
3586 C  CA    . GLY   C 105 ? 0.20271 0.22779 0.19722 0.02207  0.07101  0.02465  104 GLY   D CA    
3587 C  C     . GLY   C 105 ? 0.20831 0.20738 0.17764 -0.00149 0.05200  0.00757  104 GLY   D C     
3588 O  O     . GLY   C 105 ? 0.19051 0.21631 0.19965 0.01851  0.02840  0.01806  104 GLY   D O     
3589 N  N     . PRO   C 106 ? 0.23007 0.24367 0.20396 0.00732  0.07112  0.01489  105 PRO   D N     
3590 C  CA    . PRO   C 106 ? 0.22773 0.24318 0.20198 -0.00256 0.06976  0.01920  105 PRO   D CA    
3591 C  C     . PRO   C 106 ? 0.25619 0.18132 0.15152 0.02226  0.05620  0.01294  105 PRO   D C     
3592 O  O     . PRO   C 106 ? 0.27086 0.18918 0.21745 0.03995  0.06569  -0.00214 105 PRO   D O     
3593 C  CB    . PRO   C 106 ? 0.22151 0.30402 0.22425 0.00282  0.07298  0.02971  105 PRO   D CB    
3594 C  CG    . PRO   C 106 ? 0.24632 0.32007 0.20898 0.02707  0.05693  0.05458  105 PRO   D CG    
3595 C  CD    . PRO   C 106 ? 0.23739 0.29084 0.20484 0.02718  0.05513  0.02938  105 PRO   D CD    
3596 N  N     . ASN   C 107 ? 0.25560 0.18275 0.16299 0.02993  0.05705  0.01918  106 ASN   D N     
3597 C  CA    . ASN   C 107 ? 0.27000 0.19506 0.16595 0.01219  0.04937  0.00401  106 ASN   D CA    
3598 C  C     . ASN   C 107 ? 0.26411 0.20119 0.18234 -0.00433 0.03302  0.01821  106 ASN   D C     
3599 O  O     . ASN   C 107 ? 0.27071 0.22988 0.17864 0.01465  0.02056  -0.01441 106 ASN   D O     
3600 C  CB    . ASN   C 107 ? 0.33025 0.21019 0.13329 -0.00311 0.06839  -0.02307 106 ASN   D CB    
3601 C  CG    . ASN   C 107 ? 0.30376 0.20489 0.18936 0.01082  0.10199  -0.00684 106 ASN   D CG    
3602 O  OD1   . ASN   C 107 ? 0.30848 0.22396 0.18242 0.00708  0.07286  0.01049  106 ASN   D OD1   
3603 N  ND2   . ASN   C 107 ? 0.37221 0.23365 0.25671 0.00939  0.14422  -0.01240 106 ASN   D ND2   
3604 N  N     . THR   C 108 ? 0.22938 0.20494 0.17480 0.01069  0.03192  0.03322  107 THR   D N     
3605 C  CA    . THR   C 108 ? 0.20416 0.18881 0.18292 0.03195  0.02133  0.00950  107 THR   D CA    
3606 C  C     . THR   C 108 ? 0.21780 0.17310 0.17180 0.01230  0.02702  0.03186  107 THR   D C     
3607 O  O     . THR   C 108 ? 0.27325 0.20423 0.20656 0.05172  0.05421  0.07160  107 THR   D O     
3608 C  CB    . THR   C 108 ? 0.22618 0.19536 0.15803 0.03959  -0.01551 0.01527  107 THR   D CB    
3609 O  OG1   . THR   C 108 ? 0.21566 0.22379 0.15682 0.02068  -0.00038 0.00799  107 THR   D OG1   
3610 C  CG2   . THR   C 108 ? 0.23713 0.18453 0.17557 0.04094  0.05515  -0.00148 107 THR   D CG2   
3611 N  N     . ASN   C 109 ? 0.21385 0.15908 0.17108 0.01716  0.02532  -0.00622 108 ASN   D N     
3612 C  CA    . ASN   C 109 ? 0.19615 0.17840 0.15835 0.03561  -0.00571 -0.00297 108 ASN   D CA    
3613 C  C     . ASN   C 109 ? 0.19222 0.18031 0.15418 0.01432  0.00420  0.00393  108 ASN   D C     
3614 O  O     . ASN   C 109 ? 0.26769 0.22945 0.13124 -0.03722 -0.01117 -0.01072 108 ASN   D O     
3615 C  CB    . ASN   C 109 ? 0.21430 0.16800 0.21550 0.03601  0.01354  0.01616  108 ASN   D CB    
3616 C  CG    . ASN   C 109 ? 0.22304 0.16489 0.21386 -0.00649 0.02716  0.01494  108 ASN   D CG    
3617 O  OD1   . ASN   C 109 ? 0.25726 0.19961 0.18101 -0.02785 0.02194  -0.00643 108 ASN   D OD1   
3618 N  ND2   . ASN   C 109 ? 0.29346 0.16209 0.20906 0.00111  0.04535  0.03486  108 ASN   D ND2   
3619 N  N     . GLY   C 110 ? 0.19867 0.17545 0.15348 -0.00110 0.01634  0.00977  109 GLY   D N     
3620 C  CA    . GLY   C 110 ? 0.20728 0.17203 0.18045 0.00813  0.02053  -0.02481 109 GLY   D CA    
3621 C  C     . GLY   C 110 ? 0.18380 0.15645 0.16263 -0.00175 -0.00786 -0.00160 109 GLY   D C     
3622 O  O     . GLY   C 110 ? 0.22493 0.18663 0.19084 0.02025  0.00313  0.02496  109 GLY   D O     
3623 N  N     . SER   C 111 ? 0.17513 0.17799 0.14395 0.02214  -0.00387 -0.01714 110 SER   D N     
3624 C  CA    . SER   C 111 ? 0.19027 0.15908 0.16521 0.01352  0.00942  -0.00877 110 SER   D CA    
3625 C  C     . SER   C 111 ? 0.16545 0.14502 0.16497 0.00164  -0.01596 -0.01067 110 SER   D C     
3626 O  O     . SER   C 111 ? 0.17129 0.16354 0.16244 0.01591  -0.01453 -0.01658 110 SER   D O     
3627 C  CB    . SER   C 111 ? 0.14300 0.14902 0.21912 0.00574  0.00608  0.03404  110 SER   D CB    
3628 O  OG    . SER   C 111 ? 0.18051 0.16135 0.19944 -0.02093 -0.01126 0.00094  110 SER   D OG    
3629 N  N     . GLN   C 112 ? 0.17060 0.16540 0.14019 0.00745  -0.00104 -0.00283 111 GLN   D N     
3630 C  CA    . GLN   C 112 ? 0.18212 0.14327 0.14371 0.01122  -0.01893 0.00459  111 GLN   D CA    
3631 C  C     . GLN   C 112 ? 0.15731 0.13391 0.16343 0.00650  -0.01892 0.02923  111 GLN   D C     
3632 O  O     . GLN   C 112 ? 0.16904 0.16454 0.15776 -0.00455 -0.00731 0.01478  111 GLN   D O     
3633 C  CB    . GLN   C 112 ? 0.16021 0.14630 0.18415 0.01809  -0.02701 0.02991  111 GLN   D CB    
3634 C  CG    . GLN   C 112 ? 0.21683 0.13460 0.19754 0.01334  -0.03575 0.02323  111 GLN   D CG    
3635 C  CD    . GLN   C 112 ? 0.13684 0.15047 0.17094 -0.01714 0.01301  0.00659  111 GLN   D CD    
3636 O  OE1   . GLN   C 112 ? 0.15565 0.17313 0.18658 -0.01064 0.00159  0.01158  111 GLN   D OE1   
3637 N  NE2   . GLN   C 112 ? 0.16427 0.14194 0.21291 0.01949  0.01271  -0.00673 111 GLN   D NE2   
3638 N  N     . PHE   C 113 ? 0.14008 0.14621 0.16046 0.00805  -0.02130 0.00380  112 PHE   D N     
3639 C  CA    . PHE   C 113 ? 0.19571 0.13955 0.14571 0.02651  -0.03750 0.01301  112 PHE   D CA    
3640 C  C     . PHE   C 113 ? 0.18597 0.13288 0.14534 0.01127  -0.00043 0.01965  112 PHE   D C     
3641 O  O     . PHE   C 113 ? 0.14432 0.14633 0.16606 0.00088  -0.01397 -0.01598 112 PHE   D O     
3642 C  CB    . PHE   C 113 ? 0.20317 0.15206 0.16244 0.03482  -0.01035 0.02480  112 PHE   D CB    
3643 C  CG    . PHE   C 113 ? 0.17528 0.14832 0.14302 0.02745  0.01193  0.00610  112 PHE   D CG    
3644 C  CD1   . PHE   C 113 ? 0.16880 0.16060 0.20816 0.01836  0.01136  0.00468  112 PHE   D CD1   
3645 C  CD2   . PHE   C 113 ? 0.14295 0.14471 0.18550 0.04467  -0.01410 -0.00127 112 PHE   D CD2   
3646 C  CE1   . PHE   C 113 ? 0.13175 0.16289 0.23117 0.00772  0.01608  -0.00528 112 PHE   D CE1   
3647 C  CE2   . PHE   C 113 ? 0.11658 0.17960 0.21825 0.02164  0.01311  -0.02698 112 PHE   D CE2   
3648 C  CZ    . PHE   C 113 ? 0.15930 0.18284 0.20129 0.00699  0.02196  -0.03280 112 PHE   D CZ    
3649 N  N     . PHE   C 114 ? 0.14984 0.13486 0.16217 0.01276  0.00255  -0.02404 113 PHE   D N     
3650 C  CA    . PHE   C 114 ? 0.15643 0.12303 0.17016 0.00456  -0.00294 0.01555  113 PHE   D CA    
3651 C  C     . PHE   C 114 ? 0.15228 0.16034 0.13976 0.00918  -0.00966 0.02122  113 PHE   D C     
3652 O  O     . PHE   C 114 ? 0.18502 0.19135 0.15844 -0.02243 0.01158  -0.00683 113 PHE   D O     
3653 C  CB    . PHE   C 114 ? 0.13230 0.16293 0.18825 -0.00695 0.02157  0.01557  113 PHE   D CB    
3654 C  CG    . PHE   C 114 ? 0.14810 0.15307 0.16309 0.01078  0.00773  0.00055  113 PHE   D CG    
3655 C  CD1   . PHE   C 114 ? 0.14211 0.19755 0.15587 0.04039  0.01380  0.00275  113 PHE   D CD1   
3656 C  CD2   . PHE   C 114 ? 0.14251 0.17572 0.22439 -0.02765 -0.01471 0.03254  113 PHE   D CD2   
3657 C  CE1   . PHE   C 114 ? 0.14897 0.18328 0.21075 0.00873  0.02429  0.00993  113 PHE   D CE1   
3658 C  CE2   . PHE   C 114 ? 0.18597 0.17729 0.21588 -0.00758 -0.00504 0.00369  113 PHE   D CE2   
3659 C  CZ    . PHE   C 114 ? 0.14267 0.17965 0.20948 0.00753  0.01834  0.02148  113 PHE   D CZ    
3660 N  N     . ILE   C 115 ? 0.17561 0.14294 0.15362 -0.00175 -0.00563 0.00769  114 ILE   D N     
3661 C  CA    . ILE   C 115 ? 0.17034 0.13808 0.17736 -0.00530 -0.00068 -0.02499 114 ILE   D CA    
3662 C  C     . ILE   C 115 ? 0.18785 0.14810 0.19750 -0.01231 -0.03631 -0.00669 114 ILE   D C     
3663 O  O     . ILE   C 115 ? 0.16107 0.16508 0.19089 -0.01608 -0.01597 -0.00047 114 ILE   D O     
3664 C  CB    . ILE   C 115 ? 0.17534 0.16077 0.19209 -0.01359 -0.00037 -0.05113 114 ILE   D CB    
3665 C  CG1   . ILE   C 115 ? 0.20958 0.18876 0.22640 -0.00856 0.00394  -0.01748 114 ILE   D CG1   
3666 C  CG2   . ILE   C 115 ? 0.20672 0.16603 0.26293 0.01342  -0.00581 -0.04414 114 ILE   D CG2   
3667 C  CD1   . ILE   C 115 ? 0.19853 0.21404 0.20156 0.00773  0.03796  -0.04350 114 ILE   D CD1   
3668 N  N     . CYS   C 116 ? 0.17678 0.14171 0.22395 -0.01306 -0.01681 -0.02170 115 CYS   D N     
3669 C  CA    . CYS   C 116 ? 0.17308 0.18923 0.18406 -0.02473 0.00870  -0.03213 115 CYS   D CA    
3670 C  C     . CYS   C 116 ? 0.19428 0.20981 0.20651 0.01668  -0.02210 -0.02558 115 CYS   D C     
3671 O  O     . CYS   C 116 ? 0.20394 0.18308 0.25460 0.00881  -0.00820 -0.03084 115 CYS   D O     
3672 C  CB    . CYS   C 116 ? 0.18533 0.22419 0.19759 -0.01553 0.00250  -0.06084 115 CYS   D CB    
3673 S  SG    . CYS   C 116 ? 0.20369 0.25493 0.24978 -0.00575 -0.00520 -0.04126 115 CYS   D SG    
3674 N  N     . THR   C 117 ? 0.21188 0.23074 0.19046 -0.03580 -0.01589 -0.01437 116 THR   D N     
3675 C  CA    . THR   C 117 ? 0.24653 0.24523 0.18143 -0.04133 -0.01063 -0.03510 116 THR   D CA    
3676 C  C     . THR   C 117 ? 0.23688 0.25636 0.18467 -0.05188 -0.02734 -0.04787 116 THR   D C     
3677 O  O     . THR   C 117 ? 0.27999 0.25645 0.22117 -0.06180 -0.03463 -0.01669 116 THR   D O     
3678 C  CB    . THR   C 117 ? 0.24526 0.25269 0.23940 -0.02210 -0.01106 -0.02462 116 THR   D CB    
3679 O  OG1   . THR   C 117 ? 0.26096 0.23890 0.26379 -0.00165 -0.03687 0.00740  116 THR   D OG1   
3680 C  CG2   . THR   C 117 ? 0.21725 0.28430 0.23128 -0.00688 -0.00191 -0.02533 116 THR   D CG2   
3681 N  N     . ALA   C 118 ? 0.20560 0.26098 0.22532 -0.03310 -0.01297 0.01804  117 ALA   D N     
3682 C  CA    . ALA   C 118 ? 0.22533 0.27089 0.26925 -0.03977 -0.04476 0.02102  117 ALA   D CA    
3683 C  C     . ALA   C 118 ? 0.20792 0.27953 0.29178 -0.04176 -0.03181 0.01050  117 ALA   D C     
3684 O  O     . ALA   C 118 ? 0.19567 0.26739 0.28332 -0.03436 -0.02064 -0.04335 117 ALA   D O     
3685 C  CB    . ALA   C 118 ? 0.28191 0.29705 0.31844 -0.02244 -0.04935 0.03156  117 ALA   D CB    
3686 N  N     . LYS   C 119 ? 0.22405 0.27305 0.31872 -0.06704 -0.03283 0.02967  118 LYS   D N     
3687 C  CA    . LYS   C 119 ? 0.25862 0.26406 0.30325 -0.07925 0.01457  0.01676  118 LYS   D CA    
3688 C  C     . LYS   C 119 ? 0.30689 0.26404 0.27617 -0.03318 -0.04318 0.02755  118 LYS   D C     
3689 O  O     . LYS   C 119 ? 0.32378 0.27018 0.29252 -0.01865 -0.06515 0.00941  118 LYS   D O     
3690 C  CB    . LYS   C 119 ? 0.30570 0.27401 0.37888 -0.09306 0.06920  0.00589  118 LYS   D CB    
3691 C  CG    . LYS   C 119 ? 0.39508 0.29446 0.44222 -0.12487 0.06779  0.00353  118 LYS   D CG    
3692 C  CD    . LYS   C 119 ? 0.50779 0.32837 0.54152 -0.12748 0.02096  -0.02561 118 LYS   D CD    
3693 C  CE    . LYS   C 119 ? 0.59067 0.34547 0.62198 -0.17148 0.05945  -0.04710 118 LYS   D CE    
3694 N  NZ    . LYS   C 119 ? 0.62090 0.35594 0.66111 -0.19599 0.08543  -0.05484 118 LYS   D NZ    
3695 N  N     . THR   C 120 ? 0.18992 0.24197 0.27688 -0.03761 -0.00841 0.02296  119 THR   D N     
3696 C  CA    . THR   C 120 ? 0.23630 0.26066 0.23035 -0.02922 0.01279  0.01211  119 THR   D CA    
3697 C  C     . THR   C 120 ? 0.22955 0.25806 0.24091 -0.00732 0.02652  0.03071  119 THR   D C     
3698 O  O     . THR   C 120 ? 0.21491 0.25406 0.24975 -0.00316 -0.00709 0.03304  119 THR   D O     
3699 C  CB    . THR   C 120 ? 0.17583 0.26694 0.21293 -0.03481 0.01249  -0.00244 119 THR   D CB    
3700 O  OG1   . THR   C 120 ? 0.18743 0.27275 0.23483 -0.01466 -0.03768 -0.00935 119 THR   D OG1   
3701 C  CG2   . THR   C 120 ? 0.21604 0.25178 0.20430 -0.01793 0.00762  0.01004  119 THR   D CG2   
3702 N  N     . GLU   C 121 ? 0.21521 0.29739 0.28785 -0.05677 -0.00356 0.01787  120 GLU   D N     
3703 C  CA    . GLU   C 121 ? 0.25602 0.32607 0.28117 -0.08245 -0.00748 0.02339  120 GLU   D CA    
3704 C  C     . GLU   C 121 ? 0.19271 0.30918 0.23169 -0.06293 0.00608  0.06310  120 GLU   D C     
3705 O  O     . GLU   C 121 ? 0.24700 0.32173 0.24288 -0.06447 -0.00568 0.04977  120 GLU   D O     
3706 C  CB    . GLU   C 121 ? 0.28656 0.39706 0.37579 -0.10874 0.03958  0.02695  120 GLU   D CB    
3707 C  CG    . GLU   C 121 ? 0.31373 0.47568 0.46257 -0.10802 -0.01134 0.04649  120 GLU   D CG    
3708 C  CD    . GLU   C 121 ? 0.33501 0.53177 0.51633 -0.12030 -0.12884 0.04984  120 GLU   D CD    
3709 O  OE1   . GLU   C 121 ? 0.32123 0.52847 0.53815 -0.10340 -0.16770 0.02071  120 GLU   D OE1   
3710 O  OE2   . GLU   C 121 ? 0.41440 0.54847 0.53460 -0.12610 -0.11006 0.08754  120 GLU   D OE2   
3711 N  N     . TRP   C 122 ? 0.16200 0.27444 0.30433 -0.02117 0.02231  0.03470  121 TRP   D N     
3712 C  CA    . TRP   C 122 ? 0.22012 0.28164 0.30072 -0.02338 0.04194  0.03755  121 TRP   D CA    
3713 C  C     . TRP   C 122 ? 0.14648 0.27594 0.31076 -0.00508 0.03475  0.04055  121 TRP   D C     
3714 O  O     . TRP   C 122 ? 0.21452 0.30983 0.33928 -0.00057 0.05563  0.03727  121 TRP   D O     
3715 C  CB    . TRP   C 122 ? 0.19527 0.30497 0.32316 -0.01972 0.01382  0.05470  121 TRP   D CB    
3716 C  CG    . TRP   C 122 ? 0.19975 0.30717 0.30140 0.01077  -0.00987 0.04238  121 TRP   D CG    
3717 C  CD1   . TRP   C 122 ? 0.21495 0.30570 0.30847 0.04969  -0.04314 0.03532  121 TRP   D CD1   
3718 C  CD2   . TRP   C 122 ? 0.20243 0.28019 0.30268 -0.02089 -0.00807 0.02526  121 TRP   D CD2   
3719 N  NE1   . TRP   C 122 ? 0.25834 0.29175 0.24234 0.00239  -0.01640 0.02730  121 TRP   D NE1   
3720 C  CE2   . TRP   C 122 ? 0.25271 0.29606 0.28082 0.00174  -0.03173 0.02534  121 TRP   D CE2   
3721 C  CE3   . TRP   C 122 ? 0.25513 0.29199 0.30914 -0.04541 0.00071  0.02049  121 TRP   D CE3   
3722 C  CZ2   . TRP   C 122 ? 0.25877 0.28969 0.29154 0.00946  -0.01298 0.04513  121 TRP   D CZ2   
3723 C  CZ3   . TRP   C 122 ? 0.30616 0.27847 0.28109 -0.04287 -0.00336 0.04049  121 TRP   D CZ3   
3724 C  CH2   . TRP   C 122 ? 0.34640 0.28909 0.26191 -0.03319 0.01252  0.05145  121 TRP   D CH2   
3725 N  N     . LEU   C 123 ? 0.17124 0.24260 0.24194 -0.02550 -0.00682 0.03463  122 LEU   D N     
3726 C  CA    . LEU   C 123 ? 0.16147 0.21205 0.26010 0.01083  0.00784  0.03213  122 LEU   D CA    
3727 C  C     . LEU   C 123 ? 0.18304 0.21814 0.26569 0.00797  0.02205  0.01743  122 LEU   D C     
3728 O  O     . LEU   C 123 ? 0.17616 0.22053 0.24208 0.00168  0.04509  0.02356  122 LEU   D O     
3729 C  CB    . LEU   C 123 ? 0.18005 0.20567 0.21485 0.00013  -0.00353 0.02585  122 LEU   D CB    
3730 C  CG    . LEU   C 123 ? 0.18974 0.21872 0.23584 -0.01600 0.01735  0.04709  122 LEU   D CG    
3731 C  CD1   . LEU   C 123 ? 0.14443 0.26899 0.22002 -0.03013 0.03087  0.04760  122 LEU   D CD1   
3732 C  CD2   . LEU   C 123 ? 0.20630 0.21170 0.27671 -0.00762 -0.00330 0.01984  122 LEU   D CD2   
3733 N  N     . ASP   C 124 ? 0.19769 0.20761 0.23304 -0.01141 0.03819  0.02101  123 ASP   D N     
3734 C  CA    . ASP   C 124 ? 0.27736 0.19305 0.19803 -0.02644 0.04383  0.01892  123 ASP   D CA    
3735 C  C     . ASP   C 124 ? 0.25690 0.23238 0.21457 0.00477  0.07753  0.00671  123 ASP   D C     
3736 O  O     . ASP   C 124 ? 0.22491 0.26346 0.27685 0.02713  0.08005  0.02460  123 ASP   D O     
3737 C  CB    . ASP   C 124 ? 0.28635 0.18980 0.23421 -0.04124 0.02116  0.00716  123 ASP   D CB    
3738 C  CG    . ASP   C 124 ? 0.27559 0.21215 0.26527 -0.05327 0.02388  -0.00900 123 ASP   D CG    
3739 O  OD1   . ASP   C 124 ? 0.27707 0.22862 0.26727 -0.04278 0.06865  0.00169  123 ASP   D OD1   
3740 O  OD2   . ASP   C 124 ? 0.25282 0.22505 0.34738 -0.03824 0.03279  -0.02487 123 ASP   D OD2   
3741 N  N     . GLY   C 125 ? 0.26503 0.23028 0.17463 -0.03103 0.05851  0.00385  124 GLY   D N     
3742 C  CA    . GLY   C 125 ? 0.26688 0.22257 0.21591 -0.00952 0.07068  0.01880  124 GLY   D CA    
3743 C  C     . GLY   C 125 ? 0.21130 0.22471 0.22522 0.01008  0.07474  0.02001  124 GLY   D C     
3744 O  O     . GLY   C 125 ? 0.27393 0.27039 0.22704 0.01861  0.09170  0.01164  124 GLY   D O     
3745 N  N     . LYS   C 126 ? 0.19696 0.21545 0.23295 -0.02724 0.05131  0.03702  125 LYS   D N     
3746 C  CA    . LYS   C 126 ? 0.19291 0.22302 0.27203 0.02462  0.06151  0.03011  125 LYS   D CA    
3747 C  C     . LYS   C 126 ? 0.18354 0.20746 0.23284 0.01143  0.04148  0.02937  125 LYS   D C     
3748 O  O     . LYS   C 126 ? 0.19049 0.23060 0.24129 0.00268  0.05201  -0.02731 125 LYS   D O     
3749 C  CB    . LYS   C 126 ? 0.19492 0.25881 0.37417 0.02060  0.08431  0.08125  125 LYS   D CB    
3750 C  CG    . LYS   C 126 ? 0.18908 0.31610 0.51514 0.07379  0.09978  0.06714  125 LYS   D CG    
3751 C  CD    . LYS   C 126 ? 0.26946 0.39416 0.66268 0.05875  0.13272  0.05893  125 LYS   D CD    
3752 C  CE    . LYS   C 126 ? 0.31396 0.44799 0.75261 0.10676  0.08967  0.06000  125 LYS   D CE    
3753 N  NZ    . LYS   C 126 ? 0.39389 0.48243 0.80591 0.05603  0.06795  0.05225  125 LYS   D NZ    
3754 N  N     . HIS   C 127 ? 0.15467 0.17966 0.21203 -0.00280 0.04596  0.03154  126 HIS   D N     
3755 C  CA    . HIS   C 127 ? 0.19738 0.17404 0.16197 0.02636  0.03751  0.02685  126 HIS   D CA    
3756 C  C     . HIS   C 127 ? 0.21624 0.14189 0.17772 0.00129  0.02590  0.00411  126 HIS   D C     
3757 O  O     . HIS   C 127 ? 0.21504 0.18352 0.20053 -0.00430 0.02646  0.00497  126 HIS   D O     
3758 C  CB    . HIS   C 127 ? 0.22264 0.16935 0.17894 0.02170  0.01850  0.01845  126 HIS   D CB    
3759 C  CG    . HIS   C 127 ? 0.18952 0.15826 0.17765 0.02600  0.03344  0.00632  126 HIS   D CG    
3760 N  ND1   . HIS   C 127 ? 0.18177 0.16661 0.16347 0.00611  0.02223  0.01041  126 HIS   D ND1   
3761 C  CD2   . HIS   C 127 ? 0.17478 0.15749 0.20729 0.01201  0.02523  0.02226  126 HIS   D CD2   
3762 C  CE1   . HIS   C 127 ? 0.19628 0.17817 0.17084 0.00367  -0.00351 0.00099  126 HIS   D CE1   
3763 N  NE2   . HIS   C 127 ? 0.19260 0.18502 0.17893 0.00455  -0.00982 0.00269  126 HIS   D NE2   
3764 N  N     . VAL   C 128 ? 0.20983 0.16778 0.16451 0.02180  0.02673  0.01434  127 VAL   D N     
3765 C  CA    . VAL   C 128 ? 0.20878 0.17137 0.13010 -0.00065 0.00333  0.01504  127 VAL   D CA    
3766 C  C     . VAL   C 128 ? 0.21035 0.16007 0.15221 -0.01229 0.03868  0.02524  127 VAL   D C     
3767 O  O     . VAL   C 128 ? 0.22962 0.15108 0.17016 -0.01370 0.04434  0.00708  127 VAL   D O     
3768 C  CB    . VAL   C 128 ? 0.21094 0.17412 0.12732 -0.01781 0.00783  0.01148  127 VAL   D CB    
3769 C  CG1   . VAL   C 128 ? 0.22891 0.16490 0.16379 -0.00070 -0.00860 0.03689  127 VAL   D CG1   
3770 C  CG2   . VAL   C 128 ? 0.23288 0.20383 0.12794 0.02487  0.02781  -0.00679 127 VAL   D CG2   
3771 N  N     . VAL   C 129 ? 0.20373 0.13855 0.17718 0.01979  0.02764  0.02826  128 VAL   D N     
3772 C  CA    . VAL   C 129 ? 0.25058 0.14526 0.17792 0.00044  0.01610  -0.01400 128 VAL   D CA    
3773 C  C     . VAL   C 129 ? 0.19770 0.15240 0.19348 0.01163  0.03494  0.02337  128 VAL   D C     
3774 O  O     . VAL   C 129 ? 0.20126 0.17106 0.19334 0.00182  0.02398  0.03027  128 VAL   D O     
3775 C  CB    . VAL   C 129 ? 0.22125 0.15597 0.17259 0.00255  0.03024  0.01061  128 VAL   D CB    
3776 C  CG1   . VAL   C 129 ? 0.21431 0.15860 0.18870 -0.00339 0.00263  -0.01347 128 VAL   D CG1   
3777 C  CG2   . VAL   C 129 ? 0.20977 0.19706 0.23091 0.03283  -0.00068 0.00721  128 VAL   D CG2   
3778 N  N     . PHE   C 130 ? 0.18617 0.14857 0.17633 0.01602  0.01009  0.01400  129 PHE   D N     
3779 C  CA    . PHE   C 130 ? 0.20774 0.15126 0.21541 0.01373  0.02368  0.02047  129 PHE   D CA    
3780 C  C     . PHE   C 130 ? 0.21296 0.15804 0.18826 0.01165  0.06760  -0.00048 129 PHE   D C     
3781 O  O     . PHE   C 130 ? 0.21401 0.16473 0.23592 0.03852  -0.02651 0.00272  129 PHE   D O     
3782 C  CB    . PHE   C 130 ? 0.25229 0.14122 0.19578 -0.00354 -0.01403 0.01203  129 PHE   D CB    
3783 C  CG    . PHE   C 130 ? 0.17656 0.12203 0.19441 -0.01138 -0.00434 -0.01144 129 PHE   D CG    
3784 C  CD1   . PHE   C 130 ? 0.22484 0.15765 0.17700 0.03523  0.01369  0.01797  129 PHE   D CD1   
3785 C  CD2   . PHE   C 130 ? 0.19487 0.16504 0.19366 0.00812  0.00901  -0.00185 129 PHE   D CD2   
3786 C  CE1   . PHE   C 130 ? 0.14875 0.15601 0.25876 0.00101  0.00817  -0.02731 129 PHE   D CE1   
3787 C  CE2   . PHE   C 130 ? 0.20631 0.17593 0.20316 -0.01215 -0.02314 0.01760  129 PHE   D CE2   
3788 C  CZ    . PHE   C 130 ? 0.16779 0.17136 0.17875 -0.01113 -0.03801 -0.02904 129 PHE   D CZ    
3789 N  N     . GLY   C 131 ? 0.22607 0.14067 0.19640 0.03164  0.03021  -0.01174 130 GLY   D N     
3790 C  CA    . GLY   C 131 ? 0.24081 0.16171 0.21232 0.03341  -0.01000 -0.02490 130 GLY   D CA    
3791 C  C     . GLY   C 131 ? 0.21444 0.13955 0.21358 0.02000  0.03764  -0.01189 130 GLY   D C     
3792 O  O     . GLY   C 131 ? 0.19336 0.17395 0.20390 0.00499  0.00409  -0.01483 130 GLY   D O     
3793 N  N     . LYS   C 132 ? 0.22329 0.14754 0.23785 0.00831  0.01203  -0.01926 131 LYS   D N     
3794 C  CA    . LYS   C 132 ? 0.20557 0.16824 0.23998 -0.01225 0.04230  -0.02209 131 LYS   D CA    
3795 C  C     . LYS   C 132 ? 0.16266 0.16867 0.21173 0.00081  -0.01696 -0.01833 131 LYS   D C     
3796 O  O     . LYS   C 132 ? 0.20531 0.20812 0.21697 0.03171  -0.01704 -0.01497 131 LYS   D O     
3797 C  CB    . LYS   C 132 ? 0.25186 0.17938 0.32749 -0.02357 0.03775  0.00148  131 LYS   D CB    
3798 C  CG    . LYS   C 132 ? 0.29266 0.19896 0.40614 -0.03924 0.01834  0.01169  131 LYS   D CG    
3799 C  CD    . LYS   C 132 ? 0.42753 0.18590 0.46697 -0.01361 0.01129  0.03287  131 LYS   D CD    
3800 C  CE    . LYS   C 132 ? 0.54558 0.16831 0.52142 -0.01158 -0.00994 0.02279  131 LYS   D CE    
3801 N  NZ    . LYS   C 132 ? 0.61822 0.19077 0.56881 -0.04311 -0.07135 0.01985  131 LYS   D NZ    
3802 N  N     . VAL   C 133 ? 0.20066 0.17393 0.21254 0.00575  0.01294  -0.02237 132 VAL   D N     
3803 C  CA    . VAL   C 133 ? 0.19379 0.16165 0.21564 0.00402  0.05748  -0.00753 132 VAL   D CA    
3804 C  C     . VAL   C 133 ? 0.21258 0.15246 0.26574 -0.00884 0.01273  -0.03713 132 VAL   D C     
3805 O  O     . VAL   C 133 ? 0.22545 0.18431 0.31382 -0.00986 0.00361  -0.02345 132 VAL   D O     
3806 C  CB    . VAL   C 133 ? 0.26025 0.17074 0.19465 0.00037  0.07182  0.01039  132 VAL   D CB    
3807 C  CG1   . VAL   C 133 ? 0.25681 0.19333 0.26085 0.00220  0.04957  0.01250  132 VAL   D CG1   
3808 C  CG2   . VAL   C 133 ? 0.25999 0.16249 0.24214 -0.03133 0.03978  0.01430  132 VAL   D CG2   
3809 N  N     . LYS   C 134 ? 0.22020 0.16382 0.31291 0.04418  0.02518  -0.00457 133 LYS   D N     
3810 C  CA    . LYS   C 134 ? 0.24832 0.18923 0.35330 0.03770  0.03699  -0.00379 133 LYS   D CA    
3811 C  C     . LYS   C 134 ? 0.24284 0.20811 0.34466 0.01536  0.10966  -0.01523 133 LYS   D C     
3812 O  O     . LYS   C 134 ? 0.36467 0.28316 0.38949 -0.07870 0.12624  -0.07243 133 LYS   D O     
3813 C  CB    . LYS   C 134 ? 0.22157 0.19631 0.39258 0.05908  -0.01364 0.00606  133 LYS   D CB    
3814 C  CG    . LYS   C 134 ? 0.33050 0.23781 0.43253 0.03155  -0.01403 0.03909  133 LYS   D CG    
3815 C  CD    . LYS   C 134 ? 0.39424 0.28200 0.50257 0.03337  -0.00771 0.04134  133 LYS   D CD    
3816 C  CE    . LYS   C 134 ? 0.51056 0.33795 0.55701 -0.02350 0.00551  0.05582  133 LYS   D CE    
3817 N  NZ    . LYS   C 134 ? 0.57094 0.38384 0.59388 -0.01112 0.00326  0.06029  133 LYS   D NZ    
3818 N  N     . GLU   C 135 ? 0.31376 0.23249 0.29745 0.04439  0.07649  -0.01763 134 GLU   D N     
3819 C  CA    . GLU   C 135 ? 0.27018 0.25256 0.33263 0.08887  0.05771  -0.01766 134 GLU   D CA    
3820 C  C     . GLU   C 135 ? 0.18823 0.23166 0.30162 0.04413  0.04316  -0.02517 134 GLU   D C     
3821 O  O     . GLU   C 135 ? 0.25584 0.22583 0.26686 0.01584  0.00766  -0.06029 134 GLU   D O     
3822 C  CB    . GLU   C 135 ? 0.41442 0.30773 0.41447 0.15711  0.02650  -0.01140 134 GLU   D CB    
3823 C  CG    . GLU   C 135 ? 0.64952 0.36324 0.53508 0.17615  -0.06089 -0.01993 134 GLU   D CG    
3824 C  CD    . GLU   C 135 ? 0.89879 0.41745 0.62109 0.13452  -0.14584 -0.04645 134 GLU   D CD    
3825 O  OE1   . GLU   C 135 ? 0.95586 0.44800 0.63298 0.11252  -0.19403 -0.03694 134 GLU   D OE1   
3826 O  OE2   . GLU   C 135 ? 1.00493 0.43449 0.65479 0.12122  -0.18250 -0.06857 134 GLU   D OE2   
3827 N  N     . GLY   C 136 ? 0.27861 0.21925 0.26209 0.00838  0.03931  -0.01332 135 GLY   D N     
3828 C  CA    . GLY   C 136 ? 0.21819 0.21481 0.23733 -0.01184 0.00618  0.02045  135 GLY   D CA    
3829 C  C     . GLY   C 136 ? 0.23484 0.20936 0.26206 -0.00756 0.00961  -0.02762 135 GLY   D C     
3830 O  O     . GLY   C 136 ? 0.23661 0.20287 0.27776 -0.00003 0.03312  -0.06834 135 GLY   D O     
3831 N  N     . MET   C 137 ? 0.25564 0.21938 0.22880 0.00558  0.03974  -0.02986 136 MET   D N     
3832 C  CA    . MET   C 137 ? 0.26328 0.22977 0.23178 -0.03548 0.06624  -0.01866 136 MET   D CA    
3833 C  C     . MET   C 137 ? 0.25645 0.22325 0.21485 -0.01188 0.03518  -0.04160 136 MET   D C     
3834 O  O     . MET   C 137 ? 0.26942 0.24863 0.27448 -0.00583 0.02470  0.01379  136 MET   D O     
3835 C  CB    . MET   C 137 ? 0.28678 0.25871 0.27651 -0.04723 0.06376  -0.02102 136 MET   D CB    
3836 C  CG    . MET   C 137 ? 0.37309 0.29073 0.31116 -0.03520 0.06753  -0.04352 136 MET   D CG    
3837 S  SD    . MET   C 137 ? 0.33658 0.30242 0.31601 -0.01794 0.10184  -0.05400 136 MET   D SD    
3838 C  CE    . MET   C 137 ? 0.26936 0.30992 0.28347 0.02255  -0.02681 -0.04573 136 MET   D CE    
3839 N  N     . ASN   C 138 ? 0.27679 0.22607 0.22946 -0.00823 0.05905  -0.02842 137 ASN   D N     
3840 C  CA    . ASN   C 138 ? 0.31466 0.21122 0.23686 -0.04046 0.08322  -0.05377 137 ASN   D CA    
3841 C  C     . ASN   C 138 ? 0.24511 0.22820 0.25401 -0.02788 0.02398  -0.01808 137 ASN   D C     
3842 O  O     . ASN   C 138 ? 0.23192 0.25700 0.23224 -0.00892 0.04044  -0.03896 137 ASN   D O     
3843 C  CB    . ASN   C 138 ? 0.39525 0.21802 0.28861 -0.00125 0.11386  -0.06885 137 ASN   D CB    
3844 C  CG    . ASN   C 138 ? 0.46593 0.24167 0.36426 0.05122  0.17482  -0.05638 137 ASN   D CG    
3845 O  OD1   . ASN   C 138 ? 0.43320 0.25495 0.37360 0.04967  0.11905  -0.01898 137 ASN   D OD1   
3846 N  ND2   . ASN   C 138 ? 0.54192 0.29417 0.43665 0.01242  0.20105  -0.01844 137 ASN   D ND2   
3847 N  N     . ILE   C 139 ? 0.21178 0.23069 0.21718 -0.02487 0.01997  -0.06174 138 ILE   D N     
3848 C  CA    . ILE   C 139 ? 0.20091 0.21297 0.22348 0.00978  0.04589  -0.05025 138 ILE   D CA    
3849 C  C     . ILE   C 139 ? 0.17498 0.22443 0.20267 0.00857  0.01427  -0.04590 138 ILE   D C     
3850 O  O     . ILE   C 139 ? 0.19657 0.22676 0.23529 0.00964  0.01322  -0.02610 138 ILE   D O     
3851 C  CB    . ILE   C 139 ? 0.17372 0.20673 0.23747 0.00217  0.02806  -0.01120 138 ILE   D CB    
3852 C  CG1   . ILE   C 139 ? 0.21367 0.26641 0.26038 0.00839  0.04033  -0.03070 138 ILE   D CG1   
3853 C  CG2   . ILE   C 139 ? 0.17972 0.18487 0.28434 -0.01758 0.01563  -0.03471 138 ILE   D CG2   
3854 C  CD1   . ILE   C 139 ? 0.22326 0.29986 0.25017 0.00352  0.02101  -0.03587 138 ILE   D CD1   
3855 N  N     . VAL   C 140 ? 0.21573 0.24125 0.18988 0.01235  0.03778  -0.03845 139 VAL   D N     
3856 C  CA    . VAL   C 140 ? 0.24331 0.25911 0.19935 -0.00177 0.00535  -0.02991 139 VAL   D CA    
3857 C  C     . VAL   C 140 ? 0.21124 0.24561 0.20817 -0.00108 0.02906  -0.02084 139 VAL   D C     
3858 O  O     . VAL   C 140 ? 0.21895 0.24794 0.23312 0.00765  -0.02280 -0.03973 139 VAL   D O     
3859 C  CB    . VAL   C 140 ? 0.22456 0.25881 0.19454 0.01739  0.00506  -0.02728 139 VAL   D CB    
3860 C  CG1   . VAL   C 140 ? 0.20722 0.30169 0.22213 0.04195  0.01013  0.00386  139 VAL   D CG1   
3861 C  CG2   . VAL   C 140 ? 0.22586 0.23282 0.20539 0.02653  0.01379  -0.00283 139 VAL   D CG2   
3862 N  N     . GLU   C 141 ? 0.18528 0.26019 0.22956 -0.02385 -0.00256 -0.03329 140 GLU   D N     
3863 C  CA    . GLU   C 141 ? 0.20067 0.26636 0.23213 -0.01967 0.00713  -0.04408 140 GLU   D CA    
3864 C  C     . GLU   C 141 ? 0.21489 0.25095 0.24056 -0.04717 0.02481  -0.03711 140 GLU   D C     
3865 O  O     . GLU   C 141 ? 0.24694 0.24777 0.24996 0.00494  0.01054  -0.04092 140 GLU   D O     
3866 C  CB    . GLU   C 141 ? 0.26036 0.28411 0.26508 -0.06493 0.05125  -0.06894 140 GLU   D CB    
3867 C  CG    . GLU   C 141 ? 0.38076 0.32020 0.30684 -0.11249 0.09184  -0.06315 140 GLU   D CG    
3868 C  CD    . GLU   C 141 ? 0.46376 0.35831 0.35242 -0.13785 0.12358  -0.07905 140 GLU   D CD    
3869 O  OE1   . GLU   C 141 ? 0.49694 0.38261 0.40642 -0.08759 0.16346  -0.11824 140 GLU   D OE1   
3870 O  OE2   . GLU   C 141 ? 0.54678 0.37693 0.44122 -0.13975 0.08908  -0.05868 140 GLU   D OE2   
3871 N  N     . ALA   C 142 ? 0.19657 0.23788 0.22178 -0.04356 0.02105  -0.05269 141 ALA   D N     
3872 C  CA    . ALA   C 142 ? 0.22376 0.25644 0.23585 -0.06121 -0.00838 -0.03178 141 ALA   D CA    
3873 C  C     . ALA   C 142 ? 0.26950 0.24363 0.22796 -0.04658 -0.02461 -0.01500 141 ALA   D C     
3874 O  O     . ALA   C 142 ? 0.38832 0.23473 0.26505 -0.05864 -0.08754 -0.00436 141 ALA   D O     
3875 C  CB    . ALA   C 142 ? 0.24427 0.25367 0.25314 -0.03225 -0.02555 -0.02781 141 ALA   D CB    
3876 N  N     . MET   C 143 ? 0.19887 0.22025 0.22493 -0.03677 0.05106  -0.07742 142 MET   D N     
3877 C  CA    . MET   C 143 ? 0.19718 0.21112 0.25320 -0.02632 0.00251  -0.05359 142 MET   D CA    
3878 C  C     . MET   C 143 ? 0.20012 0.22230 0.36529 -0.03383 -0.04174 -0.07069 142 MET   D C     
3879 O  O     . MET   C 143 ? 0.22840 0.23211 0.31485 -0.01578 -0.06334 -0.07295 142 MET   D O     
3880 C  CB    . MET   C 143 ? 0.17359 0.22332 0.24093 0.01319  -0.02802 -0.05221 142 MET   D CB    
3881 C  CG    . MET   C 143 ? 0.18326 0.25499 0.21962 0.01898  -0.02165 -0.02718 142 MET   D CG    
3882 S  SD    . MET   C 143 ? 0.21002 0.25515 0.25889 -0.01434 0.01405  -0.04494 142 MET   D SD    
3883 C  CE    . MET   C 143 ? 0.29693 0.23343 0.32716 -0.00223 -0.03915 -0.09286 142 MET   D CE    
3884 N  N     . GLU   C 144 ? 0.20364 0.24317 0.50531 -0.00880 -0.05100 -0.07557 143 GLU   D N     
3885 C  CA    . GLU   C 144 ? 0.20032 0.30478 0.55649 0.01938  -0.08975 -0.07970 143 GLU   D CA    
3886 C  C     . GLU   C 144 ? 0.23938 0.35657 0.57032 0.04667  -0.14676 -0.13225 143 GLU   D C     
3887 O  O     . GLU   C 144 ? 0.26463 0.38950 0.64721 0.01979  -0.18047 -0.11887 143 GLU   D O     
3888 C  CB    . GLU   C 144 ? 0.18134 0.31901 0.54749 -0.01592 -0.00063 -0.06995 143 GLU   D CB    
3889 C  CG    . GLU   C 144 ? 0.40097 0.33512 0.46094 -0.06567 -0.02735 -0.03599 143 GLU   D CG    
3890 C  CD    . GLU   C 144 ? 0.46493 0.35028 0.45251 -0.01077 -0.04420 -0.01872 143 GLU   D CD    
3891 O  OE1   . GLU   C 144 ? 0.46395 0.36223 0.42663 -0.06558 -0.01080 -0.07481 143 GLU   D OE1   
3892 O  OE2   . GLU   C 144 ? 0.54272 0.35269 0.46144 0.08845  -0.07911 0.02772  143 GLU   D OE2   
3893 N  N     . ARG   C 145 ? 0.40903 0.37447 0.46985 0.06645  -0.12104 -0.18700 144 ARG   D N     
3894 C  CA    . ARG   C 145 ? 0.48806 0.41520 0.43119 0.07240  -0.08137 -0.14677 144 ARG   D CA    
3895 C  C     . ARG   C 145 ? 0.43118 0.42176 0.35643 0.12049  -0.10413 -0.11925 144 ARG   D C     
3896 O  O     . ARG   C 145 ? 0.47465 0.45312 0.35287 0.13758  -0.12749 -0.12603 144 ARG   D O     
3897 C  CB    . ARG   C 145 ? 0.61687 0.46494 0.44678 0.02693  -0.01586 -0.11927 144 ARG   D CB    
3898 C  CG    . ARG   C 145 ? 0.66070 0.49001 0.44236 -0.03979 0.03956  -0.11084 144 ARG   D CG    
3899 C  CD    . ARG   C 145 ? 0.72915 0.51377 0.41107 -0.09930 0.06642  -0.09916 144 ARG   D CD    
3900 N  NE    . ARG   C 145 ? 0.75976 0.52187 0.37350 -0.16250 0.08970  -0.09411 144 ARG   D NE    
3901 C  CZ    . ARG   C 145 ? 0.80968 0.52606 0.36866 -0.20685 0.03914  -0.10305 144 ARG   D CZ    
3902 N  NH1   . ARG   C 145 ? 0.82892 0.53981 0.37968 -0.20795 0.02555  -0.10664 144 ARG   D NH1   
3903 N  NH2   . ARG   C 145 ? 0.77654 0.50997 0.34117 -0.22615 0.08766  -0.09785 144 ARG   D NH2   
3904 N  N     . PHE   C 146 ? 0.33728 0.37883 0.24478 0.14825  -0.07590 -0.12150 145 PHE   D N     
3905 C  CA    . PHE   C 146 ? 0.31946 0.33179 0.22949 0.14265  -0.04566 -0.08598 145 PHE   D CA    
3906 C  C     . PHE   C 146 ? 0.27446 0.30967 0.22151 0.15311  -0.00078 -0.05100 145 PHE   D C     
3907 O  O     . PHE   C 146 ? 0.35960 0.30149 0.24461 0.11310  0.10183  0.01036  145 PHE   D O     
3908 C  CB    . PHE   C 146 ? 0.32311 0.31984 0.22868 0.11285  -0.05963 -0.06466 145 PHE   D CB    
3909 C  CG    . PHE   C 146 ? 0.26716 0.29051 0.20873 0.08220  0.00391  -0.06663 145 PHE   D CG    
3910 C  CD1   . PHE   C 146 ? 0.26399 0.29675 0.21008 -0.01892 0.02110  -0.04605 145 PHE   D CD1   
3911 C  CD2   . PHE   C 146 ? 0.27014 0.29999 0.21585 0.09840  0.00455  -0.04444 145 PHE   D CD2   
3912 C  CE1   . PHE   C 146 ? 0.20860 0.30493 0.27514 -0.03644 0.01405  -0.06463 145 PHE   D CE1   
3913 C  CE2   . PHE   C 146 ? 0.19352 0.31703 0.26816 0.01955  0.05655  -0.03070 145 PHE   D CE2   
3914 C  CZ    . PHE   C 146 ? 0.16491 0.30290 0.27925 -0.00920 0.04034  -0.03961 145 PHE   D CZ    
3915 N  N     . GLY   C 147 ? 0.26251 0.33028 0.27061 0.13800  -0.03733 -0.05191 146 GLY   D N     
3916 C  CA    . GLY   C 147 ? 0.21175 0.31571 0.20559 0.07894  -0.04455 -0.02553 146 GLY   D CA    
3917 C  C     . GLY   C 147 ? 0.25437 0.30809 0.17473 0.06448  -0.03118 -0.00219 146 GLY   D C     
3918 O  O     . GLY   C 147 ? 0.31070 0.34388 0.16958 0.09657  -0.02587 -0.00929 146 GLY   D O     
3919 N  N     . SER   C 148 ? 0.22776 0.28212 0.16907 0.06459  0.01566  0.03917  147 SER   D N     
3920 C  CA    . SER   C 148 ? 0.19354 0.30106 0.20850 0.04800  -0.01911 0.04049  147 SER   D CA    
3921 C  C     . SER   C 148 ? 0.17933 0.32201 0.22634 -0.00326 -0.04594 0.03016  147 SER   D C     
3922 O  O     . SER   C 148 ? 0.18326 0.32136 0.22903 -0.01544 -0.03733 0.01468  147 SER   D O     
3923 C  CB    . SER   C 148 ? 0.24458 0.26730 0.20855 0.03227  -0.02271 0.01119  147 SER   D CB    
3924 O  OG    . SER   C 148 ? 0.20836 0.25074 0.19131 0.03633  -0.00245 -0.00529 147 SER   D OG    
3925 N  N     A ARG   C 149 ? 0.17424 0.33979 0.22404 -0.03966 -0.02885 0.02089  148 ARG   D N     
3926 N  N     B ARG   C 149 ? 0.17611 0.33868 0.23476 -0.01917 -0.04542 0.01562  148 ARG   D N     
3927 C  CA    A ARG   C 149 ? 0.14722 0.36747 0.21902 -0.06190 -0.03592 0.03762  148 ARG   D CA    
3928 C  CA    B ARG   C 149 ? 0.15912 0.36568 0.24409 -0.01876 -0.04241 0.00814  148 ARG   D CA    
3929 C  C     A ARG   C 149 ? 0.13121 0.37070 0.21340 -0.02006 -0.03517 0.05010  148 ARG   D C     
3930 C  C     B ARG   C 149 ? 0.17423 0.37515 0.22719 0.01549  -0.03638 0.02865  148 ARG   D C     
3931 O  O     A ARG   C 149 ? 0.11998 0.39662 0.18656 -0.03235 -0.01772 0.06289  148 ARG   D O     
3932 O  O     B ARG   C 149 ? 0.17475 0.39495 0.17870 0.04064  -0.06794 0.02738  148 ARG   D O     
3933 C  CB    A ARG   C 149 ? 0.17199 0.39709 0.22063 -0.04848 -0.02981 0.04793  148 ARG   D CB    
3934 C  CB    B ARG   C 149 ? 0.14735 0.38449 0.26192 -0.01251 -0.02327 -0.01728 148 ARG   D CB    
3935 C  CG    A ARG   C 149 ? 0.20114 0.40355 0.23276 -0.06836 -0.04299 0.03976  148 ARG   D CG    
3936 C  CG    B ARG   C 149 ? 0.13447 0.38521 0.27425 -0.03100 -0.02130 -0.03673 148 ARG   D CG    
3937 C  CD    A ARG   C 149 ? 0.16212 0.41973 0.24947 -0.05261 -0.05999 0.03085  148 ARG   D CD    
3938 C  CD    B ARG   C 149 ? 0.10918 0.37460 0.29130 -0.01970 0.02277  -0.07779 148 ARG   D CD    
3939 N  NE    A ARG   C 149 ? 0.12478 0.41729 0.29461 0.00716  -0.06048 0.01788  148 ARG   D NE    
3940 N  NE    B ARG   C 149 ? 0.12631 0.37535 0.31433 0.00398  0.04182  -0.10625 148 ARG   D NE    
3941 C  CZ    A ARG   C 149 ? 0.15029 0.41812 0.27740 0.03169  -0.08432 0.00044  148 ARG   D CZ    
3942 C  CZ    B ARG   C 149 ? 0.13323 0.36980 0.35537 0.04047  0.03388  -0.09667 148 ARG   D CZ    
3943 N  NH1   A ARG   C 149 ? 0.21919 0.44283 0.24067 0.06454  -0.07810 -0.01740 148 ARG   D NH1   
3944 N  NH1   B ARG   C 149 ? 0.12565 0.35009 0.36539 0.01337  0.03058  -0.11255 148 ARG   D NH1   
3945 N  NH2   A ARG   C 149 ? 0.18619 0.46681 0.30449 0.02655  -0.06702 0.01755  148 ARG   D NH2   
