data_9BFZ
# 
_entry.id   9BFZ 
# 
_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   9BFZ         pdb_00009bfz 10.2210/pdb9bfz/pdb 
WWPDB D_1000283278 ?            ?                   
# 
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 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BFZ 
_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 
'Saldajeno-Concar, M.' 2 ?                   
'Knox, J.E.'           3 ?                   
'Yano, J.K.'           4 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' 19382.811 2    3.6.5.2 ? ? ? 
2 polymer     man 'Peptidyl-prolyl cis-trans isomerase A' 18107.516 2    5.2.1.8 ? ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   2    ?       ? ? ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    2    ?       ? ? ? 
5 non-polymer syn 
;(3R)-N-[(2S)-1-{[(1M,8R,10S,14S,21M)-22-ethyl-4-hydroxy-21-[2-(2-methoxyethyl)phenyl]-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-methyl-1-propanoylpyrrolidine-3-carboxamide (non-preferred name)
;
905.132   2    ?       ? ? ? 
6 water       nat water 18.015    1032 ?       ? ? ? 
# 
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 
;SMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETSLLDILDTAGQEEYSAMRDQYMRTGEGFL
LVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
;SMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETSLLDILDTAGQEEYSAMRDQYMRTGEGFL
LVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQGVDDAFYTL
VREIRKHKEK
;
B,A ? 
2 'polypeptide(L)' no no 
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
C,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
4 'MAGNESIUM ION' MG    
5 
;(3R)-N-[(2S)-1-{[(1M,8R,10S,14S,21M)-22-ethyl-4-hydroxy-21-[2-(2-methoxyethyl)phenyl]-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-methyl-1-propanoylpyrrolidine-3-carboxamide (non-preferred name)
;
A1AOK 
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  SER 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  LEU 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 SER 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  SER 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 
A1AOK non-polymer         . 
;(3R)-N-[(2S)-1-{[(1M,8R,10S,14S,21M)-22-ethyl-4-hydroxy-21-[2-(2-methoxyethyl)phenyl]-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-methyl-1-propanoylpyrrolidine-3-carboxamide (non-preferred name)
;
? 'C52 H68 N6 O8'     905.132 
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 B . n 
A 1 2   MET 2   1   1   MET MET B . n 
A 1 3   THR 3   2   2   THR THR B . n 
A 1 4   GLU 4   3   3   GLU GLU B . n 
A 1 5   TYR 5   4   4   TYR TYR B . n 
A 1 6   LYS 6   5   5   LYS LYS B . n 
A 1 7   LEU 7   6   6   LEU LEU B . n 
A 1 8   VAL 8   7   7   VAL VAL B . n 
A 1 9   VAL 9   8   8   VAL VAL B . n 
A 1 10  VAL 10  9   9   VAL VAL B . n 
A 1 11  GLY 11  10  10  GLY GLY B . n 
A 1 12  ALA 12  11  11  ALA ALA B . n 
A 1 13  CYS 13  12  12  CYS CYS B . n 
A 1 14  GLY 14  13  13  GLY GLY B . n 
A 1 15  VAL 15  14  14  VAL VAL B . n 
A 1 16  GLY 16  15  15  GLY GLY B . n 
A 1 17  LYS 17  16  16  LYS LYS B . n 
A 1 18  SER 18  17  17  SER SER B . n 
A 1 19  ALA 19  18  18  ALA ALA B . n 
A 1 20  LEU 20  19  19  LEU LEU B . n 
A 1 21  THR 21  20  20  THR THR B . n 
A 1 22  ILE 22  21  21  ILE ILE B . n 
A 1 23  GLN 23  22  22  GLN GLN B . n 
A 1 24  LEU 24  23  23  LEU LEU B . n 
A 1 25  ILE 25  24  24  ILE ILE B . n 
A 1 26  GLN 26  25  25  GLN GLN B . n 
A 1 27  ASN 27  26  26  ASN ASN B . n 
A 1 28  HIS 28  27  27  HIS HIS B . n 
A 1 29  PHE 29  28  28  PHE PHE B . n 
A 1 30  VAL 30  29  29  VAL VAL B . n 
A 1 31  ASP 31  30  30  ASP ASP B . n 
A 1 32  GLU 32  31  31  GLU GLU B . n 
A 1 33  TYR 33  32  32  TYR TYR B . n 
A 1 34  ASP 34  33  33  ASP ASP B . n 
A 1 35  PRO 35  34  34  PRO PRO B . n 
A 1 36  THR 36  35  35  THR THR B . n 
A 1 37  ILE 37  36  36  ILE ILE B . n 
A 1 38  GLU 38  37  37  GLU GLU B . n 
A 1 39  ASP 39  38  38  ASP ASP B . n 
A 1 40  SER 40  39  39  SER SER B . n 
A 1 41  TYR 41  40  40  TYR TYR B . n 
A 1 42  ARG 42  41  41  ARG ARG B . n 
A 1 43  LYS 43  42  42  LYS LYS B . n 
A 1 44  GLN 44  43  43  GLN GLN B . n 
A 1 45  VAL 45  44  44  VAL VAL B . n 
A 1 46  VAL 46  45  45  VAL VAL B . n 
A 1 47  ILE 47  46  46  ILE ILE B . n 
A 1 48  ASP 48  47  47  ASP ASP B . n 
A 1 49  GLY 49  48  48  GLY GLY B . n 
A 1 50  GLU 50  49  49  GLU GLU B . n 
A 1 51  THR 51  50  50  THR THR B . n 
A 1 52  SER 52  51  51  SER SER B . n 
A 1 53  LEU 53  52  52  LEU LEU B . n 
A 1 54  LEU 54  53  53  LEU LEU B . n 
A 1 55  ASP 55  54  54  ASP ASP B . n 
A 1 56  ILE 56  55  55  ILE ILE B . n 
A 1 57  LEU 57  56  56  LEU LEU B . n 
A 1 58  ASP 58  57  57  ASP ASP B . n 
A 1 59  THR 59  58  58  THR THR B . n 
A 1 60  ALA 60  59  59  ALA ALA B . n 
A 1 61  GLY 61  60  60  GLY GLY B . n 
A 1 62  GLN 62  61  61  GLN GLN B . n 
A 1 63  GLU 63  62  62  GLU GLU B . n 
A 1 64  GLU 64  63  63  GLU GLU B . n 
A 1 65  TYR 65  64  64  TYR TYR B . n 
A 1 66  SER 66  65  65  SER SER B . n 
A 1 67  ALA 67  66  66  ALA ALA B . n 
A 1 68  MET 68  67  67  MET MET B . n 
A 1 69  ARG 69  68  68  ARG ARG B . n 
A 1 70  ASP 70  69  69  ASP ASP B . n 
A 1 71  GLN 71  70  70  GLN GLN B . n 
A 1 72  TYR 72  71  71  TYR TYR B . n 
A 1 73  MET 73  72  72  MET MET B . n 
A 1 74  ARG 74  73  73  ARG ARG B . n 
A 1 75  THR 75  74  74  THR THR B . n 
A 1 76  GLY 76  75  75  GLY GLY B . n 
A 1 77  GLU 77  76  76  GLU GLU B . n 
A 1 78  GLY 78  77  77  GLY GLY B . n 
A 1 79  PHE 79  78  78  PHE PHE B . n 
A 1 80  LEU 80  79  79  LEU LEU B . n 
A 1 81  LEU 81  80  80  LEU LEU B . n 
A 1 82  VAL 82  81  81  VAL VAL B . n 
A 1 83  PHE 83  82  82  PHE PHE B . n 
A 1 84  ALA 84  83  83  ALA ALA B . n 
A 1 85  ILE 85  84  84  ILE ILE B . n 
A 1 86  ASN 86  85  85  ASN ASN B . n 
A 1 87  ASN 87  86  86  ASN ASN B . n 
A 1 88  THR 88  87  87  THR THR B . n 
A 1 89  LYS 89  88  88  LYS LYS B . n 
A 1 90  SER 90  89  89  SER SER B . n 
A 1 91  PHE 91  90  90  PHE PHE B . n 
A 1 92  GLU 92  91  91  GLU GLU B . n 
A 1 93  ASP 93  92  92  ASP ASP B . n 
A 1 94  ILE 94  93  93  ILE ILE B . n 
A 1 95  HIS 95  94  94  HIS HIS B . n 
A 1 96  HIS 96  95  95  HIS HIS B . n 
A 1 97  TYR 97  96  96  TYR TYR B . n 
A 1 98  ARG 98  97  97  ARG ARG B . n 
A 1 99  GLU 99  98  98  GLU GLU B . n 
A 1 100 GLN 100 99  99  GLN GLN B . n 
A 1 101 ILE 101 100 100 ILE ILE B . n 
A 1 102 LYS 102 101 101 LYS LYS B . n 
A 1 103 ARG 103 102 102 ARG ARG B . n 
A 1 104 VAL 104 103 103 VAL VAL B . n 
A 1 105 LYS 105 104 104 LYS LYS B . n 
A 1 106 ASP 106 105 105 ASP ASP B . n 
A 1 107 SER 107 106 106 SER SER B . n 
A 1 108 GLU 108 107 107 GLU GLU B . n 
A 1 109 ASP 109 108 108 ASP ASP B . n 
A 1 110 VAL 110 109 109 VAL VAL B . n 
A 1 111 PRO 111 110 110 PRO PRO B . n 
A 1 112 MET 112 111 111 MET MET B . n 
A 1 113 VAL 113 112 112 VAL VAL B . n 
A 1 114 LEU 114 113 113 LEU LEU B . n 
A 1 115 VAL 115 114 114 VAL VAL B . n 
A 1 116 GLY 116 115 115 GLY GLY B . n 
A 1 117 ASN 117 116 116 ASN ASN B . n 
A 1 118 LYS 118 117 117 LYS LYS B . n 
A 1 119 SER 119 118 118 SER SER B . n 
A 1 120 ASP 120 119 119 ASP ASP B . n 
A 1 121 LEU 121 120 120 LEU LEU B . n 
A 1 122 PRO 122 121 121 PRO PRO B . n 
A 1 123 SER 123 122 122 SER SER B . n 
A 1 124 ARG 124 123 123 ARG ARG B . n 
A 1 125 THR 125 124 124 THR THR B . n 
A 1 126 VAL 126 125 125 VAL VAL B . n 
A 1 127 ASP 127 126 126 ASP ASP B . n 
A 1 128 THR 128 127 127 THR THR B . n 
A 1 129 LYS 129 128 128 LYS LYS B . n 
A 1 130 GLN 130 129 129 GLN GLN B . n 
A 1 131 ALA 131 130 130 ALA ALA B . n 
A 1 132 GLN 132 131 131 GLN GLN B . n 
A 1 133 ASP 133 132 132 ASP ASP B . n 
A 1 134 LEU 134 133 133 LEU LEU B . n 
A 1 135 ALA 135 134 134 ALA ALA B . n 
A 1 136 ARG 136 135 135 ARG ARG B . n 
A 1 137 SER 137 136 136 SER SER B . n 
A 1 138 TYR 138 137 137 TYR TYR B . n 
A 1 139 GLY 139 138 138 GLY GLY B . n 
A 1 140 ILE 140 139 139 ILE ILE B . n 
A 1 141 PRO 141 140 140 PRO PRO B . n 
A 1 142 PHE 142 141 141 PHE PHE B . n 
A 1 143 ILE 143 142 142 ILE ILE B . n 
A 1 144 GLU 144 143 143 GLU GLU B . n 
A 1 145 THR 145 144 144 THR THR B . n 
A 1 146 SER 146 145 145 SER SER B . n 
A 1 147 ALA 147 146 146 ALA ALA B . n 
A 1 148 LYS 148 147 147 LYS LYS B . n 
A 1 149 THR 149 148 148 THR THR B . n 
A 1 150 ARG 150 149 149 ARG ARG B . n 
A 1 151 GLN 151 150 150 GLN GLN B . n 
A 1 152 GLY 152 151 151 GLY GLY B . n 
A 1 153 VAL 153 152 152 VAL VAL B . n 
A 1 154 ASP 154 153 153 ASP ASP B . n 
A 1 155 ASP 155 154 154 ASP ASP B . n 
A 1 156 ALA 156 155 155 ALA ALA B . n 
A 1 157 PHE 157 156 156 PHE PHE B . n 
A 1 158 TYR 158 157 157 TYR TYR B . n 
A 1 159 THR 159 158 158 THR THR B . n 
A 1 160 LEU 160 159 159 LEU LEU B . n 
A 1 161 VAL 161 160 160 VAL VAL B . n 
A 1 162 ARG 162 161 161 ARG ARG B . n 
A 1 163 GLU 163 162 162 GLU GLU B . n 
A 1 164 ILE 164 163 163 ILE ILE B . n 
A 1 165 ARG 165 164 164 ARG ARG B . n 
A 1 166 LYS 166 165 165 LYS LYS B . n 
A 1 167 HIS 167 166 166 HIS HIS B . n 
A 1 168 LYS 168 167 167 LYS LYS B . n 
A 1 169 GLU 169 168 168 GLU GLU B . n 
A 1 170 LYS 170 169 169 LYS LYS B . n 
B 1 1   SER 1   0   0   SER SER A . n 
B 1 2   MET 2   1   1   MET MET A . n 
B 1 3   THR 3   2   2   THR THR A . n 
B 1 4   GLU 4   3   3   GLU GLU A . n 
B 1 5   TYR 5   4   4   TYR TYR A . n 
B 1 6   LYS 6   5   5   LYS LYS A . n 
B 1 7   LEU 7   6   6   LEU LEU A . n 
B 1 8   VAL 8   7   7   VAL VAL A . n 
B 1 9   VAL 9   8   8   VAL VAL A . n 
B 1 10  VAL 10  9   9   VAL VAL A . n 
B 1 11  GLY 11  10  10  GLY GLY A . n 
B 1 12  ALA 12  11  11  ALA ALA A . n 
B 1 13  CYS 13  12  12  CYS CYS A . n 
B 1 14  GLY 14  13  13  GLY GLY A . n 