3946 N  NH2   B ARG   C 149 ? 0.14296 0.38435 0.38989 0.06793  0.01688  -0.08609 148 ARG   D NH2   
3947 N  N     . ASN   C 150 ? 0.14556 0.34802 0.23562 0.01181  -0.02690 0.04086  149 ASN   D N     
3948 C  CA    . ASN   C 150 ? 0.20994 0.31820 0.23954 0.01744  -0.00056 0.03690  149 ASN   D CA    
3949 C  C     . ASN   C 150 ? 0.15544 0.29511 0.20018 0.01350  -0.01735 0.01416  149 ASN   D C     
3950 O  O     . ASN   C 150 ? 0.20370 0.28783 0.19957 -0.00900 0.00870  -0.00892 149 ASN   D O     
3951 C  CB    . ASN   C 150 ? 0.18230 0.30504 0.29830 0.03686  0.00130  0.04250  149 ASN   D CB    
3952 C  CG    . ASN   C 150 ? 0.23162 0.29788 0.24138 0.06668  -0.02937 0.06410  149 ASN   D CG    
3953 O  OD1   . ASN   C 150 ? 0.22113 0.28956 0.22272 0.02184  0.01736  0.05121  149 ASN   D OD1   
3954 N  ND2   . ASN   C 150 ? 0.29348 0.28837 0.28307 0.10722  -0.01104 0.02376  149 ASN   D ND2   
3955 N  N     . GLY   C 151 ? 0.12156 0.29085 0.18369 0.03002  0.02051  0.03868  150 GLY   D N     
3956 C  CA    . GLY   C 151 ? 0.13371 0.27533 0.18753 0.02017  -0.02857 0.00999  150 GLY   D CA    
3957 C  C     . GLY   C 151 ? 0.14723 0.22889 0.16962 0.03525  0.01229  0.01476  150 GLY   D C     
3958 O  O     . GLY   C 151 ? 0.16709 0.21239 0.19084 0.00983  -0.02165 0.01268  150 GLY   D O     
3959 N  N     . LYS   C 152 ? 0.17026 0.22207 0.18326 0.05803  0.02060  0.05328  151 LYS   D N     
3960 C  CA    . LYS   C 152 ? 0.16177 0.24147 0.21881 0.01458  0.04018  0.03208  151 LYS   D CA    
3961 C  C     . LYS   C 152 ? 0.16325 0.24970 0.19297 0.00981  0.01213  0.02239  151 LYS   D C     
3962 O  O     . LYS   C 152 ? 0.17799 0.27851 0.17669 0.02595  -0.00370 0.00191  151 LYS   D O     
3963 C  CB    . LYS   C 152 ? 0.18745 0.23731 0.26635 0.03461  0.01215  0.04215  151 LYS   D CB    
3964 C  CG    . LYS   C 152 ? 0.24208 0.24707 0.31014 0.02171  0.03427  0.00012  151 LYS   D CG    
3965 C  CD    . LYS   C 152 ? 0.27540 0.27056 0.36439 -0.00660 0.04813  -0.06973 151 LYS   D CD    
3966 C  CE    . LYS   C 152 ? 0.32999 0.32417 0.43211 -0.02286 -0.01068 -0.11868 151 LYS   D CE    
3967 N  NZ    . LYS   C 152 ? 0.36776 0.37218 0.47012 -0.00364 0.00071  -0.12500 151 LYS   D NZ    
3968 N  N     . THR   C 153 ? 0.14121 0.28425 0.25220 0.02113  0.04598  0.05185  152 THR   D N     
3969 C  CA    . THR   C 153 ? 0.19093 0.33412 0.23368 0.08810  0.06245  0.09371  152 THR   D CA    
3970 C  C     . THR   C 153 ? 0.21124 0.35414 0.24273 0.10131  0.06860  0.09385  152 THR   D C     
3971 O  O     . THR   C 153 ? 0.26767 0.34946 0.28914 0.09538  0.08296  0.11836  152 THR   D O     
3972 C  CB    . THR   C 153 ? 0.22423 0.35127 0.24601 0.05518  0.02059  0.11243  152 THR   D CB    
3973 O  OG1   . THR   C 153 ? 0.19560 0.38265 0.32525 0.04115  0.03475  0.13805  152 THR   D OG1   
3974 C  CG2   . THR   C 153 ? 0.20596 0.32876 0.23068 0.05541  0.06596  0.08170  152 THR   D CG2   
3975 N  N     . SER   C 154 ? 0.25337 0.38155 0.20279 0.13432  0.07714  0.08170  153 SER   D N     
3976 C  CA    . SER   C 154 ? 0.31878 0.41291 0.21101 0.12548  0.09102  0.07883  153 SER   D CA    
3977 C  C     . SER   C 154 ? 0.32658 0.39949 0.22897 0.12502  0.08912  0.08606  153 SER   D C     
3978 O  O     . SER   C 154 ? 0.36488 0.39022 0.25466 0.11440  0.11697  0.09781  153 SER   D O     
3979 C  CB    . SER   C 154 ? 0.33853 0.45141 0.23619 0.10678  0.09909  0.07218  153 SER   D CB    
3980 O  OG    . SER   C 154 ? 0.37322 0.46287 0.24428 0.10990  0.05028  0.06181  153 SER   D OG    
3981 N  N     . LYS   C 155 ? 0.26055 0.37863 0.23800 0.12364  0.08152  0.07959  154 LYS   D N     
3982 C  CA    . LYS   C 155 ? 0.26838 0.35548 0.23493 0.10830  0.10130  0.08603  154 LYS   D CA    
3983 C  C     . LYS   C 155 ? 0.26470 0.32792 0.26219 0.07989  0.13501  0.09248  154 LYS   D C     
3984 O  O     . LYS   C 155 ? 0.26529 0.35653 0.28711 0.09770  0.13135  0.10707  154 LYS   D O     
3985 C  CB    . LYS   C 155 ? 0.26723 0.34342 0.20334 0.10216  0.09317  0.04567  154 LYS   D CB    
3986 C  CG    . LYS   C 155 ? 0.25503 0.38465 0.25704 0.11856  0.10582  0.02047  154 LYS   D CG    
3987 C  CD    . LYS   C 155 ? 0.26122 0.42135 0.29606 0.06144  0.08665  0.01699  154 LYS   D CD    
3988 C  CE    . LYS   C 155 ? 0.23437 0.46172 0.34055 0.03688  0.10442  -0.00523 154 LYS   D CE    
3989 N  NZ    . LYS   C 155 ? 0.27082 0.49111 0.39066 0.07537  0.11021  -0.02337 154 LYS   D NZ    
3990 N  N     . LYS   C 156 ? 0.30978 0.26184 0.21173 0.10092  0.13035  0.05403  155 LYS   D N     
3991 C  CA    . LYS   C 156 ? 0.34517 0.24656 0.21234 0.03472  0.14396  0.03416  155 LYS   D CA    
3992 C  C     . LYS   C 156 ? 0.26121 0.20271 0.20921 0.03105  0.08187  0.00105  155 LYS   D C     
3993 O  O     . LYS   C 156 ? 0.23946 0.19846 0.21855 0.01864  0.09475  -0.00124 155 LYS   D O     
3994 C  CB    . LYS   C 156 ? 0.47296 0.25367 0.23162 0.02412  0.17045  0.00874  155 LYS   D CB    
3995 C  CG    . LYS   C 156 ? 0.56925 0.33482 0.31993 0.02828  0.11638  0.04728  155 LYS   D CG    
3996 C  CD    . LYS   C 156 ? 0.53121 0.38548 0.38025 0.13285  0.14447  0.05146  155 LYS   D CD    
3997 C  CE    . LYS   C 156 ? 0.56063 0.42002 0.38702 0.12854  0.14470  0.05010  155 LYS   D CE    
3998 N  NZ    . LYS   C 156 ? 0.44190 0.45310 0.45460 0.13959  0.15995  0.05125  155 LYS   D NZ    
3999 N  N     . ILE   C 157 ? 0.21982 0.19699 0.17430 0.03586  0.05696  -0.00964 156 ILE   D N     
4000 C  CA    . ILE   C 157 ? 0.15443 0.20512 0.17498 0.01905  0.00234  -0.02796 156 ILE   D CA    
4001 C  C     . ILE   C 157 ? 0.18379 0.21695 0.16611 -0.02512 0.03673  -0.03291 156 ILE   D C     
4002 O  O     . ILE   C 157 ? 0.18602 0.27990 0.17020 -0.02860 0.05187  -0.06732 156 ILE   D O     
4003 C  CB    . ILE   C 157 ? 0.18657 0.21744 0.19652 0.00833  -0.01371 -0.02779 156 ILE   D CB    
4004 C  CG1   . ILE   C 157 ? 0.21832 0.28302 0.16798 0.01902  0.00987  -0.01719 156 ILE   D CG1   
4005 C  CG2   . ILE   C 157 ? 0.19063 0.19489 0.22119 0.00116  0.00365  -0.01418 156 ILE   D CG2   
4006 C  CD1   . ILE   C 157 ? 0.25409 0.30654 0.18514 -0.00977 0.01267  -0.00402 156 ILE   D CD1   
4007 N  N     . THR   C 158 ? 0.18997 0.18790 0.17638 -0.00030 0.02219  -0.05568 157 THR   D N     
4008 C  CA    . THR   C 158 ? 0.20918 0.18645 0.16007 0.00248  0.03211  -0.01076 157 THR   D CA    
4009 C  C     . THR   C 158 ? 0.14976 0.17501 0.17615 -0.00881 0.02495  -0.04697 157 THR   D C     
4010 O  O     . THR   C 158 ? 0.18504 0.18401 0.17824 -0.00519 0.01178  -0.03330 157 THR   D O     
4011 C  CB    . THR   C 158 ? 0.23961 0.18579 0.19013 -0.00869 -0.00331 -0.01316 157 THR   D CB    
4012 O  OG1   . THR   C 158 ? 0.21227 0.22636 0.22210 -0.01467 0.01033  -0.00775 157 THR   D OG1   
4013 C  CG2   . THR   C 158 ? 0.27659 0.18019 0.21612 -0.03309 0.00573  0.01191  157 THR   D CG2   
4014 N  N     . ILE   C 159 ? 0.14634 0.18909 0.14614 0.02614  -0.00448 -0.03439 158 ILE   D N     
4015 C  CA    . ILE   C 159 ? 0.17894 0.19623 0.17518 0.01787  0.00240  -0.01296 158 ILE   D CA    
4016 C  C     . ILE   C 159 ? 0.15507 0.20566 0.20085 -0.02396 0.00056  -0.02717 158 ILE   D C     
4017 O  O     . ILE   C 159 ? 0.17253 0.20461 0.23577 -0.00694 -0.01401 -0.04947 158 ILE   D O     
4018 C  CB    . ILE   C 159 ? 0.16188 0.20408 0.18792 0.03149  0.02012  -0.01481 158 ILE   D CB    
4019 C  CG1   . ILE   C 159 ? 0.16858 0.19079 0.18327 -0.00227 0.03655  -0.00401 158 ILE   D CG1   
4020 C  CG2   . ILE   C 159 ? 0.18111 0.23380 0.19412 0.05635  -0.00624 0.03246  158 ILE   D CG2   
4021 C  CD1   . ILE   C 159 ? 0.17194 0.21689 0.19824 0.00196  0.02275  0.03227  158 ILE   D CD1   
4022 N  N     . ALA   C 160 ? 0.15631 0.20932 0.18505 -0.00008 0.01021  -0.01185 159 ALA   D N     
4023 C  CA    . ALA   C 160 ? 0.15587 0.23500 0.21525 -0.01616 0.04986  0.00328  159 ALA   D CA    
4024 C  C     . ALA   C 160 ? 0.15590 0.22678 0.24743 -0.03996 0.00775  -0.01418 159 ALA   D C     
4025 O  O     . ALA   C 160 ? 0.17516 0.24044 0.25757 -0.03078 0.03018  -0.00938 159 ALA   D O     
4026 C  CB    . ALA   C 160 ? 0.16671 0.27569 0.18460 -0.01517 0.05034  -0.00538 159 ALA   D CB    
4027 N  N     . ASP   C 161 ? 0.15165 0.22783 0.23384 0.02763  0.00685  -0.01521 160 ASP   D N     
4028 C  CA    . ASP   C 161 ? 0.16576 0.25371 0.24405 0.04798  0.00445  0.00632  160 ASP   D CA    
4029 C  C     . ASP   C 161 ? 0.13989 0.23359 0.22580 0.01355  0.02093  -0.01393 160 ASP   D C     
4030 O  O     . ASP   C 161 ? 0.15052 0.21677 0.22462 -0.00217 -0.02606 -0.01329 160 ASP   D O     
4031 C  CB    . ASP   C 161 ? 0.11943 0.31229 0.29325 0.07369  0.02996  0.00291  160 ASP   D CB    
4032 C  CG    . ASP   C 161 ? 0.19713 0.35597 0.37690 0.10732  0.05408  0.00762  160 ASP   D CG    
4033 O  OD1   . ASP   C 161 ? 0.15960 0.32398 0.41906 0.03352  0.00607  0.05703  160 ASP   D OD1   
4034 O  OD2   . ASP   C 161 ? 0.20543 0.41345 0.40831 0.10230  -0.03979 -0.01922 160 ASP   D OD2   
4035 N  N     . CYS   C 162 ? 0.19441 0.22808 0.22152 0.01265  0.01434  0.03825  161 CYS   D N     
4036 C  CA    . CYS   C 162 ? 0.18924 0.21179 0.20502 0.02753  0.02108  0.01353  161 CYS   D CA    
4037 C  C     . CYS   C 162 ? 0.14805 0.25100 0.23757 0.03316  -0.00667 0.04085  161 CYS   D C     
4038 O  O     . CYS   C 162 ? 0.16026 0.28616 0.26512 0.00192  -0.02117 0.02617  161 CYS   D O     
4039 C  CB    . CYS   C 162 ? 0.19514 0.17318 0.23140 0.03775  0.00474  -0.00988 161 CYS   D CB    
4040 S  SG    . CYS   C 162 ? 0.19769 0.18921 0.21910 0.01336  -0.02026 -0.00524 161 CYS   D SG    
4041 N  N     . GLY   C 163 ? 0.21112 0.21801 0.22985 0.05310  -0.02734 0.01883  162 GLY   D N     
4042 C  CA    . GLY   C 163 ? 0.17920 0.23793 0.26544 0.03175  -0.01038 0.04087  162 GLY   D CA    
4043 C  C     . GLY   C 163 ? 0.18957 0.24783 0.22699 0.05614  -0.01309 0.03922  162 GLY   D C     
4044 O  O     . GLY   C 163 ? 0.18139 0.25795 0.26386 0.04799  -0.04994 0.04467  162 GLY   D O     
4045 N  N     . GLN   C 164 ? 0.20949 0.26624 0.25471 0.05049  -0.02421 0.06116  163 GLN   D N     
4046 C  CA    . GLN   C 164 ? 0.20416 0.26718 0.28145 0.05014  0.01356  0.06127  163 GLN   D CA    
4047 C  C     . GLN   C 164 ? 0.20353 0.25934 0.33520 0.02724  -0.00518 0.04603  163 GLN   D C     
4048 O  O     . GLN   C 164 ? 0.18844 0.26931 0.40787 0.04914  0.01869  0.04166  163 GLN   D O     
4049 C  CB    . GLN   C 164 ? 0.25505 0.26916 0.29671 0.04005  -0.02776 0.05072  163 GLN   D CB    
4050 C  CG    . GLN   C 164 ? 0.26156 0.26555 0.27400 0.05826  -0.04282 0.06884  163 GLN   D CG    
4051 C  CD    . GLN   C 164 ? 0.25823 0.28450 0.29449 0.05503  -0.01047 0.05751  163 GLN   D CD    
4052 O  OE1   . GLN   C 164 ? 0.27865 0.31879 0.31371 0.05798  -0.02341 0.05409  163 GLN   D OE1   
4053 N  NE2   . GLN   C 164 ? 0.25156 0.29436 0.29767 0.06300  -0.01229 0.08522  163 GLN   D NE2   
4054 N  N     . LEU   C 165 ? 0.23879 0.25385 0.35993 0.06553  -0.04335 0.04075  164 LEU   D N     
4055 C  CA    . LEU   C 165 ? 0.33392 0.26369 0.37809 0.08256  -0.06082 0.01176  164 LEU   D CA    
4056 C  C     . LEU   C 165 ? 0.47372 0.32410 0.36252 0.08407  -0.00592 0.02287  164 LEU   D C     
4057 O  O     . LEU   C 165 ? 0.48928 0.35345 0.43304 0.16600  -0.00096 0.05677  164 LEU   D O     
4058 C  CB    . LEU   C 165 ? 0.34681 0.26281 0.39398 0.07848  -0.03316 0.00712  164 LEU   D CB    
4059 C  CG    . LEU   C 165 ? 0.35138 0.28733 0.43040 0.06765  -0.05399 0.01927  164 LEU   D CG    
4060 C  CD1   . LEU   C 165 ? 0.34425 0.30214 0.42214 0.03740  -0.07633 0.00984  164 LEU   D CD1   
4061 C  CD2   . LEU   C 165 ? 0.34289 0.28507 0.46433 0.12463  -0.01750 0.04825  164 LEU   D CD2   
4062 N  N     . MET   D 2   ? 0.64660 0.33999 0.56241 -0.03444 -0.07491 0.10854  1   MET   C N     
4063 C  CA    . MET   D 2   ? 0.54695 0.31847 0.52272 -0.10225 -0.03008 0.10648  1   MET   C CA    
4064 C  C     . MET   D 2   ? 0.44924 0.32525 0.46866 -0.07249 -0.05506 0.11667  1   MET   C C     
4065 O  O     . MET   D 2   ? 0.37745 0.32540 0.47391 -0.04337 -0.05309 0.10701  1   MET   C O     
4066 C  CB    . MET   D 2   ? 0.53553 0.32070 0.52236 -0.11953 0.05182  0.09681  1   MET   C CB    
4067 C  CG    . MET   D 2   ? 0.52886 0.32824 0.51940 -0.12615 0.08491  0.10556  1   MET   C CG    
4068 S  SD    . MET   D 2   ? 0.47727 0.33939 0.51528 -0.08863 0.12658  0.08436  1   MET   C SD    
4069 C  CE    . MET   D 2   ? 0.49070 0.35396 0.53024 -0.01708 0.20195  0.09575  1   MET   C CE    
4070 N  N     . VAL   D 3   ? 0.37192 0.30410 0.37651 -0.09031 -0.03082 0.13199  2   VAL   C N     
4071 C  CA    . VAL   D 3   ? 0.29554 0.30056 0.37142 -0.05217 0.02057  0.10868  2   VAL   C CA    
4072 C  C     . VAL   D 3   ? 0.31563 0.28046 0.34463 -0.01275 0.05272  0.08055  2   VAL   C C     
4073 O  O     . VAL   D 3   ? 0.33012 0.26178 0.46440 0.01622  0.08430  0.04431  2   VAL   C O     
4074 C  CB    . VAL   D 3   ? 0.30239 0.32160 0.35880 -0.05076 0.00170  0.15998  2   VAL   C CB    
4075 C  CG1   . VAL   D 3   ? 0.27130 0.34444 0.40363 -0.02790 0.03193  0.14014  2   VAL   C CG1   
4076 C  CG2   . VAL   D 3   ? 0.32526 0.35619 0.33557 -0.02434 0.00271  0.17590  2   VAL   C CG2   
4077 N  N     . ASN   D 4   ? 0.23348 0.25319 0.24625 -0.02039 -0.00425 0.07072  3   ASN   C N     
4078 C  CA    . ASN   D 4   ? 0.17700 0.19243 0.20092 -0.01538 -0.01706 0.06117  3   ASN   C CA    
4079 C  C     . ASN   D 4   ? 0.24449 0.18289 0.20235 -0.05889 -0.00880 0.00657  3   ASN   C C     
4080 O  O     . ASN   D 4   ? 0.25896 0.23434 0.23945 -0.03679 -0.02579 0.00631  3   ASN   C O     
4081 C  CB    . ASN   D 4   ? 0.19132 0.19293 0.19292 -0.04892 -0.00374 0.02618  3   ASN   C CB    
4082 C  CG    . ASN   D 4   ? 0.23229 0.17944 0.20939 -0.02829 0.01219  0.03313  3   ASN   C CG    
4083 O  OD1   . ASN   D 4   ? 0.23099 0.17284 0.22287 -0.04265 -0.01316 0.03502  3   ASN   C OD1   
4084 N  ND2   . ASN   D 4   ? 0.21799 0.20053 0.24748 -0.03008 0.02248  0.02656  3   ASN   C ND2   
4085 N  N     . PRO   D 5   ? 0.22809 0.20337 0.20878 -0.03270 -0.05766 0.02824  4   PRO   C N     
4086 C  CA    . PRO   D 5   ? 0.25304 0.21520 0.23113 -0.00886 -0.01753 0.02520  4   PRO   C CA    
4087 C  C     . PRO   D 5   ? 0.22092 0.20797 0.23324 -0.01903 -0.02172 0.05232  4   PRO   C C     
4088 O  O     . PRO   D 5   ? 0.20077 0.20042 0.25926 -0.02717 -0.01527 0.05452  4   PRO   C O     
4089 C  CB    . PRO   D 5   ? 0.26079 0.21959 0.28244 -0.00889 -0.07259 -0.02639 4   PRO   C CB    
4090 C  CG    . PRO   D 5   ? 0.26289 0.19645 0.33928 -0.00492 -0.07573 -0.00727 4   PRO   C CG    
4091 C  CD    . PRO   D 5   ? 0.24650 0.16661 0.26425 0.01945  -0.05534 0.01097  4   PRO   C CD    
4092 N  N     . THR   D 6   ? 0.20044 0.21296 0.21252 -0.02118 -0.02376 0.03328  5   THR   C N     
4093 C  CA    A THR   D 6   ? 0.21997 0.20203 0.21037 -0.03461 -0.00226 0.03885  5   THR   C CA    
4094 C  CA    B THR   D 6   ? 0.24742 0.23158 0.24914 -0.02281 -0.03087 0.02290  5   THR   C CA    
4095 C  C     . THR   D 6   ? 0.18483 0.19684 0.23189 -0.01780 -0.04374 0.02239  5   THR   C C     
4096 O  O     . THR   D 6   ? 0.18068 0.24435 0.26516 -0.00612 -0.02343 0.05170  5   THR   C O     
4097 C  CB    A THR   D 6   ? 0.25839 0.18059 0.19436 -0.02400 -0.03226 0.03049  5   THR   C CB    
4098 C  CB    B THR   D 6   ? 0.32974 0.26292 0.29715 -0.00437 -0.09923 -0.00303 5   THR   C CB    
4099 O  OG1   A THR   D 6   ? 0.32796 0.16898 0.21645 -0.01235 -0.03401 0.01617  5   THR   C OG1   
4100 O  OG1   B THR   D 6   ? 0.39101 0.29535 0.34935 -0.01815 -0.13208 -0.04147 5   THR   C OG1   
4101 C  CG2   A THR   D 6   ? 0.29192 0.17246 0.16026 -0.04190 -0.02716 0.00961  5   THR   C CG2   
4102 C  CG2   B THR   D 6   ? 0.40642 0.26470 0.31217 0.02351  -0.08769 0.01983  5   THR   C CG2   
4103 N  N     . VAL   D 7   ? 0.19636 0.20546 0.18799 -0.00774 -0.03790 0.02071  6   VAL   C N     
4104 C  CA    . VAL   D 7   ? 0.21794 0.20070 0.17919 -0.01071 -0.03604 0.01738  6   VAL   C CA    
4105 C  C     . VAL   D 7   ? 0.21380 0.17615 0.18760 0.01965  -0.01463 0.01819  6   VAL   C C     
4106 O  O     . VAL   D 7   ? 0.17939 0.20158 0.21868 -0.01344 -0.03580 0.01674  6   VAL   C O     
4107 C  CB    . VAL   D 7   ? 0.22199 0.23124 0.19609 0.00527  -0.02326 -0.00324 6   VAL   C CB    
4108 C  CG1   . VAL   D 7   ? 0.25213 0.25519 0.26210 -0.01141 -0.04236 -0.03324 6   VAL   C CG1   
4109 C  CG2   . VAL   D 7   ? 0.21676 0.23421 0.23487 -0.01193 0.01684  -0.00740 6   VAL   C CG2   
4110 N  N     . PHE   D 8   ? 0.19955 0.20147 0.19489 0.00391  -0.02203 0.04471  7   PHE   C N     
4111 C  CA    . PHE   D 8   ? 0.22491 0.21503 0.20076 0.00621  -0.05298 0.03175  7   PHE   C CA    
4112 C  C     . PHE   D 8   ? 0.13245 0.21311 0.18816 0.00409  -0.01879 -0.00698 7   PHE   C C     
4113 O  O     . PHE   D 8   ? 0.14566 0.23292 0.18030 0.00189  -0.02487 -0.00673 7   PHE   C O     
4114 C  CB    . PHE   D 8   ? 0.25534 0.22482 0.26203 -0.04366 -0.04639 0.03681  7   PHE   C CB    
4115 C  CG    . PHE   D 8   ? 0.24424 0.24786 0.29993 -0.07079 -0.07856 0.01642  7   PHE   C CG    
4116 C  CD1   . PHE   D 8   ? 0.17912 0.26553 0.34403 -0.05427 -0.11166 0.01855  7   PHE   C CD1   
4117 C  CD2   . PHE   D 8   ? 0.23919 0.26671 0.32931 -0.04005 -0.11119 0.00364  7   PHE   C CD2   
4118 C  CE1   . PHE   D 8   ? 0.18362 0.26418 0.35103 -0.02109 -0.06757 0.02019  7   PHE   C CE1   
4119 C  CE2   . PHE   D 8   ? 0.20392 0.26884 0.36227 -0.05411 -0.09921 0.03726  7   PHE   C CE2   
4120 C  CZ    . PHE   D 8   ? 0.21186 0.26426 0.35868 -0.03279 -0.07703 0.02094  7   PHE   C CZ    
4121 N  N     . PHE   D 9   ? 0.19163 0.20815 0.16191 -0.00954 -0.01656 0.01452  8   PHE   C N     
4122 C  CA    . PHE   D 9   ? 0.18132 0.21745 0.17249 -0.00853 -0.04015 0.03536  8   PHE   C CA    
4123 C  C     . PHE   D 9   ? 0.14274 0.22169 0.19297 -0.00097 -0.01636 -0.01092 8   PHE   C C     
4124 O  O     . PHE   D 9   ? 0.19228 0.22940 0.19988 0.00043  -0.03392 0.00967  8   PHE   C O     
4125 C  CB    . PHE   D 9   ? 0.13937 0.23343 0.17910 -0.01165 -0.02903 0.01897  8   PHE   C CB    
4126 C  CG    . PHE   D 9   ? 0.14428 0.23397 0.18782 0.01933  0.00004  0.00539  8   PHE   C CG    
4127 C  CD1   . PHE   D 9   ? 0.20173 0.21159 0.20745 0.00451  -0.07975 0.03319  8   PHE   C CD1   
4128 C  CD2   . PHE   D 9   ? 0.14978 0.21625 0.19522 -0.02672 -0.02522 0.01340  8   PHE   C CD2   
4129 C  CE1   . PHE   D 9   ? 0.12110 0.21780 0.22592 0.00220  -0.04382 0.01073  8   PHE   C CE1   
4130 C  CE2   . PHE   D 9   ? 0.21753 0.20604 0.15868 -0.01139 -0.04086 0.01354  8   PHE   C CE2   
4131 C  CZ    . PHE   D 9   ? 0.20042 0.19534 0.18234 0.01352  -0.03714 0.02395  8   PHE   C CZ    
4132 N  N     . ASP   D 10  ? 0.15008 0.21133 0.19559 0.00320  -0.03588 0.01387  9   ASP   C N     
4133 C  CA    . ASP   D 10  ? 0.15241 0.23291 0.19019 -0.01618 -0.03450 0.01987  9   ASP   C CA    
4134 C  C     . ASP   D 10  ? 0.14764 0.19916 0.19038 -0.00475 -0.04076 0.00627  9   ASP   C C     
4135 O  O     . ASP   D 10  ? 0.17977 0.24311 0.22267 0.01254  -0.02915 -0.00394 9   ASP   C O     
4136 C  CB    . ASP   D 10  ? 0.17357 0.25266 0.22421 -0.01173 -0.05484 0.02309  9   ASP   C CB    
4137 C  CG    . ASP   D 10  ? 0.14135 0.29078 0.34485 -0.03275 -0.07975 -0.01326 9   ASP   C CG    
4138 O  OD1   . ASP   D 10  ? 0.23249 0.29526 0.38476 -0.04378 -0.03514 0.02826  9   ASP   C OD1   
4139 O  OD2   . ASP   D 10  ? 0.18330 0.31338 0.42845 -0.06635 -0.01511 -0.04328 9   ASP   C OD2   
4140 N  N     . ILE   D 11  ? 0.18428 0.19636 0.17332 0.01202  -0.02106 0.00391  10  ILE   C N     
4141 C  CA    . ILE   D 11  ? 0.19705 0.20342 0.19547 0.01821  -0.04810 0.03125  10  ILE   C CA    
4142 C  C     . ILE   D 11  ? 0.20313 0.22609 0.16442 -0.00162 -0.05432 0.03170  10  ILE   C C     
4143 O  O     . ILE   D 11  ? 0.20228 0.21716 0.19385 -0.01347 -0.05743 -0.00511 10  ILE   C O     
4144 C  CB    . ILE   D 11  ? 0.16194 0.20811 0.20403 0.00437  -0.03354 0.01837  10  ILE   C CB    
4145 C  CG1   . ILE   D 11  ? 0.17647 0.22062 0.20798 -0.00092 -0.05277 0.00496  10  ILE   C CG1   
4146 C  CG2   . ILE   D 11  ? 0.17743 0.23068 0.21103 -0.01047 -0.01663 0.01176  10  ILE   C CG2   
4147 C  CD1   . ILE   D 11  ? 0.22315 0.23509 0.19595 0.02715  -0.07110 -0.01105 10  ILE   C CD1   
4148 N  N     . ALA   D 12  ? 0.17485 0.23897 0.17190 0.02600  -0.04087 0.03080  11  ALA   C N     
4149 C  CA    . ALA   D 12  ? 0.18157 0.27151 0.18174 0.00980  -0.03371 0.05793  11  ALA   C CA    
4150 C  C     . ALA   D 12  ? 0.17004 0.25240 0.16850 -0.00575 -0.09192 0.04315  11  ALA   C C     
4151 O  O     . ALA   D 12  ? 0.18554 0.27823 0.16178 0.00242  -0.06183 0.01522  11  ALA   C O     
4152 C  CB    . ALA   D 12  ? 0.16129 0.27273 0.20263 0.03163  -0.03988 0.03697  11  ALA   C CB    
4153 N  N     . VAL   D 13  ? 0.16743 0.24809 0.17666 0.00935  -0.06268 0.03197  12  VAL   C N     
4154 C  CA    . VAL   D 13  ? 0.19781 0.26100 0.18850 0.00391  -0.03208 0.00332  12  VAL   C CA    
4155 C  C     . VAL   D 13  ? 0.20854 0.25545 0.19407 0.00201  -0.08150 0.01705  12  VAL   C C     
4156 O  O     . VAL   D 13  ? 0.19279 0.27203 0.19401 0.00232  -0.05485 -0.01357 12  VAL   C O     
4157 C  CB    . VAL   D 13  ? 0.22518 0.28544 0.19390 -0.00100 -0.01702 0.01360  12  VAL   C CB    
4158 C  CG1   . VAL   D 13  ? 0.25534 0.31793 0.17908 -0.01194 0.01938  0.03169  12  VAL   C CG1   
4159 C  CG2   . VAL   D 13  ? 0.26394 0.27547 0.22719 -0.02417 -0.01081 0.01885  12  VAL   C CG2   
4160 N  N     . ASP   D 14  ? 0.25569 0.25443 0.18929 -0.02197 -0.07034 0.04249  13  ASP   C N     
4161 C  CA    . ASP   D 14  ? 0.19053 0.29722 0.19814 -0.01395 -0.04047 0.05279  13  ASP   C CA    
4162 C  C     . ASP   D 14  ? 0.21135 0.29117 0.21463 -0.00383 -0.05122 0.02313  13  ASP   C C     
4163 O  O     . ASP   D 14  ? 0.20686 0.29317 0.24027 -0.02775 -0.07303 0.03408  13  ASP   C O     
4164 C  CB    . ASP   D 14  ? 0.27512 0.32987 0.21193 -0.06560 -0.07726 0.07000  13  ASP   C CB    
4165 C  CG    . ASP   D 14  ? 0.33772 0.37350 0.25873 -0.05232 -0.15736 0.04939  13  ASP   C CG    
4166 O  OD1   . ASP   D 14  ? 0.33016 0.37462 0.30339 -0.03562 -0.18424 0.05005  13  ASP   C OD1   
4167 O  OD2   . ASP   D 14  ? 0.39378 0.40235 0.32209 -0.07965 -0.11229 0.02619  13  ASP   C OD2   
4168 N  N     . GLY   D 15  ? 0.20540 0.26971 0.20479 0.00043  -0.04809 0.02559  14  GLY   C N     
4169 C  CA    . GLY   D 15  ? 0.18329 0.25227 0.21613 0.00795  -0.05967 0.04445  14  GLY   C CA    
4170 C  C     . GLY   D 15  ? 0.21199 0.26064 0.19573 -0.00020 -0.03825 0.03091  14  GLY   C C     
4171 O  O     . GLY   D 15  ? 0.22683 0.31040 0.24303 -0.01126 -0.00581 0.00044  14  GLY   C O     
4172 N  N     . GLU   D 16  ? 0.19867 0.24472 0.16999 0.00569  -0.06567 -0.00363 15  GLU   C N     
4173 C  CA    . GLU   D 16  ? 0.19778 0.23347 0.17638 0.00474  -0.05559 0.01160  15  GLU   C CA    
4174 C  C     . GLU   D 16  ? 0.18576 0.25178 0.18540 -0.00149 -0.05764 0.00287  15  GLU   C C     
4175 O  O     . GLU   D 16  ? 0.18894 0.23298 0.21099 0.00199  -0.06717 0.00579  15  GLU   C O     
4176 C  CB    . GLU   D 16  ? 0.18714 0.27903 0.17090 0.00720  -0.03458 0.01543  15  GLU   C CB    
4177 C  CG    . GLU   D 16  ? 0.19558 0.28969 0.19610 0.02462  -0.08208 0.03494  15  GLU   C CG    
4178 C  CD    . GLU   D 16  ? 0.22073 0.29548 0.21749 0.02195  -0.08744 0.02828  15  GLU   C CD    
4179 O  OE1   . GLU   D 16  ? 0.20051 0.31348 0.22001 0.01936  -0.04118 0.01464  15  GLU   C OE1   
4180 O  OE2   . GLU   D 16  ? 0.19283 0.31088 0.27697 0.00588  -0.06424 0.03088  15  GLU   C OE2   
4181 N  N     . PRO   D 17  ? 0.16979 0.26999 0.22797 0.01827  -0.07542 -0.00818 16  PRO   C N     
4182 C  CA    . PRO   D 17  ? 0.15308 0.26894 0.24263 0.04001  -0.02609 0.00193  16  PRO   C CA    
4183 C  C     . PRO   D 17  ? 0.21746 0.28754 0.21171 0.02025  -0.08643 -0.00798 16  PRO   C C     
4184 O  O     . PRO   D 17  ? 0.31660 0.35975 0.21794 0.06234  -0.12721 -0.04803 16  PRO   C O     
4185 C  CB    . PRO   D 17  ? 0.18441 0.27599 0.30795 -0.00242 -0.05339 0.02291  16  PRO   C CB    
4186 C  CG    . PRO   D 17  ? 0.21861 0.30634 0.36190 0.00249  -0.06303 0.03121  16  PRO   C CG    
4187 C  CD    . PRO   D 17  ? 0.19603 0.27473 0.30382 -0.00261 -0.07970 0.00036  16  PRO   C CD    
4188 N  N     . LEU   D 18  ? 0.19443 0.25430 0.21183 0.02792  -0.06345 0.01846  17  LEU   C N     
4189 C  CA    . LEU   D 18  ? 0.17250 0.25843 0.22861 0.04529  -0.04553 -0.00029 17  LEU   C CA    
4190 C  C     . LEU   D 18  ? 0.21646 0.25387 0.21256 0.02620  -0.03569 -0.02530 17  LEU   C C     
4191 O  O     . LEU   D 18  ? 0.38300 0.28471 0.22939 0.00181  -0.05289 -0.03516 17  LEU   C O     
4192 C  CB    . LEU   D 18  ? 0.17888 0.28493 0.23084 0.04292  -0.04657 -0.00155 17  LEU   C CB    
4193 C  CG    . LEU   D 18  ? 0.21735 0.31790 0.20794 0.03968  -0.05491 -0.02148 17  LEU   C CG    
4194 C  CD1   . LEU   D 18  ? 0.29336 0.36264 0.19599 -0.00126 -0.00734 -0.02209 17  LEU   C CD1   
4195 C  CD2   . LEU   D 18  ? 0.18726 0.30960 0.21682 0.00859  -0.03844 -0.01489 17  LEU   C CD2   
4196 N  N     . GLY   D 19  ? 0.20756 0.25230 0.22668 0.01400  -0.03987 0.00567  18  GLY   C N     
4197 C  CA    . GLY   D 19  ? 0.23195 0.23726 0.19918 0.00138  -0.05577 0.00888  18  GLY   C CA    
4198 C  C     . GLY   D 19  ? 0.19230 0.22267 0.18851 0.00102  -0.04254 -0.00867 18  GLY   C C     
4199 O  O     . GLY   D 19  ? 0.25145 0.22838 0.22610 0.00800  -0.04661 -0.02742 18  GLY   C O     
4200 N  N     . ARG   D 20  ? 0.23003 0.24326 0.22177 -0.02155 -0.09035 -0.00643 19  ARG   C N     
4201 C  CA    . ARG   D 20  ? 0.17722 0.25827 0.21857 -0.01768 -0.04893 0.00751  19  ARG   C CA    
4202 C  C     . ARG   D 20  ? 0.23987 0.26418 0.21830 -0.00274 -0.07721 0.00133  19  ARG   C C     
4203 O  O     . ARG   D 20  ? 0.24473 0.25807 0.24365 0.00840  -0.06239 -0.00072 19  ARG   C O     
4204 C  CB    . ARG   D 20  ? 0.20504 0.28055 0.22114 -0.03618 -0.06883 0.01505  19  ARG   C CB    
4205 C  CG    . ARG   D 20  ? 0.24390 0.27479 0.25112 -0.08150 -0.05792 0.04351  19  ARG   C CG    
4206 C  CD    . ARG   D 20  ? 0.20039 0.25751 0.30556 -0.05686 -0.02295 0.01420  19  ARG   C CD    
4207 N  NE    . ARG   D 20  ? 0.18908 0.27412 0.33402 -0.05503 -0.06334 -0.00402 19  ARG   C NE    
4208 C  CZ    . ARG   D 20  ? 0.27429 0.28939 0.32829 -0.11491 -0.09897 0.00595  19  ARG   C CZ    
4209 N  NH1   . ARG   D 20  ? 0.25885 0.33047 0.29273 -0.10120 -0.03807 0.01077  19  ARG   C NH1   
4210 N  NH2   . ARG   D 20  ? 0.37343 0.32081 0.36718 -0.10942 -0.08338 0.02268  19  ARG   C NH2   
4211 N  N     . VAL   D 21  ? 0.19205 0.25742 0.18015 -0.01237 -0.06432 0.00794  20  VAL   C N     
4212 C  CA    . VAL   D 21  ? 0.19367 0.25528 0.18657 0.00380  -0.06911 -0.00873 20  VAL   C CA    
4213 C  C     . VAL   D 21  ? 0.23011 0.22623 0.19409 0.01800  -0.06965 0.00772  20  VAL   C C     
4214 O  O     . VAL   D 21  ? 0.20900 0.27193 0.21947 -0.00975 -0.04739 0.01293  20  VAL   C O     
4215 C  CB    . VAL   D 21  ? 0.21008 0.26155 0.19873 -0.01311 -0.06895 0.00513  20  VAL   C CB    
4216 C  CG1   . VAL   D 21  ? 0.20169 0.25300 0.20244 0.03865  -0.05584 0.02778  20  VAL   C CG1   
4217 C  CG2   . VAL   D 21  ? 0.21617 0.24027 0.22087 0.00907  -0.04755 -0.00111 20  VAL   C CG2   
4218 N  N     . SER   D 22  ? 0.21013 0.19831 0.19397 0.01275  -0.03037 0.00471  21  SER   C N     
4219 C  CA    . SER   D 22  ? 0.20072 0.21357 0.23035 -0.02748 -0.05579 -0.00366 21  SER   C CA    
4220 C  C     . SER   D 22  ? 0.18901 0.19601 0.21931 0.02489  -0.03828 0.01063  21  SER   C C     
4221 O  O     . SER   D 22  ? 0.19419 0.22292 0.19872 0.00780  -0.05541 -0.00115 21  SER   C O     
4222 C  CB    . SER   D 22  ? 0.24315 0.24597 0.26028 -0.02643 -0.09160 -0.01869 21  SER   C CB    
4223 O  OG    . SER   D 22  ? 0.31923 0.23994 0.28456 -0.04604 -0.06869 -0.00847 21  SER   C OG    
4224 N  N     . PHE   D 23  ? 0.19819 0.19091 0.19258 -0.00974 -0.04426 0.02147  22  PHE   C N     
4225 C  CA    . PHE   D 23  ? 0.20304 0.17416 0.19976 -0.02488 -0.06629 0.00581  22  PHE   C CA    
4226 C  C     . PHE   D 23  ? 0.17535 0.19615 0.21981 -0.00523 -0.00499 0.00366  22  PHE   C C     
4227 O  O     . PHE   D 23  ? 0.20983 0.22433 0.23543 0.01042  -0.02134 0.04502  22  PHE   C O     
4228 C  CB    . PHE   D 23  ? 0.20747 0.15798 0.18756 -0.00918 -0.02907 0.02080  22  PHE   C CB    
4229 C  CG    . PHE   D 23  ? 0.18711 0.15727 0.19886 -0.00940 -0.02534 0.01377  22  PHE   C CG    
4230 C  CD1   . PHE   D 23  ? 0.20762 0.17446 0.20046 0.01504  0.01353  0.04382  22  PHE   C CD1   
4231 C  CD2   . PHE   D 23  ? 0.20080 0.19554 0.19511 -0.01106 -0.00012 -0.00652 22  PHE   C CD2   
4232 C  CE1   . PHE   D 23  ? 0.21703 0.22654 0.22082 -0.01681 0.00106  0.04094  22  PHE   C CE1   
4233 C  CE2   . PHE   D 23  ? 0.19012 0.21670 0.20566 -0.03025 -0.04622 -0.00933 22  PHE   C CE2   
4234 C  CZ    . PHE   D 23  ? 0.20359 0.21832 0.19917 -0.02287 -0.03434 0.00013  22  PHE   C CZ    
4235 N  N     . GLU   D 24  ? 0.20190 0.16760 0.18290 -0.00037 -0.04113 0.02472  23  GLU   C N     
4236 C  CA    . GLU   D 24  ? 0.18849 0.13515 0.18483 -0.01159 -0.01124 0.01011  23  GLU   C CA    
4237 C  C     . GLU   D 24  ? 0.16773 0.14059 0.18445 -0.02323 -0.00569 0.00141  23  GLU   C C     
4238 O  O     . GLU   D 24  ? 0.17933 0.17680 0.21710 -0.03077 -0.00034 0.00359  23  GLU   C O     
4239 C  CB    . GLU   D 24  ? 0.21783 0.17102 0.20285 -0.00491 -0.04599 0.00295  23  GLU   C CB    
4240 C  CG    . GLU   D 24  ? 0.29245 0.16756 0.18311 -0.01047 -0.07433 0.01071  23  GLU   C CG    
4241 C  CD    . GLU   D 24  ? 0.37324 0.22178 0.17494 0.03766  -0.03192 0.00856  23  GLU   C CD    
4242 O  OE1   . GLU   D 24  ? 0.51291 0.21793 0.25855 0.11505  -0.02089 0.01625  23  GLU   C OE1   
4243 O  OE2   . GLU   D 24  ? 0.37803 0.26171 0.21297 0.04292  -0.05975 0.03000  23  GLU   C OE2   
4244 N  N     . LEU   D 25  ? 0.16515 0.15273 0.17462 -0.02040 -0.03269 -0.01008 24  LEU   C N     
4245 C  CA    . LEU   D 25  ? 0.16810 0.16238 0.18690 -0.00689 -0.01626 0.00529  24  LEU   C CA    
4246 C  C     . LEU   D 25  ? 0.17681 0.17720 0.20874 -0.02291 -0.02486 0.04785  24  LEU   C C     
4247 O  O     . LEU   D 25  ? 0.18573 0.18439 0.21167 -0.03380 -0.00820 0.04434  24  LEU   C O     
4248 C  CB    . LEU   D 25  ? 0.18868 0.15259 0.18217 0.01492  0.00940  0.00583  24  LEU   C CB    
4249 C  CG    . LEU   D 25  ? 0.17370 0.16516 0.16659 0.00485  0.00026  0.03400  24  LEU   C CG    
4250 C  CD1   . LEU   D 25  ? 0.19690 0.19217 0.19691 0.00650  0.01466  0.00974  24  LEU   C CD1   
4251 C  CD2   . LEU   D 25  ? 0.17205 0.17385 0.16959 -0.03634 -0.00693 0.03094  24  LEU   C CD2   
4252 N  N     . PHE   D 26  ? 0.19087 0.18558 0.18464 -0.00010 -0.05743 0.04891  25  PHE   C N     
4253 C  CA    . PHE   D 26  ? 0.20695 0.18203 0.18921 -0.02688 -0.06421 0.03541  25  PHE   C CA    
4254 C  C     . PHE   D 26  ? 0.22708 0.14948 0.20599 -0.05687 -0.01996 0.04981  25  PHE   C C     
4255 O  O     . PHE   D 26  ? 0.22637 0.16403 0.23927 -0.05668 -0.04266 0.04370  25  PHE   C O     
4256 C  CB    . PHE   D 26  ? 0.16881 0.19534 0.24020 -0.02322 -0.05150 0.02091  25  PHE   C CB    
4257 C  CG    . PHE   D 26  ? 0.25174 0.21730 0.25290 -0.00647 -0.00774 0.03356  25  PHE   C CG    
4258 C  CD1   . PHE   D 26  ? 0.23926 0.26352 0.24288 0.00785  0.02902  -0.03461 25  PHE   C CD1   
4259 C  CD2   . PHE   D 26  ? 0.27037 0.21620 0.28870 0.08020  -0.01562 0.06742  25  PHE   C CD2   
4260 C  CE1   . PHE   D 26  ? 0.27434 0.30027 0.24717 0.04379  0.03677  0.01143  25  PHE   C CE1   
4261 C  CE2   . PHE   D 26  ? 0.33909 0.24624 0.28905 0.07527  0.05007  0.07025  25  PHE   C CE2   
4262 C  CZ    . PHE   D 26  ? 0.35503 0.28112 0.24341 0.10143  0.00994  0.02395  25  PHE   C CZ    
4263 N  N     . ALA   D 27  ? 0.23728 0.16182 0.18672 -0.04372 0.02381  0.00503  26  ALA   C N     
4264 C  CA    . ALA   D 27  ? 0.17733 0.19455 0.21129 0.04763  0.00270  0.00320  26  ALA   C CA    
4265 C  C     . ALA   D 27  ? 0.23805 0.16424 0.19748 -0.01458 -0.01193 0.02731  26  ALA   C C     
4266 O  O     . ALA   D 27  ? 0.25622 0.19403 0.21825 0.02422  -0.02553 0.00720  26  ALA   C O     
4267 C  CB    . ALA   D 27  ? 0.21492 0.24444 0.23819 0.02422  0.00842  -0.00339 26  ALA   C CB    
4268 N  N     . ASP   D 28  ? 0.21781 0.16108 0.19246 0.01042  -0.02817 0.04078  27  ASP   C N     
4269 C  CA    . ASP   D 28  ? 0.22972 0.19733 0.19986 -0.02197 -0.04112 -0.00776 27  ASP   C CA    
4270 C  C     . ASP   D 28  ? 0.24033 0.20060 0.21227 -0.04976 -0.02399 0.04003  27  ASP   C C     
4271 O  O     . ASP   D 28  ? 0.32558 0.29504 0.22379 -0.07136 -0.09288 0.06424  27  ASP   C O     
4272 C  CB    . ASP   D 28  ? 0.23657 0.20186 0.20191 0.00170  -0.01509 -0.00414 27  ASP   C CB    
4273 C  CG    . ASP   D 28  ? 0.25939 0.22060 0.26043 -0.02683 -0.02643 -0.01897 27  ASP   C CG    
4274 O  OD1   . ASP   D 28  ? 0.32855 0.21906 0.25455 -0.00196 0.00936  0.02717  27  ASP   C OD1   
4275 O  OD2   . ASP   D 28  ? 0.31369 0.26798 0.28562 -0.03850 0.02114  -0.02508 27  ASP   C OD2   
4276 N  N     . LYS   D 29  ? 0.23848 0.16964 0.23768 -0.05122 -0.02302 0.03066  28  LYS   C N     
4277 C  CA    . LYS   D 29  ? 0.19926 0.17769 0.25852 -0.02312 -0.02321 0.01015  28  LYS   C CA    
4278 C  C     . LYS   D 29  ? 0.21484 0.16521 0.18471 -0.01776 -0.03956 0.03266  28  LYS   C C     
4279 O  O     . LYS   D 29  ? 0.20636 0.18045 0.19505 -0.04421 -0.04848 0.04619  28  LYS   C O     
4280 C  CB    . LYS   D 29  ? 0.23866 0.22436 0.41151 -0.03057 0.00761  -0.05132 28  LYS   C CB    
4281 C  CG    . LYS   D 29  ? 0.31494 0.22672 0.53433 -0.04312 0.04764  -0.07056 28  LYS   C CG    
4282 C  CD    . LYS   D 29  ? 0.39796 0.26846 0.67799 -0.06244 0.06166  -0.03689 28  LYS   C CD    
4283 C  CE    . LYS   D 29  ? 0.42553 0.28297 0.74074 -0.05459 0.08386  -0.05358 28  LYS   C CE    
4284 N  NZ    . LYS   D 29  ? 0.45034 0.30547 0.77499 -0.04221 0.08131  -0.06952 28  LYS   C NZ    
4285 N  N     . VAL   D 30  ? 0.19299 0.17106 0.17895 -0.02270 0.00701  0.02780  29  VAL   C N     
4286 C  CA    . VAL   D 30  ? 0.14478 0.16907 0.23141 -0.04210 -0.00603 0.05418  29  VAL   C CA    
4287 C  C     . VAL   D 30  ? 0.16462 0.14794 0.19520 -0.00804 -0.00084 0.02503  29  VAL   C C     
4288 O  O     . VAL   D 30  ? 0.19036 0.15412 0.20152 -0.00680 -0.02587 0.02376  29  VAL   C O     
4289 C  CB    . VAL   D 30  ? 0.14132 0.22689 0.33120 0.02081  0.06009  0.08205  29  VAL   C CB    
4290 C  CG1   . VAL   D 30  ? 0.29725 0.28522 0.31101 -0.06890 0.07252  0.03740  29  VAL   C CG1   
4291 C  CG2   . VAL   D 30  ? 0.25033 0.30214 0.35101 -0.05185 0.04303  0.03656  29  VAL   C CG2   
4292 N  N     . PRO   D 31  ? 0.23427 0.13876 0.18592 -0.01079 0.02283  0.02409  30  PRO   C N     
4293 C  CA    . PRO   D 31  ? 0.21100 0.13443 0.17301 -0.01346 0.03866  0.03405  30  PRO   C CA    
4294 C  C     . PRO   D 31  ? 0.23907 0.14331 0.14024 -0.01589 0.00823  0.01119  30  PRO   C C     
4295 O  O     . PRO   D 31  ? 0.21973 0.18375 0.19363 0.00594  -0.02232 0.00282  30  PRO   C O     
4296 C  CB    . PRO   D 31  ? 0.22256 0.19280 0.17794 -0.01772 0.00078  0.04223  30  PRO   C CB    
4297 C  CG    . PRO   D 31  ? 0.25034 0.18978 0.18643 0.02225  0.01592  0.04297  30  PRO   C CG    
4298 C  CD    . PRO   D 31  ? 0.27841 0.16845 0.16688 0.01095  0.04127  0.04462  30  PRO   C CD    
4299 N  N     . LYS   D 32  ? 0.21766 0.15158 0.15108 -0.03299 -0.01202 0.02074  31  LYS   C N     
4300 C  CA    . LYS   D 32  ? 0.22621 0.17297 0.14891 -0.02237 -0.03214 0.04232  31  LYS   C CA    
4301 C  C     . LYS   D 32  ? 0.20634 0.16540 0.17529 0.01316  -0.03767 0.05430  31  LYS   C C     
4302 O  O     . LYS   D 32  ? 0.20762 0.15550 0.15825 0.00997  -0.01684 0.01378  31  LYS   C O     
4303 C  CB    . LYS   D 32  ? 0.23200 0.21850 0.13854 0.00091  -0.02646 0.03560  31  LYS   C CB    
4304 C  CG    . LYS   D 32  ? 0.37699 0.26543 0.20783 0.01673  -0.04127 0.02260  31  LYS   C CG    