B 1 15  VAL 15  14  14  VAL VAL A . n 
B 1 16  GLY 16  15  15  GLY GLY A . n 
B 1 17  LYS 17  16  16  LYS LYS A . n 
B 1 18  SER 18  17  17  SER SER A . n 
B 1 19  ALA 19  18  18  ALA ALA A . n 
B 1 20  LEU 20  19  19  LEU LEU A . n 
B 1 21  THR 21  20  20  THR THR A . n 
B 1 22  ILE 22  21  21  ILE ILE A . n 
B 1 23  GLN 23  22  22  GLN GLN A . n 
B 1 24  LEU 24  23  23  LEU LEU A . n 
B 1 25  ILE 25  24  24  ILE ILE A . n 
B 1 26  GLN 26  25  25  GLN GLN A . n 
B 1 27  ASN 27  26  26  ASN ASN A . n 
B 1 28  HIS 28  27  27  HIS HIS A . n 
B 1 29  PHE 29  28  28  PHE PHE A . n 
B 1 30  VAL 30  29  29  VAL VAL A . n 
B 1 31  ASP 31  30  30  ASP ASP A . n 
B 1 32  GLU 32  31  31  GLU GLU A . n 
B 1 33  TYR 33  32  32  TYR TYR A . n 
B 1 34  ASP 34  33  33  ASP ASP A . n 
B 1 35  PRO 35  34  34  PRO PRO A . n 
B 1 36  THR 36  35  35  THR THR A . n 
B 1 37  ILE 37  36  36  ILE ILE A . n 
B 1 38  GLU 38  37  37  GLU GLU A . n 
B 1 39  ASP 39  38  38  ASP ASP A . n 
B 1 40  SER 40  39  39  SER SER A . n 
B 1 41  TYR 41  40  40  TYR TYR A . n 
B 1 42  ARG 42  41  41  ARG ARG A . n 
B 1 43  LYS 43  42  42  LYS LYS A . n 
B 1 44  GLN 44  43  43  GLN GLN A . n 
B 1 45  VAL 45  44  44  VAL VAL A . n 
B 1 46  VAL 46  45  45  VAL VAL A . n 
B 1 47  ILE 47  46  46  ILE ILE A . n 
B 1 48  ASP 48  47  47  ASP ASP A . n 
B 1 49  GLY 49  48  48  GLY GLY A . n 
B 1 50  GLU 50  49  49  GLU GLU A . n 
B 1 51  THR 51  50  50  THR THR A . n 
B 1 52  SER 52  51  51  SER SER A . n 
B 1 53  LEU 53  52  52  LEU LEU A . n 
B 1 54  LEU 54  53  53  LEU LEU A . n 
B 1 55  ASP 55  54  54  ASP ASP A . n 
B 1 56  ILE 56  55  55  ILE ILE A . n 
B 1 57  LEU 57  56  56  LEU LEU A . n 
B 1 58  ASP 58  57  57  ASP ASP A . n 
B 1 59  THR 59  58  58  THR THR A . n 
B 1 60  ALA 60  59  59  ALA ALA A . n 
B 1 61  GLY 61  60  60  GLY GLY A . n 
B 1 62  GLN 62  61  61  GLN GLN A . n 
B 1 63  GLU 63  62  62  GLU GLU A . n 
B 1 64  GLU 64  63  63  GLU GLU A . n 
B 1 65  TYR 65  64  64  TYR TYR A . n 
B 1 66  SER 66  65  65  SER SER A . n 
B 1 67  ALA 67  66  66  ALA ALA A . n 
B 1 68  MET 68  67  67  MET MET A . n 
B 1 69  ARG 69  68  68  ARG ARG A . n 
B 1 70  ASP 70  69  69  ASP ASP A . n 
B 1 71  GLN 71  70  70  GLN GLN A . n 
B 1 72  TYR 72  71  71  TYR TYR A . n 
B 1 73  MET 73  72  72  MET MET A . n 
B 1 74  ARG 74  73  73  ARG ARG A . n 
B 1 75  THR 75  74  74  THR THR A . n 
B 1 76  GLY 76  75  75  GLY GLY A . n 
B 1 77  GLU 77  76  76  GLU GLU A . n 
B 1 78  GLY 78  77  77  GLY GLY A . n 
B 1 79  PHE 79  78  78  PHE PHE A . n 
B 1 80  LEU 80  79  79  LEU LEU A . n 
B 1 81  LEU 81  80  80  LEU LEU A . n 
B 1 82  VAL 82  81  81  VAL VAL A . n 
B 1 83  PHE 83  82  82  PHE PHE A . n 
B 1 84  ALA 84  83  83  ALA ALA A . n 
B 1 85  ILE 85  84  84  ILE ILE A . n 
B 1 86  ASN 86  85  85  ASN ASN A . n 
B 1 87  ASN 87  86  86  ASN ASN A . n 
B 1 88  THR 88  87  87  THR THR A . n 
B 1 89  LYS 89  88  88  LYS LYS A . n 
B 1 90  SER 90  89  89  SER SER A . n 
B 1 91  PHE 91  90  90  PHE PHE A . n 
B 1 92  GLU 92  91  91  GLU GLU A . n 
B 1 93  ASP 93  92  92  ASP ASP A . n 
B 1 94  ILE 94  93  93  ILE ILE A . n 
B 1 95  HIS 95  94  94  HIS HIS A . n 
B 1 96  HIS 96  95  95  HIS HIS A . n 
B 1 97  TYR 97  96  96  TYR TYR A . n 
B 1 98  ARG 98  97  97  ARG ARG A . n 
B 1 99  GLU 99  98  98  GLU GLU A . n 
B 1 100 GLN 100 99  99  GLN GLN A . n 
B 1 101 ILE 101 100 100 ILE ILE A . n 
B 1 102 LYS 102 101 101 LYS LYS A . n 
B 1 103 ARG 103 102 102 ARG ARG A . n 
B 1 104 VAL 104 103 103 VAL VAL A . n 
B 1 105 LYS 105 104 104 LYS LYS A . n 
B 1 106 ASP 106 105 105 ASP ASP A . n 
B 1 107 SER 107 106 106 SER SER A . n 
B 1 108 GLU 108 107 107 GLU GLU A . n 
B 1 109 ASP 109 108 108 ASP ASP A . n 
B 1 110 VAL 110 109 109 VAL VAL A . n 
B 1 111 PRO 111 110 110 PRO PRO A . n 
B 1 112 MET 112 111 111 MET MET A . n 
B 1 113 VAL 113 112 112 VAL VAL A . n 
B 1 114 LEU 114 113 113 LEU LEU A . n 
B 1 115 VAL 115 114 114 VAL VAL A . n 
B 1 116 GLY 116 115 115 GLY GLY A . n 
B 1 117 ASN 117 116 116 ASN ASN A . n 
B 1 118 LYS 118 117 117 LYS LYS A . n 
B 1 119 SER 119 118 118 SER SER A . n 
B 1 120 ASP 120 119 119 ASP ASP A . n 
B 1 121 LEU 121 120 120 LEU LEU A . n 
B 1 122 PRO 122 121 121 PRO PRO A . n 
B 1 123 SER 123 122 122 SER SER A . n 
B 1 124 ARG 124 123 123 ARG ARG A . n 
B 1 125 THR 125 124 124 THR THR A . n 
B 1 126 VAL 126 125 125 VAL VAL A . n 
B 1 127 ASP 127 126 126 ASP ASP A . n 
B 1 128 THR 128 127 127 THR THR A . n 
B 1 129 LYS 129 128 128 LYS LYS A . n 
B 1 130 GLN 130 129 129 GLN GLN A . n 
B 1 131 ALA 131 130 130 ALA ALA A . n 
B 1 132 GLN 132 131 131 GLN GLN A . n 
B 1 133 ASP 133 132 132 ASP ASP A . n 
B 1 134 LEU 134 133 133 LEU LEU A . n 
B 1 135 ALA 135 134 134 ALA ALA A . n 
B 1 136 ARG 136 135 135 ARG ARG A . n 
B 1 137 SER 137 136 136 SER SER A . n 
B 1 138 TYR 138 137 137 TYR TYR A . n 
B 1 139 GLY 139 138 138 GLY GLY A . n 
B 1 140 ILE 140 139 139 ILE ILE A . n 
B 1 141 PRO 141 140 140 PRO PRO A . n 
B 1 142 PHE 142 141 141 PHE PHE A . n 
B 1 143 ILE 143 142 142 ILE ILE A . n 
B 1 144 GLU 144 143 143 GLU GLU A . n 
B 1 145 THR 145 144 144 THR THR A . n 
B 1 146 SER 146 145 145 SER SER A . n 
B 1 147 ALA 147 146 146 ALA ALA A . n 
B 1 148 LYS 148 147 147 LYS LYS A . n 
B 1 149 THR 149 148 148 THR THR A . n 
B 1 150 ARG 150 149 149 ARG ARG A . n 
B 1 151 GLN 151 150 150 GLN GLN A . n 
B 1 152 GLY 152 151 151 GLY GLY A . n 
B 1 153 VAL 153 152 152 VAL VAL A . n 
B 1 154 ASP 154 153 153 ASP ASP A . n 
B 1 155 ASP 155 154 154 ASP ASP A . n 
B 1 156 ALA 156 155 155 ALA ALA A . n 
B 1 157 PHE 157 156 156 PHE PHE A . n 
B 1 158 TYR 158 157 157 TYR TYR A . n 
B 1 159 THR 159 158 158 THR THR A . n 
B 1 160 LEU 160 159 159 LEU LEU A . n 
B 1 161 VAL 161 160 160 VAL VAL A . n 
B 1 162 ARG 162 161 161 ARG ARG A . n 
B 1 163 GLU 163 162 162 GLU GLU A . n 
B 1 164 ILE 164 163 163 ILE ILE A . n 
B 1 165 ARG 165 164 164 ARG ARG A . n 
B 1 166 LYS 166 165 165 LYS LYS A . n 
B 1 167 HIS 167 166 166 HIS HIS A . n 
B 1 168 LYS 168 167 167 LYS LYS A . n 
B 1 169 GLU 169 168 168 GLU GLU A . n 
B 1 170 LYS 170 169 ?   ?   ?   A . n 
C 2 1   SER 1   0   ?   ?   ?   C . n 
C 2 2   MET 2   1   ?   ?   ?   C . n 
C 2 3   VAL 3   2   2   VAL VAL C . n 
C 2 4   ASN 4   3   3   ASN ASN C . n 
C 2 5   PRO 5   4   4   PRO PRO C . n 
C 2 6   THR 6   5   5   THR THR C . n 
C 2 7   VAL 7   6   6   VAL VAL C . n 
C 2 8   PHE 8   7   7   PHE PHE C . n 
C 2 9   PHE 9   8   8   PHE PHE C . n 
C 2 10  ASP 10  9   9   ASP ASP C . n 
C 2 11  ILE 11  10  10  ILE ILE C . n 
C 2 12  ALA 12  11  11  ALA ALA C . n 
C 2 13  VAL 13  12  12  VAL VAL C . n 
C 2 14  ASP 14  13  13  ASP ASP C . n 
C 2 15  GLY 15  14  14  GLY GLY C . n 
C 2 16  GLU 16  15  15  GLU GLU C . n 
C 2 17  PRO 17  16  16  PRO PRO C . n 
C 2 18  LEU 18  17  17  LEU LEU C . n 
C 2 19  GLY 19  18  18  GLY GLY C . n 
C 2 20  ARG 20  19  19  ARG ARG C . n 
C 2 21  VAL 21  20  20  VAL VAL C . n 
C 2 22  SER 22  21  21  SER SER C . n 
C 2 23  PHE 23  22  22  PHE PHE C . n 
C 2 24  GLU 24  23  23  GLU GLU C . n 
C 2 25  LEU 25  24  24  LEU LEU C . n 
C 2 26  PHE 26  25  25  PHE PHE C . n 
C 2 27  ALA 27  26  26  ALA ALA C . n 
C 2 28  ASP 28  27  27  ASP ASP C . n 
C 2 29  LYS 29  28  28  LYS LYS C . n 
C 2 30  VAL 30  29  29  VAL VAL C . n 
C 2 31  PRO 31  30  30  PRO PRO C . n 
C 2 32  LYS 32  31  31  LYS LYS C . n 
C 2 33  THR 33  32  32  THR THR C . n 
C 2 34  ALA 34  33  33  ALA ALA C . n 
C 2 35  GLU 35  34  34  GLU GLU C . n 
C 2 36  ASN 36  35  35  ASN ASN C . n 
C 2 37  PHE 37  36  36  PHE PHE C . n 
C 2 38  ARG 38  37  37  ARG ARG C . n 
C 2 39  ALA 39  38  38  ALA ALA C . n 
C 2 40  LEU 40  39  39  LEU LEU C . n 
C 2 41  SER 41  40  40  SER SER C . n 
C 2 42  THR 42  41  41  THR THR C . n 
C 2 43  GLY 43  42  42  GLY GLY C . n 
C 2 44  GLU 44  43  43  GLU GLU C . n 
C 2 45  LYS 45  44  44  LYS LYS C . n 
C 2 46  GLY 46  45  45  GLY GLY C . n 
C 2 47  PHE 47  46  46  PHE PHE C . n 
C 2 48  GLY 48  47  47  GLY GLY C . n 
C 2 49  TYR 49  48  48  TYR TYR C . n 
C 2 50  LYS 50  49  49  LYS LYS C . n 
C 2 51  GLY 51  50  50  GLY GLY C . n 
C 2 52  SER 52  51  51  SER SER C . n 
C 2 53  SER 53  52  52  SER SER C . n 
C 2 54  PHE 54  53  53  PHE PHE C . n 
C 2 55  HIS 55  54  54  HIS HIS C . n 
C 2 56  ARG 56  55  55  ARG ARG C . n 
C 2 57  ILE 57  56  56  ILE ILE C . n 
C 2 58  ILE 58  57  57  ILE ILE C . n 
C 2 59  PRO 59  58  58  PRO PRO C . n 
C 2 60  GLY 60  59  59  GLY GLY C . n 
C 2 61  PHE 61  60  60  PHE PHE C . n 
C 2 62  MET 62  61  61  MET MET C . n 
C 2 63  CYS 63  62  62  CYS CYS C . n 
C 2 64  GLN 64  63  63  GLN GLN C . n 
C 2 65  GLY 65  64  64  GLY GLY C . n 
C 2 66  GLY 66  65  65  GLY GLY C . n 
C 2 67  ASP 67  66  66  ASP ASP C . n 
C 2 68  PHE 68  67  67  PHE PHE C . n 
C 2 69  THR 69  68  68  THR THR C . n 
C 2 70  ARG 70  69  69  ARG ARG C . n 
C 2 71  HIS 71  70  70  HIS HIS C . n 
C 2 72  ASN 72  71  71  ASN ASN C . n 
C 2 73  GLY 73  72  72  GLY GLY C . n 
C 2 74  THR 74  73  73  THR THR C . n 
C 2 75  GLY 75  74  74  GLY GLY C . n 
C 2 76  GLY 76  75  75  GLY GLY C . n 
C 2 77  LYS 77  76  76  LYS LYS C . n 
C 2 78  SER 78  77  77  SER SER C . n 
C 2 79  ILE 79  78  78  ILE ILE C . n 
C 2 80  TYR 80  79  79  TYR TYR C . n 
C 2 81  GLY 81  80  80  GLY GLY C . n 
C 2 82  GLU 82  81  81  GLU GLU C . n 
C 2 83  LYS 83  82  82  LYS LYS C . n 
C 2 84  PHE 84  83  83  PHE PHE C . n 
C 2 85  GLU 85  84  84  GLU GLU C . n 
C 2 86  ASP 86  85  85  ASP ASP C . n 
C 2 87  GLU 87  86  86  GLU GLU C . n 
C 2 88  ASN 88  87  87  ASN ASN C . n 
C 2 89  PHE 89  88  88  PHE PHE C . n 
C 2 90  ILE 90  89  89  ILE ILE C . n 
C 2 91  LEU 91  90  90  LEU LEU C . n 
C 2 92  LYS 92  91  91  LYS LYS C . n 
C 2 93  HIS 93  92  92  HIS HIS C . n 
C 2 94  THR 94  93  93  THR THR C . n 
C 2 95  GLY 95  94  94  GLY GLY C . n 
C 2 96  PRO 96  95  95  PRO PRO C . n 
C 2 97  GLY 97  96  96  GLY GLY C . n 
C 2 98  ILE 98  97  97  ILE ILE C . n 
C 2 99  LEU 99  98  98  LEU LEU C . n 
C 2 100 SER 100 99  99  SER SER C . n 
C 2 101 MET 101 100 100 MET MET C . n 
C 2 102 ALA 102 101 101 ALA ALA C . n 
C 2 103 ASN 103 102 102 ASN ASN C . n 
C 2 104 ALA 104 103 103 ALA ALA C . n 
C 2 105 GLY 105 104 104 GLY GLY C . n 
C 2 106 PRO 106 105 105 PRO PRO C . n 
C 2 107 ASN 107 106 106 ASN ASN C . n 
C 2 108 THR 108 107 107 THR THR C . n 
C 2 109 ASN 109 108 108 ASN ASN C . n 
C 2 110 GLY 110 109 109 GLY GLY C . n 
C 2 111 SER 111 110 110 SER SER C . n 
C 2 112 GLN 112 111 111 GLN GLN C . n 
C 2 113 PHE 113 112 112 PHE PHE C . n 
C 2 114 PHE 114 113 113 PHE PHE C . n 
C 2 115 ILE 115 114 114 ILE ILE C . n 
C 2 116 CYS 116 115 115 CYS CYS C . n 
C 2 117 THR 117 116 116 THR THR C . n 
C 2 118 ALA 118 117 117 ALA ALA C . n 
C 2 119 LYS 119 118 118 LYS LYS C . n 
C 2 120 THR 120 119 119 THR THR C . n 
C 2 121 GLU 121 120 120 GLU GLU C . n 
C 2 122 TRP 122 121 121 TRP TRP C . n 
C 2 123 LEU 123 122 122 LEU LEU C . n 
C 2 124 ASP 124 123 123 ASP ASP C . n 
C 2 125 GLY 125 124 124 GLY GLY C . n 
C 2 126 LYS 126 125 125 LYS LYS C . n 
C 2 127 HIS 127 126 126 HIS HIS C . n 
C 2 128 VAL 128 127 127 VAL VAL C . n 
C 2 129 VAL 129 128 128 VAL VAL C . n 
C 2 130 PHE 130 129 129 PHE PHE C . n 
C 2 131 GLY 131 130 130 GLY GLY C . n 
C 2 132 LYS 132 131 131 LYS LYS C . n 
C 2 133 VAL 133 132 132 VAL VAL C . n 
C 2 134 LYS 134 133 133 LYS LYS C . n 
C 2 135 GLU 135 134 134 GLU GLU C . n 
C 2 136 GLY 136 135 135 GLY GLY C . n 
C 2 137 MET 137 136 136 MET MET C . n 
C 2 138 ASN 138 137 137 ASN ASN C . n 
C 2 139 ILE 139 138 138 ILE ILE C . n 
C 2 140 VAL 140 139 139 VAL VAL C . n 
C 2 141 GLU 141 140 140 GLU GLU C . n 
C 2 142 ALA 142 141 141 ALA ALA C . n 
C 2 143 MET 143 142 142 MET MET C . n 
C 2 144 GLU 144 143 143 GLU GLU C . n 
C 2 145 ARG 145 144 144 ARG ARG C . n 
C 2 146 PHE 146 145 145 PHE PHE C . n 
C 2 147 GLY 147 146 146 GLY GLY C . n 
C 2 148 SER 148 147 147 SER SER C . n 
C 2 149 ARG 149 148 148 ARG ARG C . n 
C 2 150 ASN 150 149 149 ASN ASN C . n 
C 2 151 GLY 151 150 150 GLY GLY C . n 
C 2 152 LYS 152 151 151 LYS LYS C . n 
C 2 153 THR 153 152 152 THR THR C . n 
C 2 154 SER 154 153 153 SER SER C . n 
C 2 155 LYS 155 154 154 LYS LYS C . n 
C 2 156 LYS 156 155 155 LYS LYS C . n 
C 2 157 ILE 157 156 156 ILE ILE C . n 
C 2 158 THR 158 157 157 THR THR C . n 
C 2 159 ILE 159 158 158 ILE ILE C . n 
C 2 160 ALA 160 159 159 ALA ALA C . n 
C 2 161 ASP 161 160 160 ASP ASP C . n 
C 2 162 CYS 162 161 161 CYS CYS C . n 
C 2 163 GLY 163 162 162 GLY GLY C . n 
C 2 164 GLN 164 163 163 GLN GLN C . n 
C 2 165 LEU 165 164 164 LEU LEU C . n 
C 2 166 GLU 166 165 165 GLU GLU C . n 
D 2 1   SER 1   0   0   SER SER D . n 
D 2 2   MET 2   1   1   MET MET D . n 
D 2 3   VAL 3   2   2   VAL VAL D . n 
D 2 4   ASN 4   3   3   ASN ASN D . n 
D 2 5   PRO 5   4   4   PRO PRO D . n 
D 2 6   THR 6   5   5   THR THR D . n 
D 2 7   VAL 7   6   6   VAL VAL D . n 
D 2 8   PHE 8   7   7   PHE PHE D . n 
D 2 9   PHE 9   8   8   PHE PHE D . n 
D 2 10  ASP 10  9   9   ASP ASP D . n 
D 2 11  ILE 11  10  10  ILE ILE D . n 
D 2 12  ALA 12  11  11  ALA ALA D . n 
D 2 13  VAL 13  12  12  VAL VAL D . n 
D 2 14  ASP 14  13  13  ASP ASP D . n 
D 2 15  GLY 15  14  14  GLY GLY D . n 
D 2 16  GLU 16  15  15  GLU GLU D . n 
D 2 17  PRO 17  16  16  PRO PRO D . n 
D 2 18  LEU 18  17  17  LEU LEU D . n 
D 2 19  GLY 19  18  18  GLY GLY D . n 
D 2 20  ARG 20  19  19  ARG ARG D . n 
D 2 21  VAL 21  20  20  VAL VAL D . n 
D 2 22  SER 22  21  21  SER SER D . n 
D 2 23  PHE 23  22  22  PHE PHE D . n 
D 2 24  GLU 24  23  23  GLU GLU D . n 
D 2 25  LEU 25  24  24  LEU LEU D . n 
D 2 26  PHE 26  25  25  PHE PHE D . n 
D 2 27  ALA 27  26  26  ALA ALA D . n 
D 2 28  ASP 28  27  27  ASP ASP D . n 
D 2 29  LYS 29  28  28  LYS LYS D . n 
D 2 30  VAL 30  29  29  VAL VAL D . n 
D 2 31  PRO 31  30  30  PRO PRO D . n 
D 2 32  LYS 32  31  31  LYS LYS D . n 
D 2 33  THR 33  32  32  THR THR D . n 
D 2 34  ALA 34  33  33  ALA ALA D . n 
D 2 35  GLU 35  34  34  GLU GLU D . n 
D 2 36  ASN 36  35  35  ASN ASN D . n 
D 2 37  PHE 37  36  36  PHE PHE D . n 
D 2 38  ARG 38  37  37  ARG ARG D . n 
D 2 39  ALA 39  38  38  ALA ALA D . n 
D 2 40  LEU 40  39  39  LEU LEU D . n 
D 2 41  SER 41  40  40  SER SER D . n 
D 2 42  THR 42  41  41  THR THR D . n 
D 2 43  GLY 43  42  42  GLY GLY D . n 
D 2 44  GLU 44  43  43  GLU GLU D . n 
D 2 45  LYS 45  44  44  LYS LYS D . n 
D 2 46  GLY 46  45  45  GLY GLY D . n 
D 2 47  PHE 47  46  46  PHE PHE D . n 
D 2 48  GLY 48  47  47  GLY GLY D . n 
D 2 49  TYR 49  48  48  TYR TYR D . n 
D 2 50  LYS 50  49  49  LYS LYS D . n 
D 2 51  GLY 51  50  50  GLY GLY D . n 
D 2 52  SER 52  51  51  SER SER D . n 
D 2 53  SER 53  52  52  SER SER D . n 
D 2 54  PHE 54  53  53  PHE PHE D . n 
D 2 55  HIS 55  54  54  HIS HIS D . n 
D 2 56  ARG 56  55  55  ARG ARG D . n 
D 2 57  ILE 57  56  56  ILE ILE D . n 
D 2 58  ILE 58  57  57  ILE ILE D . n 
D 2 59  PRO 59  58  58  PRO PRO D . n 
D 2 60  GLY 60  59  59  GLY GLY D . n 
D 2 61  PHE 61  60  60  PHE PHE D . n 
D 2 62  MET 62  61  61  MET MET D . n 
D 2 63  CYS 63  62  62  CYS CYS D . n 
D 2 64  GLN 64  63  63  GLN GLN D . n 
D 2 65  GLY 65  64  64  GLY GLY D . n 
D 2 66  GLY 66  65  65  GLY GLY D . n 
D 2 67  ASP 67  66  66  ASP ASP D . n 
D 2 68  PHE 68  67  67  PHE PHE D . n 
D 2 69  THR 69  68  68  THR THR D . n 
D 2 70  ARG 70  69  69  ARG ARG D . n 
D 2 71  HIS 71  70  70  HIS HIS D . n 
D 2 72  ASN 72  71  71  ASN ASN D . n 
D 2 73  GLY 73  72  72  GLY GLY D . n 
D 2 74  THR 74  73  73  THR THR D . n 
D 2 75  GLY 75  74  74  GLY GLY D . n 
D 2 76  GLY 76  75  75  GLY GLY D . n 
D 2 77  LYS 77  76  76  LYS LYS D . n 
D 2 78  SER 78  77  77  SER SER D . n 
D 2 79  ILE 79  78  78  ILE ILE D . n 
D 2 80  TYR 80  79  79  TYR TYR D . n 
D 2 81  GLY 81  80  80  GLY GLY D . n 
D 2 82  GLU 82  81  81  GLU GLU D . n 
D 2 83  LYS 83  82  82  LYS LYS D . n 
D 2 84  PHE 84  83  83  PHE PHE D . n 
D 2 85  GLU 85  84  84  GLU GLU D . n 
D 2 86  ASP 86  85  85  ASP ASP D . n 
D 2 87  GLU 87  86  86  GLU GLU D . n 
D 2 88  ASN 88  87  87  ASN ASN D . n 
D 2 89  PHE 89  88  88  PHE PHE D . n 
D 2 90  ILE 90  89  89  ILE ILE D . n 
D 2 91  LEU 91  90  90  LEU LEU D . n 
D 2 92  LYS 92  91  91  LYS LYS D . n 
D 2 93  HIS 93  92  92  HIS HIS D . n 
D 2 94  THR 94  93  93  THR THR D . n 
D 2 95  GLY 95  94  94  GLY GLY D . n 
D 2 96  PRO 96  95  95  PRO PRO D . n 
D 2 97  GLY 97  96  96  GLY GLY D . n 
D 2 98  ILE 98  97  97  ILE ILE D . n 
D 2 99  LEU 99  98  98  LEU LEU D . n 
D 2 100 SER 100 99  99  SER SER D . n 
D 2 101 MET 101 100 100 MET MET D . n 
D 2 102 ALA 102 101 101 ALA ALA D . n 
D 2 103 ASN 103 102 102 ASN ASN D . n 
D 2 104 ALA 104 103 103 ALA ALA D . n 
D 2 105 GLY 105 104 104 GLY GLY D . n 
D 2 106 PRO 106 105 105 PRO PRO D . n 
D 2 107 ASN 107 106 106 ASN ASN D . n 
D 2 108 THR 108 107 107 THR THR D . n 
D 2 109 ASN 109 108 108 ASN ASN D . n 
D 2 110 GLY 110 109 109 GLY GLY D . n 
D 2 111 SER 111 110 110 SER SER D . n 
D 2 112 GLN 112 111 111 GLN GLN D . n 
D 2 113 PHE 113 112 112 PHE PHE D . n 
D 2 114 PHE 114 113 113 PHE PHE D . n 
D 2 115 ILE 115 114 114 ILE ILE D . n 
D 2 116 CYS 116 115 115 CYS CYS D . n 
D 2 117 THR 117 116 116 THR THR D . n 
D 2 118 ALA 118 117 117 ALA ALA D . n 
D 2 119 LYS 119 118 118 LYS LYS D . n 
D 2 120 THR 120 119 119 THR THR D . n 
D 2 121 GLU 121 120 120 GLU GLU D . n 
D 2 122 TRP 122 121 121 TRP TRP D . n 
D 2 123 LEU 123 122 122 LEU LEU D . n 
D 2 124 ASP 124 123 123 ASP ASP D . n 
D 2 125 GLY 125 124 124 GLY GLY D . n 
D 2 126 LYS 126 125 125 LYS LYS D . n 
D 2 127 HIS 127 126 126 HIS HIS D . n 
D 2 128 VAL 128 127 127 VAL VAL D . n 
D 2 129 VAL 129 128 128 VAL VAL D . n 
D 2 130 PHE 130 129 129 PHE PHE D . n 
D 2 131 GLY 131 130 130 GLY GLY D . n 
D 2 132 LYS 132 131 131 LYS LYS D . n 
D 2 133 VAL 133 132 132 VAL VAL D . n 
D 2 134 LYS 134 133 133 LYS LYS D . n 
D 2 135 GLU 135 134 134 GLU GLU D . n 
D 2 136 GLY 136 135 135 GLY GLY D . n 
D 2 137 MET 137 136 136 MET MET D . n 
D 2 138 ASN 138 137 137 ASN ASN D . n 
D 2 139 ILE 139 138 138 ILE ILE D . n 
D 2 140 VAL 140 139 139 VAL VAL D . n 
D 2 141 GLU 141 140 140 GLU GLU D . n 
D 2 142 ALA 142 141 141 ALA ALA D . n 
D 2 143 MET 143 142 142 MET MET D . n 
D 2 144 GLU 144 143 143 GLU GLU D . n 
D 2 145 ARG 145 144 144 ARG ARG D . n 
D 2 146 PHE 146 145 145 PHE PHE D . n 
D 2 147 GLY 147 146 146 GLY GLY D . n 
D 2 148 SER 148 147 147 SER SER D . n 
D 2 149 ARG 149 148 148 ARG ARG D . n 
D 2 150 ASN 150 149 149 ASN ASN D . n 
D 2 151 GLY 151 150 150 GLY GLY D . n 
D 2 152 LYS 152 151 151 LYS LYS D . n 
D 2 153 THR 153 152 152 THR THR D . n 
D 2 154 SER 154 153 153 SER SER D . n 
D 2 155 LYS 155 154 154 LYS LYS D . n 
D 2 156 LYS 156 155 155 LYS LYS D . n 
D 2 157 ILE 157 156 156 ILE ILE D . n 
D 2 158 THR 158 157 157 THR THR D . n 
D 2 159 ILE 159 158 158 ILE ILE D . n 
D 2 160 ALA 160 159 159 ALA ALA D . n 
D 2 161 ASP 161 160 160 ASP ASP D . n 
D 2 162 CYS 162 161 161 CYS CYS D . n 
D 2 163 GLY 163 162 162 GLY GLY D . n 
D 2 164 GLN 164 163 163 GLN GLN D . n 
D 2 165 LEU 165 164 164 LEU LEU D . n 
D 2 166 GLU 166 165 ?   ?   ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AOK 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AOK 
_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   201 170  GNP   GNP B . 