4305 C  CD    . LYS   D 32  ? 0.49169 0.34510 0.18875 -0.01311 -0.05975 0.00016  31  LYS   C CD    
4306 C  CE    . LYS   D 32  ? 0.57120 0.39111 0.22147 -0.07346 -0.05596 -0.01897 31  LYS   C CE    
4307 N  NZ    . LYS   D 32  ? 0.59646 0.40509 0.26984 -0.11053 -0.05931 -0.04667 31  LYS   C NZ    
4308 N  N     . THR   D 33  ? 0.19729 0.16693 0.13587 -0.00923 0.00384  0.01270  32  THR   C N     
4309 C  CA    . THR   D 33  ? 0.16758 0.17850 0.14552 -0.01739 -0.00765 0.00665  32  THR   C CA    
4310 C  C     . THR   D 33  ? 0.14563 0.16198 0.18835 -0.00605 -0.00489 0.01225  32  THR   C C     
4311 O  O     . THR   D 33  ? 0.16241 0.15542 0.17645 0.00778  -0.00047 0.01024  32  THR   C O     
4312 C  CB    . THR   D 33  ? 0.13789 0.18098 0.13873 -0.00989 -0.01079 -0.01244 32  THR   C CB    
4313 O  OG1   . THR   D 33  ? 0.16229 0.17509 0.17178 -0.00026 -0.01252 -0.00390 32  THR   C OG1   
4314 C  CG2   . THR   D 33  ? 0.20113 0.18648 0.15676 -0.01259 0.01072  0.02815  32  THR   C CG2   
4315 N  N     . ALA   D 34  ? 0.16909 0.18248 0.16513 -0.01588 0.01808  0.00803  33  ALA   C N     
4316 C  CA    . ALA   D 34  ? 0.16148 0.17139 0.18831 -0.00504 0.01562  0.02093  33  ALA   C CA    
4317 C  C     . ALA   D 34  ? 0.12319 0.17129 0.21273 0.01746  0.02766  0.03153  33  ALA   C C     
4318 O  O     . ALA   D 34  ? 0.15249 0.18765 0.21305 0.01189  -0.01768 0.03669  33  ALA   C O     
4319 C  CB    . ALA   D 34  ? 0.19837 0.13879 0.19787 0.00336  -0.00526 0.03297  33  ALA   C CB    
4320 N  N     . GLU   D 35  ? 0.18154 0.16128 0.17324 -0.00472 0.05931  -0.00018 34  GLU   C N     
4321 C  CA    . GLU   D 35  ? 0.19350 0.18698 0.17677 0.00288  -0.00696 0.01738  34  GLU   C CA    
4322 C  C     . GLU   D 35  ? 0.18188 0.19011 0.17798 -0.02290 0.02213  0.02133  34  GLU   C C     
4323 O  O     . GLU   D 35  ? 0.17853 0.20468 0.22477 -0.00403 0.02393  -0.00401 34  GLU   C O     
4324 C  CB    . GLU   D 35  ? 0.21939 0.22678 0.17744 0.01358  0.02656  0.03585  34  GLU   C CB    
4325 C  CG    . GLU   D 35  ? 0.17998 0.27808 0.21854 0.01348  0.05329  0.02146  34  GLU   C CG    
4326 C  CD    . GLU   D 35  ? 0.21032 0.26495 0.22739 0.00413  0.05858  0.01765  34  GLU   C CD    
4327 O  OE1   . GLU   D 35  ? 0.20846 0.25536 0.23500 -0.00759 0.04891  0.02271  34  GLU   C OE1   
4328 O  OE2   . GLU   D 35  ? 0.21273 0.30172 0.29354 0.01730  0.02012  0.00071  34  GLU   C OE2   
4329 N  N     . ASN   D 36  ? 0.18970 0.17814 0.18628 0.00366  0.05092  0.03140  35  ASN   C N     
4330 C  CA    . ASN   D 36  ? 0.14036 0.17074 0.17868 -0.01232 -0.01655 0.02724  35  ASN   C CA    
4331 C  C     . ASN   D 36  ? 0.14120 0.17302 0.21325 0.01218  0.00112  0.01367  35  ASN   C C     
4332 O  O     . ASN   D 36  ? 0.14591 0.17588 0.19958 0.00279  -0.00627 -0.00114 35  ASN   C O     
4333 C  CB    . ASN   D 36  ? 0.18356 0.16957 0.18179 -0.00719 -0.01326 0.00042  35  ASN   C CB    
4334 C  CG    . ASN   D 36  ? 0.18595 0.17973 0.14224 -0.01103 0.00820  0.00047  35  ASN   C CG    
4335 O  OD1   . ASN   D 36  ? 0.21771 0.19310 0.17166 -0.01557 0.03978  -0.00685 35  ASN   C OD1   
4336 N  ND2   . ASN   D 36  ? 0.20532 0.17557 0.15699 -0.00362 0.01656  -0.00313 35  ASN   C ND2   
4337 N  N     . PHE   D 37  ? 0.16247 0.16109 0.18591 -0.00623 0.00889  0.01458  36  PHE   C N     
4338 C  CA    . PHE   D 37  ? 0.15274 0.17858 0.17056 -0.02492 0.00721  -0.00073 36  PHE   C CA    
4339 C  C     . PHE   D 37  ? 0.15296 0.16667 0.17024 0.00998  0.02318  -0.02281 36  PHE   C C     
4340 O  O     . PHE   D 37  ? 0.13567 0.20153 0.19822 0.00050  -0.01588 0.01767  36  PHE   C O     
4341 C  CB    . PHE   D 37  ? 0.16586 0.17635 0.17688 -0.00159 0.01305  -0.00853 36  PHE   C CB    
4342 C  CG    . PHE   D 37  ? 0.14934 0.17277 0.16208 0.02127  -0.01068 0.00193  36  PHE   C CG    
4343 C  CD1   . PHE   D 37  ? 0.14324 0.18275 0.17652 0.02120  0.04155  0.00543  36  PHE   C CD1   
4344 C  CD2   . PHE   D 37  ? 0.13270 0.20658 0.18684 0.00332  0.02568  -0.00779 36  PHE   C CD2   
4345 C  CE1   . PHE   D 37  ? 0.17097 0.18773 0.20216 0.02873  0.02855  0.01339  36  PHE   C CE1   
4346 C  CE2   . PHE   D 37  ? 0.18324 0.21852 0.18940 0.01273  0.01504  -0.00514 36  PHE   C CE2   
4347 C  CZ    . PHE   D 37  ? 0.16779 0.21387 0.17902 0.03552  0.01386  0.01495  36  PHE   C CZ    
4348 N  N     . ARG   D 38  ? 0.13752 0.17819 0.20319 -0.01525 0.01512  0.00783  37  ARG   C N     
4349 C  CA    . ARG   D 38  ? 0.12951 0.18487 0.19613 -0.02074 0.01235  0.02009  37  ARG   C CA    
4350 C  C     . ARG   D 38  ? 0.14050 0.14070 0.22883 0.00163  -0.02374 0.01148  37  ARG   C C     
4351 O  O     . ARG   D 38  ? 0.15523 0.18650 0.22523 0.00292  -0.01375 0.01794  37  ARG   C O     
4352 C  CB    . ARG   D 38  ? 0.16661 0.18912 0.21598 -0.00919 0.00599  0.00727  37  ARG   C CB    
4353 C  CG    . ARG   D 38  ? 0.16726 0.20181 0.26451 -0.03606 -0.01173 0.03582  37  ARG   C CG    
4354 C  CD    . ARG   D 38  ? 0.19884 0.20083 0.30314 -0.01913 0.05607  0.01222  37  ARG   C CD    
4355 N  NE    . ARG   D 38  ? 0.19317 0.20545 0.27551 -0.01506 0.03464  0.02382  37  ARG   C NE    
4356 C  CZ    . ARG   D 38  ? 0.20664 0.22579 0.24746 0.01225  0.00956  0.00951  37  ARG   C CZ    
4357 N  NH1   . ARG   D 38  ? 0.17041 0.25311 0.28990 -0.03852 0.03864  0.02149  37  ARG   C NH1   
4358 N  NH2   . ARG   D 38  ? 0.23019 0.23307 0.27281 0.02428  0.07392  0.02309  37  ARG   C NH2   
4359 N  N     . ALA   D 39  ? 0.17262 0.15181 0.19371 0.00463  0.01191  0.00910  38  ALA   C N     
4360 C  CA    . ALA   D 39  ? 0.18850 0.20417 0.17228 0.03039  0.00779  0.01021  38  ALA   C CA    
4361 C  C     . ALA   D 39  ? 0.17035 0.18151 0.19004 0.01307  0.02903  -0.01663 38  ALA   C C     
4362 O  O     . ALA   D 39  ? 0.17087 0.20910 0.23648 0.01040  0.01991  0.02950  38  ALA   C O     
4363 C  CB    . ALA   D 39  ? 0.18553 0.20557 0.17244 0.02401  -0.00465 -0.00347 38  ALA   C CB    
4364 N  N     . LEU   D 40  ? 0.14952 0.17592 0.19275 0.00481  0.02788  0.01397  39  LEU   C N     
4365 C  CA    . LEU   D 40  ? 0.14805 0.18923 0.18281 0.00440  0.01111  0.00673  39  LEU   C CA    
4366 C  C     . LEU   D 40  ? 0.16208 0.17174 0.19373 0.01625  0.01621  0.00673  39  LEU   C C     
4367 O  O     . LEU   D 40  ? 0.17405 0.17394 0.21064 -0.00036 -0.02521 0.02411  39  LEU   C O     
4368 C  CB    . LEU   D 40  ? 0.15424 0.18545 0.19388 -0.00807 0.03494  -0.00970 39  LEU   C CB    
4369 C  CG    . LEU   D 40  ? 0.17047 0.16864 0.21384 -0.00329 0.02142  -0.00229 39  LEU   C CG    
4370 C  CD1   . LEU   D 40  ? 0.21953 0.17692 0.19936 -0.00540 0.05597  0.00566  39  LEU   C CD1   
4371 C  CD2   . LEU   D 40  ? 0.22669 0.17612 0.22206 -0.00039 0.02973  0.00988  39  LEU   C CD2   
4372 N  N     . SER   D 41  ? 0.14427 0.18985 0.19655 -0.00324 0.02918  0.01161  40  SER   C N     
4373 C  CA    . SER   D 41  ? 0.12789 0.21854 0.21487 -0.01815 -0.01071 -0.01414 40  SER   C CA    
4374 C  C     . SER   D 41  ? 0.17410 0.24680 0.22559 -0.03572 -0.02023 -0.00664 40  SER   C C     
4375 O  O     . SER   D 41  ? 0.13377 0.30125 0.20827 -0.02403 -0.00160 0.00788  40  SER   C O     
4376 C  CB    . SER   D 41  ? 0.15391 0.21848 0.22381 -0.01248 -0.00119 0.02829  40  SER   C CB    
4377 O  OG    . SER   D 41  ? 0.14923 0.23532 0.22002 0.01960  -0.01076 0.01478  40  SER   C OG    
4378 N  N     . THR   D 42  ? 0.14869 0.22553 0.23113 -0.01960 0.01463  0.01216  41  THR   C N     
4379 C  CA    . THR   D 42  ? 0.13813 0.25437 0.26869 0.00552  -0.00083 0.02982  41  THR   C CA    
4380 C  C     . THR   D 42  ? 0.14485 0.26448 0.29471 -0.00662 0.01748  0.01039  41  THR   C C     
4381 O  O     . THR   D 42  ? 0.16565 0.30045 0.30541 0.00402  -0.00206 0.03818  41  THR   C O     
4382 C  CB    . THR   D 42  ? 0.19394 0.26109 0.24272 0.00178  0.01942  0.03025  41  THR   C CB    
4383 O  OG1   . THR   D 42  ? 0.18252 0.28855 0.23027 0.01690  0.00560  0.02109  41  THR   C OG1   
4384 C  CG2   . THR   D 42  ? 0.17272 0.26489 0.28838 0.03625  0.04048  0.02094  41  THR   C CG2   
4385 N  N     . GLY   D 43  ? 0.17797 0.26452 0.25859 0.00219  0.04220  -0.01627 42  GLY   C N     
4386 C  CA    . GLY   D 43  ? 0.21015 0.25452 0.22815 0.02440  -0.00591 0.00460  42  GLY   C CA    
4387 C  C     . GLY   D 43  ? 0.17972 0.26425 0.23395 0.03351  0.01554  -0.00103 42  GLY   C C     
4388 O  O     . GLY   D 43  ? 0.17941 0.28380 0.27325 0.04580  0.00711  -0.00530 42  GLY   C O     
4389 N  N     . GLU   D 44  ? 0.20040 0.26033 0.21195 0.03517  0.03577  -0.02352 43  GLU   C N     
4390 C  CA    . GLU   D 44  ? 0.21414 0.26344 0.26613 0.01376  0.04776  0.00147  43  GLU   C CA    
4391 C  C     . GLU   D 44  ? 0.26012 0.26974 0.27526 0.02198  0.07697  0.00841  43  GLU   C C     
4392 O  O     . GLU   D 44  ? 0.27266 0.30035 0.31217 0.01805  0.11153  0.00605  43  GLU   C O     
4393 C  CB    . GLU   D 44  ? 0.22095 0.27055 0.27068 0.04308  0.03330  -0.01132 43  GLU   C CB    
4394 C  CG    . GLU   D 44  ? 0.23767 0.29329 0.29774 0.04121  0.02954  -0.00334 43  GLU   C CG    
4395 C  CD    . GLU   D 44  ? 0.27686 0.32805 0.27326 0.03994  0.06159  0.01069  43  GLU   C CD    
4396 O  OE1   . GLU   D 44  ? 0.27884 0.33314 0.24842 0.01606  0.06292  0.02698  43  GLU   C OE1   
4397 O  OE2   . GLU   D 44  ? 0.29653 0.35381 0.29609 0.04405  0.09274  0.02584  43  GLU   C OE2   
4398 N  N     . LYS   D 45  ? 0.24514 0.27842 0.25864 0.02471  0.05029  0.01041  44  LYS   C N     
4399 C  CA    . LYS   D 45  ? 0.26158 0.28386 0.27130 0.05464  0.07354  -0.00333 44  LYS   C CA    
4400 C  C     . LYS   D 45  ? 0.22551 0.29421 0.31632 0.06366  0.08946  -0.00718 44  LYS   C C     
4401 O  O     . LYS   D 45  ? 0.34274 0.30395 0.36371 0.07810  0.12991  -0.02827 44  LYS   C O     
4402 C  CB    . LYS   D 45  ? 0.26593 0.29227 0.27620 0.03434  0.07351  0.00532  44  LYS   C CB    
4403 C  CG    . LYS   D 45  ? 0.26111 0.31382 0.27773 0.02978  0.05027  0.02243  44  LYS   C CG    
4404 C  CD    . LYS   D 45  ? 0.28442 0.35770 0.30056 0.01601  0.04664  0.03586  44  LYS   C CD    
4405 C  CE    . LYS   D 45  ? 0.35856 0.38141 0.31071 0.01503  0.03597  0.08372  44  LYS   C CE    
4406 N  NZ    . LYS   D 45  ? 0.41677 0.40140 0.31453 0.01705  -0.00992 0.09453  44  LYS   C NZ    
4407 N  N     . GLY   D 46  ? 0.23162 0.28994 0.31509 0.07025  0.09933  0.01069  45  GLY   C N     
4408 C  CA    . GLY   D 46  ? 0.22561 0.26197 0.32044 0.10296  0.08899  0.03210  45  GLY   C CA    
4409 C  C     . GLY   D 46  ? 0.25699 0.26999 0.29523 0.08369  0.06556  0.02730  45  GLY   C C     
4410 O  O     . GLY   D 46  ? 0.24025 0.28766 0.34007 0.09350  0.07534  0.03805  45  GLY   C O     
4411 N  N     . PHE   D 47  ? 0.24776 0.26500 0.27628 0.05561  0.05258  0.01840  46  PHE   C N     
4412 C  CA    . PHE   D 47  ? 0.25215 0.25290 0.22857 0.03922  0.00162  -0.02974 46  PHE   C CA    
4413 C  C     . PHE   D 47  ? 0.21038 0.23545 0.21751 0.02587  0.01962  -0.01869 46  PHE   C C     
4414 O  O     . PHE   D 47  ? 0.19111 0.23714 0.23498 0.01961  0.02690  -0.00628 46  PHE   C O     
4415 C  CB    . PHE   D 47  ? 0.22180 0.22307 0.23952 0.04829  -0.02202 -0.03396 46  PHE   C CB    
4416 C  CG    . PHE   D 47  ? 0.21814 0.22925 0.23689 0.05940  0.01044  -0.03554 46  PHE   C CG    
4417 C  CD1   . PHE   D 47  ? 0.28232 0.24343 0.24143 0.05079  -0.01484 -0.02476 46  PHE   C CD1   
4418 C  CD2   . PHE   D 47  ? 0.29508 0.25390 0.23314 0.03645  0.06480  -0.01986 46  PHE   C CD2   
4419 C  CE1   . PHE   D 47  ? 0.29718 0.25463 0.23463 0.06653  -0.00556 -0.03045 46  PHE   C CE1   
4420 C  CE2   . PHE   D 47  ? 0.29427 0.26263 0.24636 0.03708  0.02657  -0.04150 46  PHE   C CE2   
4421 C  CZ    . PHE   D 47  ? 0.31930 0.26467 0.23656 0.05268  0.00220  -0.04356 46  PHE   C CZ    
4422 N  N     . GLY   D 48  ? 0.19722 0.21789 0.17484 0.00504  0.02324  -0.01206 47  GLY   C N     
4423 C  CA    . GLY   D 48  ? 0.20150 0.21672 0.15748 0.03916  0.01427  0.00059  47  GLY   C CA    
4424 C  C     . GLY   D 48  ? 0.15534 0.18765 0.21738 0.04726  -0.00302 -0.00746 47  GLY   C C     
4425 O  O     . GLY   D 48  ? 0.15474 0.19926 0.24852 0.01972  -0.01993 0.00750  47  GLY   C O     
4426 N  N     . TYR   D 49  ? 0.14129 0.20635 0.22719 0.03349  0.01627  0.01929  48  TYR   C N     
4427 C  CA    . TYR   D 49  ? 0.14935 0.20925 0.17510 0.03234  -0.00484 0.00620  48  TYR   C CA    
4428 C  C     . TYR   D 49  ? 0.15259 0.19182 0.21553 0.00807  -0.01842 0.02758  48  TYR   C C     
4429 O  O     . TYR   D 49  ? 0.14709 0.21275 0.19609 0.01729  -0.01619 0.03467  48  TYR   C O     
4430 C  CB    . TYR   D 49  ? 0.12940 0.19482 0.22247 0.02479  -0.03181 -0.01115 48  TYR   C CB    
4431 C  CG    . TYR   D 49  ? 0.13175 0.18745 0.19106 -0.01561 0.00898  -0.01290 48  TYR   C CG    
4432 C  CD1   . TYR   D 49  ? 0.16283 0.18422 0.17779 0.00262  0.00383  0.00469  48  TYR   C CD1   
4433 C  CD2   . TYR   D 49  ? 0.13320 0.19422 0.18246 -0.00813 0.00914  -0.00957 48  TYR   C CD2   
4434 C  CE1   . TYR   D 49  ? 0.15191 0.19697 0.16590 -0.00505 0.00328  0.00057  48  TYR   C CE1   
4435 C  CE2   . TYR   D 49  ? 0.12405 0.19666 0.17120 -0.00674 -0.00992 -0.00464 48  TYR   C CE2   
4436 C  CZ    . TYR   D 49  ? 0.15716 0.18603 0.14551 -0.00351 -0.01706 -0.00061 48  TYR   C CZ    
4437 O  OH    . TYR   D 49  ? 0.14199 0.17312 0.18950 -0.00075 0.00061  -0.00149 48  TYR   C OH    
4438 N  N     . LYS   D 50  ? 0.16503 0.18228 0.18001 0.01561  -0.01966 0.01025  49  LYS   C N     
4439 C  CA    . LYS   D 50  ? 0.13954 0.20995 0.22198 -0.00282 -0.01653 0.02286  49  LYS   C CA    
4440 C  C     . LYS   D 50  ? 0.13827 0.19476 0.21302 0.03492  -0.00166 0.03045  49  LYS   C C     
4441 O  O     . LYS   D 50  ? 0.18901 0.23444 0.20368 0.05919  -0.00701 0.02043  49  LYS   C O     
4442 C  CB    . LYS   D 50  ? 0.14828 0.24326 0.27109 0.00337  -0.00977 0.01547  49  LYS   C CB    
4443 C  CG    . LYS   D 50  ? 0.13796 0.31371 0.32395 -0.04809 -0.04524 0.01147  49  LYS   C CG    
4444 C  CD    . LYS   D 50  ? 0.21295 0.39163 0.39573 -0.05480 -0.05483 0.02203  49  LYS   C CD    
4445 C  CE    . LYS   D 50  ? 0.37375 0.43954 0.46815 -0.03722 0.05117  -0.00766 49  LYS   C CE    
4446 N  NZ    . LYS   D 50  ? 0.30871 0.47964 0.49570 -0.05567 0.07507  0.01057  49  LYS   C NZ    
4447 N  N     . GLY   D 51  ? 0.16173 0.20897 0.19292 0.01298  -0.02126 0.02454  50  GLY   C N     
4448 C  CA    . GLY   D 51  ? 0.16306 0.22556 0.22424 0.00457  -0.03292 0.02074  50  GLY   C CA    
4449 C  C     . GLY   D 51  ? 0.14206 0.23586 0.19002 0.01561  -0.00735 0.01088  50  GLY   C C     
4450 O  O     . GLY   D 51  ? 0.17450 0.24963 0.22422 0.01513  -0.02872 0.03943  50  GLY   C O     
4451 N  N     . SER   D 52  ? 0.14031 0.22368 0.16935 0.01662  -0.01699 0.00538  51  SER   C N     
4452 C  CA    . SER   D 52  ? 0.14049 0.23992 0.17297 -0.00427 -0.02356 0.00650  51  SER   C CA    
4453 C  C     . SER   D 52  ? 0.17638 0.23187 0.16617 -0.00342 -0.04065 0.00131  51  SER   C C     
4454 O  O     . SER   D 52  ? 0.19457 0.21063 0.19778 -0.01400 -0.04563 -0.00232 51  SER   C O     
4455 C  CB    . SER   D 52  ? 0.18817 0.20178 0.18156 0.00300  -0.03152 0.04275  51  SER   C CB    
4456 O  OG    . SER   D 52  ? 0.17758 0.20883 0.20604 -0.01033 -0.02757 0.03564  51  SER   C OG    
4457 N  N     A CYS   D 53  ? 0.11781 0.24091 0.13609 0.00834  -0.03020 0.00638  52  CYS   C N     
4458 N  N     B CYS   D 53  ? 0.13665 0.27043 0.20702 0.01356  -0.00227 0.00152  52  CYS   C N     
4459 C  CA    A CYS   D 53  ? 0.12297 0.21271 0.13286 0.02629  -0.02997 -0.01987 52  CYS   C CA    
4460 C  CA    B CYS   D 53  ? 0.17291 0.28315 0.24508 0.02225  -0.00854 0.00718  52  CYS   C CA    
4461 C  C     A CYS   D 53  ? 0.12533 0.21027 0.15042 0.00908  -0.03906 -0.04900 52  CYS   C C     
4462 C  C     B CYS   D 53  ? 0.17190 0.25852 0.21133 0.00845  -0.00527 0.02932  52  CYS   C C     
4463 O  O     A CYS   D 53  ? 0.14129 0.20120 0.18155 0.01316  -0.07837 -0.06670 52  CYS   C O     
4464 O  O     B CYS   D 53  ? 0.19779 0.27064 0.23098 0.03033  0.03954  0.10511  52  CYS   C O     
4465 C  CB    A CYS   D 53  ? 0.13802 0.19363 0.14317 0.00585  -0.02027 0.01281  52  CYS   C CB    
4466 C  CB    B CYS   D 53  ? 0.20807 0.31977 0.30683 -0.00787 -0.03044 0.02961  52  CYS   C CB    
4467 S  SG    A CYS   D 53  ? 0.14815 0.18214 0.15567 0.01049  -0.02086 0.02564  52  CYS   C SG    
4468 S  SG    B CYS   D 53  ? 0.25891 0.32624 0.35159 0.03069  -0.02155 0.05112  52  CYS   C SG    
4469 N  N     . PHE   D 54  ? 0.13678 0.21981 0.17208 0.00236  -0.01766 -0.00694 53  PHE   C N     
4470 C  CA    . PHE   D 54  ? 0.15184 0.21049 0.18683 -0.01800 -0.01891 0.02278  53  PHE   C CA    
4471 C  C     . PHE   D 54  ? 0.12819 0.24147 0.15765 -0.01846 -0.02694 0.02014  53  PHE   C C     
4472 O  O     . PHE   D 54  ? 0.17823 0.26593 0.15876 -0.01069 -0.02430 0.02544  53  PHE   C O     
4473 C  CB    . PHE   D 54  ? 0.20814 0.18636 0.16334 -0.00623 -0.05189 0.01594  53  PHE   C CB    
4474 C  CG    . PHE   D 54  ? 0.17745 0.18319 0.17743 0.00863  0.00799  -0.00253 53  PHE   C CG    
4475 C  CD1   . PHE   D 54  ? 0.19577 0.20200 0.20726 -0.00564 -0.00391 -0.01795 53  PHE   C CD1   
4476 C  CD2   . PHE   D 54  ? 0.23353 0.18494 0.15389 0.03740  -0.01235 0.01897  53  PHE   C CD2   
4477 C  CE1   . PHE   D 54  ? 0.21571 0.22367 0.22532 -0.01289 -0.03512 -0.02707 53  PHE   C CE1   
4478 C  CE2   . PHE   D 54  ? 0.17350 0.22080 0.20295 -0.00467 -0.02886 0.01480  53  PHE   C CE2   
4479 C  CZ    . PHE   D 54  ? 0.16333 0.21680 0.22910 -0.01076 -0.04094 -0.02929 53  PHE   C CZ    
4480 N  N     . HIS   D 55  ? 0.17008 0.22040 0.16836 -0.00357 -0.01875 0.02647  54  HIS   C N     
4481 C  CA    . HIS   D 55  ? 0.17570 0.21166 0.19812 -0.01565 -0.01020 0.02773  54  HIS   C CA    
4482 C  C     . HIS   D 55  ? 0.15473 0.24010 0.17956 -0.01612 -0.02058 0.02188  54  HIS   C C     
4483 O  O     . HIS   D 55  ? 0.17965 0.24321 0.22192 -0.02788 -0.00543 0.06114  54  HIS   C O     
4484 C  CB    . HIS   D 55  ? 0.19636 0.21393 0.19173 -0.00341 -0.02837 0.04293  54  HIS   C CB    
4485 C  CG    . HIS   D 55  ? 0.19212 0.23661 0.19418 -0.01158 -0.05443 0.02639  54  HIS   C CG    
4486 N  ND1   . HIS   D 55  ? 0.19546 0.24726 0.18814 0.00181  -0.04017 0.01869  54  HIS   C ND1   
4487 C  CD2   . HIS   D 55  ? 0.23452 0.21812 0.18226 0.02976  -0.04824 -0.00151 54  HIS   C CD2   
4488 C  CE1   . HIS   D 55  ? 0.18672 0.25286 0.20960 0.01982  -0.01200 0.02331  54  HIS   C CE1   
4489 N  NE2   . HIS   D 55  ? 0.21997 0.24681 0.20062 -0.00075 -0.05973 -0.01696 54  HIS   C NE2   
4490 N  N     . ARG   D 56  ? 0.14954 0.24787 0.15258 -0.00226 -0.00687 0.00036  55  ARG   C N     
4491 C  CA    . ARG   D 56  ? 0.12632 0.25813 0.16925 -0.01448 0.00340  0.00461  55  ARG   C CA    
4492 C  C     . ARG   D 56  ? 0.15845 0.25144 0.12851 -0.02113 0.00013  0.01337  55  ARG   C C     
4493 O  O     . ARG   D 56  ? 0.17607 0.23953 0.16555 -0.02356 0.01113  0.04222  55  ARG   C O     
4494 C  CB    . ARG   D 56  ? 0.12146 0.24652 0.17191 -0.03552 -0.02442 0.01109  55  ARG   C CB    
4495 C  CG    . ARG   D 56  ? 0.16584 0.25905 0.17736 -0.02332 -0.02344 0.04702  55  ARG   C CG    
4496 C  CD    . ARG   D 56  ? 0.13614 0.21389 0.20406 -0.03023 -0.04934 0.00629  55  ARG   C CD    
4497 N  NE    . ARG   D 56  ? 0.16228 0.22138 0.25344 -0.01159 -0.05479 0.02148  55  ARG   C NE    
4498 C  CZ    . ARG   D 56  ? 0.19122 0.25229 0.25573 -0.02827 -0.07781 -0.01161 55  ARG   C CZ    
4499 N  NH1   . ARG   D 56  ? 0.19508 0.27707 0.20079 -0.01043 -0.01828 0.04036  55  ARG   C NH1   
4500 N  NH2   . ARG   D 56  ? 0.23716 0.28053 0.34585 -0.00717 -0.10995 -0.02020 55  ARG   C NH2   
4501 N  N     . ILE   D 57  ? 0.13767 0.26567 0.15285 -0.00679 -0.01882 0.01551  56  ILE   C N     
4502 C  CA    . ILE   D 57  ? 0.13457 0.28290 0.19204 -0.01315 0.00178  -0.01180 56  ILE   C CA    
4503 C  C     . ILE   D 57  ? 0.18294 0.29389 0.15391 -0.01445 0.01875  0.00685  56  ILE   C C     
4504 O  O     . ILE   D 57  ? 0.17489 0.30232 0.16764 0.00406  0.01641  0.04517  56  ILE   C O     
4505 C  CB    . ILE   D 57  ? 0.16718 0.27367 0.18902 -0.02496 -0.00134 -0.02033 56  ILE   C CB    
4506 C  CG1   . ILE   D 57  ? 0.11664 0.25835 0.20440 -0.01638 -0.02343 -0.01644 56  ILE   C CG1   
4507 C  CG2   . ILE   D 57  ? 0.19485 0.27658 0.18499 -0.02891 0.00816  -0.03387 56  ILE   C CG2   
4508 C  CD1   . ILE   D 57  ? 0.15849 0.26935 0.19730 -0.03435 0.00254  -0.01218 56  ILE   C CD1   
4509 N  N     . ILE   D 58  ? 0.14842 0.29503 0.18112 0.02828  -0.00372 0.01563  57  ILE   C N     
4510 C  CA    . ILE   D 58  ? 0.15215 0.31331 0.18885 0.01011  0.01613  0.01852  57  ILE   C CA    
4511 C  C     . ILE   D 58  ? 0.18950 0.31987 0.18669 0.01941  0.04159  0.02131  57  ILE   C C     
4512 O  O     . ILE   D 58  ? 0.20184 0.31472 0.19442 0.00715  0.01428  0.01819  57  ILE   C O     
4513 C  CB    . ILE   D 58  ? 0.16917 0.31383 0.18670 -0.02283 0.01482  0.04943  57  ILE   C CB    
4514 C  CG1   . ILE   D 58  ? 0.15427 0.32172 0.18895 -0.02838 -0.02049 0.04558  57  ILE   C CG1   
4515 C  CG2   . ILE   D 58  ? 0.16603 0.33516 0.17539 0.01990  0.02387  0.02093  57  ILE   C CG2   
4516 C  CD1   . ILE   D 58  ? 0.18495 0.31975 0.19250 -0.04874 -0.01271 0.03518  57  ILE   C CD1   
4517 N  N     . PRO   D 59  ? 0.23504 0.33627 0.18950 0.01649  0.02360  0.00038  58  PRO   C N     
4518 C  CA    . PRO   D 59  ? 0.26069 0.34447 0.17705 0.00338  -0.00176 -0.01891 58  PRO   C CA    
4519 C  C     . PRO   D 59  ? 0.27406 0.35163 0.18833 0.01213  -0.01626 -0.01715 58  PRO   C C     
4520 O  O     . PRO   D 59  ? 0.26202 0.35702 0.21607 0.04294  0.03130  -0.00407 58  PRO   C O     
4521 C  CB    . PRO   D 59  ? 0.26508 0.34025 0.19292 0.01545  0.02351  -0.02485 58  PRO   C CB    
4522 C  CG    . PRO   D 59  ? 0.30916 0.34829 0.18844 0.01141  0.02542  -0.00912 58  PRO   C CG    
4523 C  CD    . PRO   D 59  ? 0.29031 0.34804 0.18811 0.00319  0.00536  0.01153  58  PRO   C CD    
4524 N  N     . GLY   D 60  ? 0.29859 0.36880 0.17650 0.06575  0.03879  -0.00475 59  GLY   C N     
4525 C  CA    . GLY   D 60  ? 0.26774 0.37326 0.19835 0.06898  0.01638  -0.00771 59  GLY   C CA    
4526 C  C     . GLY   D 60  ? 0.23327 0.35665 0.19480 0.04120  0.02668  -0.04369 59  GLY   C C     
4527 O  O     . GLY   D 60  ? 0.26471 0.38313 0.25370 0.03298  0.06183  -0.04738 59  GLY   C O     
4528 N  N     . PHE   D 61  ? 0.18303 0.31565 0.17855 -0.00212 0.02264  -0.03119 60  PHE   C N     
4529 C  CA    . PHE   D 61  ? 0.19163 0.26984 0.18594 -0.00369 -0.00058 -0.04617 60  PHE   C CA    
4530 C  C     . PHE   D 61  ? 0.16971 0.26202 0.18489 0.01279  0.04255  -0.01584 60  PHE   C C     
4531 O  O     . PHE   D 61  ? 0.17641 0.24066 0.19778 -0.00886 0.01011  -0.00011 60  PHE   C O     
4532 C  CB    . PHE   D 61  ? 0.15311 0.26349 0.22662 -0.00361 0.04250  -0.01707 60  PHE   C CB    
4533 C  CG    . PHE   D 61  ? 0.16267 0.31827 0.24293 -0.00775 0.03293  -0.01806 60  PHE   C CG    
4534 C  CD1   . PHE   D 61  ? 0.15062 0.33185 0.27265 0.03153  0.03095  -0.00025 60  PHE   C CD1   
4535 C  CD2   . PHE   D 61  ? 0.20802 0.34106 0.24415 -0.01166 0.04139  -0.02124 60  PHE   C CD2   
4536 C  CE1   . PHE   D 61  ? 0.19458 0.36028 0.27072 -0.01836 0.04885  0.00426  60  PHE   C CE1   
4537 C  CE2   . PHE   D 61  ? 0.19801 0.37298 0.29236 -0.00789 0.03700  -0.00234 60  PHE   C CE2   
4538 C  CZ    . PHE   D 61  ? 0.19831 0.37323 0.27966 -0.01986 0.05922  0.01125  60  PHE   C CZ    
4539 N  N     . MET   D 62  ? 0.16158 0.26068 0.18901 0.00920  -0.01731 -0.01910 61  MET   C N     
4540 C  CA    . MET   D 62  ? 0.16523 0.25450 0.18070 0.01756  0.03463  -0.00006 61  MET   C CA    
4541 C  C     . MET   D 62  ? 0.19004 0.21968 0.17578 -0.00822 0.01264  0.02806  61  MET   C C     
4542 O  O     . MET   D 62  ? 0.16829 0.23816 0.18073 0.01225  0.01140  -0.01530 61  MET   C O     
4543 C  CB    . MET   D 62  ? 0.19971 0.22647 0.19384 -0.01574 -0.01330 -0.03645 61  MET   C CB    
4544 C  CG    . MET   D 62  ? 0.17475 0.26964 0.17957 -0.04987 -0.01544 0.00492  61  MET   C CG    
4545 S  SD    . MET   D 62  ? 0.16205 0.28563 0.20060 -0.01147 0.00790  0.00116  61  MET   C SD    
4546 C  CE    . MET   D 62  ? 0.18379 0.23333 0.21980 -0.00137 -0.03620 0.00901  61  MET   C CE    
4547 N  N     . CYS   D 63  ? 0.14724 0.22045 0.15922 -0.01817 0.00402  -0.00327 62  CYS   C N     
4548 C  CA    . CYS   D 63  ? 0.17036 0.24303 0.13122 0.01533  -0.01047 -0.03106 62  CYS   C CA    
4549 C  C     . CYS   D 63  ? 0.16886 0.21473 0.14104 0.01177  -0.00789 0.01666  62  CYS   C C     
4550 O  O     . CYS   D 63  ? 0.20265 0.20050 0.14676 0.00883  -0.01293 0.01213  62  CYS   C O     
4551 C  CB    . CYS   D 63  ? 0.17298 0.27194 0.16052 0.02812  -0.01903 -0.03299 62  CYS   C CB    
4552 S  SG    . CYS   D 63  ? 0.21312 0.28602 0.17133 0.00003  -0.01986 -0.01984 62  CYS   C SG    
4553 N  N     . GLN   D 64  ? 0.14699 0.20378 0.13291 -0.00585 0.00324  0.02147  63  GLN   C N     
4554 C  CA    . GLN   D 64  ? 0.14086 0.19783 0.13074 -0.00030 -0.02086 0.01135  63  GLN   C CA    
4555 C  C     . GLN   D 64  ? 0.15237 0.18633 0.16792 -0.00449 -0.03484 0.05301  63  GLN   C C     
4556 O  O     . GLN   D 64  ? 0.14832 0.18550 0.17125 -0.00629 -0.01506 0.02606  63  GLN   C O     
4557 C  CB    . GLN   D 64  ? 0.16044 0.20790 0.15442 0.00862  -0.02459 0.00842  63  GLN   C CB    
4558 C  CG    . GLN   D 64  ? 0.13839 0.21161 0.13648 -0.00541 -0.01616 0.00234  63  GLN   C CG    
4559 C  CD    . GLN   D 64  ? 0.13940 0.23618 0.15760 -0.00844 -0.00120 0.02140  63  GLN   C CD    
4560 O  OE1   . GLN   D 64  ? 0.14600 0.23977 0.17507 -0.01756 -0.01016 0.00273  63  GLN   C OE1   
4561 N  NE2   . GLN   D 64  ? 0.14993 0.19932 0.15642 -0.01427 -0.00591 0.01118  63  GLN   C NE2   
4562 N  N     . GLY   D 65  ? 0.11971 0.20701 0.16451 -0.00635 -0.01553 0.00442  64  GLY   C N     
4563 C  CA    . GLY   D 65  ? 0.15146 0.19870 0.13303 0.02304  -0.02951 -0.00468 64  GLY   C CA    
4564 C  C     . GLY   D 65  ? 0.11900 0.18347 0.17890 -0.01784 -0.02366 -0.00248 64  GLY   C C     
4565 O  O     . GLY   D 65  ? 0.14593 0.19334 0.17853 0.02273  -0.01085 0.00605  64  GLY   C O     
4566 N  N     . GLY   D 66  ? 0.15059 0.18196 0.19514 0.00881  -0.00447 0.01273  65  GLY   C N     
4567 C  CA    . GLY   D 66  ? 0.18374 0.18123 0.19145 -0.00952 0.03834  0.03865  65  GLY   C CA    
4568 C  C     . GLY   D 66  ? 0.17879 0.18742 0.15497 0.01559  -0.02504 0.01834  65  GLY   C C     
4569 O  O     . GLY   D 66  ? 0.21615 0.19795 0.16490 0.00200  -0.00496 -0.00274 65  GLY   C O     
4570 N  N     . ASP   D 67  ? 0.18574 0.18568 0.16785 0.00526  -0.04297 0.00462  66  ASP   C N     
4571 C  CA    . ASP   D 67  ? 0.19575 0.21525 0.14493 -0.01609 -0.04107 -0.01765 66  ASP   C CA    
4572 C  C     . ASP   D 67  ? 0.18059 0.22734 0.15236 0.00403  -0.03609 -0.01129 66  ASP   C C     
4573 O  O     . ASP   D 67  ? 0.24406 0.25977 0.16078 0.01234  -0.02896 0.01950  66  ASP   C O     
4574 C  CB    . ASP   D 67  ? 0.18954 0.21888 0.16967 -0.04910 -0.00874 0.00489  66  ASP   C CB    
4575 C  CG    . ASP   D 67  ? 0.24943 0.21041 0.17148 0.00335  -0.02347 0.01880  66  ASP   C CG    
4576 O  OD1   . ASP   D 67  ? 0.28223 0.19600 0.17817 -0.00766 -0.03140 -0.00640 66  ASP   C OD1   
4577 O  OD2   . ASP   D 67  ? 0.26610 0.22128 0.17490 -0.03823 -0.03442 0.02409  66  ASP   C OD2   
4578 N  N     . PHE   D 68  ? 0.17173 0.22061 0.18015 -0.01535 -0.04266 -0.00066 67  PHE   C N     
4579 C  CA    . PHE   D 68  ? 0.17252 0.21505 0.18847 -0.01163 -0.02522 -0.00306 67  PHE   C CA    
4580 C  C     . PHE   D 68  ? 0.19287 0.21403 0.18692 0.01629  -0.02576 0.00968  67  PHE   C C     
4581 O  O     . PHE   D 68  ? 0.20002 0.22185 0.25419 0.03349  -0.06114 -0.00704 67  PHE   C O     
4582 C  CB    . PHE   D 68  ? 0.22101 0.23955 0.25682 -0.01374 -0.01036 -0.02068 67  PHE   C CB    
4583 C  CG    . PHE   D 68  ? 0.17973 0.24835 0.22481 0.00203  0.00153  -0.00242 67  PHE   C CG    
4584 C  CD1   . PHE   D 68  ? 0.17219 0.23903 0.19624 -0.01879 0.00170  -0.01654 67  PHE   C CD1   
4585 C  CD2   . PHE   D 68  ? 0.19332 0.26831 0.22927 -0.00418 0.04330  0.02266  67  PHE   C CD2   
4586 C  CE1   . PHE   D 68  ? 0.22377 0.24274 0.23003 0.01007  -0.03359 -0.00382 67  PHE   C CE1   
4587 C  CE2   . PHE   D 68  ? 0.15525 0.26526 0.27028 0.00296  0.01785  0.03183  67  PHE   C CE2   
4588 C  CZ    . PHE   D 68  ? 0.17234 0.25745 0.25686 -0.02750 0.00522  0.01513  67  PHE   C CZ    
4589 N  N     . THR   D 69  ? 0.19453 0.18733 0.21555 -0.00878 -0.04042 0.00859  68  THR   C N     
4590 C  CA    . THR   D 69  ? 0.19969 0.21075 0.19987 0.00444  -0.02944 0.01201  68  THR   C CA    
4591 C  C     . THR   D 69  ? 0.25995 0.22934 0.20006 -0.01891 -0.02301 0.01874  68  THR   C C     
4592 O  O     . THR   D 69  ? 0.30565 0.22255 0.25259 0.05467  0.02415  0.03838  68  THR   C O     
4593 C  CB    . THR   D 69  ? 0.21448 0.23546 0.21149 -0.00951 -0.03347 0.03558  68  THR   C CB    
4594 O  OG1   . THR   D 69  ? 0.22548 0.24576 0.21662 0.03566  -0.02927 0.02750  68  THR   C OG1   
4595 C  CG2   . THR   D 69  ? 0.25921 0.23129 0.20268 -0.00969 -0.02479 0.02044  68  THR   C CG2   
4596 N  N     . ARG   D 70  ? 0.24277 0.22298 0.16776 -0.03582 -0.02120 0.01097  69  ARG   C N     
4597 C  CA    . ARG   D 70  ? 0.22572 0.23150 0.17501 -0.01979 -0.01208 0.01500  69  ARG   C CA    
4598 C  C     . ARG   D 70  ? 0.29890 0.22381 0.19220 -0.00038 -0.07303 0.03162  69  ARG   C C     
4599 O  O     . ARG   D 70  ? 0.33731 0.24657 0.22784 0.00334  -0.09100 0.01929  69  ARG   C O     
4600 C  CB    . ARG   D 70  ? 0.21515 0.26556 0.18224 -0.01843 -0.02609 0.02317  69  ARG   C CB    
4601 C  CG    . ARG   D 70  ? 0.29224 0.28087 0.20325 -0.01466 -0.02869 -0.01872 69  ARG   C CG    
4602 C  CD    . ARG   D 70  ? 0.51655 0.35447 0.31043 0.01227  -0.00799 -0.04033 69  ARG   C CD    
4603 N  NE    . ARG   D 70  ? 0.68448 0.41740 0.40137 0.04549  0.01878  -0.05750 69  ARG   C NE    
4604 C  CZ    . ARG   D 70  ? 0.82680 0.49119 0.47277 0.06895  0.02914  -0.07543 69  ARG   C CZ    
4605 N  NH1   . ARG   D 70  ? 0.85346 0.52146 0.49699 0.08171  0.00962  -0.07710 69  ARG   C NH1   
4606 N  NH2   . ARG   D 70  ? 0.84681 0.51928 0.49050 0.07504  0.05979  -0.07661 69  ARG   C NH2   
4607 N  N     . HIS   D 71  ? 0.25056 0.22558 0.18515 0.02227  -0.04347 0.00511  70  HIS   C N     
4608 C  CA    . HIS   D 71  ? 0.30986 0.27324 0.19485 0.02078  -0.06033 0.02786  70  HIS   C CA    
4609 C  C     . HIS   D 71  ? 0.32341 0.30097 0.22017 0.01272  -0.01208 0.04621  70  HIS   C C     
4610 O  O     . HIS   D 71  ? 0.36880 0.31436 0.17321 0.00899  -0.02653 0.05416  70  HIS   C O     
4611 C  CB    . HIS   D 71  ? 0.25450 0.28682 0.23359 0.02318  -0.10817 0.03644  70  HIS   C CB    
4612 C  CG    . HIS   D 71  ? 0.30516 0.25588 0.18978 0.03284  -0.12731 -0.01498 70  HIS   C CG    
4613 N  ND1   . HIS   D 71  ? 0.30879 0.23795 0.25287 0.02506  -0.09129 0.01631  70  HIS   C ND1   
4614 C  CD2   . HIS   D 71  ? 0.29313 0.27947 0.22946 0.03711  -0.10371 -0.01413 70  HIS   C CD2   
4615 C  CE1   . HIS   D 71  ? 0.36090 0.26360 0.25278 0.03080  -0.06410 -0.00774 70  HIS   C CE1   
4616 N  NE2   . HIS   D 71  ? 0.35096 0.26032 0.26405 0.05129  -0.12084 -0.00734 70  HIS   C NE2   
4617 N  N     . ASN   D 72  ? 0.30249 0.29029 0.23756 0.00972  0.02688  0.04793  71  ASN   C N     
4618 C  CA    . ASN   D 72  ? 0.34147 0.27074 0.27275 0.02017  0.02993  0.04527  71  ASN   C CA    
4619 C  C     . ASN   D 72  ? 0.36442 0.26891 0.25112 -0.00362 0.00357  0.06261  71  ASN   C C     
4620 O  O     . ASN   D 72  ? 0.36133 0.27214 0.22736 -0.02671 -0.03909 0.06820  71  ASN   C O     
4621 C  CB    . ASN   D 72  ? 0.38608 0.27342 0.33036 0.00225  0.04801  0.05608  71  ASN   C CB    
4622 C  CG    . ASN   D 72  ? 0.33873 0.24565 0.30836 -0.04520 0.02186  0.06926  71  ASN   C CG    
4623 O  OD1   . ASN   D 72  ? 0.32047 0.23821 0.27684 -0.02184 0.01159  0.07411  71  ASN   C OD1   
4624 N  ND2   . ASN   D 72  ? 0.43289 0.25375 0.38647 -0.02950 0.03224  0.03154  71  ASN   C ND2   
4625 N  N     . GLY   D 73  ? 0.34254 0.24940 0.19394 -0.00492 -0.00605 0.04133  72  GLY   C N     
4626 C  CA    . GLY   D 73  ? 0.32007 0.23821 0.18629 0.00815  -0.02135 0.01601  72  GLY   C CA    
4627 C  C     . GLY   D 73  ? 0.28767 0.21765 0.18290 -0.01509 0.02922  0.03197  72  GLY   C C     
4628 O  O     . GLY   D 73  ? 0.25431 0.19835 0.19881 -0.02230 0.03586  0.01536  72  GLY   C O     
4629 N  N     . THR   D 74  ? 0.27424 0.21176 0.15779 -0.03289 0.02267  0.01789  73  THR   C N     
4630 C  CA    . THR   D 74  ? 0.22157 0.19058 0.17842 -0.04358 0.02920  -0.01069 73  THR   C CA    
4631 C  C     . THR   D 74  ? 0.22492 0.20525 0.19024 -0.02826 -0.02568 0.01774  73  THR   C C     
4632 O  O     . THR   D 74  ? 0.20141 0.23255 0.21875 -0.02417 -0.03828 -0.00370 73  THR   C O     
4633 C  CB    . THR   D 74  ? 0.19009 0.20236 0.28487 -0.02916 0.01704  0.04789  73  THR   C CB    
4634 O  OG1   . THR   D 74  ? 0.28112 0.18701 0.29730 -0.01158 0.02165  0.03962  73  THR   C OG1   
4635 C  CG2   . THR   D 74  ? 0.27919 0.25553 0.33377 -0.06880 0.05690  0.05319  73  THR   C CG2   
4636 N  N     . GLY   D 75  ? 0.21170 0.18509 0.17017 -0.03927 0.00034  0.02213  74  GLY   C N     
4637 C  CA    . GLY   D 75  ? 0.19345 0.20632 0.19952 0.00165  0.00443  0.03595  74  GLY   C CA    
4638 C  C     . GLY   D 75  ? 0.24628 0.19719 0.20890 0.04182  0.02145  0.02867  74  GLY   C C     
4639 O  O     . GLY   D 75  ? 0.19457 0.18207 0.20260 -0.00266 0.00648  0.02492  74  GLY   C O     
4640 N  N     . GLY   D 76  ? 0.29674 0.17039 0.26970 0.02748  0.06394  0.03900  75  GLY   C N     
4641 C  CA    . GLY   D 76  ? 0.35623 0.16959 0.25147 -0.00717 0.11163  0.01681  75  GLY   C CA    
4642 C  C     . GLY   D 76  ? 0.21583 0.18213 0.24931 -0.00617 0.04593  0.02711  75  GLY   C C     
4643 O  O     . GLY   D 76  ? 0.26260 0.22734 0.31623 -0.04714 0.02155  0.03571  75  GLY   C O     
4644 N  N     . LYS   D 77  ? 0.22418 0.16982 0.20671 -0.01513 0.05014  0.00269  76  LYS   C N     
4645 C  CA    . LYS   D 77  ? 0.27641 0.16955 0.18599 -0.00411 0.06123  0.01673  76  LYS   C CA    
4646 C  C     . LYS   D 77  ? 0.20645 0.14796 0.18814 -0.01418 0.01279  0.00057  76  LYS   C C     
4647 O  O     . LYS   D 77  ? 0.17372 0.17682 0.18201 -0.02399 0.00526  0.00347  76  LYS   C O     
4648 C  CB    . LYS   D 77  ? 0.23439 0.19327 0.31520 0.02267  0.04441  0.02212  76  LYS   C CB    
4649 C  CG    . LYS   D 77  ? 0.22705 0.18314 0.36003 0.04172  -0.07032 -0.00204 76  LYS   C CG    
4650 C  CD    . LYS   D 77  ? 0.26665 0.20797 0.38127 0.04335  -0.08049 -0.04711 76  LYS   C CD    
4651 C  CE    . LYS   D 77  ? 0.32937 0.22085 0.40080 0.11003  -0.09463 -0.06841 76  LYS   C CE    
4652 N  NZ    . LYS   D 77  ? 0.40560 0.26294 0.42093 0.12649  -0.00161 -0.06553 76  LYS   C NZ    
4653 N  N     . SER   D 78  ? 0.19998 0.16616 0.17019 -0.02011 0.02171  0.00497  77  SER   C N     
4654 C  CA    . SER   D 78  ? 0.21344 0.15995 0.17191 -0.00020 0.04144  0.01967  77  SER   C CA    
4655 C  C     . SER   D 78  ? 0.15532 0.19117 0.20130 -0.00459 0.01849  -0.00739 77  SER   C C     
4656 O  O     . SER   D 78  ? 0.21303 0.21229 0.20933 0.03605  0.04140  0.00366  77  SER   C O     
4657 C  CB    . SER   D 78  ? 0.23791 0.17206 0.14660 0.02093  -0.01012 0.00220  77  SER   C CB    
4658 O  OG    . SER   D 78  ? 0.21297 0.20325 0.15823 -0.00297 -0.00194 -0.00107 77  SER   C OG    
4659 N  N     . ILE   D 79  ? 0.16606 0.20058 0.18806 -0.01740 0.02954  0.01975  78  ILE   C N     
4660 C  CA    . ILE   D 79  ? 0.21899 0.20138 0.18949 0.00667  0.03409  0.01307  78  ILE   C CA    
4661 C  C     . ILE   D 79  ? 0.21195 0.19999 0.20668 0.00006  0.04636  -0.01344 78  ILE   C C     
4662 O  O     . ILE   D 79  ? 0.26245 0.24251 0.25733 -0.01915 0.11103  -0.01122 78  ILE   C O     
4663 C  CB    . ILE   D 79  ? 0.21524 0.19496 0.18038 -0.01317 0.02458  0.01792  78  ILE   C CB    
4664 C  CG1   . ILE   D 79  ? 0.19945 0.18809 0.20316 -0.01060 0.02303  0.01744  78  ILE   C CG1   
4665 C  CG2   . ILE   D 79  ? 0.27631 0.20747 0.17901 -0.01592 -0.02138 -0.00280 78  ILE   C CG2   
4666 C  CD1   . ILE   D 79  ? 0.23818 0.20327 0.25810 -0.01440 0.03511  0.00066  78  ILE   C CD1   
4667 N  N     . TYR   D 80  ? 0.19938 0.18902 0.20671 -0.00082 0.01256  -0.00777 79  TYR   C N     
4668 C  CA    . TYR   D 80  ? 0.27847 0.17664 0.21256 0.00099  0.00728  -0.01211 79  TYR   C CA    
4669 C  C     . TYR   D 80  ? 0.35626 0.18564 0.21067 -0.02603 0.01502  -0.02913 79  TYR   C C     
4670 O  O     . TYR   D 80  ? 0.49390 0.21428 0.23838 -0.03342 -0.03608 -0.05378 79  TYR   C O     
4671 C  CB    . TYR   D 80  ? 0.29219 0.18286 0.17558 -0.00747 0.00937  0.00161  79  TYR   C CB    
4672 C  CG    . TYR   D 80  ? 0.25852 0.20267 0.13693 0.00343  0.00284  0.00404  79  TYR   C CG    
4673 C  CD1   . TYR   D 80  ? 0.24732 0.20664 0.18548 0.01878  0.05942  0.02748  79  TYR   C CD1   
4674 C  CD2   . TYR   D 80  ? 0.24224 0.22790 0.14523 0.01784  -0.00430 0.02188  79  TYR   C CD2   
4675 C  CE1   . TYR   D 80  ? 0.25975 0.20247 0.18747 0.03669  0.03351  0.01536  79  TYR   C CE1   
4676 C  CE2   . TYR   D 80  ? 0.23962 0.21313 0.18536 0.00090  0.00708  0.01014  79  TYR   C CE2   
4677 C  CZ    . TYR   D 80  ? 0.22251 0.19764 0.20802 0.00048  0.03872  0.01107  79  TYR   C CZ    
4678 O  OH    . TYR   D 80  ? 0.22625 0.19946 0.20883 -0.00926 0.04077  0.01948  79  TYR   C OH    
4679 N  N     . GLY   D 81  ? 0.26267 0.17481 0.22895 -0.02868 0.06042  0.00573  80  GLY   C N     
4680 C  CA    . GLY   D 81  ? 0.33582 0.19523 0.23060 -0.02138 0.01941  -0.00977 80  GLY   C CA    
4681 C  C     . GLY   D 81  ? 0.26163 0.19496 0.20764 -0.03283 -0.03057 -0.00422 80  GLY   C C     
4682 O  O     . GLY   D 81  ? 0.27291 0.22999 0.20974 -0.03943 -0.03637 -0.02173 80  GLY   C O     
4683 N  N     . GLU   D 82  ? 0.23826 0.16687 0.22532 -0.00742 -0.01329 0.01293  81  GLU   C N     
4684 C  CA    . GLU   D 82  ? 0.24950 0.18357 0.18212 0.00362  -0.00414 0.00718  81  GLU   C CA    
4685 C  C     . GLU   D 82  ? 0.28767 0.20338 0.18353 0.02542  -0.04262 -0.01675 81  GLU   C C     
4686 O  O     . GLU   D 82  ? 0.37708 0.21084 0.17678 0.02443  -0.01956 -0.02870 81  GLU   C O     
4687 C  CB    . GLU   D 82  ? 0.22388 0.19406 0.20214 -0.01454 -0.03602 -0.01950 81  GLU   C CB    
4688 C  CG    . GLU   D 82  ? 0.24494 0.23166 0.25690 0.00245  -0.02279 0.00762  81  GLU   C CG    
4689 C  CD    . GLU   D 82  ? 0.26825 0.25597 0.24292 0.02572  -0.03960 -0.03227 81  GLU   C CD    
4690 O  OE1   . GLU   D 82  ? 0.30291 0.26720 0.27658 0.00562  -0.02652 -0.02563 81  GLU   C OE1   
4691 O  OE2   . GLU   D 82  ? 0.31033 0.27161 0.24172 0.04944  -0.01960 -0.04410 81  GLU   C OE2   
4692 N  N     . LYS   D 83  ? 0.25813 0.17248 0.18374 0.01508  -0.02556 0.01625  82  LYS   C N     
4693 C  CA    . LYS   D 83  ? 0.26692 0.17554 0.25737 0.05136  -0.01742 0.03934  82  LYS   C CA    
4694 C  C     . LYS   D 83  ? 0.27259 0.18542 0.17295 0.05307  -0.00645 0.02522  82  LYS   C C     
4695 O  O     . LYS   D 83  ? 0.28108 0.18423 0.16120 0.03191  0.01811  0.00281  82  LYS   C O     
4696 C  CB    . LYS   D 83  ? 0.27049 0.22589 0.43876 0.00777  0.03100  0.08081  82  LYS   C CB    
4697 C  CG    . LYS   D 83  ? 0.37384 0.29117 0.69649 0.01681  0.04290  0.03135  82  LYS   C CG    
4698 C  CD    . LYS   D 83  ? 0.44694 0.33592 0.83356 0.01790  0.05488  -0.00935 82  LYS   C CD    
4699 C  CE    . LYS   D 83  ? 0.52395 0.37570 0.92485 0.03980  0.07575  -0.02794 82  LYS   C CE    
4700 N  NZ    . LYS   D 83  ? 0.57215 0.40026 0.97913 0.04097  0.07288  -0.02614 82  LYS   C NZ    
4701 N  N     . PHE   D 84  ? 0.21683 0.15409 0.18902 0.00897  -0.01811 0.02103  83  PHE   C N     
4702 C  CA    . PHE   D 84  ? 0.21245 0.16476 0.17975 0.00121  0.02020  0.01683  83  PHE   C CA    
4703 C  C     . PHE   D 84  ? 0.18098 0.17055 0.16801 0.00186  -0.02051 -0.00581 83  PHE   C C     
4704 O  O     . PHE   D 84  ? 0.20014 0.17542 0.16726 -0.00502 0.00237  -0.01452 83  PHE   C O     
4705 C  CB    . PHE   D 84  ? 0.21468 0.17035 0.17299 -0.00356 0.01431  -0.00496 83  PHE   C CB    
4706 C  CG    . PHE   D 84  ? 0.16746 0.18956 0.17890 0.02754  0.01508  -0.00782 83  PHE   C CG    
4707 C  CD1   . PHE   D 84  ? 0.19208 0.20705 0.16660 0.01029  -0.01954 -0.00937 83  PHE   C CD1   
4708 C  CD2   . PHE   D 84  ? 0.17916 0.19376 0.20115 0.02797  0.00203  0.01827  83  PHE   C CD2   
4709 C  CE1   . PHE   D 84  ? 0.15911 0.19887 0.18628 -0.00655 0.01902  -0.01073 83  PHE   C CE1   
4710 C  CE2   . PHE   D 84  ? 0.19804 0.21506 0.21086 0.02115  -0.02303 -0.01322 83  PHE   C CE2   
4711 C  CZ    . PHE   D 84  ? 0.16712 0.20247 0.21882 0.02411  0.00237  0.01163  83  PHE   C CZ    
4712 N  N     . GLU   D 85  ? 0.19811 0.19497 0.16666 -0.00605 -0.01433 -0.00067 84  GLU   C N     
4713 C  CA    . GLU   D 85  ? 0.25605 0.24330 0.16775 0.04610  -0.03118 -0.00112 84  GLU   C CA    
4714 C  C     . GLU   D 85  ? 0.23169 0.19552 0.15196 0.02524  -0.05121 0.01375  84  GLU   C C     
4715 O  O     . GLU   D 85  ? 0.22965 0.19815 0.19207 0.01368  -0.01133 0.01586  84  GLU   C O     
4716 C  CB    . GLU   D 85  ? 0.34001 0.31558 0.21421 0.08969  -0.04544 0.02685  84  GLU   C CB    
4717 C  CG    . GLU   D 85  ? 0.54567 0.38030 0.22361 0.09430  -0.05667 0.05953  84  GLU   C CG    
4718 C  CD    . GLU   D 85  ? 0.74073 0.42911 0.24844 0.06130  -0.02098 0.05833  84  GLU   C CD    
4719 O  OE1   . GLU   D 85  ? 0.78894 0.47835 0.28544 0.03167  -0.03022 0.05867  84  GLU   C OE1   
4720 O  OE2   . GLU   D 85  ? 0.86577 0.44838 0.24464 0.04575  0.02481  0.07793  84  GLU   C OE2   
4721 N  N     . ASP   D 86  ? 0.20691 0.19106 0.14719 0.01024  -0.02452 0.00613  85  ASP   C N     
4722 C  CA    . ASP   D 86  ? 0.19632 0.18892 0.17919 0.00808  0.00226  0.02103  85  ASP   C CA    
4723 C  C     . ASP   D 86  ? 0.18733 0.19112 0.15358 -0.01262 -0.04479 0.02894  85  ASP   C C     
4724 O  O     . ASP   D 86  ? 0.25247 0.22228 0.18138 -0.04673 -0.06678 0.03943  85  ASP   C O     
4725 C  CB    . ASP   D 86  ? 0.16852 0.21601 0.18780 0.00477  -0.01030 0.01618  85  ASP   C CB    
4726 C  CG    . ASP   D 86  ? 0.20284 0.20086 0.14999 -0.04253 -0.04106 0.00936  85  ASP   C CG    
4727 O  OD1   . ASP   D 86  ? 0.18602 0.19145 0.15954 -0.00746 -0.03603 0.00220  85  ASP   C OD1   
4728 O  OD2   . ASP   D 86  ? 0.20897 0.19533 0.15580 -0.00859 -0.05128 -0.00009 85  ASP   C OD2   
4729 N  N     . GLU   D 87  ? 0.20331 0.18170 0.14704 -0.01471 -0.01797 0.01715  86  GLU   C N     
4730 C  CA    . GLU   D 87  ? 0.22368 0.18492 0.17406 -0.01290 -0.00939 0.00640  86  GLU   C CA    
4731 C  C     . GLU   D 87  ? 0.20937 0.16379 0.18800 -0.00299 -0.05231 0.02128  86  GLU   C C     
4732 O  O     . GLU   D 87  ? 0.23026 0.18981 0.16746 -0.00070 -0.03436 0.01674  86  GLU   C O     
4733 C  CB    . GLU   D 87  ? 0.19440 0.20492 0.19976 -0.03959 -0.02808 -0.01574 86  GLU   C CB    
4734 C  CG    . GLU   D 87  ? 0.18881 0.19233 0.19786 -0.03407 -0.03326 0.03641  86  GLU   C CG    
4735 C  CD    . GLU   D 87  ? 0.24540 0.19641 0.16514 -0.01855 0.00504  0.05187  86  GLU   C CD    
4736 O  OE1   . GLU   D 87  ? 0.22020 0.19981 0.17757 -0.01718 -0.00428 0.01801  86  GLU   C OE1   
4737 O  OE2   . GLU   D 87  ? 0.21264 0.20363 0.17963 -0.03316 -0.01397 0.04645  86  GLU   C OE2   
4738 N  N     . ASN   D 88  ? 0.25671 0.14479 0.17119 0.01324  -0.04069 0.00047  87  ASN   C N     
4739 C  CA    . ASN   D 88  ? 0.21493 0.14612 0.17375 -0.01074 -0.01786 0.00507  87  ASN   C CA    
4740 C  C     . ASN   D 88  ? 0.20237 0.16203 0.16728 0.02955  -0.01426 0.00099  87  ASN   C C     
4741 O  O     . ASN   D 88  ? 0.20504 0.19788 0.19148 0.02670  -0.03135 0.02691  87  ASN   C O     
4742 C  CB    . ASN   D 88  ? 0.20021 0.15217 0.18681 -0.04185 -0.04976 -0.00023 87  ASN   C CB    
4743 C  CG    . ASN   D 88  ? 0.22349 0.15458 0.17403 0.00513  -0.02737 -0.01369 87  ASN   C CG    
4744 O  OD1   . ASN   D 88  ? 0.23850 0.16433 0.19086 0.01339  -0.05750 -0.01448 87  ASN   C OD1   
4745 N  ND2   . ASN   D 88  ? 0.21527 0.15875 0.18985 -0.03681 -0.04501 0.03909  87  ASN   C ND2   
4746 N  N     . PHE   D 89  ? 0.20144 0.21862 0.15328 0.01235  -0.03669 0.00737  88  PHE   C N     
4747 C  CA    . PHE   D 89  ? 0.18857 0.21399 0.18595 0.01764  -0.04100 -0.00137 88  PHE   C CA    
4748 C  C     . PHE   D 89  ? 0.20065 0.21646 0.22144 0.02189  -0.01820 -0.00697 88  PHE   C C     
4749 O  O     . PHE   D 89  ? 0.21620 0.25621 0.23895 0.03457  -0.01232 -0.03602 88  PHE   C O     
4750 C  CB    . PHE   D 89  ? 0.20042 0.21338 0.20177 0.01715  -0.01233 -0.01667 88  PHE   C CB    
4751 C  CG    . PHE   D 89  ? 0.18533 0.23278 0.20307 0.02293  -0.02874 -0.01323 88  PHE   C CG    
4752 C  CD1   . PHE   D 89  ? 0.19506 0.27048 0.21862 0.00342  -0.01872 -0.01206 88  PHE   C CD1   
4753 C  CD2   . PHE   D 89  ? 0.24785 0.25459 0.22497 0.02355  -0.00813 -0.02689 88  PHE   C CD2   
4754 C  CE1   . PHE   D 89  ? 0.15037 0.27980 0.21776 0.00664  -0.01241 -0.00143 88  PHE   C CE1   
4755 C  CE2   . PHE   D 89  ? 0.23248 0.27278 0.24421 -0.04521 -0.01896 -0.00956 88  PHE   C CE2   
4756 C  CZ    . PHE   D 89  ? 0.24978 0.28521 0.20100 -0.05490 0.00432  -0.02155 88  PHE   C CZ    
4757 N  N     . ILE   D 90  ? 0.19874 0.19046 0.22222 0.01791  -0.05973 0.00775  89  ILE   C N     
4758 C  CA    . ILE   D 90  ? 0.25650 0.18752 0.23410 0.04592  -0.06567 0.00232  89  ILE   C CA    
4759 C  C     . ILE   D 90  ? 0.24512 0.19127 0.21639 0.06295  -0.04904 -0.01233 89  ILE   C C     
4760 O  O     . ILE   D 90  ? 0.27977 0.19513 0.29195 0.08018  -0.02460 -0.02145 89  ILE   C O     
4761 C  CB    . ILE   D 90  ? 0.29862 0.17665 0.26661 0.03391  -0.00452 0.05508  89  ILE   C CB    
4762 C  CG1   . ILE   D 90  ? 0.36091 0.23811 0.28768 0.02631  -0.02902 0.07185  89  ILE   C CG1   
4763 C  CG2   . ILE   D 90  ? 0.35778 0.16033 0.33535 0.05596  0.01224  0.06401  89  ILE   C CG2   
4764 C  CD1   . ILE   D 90  ? 0.38265 0.26117 0.28760 0.04611  0.02620  0.07004  89  ILE   C CD1   
4765 N  N     . LEU   D 91  ? 0.21536 0.18382 0.20009 0.01273  -0.03038 0.01417  90  LEU   C N     
4766 C  CA    . LEU   D 91  ? 0.20589 0.17925 0.20198 0.02595  0.02346  0.03350  90  LEU   C CA    
4767 C  C     . LEU   D 91  ? 0.21240 0.15641 0.20157 0.01658  -0.00901 0.03833  90  LEU   C C     
4768 O  O     . LEU   D 91  ? 0.21880 0.14546 0.22066 0.02367  -0.00703 0.03302  90  LEU   C O     
4769 C  CB    . LEU   D 91  ? 0.19704 0.20144 0.25405 0.03426  0.01607  0.02715  90  LEU   C CB    
4770 C  CG    . LEU   D 91  ? 0.18418 0.18500 0.37685 0.01724  0.00930  0.04885  90  LEU   C CG    
4771 C  CD1   . LEU   D 91  ? 0.21629 0.24554 0.39101 0.02280  0.00549  0.04828  90  LEU   C CD1   
4772 C  CD2   . LEU   D 91  ? 0.26353 0.16607 0.44242 -0.00755 0.02571  0.06419  90  LEU   C CD2   
4773 N  N     . LYS   D 92  ? 0.21346 0.18969 0.21392 0.01130  -0.01472 0.01605  91  LYS   C N     
4774 C  CA    . LYS   D 92  ? 0.21535 0.21939 0.22210 0.02577  -0.01066 0.02940  91  LYS   C CA    
4775 C  C     . LYS   D 92  ? 0.15619 0.18481 0.22844 0.02077  0.01307  -0.02008 91  LYS   C C     
4776 O  O     . LYS   D 92  ? 0.17820 0.17140 0.24384 0.01738  0.00466  0.00635  91  LYS   C O     
4777 C  CB    . LYS   D 92  ? 0.20509 0.28206 0.25049 0.06991  -0.00048 0.05148  91  LYS   C CB    
4778 C  CG    . LYS   D 92  ? 0.25640 0.33192 0.30759 0.06540  -0.03272 0.07805  91  LYS   C CG    
4779 C  CD    . LYS   D 92  ? 0.48819 0.37185 0.40537 0.06143  -0.02761 0.08392  91  LYS   C CD    
4780 C  CE    . LYS   D 92  ? 0.64217 0.41028 0.46895 0.05579  -0.06007 0.10374  91  LYS   C CE    
4781 N  NZ    . LYS   D 92  ? 0.72304 0.44451 0.52900 0.05294  -0.05633 0.09967  91  LYS   C NZ    
4782 N  N     . HIS   D 93  ? 0.17296 0.20886 0.24018 0.01079  0.01911  -0.00543 92  HIS   C N     
4783 C  CA    . HIS   D 93  ? 0.23292 0.22076 0.17949 0.00389  0.00728  -0.00463 92  HIS   C CA    
4784 C  C     . HIS   D 93  ? 0.21490 0.21641 0.23457 0.00910  0.01724  -0.04613 92  HIS   C C     
4785 O  O     . HIS   D 93  ? 0.23624 0.25476 0.31173 -0.00622 0.06785  -0.05025 92  HIS   C O     
4786 C  CB    . HIS   D 93  ? 0.21557 0.19947 0.19749 0.01824  0.02816  0.00601  92  HIS   C CB    
4787 C  CG    . HIS   D 93  ? 0.14954 0.17625 0.17891 0.00691  0.02860  -0.02805 92  HIS   C CG    
4788 N  ND1   . HIS   D 93  ? 0.16788 0.18123 0.17253 0.01644  0.01088  -0.00360 92  HIS   C ND1   
4789 C  CD2   . HIS   D 93  ? 0.19811 0.17015 0.18680 0.01691  0.01690  -0.01839 92  HIS   C CD2   
4790 C  CE1   . HIS   D 93  ? 0.12452 0.18090 0.19884 0.03301  -0.01865 0.01883  92  HIS   C CE1   
4791 N  NE2   . HIS   D 93  ? 0.12408 0.19331 0.23360 -0.01471 -0.01382 0.01007  92  HIS   C NE2   
4792 N  N     . THR   D 94  ? 0.21111 0.20441 0.21239 0.04623  0.00359  -0.01332 93  THR   C N     
4793 C  CA    . THR   D 94  ? 0.30353 0.23335 0.25010 0.04510  -0.00391 -0.03164 93  THR   C CA    
4794 C  C     . THR   D 94  ? 0.40740 0.25493 0.24351 0.10842  -0.05871 -0.06160 93  THR   C C     
4795 O  O     . THR   D 94  ? 0.53572 0.30145 0.27229 0.17984  -0.03412 -0.06234 93  THR   C O     
4796 C  CB    . THR   D 94  ? 0.23991 0.23078 0.28402 0.06458  -0.03241 -0.04003 93  THR   C CB    
4797 O  OG1   . THR   D 94  ? 0.31171 0.24965 0.37275 0.04090  -0.04803 -0.06853 93  THR   C OG1   
4798 C  CG2   . THR   D 94  ? 0.31347 0.23230 0.31998 0.02753  -0.03228 -0.00283 93  THR   C CG2   
4799 N  N     . GLY   D 95  ? 0.23729 0.22873 0.25407 0.04743  -0.07355 -0.05108 94  GLY   C N     
4800 C  CA    . GLY   D 95  ? 0.24110 0.26069 0.23892 0.03607  -0.06796 -0.06277 94  GLY   C CA    
4801 C  C     . GLY   D 95  ? 0.26485 0.26979 0.19968 0.04438  -0.03766 -0.04356 94  GLY   C C     
4802 O  O     . GLY   D 95  ? 0.29333 0.24530 0.21361 0.03423  0.00315  -0.05486 94  GLY   C O     
4803 N  N     . PRO   D 96  ? 0.23160 0.28372 0.19858 0.05594  0.00157  -0.05561 95  PRO   C N     
4804 C  CA    . PRO   D 96  ? 0.21852 0.27531 0.21676 0.03862  -0.00901 -0.04108 95  PRO   C CA    
4805 C  C     . PRO   D 96  ? 0.19430 0.25930 0.25480 0.02993  0.03886  -0.04045 95  PRO   C C     
4806 O  O     . PRO   D 96  ? 0.27815 0.27122 0.28746 0.04972  0.03672  -0.05215 95  PRO   C O     
4807 C  CB    . PRO   D 96  ? 0.26433 0.27842 0.20485 0.07278  0.02136  -0.05273 95  PRO   C CB    
4808 C  CG    . PRO   D 96  ? 0.30826 0.33102 0.19026 0.05946  0.01757  -0.03861 95  PRO   C CG    
4809 C  CD    . PRO   D 96  ? 0.27487 0.31430 0.16820 0.05715  0.00386  -0.07008 95  PRO   C CD    
4810 N  N     . GLY   D 97  ? 0.21649 0.25009 0.19359 0.02375  0.00953  -0.03842 96  GLY   C N     
4811 C  CA    . GLY   D 97  ? 0.19652 0.22551 0.18532 0.00158  0.03432  -0.04330 96  GLY   C CA    
4812 C  C     . GLY   D 97  ? 0.21823 0.20542 0.16418 -0.03676 -0.00318 -0.01209 96  GLY   C C     
4813 O  O     . GLY   D 97  ? 0.19574 0.23955 0.16648 -0.00688 -0.00641 -0.00672 96  GLY   C O     
4814 N  N     . ILE   D 98  ? 0.16348 0.20346 0.18051 0.02510  -0.04667 -0.03841 97  ILE   C N     
4815 C  CA    . ILE   D 98  ? 0.18741 0.20441 0.16353 0.01837  -0.02843 -0.00715 97  ILE   C CA    
4816 C  C     . ILE   D 98  ? 0.19657 0.18503 0.20227 0.01469  -0.03067 -0.02330 97  ILE   C C     
4817 O  O     . ILE   D 98  ? 0.17893 0.18205 0.19283 0.00519  -0.02370 -0.02864 97  ILE   C O     
4818 C  CB    . ILE   D 98  ? 0.18550 0.23239 0.18264 0.04472  -0.05118 -0.03848 97  ILE   C CB    
4819 C  CG1   . ILE   D 98  ? 0.26208 0.25680 0.22315 0.07159  -0.01419 -0.00328 97  ILE   C CG1   
4820 C  CG2   . ILE   D 98  ? 0.23133 0.31155 0.16306 0.03376  -0.07249 -0.01540 97  ILE   C CG2   
4821 C  CD1   . ILE   D 98  ? 0.30770 0.27282 0.21226 0.09758  0.00580  0.02689  97  ILE   C CD1   
4822 N  N     . LEU   D 99  ? 0.15866 0.14890 0.16570 0.01892  -0.00611 -0.02181 98  LEU   C N     
4823 C  CA    . LEU   D 99  ? 0.12255 0.16749 0.17079 -0.00097 -0.03239 -0.03691 98  LEU   C CA    
4824 C  C     . LEU   D 99  ? 0.15263 0.16602 0.16217 0.03199  -0.01513 -0.01062 98  LEU   C C     
4825 O  O     . LEU   D 99  ? 0.16875 0.16874 0.15756 -0.00374 -0.01572 0.00920  98  LEU   C O     
4826 C  CB    . LEU   D 99  ? 0.13532 0.18998 0.20819 0.01175  -0.00788 -0.01565 98  LEU   C CB    
4827 C  CG    . LEU   D 99  ? 0.16450 0.16588 0.21722 0.00911  0.01959  0.01506  98  LEU   C CG    
4828 C  CD1   . LEU   D 99  ? 0.17955 0.17627 0.22055 0.03036  0.01718  0.03087  98  LEU   C CD1   
4829 C  CD2   . LEU   D 99  ? 0.14125 0.20374 0.18968 -0.02176 -0.00121 0.04595  98  LEU   C CD2   
4830 N  N     . SER   D 100 ? 0.14573 0.14171 0.17840 -0.00182 -0.01636 -0.03291 99  SER   C N     
4831 C  CA    . SER   D 100 ? 0.15735 0.13445 0.14977 -0.01309 -0.02303 -0.02260 99  SER   C CA    
4832 C  C     . SER   D 100 ? 0.13624 0.14932 0.13461 -0.01475 -0.01716 0.01269  99  SER   C C     
4833 O  O     . SER   D 100 ? 0.14393 0.15445 0.11933 -0.00067 -0.01467 0.00141  99  SER   C O     
4834 C  CB    . SER   D 100 ? 0.13633 0.15811 0.21926 -0.02078 0.01576  -0.01986 99  SER   C CB    
4835 O  OG    . SER   D 100 ? 0.15508 0.15913 0.18846 -0.01418 -0.03087 0.00831  99  SER   C OG    
4836 N  N     . MET   D 101 ? 0.13502 0.16145 0.13824 -0.01253 -0.02454 0.01119  100 MET   C N     
4837 C  CA    . MET   D 101 ? 0.18409 0.16280 0.12439 -0.00867 0.00215  -0.00181 100 MET   C CA    
4838 C  C     . MET   D 101 ? 0.15248 0.15448 0.09785 -0.02590 0.00171  0.00823  100 MET   C C     
4839 O  O     . MET   D 101 ? 0.14041 0.17303 0.15837 -0.00759 -0.01345 0.02015  100 MET   C O     
4840 C  CB    . MET   D 101 ? 0.21474 0.15947 0.14300 -0.00372 0.02560  0.01659  100 MET   C CB    
4841 C  CG    . MET   D 101 ? 0.15745 0.14969 0.17371 -0.01055 0.03861  0.00806  100 MET   C CG    
4842 S  SD    . MET   D 101 ? 0.17140 0.16367 0.18498 -0.01089 0.02356  0.00329  100 MET   C SD    
4843 C  CE    . MET   D 101 ? 0.16873 0.17263 0.21801 -0.01807 0.00767  -0.00271 100 MET   C CE    
4844 N  N     . ALA   D 102 ? 0.14184 0.15257 0.15201 -0.00047 -0.00441 0.02602  101 ALA   C N     
4845 C  CA    . ALA   D 102 ? 0.17239 0.15529 0.13303 -0.02529 -0.01743 0.02494  101 ALA   C CA    
4846 C  C     . ALA   D 102 ? 0.15116 0.12461 0.13972 -0.01125 -0.02977 0.01298  101 ALA   C C     
4847 O  O     . ALA   D 102 ? 0.15576 0.19124 0.15943 -0.00923 -0.01390 -0.00313 101 ALA   C O     
4848 C  CB    . ALA   D 102 ? 0.18108 0.16285 0.16021 -0.02159 -0.04686 0.03739  101 ALA   C CB    
4849 N  N     . ASN   D 103 ? 0.15175 0.16804 0.13450 0.00643  -0.02806 -0.00214 102 ASN   C N     
4850 C  CA    . ASN   D 103 ? 0.18077 0.17934 0.14339 -0.04273 -0.04703 0.01459  102 ASN   C CA    
4851 C  C     . ASN   D 103 ? 0.15921 0.18101 0.12887 -0.03849 -0.05151 0.02822  102 ASN   C C     
4852 O  O     . ASN   D 103 ? 0.19931 0.21697 0.15036 -0.03303 -0.02310 0.02814  102 ASN   C O     
4853 C  CB    . ASN   D 103 ? 0.15195 0.18603 0.16454 -0.02368 -0.03442 0.00997  102 ASN   C CB    
4854 C  CG    . ASN   D 103 ? 0.19096 0.17506 0.15820 -0.03828 -0.02559 0.01268  102 ASN   C CG    
4855 O  OD1   . ASN   D 103 ? 0.15681 0.20318 0.19825 -0.02789 -0.03922 0.04615  102 ASN   C OD1   
4856 N  ND2   . ASN   D 103 ? 0.25094 0.14569 0.14084 -0.01287 -0.03281 0.02751  102 ASN   C ND2   
4857 N  N     . ALA   D 104 ? 0.20696 0.17092 0.15984 -0.05998 -0.05161 0.00952  103 ALA   C N     
4858 C  CA    . ALA   D 104 ? 0.22431 0.16468 0.21280 -0.05643 -0.05408 -0.01131 103 ALA   C CA    
4859 C  C     . ALA   D 104 ? 0.24024 0.18683 0.20207 -0.07639 -0.03053 0.04657  103 ALA   C C     
4860 O  O     . ALA   D 104 ? 0.31560 0.22550 0.27194 -0.08073 -0.10603 -0.01160 103 ALA   C O     
4861 C  CB    . ALA   D 104 ? 0.25986 0.16229 0.24498 -0.00511 -0.03897 -0.00124 103 ALA   C CB    
4862 N  N     . GLY   D 105 ? 0.20341 0.21473 0.19429 -0.04542 -0.05979 0.05469  104 GLY   C N     
4863 C  CA    . GLY   D 105 ? 0.20284 0.25901 0.18083 -0.04788 -0.05243 0.06019  104 GLY   C CA    
4864 C  C     . GLY   D 105 ? 0.18053 0.25499 0.16917 -0.02967 -0.07344 0.03159  104 GLY   C C     
4865 O  O     . GLY   D 105 ? 0.18236 0.22585 0.19151 -0.02832 -0.05213 0.03788  104 GLY   C O     
4866 N  N     . PRO   D 106 ? 0.21108 0.27244 0.16414 -0.03952 -0.05432 0.05094  105 PRO   C N     
4867 C  CA    . PRO   D 106 ? 0.20985 0.27740 0.16807 -0.00449 -0.06910 0.05095  105 PRO   C CA    
4868 C  C     . PRO   D 106 ? 0.18909 0.20225 0.16554 -0.00466 -0.00827 0.01382  105 PRO   C C     
4869 O  O     . PRO   D 106 ? 0.23456 0.17570 0.21836 -0.01412 -0.05096 -0.00528 105 PRO   C O     
4870 C  CB    . PRO   D 106 ? 0.25864 0.31774 0.18923 0.01509  -0.07115 0.03324  105 PRO   C CB    
4871 C  CG    . PRO   D 106 ? 0.21875 0.32394 0.21943 -0.01687 -0.03845 0.05821  105 PRO   C CG    
4872 C  CD    . PRO   D 106 ? 0.16500 0.29658 0.23860 -0.03679 -0.09215 0.04622  105 PRO   C CD    
4873 N  N     . ASN   D 107 ? 0.22547 0.19876 0.16706 -0.01039 -0.02717 0.00150  106 ASN   C N     
4874 C  CA    . ASN   D 107 ? 0.29399 0.18809 0.14380 -0.02838 -0.02711 0.01742  106 ASN   C CA    
4875 C  C     . ASN   D 107 ? 0.24818 0.19281 0.13668 -0.00841 -0.02858 -0.01127 106 ASN   C C     
4876 O  O     . ASN   D 107 ? 0.24217 0.22555 0.15487 -0.01490 -0.03928 -0.03517 106 ASN   C O     
4877 C  CB    . ASN   D 107 ? 0.27825 0.19314 0.17847 -0.00202 -0.06760 0.00233  106 ASN   C CB    
4878 C  CG    . ASN   D 107 ? 0.31439 0.21958 0.16984 -0.00315 -0.08746 -0.00576 106 ASN   C CG    
4879 O  OD1   . ASN   D 107 ? 0.27711 0.22961 0.17391 -0.02653 -0.04340 -0.00422 106 ASN   C OD1   
4880 N  ND2   . ASN   D 107 ? 0.33336 0.23737 0.26551 0.01385  -0.13932 -0.02387 106 ASN   C ND2   
4881 N  N     . THR   D 108 ? 0.17131 0.19315 0.15452 -0.00353 -0.02316 0.00932  107 THR   C N     
4882 C  CA    . THR   D 108 ? 0.18541 0.16689 0.15801 0.00637  -0.04131 0.01248  107 THR   C CA    
4883 C  C     . THR   D 108 ? 0.18843 0.18306 0.16094 -0.00035 -0.04018 0.01203  107 THR   C C     
4884 O  O     . THR   D 108 ? 0.22194 0.22269 0.20707 -0.05241 -0.08798 0.04671  107 THR   C O     
4885 C  CB    . THR   D 108 ? 0.22341 0.19884 0.15571 -0.02708 -0.04919 0.02143  107 THR   C CB    
4886 O  OG1   . THR   D 108 ? 0.23371 0.21902 0.17666 -0.03319 0.00080  0.01619  107 THR   C OG1   
4887 C  CG2   . THR   D 108 ? 0.25673 0.19985 0.18877 -0.05004 -0.08454 0.02818  107 THR   C CG2   
4888 N  N     . ASN   D 109 ? 0.17231 0.16603 0.15157 0.01387  -0.02302 0.00586  108 ASN   C N     
4889 C  CA    . ASN   D 109 ? 0.16900 0.14436 0.17407 0.01155  -0.03567 0.00091  108 ASN   C CA    
4890 C  C     . ASN   D 109 ? 0.20357 0.17096 0.10559 0.00014  -0.01629 0.01226  108 ASN   C C     
4891 O  O     . ASN   D 109 ? 0.21555 0.18850 0.12651 0.01548  -0.02068 -0.00380 108 ASN   C O     
4892 C  CB    . ASN   D 109 ? 0.19440 0.15301 0.18245 0.03106  -0.03141 -0.00099 108 ASN   C CB    
4893 C  CG    . ASN   D 109 ? 0.16852 0.19271 0.14400 -0.00064 -0.01533 -0.00189 108 ASN   C CG    
4894 O  OD1   . ASN   D 109 ? 0.18520 0.19857 0.15967 0.02321  -0.01940 -0.01403 108 ASN   C OD1   
4895 N  ND2   . ASN   D 109 ? 0.17215 0.18371 0.19149 -0.00137 -0.03796 0.00828  108 ASN   C ND2   
4896 N  N     . GLY   D 110 ? 0.17149 0.15842 0.14360 0.03425  -0.00316 -0.00848 109 GLY   C N     
4897 C  CA    . GLY   D 110 ? 0.17054 0.17615 0.15697 0.02999  -0.01765 -0.00433 109 GLY   C CA    
4898 C  C     . GLY   D 110 ? 0.13787 0.17297 0.15217 0.02332  -0.00781 0.02954  109 GLY   C C     
4899 O  O     . GLY   D 110 ? 0.18431 0.18220 0.15239 -0.01067 -0.00659 0.01838  109 GLY   C O     
4900 N  N     . SER   D 111 ? 0.16048 0.17399 0.13842 0.00945  -0.01529 0.01123  110 SER   C N     
4901 C  CA    . SER   D 111 ? 0.14351 0.15121 0.15327 -0.00040 -0.02330 0.01644  110 SER   C CA    
4902 C  C     . SER   D 111 ? 0.15295 0.14922 0.15023 -0.01669 0.01139  0.03766  110 SER   C C     
4903 O  O     . SER   D 111 ? 0.16332 0.16098 0.17471 -0.01950 -0.00939 -0.00199 110 SER   C O     
4904 C  CB    . SER   D 111 ? 0.19320 0.16641 0.15811 0.02829  0.01595  0.03775  110 SER   C CB    
4905 O  OG    . SER   D 111 ? 0.16650 0.17332 0.17333 0.03076  -0.00749 0.00923  110 SER   C OG    
4906 N  N     . GLN   D 112 ? 0.14903 0.14588 0.15408 0.00862  0.00723  0.03191  111 GLN   C N     
4907 C  CA    . GLN   D 112 ? 0.14713 0.16869 0.14335 -0.00671 0.02485  0.02239  111 GLN   C CA    
4908 C  C     . GLN   D 112 ? 0.13996 0.16340 0.12476 -0.01085 -0.01364 0.00146  111 GLN   C C     
4909 O  O     . GLN   D 112 ? 0.15031 0.16658 0.14870 -0.00893 -0.01254 -0.00796 111 GLN   C O     
4910 C  CB    . GLN   D 112 ? 0.13607 0.14058 0.18029 0.00446  -0.00579 0.04037  111 GLN   C CB    
4911 C  CG    . GLN   D 112 ? 0.14359 0.17311 0.17963 0.01245  0.00879  0.01747  111 GLN   C CG    
4912 C  CD    . GLN   D 112 ? 0.12350 0.18519 0.14547 0.01474  -0.01093 0.01545  111 GLN   C CD    
4913 O  OE1   . GLN   D 112 ? 0.16365 0.20613 0.17623 0.00347  -0.00086 0.03143  111 GLN   C OE1   
4914 N  NE2   . GLN   D 112 ? 0.14705 0.17138 0.19090 0.02800  -0.01415 0.01273  111 GLN   C NE2   
4915 N  N     . PHE   D 113 ? 0.14480 0.13902 0.14627 -0.02374 0.00501  -0.00103 112 PHE   C N     
4916 C  CA    . PHE   D 113 ? 0.14283 0.14795 0.13303 0.00014  -0.00822 0.00311  112 PHE   C CA    
4917 C  C     . PHE   D 113 ? 0.14752 0.13606 0.16820 -0.00530 -0.02808 0.03455  112 PHE   C C     
4918 O  O     . PHE   D 113 ? 0.11085 0.15484 0.15703 -0.01516 -0.01337 -0.00834 112 PHE   C O     
4919 C  CB    . PHE   D 113 ? 0.15197 0.16308 0.16221 -0.01998 0.00524  0.01920  112 PHE   C CB    
4920 C  CG    . PHE   D 113 ? 0.14860 0.19246 0.17053 -0.02844 -0.02995 0.00988  112 PHE   C CG    
4921 C  CD1   . PHE   D 113 ? 0.15951 0.17480 0.19022 -0.04011 -0.01706 -0.03244 112 PHE   C CD1   
4922 C  CD2   . PHE   D 113 ? 0.12678 0.19005 0.20072 -0.02275 -0.01315 0.00958  112 PHE   C CD2   
4923 C  CE1   . PHE   D 113 ? 0.14490 0.20896 0.20649 -0.01207 -0.02806 -0.03802 112 PHE   C CE1   
4924 C  CE2   . PHE   D 113 ? 0.11988 0.19790 0.22487 -0.01836 -0.04948 -0.01614 112 PHE   C CE2   
4925 C  CZ    . PHE   D 113 ? 0.15496 0.20844 0.23160 0.00540  -0.01197 -0.04517 112 PHE   C CZ    
4926 N  N     . PHE   D 114 ? 0.10111 0.18230 0.15586 -0.00474 -0.00971 0.00174  113 PHE   C N     
4927 C  CA    . PHE   D 114 ? 0.14391 0.17648 0.13219 0.00811  0.01168  0.02719  113 PHE   C CA    
4928 C  C     . PHE   D 114 ? 0.11296 0.16196 0.13608 0.01205  -0.00802 0.02716  113 PHE   C C     
4929 O  O     . PHE   D 114 ? 0.13427 0.19782 0.15272 -0.00337 -0.02452 0.00466  113 PHE   C O     
4930 C  CB    . PHE   D 114 ? 0.12804 0.19324 0.15465 -0.02277 -0.01046 0.02366  113 PHE   C CB    
4931 C  CG    . PHE   D 114 ? 0.15783 0.18373 0.14620 -0.01311 0.00615  0.01924  113 PHE   C CG    
4932 C  CD1   . PHE   D 114 ? 0.15126 0.19840 0.11705 -0.03157 -0.00886 0.00353  113 PHE   C CD1   
4933 C  CD2   . PHE   D 114 ? 0.13519 0.20789 0.17306 -0.00160 -0.02588 -0.00027 113 PHE   C CD2   
4934 C  CE1   . PHE   D 114 ? 0.13926 0.18831 0.16114 -0.01479 -0.00642 -0.00333 113 PHE   C CE1   
4935 C  CE2   . PHE   D 114 ? 0.16902 0.19436 0.15359 -0.02000 -0.00479 0.02535  113 PHE   C CE2   
4936 C  CZ    . PHE   D 114 ? 0.18511 0.18692 0.17263 -0.03231 -0.00110 -0.00523 113 PHE   C CZ    
4937 N  N     . ILE   D 115 ? 0.16259 0.16337 0.13751 0.00812  -0.00956 -0.00226 114 ILE   C N     
4938 C  CA    . ILE   D 115 ? 0.16559 0.17106 0.16373 -0.00674 -0.00973 -0.01977 114 ILE   C CA    
4939 C  C     . ILE   D 115 ? 0.14894 0.18201 0.17207 -0.00446 -0.01187 -0.02005 114 ILE   C C     
4940 O  O     . ILE   D 115 ? 0.19696 0.21062 0.13931 0.01777  -0.00048 -0.01306 114 ILE   C O     
4941 C  CB    . ILE   D 115 ? 0.14040 0.18560 0.17708 0.00177  0.00718  -0.03128 114 ILE   C CB    
4942 C  CG1   . ILE   D 115 ? 0.17872 0.21703 0.18674 -0.00188 0.00371  -0.03170 114 ILE   C CG1   
4943 C  CG2   . ILE   D 115 ? 0.18215 0.17515 0.19866 -0.00181 -0.00057 -0.02741 114 ILE   C CG2   
4944 C  CD1   . ILE   D 115 ? 0.15461 0.22869 0.21040 -0.00050 -0.02991 -0.00319 114 ILE   C CD1   
4945 N  N     . CYS   D 116 ? 0.15664 0.19326 0.18885 0.01434  -0.01142 -0.01872 115 CYS   C N     
4946 C  CA    . CYS   D 116 ? 0.13416 0.24581 0.19784 0.03553  0.02004  -0.03460 115 CYS   C CA    
4947 C  C     . CYS   D 116 ? 0.16498 0.25748 0.19191 -0.00975 0.00682  -0.05209 115 CYS   C C     
4948 O  O     . CYS   D 116 ? 0.19575 0.24345 0.21963 -0.01679 -0.01507 -0.03530 115 CYS   C O     
4949 C  CB    . CYS   D 116 ? 0.14174 0.24196 0.19571 0.02790  -0.01145 -0.03349 115 CYS   C CB    
4950 S  SG    . CYS   D 116 ? 0.19026 0.25548 0.21475 0.00483  0.00119  -0.03719 115 CYS   C SG    
4951 N  N     . THR   D 117 ? 0.18340 0.28135 0.17233 0.00173  0.01743  -0.03286 116 THR   C N     
4952 C  CA    . THR   D 117 ? 0.23754 0.31276 0.18539 0.04345  -0.02783 -0.04675 116 THR   C CA    
4953 C  C     . THR   D 117 ? 0.23326 0.30841 0.18825 0.05033  0.00449  -0.05093 116 THR   C C     
4954 O  O     . THR   D 117 ? 0.31613 0.34507 0.19577 0.05792  -0.02212 -0.04946 116 THR   C O     
4955 C  CB    . THR   D 117 ? 0.23198 0.31946 0.18763 0.01511  0.00204  -0.00220 116 THR   C CB    
4956 O  OG1   . THR   D 117 ? 0.23743 0.32466 0.21787 -0.01206 -0.00302 -0.01220 116 THR   C OG1   
4957 C  CG2   . THR   D 117 ? 0.23214 0.31178 0.21542 0.05530  -0.02425 0.01713  116 THR   C CG2   
4958 N  N     . ALA   D 118 ? 0.18184 0.28880 0.23736 0.00003  -0.01110 -0.00416 117 ALA   C N     
4959 C  CA    . ALA   D 118 ? 0.17235 0.31818 0.25914 0.02318  -0.00399 -0.00691 117 ALA   C CA    
4960 C  C     . ALA   D 118 ? 0.17053 0.29817 0.23724 0.04680  -0.00346 -0.04197 117 ALA   C C     
4961 O  O     . ALA   D 118 ? 0.19664 0.30854 0.24565 0.05223  0.00466  -0.04998 117 ALA   C O     
4962 C  CB    . ALA   D 118 ? 0.17489 0.33232 0.31555 0.06628  0.01852  -0.00552 117 ALA   C CB    
4963 N  N     . LYS   D 119 ? 0.20240 0.31776 0.25727 0.06176  0.00935  -0.02466 118 LYS   C N     
4964 C  CA    . LYS   D 119 ? 0.20053 0.32942 0.24627 0.05698  -0.05327 -0.03710 118 LYS   C CA    
4965 C  C     . LYS   D 119 ? 0.22908 0.34884 0.21830 0.00956  -0.00748 -0.04591 118 LYS   C C     
4966 O  O     . LYS   D 119 ? 0.29915 0.37608 0.23820 0.01671  0.05010  -0.05662 118 LYS   C O     
4967 C  CB    . LYS   D 119 ? 0.26797 0.35024 0.31557 0.10030  -0.07719 -0.04078 118 LYS   C CB    
4968 C  CG    . LYS   D 119 ? 0.30288 0.36731 0.39403 0.11825  -0.03892 -0.05489 118 LYS   C CG    
4969 C  CD    . LYS   D 119 ? 0.37304 0.39159 0.46666 0.12160  -0.06067 -0.04463 118 LYS   C CD    
4970 C  CE    . LYS   D 119 ? 0.46444 0.38931 0.50483 0.14058  -0.05410 -0.01949 118 LYS   C CE    
4971 N  NZ    . LYS   D 119 ? 0.49158 0.37815 0.53120 0.12296  -0.05599 -0.02952 118 LYS   C NZ    
4972 N  N     . THR   D 120 ? 0.20555 0.31997 0.21854 -0.01098 -0.01388 -0.03120 119 THR   C N     
4973 C  CA    . THR   D 120 ? 0.19986 0.30192 0.19644 0.03522  -0.00659 -0.02547 119 THR   C CA    
4974 C  C     . THR   D 120 ? 0.15436 0.31254 0.19597 0.01670  -0.00697 -0.00806 119 THR   C C     
4975 O  O     . THR   D 120 ? 0.15505 0.30387 0.19789 -0.00496 0.00780  -0.00923 119 THR   C O     
4976 C  CB    . THR   D 120 ? 0.21953 0.30358 0.19822 0.05299  0.03497  0.03159  119 THR   C CB    
4977 O  OG1   . THR   D 120 ? 0.20313 0.28183 0.21025 0.03417  -0.00599 0.01539  119 THR   C OG1   
4978 C  CG2   . THR   D 120 ? 0.21019 0.30570 0.22049 0.05891  0.01496  0.02088  119 THR   C CG2   
4979 N  N     . GLU   D 121 ? 0.19912 0.33226 0.23496 0.06157  0.00093  0.01643  120 GLU   C N     
4980 C  CA    . GLU   D 121 ? 0.21406 0.32219 0.28585 0.08392  0.00710  0.01033  120 GLU   C CA    
4981 C  C     . GLU   D 121 ? 0.19954 0.31376 0.25473 0.05292  -0.00570 0.03084  120 GLU   C C     
4982 O  O     . GLU   D 121 ? 0.20430 0.32059 0.28522 0.06518  0.02586  0.07663  120 GLU   C O     
4983 C  CB    . GLU   D 121 ? 0.26801 0.36765 0.36727 0.08265  -0.00645 -0.00354 120 GLU   C CB    
4984 C  CG    . GLU   D 121 ? 0.28254 0.41879 0.48644 0.06457  0.04458  -0.03377 120 GLU   C CG    
4985 C  CD    . GLU   D 121 ? 0.34711 0.46905 0.59542 0.03301  0.09336  -0.07456 120 GLU   C CD    
4986 O  OE1   . GLU   D 121 ? 0.28814 0.46200 0.60262 0.03620  0.16285  -0.14719 120 GLU   C OE1   
4987 O  OE2   . GLU   D 121 ? 0.36947 0.50263 0.63919 0.06200  0.06410  -0.04763 120 GLU   C OE2   
4988 N  N     . TRP   D 122 ? 0.16988 0.28497 0.27794 0.06067  -0.01832 0.02035  121 TRP   C N     
4989 C  CA    . TRP   D 122 ? 0.15149 0.31317 0.24883 0.00168  0.03271  0.02457  121 TRP   C CA    
4990 C  C     . TRP   D 122 ? 0.19211 0.29450 0.25507 -0.00712 -0.01479 0.02774  121 TRP   C C     
4991 O  O     . TRP   D 122 ? 0.18238 0.30595 0.29258 -0.02779 -0.00172 0.03860  121 TRP   C O     
4992 C  CB    . TRP   D 122 ? 0.13887 0.33416 0.24724 0.00795  0.02930  0.04367  121 TRP   C CB    
4993 C  CG    . TRP   D 122 ? 0.16163 0.33253 0.26769 -0.02765 0.01137  0.03455  121 TRP   C CG    
4994 C  CD1   . TRP   D 122 ? 0.19489 0.32291 0.27063 -0.01749 0.03851  0.04428  121 TRP   C CD1   
4995 C  CD2   . TRP   D 122 ? 0.16087 0.32123 0.26802 -0.02102 0.01931  0.04812  121 TRP   C CD2   
4996 N  NE1   . TRP   D 122 ? 0.22321 0.30482 0.26998 -0.01963 0.03011  0.05972  121 TRP   C NE1   
4997 C  CE2   . TRP   D 122 ? 0.18255 0.32435 0.27631 -0.02211 -0.01979 0.04624  121 TRP   C CE2   
4998 C  CE3   . TRP   D 122 ? 0.19493 0.33228 0.28342 -0.01353 0.01498  0.02462  121 TRP   C CE3   
4999 C  CZ2   . TRP   D 122 ? 0.19750 0.30813 0.20920 0.00321  -0.00055 0.01703  121 TRP   C CZ2   
5000 C  CZ3   . TRP   D 122 ? 0.25672 0.32781 0.25375 0.00589  0.05937  0.00679  121 TRP   C CZ3   
5001 C  CH2   . TRP   D 122 ? 0.23683 0.30219 0.22131 0.03968  0.02235  0.00113  121 TRP   C CH2   
5002 N  N     . LEU   D 123 ? 0.14552 0.28241 0.23576 0.01712  -0.02056 0.04838  122 LEU   C N     
5003 C  CA    . LEU   D 123 ? 0.12776 0.27022 0.23942 -0.00834 -0.04930 0.05314  122 LEU   C CA    
5004 C  C     . LEU   D 123 ? 0.20491 0.24877 0.20360 0.00596  -0.00136 0.04776  122 LEU   C C     
5005 O  O     . LEU   D 123 ? 0.15404 0.27373 0.20258 0.02467  -0.00531 0.02371  122 LEU   C O     
5006 C  CB    . LEU   D 123 ? 0.15623 0.23052 0.21163 -0.01887 -0.00645 0.05237  122 LEU   C CB    
5007 C  CG    . LEU   D 123 ? 0.14317 0.22513 0.24956 -0.00334 -0.02783 0.02929  122 LEU   C CG    
5008 C  CD1   . LEU   D 123 ? 0.16003 0.25340 0.29711 0.01492  -0.02697 0.03182  122 LEU   C CD1   
5009 C  CD2   . LEU   D 123 ? 0.22064 0.22710 0.22138 -0.03830 -0.00674 0.03542  122 LEU   C CD2   
5010 N  N     . ASP   D 124 ? 0.18291 0.23464 0.21544 0.00213  -0.00999 0.05485  123 ASP   C N     
5011 C  CA    . ASP   D 124 ? 0.21832 0.23779 0.19995 0.05091  -0.03705 0.04279  123 ASP   C CA    
5012 C  C     . ASP   D 124 ? 0.18740 0.25093 0.21507 0.01949  -0.06478 0.01662  123 ASP   C C     
5013 O  O     . ASP   D 124 ? 0.14956 0.27457 0.28895 -0.00950 -0.05956 0.00177  123 ASP   C O     
5014 C  CB    . ASP   D 124 ? 0.18757 0.25483 0.24452 0.01420  -0.03661 0.02538  123 ASP   C CB    
5015 C  CG    . ASP   D 124 ? 0.15636 0.26612 0.27779 0.03394  0.01362  0.02384  123 ASP   C CG    
5016 O  OD1   . ASP   D 124 ? 0.15733 0.23968 0.28507 0.03801  -0.02600 -0.00589 123 ASP   C OD1   
5017 O  OD2   . ASP   D 124 ? 0.19215 0.32495 0.30905 0.02980  0.01546  0.01222  123 ASP   C OD2   
5018 N  N     . GLY   D 125 ? 0.22302 0.25159 0.18623 0.04726  -0.02818 0.02741  124 GLY   C N     
5019 C  CA    . GLY   D 125 ? 0.16342 0.24008 0.18108 0.01741  -0.02412 0.00493  124 GLY   C CA    
5020 C  C     . GLY   D 125 ? 0.18234 0.25504 0.18766 0.01306  -0.03637 -0.01095 124 GLY   C C     
5021 O  O     . GLY   D 125 ? 0.19785 0.31880 0.22336 -0.00954 -0.05905 -0.02173 124 GLY   C O     
5022 N  N     . LYS   D 126 ? 0.16476 0.21716 0.19676 0.01103  -0.02488 0.01510  125 LYS   C N     
5023 C  CA    . LYS   D 126 ? 0.17195 0.24158 0.26339 -0.01092 -0.03673 0.01510  125 LYS   C CA    
5024 C  C     . LYS   D 126 ? 0.15252 0.21182 0.23525 -0.00528 -0.04991 0.00339  125 LYS   C C     