F 4 MG    1   202 171  MG    MG  B . 
G 5 A1AOK 1   203 9937 A1AOK RMC B . 
H 3 GNP   1   201 170  GNP   GNP A . 
I 4 MG    1   202 171  MG    MG  A . 
J 5 A1AOK 1   203 9937 A1AOK RMC A . 
K 6 HOH   1   301 709  HOH   HOH B . 
K 6 HOH   2   302 408  HOH   HOH B . 
K 6 HOH   3   303 594  HOH   HOH B . 
K 6 HOH   4   304 405  HOH   HOH B . 
K 6 HOH   5   305 284  HOH   HOH B . 
K 6 HOH   6   306 784  HOH   HOH B . 
K 6 HOH   7   307 163  HOH   HOH B . 
K 6 HOH   8   308 291  HOH   HOH B . 
K 6 HOH   9   309 47   HOH   HOH B . 
K 6 HOH   10  310 426  HOH   HOH B . 
K 6 HOH   11  311 421  HOH   HOH B . 
K 6 HOH   12  312 1030 HOH   HOH B . 
K 6 HOH   13  313 396  HOH   HOH B . 
K 6 HOH   14  314 651  HOH   HOH B . 
K 6 HOH   15  315 666  HOH   HOH B . 
K 6 HOH   16  316 424  HOH   HOH B . 
K 6 HOH   17  317 218  HOH   HOH B . 
K 6 HOH   18  318 897  HOH   HOH B . 
K 6 HOH   19  319 281  HOH   HOH B . 
K 6 HOH   20  320 513  HOH   HOH B . 
K 6 HOH   21  321 498  HOH   HOH B . 
K 6 HOH   22  322 611  HOH   HOH B . 
K 6 HOH   23  323 17   HOH   HOH B . 
K 6 HOH   24  324 174  HOH   HOH B . 
K 6 HOH   25  325 933  HOH   HOH B . 
K 6 HOH   26  326 250  HOH   HOH B . 
K 6 HOH   27  327 25   HOH   HOH B . 
K 6 HOH   28  328 1039 HOH   HOH B . 
K 6 HOH   29  329 189  HOH   HOH B . 
K 6 HOH   30  330 188  HOH   HOH B . 
K 6 HOH   31  331 33   HOH   HOH B . 
K 6 HOH   32  332 466  HOH   HOH B . 
K 6 HOH   33  333 679  HOH   HOH B . 
K 6 HOH   34  334 854  HOH   HOH B . 
K 6 HOH   35  335 179  HOH   HOH B . 
K 6 HOH   36  336 391  HOH   HOH B . 
K 6 HOH   37  337 244  HOH   HOH B . 
K 6 HOH   38  338 2    HOH   HOH B . 
K 6 HOH   39  339 387  HOH   HOH B . 
K 6 HOH   40  340 220  HOH   HOH B . 
K 6 HOH   41  341 206  HOH   HOH B . 
K 6 HOH   42  342 133  HOH   HOH B . 
K 6 HOH   43  343 83   HOH   HOH B . 
K 6 HOH   44  344 50   HOH   HOH B . 
K 6 HOH   45  345 788  HOH   HOH B . 
K 6 HOH   46  346 127  HOH   HOH B . 
K 6 HOH   47  347 736  HOH   HOH B . 
K 6 HOH   48  348 453  HOH   HOH B . 
K 6 HOH   49  349 346  HOH   HOH B . 
K 6 HOH   50  350 19   HOH   HOH B . 
K 6 HOH   51  351 27   HOH   HOH B . 
K 6 HOH   52  352 607  HOH   HOH B . 
K 6 HOH   53  353 758  HOH   HOH B . 
K 6 HOH   54  354 34   HOH   HOH B . 
K 6 HOH   55  355 54   HOH   HOH B . 
K 6 HOH   56  356 285  HOH   HOH B . 
K 6 HOH   57  357 848  HOH   HOH B . 
K 6 HOH   58  358 697  HOH   HOH B . 
K 6 HOH   59  359 630  HOH   HOH B . 
K 6 HOH   60  360 308  HOH   HOH B . 
K 6 HOH   61  361 318  HOH   HOH B . 
K 6 HOH   62  362 530  HOH   HOH B . 
K 6 HOH   63  363 572  HOH   HOH B . 
K 6 HOH   64  364 753  HOH   HOH B . 
K 6 HOH   65  365 144  HOH   HOH B . 
K 6 HOH   66  366 333  HOH   HOH B . 
K 6 HOH   67  367 311  HOH   HOH B . 
K 6 HOH   68  368 872  HOH   HOH B . 
K 6 HOH   69  369 984  HOH   HOH B . 
K 6 HOH   70  370 53   HOH   HOH B . 
K 6 HOH   71  371 400  HOH   HOH B . 
K 6 HOH   72  372 845  HOH   HOH B . 
K 6 HOH   73  373 260  HOH   HOH B . 
K 6 HOH   74  374 931  HOH   HOH B . 
K 6 HOH   75  375 420  HOH   HOH B . 
K 6 HOH   76  376 364  HOH   HOH B . 
K 6 HOH   77  377 267  HOH   HOH B . 
K 6 HOH   78  378 598  HOH   HOH B . 
K 6 HOH   79  379 79   HOH   HOH B . 
K 6 HOH   80  380 238  HOH   HOH B . 
K 6 HOH   81  381 322  HOH   HOH B . 
K 6 HOH   82  382 828  HOH   HOH B . 
K 6 HOH   83  383 946  HOH   HOH B . 
K 6 HOH   84  384 316  HOH   HOH B . 
K 6 HOH   85  385 621  HOH   HOH B . 
K 6 HOH   86  386 389  HOH   HOH B . 
K 6 HOH   87  387 160  HOH   HOH B . 
K 6 HOH   88  388 507  HOH   HOH B . 
K 6 HOH   89  389 286  HOH   HOH B . 
K 6 HOH   90  390 41   HOH   HOH B . 
K 6 HOH   91  391 142  HOH   HOH B . 
K 6 HOH   92  392 1008 HOH   HOH B . 
K 6 HOH   93  393 504  HOH   HOH B . 
K 6 HOH   94  394 52   HOH   HOH B . 
K 6 HOH   95  395 495  HOH   HOH B . 
K 6 HOH   96  396 293  HOH   HOH B . 
K 6 HOH   97  397 51   HOH   HOH B . 
K 6 HOH   98  398 627  HOH   HOH B . 
K 6 HOH   99  399 16   HOH   HOH B . 
K 6 HOH   100 400 497  HOH   HOH B . 
K 6 HOH   101 401 77   HOH   HOH B . 
K 6 HOH   102 402 849  HOH   HOH B . 
K 6 HOH   103 403 1    HOH   HOH B . 
K 6 HOH   104 404 282  HOH   HOH B . 
K 6 HOH   105 405 534  HOH   HOH B . 
K 6 HOH   106 406 263  HOH   HOH B . 
K 6 HOH   107 407 360  HOH   HOH B . 
K 6 HOH   108 408 437  HOH   HOH B . 
K 6 HOH   109 409 395  HOH   HOH B . 
K 6 HOH   110 410 482  HOH   HOH B . 
K 6 HOH   111 411 94   HOH   HOH B . 
K 6 HOH   112 412 948  HOH   HOH B . 
K 6 HOH   113 413 365  HOH   HOH B . 
K 6 HOH   114 414 993  HOH   HOH B . 
K 6 HOH   115 415 430  HOH   HOH B . 
K 6 HOH   116 416 890  HOH   HOH B . 
K 6 HOH   117 417 1009 HOH   HOH B . 
K 6 HOH   118 418 920  HOH   HOH B . 
K 6 HOH   119 419 416  HOH   HOH B . 
K 6 HOH   120 420 1067 HOH   HOH B . 
K 6 HOH   121 421 620  HOH   HOH B . 
K 6 HOH   122 422 815  HOH   HOH B . 
K 6 HOH   123 423 485  HOH   HOH B . 
K 6 HOH   124 424 444  HOH   HOH B . 
K 6 HOH   125 425 402  HOH   HOH B . 
K 6 HOH   126 426 839  HOH   HOH B . 
K 6 HOH   127 427 412  HOH   HOH B . 
K 6 HOH   128 428 199  HOH   HOH B . 
K 6 HOH   129 429 314  HOH   HOH B . 
K 6 HOH   130 430 665  HOH   HOH B . 
K 6 HOH   131 431 192  HOH   HOH B . 
K 6 HOH   132 432 680  HOH   HOH B . 
K 6 HOH   133 433 312  HOH   HOH B . 
K 6 HOH   134 434 835  HOH   HOH B . 
K 6 HOH   135 435 344  HOH   HOH B . 
K 6 HOH   136 436 331  HOH   HOH B . 
K 6 HOH   137 437 356  HOH   HOH B . 
K 6 HOH   138 438 1068 HOH   HOH B . 
K 6 HOH   139 439 705  HOH   HOH B . 
K 6 HOH   140 440 957  HOH   HOH B . 
K 6 HOH   141 441 502  HOH   HOH B . 
K 6 HOH   142 442 258  HOH   HOH B . 
K 6 HOH   143 443 447  HOH   HOH B . 
K 6 HOH   144 444 1042 HOH   HOH B . 
K 6 HOH   145 445 325  HOH   HOH B . 
K 6 HOH   146 446 566  HOH   HOH B . 
K 6 HOH   147 447 696  HOH   HOH B . 
K 6 HOH   148 448 902  HOH   HOH B . 
K 6 HOH   149 449 243  HOH   HOH B . 
K 6 HOH   150 450 254  HOH   HOH B . 
K 6 HOH   151 451 36   HOH   HOH B . 
K 6 HOH   152 452 687  HOH   HOH B . 
K 6 HOH   153 453 1065 HOH   HOH B . 
K 6 HOH   154 454 1044 HOH   HOH B . 
K 6 HOH   155 455 875  HOH   HOH B . 
K 6 HOH   156 456 729  HOH   HOH B . 
K 6 HOH   157 457 490  HOH   HOH B . 
K 6 HOH   158 458 223  HOH   HOH B . 
K 6 HOH   159 459 1059 HOH   HOH B . 
K 6 HOH   160 460 313  HOH   HOH B . 
K 6 HOH   161 461 585  HOH   HOH B . 
K 6 HOH   162 462 512  HOH   HOH B . 
K 6 HOH   163 463 743  HOH   HOH B . 
K 6 HOH   164 464 632  HOH   HOH B . 
K 6 HOH   165 465 610  HOH   HOH B . 
K 6 HOH   166 466 131  HOH   HOH B . 
K 6 HOH   167 467 911  HOH   HOH B . 
K 6 HOH   168 468 12   HOH   HOH B . 
K 6 HOH   169 469 977  HOH   HOH B . 
K 6 HOH   170 470 949  HOH   HOH B . 
K 6 HOH   171 471 966  HOH   HOH B . 
K 6 HOH   172 472 533  HOH   HOH B . 
K 6 HOH   173 473 834  HOH   HOH B . 
K 6 HOH   174 474 170  HOH   HOH B . 
K 6 HOH   175 475 71   HOH   HOH B . 
K 6 HOH   176 476 723  HOH   HOH B . 
K 6 HOH   177 477 187  HOH   HOH B . 
K 6 HOH   178 478 998  HOH   HOH B . 
K 6 HOH   179 479 851  HOH   HOH B . 
K 6 HOH   180 480 615  HOH   HOH B . 
K 6 HOH   181 481 580  HOH   HOH B . 
K 6 HOH   182 482 960  HOH   HOH B . 
K 6 HOH   183 483 399  HOH   HOH B . 
K 6 HOH   184 484 1019 HOH   HOH B . 
K 6 HOH   185 485 1004 HOH   HOH B . 
K 6 HOH   186 486 896  HOH   HOH B . 
K 6 HOH   187 487 912  HOH   HOH B . 
K 6 HOH   188 488 941  HOH   HOH B . 
K 6 HOH   189 489 591  HOH   HOH B . 
K 6 HOH   190 490 832  HOH   HOH B . 
K 6 HOH   191 491 662  HOH   HOH B . 
K 6 HOH   192 492 363  HOH   HOH B . 