5025 O  O     . LYS   D 126 ? 0.17027 0.23790 0.23142 0.01384  -0.06770 -0.00642 125 LYS   C O     
5026 C  CB    . LYS   D 126 ? 0.16935 0.27661 0.34128 -0.05630 -0.02363 0.05397  125 LYS   C CB    
5027 C  CG    . LYS   D 126 ? 0.23529 0.34532 0.49240 -0.06871 -0.04442 0.05109  125 LYS   C CG    
5028 C  CD    . LYS   D 126 ? 0.33501 0.41625 0.63719 -0.02827 -0.06272 0.04048  125 LYS   C CD    
5029 C  CE    . LYS   D 126 ? 0.40937 0.46680 0.73094 -0.05028 -0.02769 0.05117  125 LYS   C CE    
5030 N  NZ    . LYS   D 126 ? 0.42270 0.48912 0.80146 -0.06521 -0.00413 0.06151  125 LYS   C NZ    
5031 N  N     . HIS   D 127 ? 0.13707 0.19979 0.16407 -0.01145 -0.02087 0.00389  126 HIS   C N     
5032 C  CA    . HIS   D 127 ? 0.14669 0.20645 0.17913 -0.01299 -0.01875 0.03909  126 HIS   C CA    
5033 C  C     . HIS   D 127 ? 0.16268 0.14740 0.18581 0.01894  -0.00955 0.03392  126 HIS   C C     
5034 O  O     . HIS   D 127 ? 0.16144 0.15905 0.20682 0.01929  -0.01478 0.02767  126 HIS   C O     
5035 C  CB    . HIS   D 127 ? 0.17495 0.19459 0.17813 -0.00669 0.00228  0.04156  126 HIS   C CB    
5036 C  CG    . HIS   D 127 ? 0.16437 0.19967 0.16991 -0.01092 0.00868  0.03012  126 HIS   C CG    
5037 N  ND1   . HIS   D 127 ? 0.16785 0.16694 0.14930 -0.00996 -0.01295 0.02341  126 HIS   C ND1   
5038 C  CD2   . HIS   D 127 ? 0.18015 0.23117 0.19249 -0.03905 0.00504  0.01626  126 HIS   C CD2   
5039 C  CE1   . HIS   D 127 ? 0.17684 0.18720 0.17007 -0.01890 -0.02193 0.04146  126 HIS   C CE1   
5040 N  NE2   . HIS   D 127 ? 0.18407 0.23925 0.18486 -0.02992 -0.01178 0.04871  126 HIS   C NE2   
5041 N  N     . VAL   D 128 ? 0.14747 0.17228 0.17623 0.01022  -0.01263 0.02054  127 VAL   C N     
5042 C  CA    . VAL   D 128 ? 0.18005 0.17865 0.14204 -0.00078 -0.02366 0.00312  127 VAL   C CA    
5043 C  C     . VAL   D 128 ? 0.13227 0.15901 0.15027 0.00212  -0.01681 0.00952  127 VAL   C C     
5044 O  O     . VAL   D 128 ? 0.16123 0.14649 0.17163 0.00111  -0.02977 -0.00212 127 VAL   C O     
5045 C  CB    . VAL   D 128 ? 0.16220 0.15898 0.14242 -0.01051 -0.02882 -0.00794 127 VAL   C CB    
5046 C  CG1   . VAL   D 128 ? 0.19338 0.15994 0.12814 -0.02745 -0.00669 0.00948  127 VAL   C CG1   
5047 C  CG2   . VAL   D 128 ? 0.17478 0.17475 0.14533 0.00665  -0.01120 -0.00021 127 VAL   C CG2   
5048 N  N     . VAL   D 129 ? 0.15765 0.16688 0.14610 -0.00390 -0.01430 0.01423  128 VAL   C N     
5049 C  CA    . VAL   D 129 ? 0.12926 0.17763 0.14857 0.02893  -0.01961 -0.01675 128 VAL   C CA    
5050 C  C     . VAL   D 129 ? 0.14774 0.16511 0.12990 -0.01136 -0.01537 0.00509  128 VAL   C C     
5051 O  O     . VAL   D 129 ? 0.16615 0.19773 0.15261 0.00197  -0.03073 0.02212  128 VAL   C O     
5052 C  CB    . VAL   D 129 ? 0.16543 0.17387 0.16038 0.01941  0.01545  0.01112  128 VAL   C CB    
5053 C  CG1   . VAL   D 129 ? 0.19547 0.17027 0.16993 0.00617  -0.02039 -0.00642 128 VAL   C CG1   
5054 C  CG2   . VAL   D 129 ? 0.17176 0.21587 0.18101 0.02751  0.03163  -0.00330 128 VAL   C CG2   
5055 N  N     . PHE   D 130 ? 0.14903 0.16603 0.15644 0.00973  -0.03076 0.02144  129 PHE   C N     
5056 C  CA    . PHE   D 130 ? 0.14262 0.16859 0.19328 -0.02101 -0.00101 -0.00893 129 PHE   C CA    
5057 C  C     . PHE   D 130 ? 0.15695 0.14780 0.15092 0.00774  -0.00204 -0.01717 129 PHE   C C     
5058 O  O     . PHE   D 130 ? 0.17450 0.16429 0.20246 -0.01420 0.01781  0.01352  129 PHE   C O     
5059 C  CB    . PHE   D 130 ? 0.14981 0.15096 0.18168 -0.01000 0.01001  0.01025  129 PHE   C CB    
5060 C  CG    . PHE   D 130 ? 0.16480 0.11475 0.14819 0.01528  -0.01763 0.00627  129 PHE   C CG    
5061 C  CD1   . PHE   D 130 ? 0.17862 0.13945 0.16658 -0.00054 0.03415  0.02269  129 PHE   C CD1   
5062 C  CD2   . PHE   D 130 ? 0.14940 0.14913 0.18651 0.01464  0.00237  -0.00115 129 PHE   C CD2   
5063 C  CE1   . PHE   D 130 ? 0.12957 0.11802 0.22457 0.00677  0.01252  0.00689  129 PHE   C CE1   
5064 C  CE2   . PHE   D 130 ? 0.19393 0.15429 0.22169 0.01532  0.02755  0.00181  129 PHE   C CE2   
5065 C  CZ    . PHE   D 130 ? 0.15876 0.15936 0.25255 0.00311  0.01345  0.01834  129 PHE   C CZ    
5066 N  N     . GLY   D 131 ? 0.17363 0.14482 0.15796 -0.00810 -0.00663 -0.00365 130 GLY   C N     
5067 C  CA    . GLY   D 131 ? 0.18482 0.17956 0.16643 -0.02881 -0.02962 -0.00570 130 GLY   C CA    
5068 C  C     . GLY   D 131 ? 0.19886 0.15860 0.20740 -0.02934 -0.01651 0.01300  130 GLY   C C     
5069 O  O     . GLY   D 131 ? 0.15618 0.16148 0.21161 -0.00183 -0.00791 0.01125  130 GLY   C O     
5070 N  N     . LYS   D 132 ? 0.18409 0.15712 0.20492 -0.00215 -0.02724 -0.01475 131 LYS   C N     
5071 C  CA    . LYS   D 132 ? 0.18291 0.15988 0.20502 -0.01916 -0.01922 -0.00161 131 LYS   C CA    
5072 C  C     . LYS   D 132 ? 0.21438 0.17160 0.20450 -0.01842 -0.01348 0.00728  131 LYS   C C     
5073 O  O     . LYS   D 132 ? 0.18849 0.22549 0.21263 -0.00905 -0.04077 0.00201  131 LYS   C O     
5074 C  CB    . LYS   D 132 ? 0.24353 0.17566 0.22763 0.01041  -0.00786 0.01134  131 LYS   C CB    
5075 C  CG    . LYS   D 132 ? 0.44538 0.20514 0.42397 0.04708  0.03588  0.00223  131 LYS   C CG    
5076 C  CD    . LYS   D 132 ? 0.56576 0.22453 0.52019 0.07745  0.09943  0.01224  131 LYS   C CD    
5077 C  CE    . LYS   D 132 ? 0.62719 0.22732 0.57830 0.08796  0.14645  0.02243  131 LYS   C CE    
5078 N  NZ    . LYS   D 132 ? 0.74491 0.26780 0.63262 0.11046  0.15209  0.03083  131 LYS   C NZ    
5079 N  N     . VAL   D 133 ? 0.21002 0.18053 0.17066 0.00525  -0.02282 -0.01518 132 VAL   C N     
5080 C  CA    . VAL   D 133 ? 0.21441 0.18804 0.18361 0.00669  -0.04959 -0.03051 132 VAL   C CA    
5081 C  C     . VAL   D 133 ? 0.23562 0.17790 0.20149 0.01407  -0.05498 -0.02004 132 VAL   C C     
5082 O  O     . VAL   D 133 ? 0.22600 0.21367 0.23979 0.04431  -0.06915 -0.03160 132 VAL   C O     
5083 C  CB    . VAL   D 133 ? 0.17623 0.20198 0.19683 0.00961  -0.02817 -0.04927 132 VAL   C CB    
5084 C  CG1   . VAL   D 133 ? 0.19369 0.23370 0.18190 -0.00113 -0.04919 -0.03343 132 VAL   C CG1   
5085 C  CG2   . VAL   D 133 ? 0.17591 0.18514 0.25221 0.00843  -0.02704 -0.05682 132 VAL   C CG2   
5086 N  N     . LYS   D 134 ? 0.25303 0.19298 0.24661 -0.04700 -0.06416 -0.01477 133 LYS   C N     
5087 C  CA    . LYS   D 134 ? 0.22613 0.21658 0.34540 -0.05659 -0.07444 -0.01744 133 LYS   C CA    
5088 C  C     . LYS   D 134 ? 0.24388 0.22701 0.37196 -0.02258 -0.12229 -0.04666 133 LYS   C C     
5089 O  O     . LYS   D 134 ? 0.38035 0.32135 0.40631 0.05974  -0.15335 -0.07692 133 LYS   C O     
5090 C  CB    . LYS   D 134 ? 0.28112 0.25612 0.46332 -0.10679 -0.07162 -0.01023 133 LYS   C CB    
5091 C  CG    . LYS   D 134 ? 0.42459 0.30088 0.58112 -0.08618 -0.09447 -0.01471 133 LYS   C CG    
5092 C  CD    . LYS   D 134 ? 0.45467 0.32488 0.67948 -0.09450 -0.10132 -0.00899 133 LYS   C CD    
5093 C  CE    . LYS   D 134 ? 0.53657 0.35570 0.75159 -0.08665 -0.11153 0.01653  133 LYS   C CE    
5094 N  NZ    . LYS   D 134 ? 0.60092 0.39192 0.79230 -0.04534 -0.09433 0.02771  133 LYS   C NZ    
5095 N  N     . GLU   D 135 ? 0.28597 0.20752 0.32358 -0.02906 -0.08357 -0.04020 134 GLU   C N     
5096 C  CA    . GLU   D 135 ? 0.29475 0.23766 0.34212 -0.03282 -0.07114 -0.04528 134 GLU   C CA    
5097 C  C     . GLU   D 135 ? 0.27287 0.22180 0.24392 -0.00464 -0.04799 -0.06118 134 GLU   C C     
5098 O  O     . GLU   D 135 ? 0.30191 0.18467 0.22905 0.00076  -0.05504 -0.01762 134 GLU   C O     
5099 C  CB    . GLU   D 135 ? 0.44215 0.28554 0.49758 -0.11503 -0.09464 -0.05862 134 GLU   C CB    
5100 C  CG    . GLU   D 135 ? 0.62042 0.35632 0.66859 -0.10917 -0.11355 -0.01037 134 GLU   C CG    
5101 C  CD    . GLU   D 135 ? 0.84560 0.43156 0.81947 -0.07828 -0.12658 0.01764  134 GLU   C CD    
5102 O  OE1   . GLU   D 135 ? 0.90682 0.46940 0.89730 -0.06653 -0.14023 0.03119  134 GLU   C OE1   
5103 O  OE2   . GLU   D 135 ? 0.92379 0.46773 0.87439 -0.06607 -0.13575 0.01381  134 GLU   C OE2   
5104 N  N     . GLY   D 136 ? 0.25922 0.22751 0.23042 -0.02175 -0.02308 -0.02985 135 GLY   C N     
5105 C  CA    . GLY   D 136 ? 0.28451 0.21160 0.22937 -0.01407 -0.03518 -0.01646 135 GLY   C CA    
5106 C  C     . GLY   D 136 ? 0.25383 0.21816 0.23528 0.00199  -0.04781 -0.02182 135 GLY   C C     
5107 O  O     . GLY   D 136 ? 0.28119 0.20089 0.22426 0.01234  -0.07610 -0.03734 135 GLY   C O     
5108 N  N     . MET   D 137 ? 0.22783 0.23736 0.23140 0.04313  -0.03651 -0.01710 136 MET   C N     
5109 C  CA    . MET   D 137 ? 0.28341 0.26573 0.23872 0.01508  -0.05564 -0.03776 136 MET   C CA    
5110 C  C     . MET   D 137 ? 0.28975 0.27228 0.24779 0.00401  -0.08155 -0.05271 136 MET   C C     
5111 O  O     . MET   D 137 ? 0.26608 0.28523 0.29220 0.02119  -0.06985 -0.03949 136 MET   C O     
5112 C  CB    . MET   D 137 ? 0.28749 0.29601 0.28250 0.03056  -0.08347 -0.04863 136 MET   C CB    
5113 C  CG    . MET   D 137 ? 0.32080 0.32218 0.31204 0.05484  -0.09372 -0.08923 136 MET   C CG    
5114 S  SD    . MET   D 137 ? 0.29163 0.37412 0.27060 0.04908  -0.08186 -0.06952 136 MET   C SD    
5115 C  CE    . MET   D 137 ? 0.29407 0.39393 0.29210 0.06968  -0.03616 -0.03949 136 MET   C CE    
5116 N  N     . ASN   D 138 ? 0.32579 0.26288 0.22072 0.05839  -0.08981 -0.04367 137 ASN   C N     
5117 C  CA    . ASN   D 138 ? 0.31183 0.25141 0.20206 0.00097  -0.05729 -0.04029 137 ASN   C CA    
5118 C  C     . ASN   D 138 ? 0.26947 0.23239 0.20811 0.00019  -0.03578 -0.01230 137 ASN   C C     
5119 O  O     . ASN   D 138 ? 0.27612 0.23428 0.27289 -0.00539 -0.09026 -0.03623 137 ASN   C O     
5120 C  CB    . ASN   D 138 ? 0.33554 0.30693 0.25055 -0.00144 -0.05134 -0.07180 137 ASN   C CB    
5121 C  CG    . ASN   D 138 ? 0.35299 0.35217 0.25476 -0.02763 -0.12374 -0.04554 137 ASN   C CG    
5122 O  OD1   . ASN   D 138 ? 0.48699 0.38492 0.27229 -0.05757 -0.08078 -0.07001 137 ASN   C OD1   
5123 N  ND2   . ASN   D 138 ? 0.44856 0.38080 0.30768 -0.03188 -0.08961 -0.02524 137 ASN   C ND2   
5124 N  N     . ILE   D 139 ? 0.27936 0.21416 0.18477 -0.01214 -0.04566 -0.02341 138 ILE   C N     
5125 C  CA    . ILE   D 139 ? 0.26985 0.20729 0.21928 -0.00974 -0.04447 -0.04551 138 ILE   C CA    
5126 C  C     . ILE   D 139 ? 0.24110 0.22428 0.22219 0.02705  -0.05028 -0.05709 138 ILE   C C     
5127 O  O     . ILE   D 139 ? 0.21038 0.22711 0.19416 0.02679  -0.05492 -0.01220 138 ILE   C O     
5128 C  CB    . ILE   D 139 ? 0.19766 0.22471 0.23595 0.00468  -0.06428 -0.00552 138 ILE   C CB    
5129 C  CG1   . ILE   D 139 ? 0.24114 0.27085 0.20752 0.01504  -0.06073 -0.01107 138 ILE   C CG1   
5130 C  CG2   . ILE   D 139 ? 0.25533 0.22924 0.26120 -0.01203 -0.02435 -0.03070 138 ILE   C CG2   
5131 C  CD1   . ILE   D 139 ? 0.20977 0.29991 0.26182 -0.00287 -0.01966 -0.00649 138 ILE   C CD1   
5132 N  N     . VAL   D 140 ? 0.21914 0.25733 0.19365 0.01016  -0.05681 -0.05677 139 VAL   C N     
5133 C  CA    . VAL   D 140 ? 0.22931 0.28776 0.14972 0.00420  -0.03755 -0.00979 139 VAL   C CA    
5134 C  C     . VAL   D 140 ? 0.23368 0.29404 0.16937 0.00923  -0.03135 -0.04808 139 VAL   C C     
5135 O  O     . VAL   D 140 ? 0.20015 0.30012 0.19721 0.01978  -0.02210 -0.04880 139 VAL   C O     
5136 C  CB    . VAL   D 140 ? 0.19716 0.29804 0.16563 -0.00534 -0.05414 0.01422  139 VAL   C CB    
5137 C  CG1   . VAL   D 140 ? 0.21186 0.31637 0.19845 -0.02943 -0.07276 -0.00482 139 VAL   C CG1   
5138 C  CG2   . VAL   D 140 ? 0.20684 0.28922 0.18568 -0.01732 -0.03506 0.00036  139 VAL   C CG2   
5139 N  N     . GLU   D 141 ? 0.23755 0.29936 0.17787 0.00231  -0.02999 -0.04695 140 GLU   C N     
5140 C  CA    . GLU   D 141 ? 0.27681 0.32032 0.16681 0.03873  -0.01570 -0.02559 140 GLU   C CA    
5141 C  C     . GLU   D 141 ? 0.26015 0.31539 0.16599 0.03716  -0.03279 -0.02685 140 GLU   C C     
5142 O  O     . GLU   D 141 ? 0.29005 0.34021 0.19281 -0.00943 0.00177  -0.02749 140 GLU   C O     
5143 C  CB    . GLU   D 141 ? 0.31605 0.35379 0.23178 0.06001  0.01900  -0.02624 140 GLU   C CB    
5144 C  CG    . GLU   D 141 ? 0.40129 0.37791 0.30069 0.11815  -0.02472 -0.01736 140 GLU   C CG    
5145 C  CD    . GLU   D 141 ? 0.44664 0.41087 0.34913 0.14728  -0.06802 -0.03453 140 GLU   C CD    
5146 O  OE1   . GLU   D 141 ? 0.48047 0.41996 0.39486 0.12939  -0.10098 -0.04586 140 GLU   C OE1   
5147 O  OE2   . GLU   D 141 ? 0.48885 0.42489 0.36893 0.14810  -0.10449 -0.06184 140 GLU   C OE2   
5148 N  N     . ALA   D 142 ? 0.23171 0.30019 0.20556 0.04681  -0.04599 -0.02684 141 ALA   C N     
5149 C  CA    . ALA   D 142 ? 0.23373 0.31603 0.19364 0.02550  -0.03854 -0.01306 141 ALA   C CA    
5150 C  C     . ALA   D 142 ? 0.23020 0.30823 0.18024 0.01049  -0.05227 0.01361  141 ALA   C C     
5151 O  O     . ALA   D 142 ? 0.33765 0.33973 0.18856 0.01630  -0.02596 0.00762  141 ALA   C O     
5152 C  CB    . ALA   D 142 ? 0.23947 0.33530 0.22420 -0.02946 -0.05842 -0.00430 141 ALA   C CB    
5153 N  N     . MET   D 143 ? 0.19818 0.29648 0.16700 0.00996  -0.02665 -0.03492 142 MET   C N     
5154 C  CA    . MET   D 143 ? 0.23735 0.30729 0.22360 -0.03797 -0.01148 -0.05053 142 MET   C CA    
5155 C  C     . MET   D 143 ? 0.25600 0.32112 0.24236 -0.01759 -0.01894 -0.06487 142 MET   C C     
5156 O  O     . MET   D 143 ? 0.19737 0.30008 0.26035 0.00145  0.00487  -0.05070 142 MET   C O     
5157 C  CB    . MET   D 143 ? 0.27629 0.32240 0.21413 -0.03493 -0.02301 -0.03545 142 MET   C CB    
5158 C  CG    . MET   D 143 ? 0.20226 0.31712 0.23403 -0.04432 -0.03990 -0.02029 142 MET   C CG    
5159 S  SD    . MET   D 143 ? 0.21846 0.31539 0.23995 0.02692  -0.03929 -0.02192 142 MET   C SD    
5160 C  CE    . MET   D 143 ? 0.27066 0.30907 0.23767 -0.01561 -0.00555 -0.06890 142 MET   C CE    
5161 N  N     . GLU   D 144 ? 0.22594 0.34862 0.29761 -0.01254 0.01678  -0.03698 143 GLU   C N     
5162 C  CA    . GLU   D 144 ? 0.21977 0.37081 0.33658 0.01281  0.00591  -0.06219 143 GLU   C CA    
5163 C  C     . GLU   D 144 ? 0.26066 0.42606 0.33304 -0.02089 0.04370  -0.08442 143 GLU   C C     
5164 O  O     . GLU   D 144 ? 0.21864 0.46081 0.36694 -0.03081 0.04840  -0.08051 143 GLU   C O     
5165 C  CB    . GLU   D 144 ? 0.26516 0.35809 0.30322 0.04550  -0.04798 -0.07226 143 GLU   C CB    
5166 C  CG    . GLU   D 144 ? 0.34963 0.38615 0.34135 0.04537  -0.09454 -0.03555 143 GLU   C CG    
5167 C  CD    . GLU   D 144 ? 0.37086 0.41117 0.35247 0.04463  -0.07184 0.02308  143 GLU   C CD    
5168 O  OE1   . GLU   D 144 ? 0.40686 0.42033 0.33467 0.00448  -0.06693 0.02455  143 GLU   C OE1   
5169 O  OE2   . GLU   D 144 ? 0.36240 0.43461 0.38609 0.04958  -0.02199 0.03888  143 GLU   C OE2   
5170 N  N     . ARG   D 145 ? 0.32783 0.46008 0.32947 -0.00821 0.03082  -0.11188 144 ARG   C N     
5171 C  CA    . ARG   D 145 ? 0.37282 0.48594 0.33813 -0.04677 0.04375  -0.13078 144 ARG   C CA    
5172 C  C     . ARG   D 145 ? 0.27789 0.50136 0.30909 -0.04288 0.04146  -0.08429 144 ARG   C C     
5173 O  O     . ARG   D 145 ? 0.30342 0.51391 0.29205 -0.04231 0.08897  -0.04265 144 ARG   C O     
5174 C  CB    . ARG   D 145 ? 0.60902 0.50192 0.37684 -0.06405 0.04903  -0.20632 144 ARG   C CB    
5175 C  CG    . ARG   D 145 ? 0.80545 0.52490 0.43114 -0.07858 0.03184  -0.25124 144 ARG   C CG    
5176 C  CD    . ARG   D 145 ? 0.92026 0.54164 0.50944 -0.06940 0.07520  -0.27996 144 ARG   C CD    
5177 N  NE    . ARG   D 145 ? 1.01124 0.56657 0.57586 -0.09709 0.07478  -0.30036 144 ARG   C NE    
5178 C  CZ    . ARG   D 145 ? 1.03642 0.58365 0.61863 -0.09517 0.09088  -0.31999 144 ARG   C CZ    
5179 N  NH1   . ARG   D 145 ? 0.97512 0.59387 0.60564 -0.08128 0.12112  -0.32465 144 ARG   C NH1   
5180 N  NH2   . ARG   D 145 ? 1.10028 0.59010 0.65674 -0.11933 0.08782  -0.30766 144 ARG   C NH2   
5181 N  N     . PHE   D 146 ? 0.26265 0.48866 0.28604 -0.05768 -0.00158 -0.07556 145 PHE   C N     
5182 C  CA    . PHE   D 146 ? 0.24039 0.46343 0.23625 -0.07151 -0.00886 -0.05094 145 PHE   C CA    
5183 C  C     . PHE   D 146 ? 0.27166 0.46772 0.21124 -0.06919 -0.02734 0.01121  145 PHE   C C     
5184 O  O     . PHE   D 146 ? 0.28902 0.45161 0.22723 -0.10240 -0.05797 0.03718  145 PHE   C O     
5185 C  CB    . PHE   D 146 ? 0.18609 0.45359 0.18651 -0.01240 0.00991  -0.02507 145 PHE   C CB    
5186 C  CG    . PHE   D 146 ? 0.18507 0.44507 0.20556 -0.00136 -0.01441 -0.08836 145 PHE   C CG    
5187 C  CD1   . PHE   D 146 ? 0.22181 0.46883 0.27021 0.02029  -0.04704 -0.10366 145 PHE   C CD1   
5188 C  CD2   . PHE   D 146 ? 0.20587 0.43947 0.26630 -0.03034 -0.02894 -0.06757 145 PHE   C CD2   
5189 C  CE1   . PHE   D 146 ? 0.22776 0.48442 0.27012 0.00717  -0.08130 -0.08778 145 PHE   C CE1   
5190 C  CE2   . PHE   D 146 ? 0.21897 0.44556 0.28907 0.00508  -0.03061 -0.06588 145 PHE   C CE2   
5191 C  CZ    . PHE   D 146 ? 0.24459 0.46205 0.27254 -0.00444 -0.05781 -0.07363 145 PHE   C CZ    
5192 N  N     . GLY   D 147 ? 0.23427 0.47665 0.16673 -0.08099 -0.00760 0.01972  146 GLY   C N     
5193 C  CA    . GLY   D 147 ? 0.18999 0.47456 0.14206 -0.07311 -0.00686 0.03400  146 GLY   C CA    
5194 C  C     . GLY   D 147 ? 0.19216 0.47329 0.15839 -0.04435 -0.00798 0.02109  146 GLY   C C     
5195 O  O     . GLY   D 147 ? 0.25209 0.49556 0.16844 -0.05519 0.00912  -0.01495 146 GLY   C O     
5196 N  N     . SER   D 148 ? 0.18355 0.45527 0.17189 -0.05892 0.01233  0.04171  147 SER   C N     
5197 C  CA    . SER   D 148 ? 0.18640 0.45600 0.17024 -0.00422 -0.00401 0.04190  147 SER   C CA    
5198 C  C     . SER   D 148 ? 0.19462 0.44347 0.16195 0.00448  0.01367  0.00836  147 SER   C C     
5199 O  O     . SER   D 148 ? 0.20259 0.42576 0.16295 -0.04077 0.01326  -0.00199 147 SER   C O     
5200 C  CB    . SER   D 148 ? 0.20260 0.47030 0.17044 -0.00752 0.00958  0.07879  147 SER   C CB    
5201 O  OG    . SER   D 148 ? 0.23684 0.47759 0.22797 -0.01166 -0.03162 0.09145  147 SER   C OG    
5202 N  N     . ARG   D 149 ? 0.19869 0.44903 0.23452 -0.04461 0.00012  0.02288  148 ARG   C N     
5203 C  CA    . ARG   D 149 ? 0.19428 0.45751 0.22224 -0.06827 -0.00205 0.03535  148 ARG   C CA    
5204 C  C     . ARG   D 149 ? 0.23274 0.46539 0.18965 -0.07167 0.00278  0.07099  148 ARG   C C     
5205 O  O     . ARG   D 149 ? 0.20434 0.50061 0.19847 -0.05186 -0.01589 0.09060  148 ARG   C O     
5206 C  CB    . ARG   D 149 ? 0.18212 0.46892 0.24050 -0.02442 0.04512  0.03627  148 ARG   C CB    
5207 C  CG    . ARG   D 149 ? 0.16533 0.43854 0.20928 -0.00233 0.04058  0.05002  148 ARG   C CG    
5208 C  CD    . ARG   D 149 ? 0.17361 0.43777 0.28768 -0.02075 0.04704  0.01088  148 ARG   C CD    
5209 N  NE    . ARG   D 149 ? 0.15807 0.42705 0.32730 -0.03979 0.09820  0.00401  148 ARG   C NE    
5210 C  CZ    . ARG   D 149 ? 0.16584 0.44919 0.27959 -0.07166 0.05309  0.00136  148 ARG   C CZ    
5211 N  NH1   . ARG   D 149 ? 0.23334 0.42573 0.18928 -0.06845 0.04966  -0.01237 148 ARG   C NH1   
5212 N  NH2   . ARG   D 149 ? 0.20434 0.47684 0.32931 -0.06517 0.06193  -0.00637 148 ARG   C NH2   
5213 N  N     . ASN   D 150 ? 0.21264 0.44017 0.21438 -0.06804 0.02843  0.05828  149 ASN   C N     
5214 C  CA    . ASN   D 150 ? 0.22921 0.40903 0.23371 -0.08908 -0.01804 0.06306  149 ASN   C CA    
5215 C  C     . ASN   D 150 ? 0.22032 0.37730 0.21605 -0.04739 -0.03084 0.07181  149 ASN   C C     
5216 O  O     . ASN   D 150 ? 0.24020 0.37542 0.21604 -0.09084 -0.03377 0.06985  149 ASN   C O     
5217 C  CB    . ASN   D 150 ? 0.30420 0.41833 0.28595 -0.10202 -0.01620 0.08587  149 ASN   C CB    
5218 C  CG    . ASN   D 150 ? 0.41727 0.40801 0.24851 -0.13741 0.00249  0.14008  149 ASN   C CG    
5219 O  OD1   . ASN   D 150 ? 0.39442 0.42086 0.25400 -0.11847 -0.04471 0.15045  149 ASN   C OD1   
5220 N  ND2   . ASN   D 150 ? 0.45470 0.41243 0.31721 -0.14629 -0.01190 0.10564  149 ASN   C ND2   
5221 N  N     . GLY   D 151 ? 0.18454 0.34745 0.18243 -0.03531 -0.03847 0.06873  150 GLY   C N     
5222 C  CA    . GLY   D 151 ? 0.16933 0.32684 0.19740 -0.00537 0.01672  0.07953  150 GLY   C CA    
5223 C  C     . GLY   D 151 ? 0.16914 0.30383 0.17286 -0.03559 -0.03113 0.06939  150 GLY   C C     
5224 O  O     . GLY   D 151 ? 0.19438 0.29937 0.17306 -0.03207 -0.01741 0.05733  150 GLY   C O     
5225 N  N     . LYS   D 152 ? 0.18811 0.31389 0.19305 -0.05455 -0.05225 0.07635  151 LYS   C N     
5226 C  CA    . LYS   D 152 ? 0.17231 0.32920 0.21733 -0.06803 -0.06247 0.09707  151 LYS   C CA    
5227 C  C     . LYS   D 152 ? 0.16634 0.36793 0.20954 -0.05609 -0.05538 0.08926  151 LYS   C C     
5228 O  O     . LYS   D 152 ? 0.20052 0.39399 0.20465 -0.03296 -0.03100 0.05488  151 LYS   C O     
5229 C  CB    . LYS   D 152 ? 0.22634 0.35522 0.29521 -0.09270 -0.06000 0.11421  151 LYS   C CB    
5230 C  CG    . LYS   D 152 ? 0.30345 0.36667 0.35345 -0.08762 -0.03982 0.10538  151 LYS   C CG    
5231 C  CD    . LYS   D 152 ? 0.39945 0.38954 0.40456 -0.04576 -0.04839 0.04944  151 LYS   C CD    
5232 C  CE    . LYS   D 152 ? 0.44767 0.40503 0.45143 0.00965  0.02056  0.00266  151 LYS   C CE    
5233 N  NZ    . LYS   D 152 ? 0.51307 0.41962 0.46863 0.00027  0.02661  0.00338  151 LYS   C NZ    
5234 N  N     . THR   D 153 ? 0.20572 0.37814 0.22372 -0.06647 -0.06510 0.10846  152 THR   C N     
5235 C  CA    . THR   D 153 ? 0.19046 0.40427 0.22494 -0.04782 -0.06209 0.08856  152 THR   C CA    
5236 C  C     . THR   D 153 ? 0.21219 0.41849 0.24663 -0.04809 -0.03599 0.07861  152 THR   C C     
5237 O  O     . THR   D 153 ? 0.25941 0.41315 0.25228 -0.08547 -0.06098 0.08974  152 THR   C O     
5238 C  CB    . THR   D 153 ? 0.18604 0.39865 0.21210 -0.02635 0.00937  0.10405  152 THR   C CB    
5239 O  OG1   . THR   D 153 ? 0.20740 0.38027 0.26285 -0.00644 -0.03319 0.11246  152 THR   C OG1   
5240 C  CG2   . THR   D 153 ? 0.20215 0.40819 0.21476 -0.03452 -0.02066 0.13961  152 THR   C CG2   
5241 N  N     . SER   D 154 ? 0.21696 0.44609 0.21737 -0.03387 -0.06627 0.07313  153 SER   C N     
5242 C  CA    . SER   D 154 ? 0.23047 0.47234 0.22806 -0.02740 -0.05368 0.08459  153 SER   C CA    
5243 C  C     . SER   D 154 ? 0.25153 0.47982 0.24626 -0.03096 -0.07662 0.11187  153 SER   C C     
5244 O  O     . SER   D 154 ? 0.31169 0.50171 0.24057 -0.03299 -0.06915 0.13634  153 SER   C O     
5245 C  CB    . SER   D 154 ? 0.27604 0.49953 0.25197 -0.03716 -0.01647 0.06434  153 SER   C CB    
5246 O  OG    . SER   D 154 ? 0.33252 0.52014 0.26022 -0.04394 -0.00693 0.06383  153 SER   C OG    
5247 N  N     . LYS   D 155 ? 0.21740 0.44879 0.27567 -0.05096 -0.08685 0.10137  154 LYS   C N     
5248 C  CA    . LYS   D 155 ? 0.25315 0.41496 0.26103 -0.06596 -0.09788 0.07184  154 LYS   C CA    
5249 C  C     . LYS   D 155 ? 0.24748 0.37988 0.21513 -0.03749 -0.07747 0.06868  154 LYS   C C     
5250 O  O     . LYS   D 155 ? 0.22296 0.40042 0.21581 -0.03116 -0.06765 0.06804  154 LYS   C O     
5251 C  CB    . LYS   D 155 ? 0.19764 0.43489 0.29675 -0.08207 -0.06935 0.04139  154 LYS   C CB    
5252 C  CG    . LYS   D 155 ? 0.23802 0.44663 0.25952 -0.10155 -0.06687 0.04393  154 LYS   C CG    
5253 C  CD    . LYS   D 155 ? 0.31606 0.46212 0.29164 -0.13927 -0.05072 0.04725  154 LYS   C CD    
5254 C  CE    . LYS   D 155 ? 0.52136 0.46823 0.28608 -0.15887 -0.08541 0.04056  154 LYS   C CE    
5255 N  NZ    . LYS   D 155 ? 0.69827 0.48073 0.34483 -0.16047 -0.08133 0.02114  154 LYS   C NZ    
5256 N  N     . LYS   D 156 ? 0.24249 0.33847 0.20054 -0.03183 -0.09664 0.04231  155 LYS   C N     
5257 C  CA    . LYS   D 156 ? 0.26563 0.28821 0.19788 -0.02099 -0.09274 0.00333  155 LYS   C CA    
5258 C  C     . LYS   D 156 ? 0.25771 0.25724 0.15080 -0.00734 -0.07892 0.02551  155 LYS   C C     
5259 O  O     . LYS   D 156 ? 0.21221 0.25224 0.21529 -0.02036 -0.08791 0.02355  155 LYS   C O     
5260 C  CB    . LYS   D 156 ? 0.36836 0.27576 0.20267 -0.03922 -0.07772 0.01995  155 LYS   C CB    
5261 C  CG    . LYS   D 156 ? 0.38022 0.26009 0.20095 -0.00121 -0.04126 0.04286  155 LYS   C CG    
5262 C  CD    . LYS   D 156 ? 0.41868 0.26695 0.23683 0.02118  -0.00882 0.02715  155 LYS   C CD    
5263 C  CE    . LYS   D 156 ? 0.45683 0.29404 0.24925 -0.00392 -0.02178 -0.00038 155 LYS   C CE    
5264 N  NZ    . LYS   D 156 ? 0.45227 0.32499 0.27365 0.01948  0.02395  0.02112  155 LYS   C NZ    
5265 N  N     . ILE   D 157 ? 0.22296 0.23526 0.14418 -0.03217 -0.06792 0.01111  156 ILE   C N     
5266 C  CA    . ILE   D 157 ? 0.17230 0.23757 0.15823 -0.00200 -0.02573 0.02588  156 ILE   C CA    
5267 C  C     . ILE   D 157 ? 0.18565 0.24138 0.13090 -0.01764 -0.00918 0.00675  156 ILE   C C     
5268 O  O     . ILE   D 157 ? 0.17178 0.29693 0.18776 0.00738  -0.04179 -0.01285 156 ILE   C O     
5269 C  CB    . ILE   D 157 ? 0.20518 0.21995 0.17355 0.02813  -0.03064 0.00815  156 ILE   C CB    
5270 C  CG1   . ILE   D 157 ? 0.25018 0.25813 0.17059 -0.00639 -0.03052 -0.00993 156 ILE   C CG1   
5271 C  CG2   . ILE   D 157 ? 0.19885 0.22019 0.26261 0.01932  -0.08059 0.02268  156 ILE   C CG2   
5272 C  CD1   . ILE   D 157 ? 0.30575 0.28247 0.20246 -0.01404 -0.06040 -0.00848 156 ILE   C CD1   
5273 N  N     . THR   D 158 ? 0.19928 0.24366 0.14356 -0.01029 -0.01860 0.02031  157 THR   C N     
5274 C  CA    . THR   D 158 ? 0.17717 0.22551 0.16653 -0.00623 -0.04561 0.00335  157 THR   C CA    
5275 C  C     . THR   D 158 ? 0.15759 0.20228 0.16879 -0.01070 -0.01445 -0.01074 157 THR   C C     
5276 O  O     . THR   D 158 ? 0.18447 0.22075 0.18191 -0.01870 -0.04127 -0.02297 157 THR   C O     
5277 C  CB    . THR   D 158 ? 0.21325 0.21351 0.21238 -0.00690 -0.03907 0.01251  157 THR   C CB    
5278 O  OG1   . THR   D 158 ? 0.18450 0.23753 0.23964 -0.01346 -0.06103 0.02705  157 THR   C OG1   
5279 C  CG2   . THR   D 158 ? 0.25358 0.20908 0.26267 -0.02425 -0.06899 0.02793  157 THR   C CG2   
5280 N  N     . ILE   D 159 ? 0.17500 0.21686 0.15371 -0.01228 -0.00306 -0.00651 158 ILE   C N     
5281 C  CA    . ILE   D 159 ? 0.14071 0.22540 0.18333 -0.02155 -0.00084 -0.01112 158 ILE   C CA    
5282 C  C     . ILE   D 159 ? 0.14809 0.22600 0.23035 -0.00025 -0.00492 -0.01479 158 ILE   C C     
5283 O  O     . ILE   D 159 ? 0.19929 0.23709 0.26544 0.01692  -0.01550 -0.01989 158 ILE   C O     
5284 C  CB    . ILE   D 159 ? 0.17021 0.23155 0.18625 -0.02836 -0.00917 -0.00383 158 ILE   C CB    
5285 C  CG1   . ILE   D 159 ? 0.15033 0.22189 0.21503 -0.02499 -0.01064 -0.00974 158 ILE   C CG1   
5286 C  CG2   . ILE   D 159 ? 0.18262 0.21868 0.18893 -0.03424 0.01776  0.02667  158 ILE   C CG2   
5287 C  CD1   . ILE   D 159 ? 0.17901 0.20211 0.18516 0.00488  -0.02095 -0.01300 158 ILE   C CD1   
5288 N  N     . ALA   D 160 ? 0.15579 0.22748 0.20887 0.02413  -0.06064 -0.01884 159 ALA   C N     
5289 C  CA    . ALA   D 160 ? 0.18944 0.24608 0.23297 0.02176  -0.03094 -0.01456 159 ALA   C CA    
5290 C  C     . ALA   D 160 ? 0.18050 0.23530 0.26484 0.02631  -0.05103 0.00244  159 ALA   C C     
5291 O  O     . ALA   D 160 ? 0.20634 0.24766 0.30571 0.04501  -0.03218 0.04875  159 ALA   C O     
5292 C  CB    . ALA   D 160 ? 0.19550 0.30384 0.21728 0.05433  -0.04806 0.01300  159 ALA   C CB    
5293 N  N     . ASP   D 161 ? 0.16990 0.20807 0.24345 -0.01260 -0.03232 0.01768  160 ASP   C N     
5294 C  CA    . ASP   D 161 ? 0.12643 0.20943 0.24264 0.00104  -0.03660 0.03540  160 ASP   C CA    
5295 C  C     . ASP   D 161 ? 0.16917 0.20767 0.21692 -0.00566 -0.04365 0.03054  160 ASP   C C     
5296 O  O     . ASP   D 161 ? 0.15328 0.23720 0.20260 0.01986  -0.00838 0.01775  160 ASP   C O     
5297 C  CB    . ASP   D 161 ? 0.14624 0.26208 0.28314 -0.02283 -0.04434 0.06179  160 ASP   C CB    
5298 C  CG    . ASP   D 161 ? 0.20644 0.33395 0.26226 -0.05947 -0.07111 0.03534  160 ASP   C CG    
5299 O  OD1   . ASP   D 161 ? 0.17855 0.34113 0.26504 0.02643  -0.03750 0.04594  160 ASP   C OD1   
5300 O  OD2   . ASP   D 161 ? 0.27917 0.39547 0.31303 -0.10330 -0.03070 0.02293  160 ASP   C OD2   
5301 N  N     . CYS   D 162 ? 0.16180 0.21538 0.19252 -0.00088 -0.01317 0.02345  161 CYS   C N     
5302 C  CA    . CYS   D 162 ? 0.18364 0.21961 0.19077 0.00599  -0.04338 0.01354  161 CYS   C CA    
5303 C  C     . CYS   D 162 ? 0.15238 0.24102 0.22277 0.01206  -0.02233 0.03548  161 CYS   C C     
5304 O  O     . CYS   D 162 ? 0.17294 0.26881 0.27518 0.00688  -0.02021 0.01696  161 CYS   C O     
5305 C  CB    . CYS   D 162 ? 0.20188 0.18818 0.19348 -0.00074 -0.05618 0.01256  161 CYS   C CB    
5306 S  SG    . CYS   D 162 ? 0.18404 0.21022 0.23569 -0.00451 -0.00910 0.00616  161 CYS   C SG    
5307 N  N     . GLY   D 163 ? 0.15046 0.23655 0.21683 -0.02000 -0.01650 0.04859  162 GLY   C N     
5308 C  CA    . GLY   D 163 ? 0.18084 0.25797 0.22485 -0.01135 -0.01587 0.05051  162 GLY   C CA    
5309 C  C     . GLY   D 163 ? 0.17291 0.24450 0.22266 0.01159  -0.02519 0.04767  162 GLY   C C     
5310 O  O     . GLY   D 163 ? 0.17331 0.21253 0.23053 0.00294  -0.03395 0.03080  162 GLY   C O     
5311 N  N     . GLN   D 164 ? 0.16646 0.25545 0.23948 -0.02282 -0.02128 0.06847  163 GLN   C N     
5312 C  CA    . GLN   D 164 ? 0.17222 0.26619 0.24723 -0.04000 -0.02774 0.08854  163 GLN   C CA    
5313 C  C     . GLN   D 164 ? 0.22642 0.30042 0.27265 -0.01904 -0.03560 0.07822  163 GLN   C C     
5314 O  O     . GLN   D 164 ? 0.18857 0.30615 0.32385 -0.02750 -0.03944 0.02545  163 GLN   C O     
5315 C  CB    . GLN   D 164 ? 0.19378 0.25722 0.24636 -0.02598 -0.02775 0.06155  163 GLN   C CB    
5316 C  CG    . GLN   D 164 ? 0.21620 0.25885 0.28061 -0.02537 -0.02642 0.07853  163 GLN   C CG    
5317 C  CD    . GLN   D 164 ? 0.21014 0.27115 0.32841 -0.02327 -0.00161 0.04214  163 GLN   C CD    
5318 O  OE1   . GLN   D 164 ? 0.20750 0.29207 0.26237 -0.02614 0.00969  0.04906  163 GLN   C OE1   
5319 N  NE2   . GLN   D 164 ? 0.22747 0.25273 0.32746 -0.02856 0.02549  0.02090  163 GLN   C NE2   
5320 N  N     . LEU   D 165 ? 0.19277 0.32815 0.33123 -0.04876 -0.09057 0.06542  164 LEU   C N     
5321 C  CA    . LEU   D 165 ? 0.25479 0.36339 0.40369 -0.10606 -0.08816 0.04265  164 LEU   C CA    
5322 C  C     . LEU   D 165 ? 0.35687 0.41012 0.48929 -0.16430 -0.06283 0.03727  164 LEU   C C     
5323 O  O     . LEU   D 165 ? 0.38314 0.40380 0.47453 -0.17956 -0.08929 0.07982  164 LEU   C O     
5324 C  CB    . LEU   D 165 ? 0.33908 0.35259 0.38103 -0.11238 -0.08132 0.03783  164 LEU   C CB    
5325 C  CG    . LEU   D 165 ? 0.37078 0.37404 0.41827 -0.09097 -0.02947 0.02895  164 LEU   C CG    
5326 C  CD1   . LEU   D 165 ? 0.41160 0.38179 0.41430 -0.07669 -0.06070 0.00487  164 LEU   C CD1   
5327 C  CD2   . LEU   D 165 ? 0.33879 0.37439 0.43709 -0.10260 -0.01322 0.04734  164 LEU   C CD2   
5328 N  N     . GLU   D 166 ? 0.52520 0.47418 0.58006 -0.16934 -0.00104 0.03193  165 GLU   C N     
5329 C  CA    . GLU   D 166 ? 0.74432 0.56335 0.68257 -0.10987 0.10181  0.03843  165 GLU   C CA    
5330 C  C     . GLU   D 166 ? 0.89191 0.59994 0.71490 -0.05596 0.23588  0.05239  165 GLU   C C     
5331 O  O     . GLU   D 166 ? 0.93160 0.62109 0.72912 -0.04931 0.26168  0.05221  165 GLU   C O     
5332 C  CB    . GLU   D 166 ? 0.78889 0.61822 0.76138 -0.11588 -0.01169 0.01291  165 GLU   C CB    
5333 C  CG    . GLU   D 166 ? 0.86771 0.67100 0.84394 -0.10707 -0.08555 -0.00382 165 GLU   C CG    
5334 C  CD    . GLU   D 166 ? 0.94745 0.71140 0.91008 -0.11801 -0.15688 -0.01875 165 GLU   C CD    
5335 O  OE1   . GLU   D 166 ? 0.93730 0.72290 0.93771 -0.12633 -0.17871 -0.01997 165 GLU   C OE1   
5336 O  OE2   . GLU   D 166 ? 1.02590 0.72550 0.92402 -0.11651 -0.18277 -0.02659 165 GLU   C OE2   
5337 O  OXT   . GLU   D 166 ? 0.94524 0.60502 0.72907 -0.02912 0.31172  0.04887  165 GLU   C OXT   
5338 P  PG    . GNP   E .   ? 0.13716 0.20641 0.18129 0.02743  -0.02261 0.02740  201 GNP   A PG    
5339 O  O1G   . GNP   E .   ? 0.21429 0.19402 0.21058 -0.00090 -0.02982 -0.01524 201 GNP   A O1G   
5340 O  O2G   . GNP   E .   ? 0.18968 0.19196 0.21579 0.02071  -0.01208 0.02315  201 GNP   A O2G   
5341 O  O3G   . GNP   E .   ? 0.20135 0.23336 0.23681 0.02306  -0.03713 0.00008  201 GNP   A O3G   
5342 N  N3B   . GNP   E .   ? 0.14948 0.20230 0.21591 -0.00618 -0.02095 0.00529  201 GNP   A N3B   
5343 P  PB    . GNP   E .   ? 0.13446 0.18456 0.20259 0.00464  -0.04479 0.01926  201 GNP   A PB    
5344 O  O1B   . GNP   E .   ? 0.15374 0.20611 0.17428 -0.00577 -0.02615 0.02266  201 GNP   A O1B   
5345 O  O2B   . GNP   E .   ? 0.12190 0.19582 0.20671 0.00938  -0.01674 -0.02982 201 GNP   A O2B   
5346 O  O3A   . GNP   E .   ? 0.17198 0.21432 0.20698 -0.03327 -0.04768 -0.00042 201 GNP   A O3A   
5347 P  PA    . GNP   E .   ? 0.15111 0.20659 0.22238 -0.00305 -0.03524 0.00688  201 GNP   A PA    
5348 O  O1A   . GNP   E .   ? 0.14180 0.21769 0.25030 -0.00856 -0.04691 0.01928  201 GNP   A O1A   
5349 O  O2A   . GNP   E .   ? 0.21728 0.20997 0.21083 -0.00868 -0.05182 0.01680  201 GNP   A O2A   
5350 O  "O5'" . GNP   E .   ? 0.16106 0.19634 0.22497 0.00229  -0.06434 -0.01425 201 GNP   A "O5'" 
5351 C  "C5'" . GNP   E .   ? 0.16563 0.23069 0.24805 -0.01246 -0.09322 -0.03032 201 GNP   A "C5'" 
5352 C  "C4'" . GNP   E .   ? 0.17810 0.23971 0.25214 -0.02038 -0.06357 -0.01003 201 GNP   A "C4'" 
5353 O  "O4'" . GNP   E .   ? 0.18741 0.22355 0.25513 -0.02216 -0.08707 -0.01253 201 GNP   A "O4'" 
5354 C  "C3'" . GNP   E .   ? 0.15826 0.25480 0.29915 -0.03382 -0.05883 0.00551  201 GNP   A "C3'" 
5355 O  "O3'" . GNP   E .   ? 0.16228 0.30366 0.33410 -0.01304 -0.08604 -0.00903 201 GNP   A "O3'" 
5356 C  "C2'" . GNP   E .   ? 0.15539 0.25036 0.30355 -0.04941 -0.06495 -0.01171 201 GNP   A "C2'" 
5357 O  "O2'" . GNP   E .   ? 0.16254 0.26945 0.34940 -0.04112 -0.04784 -0.01032 201 GNP   A "O2'" 
5358 C  "C1'" . GNP   E .   ? 0.18319 0.24775 0.25736 -0.01214 -0.06829 0.00686  201 GNP   A "C1'" 
5359 N  N9    . GNP   E .   ? 0.17380 0.24954 0.26579 -0.02596 -0.06311 -0.00986 201 GNP   A N9    
5360 C  C8    . GNP   E .   ? 0.16329 0.23879 0.25286 -0.01202 -0.06626 0.01274  201 GNP   A C8    
5361 N  N7    . GNP   E .   ? 0.13271 0.24022 0.22953 -0.01517 -0.03533 -0.01643 201 GNP   A N7    
5362 C  C5    . GNP   E .   ? 0.18311 0.22218 0.21483 -0.00833 -0.06747 0.02799  201 GNP   A C5    
5363 C  C6    . GNP   E .   ? 0.18809 0.23451 0.20442 -0.01872 -0.05929 0.00052  201 GNP   A C6    
5364 O  O6    . GNP   E .   ? 0.22385 0.20227 0.20905 0.00676  -0.08036 -0.00436 201 GNP   A O6    
5365 N  N1    . GNP   E .   ? 0.21194 0.25392 0.23158 -0.01587 -0.06175 -0.00160 201 GNP   A N1    
5366 C  C2    . GNP   E .   ? 0.18653 0.25802 0.27953 -0.02634 -0.02328 -0.02190 201 GNP   A C2    
5367 N  N2    . GNP   E .   ? 0.25856 0.26918 0.33863 -0.06921 -0.09902 -0.05452 201 GNP   A N2    
5368 N  N3    . GNP   E .   ? 0.15788 0.26889 0.30461 -0.03887 -0.02915 -0.04161 201 GNP   A N3    
5369 C  C4    . GNP   E .   ? 0.17963 0.25040 0.26189 -0.04357 -0.04313 -0.00574 201 GNP   A C4    
5370 C  C1    . A1AOV F .   ? 0.15003 0.18873 0.10469 0.00360  -0.01734 0.02255  202 A1AOV A C1    
5371 C  C10   . A1AOV F .   ? 0.21573 0.17216 0.21099 0.00421  -0.01996 0.00155  202 A1AOV A C10   
5372 C  C11   . A1AOV F .   ? 0.21283 0.18075 0.25511 0.03972  -0.05183 -0.01075 202 A1AOV A C11   
5373 C  C12   . A1AOV F .   ? 0.30609 0.17068 0.28999 0.03930  -0.08728 -0.03568 202 A1AOV A C12   
5374 C  C13   . A1AOV F .   ? 0.33969 0.24789 0.26469 0.04173  -0.06859 -0.04683 202 A1AOV A C13   
5375 C  C14   . A1AOV F .   ? 0.43913 0.36234 0.31859 0.14558  0.01617  0.02569  202 A1AOV A C14   
5376 C  C15   . A1AOV F .   ? 0.51407 0.40186 0.29975 0.23027  -0.04915 0.05948  202 A1AOV A C15   
5377 C  C16   . A1AOV F .   ? 0.49347 0.43270 0.29566 0.22846  -0.00251 0.09912  202 A1AOV A C16   
5378 C  C17   . A1AOV F .   ? 0.80248 0.55433 0.45541 0.20547  0.05857  0.12621  202 A1AOV A C17   
5379 C  C18   . A1AOV F .   ? 0.81691 0.57368 0.48632 0.20005  0.07754  0.12246  202 A1AOV A C18   
5380 C  C19   . A1AOV F .   ? 1.08975 0.64167 0.59272 0.19296  0.07173  0.13641  202 A1AOV A C19   
5381 C  C2    . A1AOV F .   ? 0.15075 0.16530 0.16802 0.00370  -0.01110 0.01546  202 A1AOV A C2    
5382 C  C20   . A1AOV F .   ? 1.07628 0.63912 0.60561 0.16300  0.07494  0.13336  202 A1AOV A C20   
5383 C  C21   . A1AOV F .   ? 0.82596 0.58094 0.50508 0.18406  0.06078  0.09986  202 A1AOV A C21   
5384 C  C22   . A1AOV F .   ? 0.21825 0.24787 0.27099 0.05833  -0.03262 -0.03062 202 A1AOV A C22   
5385 C  C23   . A1AOV F .   ? 0.14610 0.17278 0.15919 0.04460  0.01021  0.03385  202 A1AOV A C23   
5386 C  C24   . A1AOV F .   ? 0.15100 0.18196 0.18505 0.03941  -0.01145 0.04506  202 A1AOV A C24   
5387 C  C25   . A1AOV F .   ? 0.15944 0.22181 0.14110 -0.00063 -0.03691 0.01829  202 A1AOV A C25   
5388 C  C26   . A1AOV F .   ? 0.12700 0.19961 0.20035 -0.00426 -0.00778 0.01349  202 A1AOV A C26   
5389 C  C27   . A1AOV F .   ? 0.20331 0.18097 0.22163 0.01422  -0.03635 0.02079  202 A1AOV A C27   
5390 C  C28   . A1AOV F .   ? 0.16523 0.25690 0.15775 0.00081  -0.04250 0.02485  202 A1AOV A C28   
5391 C  C29   . A1AOV F .   ? 0.13684 0.17866 0.21411 -0.01309 -0.03739 0.00584  202 A1AOV A C29   
5392 C  C3    . A1AOV F .   ? 0.13424 0.19927 0.19820 0.02907  -0.00939 0.03951  202 A1AOV A C3    
5393 C  C30   . A1AOV F .   ? 0.14541 0.17625 0.19267 -0.00422 -0.01633 0.03174  202 A1AOV A C30   
5394 C  C31   . A1AOV F .   ? 0.14273 0.21455 0.19898 -0.00298 -0.01872 0.04771  202 A1AOV A C31   
5395 C  C32   . A1AOV F .   ? 0.17518 0.19272 0.20364 -0.03114 -0.02123 0.01822  202 A1AOV A C32   
5396 C  C33   . A1AOV F .   ? 0.16046 0.20380 0.23289 -0.03281 -0.03365 0.02439  202 A1AOV A C33   
5397 C  C34   . A1AOV F .   ? 0.19308 0.22618 0.20462 0.00422  -0.02648 0.03966  202 A1AOV A C34   
5398 C  C35   . A1AOV F .   ? 0.17813 0.27309 0.28615 -0.02629 0.02783  0.05096  202 A1AOV A C35   
5399 C  C36   . A1AOV F .   ? 0.17041 0.24827 0.23130 -0.01209 -0.01496 0.01316  202 A1AOV A C36   
5400 C  C37   . A1AOV F .   ? 0.19476 0.25187 0.22611 -0.06910 -0.02526 0.00671  202 A1AOV A C37   
5401 C  C38   . A1AOV F .   ? 0.18838 0.24431 0.23281 -0.05270 -0.01148 0.00432  202 A1AOV A C38   
5402 C  C39   . A1AOV F .   ? 0.17846 0.23039 0.23410 -0.04896 -0.02031 0.00616  202 A1AOV A C39   
5403 C  C4    . A1AOV F .   ? 0.14989 0.17998 0.16594 -0.00809 -0.00220 -0.01487 202 A1AOV A C4    
5404 C  C40   . A1AOV F .   ? 0.12293 0.24660 0.18172 0.01812  0.01748  0.04026  202 A1AOV A C40   
5405 C  C41   . A1AOV F .   ? 0.17906 0.26344 0.20780 0.01483  -0.03643 0.01562  202 A1AOV A C41   
5406 C  C42   . A1AOV F .   ? 0.15837 0.20131 0.22773 0.01014  -0.02325 0.01694  202 A1AOV A C42   
5407 C  C43   . A1AOV F .   ? 0.13458 0.19334 0.20326 -0.00627 -0.00902 0.00327  202 A1AOV A C43   
5408 C  C44   . A1AOV F .   ? 0.15737 0.19263 0.18038 0.00905  0.00755  -0.00244 202 A1AOV A C44   
5409 C  C45   . A1AOV F .   ? 0.10662 0.18110 0.23081 0.00272  -0.01989 0.02161  202 A1AOV A C45   
5410 C  C46   . A1AOV F .   ? 0.11049 0.16248 0.23786 0.02728  -0.01302 0.02407  202 A1AOV A C46   
5411 C  C47   . A1AOV F .   ? 0.13302 0.16243 0.19245 0.02493  -0.01647 0.01734  202 A1AOV A C47   
5412 C  C48   . A1AOV F .   ? 0.15113 0.15941 0.20070 0.01475  -0.01916 0.01134  202 A1AOV A C48   
5413 C  C49   . A1AOV F .   ? 0.14145 0.21097 0.15569 0.01690  -0.02750 0.02057  202 A1AOV A C49   
5414 C  C5    . A1AOV F .   ? 0.14174 0.15878 0.18597 -0.00897 -0.01910 0.01970  202 A1AOV A C5    
5415 C  C50   . A1AOV F .   ? 0.17985 0.21493 0.18775 0.02930  -0.01121 0.03157  202 A1AOV A C50   
5416 C  C51   . A1AOV F .   ? 0.18192 0.18822 0.19028 0.02171  -0.00575 0.04019  202 A1AOV A C51   
5417 C  C52   . A1AOV F .   ? 0.13371 0.16975 0.19338 0.02375  0.00134  0.03202  202 A1AOV A C52   
5418 C  C53   . A1AOV F .   ? 0.11412 0.21383 0.15877 0.03149  0.01165  0.03812  202 A1AOV A C53   
5419 C  C54   . A1AOV F .   ? 0.15879 0.18882 0.19985 0.01473  -0.02675 0.01869  202 A1AOV A C54   
5420 C  C55   . A1AOV F .   ? 0.20090 0.18513 0.16273 -0.00430 -0.03485 0.01895  202 A1AOV A C55   
5421 C  C56   . A1AOV F .   ? 0.21228 0.16300 0.17032 0.00703  -0.03850 -0.00753 202 A1AOV A C56   
5422 C  C6    . A1AOV F .   ? 0.21844 0.16158 0.16384 -0.00721 0.03222  0.01385  202 A1AOV A C6    
5423 C  C7    . A1AOV F .   ? 0.16060 0.20945 0.16921 0.00672  0.01252  0.00813  202 A1AOV A C7    
5424 C  C8    . A1AOV F .   ? 0.14329 0.18565 0.21290 0.00758  -0.01430 -0.04055 202 A1AOV A C8    
5425 C  C9    . A1AOV F .   ? 0.22831 0.16046 0.18089 -0.01714 0.01770  0.04702  202 A1AOV A C9    
5426 N  N1    . A1AOV F .   ? 0.14937 0.17911 0.15344 0.00307  -0.01203 0.01768  202 A1AOV A N1    
5427 N  N2    . A1AOV F .   ? 0.19913 0.16442 0.19111 0.01065  0.02929  0.02602  202 A1AOV A N2    
5428 N  N3    . A1AOV F .   ? 0.30130 0.27281 0.26849 0.08856  -0.02413 -0.03176 202 A1AOV A N3    
5429 N  N4    . A1AOV F .   ? 1.00617 0.61847 0.55249 0.19599  0.07589  0.13795  202 A1AOV A N4    
5430 N  N5    . A1AOV F .   ? 0.17565 0.17519 0.13385 0.01481  -0.01296 0.01450  202 A1AOV A N5    
5431 N  N6    . A1AOV F .   ? 0.10947 0.20428 0.17807 0.00086  -0.02777 0.01921  202 A1AOV A N6    
5432 N  N7    . A1AOV F .   ? 0.16931 0.25645 0.24776 -0.06223 -0.03352 0.04578  202 A1AOV A N7    
5433 N  N8    . A1AOV F .   ? 0.12569 0.21350 0.20201 0.00335  -0.04417 0.03395  202 A1AOV A N8    
5434 O  O1    . A1AOV F .   ? 0.15456 0.18543 0.15735 0.01011  0.00542  0.01314  202 A1AOV A O1    
5435 O  O2    . A1AOV F .   ? 0.37920 0.36206 0.31076 0.16381  0.02762  0.06392  202 A1AOV A O2    
5436 O  O3    . A1AOV F .   ? 0.15428 0.19135 0.23151 0.02941  0.00370  0.00982  202 A1AOV A O3    
5437 O  O4    . A1AOV F .   ? 0.16434 0.17378 0.16634 0.01024  -0.00049 -0.01291 202 A1AOV A O4    
5438 O  O5    . A1AOV F .   ? 0.13612 0.20460 0.18843 0.00038  -0.01335 0.00423  202 A1AOV A O5    
5439 O  O6    . A1AOV F .   ? 0.16081 0.24600 0.23382 -0.03179 -0.02913 0.04683  202 A1AOV A O6    
5440 O  O7    . A1AOV F .   ? 0.13199 0.19779 0.17534 -0.00216 -0.01694 0.03573  202 A1AOV A O7    
5441 MG MG    . MG    G .   ? 0.14906 0.18524 0.18500 0.00605  -0.00907 -0.00310 203 MG    A MG    
5442 P  PG    . GNP   H .   ? 0.21012 0.25094 0.24597 -0.00712 0.07698  0.06344  201 GNP   B PG    
5443 O  O1G   . GNP   H .   ? 0.21577 0.29778 0.35830 0.00449  0.09266  0.05937  201 GNP   B O1G   
5444 O  O2G   . GNP   H .   ? 0.21087 0.23085 0.28649 0.01246  0.06005  0.06463  201 GNP   B O2G   
5445 O  O3G   . GNP   H .   ? 0.25938 0.25148 0.25036 0.00752  0.04301  0.02145  201 GNP   B O3G   
5446 N  N3B   . GNP   H .   ? 0.30948 0.23520 0.25780 0.00364  0.12063  0.05635  201 GNP   B N3B   
5447 P  PB    . GNP   H .   ? 0.23592 0.22779 0.25031 0.01322  0.10635  0.06213  201 GNP   B PB    
5448 O  O1B   . GNP   H .   ? 0.26241 0.23573 0.31689 0.05463  0.10736  0.12106  201 GNP   B O1B   
5449 O  O2B   . GNP   H .   ? 0.22883 0.23554 0.26183 0.00131  0.06263  0.04587  201 GNP   B O2B   
5450 O  O3A   . GNP   H .   ? 0.28124 0.28570 0.26192 0.02963  0.11813  0.04748  201 GNP   B O3A   
5451 P  PA    . GNP   H .   ? 0.27823 0.28963 0.29763 0.03710  0.13578  0.05524  201 GNP   B PA    
5452 O  O1A   . GNP   H .   ? 0.23740 0.30183 0.28932 0.07157  0.11190  0.07895  201 GNP   B O1A   
5453 O  O2A   . GNP   H .   ? 0.27056 0.30485 0.31506 0.04736  0.11855  0.07474  201 GNP   B O2A   
5454 O  "O5'" . GNP   H .   ? 0.30341 0.27744 0.30261 0.05059  0.12306  0.07348  201 GNP   B "O5'" 
5455 C  "C5'" . GNP   H .   ? 0.31130 0.28493 0.32469 0.08235  0.14038  0.06091  201 GNP   B "C5'" 
5456 C  "C4'" . GNP   H .   ? 0.29463 0.31860 0.38553 0.05610  0.17098  0.07356  201 GNP   B "C4'" 
5457 O  "O4'" . GNP   H .   ? 0.27640 0.31308 0.36864 0.07806  0.16966  0.06051  201 GNP   B "O4'" 
5458 C  "C3'" . GNP   H .   ? 0.27855 0.34206 0.42480 0.05367  0.17737  0.09529  201 GNP   B "C3'" 
5459 O  "O3'" . GNP   H .   ? 0.29765 0.37340 0.45633 0.02392  0.18107  0.08604  201 GNP   B "O3'" 
5460 C  "C2'" . GNP   H .   ? 0.31621 0.32023 0.42775 0.07099  0.16457  0.09782  201 GNP   B "C2'" 
5461 O  "O2'" . GNP   H .   ? 0.34815 0.35285 0.46978 0.05990  0.17360  0.08729  201 GNP   B "O2'" 
5462 C  "C1'" . GNP   H .   ? 0.30504 0.30618 0.37976 0.09733  0.16816  0.09246  201 GNP   B "C1'" 
5463 N  N9    . GNP   H .   ? 0.31543 0.29656 0.38603 0.09081  0.18112  0.08174  201 GNP   B N9    
5464 C  C8    . GNP   H .   ? 0.29821 0.28662 0.36246 0.08479  0.18424  0.09156  201 GNP   B C8    
5465 N  N7    . GNP   H .   ? 0.38043 0.30938 0.34960 0.05385  0.21500  0.04401  201 GNP   B N7    
5466 C  C5    . GNP   H .   ? 0.38600 0.30187 0.35724 0.06016  0.21037  0.05337  201 GNP   B C5    
5467 C  C6    . GNP   H .   ? 0.40031 0.29432 0.34493 0.08218  0.20743  0.05224  201 GNP   B C6    
5468 O  O6    . GNP   H .   ? 0.38879 0.28350 0.30565 0.05221  0.17512  0.04587  201 GNP   B O6    
5469 N  N1    . GNP   H .   ? 0.39269 0.31248 0.38860 0.09631  0.21028  0.07072  201 GNP   B N1    
5470 C  C2    . GNP   H .   ? 0.38203 0.32530 0.43524 0.09113  0.18825  0.06779  201 GNP   B C2    
5471 N  N2    . GNP   H .   ? 0.36470 0.33677 0.46354 0.11421  0.19190  0.05216  201 GNP   B N2    
5472 N  N3    . GNP   H .   ? 0.35837 0.31019 0.40231 0.08241  0.21129  0.05207  201 GNP   B N3    
5473 C  C4    . GNP   H .   ? 0.38335 0.30525 0.38643 0.05609  0.21855  0.05053  201 GNP   B C4    
5474 C  C1    . A1AOV I .   ? 0.15017 0.20873 0.14668 0.00624  -0.00185 0.01764  202 A1AOV B C1    
5475 C  C10   . A1AOV I .   ? 0.17847 0.19557 0.27704 -0.02580 -0.02541 0.03334  202 A1AOV B C10   
5476 C  C11   . A1AOV I .   ? 0.16288 0.23048 0.40620 -0.05254 -0.03558 0.01393  202 A1AOV B C11   
5477 C  C12   . A1AOV I .   ? 0.24745 0.25976 0.43930 -0.00165 0.07693  -0.00625 202 A1AOV B C12   
5478 C  C13   . A1AOV I .   ? 0.33279 0.30047 0.41030 -0.08300 0.05790  0.01669  202 A1AOV B C13   
5479 C  C14   . A1AOV I .   ? 0.67593 0.38032 0.50897 -0.14312 0.06237  0.06236  202 A1AOV B C14   
5480 C  C15   . A1AOV I .   ? 0.72548 0.42469 0.45783 -0.15827 0.08470  0.09023  202 A1AOV B C15   
5481 C  C16   . A1AOV I .   ? 0.70573 0.44722 0.43961 -0.15970 0.10415  0.12014  202 A1AOV B C16   
5482 C  C17   . A1AOV I .   ? 0.87599 0.53806 0.62783 -0.12741 0.05489  0.15088  202 A1AOV B C17   
5483 C  C18   . A1AOV I .   ? 0.84135 0.55653 0.65410 -0.15962 0.07460  0.15736  202 A1AOV B C18   
5484 C  C19   . A1AOV I .   ? 0.99599 0.60845 0.73958 -0.06263 -0.00754 0.14624  202 A1AOV B C19   
5485 C  C2    . A1AOV I .   ? 0.14835 0.18175 0.20091 -0.01395 -0.02163 -0.00490 202 A1AOV B C2    
5486 C  C20   . A1AOV I .   ? 1.03818 0.60673 0.73159 -0.09091 0.00493  0.15515  202 A1AOV B C20   
5487 C  C21   . A1AOV I .   ? 0.90238 0.56606 0.66170 -0.10166 0.04939  0.13832  202 A1AOV B C21   
5488 C  C22   . A1AOV I .   ? 0.30934 0.27478 0.40709 -0.09110 -0.04949 0.01740  202 A1AOV B C22   
5489 C  C23   . A1AOV I .   ? 0.16296 0.22334 0.14040 -0.05687 0.00176  0.02903  202 A1AOV B C23   
5490 C  C24   . A1AOV I .   ? 0.16454 0.24207 0.15582 -0.01193 -0.02075 0.04621  202 A1AOV B C24   
5491 C  C25   . A1AOV I .   ? 0.14659 0.28565 0.11673 0.01496  0.03388  0.03888  202 A1AOV B C25   
5492 C  C26   . A1AOV I .   ? 0.14977 0.25976 0.19871 -0.03332 0.01730  0.04370  202 A1AOV B C26   
5493 C  C27   . A1AOV I .   ? 0.19465 0.26133 0.23627 -0.04559 -0.01399 0.02101  202 A1AOV B C27   
5494 C  C28   . A1AOV I .   ? 0.18731 0.27821 0.16817 -0.01421 0.03347  0.02573  202 A1AOV B C28   
5495 C  C29   . A1AOV I .   ? 0.15926 0.21791 0.21699 -0.01713 -0.02327 0.05008  202 A1AOV B C29   
5496 C  C3    . A1AOV I .   ? 0.17212 0.20221 0.19797 -0.01415 -0.01958 0.02896  202 A1AOV B C3    
5497 C  C30   . A1AOV I .   ? 0.15228 0.23181 0.21315 0.00204  -0.00230 0.05958  202 A1AOV B C30   
5498 C  C31   . A1AOV I .   ? 0.18781 0.25978 0.21032 -0.01221 0.03830  0.05515  202 A1AOV B C31   
5499 C  C32   . A1AOV I .   ? 0.16914 0.26563 0.20321 0.00701  -0.01338 0.04478  202 A1AOV B C32   
5500 C  C33   . A1AOV I .   ? 0.14726 0.30363 0.22892 0.03207  0.01289  0.04321  202 A1AOV B C33   
5501 C  C34   . A1AOV I .   ? 0.17349 0.33197 0.20725 -0.00265 0.00285  0.05020  202 A1AOV B C34   
5502 C  C35   . A1AOV I .   ? 0.21389 0.33720 0.18505 0.01044  -0.03247 0.10470  202 A1AOV B C35   
5503 C  C36   . A1AOV I .   ? 0.21456 0.35541 0.20002 0.01269  0.00509  0.05979  202 A1AOV B C36   
5504 C  C37   . A1AOV I .   ? 0.16207 0.34362 0.24039 0.05844  0.00807  0.05028  202 A1AOV B C37   
5505 C  C38   . A1AOV I .   ? 0.20996 0.32227 0.23398 0.02804  0.00167  0.06069  202 A1AOV B C38   
5506 C  C39   . A1AOV I .   ? 0.19487 0.29963 0.22556 0.01185  -0.00483 0.06006  202 A1AOV B C39   
5507 C  C4    . A1AOV I .   ? 0.18089 0.17592 0.17423 -0.04242 -0.04307 0.00818  202 A1AOV B C4    
5508 C  C40   . A1AOV I .   ? 0.11758 0.33363 0.20133 -0.04116 -0.00624 0.06125  202 A1AOV B C40   
5509 C  C41   . A1AOV I .   ? 0.20746 0.33048 0.21605 -0.03945 0.02444  0.05734  202 A1AOV B C41   
5510 C  C42   . A1AOV I .   ? 0.16225 0.24426 0.23514 -0.01091 -0.00464 0.04036  202 A1AOV B C42   
5511 C  C43   . A1AOV I .   ? 0.14775 0.23592 0.22339 -0.01520 -0.00854 0.05163  202 A1AOV B C43   
5512 C  C44   . A1AOV I .   ? 0.13827 0.25308 0.20591 -0.01820 0.00968  0.05226  202 A1AOV B C44   
5513 C  C45   . A1AOV I .   ? 0.15154 0.24951 0.19811 0.00726  -0.00204 0.04288  202 A1AOV B C45   
5514 C  C46   . A1AOV I .   ? 0.12793 0.25472 0.21215 -0.01676 -0.01610 0.01235  202 A1AOV B C46   
5515 C  C47   . A1AOV I .   ? 0.16224 0.22968 0.19059 -0.02449 0.01511  0.05445  202 A1AOV B C47   
5516 C  C48   . A1AOV I .   ? 0.16607 0.21802 0.20363 -0.02316 0.01907  0.03151  202 A1AOV B C48   
5517 C  C49   . A1AOV I .   ? 0.17277 0.22954 0.21356 -0.03260 -0.00485 0.05915  202 A1AOV B C49   
5518 C  C5    . A1AOV I .   ? 0.17357 0.15963 0.19785 -0.03140 -0.01221 0.02047  202 A1AOV B C5    
5519 C  C50   . A1AOV I .   ? 0.19911 0.22378 0.22505 -0.04454 -0.03410 0.06153  202 A1AOV B C50   
5520 C  C51   . A1AOV I .   ? 0.16044 0.18792 0.22334 -0.03910 -0.04353 0.07049  202 A1AOV B C51   
5521 C  C52   . A1AOV I .   ? 0.20633 0.17918 0.18602 -0.03262 -0.02085 0.05271  202 A1AOV B C52   
5522 C  C53   . A1AOV I .   ? 0.18132 0.21705 0.15941 -0.03967 -0.00869 0.04587  202 A1AOV B C53   
5523 C  C54   . A1AOV I .   ? 0.18293 0.23426 0.16419 -0.03075 -0.00532 0.01494  202 A1AOV B C54   
5524 C  C55   . A1AOV I .   ? 0.12755 0.24019 0.17879 -0.00127 0.03618  0.01268  202 A1AOV B C55   
5525 C  C56   . A1AOV I .   ? 0.12369 0.20993 0.17263 -0.04281 0.00817  0.01730  202 A1AOV B C56   
5526 C  C6    . A1AOV I .   ? 0.21895 0.14464 0.20809 -0.02926 -0.02072 0.00809  202 A1AOV B C6    
5527 C  C7    . A1AOV I .   ? 0.17677 0.17836 0.23511 -0.01346 -0.02141 0.02446  202 A1AOV B C7    
5528 C  C8    . A1AOV I .   ? 0.22172 0.18491 0.18700 -0.00854 -0.02638 -0.00704 202 A1AOV B C8    
5529 C  C9    . A1AOV I .   ? 0.22341 0.19384 0.28441 -0.03592 -0.04438 0.08439  202 A1AOV B C9    
5530 N  N1    . A1AOV I .   ? 0.17168 0.16256 0.16442 -0.01207 -0.00786 0.04898  202 A1AOV B N1    
5531 N  N2    . A1AOV I .   ? 0.20317 0.16066 0.23807 -0.02403 -0.03681 0.03237  202 A1AOV B N2    
5532 N  N3    . A1AOV I .   ? 0.38287 0.31230 0.44305 -0.11768 0.00692  0.03038  202 A1AOV B N3    
5533 N  N4    . A1AOV I .   ? 0.97839 0.58701 0.71010 -0.09125 -0.00220 0.15710  202 A1AOV B N4    
5534 N  N5    . A1AOV I .   ? 0.12706 0.20677 0.14463 -0.03470 0.02288  0.04054  202 A1AOV B N5    
5535 N  N6    . A1AOV I .   ? 0.11581 0.21029 0.15595 -0.01062 0.01714  0.01552  202 A1AOV B N6    
5536 N  N7    . A1AOV I .   ? 0.18097 0.33549 0.21666 0.05703  0.01455  0.04389  202 A1AOV B N7    
5537 N  N8    . A1AOV I .   ? 0.15367 0.26605 0.21956 -0.00756 0.02400  0.06875  202 A1AOV B N8    
5538 O  O1    . A1AOV I .   ? 0.17957 0.17337 0.18008 -0.01927 -0.01234 0.01804  202 A1AOV B O1    
5539 O  O2    . A1AOV I .   ? 0.83026 0.39201 0.58478 -0.14413 0.08834  0.06588  202 A1AOV B O2    
5540 O  O3    . A1AOV I .   ? 0.19352 0.18727 0.27856 -0.04718 -0.02361 -0.00529 202 A1AOV B O3    
5541 O  O4    . A1AOV I .   ? 0.18003 0.18709 0.17096 -0.03752 -0.02157 0.02242  202 A1AOV B O4    
5542 O  O5    . A1AOV I .   ? 0.13488 0.26345 0.17127 -0.00281 -0.03319 0.00455  202 A1AOV B O5    
5543 O  O6    . A1AOV I .   ? 0.15623 0.34205 0.18221 -0.01813 0.01083  0.06629  202 A1AOV B O6    
5544 O  O7    . A1AOV I .   ? 0.16090 0.24728 0.14505 -0.01200 0.01172  0.02892  202 A1AOV B O7    
5545 MG MG    . MG    J .   ? 0.20851 0.25230 0.24921 0.00159  0.05183  0.05229  203 MG    B MG    
5546 O  O     . HOH   K .   ? 0.64384 0.41763 0.80459 -0.04257 0.09851  0.06737  301 HOH   A O     
5547 O  O     . HOH   K .   ? 0.71056 0.81435 0.59930 0.02061  0.28193  -0.05613 302 HOH   A O     
5548 O  O     . HOH   K .   ? 0.61608 0.59481 0.47573 -0.09984 0.14881  -0.04978 303 HOH   A O     
5549 O  O     . HOH   K .   ? 0.68376 0.36277 0.61808 0.07831  -0.11989 -0.24065 304 HOH   A O     
5550 O  O     . HOH   K .   ? 1.15800 0.48657 0.90794 -0.02976 -0.03783 -0.34423 305 HOH   A O     
5551 O  O     . HOH   K .   ? 0.37936 0.26248 0.42329 0.00367  0.01139  0.14038  306 HOH   A O     
5552 O  O     . HOH   K .   ? 0.60491 0.80772 0.52875 0.04391  0.27926  0.15183  307 HOH   A O     
5553 O  O     . HOH   K .   ? 0.23027 0.69748 0.31234 0.01542  -0.06080 0.04292  308 HOH   A O     
5554 O  O     . HOH   K .   ? 0.47689 0.31785 0.45943 0.01247  0.16669  -0.05594 309 HOH   A O     
5555 O  O     . HOH   K .   ? 0.55260 0.89634 0.88420 -0.25502 0.09703  -0.11589 310 HOH   A O     
5556 O  O     . HOH   K .   ? 0.41934 0.82543 0.89092 0.17012  -0.20479 -0.39839 311 HOH   A O     
5557 O  O     . HOH   K .   ? 0.46218 0.74267 0.96944 0.02500  -0.08250 0.46752  312 HOH   A O     
5558 O  O     . HOH   K .   ? 0.49648 0.47948 0.81933 -0.01288 0.24702  -0.26467 313 HOH   A O     
5559 O  O     . HOH   K .   ? 0.14480 0.19900 0.21544 0.00695  -0.01029 -0.04829 314 HOH   A O     
5560 O  O     . HOH   K .   ? 0.56088 0.52548 0.82905 -0.16522 -0.25778 0.24235  315 HOH   A O     
5561 O  O     . HOH   K .   ? 0.92096 0.39502 0.55679 0.07546  -0.39939 -0.06566 316 HOH   A O     
5562 O  O     . HOH   K .   ? 0.53822 0.48316 0.59349 -0.15444 -0.27531 0.05291  317 HOH   A O     
5563 O  O     . HOH   K .   ? 0.34610 0.48378 0.68810 0.03543  -0.04659 0.18049  318 HOH   A O     
5564 O  O     . HOH   K .   ? 0.57883 0.70789 0.50919 -0.07883 -0.16664 0.25843  319 HOH   A O     
5565 O  O     . HOH   K .   ? 0.57287 0.38204 0.50103 0.20545  0.04144  0.17568  320 HOH   A O     
5566 O  O     . HOH   K .   ? 0.63137 0.60539 0.55064 -0.33797 0.11943  0.03545  321 HOH   A O     
5567 O  O     A HOH   K .   ? 0.28640 0.44863 0.46737 0.14828  0.14753  0.03026  322 HOH   A O     
5568 O  O     B HOH   K .   ? 0.23620 0.47284 0.62541 0.12156  0.05107  -0.03556 322 HOH   A O     
5569 O  O     . HOH   K .   ? 0.79816 0.31868 0.70438 0.02898  0.15894  0.12206  323 HOH   A O     
5570 O  O     . HOH   K .   ? 0.57977 0.36214 0.38742 -0.06674 0.00840  -0.11800 324 HOH   A O     
5571 O  O     . HOH   K .   ? 0.23696 0.48732 0.29613 -0.00990 0.01479  0.09304  325 HOH   A O     
5572 O  O     . HOH   K .   ? 0.42017 0.61304 0.59730 0.01136  0.14416  0.10162  326 HOH   A O     
5573 O  O     . HOH   K .   ? 0.44861 0.75488 0.32674 -0.12681 0.04417  -0.15555 327 HOH   A O     
5574 O  O     . HOH   K .   ? 0.55095 0.67950 0.36673 0.10209  -0.13051 -0.03909 328 HOH   A O     
5575 O  O     . HOH   K .   ? 0.54748 0.42201 0.73028 -0.10664 0.21772  0.03104  329 HOH   A O     
5576 O  O     . HOH   K .   ? 0.85550 0.29668 0.61985 -0.09585 -0.33779 0.07465  330 HOH   A O     
5577 O  O     . HOH   K .   ? 0.44959 0.54936 0.61244 0.19098  -0.13732 0.07822  331 HOH   A O     
5578 O  O     . HOH   K .   ? 0.79798 0.65120 0.42774 0.36102  -0.18648 -0.03703 332 HOH   A O     
5579 O  O     . HOH   K .   ? 0.37675 0.36389 0.57765 -0.16227 -0.13869 -0.05373 333 HOH   A O     
5580 O  O     . HOH   K .   ? 0.43875 0.91806 0.28925 0.23428  0.05270  0.13700  334 HOH   A O     
5581 O  O     . HOH   K .   ? 0.54119 0.67994 0.58434 -0.32606 0.15771  -0.20460 335 HOH   A O     
5582 O  O     . HOH   K .   ? 0.37829 0.87839 0.67238 0.02811  -0.22171 0.15442  336 HOH   A O     
5583 O  O     . HOH   K .   ? 0.37990 0.47516 0.48084 0.07910  -0.15926 -0.20334 337 HOH   A O     
5584 O  O     . HOH   K .   ? 0.14782 0.21400 0.27403 0.00061  0.01311  -0.01119 338 HOH   A O     
5585 O  O     . HOH   K .   ? 0.27934 0.27797 0.24438 0.03318  -0.02385 0.02838  339 HOH   A O     
5586 O  O     . HOH   K .   ? 0.25659 0.43950 0.38478 -0.01243 -0.15680 0.10886  340 HOH   A O     
5587 O  O     . HOH   K .   ? 0.75088 0.42332 0.65794 -0.17620 -0.02566 -0.24433 341 HOH   A O     
5588 O  O     . HOH   K .   ? 0.64655 0.36946 0.51058 0.00676  0.09812  0.07271  342 HOH   A O     
5589 O  O     . HOH   K .   ? 0.65065 0.21463 0.49981 0.05443  -0.23854 -0.02291 343 HOH   A O     
5590 O  O     . HOH   K .   ? 0.15711 0.20873 0.32793 -0.00098 -0.01575 0.03944  344 HOH   A O     
5591 O  O     . HOH   K .   ? 0.26494 0.60800 0.41646 0.12814  -0.00641 0.14927  345 HOH   A O     
5592 O  O     . HOH   K .   ? 0.22390 0.28115 0.27508 0.00993  -0.05307 0.03256  346 HOH   A O     
5593 O  O     . HOH   K .   ? 0.25297 0.34804 0.17826 0.02030  -0.05939 -0.02212 347 HOH   A O     
5594 O  O     . HOH   K .   ? 0.61973 0.71464 0.59637 -0.37163 0.13262  -0.00985 348 HOH   A O     
5595 O  O     . HOH   K .   ? 0.14439 0.24439 0.24399 0.00778  -0.00355 0.06869  349 HOH   A O     
5596 O  O     . HOH   K .   ? 0.12993 0.22868 0.22613 0.01369  -0.02723 0.00610  350 HOH   A O     
5597 O  O     . HOH   K .   ? 0.80907 0.44362 0.68591 0.24135  0.19540  -0.09929 351 HOH   A O     
5598 O  O     . HOH   K .   ? 0.47052 0.29577 0.45156 0.01883  -0.12537 -0.12603 352 HOH   A O     
5599 O  O     . HOH   K .   ? 0.49989 0.50002 1.14255 -0.16720 0.19666  0.03491  353 HOH   A O     
5600 O  O     . HOH   K .   ? 0.41846 0.22167 0.18877 -0.06009 0.01094  0.01127  354 HOH   A O     
5601 O  O     . HOH   K .   ? 0.75015 0.33857 0.59932 -0.05781 -0.10145 0.09936  355 HOH   A O     
5602 O  O     . HOH   K .   ? 0.41167 0.94878 0.47473 -0.28896 0.09532  -0.13630 356 HOH   A O     
5603 O  O     . HOH   K .   ? 0.32493 0.25074 0.37675 0.01142  -0.07490 0.00589  357 HOH   A O     
5604 O  O     . HOH   K .   ? 0.17161 0.18908 0.45371 -0.00391 0.01344  -0.07357 358 HOH   A O     
5605 O  O     . HOH   K .   ? 0.48904 0.70765 0.75848 -0.02783 -0.17989 -0.35149 359 HOH   A O     
5606 O  O     . HOH   K .   ? 0.16015 0.27703 0.19612 -0.01394 0.01661  0.01877  360 HOH   A O     
5607 O  O     . HOH   K .   ? 0.34425 0.62505 0.55004 -0.03483 -0.17756 0.23473  361 HOH   A O     
5608 O  O     . HOH   K .   ? 0.34602 0.51666 0.38855 0.15933  0.14438  0.12012  362 HOH   A O     
5609 O  O     . HOH   K .   ? 0.64923 0.74044 0.53623 0.26648  -0.20843 -0.01866 363 HOH   A O     
5610 O  O     . HOH   K .   ? 0.22328 0.30044 0.20719 0.08853  -0.02899 -0.04915 364 HOH   A O     
5611 O  O     . HOH   K .   ? 0.67629 0.66665 0.72906 -0.05812 -0.18912 0.38707  365 HOH   A O     
5612 O  O     . HOH   K .   ? 0.38119 0.62624 0.49345 0.18299  0.09883  -0.10482 366 HOH   A O     
5613 O  O     . HOH   K .   ? 0.60387 0.32120 0.31719 0.18385  -0.13947 -0.08755 367 HOH   A O     
5614 O  O     . HOH   K .   ? 0.39091 0.71816 0.29365 0.19702  -0.11837 -0.09114 368 HOH   A O     
5615 O  O     . HOH   K .   ? 0.16357 0.19008 0.21250 0.00002  0.01190  -0.02067 369 HOH   A O     
5616 O  O     . HOH   K .   ? 0.20650 0.34806 0.36568 0.02506  -0.02840 0.04669  370 HOH   A O     
5617 O  O     . HOH   K .   ? 0.23655 0.19804 0.17069 0.02365  -0.03470 0.00234  371 HOH   A O     
5618 O  O     . HOH   K .   ? 0.24075 0.31886 0.34821 -0.08916 -0.01987 0.07912  372 HOH   A O     
5619 O  O     . HOH   K .   ? 0.78459 0.36992 0.30313 0.08134  -0.06509 -0.01511 373 HOH   A O     
5620 O  O     . HOH   K .   ? 0.41344 0.71959 0.81593 0.00335  -0.08055 0.07023  374 HOH   A O     
5621 O  O     . HOH   K .   ? 0.56150 0.22966 0.39162 -0.02023 -0.06170 0.01798  375 HOH   A O     
5622 O  O     . HOH   K .   ? 0.50020 0.60228 0.46320 0.11993  0.14600  -0.15110 376 HOH   A O     
5623 O  O     . HOH   K .   ? 0.34202 0.28960 0.31029 -0.09394 -0.06423 0.04031  377 HOH   A O     
5624 O  O     . HOH   K .   ? 0.34917 0.22922 0.27017 -0.01780 -0.01999 -0.00546 378 HOH   A O     
5625 O  O     . HOH   K .   ? 0.63464 0.86302 0.39143 0.22832  0.08032  0.12826  379 HOH   A O     
5626 O  O     . HOH   K .   ? 0.40757 0.24201 0.31034 0.03912  -0.07666 0.01975  380 HOH   A O     
5627 O  O     . HOH   K .   ? 0.36326 0.43706 0.29590 0.05473  0.07993  0.07681  381 HOH   A O     
5628 O  O     . HOH   K .   ? 0.26264 0.69405 0.42079 -0.11656 -0.04917 0.05130  382 HOH   A O     
5629 O  O     A HOH   K .   ? 0.31286 0.35734 0.37032 0.14803  -0.15109 -0.04733 383 HOH   A O     
5630 O  O     B HOH   K .   ? 0.23847 0.17964 0.26138 -0.04537 0.00476  0.03123  383 HOH   A O     
5631 O  O     . HOH   K .   ? 1.00837 0.62052 0.34722 0.32408  0.12973  0.00311  384 HOH   A O     
5632 O  O     . HOH   K .   ? 0.37890 0.53600 0.32582 0.08410  0.11145  0.02714  385 HOH   A O     
5633 O  O     . HOH   K .   ? 0.17370 0.32005 0.23601 -0.07321 0.02086  -0.03615 386 HOH   A O     
5634 O  O     . HOH   K .   ? 0.16055 0.38157 0.38106 -0.02016 -0.02940 -0.11373 387 HOH   A O     
5635 O  O     . HOH   K .   ? 0.19333 0.35506 0.44556 -0.02504 -0.01880 -0.00383 388 HOH   A O     
5636 O  O     . HOH   K .   ? 0.26683 0.60324 0.26801 -0.06982 -0.02156 -0.09593 389 HOH   A O     
5637 O  O     . HOH   K .   ? 0.83296 0.98522 0.41528 0.18218  -0.07794 0.24729  390 HOH   A O     
5638 O  O     . HOH   K .   ? 0.42888 0.39091 0.53443 -0.01292 -0.23105 0.06294  391 HOH   A O     
5639 O  O     . HOH   K .   ? 0.77645 0.48880 0.73436 -0.06725 0.43991  0.01014  392 HOH   A O     
5640 O  O     . HOH   K .   ? 0.42201 0.53579 0.62397 0.01603  0.01314  0.25642  393 HOH   A O     
5641 O  O     . HOH   K .   ? 0.25812 0.38877 0.30690 -0.00680 -0.00739 -0.03462 394 HOH   A O     
5642 O  O     . HOH   K .   ? 0.23467 0.39881 0.29668 -0.05425 0.03825  0.03908  395 HOH   A O     
5643 O  O     . HOH   K .   ? 0.39692 0.33599 0.46836 0.07610  -0.10021 -0.11718 396 HOH   A O     
5644 O  O     . HOH   K .   ? 0.35628 0.76607 0.36617 -0.04792 0.04990  0.22008  397 HOH   A O     
5645 O  O     . HOH   K .   ? 0.84098 0.39379 0.87392 0.12474  -0.09265 -0.09733 398 HOH   A O     
5646 O  O     . HOH   K .   ? 0.72379 0.35194 0.53197 0.21874  -0.05519 -0.13824 399 HOH   A O     
5647 O  O     . HOH   K .   ? 0.47565 0.54691 0.22180 0.00015  -0.02867 0.02235  400 HOH   A O     
5648 O  O     . HOH   K .   ? 0.35755 0.55619 0.37363 0.02333  -0.00812 -0.06480 401 HOH   A O     
5649 O  O     . HOH   K .   ? 0.39615 1.21784 0.36027 0.05581  -0.03676 0.06444  402 HOH   A O     
5650 O  O     . HOH   K .   ? 0.88887 0.76521 0.45950 -0.45439 -0.05831 0.13160  403 HOH   A O     
5651 O  O     . HOH   K .   ? 1.04784 0.45848 0.78838 0.32383  0.16799  0.04331  404 HOH   A O     
5652 O  O     . HOH   K .   ? 0.30767 0.43068 0.33458 -0.05585 -0.11378 0.09510  405 HOH   A O     
5653 O  O     . HOH   K .   ? 0.65610 0.75932 0.66007 0.36591  -0.26121 -0.17920 406 HOH   A O     
5654 O  O     . HOH   K .   ? 0.27989 0.37054 0.22306 0.04893  -0.03920 -0.02403 407 HOH   A O     
5655 O  O     . HOH   K .   ? 0.39500 0.45863 0.49637 -0.10376 -0.07268 0.05460  408 HOH   A O     
5656 O  O     . HOH   K .   ? 0.22410 0.29902 0.22199 -0.00813 -0.02203 0.01934  409 HOH   A O     
5657 O  O     . HOH   K .   ? 0.58693 0.69717 0.65742 -0.19226 0.11832  -0.38103 410 HOH   A O     
5658 O  O     . HOH   K .   ? 0.58881 0.54723 0.75489 0.07104  -0.16989 0.06855  411 HOH   A O     
5659 O  O     . HOH   K .   ? 0.38636 0.94000 0.79798 0.11629  -0.25740 0.03001  412 HOH   A O     
5660 O  O     . HOH   K .   ? 0.76162 0.43965 0.42271 0.17588  0.00409  0.00212  413 HOH   A O     
5661 O  O     . HOH   K .   ? 0.34027 0.23865 0.20013 0.02615  -0.01153 -0.04616 414 HOH   A O     
5662 O  O     A HOH   K .   ? 0.32406 0.73222 0.34273 -0.12979 -0.02536 -0.19159 415 HOH   A O     
5663 O  O     B HOH   K .   ? 0.45538 0.64558 0.24859 -0.08125 -0.10257 0.13870  415 HOH   A O     
5664 O  O     . HOH   K .   ? 0.33867 0.44168 0.26163 -0.05859 0.00853  -0.04421 416 HOH   A O     
5665 O  O     . HOH   K .   ? 0.24841 0.32777 0.26206 -0.02479 0.02673  -0.06593 417 HOH   A O     
5666 O  O     . HOH   K .   ? 0.19235 0.19391 0.20807 0.03573  -0.00084 0.01561  418 HOH   A O     
5667 O  O     . HOH   K .   ? 0.72394 0.38688 0.50468 0.18940  -0.31860 -0.08456 419 HOH   A O     
5668 O  O     . HOH   K .   ? 0.64331 0.27666 0.59092 -0.13360 -0.23523 0.11787  420 HOH   A O     
5669 O  O     . HOH   K .   ? 0.37943 0.52121 0.62409 -0.04039 -0.01835 -0.33002 421 HOH   A O     
5670 O  O     . HOH   K .   ? 0.47569 0.31573 0.73469 0.13848  -0.23061 -0.15583 422 HOH   A O     
5671 O  O     . HOH   K .   ? 0.46376 0.30388 0.19745 -0.11920 -0.02450 0.02843  423 HOH   A O     
5672 O  O     A HOH   K .   ? 0.34070 0.50367 0.53430 -0.21483 0.11510  -0.08432 424 HOH   A O     
5673 O  O     B HOH   K .   ? 0.38018 0.51902 0.76500 -0.15699 0.05728  0.19248  424 HOH   A O     
5674 O  O     . HOH   K .   ? 0.41003 0.60996 0.87384 0.07925  -0.24510 -0.30990 425 HOH   A O     
5675 O  O     . HOH   K .   ? 0.38928 0.69778 0.77885 -0.05325 0.11313  0.17456  426 HOH   A O     
5676 O  O     . HOH   K .   ? 0.24111 0.31928 0.39280 0.02431  -0.02627 -0.01723 427 HOH   A O     
5677 O  O     . HOH   K .   ? 0.29990 0.44909 0.34482 -0.15344 -0.04351 0.06024  428 HOH   A O     
5678 O  O     . HOH   K .   ? 0.29610 0.32483 0.19034 -0.03465 -0.07539 -0.00854 429 HOH   A O     
5679 O  O     . HOH   K .   ? 0.54627 0.21097 0.50310 0.06310  0.07016  0.00384  430 HOH   A O     
5680 O  O     . HOH   K .   ? 0.69089 0.59285 0.55740 0.32200  -0.24051 -0.07345 431 HOH   A O     
5681 O  O     . HOH   K .   ? 1.08655 0.45295 0.39805 -0.08910 0.23832  0.00744  432 HOH   A O     
5682 O  O     . HOH   K .   ? 0.38735 0.38986 0.56694 -0.00902 -0.18124 -0.19759 433 HOH   A O     
5683 O  O     . HOH   K .   ? 0.46018 0.63738 0.50984 0.26089  -0.20090 -0.14322 434 HOH   A O     
5684 O  O     . HOH   K .   ? 1.12289 0.34695 0.37920 -0.06429 -0.19588 0.05779  435 HOH   A O     
5685 O  O     . HOH   K .   ? 0.26883 0.49523 0.47480 0.10438  0.15747  0.17415  436 HOH   A O     
5686 O  O     . HOH   K .   ? 0.24095 0.47360 0.30322 0.04009  0.02190  0.08765  437 HOH   A O     
5687 O  O     . HOH   K .   ? 0.63672 0.85223 0.36211 0.15356  0.11494  -0.17946 438 HOH   A O     
5688 O  O     . HOH   K .   ? 0.33907 0.70767 0.24573 0.18211  0.05811  -0.01247 439 HOH   A O     
5689 O  O     . HOH   K .   ? 0.19130 0.69187 0.67546 -0.03274 0.03137  0.06208  440 HOH   A O     
5690 O  O     . HOH   K .   ? 0.85877 0.45044 0.74866 -0.03204 -0.39273 0.03880  441 HOH   A O     
5691 O  O     . HOH   K .   ? 0.23241 0.45652 0.52619 0.05486  0.00208  -0.01128 442 HOH   A O     
5692 O  O     . HOH   K .   ? 0.38534 0.21889 0.80168 0.04639  0.03006  -0.04193 443 HOH   A O     
5693 O  O     . HOH   K .   ? 0.98581 0.58015 0.62231 0.18908  0.27373  0.15316  444 HOH   A O     
5694 O  O     . HOH   K .   ? 0.99468 0.64775 0.40630 -0.19910 -0.24079 0.12878  445 HOH   A O     
5695 O  O     . HOH   K .   ? 0.20297 0.41056 0.45330 0.00129  0.01519  0.00729  446 HOH   A O     
5696 O  O     . HOH   K .   ? 0.22145 0.31217 0.24410 -0.00184 -0.06082 0.03264  447 HOH   A O     
5697 O  O     . HOH   K .   ? 0.32807 0.65433 0.44597 0.19225  0.13349  0.29356  448 HOH   A O     
5698 O  O     . HOH   K .   ? 0.50246 0.37895 0.88242 -0.12501 -0.34175 0.15650  449 HOH   A O     
5699 O  O     . HOH   K .   ? 0.83751 0.46609 1.11160 0.07302  0.51834  0.17618  450 HOH   A O     
5700 O  O     . HOH   K .   ? 0.76895 0.44782 0.31654 -0.15648 0.14953  -0.13878 451 HOH   A O     
5701 O  O     . HOH   K .   ? 0.23659 0.50970 0.57867 0.07729  -0.00425 0.09494  452 HOH   A O     
5702 O  O     . HOH   K .   ? 0.42932 0.20028 0.36019 -0.11878 -0.13394 0.03058  453 HOH   A O     
5703 O  O     . HOH   K .   ? 0.22931 0.38182 0.40288 -0.02522 -0.08581 -0.15422 454 HOH   A O     
5704 O  O     . HOH   K .   ? 0.44642 0.27347 0.60916 0.09728  -0.07800 -0.10299 455 HOH   A O     
5705 O  O     . HOH   K .   ? 0.51206 0.30424 0.87087 -0.07685 -0.10988 0.10790  456 HOH   A O     
5706 O  O     . HOH   K .   ? 0.28408 0.70416 0.43171 -0.08922 -0.14120 0.12658  457 HOH   A O     
5707 O  O     . HOH   K .   ? 0.64607 0.26630 0.52348 -0.07907 -0.31189 0.02038  458 HOH   A O     
5708 O  O     . HOH   K .   ? 0.46963 0.63772 0.79380 -0.24623 0.03602  0.21922  459 HOH   A O     
5709 O  O     . HOH   K .   ? 0.61954 0.54371 0.77161 -0.00718 -0.19214 0.32143  460 HOH   A O     
5710 O  O     . HOH   K .   ? 0.48091 0.59703 0.84734 -0.12222 -0.06961 0.21586  461 HOH   A O     
5711 O  O     . HOH   K .   ? 0.57870 0.90966 0.46832 -0.33767 -0.20370 0.22498  462 HOH   A O     
5712 O  O     . HOH   K .   ? 0.40196 0.56193 0.32869 0.18243  0.01466  0.14386  463 HOH   A O     
5713 O  O     . HOH   K .   ? 0.30611 0.51278 0.34361 0.07220  0.04261  0.04986  464 HOH   A O     
5714 O  O     . HOH   K .   ? 0.52385 0.36036 0.53270 0.17738  -0.06316 0.09197  465 HOH   A O     
5715 O  O     . HOH   K .   ? 0.88192 0.30249 0.80621 0.06132  0.25898  -0.06491 466 HOH   A O     
5716 O  O     . HOH   K .   ? 0.51429 1.12719 0.42649 0.31056  0.02092  0.01443  467 HOH   A O     
5717 O  O     . HOH   K .   ? 0.37773 0.31445 0.26426 -0.00986 -0.04034 -0.04701 468 HOH   A O     
5718 O  O     . HOH   K .   ? 0.63894 0.68235 0.88851 0.05852  0.13673  0.39067  469 HOH   A O     
5719 O  O     . HOH   K .   ? 0.42998 0.45801 0.80236 0.12951  -0.17267 0.15036  470 HOH   A O     
5720 O  O     . HOH   K .   ? 0.85263 0.35885 0.35889 0.22468  0.04280  0.00723  471 HOH   A O     
5721 O  O     . HOH   K .   ? 0.99267 0.49521 0.44662 0.25975  0.30238  0.09204  472 HOH   A O     
5722 O  O     . HOH   K .   ? 0.72424 0.59482 0.95520 -0.22463 0.45702  -0.22928 473 HOH   A O     
5723 O  O     . HOH   K .   ? 1.07235 0.56399 0.42020 -0.08579 0.16619  0.01323  474 HOH   A O     
5724 O  O     . HOH   K .   ? 0.62531 0.51829 0.79737 0.15473  0.25246  0.25261  475 HOH   A O     
5725 O  O     . HOH   K .   ? 0.18218 0.45035 0.57318 0.03028  0.01531  0.13425  476 HOH   A O     
5726 O  O     . HOH   K .   ? 0.47342 0.69379 0.29169 -0.05637 -0.00408 0.04635  477 HOH   A O     
5727 O  O     . HOH   K .   ? 1.09557 0.37646 1.01017 -0.12876 0.07025  0.21698  478 HOH   A O     
5728 O  O     . HOH   K .   ? 0.63658 0.37006 0.56398 -0.08163 -0.01821 0.08854  479 HOH   A O     
5729 O  O     . HOH   K .   ? 0.51282 0.69864 0.52758 0.20716  -0.01371 0.28156  480 HOH   A O     
5730 O  O     . HOH   K .   ? 0.97540 0.36498 0.71287 0.18410  0.01038  0.00435  481 HOH   A O     
5731 O  O     . HOH   K .   ? 0.83123 0.54902 0.27275 0.32372  -0.01711 0.02484  482 HOH   A O     
5732 O  O     . HOH   K .   ? 0.49645 0.68462 0.46458 -0.11231 -0.19038 0.26750  483 HOH   A O     
5733 O  O     . HOH   K .   ? 0.60594 0.54940 0.78376 0.14794  -0.05138 -0.09323 484 HOH   A O     
5734 O  O     . HOH   K .   ? 0.52570 0.38782 0.55761 0.11270  0.14083  -0.03804 485 HOH   A O     
5735 O  O     . HOH   K .   ? 0.45198 0.58587 0.35150 -0.21443 -0.04760 0.03517  486 HOH   A O     
5736 O  O     . HOH   K .   ? 0.33281 0.63794 0.28849 0.17951  0.01162  -0.00870 487 HOH   A O     
5737 O  O     . HOH   K .   ? 0.50871 0.70136 0.46686 0.17601  0.04597  -0.08314 488 HOH   A O     
5738 O  O     A HOH   K .   ? 0.59413 0.40253 0.46630 0.24000  0.25030  0.18044  489 HOH   A O     
5739 O  O     B HOH   K .   ? 0.80838 0.50355 0.78105 0.08633  0.34184  0.19956  489 HOH   A O     
5740 O  O     . HOH   K .   ? 1.14925 0.42495 0.66864 0.10677  0.18982  0.01892  490 HOH   A O     
5741 O  O     . HOH   K .   ? 0.85944 1.09847 0.61786 0.53639  0.24817  0.29830  491 HOH   A O     
5742 O  O     . HOH   K .   ? 0.49753 0.62671 0.99315 -0.19053 -0.09596 0.14006  492 HOH   A O     
5743 O  O     . HOH   K .   ? 1.19229 0.49070 0.76542 0.28136  0.12543  -0.01128 493 HOH   A O     
5744 O  O     . HOH   K .   ? 0.74974 0.36360 1.12539 0.09154  -0.14910 -0.15325 494 HOH   A O     