K 6 HOH   193 493 1007 HOH   HOH B . 
K 6 HOH   194 494 1041 HOH   HOH B . 
K 6 HOH   195 495 905  HOH   HOH B . 
K 6 HOH   196 496 797  HOH   HOH B . 
K 6 HOH   197 497 624  HOH   HOH B . 
K 6 HOH   198 498 670  HOH   HOH B . 
K 6 HOH   199 499 602  HOH   HOH B . 
K 6 HOH   200 500 334  HOH   HOH B . 
K 6 HOH   201 501 557  HOH   HOH B . 
K 6 HOH   202 502 429  HOH   HOH B . 
K 6 HOH   203 503 752  HOH   HOH B . 
K 6 HOH   204 504 69   HOH   HOH B . 
K 6 HOH   205 505 362  HOH   HOH B . 
K 6 HOH   206 506 981  HOH   HOH B . 
K 6 HOH   207 507 673  HOH   HOH B . 
K 6 HOH   208 508 818  HOH   HOH B . 
K 6 HOH   209 509 657  HOH   HOH B . 
K 6 HOH   210 510 654  HOH   HOH B . 
K 6 HOH   211 511 458  HOH   HOH B . 
K 6 HOH   212 512 449  HOH   HOH B . 
K 6 HOH   213 513 874  HOH   HOH B . 
K 6 HOH   214 514 924  HOH   HOH B . 
K 6 HOH   215 515 354  HOH   HOH B . 
K 6 HOH   216 516 699  HOH   HOH B . 
K 6 HOH   217 517 715  HOH   HOH B . 
K 6 HOH   218 518 766  HOH   HOH B . 
K 6 HOH   219 519 800  HOH   HOH B . 
K 6 HOH   220 520 1066 HOH   HOH B . 
K 6 HOH   221 521 795  HOH   HOH B . 
K 6 HOH   222 522 568  HOH   HOH B . 
K 6 HOH   223 523 370  HOH   HOH B . 
K 6 HOH   224 524 963  HOH   HOH B . 
K 6 HOH   225 525 562  HOH   HOH B . 
K 6 HOH   226 526 678  HOH   HOH B . 
K 6 HOH   227 527 525  HOH   HOH B . 
K 6 HOH   228 528 522  HOH   HOH B . 
K 6 HOH   229 529 858  HOH   HOH B . 
K 6 HOH   230 530 623  HOH   HOH B . 
K 6 HOH   231 531 492  HOH   HOH B . 
K 6 HOH   232 532 371  HOH   HOH B . 
K 6 HOH   233 533 658  HOH   HOH B . 
K 6 HOH   234 534 35   HOH   HOH B . 
K 6 HOH   235 535 991  HOH   HOH B . 
K 6 HOH   236 536 793  HOH   HOH B . 
K 6 HOH   237 537 388  HOH   HOH B . 
K 6 HOH   238 538 943  HOH   HOH B . 
K 6 HOH   239 539 777  HOH   HOH B . 
K 6 HOH   240 540 1069 HOH   HOH B . 
K 6 HOH   241 541 860  HOH   HOH B . 
K 6 HOH   242 542 633  HOH   HOH B . 
K 6 HOH   243 543 1018 HOH   HOH B . 
K 6 HOH   244 544 593  HOH   HOH B . 
K 6 HOH   245 545 866  HOH   HOH B . 
K 6 HOH   246 546 639  HOH   HOH B . 
K 6 HOH   247 547 186  HOH   HOH B . 
K 6 HOH   248 548 714  HOH   HOH B . 
K 6 HOH   249 549 816  HOH   HOH B . 
K 6 HOH   250 550 962  HOH   HOH B . 
K 6 HOH   251 551 914  HOH   HOH B . 
K 6 HOH   252 552 995  HOH   HOH B . 
K 6 HOH   253 553 1070 HOH   HOH B . 
K 6 HOH   254 554 477  HOH   HOH B . 
K 6 HOH   255 555 734  HOH   HOH B . 
K 6 HOH   256 556 901  HOH   HOH B . 
K 6 HOH   257 557 913  HOH   HOH B . 
K 6 HOH   258 558 988  HOH   HOH B . 
K 6 HOH   259 559 883  HOH   HOH B . 
K 6 HOH   260 560 1010 HOH   HOH B . 
K 6 HOH   261 561 700  HOH   HOH B . 
K 6 HOH   262 562 704  HOH   HOH B . 
L 6 HOH   1   301 660  HOH   HOH A . 
L 6 HOH   2   302 549  HOH   HOH A . 
L 6 HOH   3   303 652  HOH   HOH A . 
L 6 HOH   4   304 782  HOH   HOH A . 
L 6 HOH   5   305 726  HOH   HOH A . 
L 6 HOH   6   306 1048 HOH   HOH A . 
L 6 HOH   7   307 691  HOH   HOH A . 
L 6 HOH   8   308 336  HOH   HOH A . 
L 6 HOH   9   309 454  HOH   HOH A . 
L 6 HOH   10  310 965  HOH   HOH A . 
L 6 HOH   11  311 91   HOH   HOH A . 
L 6 HOH   12  312 634  HOH   HOH A . 
L 6 HOH   13  313 237  HOH   HOH A . 
L 6 HOH   14  314 1056 HOH   HOH A . 
L 6 HOH   15  315 378  HOH   HOH A . 
L 6 HOH   16  316 215  HOH   HOH A . 
L 6 HOH   17  317 1020 HOH   HOH A . 
L 6 HOH   18  318 247  HOH   HOH A . 
L 6 HOH   19  319 40   HOH   HOH A . 
L 6 HOH   20  320 491  HOH   HOH A . 
L 6 HOH   21  321 62   HOH   HOH A . 
L 6 HOH   22  322 558  HOH   HOH A . 
L 6 HOH   23  323 102  HOH   HOH A . 
L 6 HOH   24  324 501  HOH   HOH A . 
L 6 HOH   25  325 509  HOH   HOH A . 
L 6 HOH   26  326 541  HOH   HOH A . 
L 6 HOH   27  327 303  HOH   HOH A . 
L 6 HOH   28  328 180  HOH   HOH A . 
L 6 HOH   29  329 18   HOH   HOH A . 
L 6 HOH   30  330 1005 HOH   HOH A . 
L 6 HOH   31  331 1013 HOH   HOH A . 
L 6 HOH   32  332 555  HOH   HOH A . 
L 6 HOH   33  333 280  HOH   HOH A . 
L 6 HOH   34  334 584  HOH   HOH A . 
L 6 HOH   35  335 98   HOH   HOH A . 
L 6 HOH   36  336 648  HOH   HOH A . 
L 6 HOH   37  337 239  HOH   HOH A . 
L 6 HOH   38  338 586  HOH   HOH A . 
L 6 HOH   39  339 655  HOH   HOH A . 
L 6 HOH   40  340 463  HOH   HOH A . 
L 6 HOH   41  341 433  HOH   HOH A . 
L 6 HOH   42  342 106  HOH   HOH A . 
L 6 HOH   43  343 119  HOH   HOH A . 
L 6 HOH   44  344 468  HOH   HOH A . 
L 6 HOH   45  345 779  HOH   HOH A . 
L 6 HOH   46  346 762  HOH   HOH A . 
L 6 HOH   47  347 226  HOH   HOH A . 
L 6 HOH   48  348 235  HOH   HOH A . 
L 6 HOH   49  349 996  HOH   HOH A . 
L 6 HOH   50  350 21   HOH   HOH A . 
L 6 HOH   51  351 546  HOH   HOH A . 
L 6 HOH   52  352 925  HOH   HOH A . 
L 6 HOH   53  353 29   HOH   HOH A . 
L 6 HOH   54  354 717  HOH   HOH A . 
L 6 HOH   55  355 465  HOH   HOH A . 
L 6 HOH   56  356 207  HOH   HOH A . 
L 6 HOH   57  357 403  HOH   HOH A . 
L 6 HOH   58  358 645  HOH   HOH A . 
L 6 HOH   59  359 342  HOH   HOH A . 
L 6 HOH   60  360 125  HOH   HOH A . 
L 6 HOH   61  361 440  HOH   HOH A . 
L 6 HOH   62  362 147  HOH   HOH A . 
L 6 HOH   63  363 45   HOH   HOH A . 
L 6 HOH   64  364 787  HOH   HOH A . 
L 6 HOH   65  365 255  HOH   HOH A . 
L 6 HOH   66  366 48   HOH   HOH A . 
L 6 HOH   67  367 1026 HOH   HOH A . 
L 6 HOH   68  368 511  HOH   HOH A . 
L 6 HOH   69  369 805  HOH   HOH A . 
L 6 HOH   70  370 434  HOH   HOH A . 
L 6 HOH   71  371 464  HOH   HOH A . 
L 6 HOH   72  372 109  HOH   HOH A . 
L 6 HOH   73  373 335  HOH   HOH A . 
L 6 HOH   74  374 178  HOH   HOH A . 
L 6 HOH   75  375 161  HOH   HOH A . 
L 6 HOH   76  376 625  HOH   HOH A . 
L 6 HOH   77  377 151  HOH   HOH A . 
L 6 HOH   78  378 270  HOH   HOH A . 
L 6 HOH   79  379 801  HOH   HOH A . 
L 6 HOH   80  380 1045 HOH   HOH A . 
L 6 HOH   81  381 141  HOH   HOH A . 
L 6 HOH   82  382 37   HOH   HOH A . 
L 6 HOH   83  383 276  HOH   HOH A . 
L 6 HOH   84  384 394  HOH   HOH A . 
L 6 HOH   85  385 719  HOH   HOH A . 
L 6 HOH   86  386 130  HOH   HOH A . 
L 6 HOH   87  387 111  HOH   HOH A . 
L 6 HOH   88  388 152  HOH   HOH A . 
L 6 HOH   89  389 756  HOH   HOH A . 
L 6 HOH   90  390 992  HOH   HOH A . 
L 6 HOH   91  391 14   HOH   HOH A . 
L 6 HOH   92  392 713  HOH   HOH A . 
L 6 HOH   93  393 182  HOH   HOH A . 
L 6 HOH   94  394 248  HOH   HOH A . 
L 6 HOH   95  395 698  HOH   HOH A . 
L 6 HOH   96  396 193  HOH   HOH A . 
L 6 HOH   97  397 251  HOH   HOH A . 
L 6 HOH   98  398 908  HOH   HOH A . 
L 6 HOH   99  399 821  HOH   HOH A . 
L 6 HOH   100 400 202  HOH   HOH A . 
L 6 HOH   101 401 747  HOH   HOH A . 
L 6 HOH   102 402 224  HOH   HOH A . 
L 6 HOH   103 403 506  HOH   HOH A . 
L 6 HOH   104 404 61   HOH   HOH A . 
L 6 HOH   105 405 411  HOH   HOH A . 
L 6 HOH   106 406 887  HOH   HOH A . 
L 6 HOH   107 407 1049 HOH   HOH A . 
L 6 HOH   108 408 631  HOH   HOH A . 
L 6 HOH   109 409 6    HOH   HOH A . 
L 6 HOH   110 410 573  HOH   HOH A . 
L 6 HOH   111 411 565  HOH   HOH A . 
L 6 HOH   112 412 881  HOH   HOH A . 
L 6 HOH   113 413 232  HOH   HOH A . 
L 6 HOH   114 414 81   HOH   HOH A . 
L 6 HOH   115 415 983  HOH   HOH A . 
L 6 HOH   116 416 937  HOH   HOH A . 
L 6 HOH   117 417 355  HOH   HOH A . 
L 6 HOH   118 418 145  HOH   HOH A . 
L 6 HOH   119 419 64   HOH   HOH A . 
L 6 HOH   120 420 609  HOH   HOH A . 
L 6 HOH   121 421 225  HOH   HOH A . 
L 6 HOH   122 422 741  HOH   HOH A . 
L 6 HOH   123 423 1050 HOH   HOH A . 
L 6 HOH   124 424 431  HOH   HOH A . 
L 6 HOH   125 425 324  HOH   HOH A . 
L 6 HOH   126 426 24   HOH   HOH A . 
L 6 HOH   127 427 852  HOH   HOH A . 
L 6 HOH   128 428 367  HOH   HOH A . 
L 6 HOH   129 429 663  HOH   HOH A . 
L 6 HOH   130 430 409  HOH   HOH A . 
L 6 HOH   131 431 807  HOH   HOH A . 
L 6 HOH   132 432 783  HOH   HOH A . 
L 6 HOH   133 433 742  HOH   HOH A . 
L 6 HOH   134 434 15   HOH   HOH A . 
L 6 HOH   135 435 257  HOH   HOH A . 
L 6 HOH   136 436 489  HOH   HOH A . 
L 6 HOH   137 437 737  HOH   HOH A . 
L 6 HOH   138 438 760  HOH   HOH A . 
L 6 HOH   139 439 268  HOH   HOH A . 
L 6 HOH   140 440 384  HOH   HOH A . 
L 6 HOH   141 441 290  HOH   HOH A . 
L 6 HOH   142 442 535  HOH   HOH A . 
L 6 HOH   143 443 184  HOH   HOH A . 
L 6 HOH   144 444 43   HOH   HOH A . 
L 6 HOH   145 445 842  HOH   HOH A . 
L 6 HOH   146 446 831  HOH   HOH A . 
L 6 HOH   147 447 695  HOH   HOH A . 
L 6 HOH   148 448 66   HOH   HOH A . 
L 6 HOH   149 449 532  HOH   HOH A . 
L 6 HOH   150 450 56   HOH   HOH A . 
L 6 HOH   151 451 500  HOH   HOH A . 
L 6 HOH   152 452 159  HOH   HOH A . 
L 6 HOH   153 453 228  HOH   HOH A . 
L 6 HOH   154 454 536  HOH   HOH A . 
L 6 HOH   155 455 126  HOH   HOH A . 
L 6 HOH   156 456 30   HOH   HOH A . 
L 6 HOH   157 457 539  HOH   HOH A . 
L 6 HOH   158 458 1053 HOH   HOH A . 
L 6 HOH   159 459 643  HOH   HOH A . 
L 6 HOH   160 460 604  HOH   HOH A . 
L 6 HOH   161 461 348  HOH   HOH A . 
L 6 HOH   162 462 636  HOH   HOH A . 
L 6 HOH   163 463 850  HOH   HOH A . 
L 6 HOH   164 464 886  HOH   HOH A . 
L 6 HOH   165 465 973  HOH   HOH A . 
L 6 HOH   166 466 1072 HOH   HOH A . 
L 6 HOH   167 467 986  HOH   HOH A . 
L 6 HOH   168 468 475  HOH   HOH A . 
L 6 HOH   169 469 814  HOH   HOH A . 
L 6 HOH   170 470 1051 HOH   HOH A . 
L 6 HOH   171 471 971  HOH   HOH A . 
L 6 HOH   172 472 889  HOH   HOH A . 
L 6 HOH   173 473 907  HOH   HOH A . 
L 6 HOH   174 474 113  HOH   HOH A . 
L 6 HOH   175 475 300  HOH   HOH A . 
L 6 HOH   176 476 812  HOH   HOH A . 
L 6 HOH   177 477 869  HOH   HOH A . 
L 6 HOH   178 478 1043 HOH   HOH A . 
L 6 HOH   179 479 972  HOH   HOH A . 
L 6 HOH   180 480 786  HOH   HOH A . 
L 6 HOH   181 481 827  HOH   HOH A . 
L 6 HOH   182 482 518  HOH   HOH A . 
L 6 HOH   183 483 840  HOH   HOH A . 
L 6 HOH   184 484 1054 HOH   HOH A . 
L 6 HOH   185 485 382  HOH   HOH A . 
L 6 HOH   186 486 167  HOH   HOH A . 
L 6 HOH   187 487 989  HOH   HOH A . 
L 6 HOH   188 488 923  HOH   HOH A . 
L 6 HOH   189 489 136  HOH   HOH A . 
L 6 HOH   190 490 683  HOH   HOH A . 
L 6 HOH   191 491 904  HOH   HOH A . 
L 6 HOH   192 492 1055 HOH   HOH A . 
L 6 HOH   193 493 703  HOH   HOH A . 
L 6 HOH   194 494 425  HOH   HOH A . 
L 6 HOH   195 495 339  HOH   HOH A . 
L 6 HOH   196 496 350  HOH   HOH A . 
L 6 HOH   197 497 97   HOH   HOH A . 
L 6 HOH   198 498 763  HOH   HOH A . 
L 6 HOH   199 499 1047 HOH   HOH A . 
L 6 HOH   200 500 956  HOH   HOH A . 
L 6 HOH   201 501 942  HOH   HOH A . 
L 6 HOH   202 502 393  HOH   HOH A . 
L 6 HOH   203 503 456  HOH   HOH A . 
L 6 HOH   204 504 716  HOH   HOH A . 
L 6 HOH   205 505 823  HOH   HOH A . 
L 6 HOH   206 506 1046 HOH   HOH A . 
L 6 HOH   207 507 289  HOH   HOH A . 
L 6 HOH   208 508 295  HOH   HOH A . 
L 6 HOH   209 509 772  HOH   HOH A . 
L 6 HOH   210 510 472  HOH   HOH A . 
L 6 HOH   211 511 909  HOH   HOH A . 
L 6 HOH   212 512 1035 HOH   HOH A . 
L 6 HOH   213 513 891  HOH   HOH A . 
L 6 HOH   214 514 975  HOH   HOH A . 
L 6 HOH   215 515 646  HOH   HOH A . 
L 6 HOH   216 516 529  HOH   HOH A . 
L 6 HOH   217 517 826  HOH   HOH A . 
L 6 HOH   218 518 796  HOH   HOH A . 
L 6 HOH   219 519 961  HOH   HOH A . 
L 6 HOH   220 520 690  HOH   HOH A . 
L 6 HOH   221 521 618  HOH   HOH A . 
L 6 HOH   222 522 603  HOH   HOH A . 
L 6 HOH   223 523 1000 HOH   HOH A . 
L 6 HOH   224 524 383  HOH   HOH A . 
L 6 HOH   225 525 785  HOH   HOH A . 
L 6 HOH   226 526 745  HOH   HOH A . 
L 6 HOH   227 527 880  HOH   HOH A . 
L 6 HOH   228 528 754  HOH   HOH A . 
L 6 HOH   229 529 521  HOH   HOH A . 
L 6 HOH   230 530 474  HOH   HOH A . 
L 6 HOH   231 531 49   HOH   HOH A . 
L 6 HOH   232 532 486  HOH   HOH A . 
L 6 HOH   233 533 1057 HOH   HOH A . 
L 6 HOH   234 534 493  HOH   HOH A . 
L 6 HOH   235 535 916  HOH   HOH A . 
L 6 HOH   236 536 915  HOH   HOH A . 
L 6 HOH   237 537 799  HOH   HOH A . 
L 6 HOH   238 538 1032 HOH   HOH A . 
L 6 HOH   239 539 380  HOH   HOH A . 
L 6 HOH   240 540 824  HOH   HOH A . 
L 6 HOH   241 541 868  HOH   HOH A . 
L 6 HOH   242 542 647  HOH   HOH A . 
L 6 HOH   243 543 514  HOH   HOH A . 
L 6 HOH   244 544 115  HOH   HOH A . 
L 6 HOH   245 545 894  HOH   HOH A . 
L 6 HOH   246 546 861  HOH   HOH A . 
L 6 HOH   247 547 1052 HOH   HOH A . 
L 6 HOH   248 548 708  HOH   HOH A . 
L 6 HOH   249 549 994  HOH   HOH A . 
L 6 HOH   250 550 599  HOH   HOH A . 
L 6 HOH   251 551 614  HOH   HOH A . 
L 6 HOH   252 552 863  HOH   HOH A . 
L 6 HOH   253 553 644  HOH   HOH A . 
L 6 HOH   254 554 1003 HOH   HOH A . 
L 6 HOH   255 555 952  HOH   HOH A . 
L 6 HOH   256 556 798  HOH   HOH A . 
L 6 HOH   257 557 744  HOH   HOH A . 
L 6 HOH   258 558 1006 HOH   HOH A . 
L 6 HOH   259 559 893  HOH   HOH A . 
L 6 HOH   260 560 769  HOH   HOH A . 
L 6 HOH   261 561 876  HOH   HOH A . 
L 6 HOH   262 562 1002 HOH   HOH A . 
M 6 HOH   1   201 587  HOH   HOH C . 
M 6 HOH   2   202 265  HOH   HOH C . 
M 6 HOH   3   203 510  HOH   HOH C . 
M 6 HOH   4   204 481  HOH   HOH C . 
M 6 HOH   5   205 595  HOH   HOH C . 
M 6 HOH   6   206 846  HOH   HOH C . 
M 6 HOH   7   207 612  HOH   HOH C . 
M 6 HOH   8   208 181  HOH   HOH C . 
M 6 HOH   9   209 706  HOH   HOH C . 
M 6 HOH   10  210 574  HOH   HOH C . 
M 6 HOH   11  211 448  HOH   HOH C . 
M 6 HOH   12  212 817  HOH   HOH C . 
M 6 HOH   13  213 445  HOH   HOH C . 
M 6 HOH   14  214 684  HOH   HOH C . 
M 6 HOH   15  215 761  HOH   HOH C . 
M 6 HOH   16  216 216  HOH   HOH C . 
M 6 HOH   17  217 376  HOH   HOH C . 
M 6 HOH   18  218 329  HOH   HOH C . 
M 6 HOH   19  219 166  HOH   HOH C . 
M 6 HOH   20  220 531  HOH   HOH C . 
M 6 HOH   21  221 86   HOH   HOH C . 
M 6 HOH   22  222 277  HOH   HOH C . 
M 6 HOH   23  223 478  HOH   HOH C . 
M 6 HOH   24  224 114  HOH   HOH C . 
M 6 HOH   25  225 508  HOH   HOH C . 
M 6 HOH   26  226 543  HOH   HOH C . 
M 6 HOH   27  227 685  HOH   HOH C . 
M 6 HOH   28  228 240  HOH   HOH C . 
M 6 HOH   29  229 778  HOH   HOH C . 
M 6 HOH   30  230 101  HOH   HOH C . 
M 6 HOH   31  231 404  HOH   HOH C . 
M 6 HOH   32  232 767  HOH   HOH C . 
M 6 HOH   33  233 369  HOH   HOH C . 
M 6 HOH   34  234 112  HOH   HOH C . 
M 6 HOH   35  235 38   HOH   HOH C . 
M 6 HOH   36  236 32   HOH   HOH C . 
M 6 HOH   37  237 516  HOH   HOH C . 
M 6 HOH   38  238 177  HOH   HOH C . 
M 6 HOH   39  239 75   HOH   HOH C . 
M 6 HOH   40  240 375  HOH   HOH C . 
M 6 HOH   41  241 337  HOH   HOH C . 
M 6 HOH   42  242 275  HOH   HOH C . 
M 6 HOH   43  243 414  HOH   HOH C . 
M 6 HOH   44  244 1037 HOH   HOH C . 
M 6 HOH   45  245 462  HOH   HOH C . 
M 6 HOH   46  246 212  HOH   HOH C . 
M 6 HOH   47  247 470  HOH   HOH C . 
M 6 HOH   48  248 173  HOH   HOH C . 
M 6 HOH   49  249 57   HOH   HOH C . 
M 6 HOH   50  250 1034 HOH   HOH C . 
M 6 HOH   51  251 505  HOH   HOH C . 
M 6 HOH   52  252 205  HOH   HOH C . 
M 6 HOH   53  253 165  HOH   HOH C . 
M 6 HOH   54  254 11   HOH   HOH C . 
M 6 HOH   55  255 413  HOH   HOH C . 
M 6 HOH   56  256 976  HOH   HOH C . 
M 6 HOH   57  257 494  HOH   HOH C . 
M 6 HOH   58  258 137  HOH   HOH C . 
M 6 HOH   59  259 135  HOH   HOH C . 
M 6 HOH   60  260 23   HOH   HOH C . 
M 6 HOH   61  261 153  HOH   HOH C . 
M 6 HOH   62  262 261  HOH   HOH C . 
M 6 HOH   63  263 73   HOH   HOH C . 
M 6 HOH   64  264 283  HOH   HOH C . 
M 6 HOH   65  265 321  HOH   HOH C . 
M 6 HOH   66  266 417  HOH   HOH C . 
M 6 HOH   67  267 234  HOH   HOH C . 
M 6 HOH   68  268 157  HOH   HOH C . 
M 6 HOH   69  269 13   HOH   HOH C . 
M 6 HOH   70  270 42   HOH   HOH C . 
M 6 HOH   71  271 107  HOH   HOH C . 
M 6 HOH   72  272 523  HOH   HOH C . 
M 6 HOH   73  273 262  HOH   HOH C . 
M 6 HOH   74  274 213  HOH   HOH C . 
M 6 HOH   75  275 479  HOH   HOH C . 
M 6 HOH   76  276 60   HOH   HOH C . 
M 6 HOH   77  277 731  HOH   HOH C . 
M 6 HOH   78  278 196  HOH   HOH C . 
M 6 HOH   79  279 327  HOH   HOH C . 
M 6 HOH   80  280 65   HOH   HOH C . 
M 6 HOH   81  281 571  HOH   HOH C . 
M 6 HOH   82  282 809  HOH   HOH C . 
M 6 HOH   83  283 397  HOH   HOH C . 
M 6 HOH   84  284 143  HOH   HOH C . 
M 6 HOH   85  285 438  HOH   HOH C . 
M 6 HOH   86  286 681  HOH   HOH C . 
M 6 HOH   87  287 210  HOH   HOH C . 
M 6 HOH   88  288 385  HOH   HOH C . 
M 6 HOH   89  289 829  HOH   HOH C . 
M 6 HOH   90  290 175  HOH   HOH C . 
M 6 HOH   91  291 707  HOH   HOH C . 
M 6 HOH   92  292 725  HOH   HOH C . 
M 6 HOH   93  293 124  HOH   HOH C . 
M 6 HOH   94  294 90   HOH   HOH C . 
M 6 HOH   95  295 76   HOH   HOH C . 
M 6 HOH   96  296 548  HOH   HOH C . 
M 6 HOH   97  297 55   HOH   HOH C . 
M 6 HOH   98  298 121  HOH   HOH C . 
M 6 HOH   99  299 759  HOH   HOH C . 
M 6 HOH   100 300 7    HOH   HOH C . 
M 6 HOH   101 301 80   HOH   HOH C . 
M 6 HOH   102 302 718  HOH   HOH C . 
M 6 HOH   103 303 264  HOH   HOH C . 
M 6 HOH   104 304 227  HOH   HOH C . 
M 6 HOH   105 305 278  HOH   HOH C . 
M 6 HOH   106 306 190  HOH   HOH C . 
M 6 HOH   107 307 158  HOH   HOH C . 
M 6 HOH   108 308 39   HOH   HOH C . 
M 6 HOH   109 309 306  HOH   HOH C . 
M 6 HOH   110 310 296  HOH   HOH C . 
M 6 HOH   111 311 1033 HOH   HOH C . 
M 6 HOH   112 312 229  HOH   HOH C . 
M 6 HOH   113 313 272  HOH   HOH C . 
M 6 HOH   114 314 171  HOH   HOH C . 
M 6 HOH   115 315 217  HOH   HOH C . 
M 6 HOH   116 316 583  HOH   HOH C . 
M 6 HOH   117 317 527  HOH   HOH C . 
M 6 HOH   118 318 422  HOH   HOH C . 
M 6 HOH   119 319 974  HOH   HOH C . 
M 6 HOH   120 320 900  HOH   HOH C . 
M 6 HOH   121 321 622  HOH   HOH C . 
M 6 HOH   122 322 693  HOH   HOH C . 
M 6 HOH   123 323 242  HOH   HOH C . 
M 6 HOH   124 324 169  HOH   HOH C . 
M 6 HOH   125 325 471  HOH   HOH C . 
M 6 HOH   126 326 320  HOH   HOH C . 
M 6 HOH   127 327 128  HOH   HOH C . 
M 6 HOH   128 328 545  HOH   HOH C . 
M 6 HOH   129 329 770  HOH   HOH C . 
M 6 HOH   130 330 315  HOH   HOH C . 
M 6 HOH   131 331 22   HOH   HOH C . 
M 6 HOH   132 332 301  HOH   HOH C . 
M 6 HOH   133 333 701  HOH   HOH C . 
M 6 HOH   134 334 269  HOH   HOH C . 
M 6 HOH   135 335 997  HOH   HOH C . 
M 6 HOH   136 336 259  HOH   HOH C . 
M 6 HOH   137 337 435  HOH   HOH C . 
M 6 HOH   138 338 751  HOH   HOH C . 
M 6 HOH   139 339 556  HOH   HOH C . 
M 6 HOH   140 340 221  HOH   HOH C . 