5745 O  O     . HOH   K .   ? 0.37620 0.72939 0.80825 0.05358  0.24461  0.20253  495 HOH   A O     
5746 O  O     . HOH   K .   ? 0.33589 0.70096 0.42117 0.17189  -0.10438 -0.15042 496 HOH   A O     
5747 O  O     . HOH   K .   ? 0.36195 0.52433 0.76096 -0.10838 0.23854  -0.22343 497 HOH   A O     
5748 O  O     . HOH   K .   ? 0.26784 0.52792 0.21970 -0.00678 -0.03848 -0.01123 498 HOH   A O     
5749 O  O     . HOH   K .   ? 0.47675 0.40026 0.46669 0.02112  0.22486  -0.08800 499 HOH   A O     
5750 O  O     . HOH   K .   ? 0.53115 0.54762 0.62394 -0.20004 -0.06494 0.20468  500 HOH   A O     
5751 O  O     . HOH   K .   ? 0.56854 0.60862 0.50875 0.18062  0.13005  -0.08259 501 HOH   A O     
5752 O  O     . HOH   K .   ? 0.34570 0.34029 0.52216 0.07735  0.14441  0.11456  502 HOH   A O     
5753 O  O     A HOH   K .   ? 0.31182 0.15505 0.43307 -0.04064 0.07849  -0.06679 503 HOH   A O     
5754 O  O     B HOH   K .   ? 0.53262 0.42490 0.50806 -0.10210 0.27046  -0.04523 503 HOH   A O     
5755 O  O     . HOH   K .   ? 0.62328 0.56810 0.43354 -0.14713 0.27490  -0.14547 504 HOH   A O     
5756 O  O     . HOH   K .   ? 0.58640 0.43432 0.40206 -0.18735 -0.23559 0.09057  505 HOH   A O     
5757 O  O     . HOH   K .   ? 0.50288 0.98702 0.33787 0.14996  0.07224  0.01491  506 HOH   A O     
5758 O  O     . HOH   K .   ? 0.44838 0.58181 0.75066 -0.07029 0.07379  -0.22264 507 HOH   A O     
5759 O  O     . HOH   K .   ? 0.57011 0.31758 0.92573 -0.14793 -0.04131 0.07846  508 HOH   A O     
5760 O  O     . HOH   K .   ? 0.17796 0.64796 0.39099 0.01946  -0.01421 -0.08578 509 HOH   A O     
5761 O  O     . HOH   K .   ? 0.93724 0.46681 1.17028 0.32704  -0.01263 0.06358  510 HOH   A O     
5762 O  O     . HOH   K .   ? 0.40225 0.61299 0.77465 0.25009  -0.01648 -0.01845 511 HOH   A O     
5763 O  O     . HOH   K .   ? 0.73384 0.86554 0.48990 0.33768  -0.10513 0.06891  512 HOH   A O     
5764 O  O     . HOH   K .   ? 0.43598 0.78104 0.91282 -0.14013 -0.07291 0.34506  513 HOH   A O     
5765 O  O     . HOH   K .   ? 0.55186 0.99772 0.45548 0.34248  0.16493  0.15321  514 HOH   A O     
5766 O  O     . HOH   K .   ? 0.69058 0.94929 0.53318 -0.25906 0.01781  -0.15464 515 HOH   A O     
5767 O  O     . HOH   K .   ? 0.68250 0.34086 0.66161 0.20401  0.09904  0.15231  516 HOH   A O     
5768 O  O     . HOH   K .   ? 1.03238 0.29020 0.35452 0.00000  0.21796  -0.01260 517 HOH   A O     
5769 O  O     . HOH   K .   ? 0.49003 0.36175 0.28095 -0.10809 0.05710  0.00184  518 HOH   A O     
5770 O  O     . HOH   K .   ? 0.61613 0.44804 0.41141 0.07769  0.00282  -0.03957 519 HOH   A O     
5771 O  O     . HOH   K .   ? 0.40816 0.55845 0.44229 0.09967  -0.05251 0.20652  520 HOH   A O     
5772 O  O     . HOH   K .   ? 0.92224 0.38741 0.36140 0.17575  -0.03516 0.02701  521 HOH   A O     
5773 O  O     . HOH   K .   ? 0.29027 0.45381 0.45506 -0.08925 0.09442  -0.14196 522 HOH   A O     
5774 O  O     . HOH   K .   ? 0.91361 0.25764 0.95050 0.10316  -0.02358 0.02374  523 HOH   A O     
5775 O  O     . HOH   K .   ? 1.03143 0.51406 0.81765 0.06859  0.49614  0.16065  524 HOH   A O     
5776 O  O     . HOH   K .   ? 0.50399 0.45945 1.18770 -0.12677 -0.27362 0.04555  525 HOH   A O     
5777 O  O     . HOH   K .   ? 0.32153 0.43243 0.41944 -0.05352 -0.04452 0.07752  526 HOH   A O     
5778 O  O     . HOH   K .   ? 0.84613 1.03077 0.32293 0.19593  0.01797  0.08456  527 HOH   A O     
5779 O  O     . HOH   K .   ? 0.97312 0.80894 0.50238 -0.18100 0.06112  -0.25362 528 HOH   A O     
5780 O  O     . HOH   K .   ? 0.76412 0.57970 0.61309 0.17387  0.30545  -0.03060 529 HOH   A O     
5781 O  O     . HOH   K .   ? 0.62618 0.51687 0.43056 0.10532  -0.21790 -0.06774 530 HOH   A O     
5782 O  O     . HOH   K .   ? 1.04907 1.15035 0.54051 -0.13807 0.31456  0.07010  531 HOH   A O     
5783 O  O     . HOH   K .   ? 0.33800 0.51131 0.47085 -0.15679 0.00036  -0.04045 532 HOH   A O     
5784 O  O     . HOH   K .   ? 0.35381 0.65457 0.56651 0.16073  -0.05797 0.12154  533 HOH   A O     
5785 O  O     . HOH   K .   ? 0.33112 0.77792 0.71819 0.07891  0.12923  -0.23442 534 HOH   A O     
5786 O  O     . HOH   K .   ? 0.63016 0.49651 0.46896 0.00257  -0.24369 -0.12508 535 HOH   A O     
5787 O  O     . HOH   K .   ? 0.43891 1.08113 0.41272 -0.10799 0.05164  -0.21485 536 HOH   A O     
5788 O  O     . HOH   K .   ? 0.35252 0.32768 0.28660 -0.01612 0.02309  -0.05765 537 HOH   A O     
5789 O  O     . HOH   K .   ? 0.89126 0.49896 0.80201 -0.30203 -0.17990 0.22041  538 HOH   A O     
5790 O  O     A HOH   K .   ? 0.69723 0.31689 0.48768 -0.02783 0.33547  0.00407  539 HOH   A O     
5791 O  O     B HOH   K .   ? 0.55079 0.50657 0.41080 -0.05511 0.27039  -0.08349 539 HOH   A O     
5792 O  O     . HOH   K .   ? 0.32685 0.45105 0.43951 0.09839  -0.12436 -0.09437 540 HOH   A O     
5793 O  O     . HOH   K .   ? 0.52984 0.41820 1.06919 0.08736  0.08438  0.20232  541 HOH   A O     
5794 O  O     . HOH   K .   ? 0.72607 0.89422 0.55222 0.17031  -0.34193 -0.07202 542 HOH   A O     
5795 O  O     . HOH   K .   ? 0.51566 0.45101 0.97862 0.17875  0.23963  0.24140  543 HOH   A O     
5796 O  O     . HOH   K .   ? 0.82215 0.46226 0.52742 0.04727  0.09055  0.20023  544 HOH   A O     
5797 O  O     . HOH   K .   ? 0.30648 0.28071 0.32843 0.01258  -0.01850 -0.03203 545 HOH   A O     
5798 O  O     . HOH   K .   ? 0.42816 0.57407 0.63431 0.09960  0.25597  0.03033  546 HOH   A O     
5799 O  O     . HOH   K .   ? 0.48394 0.54909 0.69853 -0.14515 0.13319  -0.09473 547 HOH   A O     
5800 O  O     . HOH   K .   ? 0.78370 0.45844 0.68352 0.19264  0.25564  0.22942  548 HOH   A O     
5801 O  O     . HOH   K .   ? 1.26327 0.44763 0.57704 -0.15181 0.15080  -0.05594 549 HOH   A O     
5802 O  O     . HOH   K .   ? 0.40051 0.57948 0.80181 -0.17214 0.23830  -0.28949 550 HOH   A O     
5803 O  O     . HOH   K .   ? 0.73252 0.58480 0.55738 -0.05422 0.37478  -0.04279 551 HOH   A O     
5804 O  O     . HOH   L .   ? 0.48959 0.48005 0.52113 -0.14634 -0.00874 0.03893  301 HOH   B O     
5805 O  O     . HOH   L .   ? 0.45160 0.99693 0.87052 0.15915  -0.10220 -0.53407 302 HOH   B O     
5806 O  O     . HOH   L .   ? 0.66306 0.55434 0.62745 -0.02105 -0.11285 -0.12448 303 HOH   B O     
5807 O  O     . HOH   L .   ? 0.57383 0.57951 0.46117 0.24466  0.11871  0.11716  304 HOH   B O     
5808 O  O     . HOH   L .   ? 0.38600 0.55747 0.38218 0.00992  0.19344  -0.06351 305 HOH   B O     
5809 O  O     . HOH   L .   ? 0.61497 0.41736 0.30487 -0.11570 -0.09565 0.13124  306 HOH   B O     
5810 O  O     . HOH   L .   ? 0.25922 0.44848 0.46378 -0.01078 0.03439  0.17291  307 HOH   B O     
5811 O  O     . HOH   L .   ? 0.40843 0.82029 0.60046 0.23581  0.05508  0.20417  308 HOH   B O     
5812 O  O     . HOH   L .   ? 0.17374 0.33751 0.25243 0.01064  -0.02010 0.00625  309 HOH   B O     
5813 O  O     . HOH   L .   ? 0.34786 0.66249 0.81595 0.08642  0.10857  0.43187  310 HOH   B O     
5814 O  O     . HOH   L .   ? 0.31045 0.58000 0.86978 0.14387  0.04753  0.19322  311 HOH   B O     
5815 O  O     . HOH   L .   ? 0.76316 0.62203 0.57072 0.36471  -0.12370 0.06189  312 HOH   B O     
5816 O  O     . HOH   L .   ? 0.20792 0.24592 0.25595 0.02107  0.08328  0.03827  313 HOH   B O     
5817 O  O     . HOH   L .   ? 0.42582 0.50427 0.32128 -0.09805 0.08056  0.11606  314 HOH   B O     
5818 O  O     . HOH   L .   ? 0.71444 0.38119 0.61475 -0.18433 -0.37899 0.15452  315 HOH   B O     
5819 O  O     . HOH   L .   ? 0.56580 0.35757 0.26797 -0.11888 -0.00657 -0.03583 316 HOH   B O     
5820 O  O     . HOH   L .   ? 0.89913 0.30376 0.90389 0.00280  -0.29456 0.03986  317 HOH   B O     
5821 O  O     . HOH   L .   ? 0.54340 0.56762 0.83129 -0.13533 -0.10404 0.36397  318 HOH   B O     
5822 O  O     . HOH   L .   ? 0.35748 0.29665 0.42588 -0.04857 0.01654  -0.02038 319 HOH   B O     
5823 O  O     . HOH   L .   ? 0.60433 0.92289 0.44767 0.16907  0.08926  0.31895  320 HOH   B O     
5824 O  O     . HOH   L .   ? 0.80743 0.53621 0.35928 0.09606  0.23334  -0.06296 321 HOH   B O     
5825 O  O     . HOH   L .   ? 0.62527 0.76014 0.40991 0.26097  -0.18742 -0.13405 322 HOH   B O     
5826 O  O     . HOH   L .   ? 0.46172 0.90173 0.41576 0.20082  -0.17235 -0.08515 323 HOH   B O     
5827 O  O     . HOH   L .   ? 0.91455 1.05455 0.38203 0.42399  -0.05867 -0.12661 324 HOH   B O     
5828 O  O     . HOH   L .   ? 0.25115 0.56762 0.43110 0.02989  0.01483  0.22239  325 HOH   B O     
5829 O  O     . HOH   L .   ? 0.83951 0.51651 0.66276 -0.29793 -0.19787 0.03720  326 HOH   B O     
5830 O  O     . HOH   L .   ? 0.40462 0.71583 0.42392 0.10381  0.02312  -0.01736 327 HOH   B O     
5831 O  O     . HOH   L .   ? 0.32962 0.31374 0.25418 -0.11097 -0.05015 0.00945  328 HOH   B O     
5832 O  O     . HOH   L .   ? 0.48894 0.53161 0.40629 -0.07583 0.16848  -0.13926 329 HOH   B O     
5833 O  O     . HOH   L .   ? 0.44438 0.27801 0.22811 -0.01221 0.11663  0.03166  330 HOH   B O     
5834 O  O     . HOH   L .   ? 0.28423 0.48300 0.43088 0.08126  -0.03798 0.00562  331 HOH   B O     
5835 O  O     . HOH   L .   ? 0.25146 0.66303 0.29593 -0.06158 -0.04758 0.14517  332 HOH   B O     
5836 O  O     . HOH   L .   ? 0.36878 0.38065 0.50802 0.15332  0.14974  0.14383  333 HOH   B O     
5837 O  O     . HOH   L .   ? 0.42357 1.00546 1.07476 0.09604  0.26508  -0.13062 334 HOH   B O     
5838 O  O     . HOH   L .   ? 0.68616 0.25706 0.58767 -0.08306 0.28600  -0.05361 335 HOH   B O     
5839 O  O     . HOH   L .   ? 0.74693 0.81017 0.52390 -0.16724 -0.17306 0.01107  336 HOH   B O     
5840 O  O     . HOH   L .   ? 0.32192 0.66935 0.89364 0.08893  0.01287  0.12321  337 HOH   B O     
5841 O  O     . HOH   L .   ? 0.53901 0.62699 1.03200 0.30401  0.10870  0.02601  338 HOH   B O     
5842 O  O     . HOH   L .   ? 0.46938 0.23487 0.19236 0.08391  -0.02577 0.03260  339 HOH   B O     
5843 O  O     . HOH   L .   ? 0.50899 0.81655 0.23443 0.02942  0.01191  0.09945  340 HOH   B O     
5844 O  O     . HOH   L .   ? 0.24153 0.29819 0.34880 0.03268  0.04740  0.16383  341 HOH   B O     
5845 O  O     . HOH   L .   ? 0.16026 0.25889 0.26913 -0.01678 -0.03513 0.03371  342 HOH   B O     
5846 O  O     . HOH   L .   ? 0.21108 0.23653 0.25012 -0.02122 0.00220  -0.04538 343 HOH   B O     
5847 O  O     . HOH   L .   ? 0.58816 0.41955 0.71886 0.12924  0.35487  0.04819  344 HOH   B O     
5848 O  O     . HOH   L .   ? 0.52175 0.52197 0.84922 -0.10569 0.31891  0.07849  345 HOH   B O     
5849 O  O     . HOH   L .   ? 0.50423 0.32157 0.20304 0.01042  0.04844  0.00709  346 HOH   B O     
5850 O  O     . HOH   L .   ? 0.86294 0.69613 0.35997 0.05936  -0.09267 0.00288  347 HOH   B O     
5851 O  O     . HOH   L .   ? 0.57447 0.55757 0.43963 0.18551  -0.23207 -0.02605 348 HOH   B O     
5852 O  O     . HOH   L .   ? 0.36610 0.27001 0.58335 -0.03692 -0.01518 0.18087  349 HOH   B O     
5853 O  O     . HOH   L .   ? 0.30829 0.60209 0.51856 0.11132  -0.07063 -0.20335 350 HOH   B O     
5854 O  O     . HOH   L .   ? 0.58493 0.67378 0.66075 0.07020  -0.08330 -0.12902 351 HOH   B O     
5855 O  O     . HOH   L .   ? 0.29645 0.25616 0.22563 -0.04311 -0.01774 0.01602  352 HOH   B O     
5856 O  O     . HOH   L .   ? 0.62403 0.33312 0.93884 0.02357  -0.25669 -0.10812 353 HOH   B O     
5857 O  O     . HOH   L .   ? 0.39127 0.25811 0.19940 -0.06971 0.07751  0.01516  354 HOH   B O     
5858 O  O     . HOH   L .   ? 0.69210 0.63759 0.44218 -0.17121 0.26652  -0.12050 355 HOH   B O     
5859 O  O     . HOH   L .   ? 0.33239 0.48395 0.24124 -0.02294 -0.04231 -0.03242 356 HOH   B O     
5860 O  O     . HOH   L .   ? 0.52349 0.63836 0.25011 -0.13647 -0.08289 -0.08769 357 HOH   B O     
5861 O  O     . HOH   L .   ? 0.49961 0.46102 0.79341 -0.09676 -0.16637 0.21492  358 HOH   B O     
5862 O  O     . HOH   L .   ? 0.42446 0.41123 0.42445 0.15921  0.18083  0.14785  359 HOH   B O     
5863 O  O     . HOH   L .   ? 0.21068 0.30549 0.23897 0.03782  0.05990  0.07527  360 HOH   B O     
5864 O  O     . HOH   L .   ? 0.23965 0.35044 0.30652 0.06250  -0.00514 0.06177  361 HOH   B O     
5865 O  O     . HOH   L .   ? 0.15190 0.48025 0.38446 -0.03129 -0.00154 -0.07193 362 HOH   B O     
5866 O  O     . HOH   L .   ? 0.43307 0.33549 0.24630 0.03465  0.06862  0.06071  363 HOH   B O     
5867 O  O     . HOH   L .   ? 0.44113 0.35185 0.43209 0.03954  0.19623  0.07979  364 HOH   B O     
5868 O  O     . HOH   L .   ? 0.52066 0.31676 0.46147 0.07686  0.21096  0.03844  365 HOH   B O     
5869 O  O     . HOH   L .   ? 0.22181 0.25756 0.25329 0.00365  0.04259  -0.01475 366 HOH   B O     
5870 O  O     . HOH   L .   ? 0.17654 0.36079 0.24124 0.01147  -0.00455 0.09511  367 HOH   B O     
5871 O  O     . HOH   L .   ? 0.23270 0.57135 0.77043 -0.08709 -0.06934 0.03667  368 HOH   B O     
5872 O  O     . HOH   L .   ? 0.37903 0.18082 0.33188 0.01617  0.09172  -0.01240 369 HOH   B O     
5873 O  O     . HOH   L .   ? 0.21891 0.51144 0.26882 0.03391  0.00738  0.11557  370 HOH   B O     
5874 O  O     . HOH   L .   ? 0.38647 0.88182 0.46640 -0.00550 -0.03072 0.32506  371 HOH   B O     
5875 O  O     . HOH   L .   ? 0.29549 0.39973 0.38941 0.01623  -0.06086 -0.11307 372 HOH   B O     
5876 O  O     . HOH   L .   ? 0.37687 0.35644 0.20698 -0.09141 0.03765  -0.01947 373 HOH   B O     
5877 O  O     A HOH   L .   ? 0.34641 0.49109 0.31933 0.15486  0.14180  0.18550  374 HOH   B O     
5878 O  O     B HOH   L .   ? 0.48850 0.41921 0.44338 0.11181  0.16103  0.01964  374 HOH   B O     
5879 O  O     . HOH   L .   ? 0.42774 0.58749 0.65406 -0.03151 -0.06034 0.27588  375 HOH   B O     
5880 O  O     . HOH   L .   ? 0.21669 0.33308 0.24952 0.00674  -0.03074 -0.08835 376 HOH   B O     
5881 O  O     . HOH   L .   ? 0.60280 0.57577 0.53318 0.13813  0.07175  0.31420  377 HOH   B O     
5882 O  O     . HOH   L .   ? 0.39088 0.67048 0.51611 0.04456  0.22352  0.10616  378 HOH   B O     
5883 O  O     . HOH   L .   ? 0.26000 0.46191 0.33705 0.00366  0.07238  0.05665  379 HOH   B O     
5884 O  O     . HOH   L .   ? 0.30425 0.21341 0.24351 -0.04208 0.03466  0.00632  380 HOH   B O     
5885 O  O     . HOH   L .   ? 0.26303 0.36986 0.84935 0.04953  0.10651  -0.06963 381 HOH   B O     
5886 O  O     . HOH   L .   ? 0.59667 0.45383 1.20444 -0.13601 0.36883  -0.11538 382 HOH   B O     
5887 O  O     . HOH   L .   ? 0.49245 0.45260 0.30912 0.06863  0.04579  -0.10897 383 HOH   B O     
5888 O  O     . HOH   L .   ? 0.50641 0.61256 0.55727 -0.10566 -0.10903 0.20557  384 HOH   B O     
5889 O  O     . HOH   L .   ? 0.45471 0.30079 0.47034 0.14990  -0.25474 -0.15895 385 HOH   B O     
5890 O  O     . HOH   L .   ? 0.31088 0.20404 0.21833 0.00745  0.01125  -0.00289 386 HOH   B O     
5891 O  O     . HOH   L .   ? 0.31115 0.48592 0.30043 0.13923  0.01523  0.06109  387 HOH   B O     
5892 O  O     . HOH   L .   ? 0.45559 0.75885 0.66550 -0.29339 -0.11436 0.23868  388 HOH   B O     
5893 O  O     . HOH   L .   ? 0.13158 0.26193 0.19457 -0.01310 -0.02450 0.06595  389 HOH   B O     
5894 O  O     . HOH   L .   ? 0.55159 0.45966 0.50567 -0.03678 0.23137  -0.01407 390 HOH   B O     
5895 O  O     . HOH   L .   ? 0.34681 0.53835 0.94610 -0.07722 0.16600  0.14963  391 HOH   B O     
5896 O  O     . HOH   L .   ? 1.21965 0.41129 0.56075 -0.15834 0.40723  -0.06256 392 HOH   B O     
5897 O  O     . HOH   L .   ? 0.68020 0.46238 0.33212 0.13253  0.16855  0.15420  393 HOH   B O     
5898 O  O     . HOH   L .   ? 0.21924 0.57559 0.51696 -0.03749 -0.08402 0.22120  394 HOH   B O     
5899 O  O     . HOH   L .   ? 0.35525 0.40777 0.72920 -0.12961 0.09904  -0.21847 395 HOH   B O     
5900 O  O     . HOH   L .   ? 0.66860 0.57595 0.55744 -0.03760 -0.12806 0.24968  396 HOH   B O     
5901 O  O     . HOH   L .   ? 0.82278 0.58564 0.76973 0.12288  -0.43735 0.01417  397 HOH   B O     
5902 O  O     . HOH   L .   ? 0.34153 1.04952 0.75416 0.02814  0.11979  0.27625  398 HOH   B O     
5903 O  O     . HOH   L .   ? 0.35504 0.53954 0.87437 -0.07513 0.19716  0.11470  399 HOH   B O     
5904 O  O     . HOH   L .   ? 0.21728 0.59854 0.36787 0.11635  0.03182  0.18203  400 HOH   B O     
5905 O  O     . HOH   L .   ? 0.79696 0.28205 0.48989 0.02099  0.29376  0.06812  401 HOH   B O     
5906 O  O     . HOH   L .   ? 0.37615 0.61239 0.43227 -0.22812 -0.16542 0.26378  402 HOH   B O     
5907 O  O     . HOH   L .   ? 0.67096 0.59087 0.49712 -0.21570 0.27897  -0.00594 403 HOH   B O     
5908 O  O     . HOH   L .   ? 0.56085 0.33229 0.41514 0.15220  0.25047  0.08379  404 HOH   B O     
5909 O  O     . HOH   L .   ? 0.24328 0.34910 0.35887 -0.06230 0.08533  -0.14943 405 HOH   B O     
5910 O  O     . HOH   L .   ? 0.41135 0.26697 0.27395 -0.01501 -0.04840 -0.06701 406 HOH   B O     
5911 O  O     . HOH   L .   ? 0.86689 0.82659 0.55381 0.03793  -0.01443 -0.31259 407 HOH   B O     
5912 O  O     . HOH   L .   ? 0.51145 0.54264 0.59025 -0.06587 0.05671  0.12839  408 HOH   B O     
5913 O  O     . HOH   L .   ? 0.29874 0.34100 0.31118 -0.01982 -0.06149 -0.03374 409 HOH   B O     
5914 O  O     . HOH   L .   ? 0.83666 0.46300 0.57313 -0.27116 -0.04495 0.07355  410 HOH   B O     
5915 O  O     . HOH   L .   ? 0.44891 0.58850 0.70593 0.17190  0.28068  0.24515  411 HOH   B O     
5916 O  O     . HOH   L .   ? 0.56922 0.55698 0.30433 0.31338  -0.05796 -0.09049 412 HOH   B O     
5917 O  O     . HOH   L .   ? 0.35172 0.38003 0.27605 -0.04068 0.16084  -0.00929 413 HOH   B O     
5918 O  O     . HOH   L .   ? 0.72567 0.41430 0.66064 0.01188  -0.25460 -0.13148 414 HOH   B O     
5919 O  O     . HOH   L .   ? 0.54569 0.40736 0.29087 0.20641  -0.17305 -0.10609 415 HOH   B O     
5920 O  O     . HOH   L .   ? 0.38609 0.53817 0.40993 0.22938  0.12706  0.18804  416 HOH   B O     
5921 O  O     . HOH   L .   ? 0.72188 0.27602 0.60310 -0.18907 0.07280  -0.04539 417 HOH   B O     
5922 O  O     . HOH   L .   ? 0.23755 0.27354 0.21566 -0.00289 0.02551  -0.01390 418 HOH   B O     
5923 O  O     . HOH   L .   ? 0.64853 0.51827 0.58143 -0.28189 -0.30261 0.19269  419 HOH   B O     
5924 O  O     . HOH   L .   ? 0.31850 0.60979 0.99716 0.09686  -0.02402 0.22880  420 HOH   B O     
5925 O  O     . HOH   L .   ? 0.60711 0.91554 0.97986 0.20595  0.06445  0.51445  421 HOH   B O     
5926 O  O     . HOH   L .   ? 0.24170 0.49681 0.38027 -0.00768 -0.05542 0.09808  422 HOH   B O     
5927 O  O     . HOH   L .   ? 0.46198 0.33639 0.25623 -0.06675 0.10966  -0.09603 423 HOH   B O     
5928 O  O     . HOH   L .   ? 0.35571 0.52286 0.81219 0.16459  0.12174  0.24960  424 HOH   B O     
5929 O  O     . HOH   L .   ? 0.91323 0.56969 0.84027 0.32994  0.20283  0.26654  425 HOH   B O     
5930 O  O     . HOH   L .   ? 0.45568 0.37406 0.53798 -0.07814 0.05968  0.08884  426 HOH   B O     
5931 O  O     . HOH   L .   ? 0.38288 0.22681 0.28727 -0.01737 0.03856  -0.03516 427 HOH   B O     
5932 O  O     . HOH   L .   ? 0.81492 1.14540 0.59064 0.05944  0.38884  -0.06599 428 HOH   B O     
5933 O  O     . HOH   L .   ? 0.58027 0.80531 0.42347 0.10096  0.16181  0.08812  429 HOH   B O     
5934 O  O     . HOH   L .   ? 0.50008 0.33428 0.30441 0.05213  -0.09876 0.04522  430 HOH   B O     
5935 O  O     . HOH   L .   ? 0.35303 0.86553 0.27550 -0.04693 -0.02661 0.16923  431 HOH   B O     
5936 O  O     . HOH   L .   ? 0.41504 0.22225 0.22464 0.00897  0.06137  -0.00409 432 HOH   B O     
5937 O  O     . HOH   L .   ? 0.41233 0.33546 0.27292 -0.03884 0.12508  -0.00473 433 HOH   B O     
5938 O  O     . HOH   L .   ? 0.45840 0.97072 0.42680 0.29722  -0.10109 -0.03159 434 HOH   B O     
5939 O  O     . HOH   L .   ? 0.60609 0.40205 0.45528 0.06357  0.04487  0.03929  435 HOH   B O     
5940 O  O     . HOH   L .   ? 0.52524 0.95346 0.84818 -0.25579 0.26515  0.09459  436 HOH   B O     
5941 O  O     . HOH   L .   ? 0.53847 0.80851 0.43948 0.11673  0.22118  0.20024  437 HOH   B O     
5942 O  O     . HOH   L .   ? 1.01555 0.38628 0.78098 -0.07197 -0.06693 0.13141  438 HOH   B O     
5943 O  O     . HOH   L .   ? 0.85563 0.96188 0.54225 0.07818  0.36800  -0.10249 439 HOH   B O     
5944 O  O     . HOH   L .   ? 0.29559 0.43874 0.41615 -0.00194 -0.02068 0.09852  440 HOH   B O     
5945 O  O     . HOH   L .   ? 0.51177 0.61049 0.79505 -0.21351 0.00864  0.15852  441 HOH   B O     
5946 O  O     . HOH   L .   ? 0.69933 0.95245 0.49153 0.00895  0.30849  0.12477  442 HOH   B O     
5947 O  O     . HOH   L .   ? 0.63382 0.58384 0.34204 -0.14257 -0.12440 0.08428  443 HOH   B O     
5948 O  O     . HOH   L .   ? 0.66956 0.66816 0.42395 -0.15147 -0.22566 0.02133  444 HOH   B O     
5949 O  O     . HOH   L .   ? 0.76467 0.65732 0.40015 0.21014  -0.11022 0.05289  445 HOH   B O     
5950 O  O     . HOH   L .   ? 0.57188 0.94793 0.29952 0.20171  -0.10555 -0.07831 446 HOH   B O     
5951 O  O     . HOH   L .   ? 0.97729 0.57097 0.71489 0.38900  0.24335  0.14473  447 HOH   B O     
5952 O  O     . HOH   L .   ? 0.84676 0.59176 0.59245 0.28669  0.31932  0.16598  448 HOH   B O     
5953 O  O     . HOH   L .   ? 0.41754 0.61168 0.43732 -0.14720 -0.16459 0.14617  449 HOH   B O     
5954 O  O     . HOH   L .   ? 0.78147 0.94154 0.34194 0.21701  -0.14772 -0.06680 450 HOH   B O     
5955 O  O     . HOH   L .   ? 0.59196 0.62406 0.74487 0.18101  0.35218  0.27329  451 HOH   B O     
5956 O  O     . HOH   L .   ? 0.37334 0.50041 0.67501 -0.00781 0.23282  -0.02650 452 HOH   B O     
5957 O  O     . HOH   L .   ? 0.51093 0.73781 0.65510 0.03644  -0.32326 -0.13341 453 HOH   B O     
5958 O  O     . HOH   L .   ? 0.26516 0.73464 0.41033 -0.10160 -0.09236 0.22698  454 HOH   B O     
5959 O  O     . HOH   L .   ? 0.21390 0.33225 0.60956 -0.01909 -0.01356 -0.02442 455 HOH   B O     
5960 O  O     . HOH   L .   ? 0.38397 0.47010 0.33861 0.05169  0.11696  0.03089  456 HOH   B O     
5961 O  O     . HOH   L .   ? 0.53753 0.65940 0.38242 0.13023  0.17094  -0.02048 457 HOH   B O     
5962 O  O     . HOH   L .   ? 0.50632 0.57998 0.59915 0.06746  -0.00969 -0.16800 458 HOH   B O     
5963 O  O     . HOH   L .   ? 0.27662 0.49173 0.22524 -0.16152 -0.00133 -0.00739 459 HOH   B O     
5964 O  O     . HOH   L .   ? 0.74542 0.52499 0.28362 0.24969  -0.12225 0.00449  460 HOH   B O     
5965 O  O     . HOH   L .   ? 0.51358 0.60425 0.74290 0.11323  -0.03095 -0.07143 461 HOH   B O     
5966 O  O     . HOH   L .   ? 0.61553 0.50083 1.14694 -0.16474 -0.01643 0.28796  462 HOH   B O     
5967 O  O     . HOH   L .   ? 0.82816 0.36891 0.72551 0.05981  -0.28242 -0.11981 463 HOH   B O     
5968 O  O     . HOH   L .   ? 0.24238 0.28970 0.47688 0.02498  -0.11823 0.02373  464 HOH   B O     
5969 O  O     . HOH   L .   ? 0.61591 0.59629 1.14575 0.27439  0.02247  0.03473  465 HOH   B O     
5970 O  O     . HOH   L .   ? 0.64981 0.40940 1.11286 0.11598  0.01708  -0.24051 466 HOH   B O     
5971 O  O     . HOH   L .   ? 0.53751 0.73126 0.84380 -0.23861 0.06564  0.29809  467 HOH   B O     
5972 O  O     . HOH   L .   ? 0.51075 0.51838 1.42648 0.10801  -0.06909 -0.28284 468 HOH   B O     
5973 O  O     . HOH   L .   ? 0.47073 0.52830 0.52898 -0.01253 0.21736  -0.00390 469 HOH   B O     
5974 O  O     . HOH   L .   ? 0.88803 0.45797 0.24965 0.20965  -0.05258 -0.00415 470 HOH   B O     
5975 O  O     . HOH   L .   ? 0.28900 0.45678 0.60101 0.00470  -0.01601 -0.18187 471 HOH   B O     
5976 O  O     . HOH   L .   ? 0.70684 0.55816 0.47943 0.14277  0.12176  0.25625  472 HOH   B O     
5977 O  O     . HOH   L .   ? 0.75272 0.61844 0.55525 -0.08966 0.24550  -0.01994 473 HOH   B O     
5978 O  O     . HOH   L .   ? 0.55693 0.58979 0.60072 0.28444  0.27239  0.29505  474 HOH   B O     
5979 O  O     . HOH   L .   ? 0.58647 0.47558 0.34661 -0.03572 -0.01578 0.04102  475 HOH   B O     
5980 O  O     . HOH   L .   ? 0.60504 0.27189 0.66937 0.05693  0.33107  0.01078  476 HOH   B O     
5981 O  O     . HOH   L .   ? 0.35589 0.51395 0.77829 0.08727  0.21130  0.14883  477 HOH   B O     
5982 O  O     . HOH   L .   ? 0.73918 0.49845 0.73698 0.25846  0.13377  -0.06526 478 HOH   B O     
5983 O  O     . HOH   L .   ? 0.62837 0.66329 1.20764 0.27231  0.10522  0.29955  479 HOH   B O     
5984 O  O     . HOH   L .   ? 0.40012 0.65326 0.41699 0.24905  0.14430  0.25736  480 HOH   B O     
5985 O  O     . HOH   L .   ? 1.02096 0.71940 0.62791 -0.14531 -0.01752 -0.03616 481 HOH   B O     
5986 O  O     . HOH   L .   ? 0.91257 0.32495 1.02955 -0.14746 0.06167  -0.12586 482 HOH   B O     
5987 O  O     . HOH   L .   ? 0.59659 0.75481 0.66647 0.30315  0.20415  0.26069  483 HOH   B O     
5988 O  O     . HOH   L .   ? 0.36698 0.48762 0.49891 -0.06372 -0.10606 0.02635  484 HOH   B O     
5989 O  O     . HOH   L .   ? 0.40967 1.04938 0.33897 0.12194  -0.04796 -0.10926 485 HOH   B O     
5990 O  O     . HOH   L .   ? 0.80083 0.62635 0.38253 0.00920  -0.19932 -0.07276 486 HOH   B O     
5991 O  O     . HOH   L .   ? 0.61675 0.54605 1.12982 0.09900  0.18551  0.39506  487 HOH   B O     
5992 O  O     . HOH   L .   ? 0.25616 0.48561 0.24212 0.05273  -0.01696 -0.02068 488 HOH   B O     
5993 O  O     . HOH   L .   ? 0.57946 0.70169 0.71914 0.15440  0.12019  0.20420  489 HOH   B O     
5994 O  O     . HOH   L .   ? 0.47363 0.38097 0.34594 0.11844  0.03513  -0.03297 490 HOH   B O     
5995 O  O     . HOH   L .   ? 0.81835 0.54282 0.57304 -0.11861 0.08647  -0.13046 491 HOH   B O     
5996 O  O     . HOH   L .   ? 0.61775 0.48031 0.95816 -0.08917 0.13859  0.14565  492 HOH   B O     
5997 O  O     . HOH   L .   ? 0.52300 0.54156 1.17738 0.02749  -0.27062 -0.26746 493 HOH   B O     
5998 O  O     . HOH   L .   ? 0.26950 0.40234 0.38813 0.10107  0.00333  0.19828  494 HOH   B O     
5999 O  O     . HOH   L .   ? 0.18307 0.38635 0.31394 0.00852  0.06095  0.02221  495 HOH   B O     
6000 O  O     . HOH   L .   ? 0.44362 0.76208 1.04448 0.18084  0.07610  0.39862  496 HOH   B O     
6001 O  O     . HOH   M .   ? 0.68276 0.45184 0.23008 -0.19316 -0.00249 0.07520  201 HOH   D O     
6002 O  O     . HOH   M .   ? 0.29256 0.66872 0.67530 -0.02431 -0.07575 0.18717  202 HOH   D O     
6003 O  O     . HOH   M .   ? 0.30581 0.68944 0.78989 -0.13477 0.03947  0.21444  203 HOH   D O     
6004 O  O     . HOH   M .   ? 0.47271 0.70364 0.47844 0.01324  0.20844  -0.18520 204 HOH   D O     
6005 O  O     . HOH   M .   ? 0.49128 0.40402 0.54769 -0.14190 -0.25540 0.12806  205 HOH   D O     
6006 O  O     . HOH   M .   ? 0.43986 1.19821 0.46294 0.01524  0.08045  -0.26607 206 HOH   D O     
6007 O  O     . HOH   M .   ? 0.66167 0.38579 0.28538 0.08827  -0.06340 0.07648  207 HOH   D O     
6008 O  O     . HOH   M .   ? 0.27269 0.54146 0.56823 0.00856  0.05557  -0.29464 208 HOH   D O     
6009 O  O     . HOH   M .   ? 0.80830 0.63272 0.45874 0.15087  0.31299  0.13420  209 HOH   D O     
6010 O  O     . HOH   M .   ? 0.47817 0.68762 0.40139 -0.02569 -0.07356 -0.01118 210 HOH   D O     
6011 O  O     . HOH   M .   ? 0.59708 0.56093 0.72912 -0.09877 -0.09358 -0.20652 211 HOH   D O     
6012 O  O     . HOH   M .   ? 0.85370 0.58781 0.92618 -0.30718 -0.23087 0.24069  212 HOH   D O     
6013 O  O     . HOH   M .   ? 0.44572 0.30756 0.78653 0.06154  0.10180  -0.17390 213 HOH   D O     
6014 O  O     . HOH   M .   ? 0.58312 0.67795 0.30506 0.29717  0.10609  0.00610  214 HOH   D O     
6015 O  O     . HOH   M .   ? 0.60496 0.40344 0.33212 0.25352  -0.17023 -0.11951 215 HOH   D O     
6016 O  O     . HOH   M .   ? 0.42175 0.58993 0.39403 0.17623  0.04119  -0.11356 216 HOH   D O     
6017 O  O     . HOH   M .   ? 0.36476 0.26470 0.26624 -0.04732 -0.03528 0.02050  217 HOH   D O     
6018 O  O     . HOH   M .   ? 0.68178 0.42539 0.26978 0.18146  -0.10389 0.05209  218 HOH   D O     
6019 O  O     . HOH   M .   ? 0.45443 0.68342 0.81457 0.07473  -0.19726 0.11865  219 HOH   D O     
6020 O  O     . HOH   M .   ? 0.22170 0.26529 0.27754 0.01022  -0.10278 0.01348  220 HOH   D O     
6021 O  O     . HOH   M .   ? 0.17047 0.22508 0.18698 0.01229  0.00448  -0.01752 221 HOH   D O     
6022 O  O     . HOH   M .   ? 0.45431 0.83143 0.26782 -0.33409 0.04137  -0.06995 222 HOH   D O     
6023 O  O     . HOH   M .   ? 0.34259 0.42372 0.34574 0.02487  0.04807  0.02765  223 HOH   D O     
6024 O  O     . HOH   M .   ? 0.14375 0.36903 0.24454 0.01985  0.00081  0.02032  224 HOH   D O     
6025 O  O     . HOH   M .   ? 0.28559 0.50311 0.86884 -0.12029 0.07334  -0.12776 225 HOH   D O     
6026 O  O     . HOH   M .   ? 0.39121 0.83798 0.31085 -0.14420 -0.07119 0.03347  226 HOH   D O     
6027 O  O     . HOH   M .   ? 0.21772 0.18526 0.27129 0.01449  -0.00523 -0.01979 227 HOH   D O     
6028 O  O     . HOH   M .   ? 0.31958 0.48413 0.90365 0.01583  0.04009  0.16616  228 HOH   D O     
6029 O  O     . HOH   M .   ? 0.73974 0.53668 0.64494 -0.17566 0.16186  -0.03718 229 HOH   D O     
6030 O  O     . HOH   M .   ? 0.40992 0.56771 0.78223 -0.19970 -0.22018 0.20144  230 HOH   D O     
6031 O  O     . HOH   M .   ? 0.42081 0.50763 0.40794 0.24436  0.02501  0.14049  231 HOH   D O     
6032 O  O     . HOH   M .   ? 0.45153 1.20205 0.38468 -0.25744 -0.02657 0.06130  232 HOH   D O     
6033 O  O     . HOH   M .   ? 0.32422 0.92285 0.72569 0.07460  -0.11478 0.21713  233 HOH   D O     
6034 O  O     . HOH   M .   ? 0.29216 0.32061 0.21421 0.00806  -0.02375 0.07602  234 HOH   D O     
6035 O  O     . HOH   M .   ? 0.32799 0.32724 0.37399 0.02076  -0.12439 0.08472  235 HOH   D O     
6036 O  O     . HOH   M .   ? 0.98013 0.36238 0.26331 -0.01661 -0.02370 -0.04429 236 HOH   D O     
6037 O  O     . HOH   M .   ? 0.25722 0.24812 0.73460 0.03124  0.10716  -0.01209 237 HOH   D O     
6038 O  O     . HOH   M .   ? 0.22297 0.32224 0.27928 -0.06646 -0.03775 -0.00839 238 HOH   D O     
6039 O  O     . HOH   M .   ? 0.18468 0.20470 0.13129 -0.00558 -0.00599 0.00747  239 HOH   D O     
6040 O  O     . HOH   M .   ? 0.57324 0.96095 0.75489 0.09758  0.33931  0.22293  240 HOH   D O     
6041 O  O     . HOH   M .   ? 0.31931 0.41512 0.43363 -0.04497 0.04342  -0.13211 241 HOH   D O     
6042 O  O     . HOH   M .   ? 0.25304 0.44382 0.70567 0.02744  0.05335  -0.05652 242 HOH   D O     
6043 O  O     . HOH   M .   ? 0.93509 0.87031 0.49396 0.17203  0.33737  0.12626  243 HOH   D O     
6044 O  O     . HOH   M .   ? 0.24164 0.27546 0.16326 -0.04023 0.05343  -0.01745 244 HOH   D O     
6045 O  O     . HOH   M .   ? 0.80910 0.34129 0.33993 -0.16228 -0.14321 -0.03874 245 HOH   D O     
6046 O  O     . HOH   M .   ? 0.28842 0.27772 0.25236 -0.01156 0.06342  0.05090  246 HOH   D O     
6047 O  O     . HOH   M .   ? 0.57424 0.53782 0.36273 -0.17713 -0.07922 -0.07982 247 HOH   D O     
6048 O  O     . HOH   M .   ? 0.37963 0.56762 0.68405 0.04316  0.07124  -0.12552 248 HOH   D O     
6049 O  O     . HOH   M .   ? 0.87234 0.53916 0.22851 -0.07631 -0.05376 0.01985  249 HOH   D O     
6050 O  O     . HOH   M .   ? 0.39901 0.49675 0.32889 -0.13873 0.13947  -0.12451 250 HOH   D O     
6051 O  O     . HOH   M .   ? 0.72020 0.56474 0.58624 -0.06953 -0.01896 -0.31878 251 HOH   D O     
6052 O  O     . HOH   M .   ? 0.45970 0.53014 0.48571 -0.13065 -0.06827 -0.22446 252 HOH   D O     
6053 O  O     . HOH   M .   ? 0.52677 0.50670 0.35704 0.22094  -0.02014 -0.17500 253 HOH   D O     
6054 O  O     . HOH   M .   ? 0.36325 0.28318 0.31296 0.10765  0.03131  0.04030  254 HOH   D O     
6055 O  O     . HOH   M .   ? 0.31638 0.27821 0.25242 0.02279  0.03778  0.02867  255 HOH   D O     
6056 O  O     . HOH   M .   ? 0.22895 0.23680 0.19598 0.01960  0.05075  0.04032  256 HOH   D O     
6057 O  O     . HOH   M .   ? 0.32149 0.64953 0.60265 -0.01023 -0.11320 0.02506  257 HOH   D O     
6058 O  O     . HOH   M .   ? 0.53466 0.25773 0.65239 -0.04900 -0.27614 0.06489  258 HOH   D O     
6059 O  O     . HOH   M .   ? 0.16547 0.23937 0.21600 0.00399  0.01892  0.00034  259 HOH   D O     
6060 O  O     . HOH   M .   ? 0.78477 0.55077 0.45812 -0.23196 -0.14749 0.23701  260 HOH   D O     
6061 O  O     . HOH   M .   ? 0.22954 0.36745 0.24888 -0.03408 0.04560  0.00396  261 HOH   D O     
6062 O  O     . HOH   M .   ? 0.29818 0.24508 0.15737 0.04716  0.05351  0.02215  262 HOH   D O     
6063 O  O     . HOH   M .   ? 0.37716 0.91531 0.82912 -0.09513 -0.02503 0.46795  263 HOH   D O     
6064 O  O     . HOH   M .   ? 0.99545 0.53872 0.95116 -0.26948 0.28561  0.12400  264 HOH   D O     
6065 O  O     . HOH   M .   ? 0.77816 0.24168 0.34461 -0.00932 -0.02317 0.02447  265 HOH   D O     
6066 O  O     . HOH   M .   ? 0.31688 0.40421 0.17271 0.05088  0.02412  -0.04614 266 HOH   D O     
6067 O  O     . HOH   M .   ? 0.52284 0.23564 0.69220 0.02096  -0.19523 0.08732  267 HOH   D O     
6068 O  O     . HOH   M .   ? 0.43553 0.21589 0.25325 0.07794  -0.08058 -0.05130 268 HOH   D O     
6069 O  O     . HOH   M .   ? 0.47809 0.23238 0.53706 0.06556  0.25619  0.10463  269 HOH   D O     
6070 O  O     . HOH   M .   ? 0.36074 0.26019 0.45354 -0.05706 0.00417  0.02419  270 HOH   D O     
6071 O  O     . HOH   M .   ? 0.52669 0.38239 0.57025 -0.03181 0.16265  -0.23932 271 HOH   D O     
6072 O  O     . HOH   M .   ? 0.21636 0.17571 0.22678 -0.00415 0.02389  0.01440  272 HOH   D O     
6073 O  O     . HOH   M .   ? 0.62574 0.39713 0.71002 -0.20642 0.00471  -0.03340 273 HOH   D O     
6074 O  O     . HOH   M .   ? 0.36686 0.31908 0.29891 -0.03311 0.10772  -0.04485 274 HOH   D O     
6075 O  O     . HOH   M .   ? 0.25971 0.33000 0.46673 -0.03913 -0.07392 0.05861  275 HOH   D O     
6076 O  O     . HOH   M .   ? 0.30880 0.42559 0.35945 0.06405  0.00411  0.03723  276 HOH   D O     
6077 O  O     . HOH   M .   ? 0.22415 0.16171 0.25324 -0.00762 -0.05107 0.03464  277 HOH   D O     
6078 O  O     . HOH   M .   ? 0.24191 0.18366 0.17233 0.01406  0.03327  0.00187  278 HOH   D O     
6079 O  O     . HOH   M .   ? 0.94360 0.45161 0.38949 -0.11419 0.17859  -0.15023 279 HOH   D O     
6080 O  O     . HOH   M .   ? 0.49837 0.30435 0.27954 0.08634  -0.05537 0.08822  280 HOH   D O     
6081 O  O     . HOH   M .   ? 0.24938 0.27189 0.37320 0.02108  -0.06619 0.05543  281 HOH   D O     
6082 O  O     . HOH   M .   ? 0.20618 0.29444 0.24241 0.01679  0.05025  -0.01449 282 HOH   D O     
6083 O  O     . HOH   M .   ? 0.82769 0.37030 0.65535 0.03847  0.39373  0.01354  283 HOH   D O     
6084 O  O     . HOH   M .   ? 0.30088 0.22504 0.46456 0.04319  0.03223  0.03673  284 HOH   D O     
6085 O  O     . HOH   M .   ? 0.27260 0.38792 0.47965 -0.03367 0.00389  0.11514  285 HOH   D O     
6086 O  O     . HOH   M .   ? 0.65409 0.55645 0.39740 -0.21705 -0.05945 0.22072  286 HOH   D O     
6087 O  O     . HOH   M .   ? 0.40418 0.24483 0.79963 0.04240  0.14383  -0.07202 287 HOH   D O     
6088 O  O     . HOH   M .   ? 0.16725 0.23271 0.41347 -0.02192 0.03106  -0.02153 288 HOH   D O     
6089 O  O     . HOH   M .   ? 0.75817 0.49741 0.94366 -0.07527 0.29368  -0.23863 289 HOH   D O     
6090 O  O     . HOH   M .   ? 0.41011 0.80323 0.82556 0.08926  -0.08916 0.37542  290 HOH   D O     
6091 O  O     . HOH   M .   ? 0.44711 0.38918 0.30609 -0.00235 0.04760  0.13677  291 HOH   D O     
6092 O  O     . HOH   M .   ? 0.61049 0.33899 0.35618 0.12553  -0.20451 -0.08607 292 HOH   D O     
6093 O  O     . HOH   M .   ? 0.19489 0.53931 0.23567 0.03403  0.05254  -0.06569 293 HOH   D O     
6094 O  O     . HOH   M .   ? 0.53937 0.33440 0.85788 -0.05542 -0.37824 0.04394  294 HOH   D O     
6095 O  O     . HOH   M .   ? 0.77596 0.30384 0.24675 0.20899  0.03117  -0.00769 295 HOH   D O     
6096 O  O     . HOH   M .   ? 0.23279 0.27510 0.22094 -0.01761 0.01076  -0.03762 296 HOH   D O     
6097 O  O     . HOH   M .   ? 1.31568 0.43127 0.45139 0.14591  -0.20969 0.01409  297 HOH   D O     
6098 O  O     . HOH   M .   ? 0.26104 0.17837 0.19525 0.01987  0.01504  0.03069  298 HOH   D O     
6099 O  O     . HOH   M .   ? 0.21948 0.25741 0.24935 0.01583  0.03040  0.00240  299 HOH   D O     
6100 O  O     . HOH   M .   ? 0.84389 0.37064 0.37555 0.22473  -0.03393 -0.09745 300 HOH   D O     
6101 O  O     . HOH   M .   ? 0.22628 0.88842 0.22657 0.04303  0.00096  -0.00921 301 HOH   D O     
6102 O  O     . HOH   M .   ? 0.19573 0.32536 0.56707 -0.02155 0.00042  0.07762  302 HOH   D O     
6103 O  O     . HOH   M .   ? 0.51244 0.31635 0.48443 -0.06697 -0.18719 -0.05146 303 HOH   D O     