M 6 HOH   141 341 123  HOH   HOH C . 
M 6 HOH   142 342 569  HOH   HOH C . 
M 6 HOH   143 343 774  HOH   HOH C . 
M 6 HOH   144 344 298  HOH   HOH C . 
M 6 HOH   145 345 118  HOH   HOH C . 
M 6 HOH   146 346 201  HOH   HOH C . 
M 6 HOH   147 347 357  HOH   HOH C . 
M 6 HOH   148 348 150  HOH   HOH C . 
M 6 HOH   149 349 332  HOH   HOH C . 
M 6 HOH   150 350 88   HOH   HOH C . 
M 6 HOH   151 351 930  HOH   HOH C . 
M 6 HOH   152 352 459  HOH   HOH C . 
M 6 HOH   153 353 564  HOH   HOH C . 
M 6 HOH   154 354 172  HOH   HOH C . 
M 6 HOH   155 355 550  HOH   HOH C . 
M 6 HOH   156 356 879  HOH   HOH C . 
M 6 HOH   157 357 968  HOH   HOH C . 
M 6 HOH   158 358 642  HOH   HOH C . 
M 6 HOH   159 359 194  HOH   HOH C . 
M 6 HOH   160 360 616  HOH   HOH C . 
M 6 HOH   161 361 950  HOH   HOH C . 
M 6 HOH   162 362 307  HOH   HOH C . 
M 6 HOH   163 363 689  HOH   HOH C . 
M 6 HOH   164 364 979  HOH   HOH C . 
M 6 HOH   165 365 442  HOH   HOH C . 
M 6 HOH   166 366 480  HOH   HOH C . 
M 6 HOH   167 367 728  HOH   HOH C . 
M 6 HOH   168 368 526  HOH   HOH C . 
M 6 HOH   169 369 110  HOH   HOH C . 
M 6 HOH   170 370 330  HOH   HOH C . 
M 6 HOH   171 371 538  HOH   HOH C . 
M 6 HOH   172 372 499  HOH   HOH C . 
M 6 HOH   173 373 935  HOH   HOH C . 
M 6 HOH   174 374 1025 HOH   HOH C . 
M 6 HOH   175 375 266  HOH   HOH C . 
M 6 HOH   176 376 441  HOH   HOH C . 
M 6 HOH   177 377 939  HOH   HOH C . 
M 6 HOH   178 378 1058 HOH   HOH C . 
M 6 HOH   179 379 349  HOH   HOH C . 
M 6 HOH   180 380 1021 HOH   HOH C . 
M 6 HOH   181 381 1011 HOH   HOH C . 
M 6 HOH   182 382 347  HOH   HOH C . 
M 6 HOH   183 383 559  HOH   HOH C . 
M 6 HOH   184 384 953  HOH   HOH C . 
M 6 HOH   185 385 836  HOH   HOH C . 
M 6 HOH   186 386 669  HOH   HOH C . 
M 6 HOH   187 387 733  HOH   HOH C . 
M 6 HOH   188 388 1014 HOH   HOH C . 
M 6 HOH   189 389 366  HOH   HOH C . 
M 6 HOH   190 390 628  HOH   HOH C . 
M 6 HOH   191 391 677  HOH   HOH C . 
M 6 HOH   192 392 808  HOH   HOH C . 
M 6 HOH   193 393 635  HOH   HOH C . 
M 6 HOH   194 394 727  HOH   HOH C . 
M 6 HOH   195 395 959  HOH   HOH C . 
M 6 HOH   196 396 870  HOH   HOH C . 
M 6 HOH   197 397 63   HOH   HOH C . 
M 6 HOH   198 398 830  HOH   HOH C . 
M 6 HOH   199 399 739  HOH   HOH C . 
M 6 HOH   200 400 899  HOH   HOH C . 
M 6 HOH   201 401 847  HOH   HOH C . 
M 6 HOH   202 402 746  HOH   HOH C . 
M 6 HOH   203 403 906  HOH   HOH C . 
M 6 HOH   204 404 561  HOH   HOH C . 
M 6 HOH   205 405 638  HOH   HOH C . 
M 6 HOH   206 406 198  HOH   HOH C . 
M 6 HOH   207 407 563  HOH   HOH C . 
M 6 HOH   208 408 792  HOH   HOH C . 
M 6 HOH   209 409 211  HOH   HOH C . 
M 6 HOH   210 410 755  HOH   HOH C . 
M 6 HOH   211 411 982  HOH   HOH C . 
M 6 HOH   212 412 120  HOH   HOH C . 
M 6 HOH   213 413 892  HOH   HOH C . 
M 6 HOH   214 414 730  HOH   HOH C . 
M 6 HOH   215 415 811  HOH   HOH C . 
M 6 HOH   216 416 406  HOH   HOH C . 
M 6 HOH   217 417 749  HOH   HOH C . 
M 6 HOH   218 418 855  HOH   HOH C . 
M 6 HOH   219 419 1017 HOH   HOH C . 
M 6 HOH   220 420 757  HOH   HOH C . 
M 6 HOH   221 421 577  HOH   HOH C . 
M 6 HOH   222 422 877  HOH   HOH C . 
M 6 HOH   223 423 155  HOH   HOH C . 
M 6 HOH   224 424 343  HOH   HOH C . 
M 6 HOH   225 425 162  HOH   HOH C . 
M 6 HOH   226 426 457  HOH   HOH C . 
M 6 HOH   227 427 938  HOH   HOH C . 
M 6 HOH   228 428 309  HOH   HOH C . 
M 6 HOH   229 429 581  HOH   HOH C . 
M 6 HOH   230 430 496  HOH   HOH C . 
M 6 HOH   231 431 674  HOH   HOH C . 
M 6 HOH   232 432 804  HOH   HOH C . 
M 6 HOH   233 433 553  HOH   HOH C . 
M 6 HOH   234 434 524  HOH   HOH C . 
M 6 HOH   235 435 967  HOH   HOH C . 
M 6 HOH   236 436 929  HOH   HOH C . 
M 6 HOH   237 437 711  HOH   HOH C . 
M 6 HOH   238 438 650  HOH   HOH C . 
M 6 HOH   239 439 249  HOH   HOH C . 
M 6 HOH   240 440 373  HOH   HOH C . 
M 6 HOH   241 441 374  HOH   HOH C . 
M 6 HOH   242 442 84   HOH   HOH C . 
M 6 HOH   243 443 659  HOH   HOH C . 
M 6 HOH   244 444 626  HOH   HOH C . 
M 6 HOH   245 445 910  HOH   HOH C . 
N 6 HOH   1   201 721  HOH   HOH D . 
N 6 HOH   2   202 551  HOH   HOH D . 
N 6 HOH   3   203 688  HOH   HOH D . 
N 6 HOH   4   204 653  HOH   HOH D . 
N 6 HOH   5   205 319  HOH   HOH D . 
N 6 HOH   6   206 452  HOH   HOH D . 
N 6 HOH   7   207 455  HOH   HOH D . 
N 6 HOH   8   208 436  HOH   HOH D . 
N 6 HOH   9   209 129  HOH   HOH D . 
N 6 HOH   10  210 338  HOH   HOH D . 
N 6 HOH   11  211 214  HOH   HOH D . 
N 6 HOH   12  212 528  HOH   HOH D . 
N 6 HOH   13  213 686  HOH   HOH D . 
N 6 HOH   14  214 219  HOH   HOH D . 
N 6 HOH   15  215 10   HOH   HOH D . 
N 6 HOH   16  216 341  HOH   HOH D . 
N 6 HOH   17  217 732  HOH   HOH D . 
N 6 HOH   18  218 74   HOH   HOH D . 
N 6 HOH   19  219 806  HOH   HOH D . 
N 6 HOH   20  220 222  HOH   HOH D . 
N 6 HOH   21  221 326  HOH   HOH D . 
N 6 HOH   22  222 317  HOH   HOH D . 
N 6 HOH   23  223 241  HOH   HOH D . 
N 6 HOH   24  224 195  HOH   HOH D . 
N 6 HOH   25  225 702  HOH   HOH D . 
N 6 HOH   26  226 641  HOH   HOH D . 
N 6 HOH   27  227 78   HOH   HOH D . 
N 6 HOH   28  228 1001 HOH   HOH D . 
N 6 HOH   29  229 138  HOH   HOH D . 
N 6 HOH   30  230 410  HOH   HOH D . 
N 6 HOH   31  231 252  HOH   HOH D . 
N 6 HOH   32  232 3    HOH   HOH D . 
N 6 HOH   33  233 92   HOH   HOH D . 
N 6 HOH   34  234 236  HOH   HOH D . 
N 6 HOH   35  235 4    HOH   HOH D . 
N 6 HOH   36  236 461  HOH   HOH D . 
N 6 HOH   37  237 519  HOH   HOH D . 
N 6 HOH   38  238 791  HOH   HOH D . 
N 6 HOH   39  239 146  HOH   HOH D . 
N 6 HOH   40  240 148  HOH   HOH D . 
N 6 HOH   41  241 253  HOH   HOH D . 
N 6 HOH   42  242 517  HOH   HOH D . 
N 6 HOH   43  243 401  HOH   HOH D . 
N 6 HOH   44  244 588  HOH   HOH D . 
N 6 HOH   45  245 515  HOH   HOH D . 
N 6 HOH   46  246 740  HOH   HOH D . 
N 6 HOH   47  247 353  HOH   HOH D . 
N 6 HOH   48  248 985  HOH   HOH D . 
N 6 HOH   49  249 694  HOH   HOH D . 
N 6 HOH   50  250 819  HOH   HOH D . 
N 6 HOH   51  251 469  HOH   HOH D . 
N 6 HOH   52  252 154  HOH   HOH D . 
N 6 HOH   53  253 122  HOH   HOH D . 
N 6 HOH   54  254 46   HOH   HOH D . 
N 6 HOH   55  255 351  HOH   HOH D . 
N 6 HOH   56  256 87   HOH   HOH D . 
N 6 HOH   57  257 176  HOH   HOH D . 
N 6 HOH   58  258 231  HOH   HOH D . 
N 6 HOH   59  259 26   HOH   HOH D . 
N 6 HOH   60  260 197  HOH   HOH D . 
N 6 HOH   61  261 96   HOH   HOH D . 
N 6 HOH   62  262 601  HOH   HOH D . 
N 6 HOH   63  263 200  HOH   HOH D . 
N 6 HOH   64  264 168  HOH   HOH D . 
N 6 HOH   65  265 768  HOH   HOH D . 
N 6 HOH   66  266 132  HOH   HOH D . 
N 6 HOH   67  267 164  HOH   HOH D . 
N 6 HOH   68  268 99   HOH   HOH D . 
N 6 HOH   69  269 103  HOH   HOH D . 
N 6 HOH   70  270 100  HOH   HOH D . 
N 6 HOH   71  271 299  HOH   HOH D . 
N 6 HOH   72  272 149  HOH   HOH D . 
N 6 HOH   73  273 802  HOH   HOH D . 
N 6 HOH   74  274 392  HOH   HOH D . 
N 6 HOH   75  275 271  HOH   HOH D . 
N 6 HOH   76  276 156  HOH   HOH D . 
N 6 HOH   77  277 945  HOH   HOH D . 
N 6 HOH   78  278 108  HOH   HOH D . 
N 6 HOH   79  279 20   HOH   HOH D . 
N 6 HOH   80  280 95   HOH   HOH D . 
N 6 HOH   81  281 191  HOH   HOH D . 
N 6 HOH   82  282 297  HOH   HOH D . 
N 6 HOH   83  283 8    HOH   HOH D . 
N 6 HOH   84  284 888  HOH   HOH D . 
N 6 HOH   85  285 134  HOH   HOH D . 
N 6 HOH   86  286 649  HOH   HOH D . 
N 6 HOH   87  287 748  HOH   HOH D . 
N 6 HOH   88  288 287  HOH   HOH D . 
N 6 HOH   89  289 359  HOH   HOH D . 
N 6 HOH   90  290 9    HOH   HOH D . 
N 6 HOH   91  291 862  HOH   HOH D . 
N 6 HOH   92  292 204  HOH   HOH D . 
N 6 HOH   93  293 89   HOH   HOH D . 
N 6 HOH   94  294 68   HOH   HOH D . 
N 6 HOH   95  295 1071 HOH   HOH D . 
N 6 HOH   96  296 72   HOH   HOH D . 
N 6 HOH   97  297 882  HOH   HOH D . 
N 6 HOH   98  298 105  HOH   HOH D . 
N 6 HOH   99  299 813  HOH   HOH D . 
N 6 HOH   100 300 288  HOH   HOH D . 
N 6 HOH   101 301 780  HOH   HOH D . 
N 6 HOH   102 302 246  HOH   HOH D . 
N 6 HOH   103 303 304  HOH   HOH D . 
N 6 HOH   104 304 5    HOH   HOH D . 
N 6 HOH   105 305 323  HOH   HOH D . 
N 6 HOH   106 306 451  HOH   HOH D . 
N 6 HOH   107 307 656  HOH   HOH D . 
N 6 HOH   108 308 423  HOH   HOH D . 
N 6 HOH   109 309 450  HOH   HOH D . 
N 6 HOH   110 310 606  HOH   HOH D . 
N 6 HOH   111 311 256  HOH   HOH D . 
N 6 HOH   112 312 377  HOH   HOH D . 
N 6 HOH   113 313 59   HOH   HOH D . 
N 6 HOH   114 314 833  HOH   HOH D . 
N 6 HOH   115 315 31   HOH   HOH D . 
N 6 HOH   116 316 328  HOH   HOH D . 
N 6 HOH   117 317 476  HOH   HOH D . 
N 6 HOH   118 318 104  HOH   HOH D . 
N 6 HOH   119 319 810  HOH   HOH D . 
N 6 HOH   120 320 418  HOH   HOH D . 
N 6 HOH   121 321 292  HOH   HOH D . 
N 6 HOH   122 322 140  HOH   HOH D . 
N 6 HOH   123 323 279  HOH   HOH D . 
N 6 HOH   124 324 230  HOH   HOH D . 
N 6 HOH   125 325 209  HOH   HOH D . 
N 6 HOH   126 326 44   HOH   HOH D . 
N 6 HOH   127 327 503  HOH   HOH D . 
N 6 HOH   128 328 183  HOH   HOH D . 
N 6 HOH   129 329 1060 HOH   HOH D . 
N 6 HOH   130 330 139  HOH   HOH D . 
N 6 HOH   131 331 67   HOH   HOH D . 
N 6 HOH   132 332 537  HOH   HOH D . 
N 6 HOH   133 333 940  HOH   HOH D . 
N 6 HOH   134 334 208  HOH   HOH D . 
N 6 HOH   135 335 668  HOH   HOH D . 
N 6 HOH   136 336 446  HOH   HOH D . 
N 6 HOH   137 337 361  HOH   HOH D . 
N 6 HOH   138 338 28   HOH   HOH D . 
N 6 HOH   139 339 390  HOH   HOH D . 
N 6 HOH   140 340 867  HOH   HOH D . 
N 6 HOH   141 341 575  HOH   HOH D . 
N 6 HOH   142 342 488  HOH   HOH D . 
N 6 HOH   143 343 773  HOH   HOH D . 
N 6 HOH   144 344 310  HOH   HOH D . 
N 6 HOH   145 345 185  HOH   HOH D . 
N 6 HOH   146 346 859  HOH   HOH D . 
N 6 HOH   147 347 415  HOH   HOH D . 
N 6 HOH   148 348 597  HOH   HOH D . 
N 6 HOH   149 349 117  HOH   HOH D . 
N 6 HOH   150 350 273  HOH   HOH D . 
N 6 HOH   151 351 1062 HOH   HOH D . 
N 6 HOH   152 352 884  HOH   HOH D . 
N 6 HOH   153 353 1024 HOH   HOH D . 
N 6 HOH   154 354 302  HOH   HOH D . 
N 6 HOH   155 355 878  HOH   HOH D . 
N 6 HOH   156 356 85   HOH   HOH D . 
N 6 HOH   157 357 305  HOH   HOH D . 
N 6 HOH   158 358 93   HOH   HOH D . 
N 6 HOH   159 359 664  HOH   HOH D . 
N 6 HOH   160 360 825  HOH   HOH D . 
N 6 HOH   161 361 932  HOH   HOH D . 
N 6 HOH   162 362 856  HOH   HOH D . 
N 6 HOH   163 363 592  HOH   HOH D . 
N 6 HOH   164 364 682  HOH   HOH D . 
N 6 HOH   165 365 600  HOH   HOH D . 
N 6 HOH   166 366 1063 HOH   HOH D . 
N 6 HOH   167 367 947  HOH   HOH D . 
N 6 HOH   168 368 560  HOH   HOH D . 
N 6 HOH   169 369 864  HOH   HOH D . 
N 6 HOH   170 370 578  HOH   HOH D . 
N 6 HOH   171 371 1016 HOH   HOH D . 
N 6 HOH   172 372 803  HOH   HOH D . 
N 6 HOH   173 373 233  HOH   HOH D . 
N 6 HOH   174 374 885  HOH   HOH D . 
N 6 HOH   175 375 340  HOH   HOH D . 
N 6 HOH   176 376 483  HOH   HOH D . 
N 6 HOH   177 377 1029 HOH   HOH D . 
N 6 HOH   178 378 358  HOH   HOH D . 
N 6 HOH   179 379 903  HOH   HOH D . 
N 6 HOH   180 380 928  HOH   HOH D . 
N 6 HOH   181 381 520  HOH   HOH D . 
N 6 HOH   182 382 1027 HOH   HOH D . 
N 6 HOH   183 383 70   HOH   HOH D . 
N 6 HOH   184 384 964  HOH   HOH D . 
N 6 HOH   185 385 432  HOH   HOH D . 
N 6 HOH   186 386 987  HOH   HOH D . 
N 6 HOH   187 387 775  HOH   HOH D . 
N 6 HOH   188 388 576  HOH   HOH D . 
N 6 HOH   189 389 582  HOH   HOH D . 
N 6 HOH   190 390 844  HOH   HOH D . 
N 6 HOH   191 391 473  HOH   HOH D . 
N 6 HOH   192 392 898  HOH   HOH D . 
N 6 HOH   193 393 58   HOH   HOH D . 
N 6 HOH   194 394 617  HOH   HOH D . 
N 6 HOH   195 395 1023 HOH   HOH D . 
N 6 HOH   196 396 951  HOH   HOH D . 
N 6 HOH   197 397 544  HOH   HOH D . 
N 6 HOH   198 398 345  HOH   HOH D . 
N 6 HOH   199 399 853  HOH   HOH D . 
N 6 HOH   200 400 407  HOH   HOH D . 
N 6 HOH   201 401 608  HOH   HOH D . 
N 6 HOH   202 402 676  HOH   HOH D . 
N 6 HOH   203 403 675  HOH   HOH D . 
N 6 HOH   204 404 865  HOH   HOH D . 
N 6 HOH   205 405 274  HOH   HOH D . 
N 6 HOH   206 406 467  HOH   HOH D . 
N 6 HOH   207 407 926  HOH   HOH D . 
N 6 HOH   208 408 919  HOH   HOH D . 
N 6 HOH   209 409 917  HOH   HOH D . 
N 6 HOH   210 410 1040 HOH   HOH D . 
N 6 HOH   211 411 661  HOH   HOH D . 
N 6 HOH   212 412 999  HOH   HOH D . 
N 6 HOH   213 413 589  HOH   HOH D . 
N 6 HOH   214 414 427  HOH   HOH D . 
N 6 HOH   215 415 294  HOH   HOH D . 
N 6 HOH   216 416 776  HOH   HOH D . 
N 6 HOH   217 417 820  HOH   HOH D . 
N 6 HOH   218 418 579  HOH   HOH D . 
N 6 HOH   219 419 980  HOH   HOH D . 
N 6 HOH   220 420 596  HOH   HOH D . 
N 6 HOH   221 421 1022 HOH   HOH D . 
N 6 HOH   222 422 439  HOH   HOH D . 
N 6 HOH   223 423 841  HOH   HOH D . 
N 6 HOH   224 424 547  HOH   HOH D . 
N 6 HOH   225 425 857  HOH   HOH D . 
N 6 HOH   226 426 750  HOH   HOH D . 
N 6 HOH   227 427 712  HOH   HOH D . 
N 6 HOH   228 428 710  HOH   HOH D . 
N 6 HOH   229 429 554  HOH   HOH D . 
N 6 HOH   230 430 443  HOH   HOH D . 
N 6 HOH   231 431 613  HOH   HOH D . 
N 6 HOH   232 432 735  HOH   HOH D . 
N 6 HOH   233 433 381  HOH   HOH D . 
N 6 HOH   234 434 837  HOH   HOH D . 
N 6 HOH   235 435 871  HOH   HOH D . 
N 6 HOH   236 436 955  HOH   HOH D . 
N 6 HOH   237 437 954  HOH   HOH D . 
N 6 HOH   238 438 720  HOH   HOH D . 
N 6 HOH   239 439 1061 HOH   HOH D . 
N 6 HOH   240 440 419  HOH   HOH D . 
N 6 HOH   241 441 203  HOH   HOH D . 
N 6 HOH   242 442 619  HOH   HOH D . 
N 6 HOH   243 443 567  HOH   HOH D . 
N 6 HOH   244 444 82   HOH   HOH D . 
N 6 HOH   245 445 540  HOH   HOH D . 
N 6 HOH   246 446 245  HOH   HOH D . 
N 6 HOH   247 447 990  HOH   HOH D . 
N 6 HOH   248 448 978  HOH   HOH D . 
N 6 HOH   249 449 379  HOH   HOH D . 
N 6 HOH   250 450 368  HOH   HOH D . 
N 6 HOH   251 451 1064 HOH   HOH D . 
N 6 HOH   252 452 738  HOH   HOH D . 
N 6 HOH   253 453 1012 HOH   HOH D . 
N 6 HOH   254 454 1028 HOH   HOH D . 
N 6 HOH   255 455 724  HOH   HOH D . 
N 6 HOH   256 456 398  HOH   HOH D . 
N 6 HOH   257 457 692  HOH   HOH D . 
N 6 HOH   258 458 637  HOH   HOH D . 
N 6 HOH   259 459 838  HOH   HOH D . 
N 6 HOH   260 460 790  HOH   HOH D . 
N 6 HOH   261 461 552  HOH   HOH D . 
N 6 HOH   262 462 843  HOH   HOH D . 
N 6 HOH   263 463 918  HOH   HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.880 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BFZ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.894 
_cell.length_a_esd                 ? 
_cell.length_b                     48.168 
_cell.length_b_esd                 ? 
_cell.length_c                     102.112 
_cell.length_c_esd                 ? 
_cell.volume                       328266.073 
_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                         9BFZ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            'P 2y' 
_symmetry.space_group_name_H-M             'P 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BFZ 
_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             2.20 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.17 
_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         2019-03-25 
_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   .97946 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRL BEAMLINE BL9-2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        .97946 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL9-2 
_diffrn_source.pdbx_synchrotron_site       SSRL 
# 
_reflns.B_iso_Wilson_estimate                          12.90 
_reflns.entry_id                                       9BFZ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               39.23 
_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                                     59688 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.6 
_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                                .165 
_reflns.pdbx_Rpim_I_all                                .089 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .975 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              .138 
_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                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3403 
_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                               3.2 
_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                               .885 
_reflns_shell.pdbx_Rpim_I_all                               .485 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .743 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          96.2 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  .734 
_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                               16.77 
_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                                 9BFZ 
_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                            1.80 
_refine.ls_d_res_low                             39.23 
_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                     59521 
_refine.ls_number_reflns_R_free                  3049 
_refine.ls_number_reflns_R_work                  56472 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.26 
_refine.ls_percent_reflns_R_free                 5.12 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1831 
_refine.ls_R_factor_R_free                       0.2221 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1809 
_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                          1.34 
_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                 23.6903 
_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                            0.2305 
_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                       1.80 
_refine_hist.d_res_low                        39.23 
_refine_hist.number_atoms_solvent             1032 
_refine_hist.number_atoms_total               6462 
_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        5232 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         198 
_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' ? 0.0068  ? 5545 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8876  ? 7489 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0547  ? 796  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0075  ? 967  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.6835 ? 2072 ? 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' 1.80 1.83  . . 144 2450 94.88 . . . . 0.2717 . . . . . . . . . . . 0.3159 
'X-RAY DIFFRACTION' 1.83 1.86  . . 126 2589 99.34 . . . . 0.2434 . . . . . . . . . . . 0.3165 
'X-RAY DIFFRACTION' 1.86 1.89  . . 129 2528 98.92 . . . . 0.2496 . . . . . . . . . . . 0.2890 
'X-RAY DIFFRACTION' 1.89 1.92  . . 124 2568 97.01 . . . . 0.2648 . . . . . . . . . . . 0.3271 
'X-RAY DIFFRACTION' 1.92 1.96  . . 150 2538 98.21 . . . . 0.2247 . . . . . . . . . . . 0.2720 
'X-RAY DIFFRACTION' 1.96 2.00  . . 139 2567 98.54 . . . . 0.2028 . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 2.00 2.05  . . 128 2513 98.62 . . . . 0.2053 . . . . . . . . . . . 0.2622 
'X-RAY DIFFRACTION' 2.05 2.09  . . 137 2559 96.60 . . . . 0.2288 . . . . . . . . . . . 0.2643 
'X-RAY DIFFRACTION' 2.09 2.15  . . 150 2485 97.92 . . . . 0.1954 . . . . . . . . . . . 0.2733 
'X-RAY DIFFRACTION' 2.15 2.20  . . 146 2525 97.13 . . . . 0.1921 . . . . . . . . . . . 0.2513 
'X-RAY DIFFRACTION' 2.20 2.27  . . 155 2526 98.24 . . . . 0.2034 . . . . . . . . . . . 0.2766 
'X-RAY DIFFRACTION' 2.27 2.34  . . 120 2612 99.02 . . . . 0.1758 . . . . . . . . . . . 0.1859 
'X-RAY DIFFRACTION' 2.34 2.42  . . 108 2622 99.13 . . . . 0.1743 . . . . . . . . . . . 0.2453 
'X-RAY DIFFRACTION' 2.42 2.52  . . 115 2588 99.16 . . . . 0.1823 . . . . . . . . . . . 0.2244 
'X-RAY DIFFRACTION' 2.52 2.64  . . 143 2559 98.51 . . . . 0.1887 . . . . . . . . . . . 0.2159 
'X-RAY DIFFRACTION' 2.64 2.78  . . 131 2583 98.23 . . . . 0.1985 . . . . . . . . . . . 0.2770 
'X-RAY DIFFRACTION' 2.78 2.95  . . 127 2600 98.31 . . . . 0.1832 . . . . . . . . . . . 0.2377 
'X-RAY DIFFRACTION' 2.95 3.18  . . 158 2591 99.42 . . . . 0.1672 . . . . . . . . . . . 0.2208 
'X-RAY DIFFRACTION' 3.18 3.50  . . 135 2597 99.24 . . . . 0.1486 . . . . . . . . . . . 0.1849 
'X-RAY DIFFRACTION' 3.50 4.00  . . 143 2591 97.96 . . . . 0.1423 . . . . . . . . . . . 0.1700 
'X-RAY DIFFRACTION' 4.00 5.04  . . 164 2606 99.00 . . . . 0.1274 . . . . . . . . . . . 0.1601 
'X-RAY DIFFRACTION' 5.04 39.23 . . 177 2675 98.48 . . . . 0.1601 . . . . . . . . . . . 0.1644 
# 
_struct.entry_id                     9BFZ 
_struct.title                        'Tri-complex of Compound-5, 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        9BFZ 
_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 9BFZ B 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 1 9BFZ A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
3 2 9BFZ C 2 ? 166 ? P62937 1 ? 165 ? 1 165 
4 2 9BFZ D 2 ? 166 ? P62937 1 ? 165 ? 1 165 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BFZ SER B 1   ? UNP P01116 ?   ?   'expression tag'      0   1  
1 9BFZ CYS B 13  ? UNP P01116 GLY 12  'engineered mutation' 12  2  
1 9BFZ SER B 52  ? UNP P01116 CYS 51  conflict              51  3  
1 9BFZ LEU B 81  ? UNP P01116 CYS 80  conflict              80  4  
1 9BFZ SER B 119 ? UNP P01116 CYS 118 conflict              118 5  
2 9BFZ SER A 1   ? UNP P01116 ?   ?   'expression tag'      0   6  
2 9BFZ CYS A 13  ? UNP P01116 GLY 12  'engineered mutation' 12  7  
2 9BFZ SER A 52  ? UNP P01116 CYS 51  conflict              51  8  
2 9BFZ LEU A 81  ? UNP P01116 CYS 80  conflict              80  9  
2 9BFZ SER A 119 