6104 O  O     . HOH   M .   ? 0.56402 0.28658 0.37493 0.04480  0.09574  -0.10370 304 HOH   D O     
6105 O  O     . HOH   M .   ? 0.67721 0.55687 0.40960 0.17255  0.26890  0.03566  305 HOH   D O     
6106 O  O     A HOH   M .   ? 0.33850 0.42778 0.64043 -0.05518 -0.15293 -0.18738 306 HOH   D O     
6107 O  O     B HOH   M .   ? 0.31873 0.39415 0.47826 0.15681  -0.09058 -0.15137 306 HOH   D O     
6108 O  O     . HOH   M .   ? 0.31849 0.41949 0.60063 0.08013  0.17182  0.05346  307 HOH   D O     
6109 O  O     . HOH   M .   ? 0.23628 0.22975 0.24959 -0.00489 0.02480  0.03503  308 HOH   D O     
6110 O  O     . HOH   M .   ? 0.30049 0.82824 0.67800 0.17108  -0.03895 -0.03240 309 HOH   D O     
6111 O  O     . HOH   M .   ? 0.58576 0.79770 1.28155 -0.33859 0.02357  0.11811  310 HOH   D O     
6112 O  O     . HOH   M .   ? 0.21290 0.40244 0.40045 0.03601  0.01051  0.05568  311 HOH   D O     
6113 O  O     . HOH   M .   ? 0.49626 0.42967 0.40351 0.02348  -0.16960 -0.02734 312 HOH   D O     
6114 O  O     . HOH   M .   ? 0.75052 0.32747 0.41898 0.02771  -0.15305 0.10919  313 HOH   D O     
6115 O  O     . HOH   M .   ? 0.37018 0.70953 0.64922 -0.01655 -0.19879 -0.22278 314 HOH   D O     
6116 O  O     . HOH   M .   ? 0.95011 0.68524 0.31256 -0.22894 0.07855  -0.12226 315 HOH   D O     
6117 O  O     . HOH   M .   ? 0.41625 0.36749 0.86156 0.07834  -0.11819 -0.07569 316 HOH   D O     
6118 O  O     . HOH   M .   ? 0.39351 0.39300 0.25520 -0.02893 0.01720  -0.08628 317 HOH   D O     
6119 O  O     . HOH   M .   ? 0.29664 0.33435 0.27767 0.03294  0.05890  -0.03444 318 HOH   D O     
6120 O  O     . HOH   M .   ? 0.34914 0.38651 0.74023 -0.02402 0.09154  -0.27989 319 HOH   D O     
6121 O  O     . HOH   M .   ? 0.18322 0.25285 0.22867 0.02266  -0.01367 0.02190  320 HOH   D O     
6122 O  O     . HOH   M .   ? 0.22903 0.39525 0.76022 0.01082  0.00175  0.27030  321 HOH   D O     
6123 O  O     . HOH   M .   ? 0.53682 0.47295 0.86571 -0.13835 -0.34971 0.07191  322 HOH   D O     
6124 O  O     . HOH   M .   ? 1.09514 0.47821 0.33561 0.16494  0.09524  0.03360  323 HOH   D O     
6125 O  O     . HOH   M .   ? 0.20584 0.51434 0.48842 0.02032  -0.07465 0.04582  324 HOH   D O     
6126 O  O     . HOH   M .   ? 0.34671 0.26047 0.18359 0.12581  -0.07023 -0.03518 325 HOH   D O     
6127 O  O     . HOH   M .   ? 0.48663 0.23286 0.38068 -0.00073 0.11910  -0.01808 326 HOH   D O     
6128 O  O     . HOH   M .   ? 0.28558 0.30829 0.54085 0.08769  0.04351  0.01554  327 HOH   D O     
6129 O  O     . HOH   M .   ? 0.85991 0.35633 0.73701 -0.06793 0.03917  0.25601  328 HOH   D O     
6130 O  O     . HOH   M .   ? 0.51098 0.62810 0.39650 0.27952  -0.04753 0.08925  329 HOH   D O     
6131 O  O     . HOH   M .   ? 0.51007 0.69830 0.19804 -0.07295 -0.07043 0.03373  330 HOH   D O     
6132 O  O     . HOH   M .   ? 0.44897 0.34875 0.41558 -0.02861 0.09724  -0.09209 331 HOH   D O     
6133 O  O     . HOH   M .   ? 0.30527 0.34626 0.77439 -0.10247 0.15571  -0.09304 332 HOH   D O     
6134 O  O     . HOH   M .   ? 0.45885 0.17442 0.32115 -0.02991 0.09126  0.01515  333 HOH   D O     
6135 O  O     . HOH   M .   ? 0.38182 0.23747 0.34170 -0.01316 -0.03699 -0.00028 334 HOH   D O     
6136 O  O     . HOH   M .   ? 0.81699 0.53979 0.38008 0.34856  0.17976  0.07400  335 HOH   D O     
6137 O  O     . HOH   M .   ? 0.55978 0.69825 0.69391 0.25749  0.28322  0.37016  336 HOH   D O     
6138 O  O     . HOH   M .   ? 0.82921 0.37327 0.62509 0.06244  0.07934  0.07729  337 HOH   D O     
6139 O  O     . HOH   M .   ? 0.67205 0.50755 0.85239 0.08093  0.42501  -0.02125 338 HOH   D O     
6140 O  O     . HOH   M .   ? 0.26804 0.36078 0.32259 0.00321  -0.00658 0.01598  339 HOH   D O     
6141 O  O     . HOH   M .   ? 0.49058 0.51072 0.18530 -0.02569 -0.02995 0.04338  340 HOH   D O     
6142 O  O     . HOH   M .   ? 0.18575 0.50373 0.29061 -0.01694 0.02518  0.10483  341 HOH   D O     
6143 O  O     . HOH   M .   ? 0.58430 0.35261 0.43534 0.06591  0.09703  0.07464  342 HOH   D O     
6144 O  O     . HOH   M .   ? 0.56559 0.37304 0.64922 0.01369  0.04497  0.21159  343 HOH   D O     
6145 O  O     . HOH   M .   ? 0.66524 0.76130 0.67609 0.06323  -0.05561 0.41431  344 HOH   D O     
6146 O  O     A HOH   M .   ? 0.69368 0.50841 0.55529 0.21946  0.16704  0.05178  345 HOH   D O     
6147 O  O     B HOH   M .   ? 0.79805 0.53029 0.52321 0.36685  0.01156  -0.05329 345 HOH   D O     
6148 O  O     . HOH   M .   ? 0.55181 0.25970 0.37966 0.01731  0.12856  0.01013  346 HOH   D O     
6149 O  O     . HOH   M .   ? 0.32018 0.37327 0.26107 0.04804  0.10946  0.05621  347 HOH   D O     
6150 O  O     . HOH   M .   ? 0.41846 0.86467 0.36571 0.03726  -0.09223 -0.13168 348 HOH   D O     
6151 O  O     . HOH   M .   ? 0.26231 0.44247 0.32042 -0.01323 0.03339  -0.10284 349 HOH   D O     
6152 O  O     . HOH   M .   ? 0.61576 0.32559 0.94967 -0.13996 0.20225  -0.01858 350 HOH   D O     
6153 O  O     . HOH   M .   ? 0.62547 0.85889 0.52967 0.16458  -0.21530 0.20736  351 HOH   D O     
6154 O  O     . HOH   M .   ? 0.29857 0.24418 0.32582 -0.00441 0.07086  -0.03706 352 HOH   D O     
6155 O  O     . HOH   M .   ? 0.20365 0.27147 0.35892 -0.03366 -0.02327 0.06749  353 HOH   D O     
6156 O  O     . HOH   M .   ? 0.94051 0.33751 0.41889 0.14475  0.11824  -0.07001 354 HOH   D O     
6157 O  O     . HOH   M .   ? 0.57298 0.86622 0.36843 -0.10237 -0.07126 -0.07996 355 HOH   D O     
6158 O  O     . HOH   M .   ? 0.96692 0.54929 0.42586 -0.05023 -0.20753 -0.00503 356 HOH   D O     
6159 O  O     . HOH   M .   ? 0.22211 0.36113 0.28473 0.05494  0.01588  0.04052  357 HOH   D O     
6160 O  O     . HOH   M .   ? 0.58088 0.62201 1.14820 0.13664  0.35707  0.34815  358 HOH   D O     
6161 O  O     . HOH   M .   ? 0.22602 0.20961 0.34172 -0.01335 -0.00565 -0.01098 359 HOH   D O     
6162 O  O     . HOH   M .   ? 0.48865 1.09348 0.42882 -0.11364 -0.07348 0.04439  360 HOH   D O     
6163 O  O     . HOH   M .   ? 0.37442 0.42242 0.56361 0.02672  0.24653  0.05235  361 HOH   D O     
6164 O  O     . HOH   M .   ? 0.66788 0.69667 0.83448 -0.21443 -0.33449 0.37803  362 HOH   D O     
6165 O  O     . HOH   M .   ? 0.56712 0.42536 1.05756 0.08183  0.39896  0.19432  363 HOH   D O     
6166 O  O     . HOH   M .   ? 0.69201 0.49036 0.49073 -0.02656 0.18159  0.14651  364 HOH   D O     
6167 O  O     . HOH   M .   ? 0.43155 0.70314 0.31384 0.09611  0.01329  0.13774  365 HOH   D O     
6168 O  O     . HOH   M .   ? 0.47474 0.64169 0.42952 0.13916  0.22370  0.18206  366 HOH   D O     
6169 O  O     . HOH   M .   ? 0.71572 0.73559 0.90973 -0.29587 -0.40058 0.41489  367 HOH   D O     
6170 O  O     . HOH   M .   ? 0.96005 0.50279 0.62447 -0.19135 0.19080  -0.04211 368 HOH   D O     
6171 O  O     . HOH   M .   ? 0.58969 0.39002 0.31105 -0.04352 0.07860  -0.00804 369 HOH   D O     
6172 O  O     . HOH   M .   ? 0.54730 0.78266 0.34158 -0.00734 0.13636  -0.19883 370 HOH   D O     
6173 O  O     . HOH   M .   ? 0.69058 0.62984 0.58283 -0.06270 -0.10146 -0.31969 371 HOH   D O     
6174 O  O     . HOH   M .   ? 0.38166 0.86518 1.13630 0.13880  0.04784  0.32724  372 HOH   D O     
6175 O  O     . HOH   M .   ? 1.20687 0.31703 0.33431 0.01171  0.11935  -0.01036 373 HOH   D O     
6176 O  O     . HOH   M .   ? 0.22513 0.31148 0.32749 -0.00390 0.00220  -0.01268 374 HOH   D O     
6177 O  O     . HOH   M .   ? 0.63749 0.37572 0.89402 -0.19811 -0.04371 -0.14325 375 HOH   D O     
6178 O  O     . HOH   M .   ? 0.48781 0.41874 0.76516 0.12830  0.26305  0.02736  376 HOH   D O     
6179 O  O     . HOH   M .   ? 0.32820 1.09182 0.42173 -0.03087 -0.08676 -0.03926 377 HOH   D O     
6180 O  O     . HOH   M .   ? 0.55833 0.68222 0.93872 0.10812  0.17427  0.45628  378 HOH   D O     
6181 O  O     . HOH   M .   ? 0.34945 0.38136 0.28850 0.08817  0.06664  0.07881  379 HOH   D O     
6182 O  O     . HOH   M .   ? 0.50675 0.33479 0.37601 -0.03082 0.18261  -0.02638 380 HOH   D O     
6183 O  O     . HOH   M .   ? 0.72658 0.31327 0.54816 -0.00490 -0.13024 -0.02004 381 HOH   D O     
6184 O  O     . HOH   M .   ? 0.91458 0.35580 0.76423 0.00859  -0.48705 0.01573  382 HOH   D O     
6185 O  O     . HOH   M .   ? 0.38063 0.53843 1.23415 -0.10562 0.13545  -0.02740 383 HOH   D O     
6186 O  O     . HOH   M .   ? 0.99980 0.35901 0.33483 -0.10276 -0.20291 0.02708  384 HOH   D O     
6187 O  O     . HOH   M .   ? 0.55563 0.45355 1.08375 0.13588  0.04025  0.16380  385 HOH   D O     
6188 O  O     . HOH   M .   ? 0.41082 0.63423 1.23340 -0.16380 -0.12268 0.12160  386 HOH   D O     
6189 O  O     . HOH   M .   ? 0.61939 0.51519 0.32193 -0.32622 0.09138  -0.04395 387 HOH   D O     
6190 O  O     . HOH   M .   ? 0.89588 0.72150 0.71249 -0.15402 -0.03786 0.18700  388 HOH   D O     
6191 O  O     . HOH   M .   ? 0.38736 0.42540 0.39332 0.02973  -0.06406 0.03447  389 HOH   D O     
6192 O  O     . HOH   M .   ? 1.14743 0.47632 0.33460 -0.34664 -0.05323 0.02862  390 HOH   D O     
6193 O  O     . HOH   M .   ? 0.81313 0.50477 0.61253 0.06308  0.08805  -0.07470 391 HOH   D O     
6194 O  O     . HOH   M .   ? 0.42896 0.33689 0.46393 -0.02249 0.01286  -0.14055 392 HOH   D O     
6195 O  O     . HOH   M .   ? 0.80535 0.71476 0.61191 0.22711  0.36280  0.24755  393 HOH   D O     
6196 O  O     . HOH   M .   ? 0.35170 0.27122 0.24332 -0.08595 0.05384  -0.06977 394 HOH   D O     
6197 O  O     . HOH   M .   ? 0.92010 0.66423 0.36164 0.15533  -0.03846 -0.20661 395 HOH   D O     
6198 O  O     . HOH   M .   ? 0.50062 0.68111 0.48511 0.02473  -0.01831 0.08778  396 HOH   D O     
6199 O  O     . HOH   M .   ? 0.70367 0.42614 0.88723 0.10587  0.10864  -0.17109 397 HOH   D O     
6200 O  O     . HOH   M .   ? 0.84617 0.42098 0.95163 0.22188  -0.02430 0.21717  398 HOH   D O     
6201 O  O     . HOH   M .   ? 0.58845 0.84451 0.74393 -0.00606 0.19290  -0.06041 399 HOH   D O     
6202 O  O     . HOH   M .   ? 0.50276 0.89142 0.51628 -0.28217 0.13730  -0.33983 400 HOH   D O     
6203 O  O     A HOH   M .   ? 0.27785 0.42657 0.68243 -0.02540 0.10079  -0.22030 401 HOH   D O     
6204 O  O     B HOH   M .   ? 0.49253 0.37588 0.25473 -0.17250 -0.15920 0.08518  401 HOH   D O     
6205 O  O     . HOH   M .   ? 0.72183 0.54291 0.52112 0.16245  -0.20155 0.01765  402 HOH   D O     
6206 O  O     . HOH   M .   ? 0.53804 0.65786 0.46305 0.05966  -0.28807 0.04581  403 HOH   D O     
6207 O  O     . HOH   M .   ? 0.47854 0.73009 0.42569 0.00129  0.12476  -0.13787 404 HOH   D O     
6208 O  O     . HOH   M .   ? 0.75873 0.65298 0.69123 0.12784  -0.31928 0.01110  405 HOH   D O     
6209 O  O     . HOH   M .   ? 0.89705 0.60607 0.75763 -0.34605 0.35417  -0.16094 406 HOH   D O     
6210 O  O     . HOH   M .   ? 0.48743 0.80634 0.33450 0.33531  0.06399  0.02963  407 HOH   D O     
6211 O  O     . HOH   M .   ? 1.05312 0.45641 0.96964 0.29014  -0.15998 0.09022  408 HOH   D O     
6212 O  O     . HOH   M .   ? 0.21900 0.23481 0.33335 -0.02605 0.02129  -0.00277 409 HOH   D O     
6213 O  O     . HOH   M .   ? 0.50444 0.41743 1.45086 0.07010  -0.16932 0.00847  410 HOH   D O     
6214 O  O     . HOH   M .   ? 0.37844 0.61134 0.74387 -0.17845 -0.15435 0.12074  411 HOH   D O     
6215 O  O     . HOH   M .   ? 0.40778 0.29451 0.32663 0.06193  0.09048  0.08170  412 HOH   D O     
6216 O  O     . HOH   M .   ? 0.44601 0.37274 0.25579 -0.15728 0.02230  -0.01982 413 HOH   D O     
6217 O  O     . HOH   M .   ? 0.49963 0.32181 0.37214 0.14216  -0.08865 0.00028  414 HOH   D O     
6218 O  O     . HOH   M .   ? 0.77967 0.37721 0.97212 0.21855  -0.09405 -0.00114 415 HOH   D O     
6219 O  O     . HOH   M .   ? 0.93686 0.49389 0.44582 0.11695  0.09704  0.12322  416 HOH   D O     
6220 O  O     . HOH   M .   ? 0.53297 1.10718 0.63691 0.29614  -0.20361 -0.41567 417 HOH   D O     
6221 O  O     . HOH   M .   ? 0.50443 1.23537 0.36699 0.28982  -0.05807 -0.14996 418 HOH   D O     
6222 O  O     . HOH   M .   ? 0.56234 0.56342 0.57635 0.01437  0.24718  0.07561  419 HOH   D O     
6223 O  O     . HOH   M .   ? 0.55614 0.26642 0.79716 -0.03673 -0.27870 0.09644  420 HOH   D O     
6224 O  O     . HOH   M .   ? 0.77201 0.37725 0.85373 0.09906  0.42725  0.16143  421 HOH   D O     
6225 O  O     . HOH   M .   ? 0.24462 0.78579 0.69896 0.05037  -0.05168 -0.19383 422 HOH   D O     
6226 O  O     . HOH   M .   ? 0.95181 0.70890 0.44263 0.39659  -0.06869 0.08957  423 HOH   D O     
6227 O  O     . HOH   M .   ? 0.39869 1.04160 0.59695 0.23247  -0.11854 -0.32334 424 HOH   D O     
6228 O  O     . HOH   M .   ? 1.05694 0.33445 0.49278 0.08027  0.20785  -0.06074 425 HOH   D O     
6229 O  O     . HOH   M .   ? 0.39120 1.26072 0.48087 -0.07271 -0.10776 0.02770  426 HOH   D O     
6230 O  O     . HOH   M .   ? 0.60115 0.39576 0.91393 0.00782  -0.31945 0.17182  427 HOH   D O     
6231 O  O     . HOH   M .   ? 0.45089 0.31308 0.36337 0.15208  -0.04915 -0.03152 428 HOH   D O     
6232 O  O     . HOH   M .   ? 0.44050 0.28695 0.51874 0.02341  0.04228  -0.00794 429 HOH   D O     
6233 O  O     . HOH   M .   ? 0.35718 0.32640 0.43439 -0.02560 0.18044  -0.01654 430 HOH   D O     
6234 O  O     . HOH   M .   ? 0.51101 0.66500 1.08417 0.01761  0.19260  -0.27441 431 HOH   D O     
6235 O  O     . HOH   M .   ? 0.82742 0.36796 0.48876 -0.20395 0.28119  -0.11755 432 HOH   D O     
6236 O  O     . HOH   M .   ? 0.74043 0.43198 0.86039 -0.01222 0.21488  0.13315  433 HOH   D O     
6237 O  O     . HOH   M .   ? 0.63517 0.48491 0.52383 0.11656  0.19623  0.20742  434 HOH   D O     
6238 O  O     . HOH   M .   ? 0.38236 1.01908 0.81785 0.17791  0.07635  0.37002  435 HOH   D O     
6239 O  O     . HOH   M .   ? 0.27811 0.98889 0.39113 -0.12976 -0.01568 0.07169  436 HOH   D O     
6240 O  O     . HOH   M .   ? 0.67860 0.50691 0.74914 0.00066  -0.31606 0.23300  437 HOH   D O     
6241 O  O     . HOH   M .   ? 0.36869 0.76649 0.46825 0.18895  -0.04818 -0.22570 438 HOH   D O     
6242 O  O     . HOH   M .   ? 0.85301 0.62879 0.84556 0.29904  -0.22814 0.18912  439 HOH   D O     
6243 O  O     . HOH   N .   ? 0.56804 0.52430 0.78261 -0.07788 -0.36015 -0.05957 201 HOH   C O     
6244 O  O     . HOH   N .   ? 0.32936 0.73596 0.90401 0.07139  0.21839  -0.02240 202 HOH   C O     
6245 O  O     . HOH   N .   ? 0.61724 0.29735 0.74236 0.11581  0.10195  -0.14949 203 HOH   C O     
6246 O  O     . HOH   N .   ? 0.51019 0.51712 0.57490 -0.12701 0.10320  0.02016  204 HOH   C O     
6247 O  O     . HOH   N .   ? 0.23358 0.69084 0.45368 -0.03288 0.05095  0.05741  205 HOH   C O     
6248 O  O     . HOH   N .   ? 0.46491 0.44817 0.93521 0.17179  0.24265  0.13495  206 HOH   C O     
6249 O  O     . HOH   N .   ? 0.31910 0.52138 0.29413 -0.09756 -0.07779 0.06789  207 HOH   C O     
6250 O  O     . HOH   N .   ? 0.54287 0.40997 0.64713 0.05260  -0.18949 -0.25167 208 HOH   C O     
6251 O  O     . HOH   N .   ? 0.89247 0.63494 0.62289 0.37990  -0.25423 -0.04717 209 HOH   C O     
6252 O  O     . HOH   N .   ? 0.37247 0.60121 0.38911 0.05286  0.13324  -0.01711 210 HOH   C O     
6253 O  O     . HOH   N .   ? 0.98930 0.46989 0.37619 0.16732  0.07515  0.00800  211 HOH   C O     
6254 O  O     . HOH   N .   ? 0.52305 0.44044 0.42045 -0.00973 -0.07381 -0.01736 212 HOH   C O     
6255 O  O     . HOH   N .   ? 0.39528 0.76433 1.07371 0.13179  -0.17935 -0.37798 213 HOH   C O     
6256 O  O     . HOH   N .   ? 0.76881 0.42209 0.34857 -0.07245 -0.24318 0.02129  214 HOH   C O     
6257 O  O     . HOH   N .   ? 0.44927 0.61034 0.52682 -0.16136 0.03668  -0.25731 215 HOH   C O     
6258 O  O     . HOH   N .   ? 0.45333 0.54191 0.69177 0.18442  0.27788  0.16555  216 HOH   C O     
6259 O  O     . HOH   N .   ? 0.78644 0.76422 0.71402 0.07725  -0.25770 -0.21443 217 HOH   C O     
6260 O  O     . HOH   N .   ? 0.64051 0.40284 0.64053 0.06208  0.37486  0.00593  218 HOH   C O     
6261 O  O     . HOH   N .   ? 0.36897 0.56449 0.26221 -0.11181 -0.07155 0.16223  219 HOH   C O     
6262 O  O     . HOH   N .   ? 0.70774 0.47748 0.31933 -0.14316 -0.07033 -0.06001 220 HOH   C O     
6263 O  O     . HOH   N .   ? 0.44384 0.26932 0.64400 -0.07497 -0.08830 0.06034  221 HOH   C O     
6264 O  O     . HOH   N .   ? 0.33846 0.62155 0.97454 -0.01193 0.23065  0.02563  222 HOH   C O     
6265 O  O     . HOH   N .   ? 0.70797 0.26986 0.80903 -0.05287 -0.24786 0.02509  223 HOH   C O     
6266 O  O     . HOH   N .   ? 0.35167 0.65941 0.39210 -0.19540 -0.07110 0.24165  224 HOH   C O     
6267 O  O     . HOH   N .   ? 0.19427 0.19611 0.18111 -0.00512 -0.04207 -0.00583 225 HOH   C O     
6268 O  O     . HOH   N .   ? 0.17018 0.17713 0.23886 0.00830  -0.01574 0.00458  226 HOH   C O     
6269 O  O     . HOH   N .   ? 0.27688 0.84267 0.38960 0.07217  0.08118  0.09260  227 HOH   C O     
6270 O  O     . HOH   N .   ? 0.84913 0.63983 0.36608 0.26616  0.09148  -0.07305 228 HOH   C O     
6271 O  O     . HOH   N .   ? 0.42452 0.35268 0.26199 0.01379  -0.05369 -0.02627 229 HOH   C O     
6272 O  O     . HOH   N .   ? 0.36092 0.35511 0.53551 -0.02352 -0.11704 -0.13007 230 HOH   C O     
6273 O  O     . HOH   N .   ? 0.42873 0.51699 0.47128 0.01907  0.25360  -0.08693 231 HOH   C O     
6274 O  O     . HOH   N .   ? 0.47843 0.29377 0.22290 -0.07447 0.08036  -0.05392 232 HOH   C O     
6275 O  O     . HOH   N .   ? 0.29035 0.30419 0.25591 -0.02205 -0.02498 -0.00890 233 HOH   C O     
6276 O  O     . HOH   N .   ? 0.37648 0.63936 0.50915 0.18292  -0.18810 -0.27457 234 HOH   C O     
6277 O  O     . HOH   N .   ? 0.15970 0.21039 0.16262 -0.02045 -0.00214 -0.03923 235 HOH   C O     
6278 O  O     . HOH   N .   ? 0.29740 0.39711 0.53392 -0.01964 -0.15499 0.12417  236 HOH   C O     
6279 O  O     . HOH   N .   ? 0.68305 0.40482 0.32051 -0.12557 0.20666  -0.11319 237 HOH   C O     
6280 O  O     . HOH   N .   ? 0.35684 0.73507 0.72281 0.13466  -0.17104 -0.36731 238 HOH   C O     
6281 O  O     . HOH   N .   ? 0.22848 0.35647 0.26489 0.07869  -0.07145 0.00403  239 HOH   C O     
6282 O  O     . HOH   N .   ? 0.18539 0.18506 0.17486 0.01204  -0.03857 0.03092  240 HOH   C O     
6283 O  O     . HOH   N .   ? 0.21235 0.20287 0.20612 -0.01494 -0.01270 0.01402  241 HOH   C O     
6284 O  O     . HOH   N .   ? 0.31361 0.40372 0.30464 -0.04818 -0.08648 0.04671  242 HOH   C O     
6285 O  O     . HOH   N .   ? 0.17773 0.27273 0.26658 0.02945  0.03147  -0.02149 243 HOH   C O     
6286 O  O     . HOH   N .   ? 0.37953 0.58873 0.24874 0.14116  -0.05478 -0.01646 244 HOH   C O     
6287 O  O     . HOH   N .   ? 0.30824 0.26037 0.43766 -0.08659 -0.04582 0.01881  245 HOH   C O     
6288 O  O     . HOH   N .   ? 0.33959 0.47030 0.40780 -0.13022 -0.11481 0.13569  246 HOH   C O     
6289 O  O     . HOH   N .   ? 0.22097 0.29524 0.19322 -0.00868 -0.08503 0.03310  247 HOH   C O     
6290 O  O     . HOH   N .   ? 0.20127 0.31373 0.23872 0.02179  -0.03949 0.03845  248 HOH   C O     
6291 O  O     . HOH   N .   ? 0.37606 0.58675 0.57549 0.19963  0.17786  0.30454  249 HOH   C O     
6292 O  O     . HOH   N .   ? 0.44500 0.58502 0.47657 0.02250  -0.13914 -0.02678 250 HOH   C O     
6293 O  O     . HOH   N .   ? 0.27311 0.32966 0.22617 -0.05657 -0.00804 0.05530  251 HOH   C O     
6294 O  O     . HOH   N .   ? 0.39680 0.84279 0.68403 -0.08539 0.10917  0.06171  252 HOH   C O     
6295 O  O     . HOH   N .   ? 0.44200 0.65886 0.60258 0.07496  0.01733  -0.22233 253 HOH   C O     
6296 O  O     . HOH   N .   ? 0.29391 0.46260 0.48907 0.00654  0.10844  -0.06112 254 HOH   C O     
6297 O  O     . HOH   N .   ? 0.49310 0.78182 0.36107 0.05494  0.14010  0.14381  255 HOH   C O     
6298 O  O     . HOH   N .   ? 0.30345 0.87651 0.72441 0.01749  0.11335  0.26072  256 HOH   C O     
6299 O  O     . HOH   N .   ? 0.63527 0.24424 0.41524 -0.03583 0.21162  0.05634  257 HOH   C O     
6300 O  O     . HOH   N .   ? 0.61755 0.27320 0.63782 -0.11732 -0.17134 0.10523  258 HOH   C O     
6301 O  O     . HOH   N .   ? 0.22601 0.27361 0.28591 -0.02783 -0.00415 0.02233  259 HOH   C O     
6302 O  O     . HOH   N .   ? 0.49018 0.30477 0.25946 -0.04091 0.10308  0.01727  260 HOH   C O     
6303 O  O     . HOH   N .   ? 0.30910 0.24841 0.31995 -0.03920 -0.03485 -0.00784 261 HOH   C O     
6304 O  O     . HOH   N .   ? 0.75667 0.44481 0.42672 0.25317  -0.12959 -0.03641 262 HOH   C O     
6305 O  O     . HOH   N .   ? 0.30737 0.29940 0.43942 -0.03373 -0.15279 0.03144  263 HOH   C O     
6306 O  O     . HOH   N .   ? 0.66660 0.48452 0.59719 0.28484  0.28035  0.19281  264 HOH   C O     
6307 O  O     . HOH   N .   ? 0.30928 0.21191 0.42910 -0.00601 -0.05047 0.02622  265 HOH   C O     
6308 O  O     . HOH   N .   ? 0.98570 0.32976 0.84119 0.20360  -0.02996 -0.07791 266 HOH   C O     
6309 O  O     . HOH   N .   ? 0.53147 0.24128 0.23163 0.00238  0.06877  0.01551  267 HOH   C O     
6310 O  O     . HOH   N .   ? 0.25554 0.26173 0.19755 -0.07210 -0.06793 0.03366  268 HOH   C O     
6311 O  O     . HOH   N .   ? 0.54654 0.53261 0.38938 0.19723  -0.02385 -0.21009 269 HOH   C O     
6312 O  O     . HOH   N .   ? 0.75922 0.36586 0.33654 -0.01345 -0.03598 0.01557  270 HOH   C O     
6313 O  O     . HOH   N .   ? 0.19117 0.16633 0.21367 0.01536  0.03027  0.03614  271 HOH   C O     
6314 O  O     . HOH   N .   ? 0.20490 0.29190 0.15456 -0.00160 -0.07281 0.01924  272 HOH   C O     
6315 O  O     . HOH   N .   ? 0.90754 0.69525 0.32205 0.07893  0.13536  -0.06364 273 HOH   C O     
6316 O  O     . HOH   N .   ? 0.19488 0.28038 0.25206 -0.01109 -0.01273 -0.00067 274 HOH   C O     
6317 O  O     . HOH   N .   ? 0.25852 0.43320 0.34084 -0.05167 -0.07513 0.07809  275 HOH   C O     
6318 O  O     . HOH   N .   ? 0.42113 0.78239 0.59622 0.15387  0.02669  -0.32498 276 HOH   C O     
6319 O  O     . HOH   N .   ? 0.33814 0.41146 0.23222 0.08626  -0.04710 -0.03326 277 HOH   C O     
6320 O  O     . HOH   N .   ? 0.74499 0.37959 0.73793 -0.19044 0.23032  -0.20074 278 HOH   C O     
6321 O  O     . HOH   N .   ? 0.61331 0.36385 0.63448 0.03385  0.29406  -0.09291 279 HOH   C O     
6322 O  O     . HOH   N .   ? 0.60437 0.61057 0.38203 0.33733  0.19902  0.19808  280 HOH   C O     
6323 O  O     . HOH   N .   ? 0.39435 1.02074 0.55025 -0.03595 0.04221  0.25753  281 HOH   C O     
6324 O  O     . HOH   N .   ? 0.73300 0.46497 0.73467 -0.06369 -0.10342 -0.30945 282 HOH   C O     
6325 O  O     . HOH   N .   ? 0.16475 0.25181 0.25706 -0.02695 -0.04392 0.00475  283 HOH   C O     
6326 O  O     . HOH   N .   ? 0.32526 0.46841 0.40796 -0.01598 0.12262  -0.08742 284 HOH   C O     
6327 O  O     . HOH   N .   ? 0.22608 0.17980 0.16728 -0.02108 -0.04074 0.01745  285 HOH   C O     
6328 O  O     . HOH   N .   ? 0.40821 0.31784 0.61031 -0.07862 -0.05734 -0.09678 286 HOH   C O     
6329 O  O     . HOH   N .   ? 0.31368 0.28558 0.32123 -0.05061 -0.11698 0.02221  287 HOH   C O     
6330 O  O     . HOH   N .   ? 0.89917 0.37352 0.55651 0.02564  -0.28222 -0.08203 288 HOH   C O     
6331 O  O     . HOH   N .   ? 0.44902 0.37997 0.72913 -0.19785 -0.14568 0.06658  289 HOH   C O     
6332 O  O     . HOH   N .   ? 0.64550 0.36783 0.85009 -0.25634 0.02618  -0.00380 290 HOH   C O     
6333 O  O     . HOH   N .   ? 0.26820 0.78247 0.32234 0.01978  -0.02454 -0.00820 291 HOH   C O     
6334 O  O     . HOH   N .   ? 0.25969 0.42912 0.25097 -0.01350 -0.10770 0.03902  292 HOH   C O     
6335 O  O     . HOH   N .   ? 0.84466 0.40138 0.40598 0.13317  -0.20307 -0.14754 293 HOH   C O     
6336 O  O     . HOH   N .   ? 0.33037 0.25501 0.44460 -0.01948 0.04777  0.09486  294 HOH   C O     
6337 O  O     . HOH   N .   ? 0.57559 0.34232 1.24969 0.05337  -0.22018 -0.01173 295 HOH   C O     
6338 O  O     . HOH   N .   ? 0.20680 0.19864 0.14945 -0.01736 -0.01659 -0.02517 296 HOH   C O     
6339 O  O     . HOH   N .   ? 0.84630 0.33296 0.55830 -0.06605 0.39423  -0.04728 297 HOH   C O     
6340 O  O     . HOH   N .   ? 0.61735 0.33664 0.33216 -0.14307 -0.18236 0.11317  298 HOH   C O     
6341 O  O     . HOH   N .   ? 0.34508 0.92397 0.62824 -0.19107 0.09911  -0.18926 299 HOH   C O     
6342 O  O     . HOH   N .   ? 0.77827 0.47146 0.23791 -0.00888 0.01986  -0.10253 300 HOH   C O     
6343 O  O     . HOH   N .   ? 0.45510 0.50183 0.37188 -0.17571 -0.11619 0.03926  301 HOH   C O     
6344 O  O     . HOH   N .   ? 0.61629 0.46954 0.30850 -0.01553 0.03635  0.11212  302 HOH   C O     
6345 O  O     . HOH   N .   ? 0.67246 0.37488 0.35246 -0.18392 0.04963  -0.14575 303 HOH   C O     
6346 O  O     . HOH   N .   ? 0.52377 0.42049 0.20226 0.26172  0.06479  0.05733  304 HOH   C O     
6347 O  O     . HOH   N .   ? 0.20389 0.19204 0.17599 0.03115  -0.04109 -0.02465 305 HOH   C O     
6348 O  O     . HOH   N .   ? 1.04065 0.62700 0.83366 0.37394  -0.13341 -0.26505 306 HOH   C O     
6349 O  O     . HOH   N .   ? 0.76042 0.48454 1.03738 0.05538  0.43162  0.22908  307 HOH   C O     
6350 O  O     . HOH   N .   ? 0.50374 0.48122 0.76624 0.20085  -0.05363 -0.14105 308 HOH   C O     
6351 O  O     . HOH   N .   ? 0.62526 0.57095 0.21442 -0.04377 -0.08088 0.03252  309 HOH   C O     
6352 O  O     . HOH   N .   ? 0.31169 0.50201 0.19712 0.15628  -0.03672 -0.05313 310 HOH   C O     
6353 O  O     . HOH   N .   ? 0.70776 0.55152 0.36950 0.33619  -0.01532 0.07784  311 HOH   C O     
6354 O  O     . HOH   N .   ? 0.34612 0.29086 0.68810 -0.01700 0.09474  -0.05118 312 HOH   C O     
6355 O  O     . HOH   N .   ? 0.46683 0.41789 0.40295 -0.05873 -0.05235 -0.08669 313 HOH   C O     
6356 O  O     . HOH   N .   ? 0.36244 0.45793 0.51349 -0.03976 -0.13522 -0.01401 314 HOH   C O     
6357 O  O     . HOH   N .   ? 0.33754 0.36539 0.23340 -0.01968 -0.00787 0.01453  315 HOH   C O     
6358 O  O     . HOH   N .   ? 0.66597 0.53785 0.38394 0.25189  0.09042  -0.11465 316 HOH   C O     
6359 O  O     . HOH   N .   ? 0.31737 0.48779 0.46295 0.10102  -0.09062 -0.03290 317 HOH   C O     
6360 O  O     . HOH   N .   ? 0.18129 0.33992 0.21649 0.01197  -0.01745 0.04111  318 HOH   C O     
6361 O  O     . HOH   N .   ? 0.20449 0.57227 0.30780 0.00288  0.02922  0.08045  319 HOH   C O     
6362 O  O     . HOH   N .   ? 0.44299 0.22437 0.31851 -0.05321 0.01114  0.04583  320 HOH   C O     
6363 O  O     . HOH   N .   ? 0.18133 0.25767 0.24245 0.00674  -0.01288 0.01878  321 HOH   C O     
6364 O  O     . HOH   N .   ? 0.25980 0.24549 0.19745 -0.09868 0.03554  -0.03579 322 HOH   C O     
6365 O  O     . HOH   N .   ? 0.68842 0.79824 0.52957 -0.25577 0.07458  -0.09074 323 HOH   C O     
6366 O  O     . HOH   N .   ? 0.33966 0.27160 0.57723 0.04431  -0.02353 0.03128  324 HOH   C O     
6367 O  O     . HOH   N .   ? 0.78462 0.49659 0.46354 -0.03704 -0.05564 0.07096  325 HOH   C O     
6368 O  O     . HOH   N .   ? 0.28855 0.52419 0.46988 0.08568  0.01016  0.13978  326 HOH   C O     
6369 O  O     . HOH   N .   ? 0.38400 0.80982 0.25314 0.20853  0.06239  0.08966  327 HOH   C O     
6370 O  O     . HOH   N .   ? 0.66403 0.26813 0.42374 -0.08560 -0.21980 -0.03859 328 HOH   C O     
6371 O  O     . HOH   N .   ? 0.40759 0.38363 0.22190 -0.06121 -0.00904 0.06553  329 HOH   C O     
6372 O  O     . HOH   N .   ? 0.62062 0.62969 0.30201 0.01865  0.08451  0.01086  330 HOH   C O     
6373 O  O     . HOH   N .   ? 0.55760 0.33876 0.80070 -0.15073 0.22203  -0.04496 331 HOH   C O     
6374 O  O     . HOH   N .   ? 0.20903 0.44928 0.28892 0.03567  -0.00828 0.07083  332 HOH   C O     
6375 O  O     . HOH   N .   ? 0.43275 0.43378 0.53602 -0.05545 0.17967  0.10673  333 HOH   C O     
6376 O  O     . HOH   N .   ? 0.23128 0.52856 0.49536 0.01610  -0.09288 -0.03214 334 HOH   C O     
6377 O  O     . HOH   N .   ? 0.56461 0.59456 0.58391 -0.01979 0.29921  0.07774  335 HOH   C O     
6378 O  O     . HOH   N .   ? 0.32485 0.68244 0.76051 0.08984  -0.00674 0.35066  336 HOH   C O     
6379 O  O     . HOH   N .   ? 0.55334 0.32609 0.89662 0.03541  -0.01377 0.01990  337 HOH   C O     
6380 O  O     . HOH   N .   ? 0.61661 0.74842 0.39013 -0.01790 -0.00273 -0.11415 338 HOH   C O     
6381 O  O     . HOH   N .   ? 0.75913 0.68254 0.34961 0.38755  -0.15947 -0.10941 339 HOH   C O     
6382 O  O     . HOH   N .   ? 0.45896 0.55577 0.31601 -0.19495 0.00923  0.10626  340 HOH   C O     
6383 O  O     . HOH   N .   ? 0.78676 0.38251 0.36361 -0.21659 -0.21063 0.03219  341 HOH   C O     
6384 O  O     . HOH   N .   ? 0.27332 0.30252 0.23886 0.04076  -0.02252 0.00847  342 HOH   C O     
6385 O  O     . HOH   N .   ? 0.50432 0.78867 0.28221 0.12429  -0.08114 -0.10805 343 HOH   C O     
6386 O  O     . HOH   N .   ? 0.53231 0.45673 0.90686 -0.07290 -0.35092 -0.04721 344 HOH   C O     
6387 O  O     . HOH   N .   ? 0.66254 0.63412 0.61484 0.01175  -0.07386 0.09831  345 HOH   C O     
6388 O  O     . HOH   N .   ? 0.27090 0.51230 0.33196 -0.08807 -0.07813 0.16778  346 HOH   C O     
6389 O  O     . HOH   N .   ? 0.59136 0.51051 0.39743 -0.13137 0.19034  -0.11497 347 HOH   C O     
6390 O  O     . HOH   N .   ? 0.62769 0.68459 0.62359 -0.11908 0.00803  -0.27726 348 HOH   C O     
6391 O  O     . HOH   N .   ? 0.74063 0.34370 0.38614 -0.19036 0.16469  -0.02350 349 HOH   C O     
6392 O  O     . HOH   N .   ? 0.46087 0.81434 0.20980 0.01870  -0.01472 0.01527  350 HOH   C O     
6393 O  O     . HOH   N .   ? 0.29133 0.30922 0.23571 -0.01536 0.00962  0.02543  351 HOH   C O     
6394 O  O     . HOH   N .   ? 0.36533 0.22414 0.20398 0.06692  -0.06804 -0.03551 352 HOH   C O     
6395 O  O     . HOH   N .   ? 0.40221 0.64706 0.67726 0.16754  -0.00919 -0.11265 353 HOH   C O     
6396 O  O     . HOH   N .   ? 0.75265 0.40005 0.86654 -0.10669 0.13068  -0.06321 354 HOH   C O     
6397 O  O     . HOH   N .   ? 0.58897 0.38485 0.63527 -0.12822 -0.19010 0.15731  355 HOH   C O     
6398 O  O     . HOH   N .   ? 0.65683 0.97442 0.37298 0.25332  0.15704  0.07140  356 HOH   C O     
6399 O  O     . HOH   N .   ? 0.32585 0.21475 0.34772 0.03793  -0.02975 0.01137  357 HOH   C O     
6400 O  O     . HOH   N .   ? 0.37572 0.25715 0.50844 -0.08657 -0.08477 0.11185  358 HOH   C O     
6401 O  O     . HOH   N .   ? 0.58524 0.42421 0.64763 -0.12431 0.25563  -0.11396 359 HOH   C O     
6402 O  O     . HOH   N .   ? 0.79656 0.39783 0.62936 -0.01654 -0.14863 0.06433  360 HOH   C O     
6403 O  O     . HOH   N .   ? 0.61187 0.48576 0.45230 0.14402  0.08960  0.09468  361 HOH   C O     
6404 O  O     . HOH   N .   ? 0.73469 0.65225 0.40688 -0.08469 0.02361  0.02365  362 HOH   C O     
6405 O  O     . HOH   N .   ? 0.64979 0.43484 0.37907 -0.17350 -0.21096 0.12367  363 HOH   C O     
6406 O  O     . HOH   N .   ? 0.53427 0.73674 0.84994 0.07935  0.17125  0.38290  364 HOH   C O     
6407 O  O     . HOH   N .   ? 0.48610 0.59965 0.76600 -0.00018 0.02979  -0.22622 365 HOH   C O     
6408 O  O     . HOH   N .   ? 0.38026 0.82937 0.31884 0.21241  0.05390  0.06084  366 HOH   C O     
6409 O  O     . HOH   N .   ? 0.44295 0.74831 0.98065 0.02822  0.02274  0.24144  367 HOH   C O     
6410 O  O     . HOH   N .   ? 0.67722 0.62329 0.77499 0.00465  0.02978  -0.28589 368 HOH   C O     
6411 O  O     . HOH   N .   ? 0.96164 0.46730 0.62297 -0.28978 0.37478  -0.17196 369 HOH   C O     
6412 O  O     . HOH   N .   ? 0.48928 0.66028 0.86303 -0.04954 -0.01439 0.11215  370 HOH   C O     
6413 O  O     . HOH   N .   ? 0.42269 0.49332 0.30817 0.07980  -0.11805 -0.02064 371 HOH   C O     
6414 O  O     . HOH   N .   ? 0.78927 0.59331 0.55649 0.20625  0.15216  0.29942  372 HOH   C O     
6415 O  O     . HOH   N .   ? 1.18554 0.69974 0.44161 -0.10449 0.02274  -0.06502 373 HOH   C O     
6416 O  O     . HOH   N .   ? 0.40251 0.30438 0.20039 0.06090  -0.08267 0.00682  374 HOH   C O     
6417 O  O     . HOH   N .   ? 0.28807 0.66049 0.36806 -0.10777 -0.11589 0.04865  375 HOH   C O     
6418 O  O     . HOH   N .   ? 0.51490 0.93874 0.35304 0.07723  0.08054  0.23478  376 HOH   C O     
6419 O  O     . HOH   N .   ? 0.40960 0.55568 0.85800 0.06117  0.09263  -0.33111 377 HOH   C O     
6420 O  O     . HOH   N .   ? 0.88346 0.44683 0.66074 -0.06345 0.01093  0.08370  378 HOH   C O     
6421 O  O     . HOH   N .   ? 0.59848 0.50953 0.58882 0.02404  -0.19445 0.06905  379 HOH   C O     
6422 O  O     . HOH   N .   ? 1.00047 0.35080 1.04094 0.07014  0.20311  -0.13658 380 HOH   C O     
6423 O  O     . HOH   N .   ? 0.53051 0.43049 0.86251 0.13876  -0.21266 -0.29076 381 HOH   C O     
6424 O  O     . HOH   N .   ? 0.92161 0.46616 0.55015 -0.28774 -0.20805 0.18228  382 HOH   C O     
6425 O  O     . HOH   N .   ? 0.67632 0.68403 0.53585 0.24126  0.09582  -0.01444 383 HOH   C O     
6426 O  O     . HOH   N .   ? 0.46150 0.56558 0.76939 -0.07047 -0.02402 -0.05351 384 HOH   C O     
6427 O  O     . HOH   N .   ? 0.60378 0.37108 0.40003 0.12340  -0.16973 -0.14425 385 HOH   C O     
6428 O  O     . HOH   N .   ? 0.50033 0.33327 0.50710 -0.04529 -0.27209 0.09788  386 HOH   C O     
6429 O  O     . HOH   N .   ? 0.77002 0.90767 0.44707 0.10455  0.16101  -0.08126 387 HOH   C O     
6430 O  O     . HOH   N .   ? 0.45897 0.44158 0.34104 -0.06278 0.01935  0.08113  388 HOH   C O     
6431 O  O     . HOH   N .   ? 0.89319 0.36218 0.35933 0.02591  -0.10731 0.03690  389 HOH   C O     
6432 O  O     . HOH   N .   ? 0.73424 0.53253 0.81420 -0.18872 -0.03553 0.32964  390 HOH   C O     
6433 O  O     . HOH   N .   ? 0.95456 0.51053 0.43412 0.10883  -0.01419 -0.04424 391 HOH   C O     
6434 O  O     . HOH   N .   ? 0.27488 0.30093 0.40842 0.03067  -0.04087 0.01381  392 HOH   C O     
6435 O  O     . HOH   N .   ? 0.96243 0.41399 0.64142 -0.04013 -0.15730 0.02681  393 HOH   C O     
6436 O  O     . HOH   N .   ? 0.56784 0.62588 0.60871 0.31490  0.15586  0.23978  394 HOH   C O     
6437 O  O     . HOH   N .   ? 1.05633 0.65695 0.38565 0.15488  0.20585  -0.07976 395 HOH   C O     
6438 O  O     . HOH   N .   ? 0.32605 0.81857 0.68663 -0.08425 0.20484  0.07799  396 HOH   C O     
6439 O  O     . HOH   N .   ? 1.17530 0.52840 0.56760 -0.09512 0.17377  -0.10462 397 HOH   C O     
6440 O  O     . HOH   N .   ? 0.96088 0.26771 0.63457 0.03196  -0.07951 0.08679  398 HOH   C O     
6441 O  O     . HOH   N .   ? 0.58350 0.32503 0.41455 0.15509  0.20294  0.09338  399 HOH   C O     
6442 O  O     . HOH   N .   ? 0.49076 0.80304 0.60558 0.16861  -0.07603 0.10316  400 HOH   C O     
6443 O  O     . HOH   N .   ? 0.40431 0.82377 0.40750 0.03736  0.12457  -0.09457 401 HOH   C O     
6444 O  O     . HOH   N .   ? 0.42702 0.76047 0.89178 0.27188  0.15195  -0.00797 402 HOH   C O     
6445 O  O     . HOH   N .   ? 0.53438 0.49087 0.54738 -0.04466 -0.17172 0.03403  403 HOH   C O     
6446 O  O     . HOH   N .   ? 0.40241 0.37156 0.65846 -0.04282 0.18460  0.01633  404 HOH   C O     
6447 O  O     . HOH   N .   ? 0.54401 0.32437 0.57091 -0.18752 -0.05054 0.09663  405 HOH   C O     
6448 O  O     . HOH   N .   ? 0.70236 0.55078 0.28685 -0.03425 -0.13517 0.02341  406 HOH   C O     
6449 O  O     . HOH   N .   ? 0.81867 0.51012 0.54680 -0.26944 -0.07586 -0.01244 407 HOH   C O     
6450 O  O     . HOH   N .   ? 0.82726 0.29804 0.40606 -0.08711 -0.11452 -0.04044 408 HOH   C O     
6451 O  O     . HOH   N .   ? 0.88294 0.55934 0.25837 0.19314  -0.07160 -0.01907 409 HOH   C O     
6452 O  O     . HOH   N .   ? 0.91840 0.95874 0.25481 -0.01697 -0.09021 -0.03119 410 HOH   C O     
6453 O  O     . HOH   N .   ? 0.80810 0.60246 0.76293 -0.07660 0.03715  0.39095  411 HOH   C O     
6454 O  O     . HOH   N .   ? 0.40288 1.27432 0.67465 -0.02808 0.09786  -0.25135 412 HOH   C O     
6455 O  O     . HOH   N .   ? 0.44068 0.65895 1.02645 0.10037  0.18353  0.45485  413 HOH   C O     
6456 O  O     . HOH   N .   ? 0.35594 0.45508 1.27702 0.01859  0.15471  -0.03846 414 HOH   C O     
6457 O  O     . HOH   N .   ? 0.58115 0.81860 0.76564 -0.30659 -0.30250 0.41650  415 HOH   C O     
6458 O  O     . HOH   N .   ? 0.39738 0.66634 0.41761 -0.00872 0.06103  -0.11186 416 HOH   C O     
6459 O  O     . HOH   N .   ? 0.55428 0.91435 0.52107 0.02133  0.23577  0.19654  417 HOH   C O     
6460 O  O     . HOH   N .   ? 0.81281 0.75986 0.44935 -0.21453 -0.28762 0.15780  418 HOH   C O     
6461 O  O     A HOH   N .   ? 0.38308 0.60337 0.59459 0.18107  0.09058  0.24639  419 HOH   C O     
6462 O  O     B HOH   N .   ? 0.30831 0.64694 0.56780 0.08483  -0.09376 0.11258  419 HOH   C O     
6463 O  O     . HOH   N .   ? 0.31168 0.70708 0.37196 -0.16785 -0.05698 0.16105  420 HOH   C O     
# 
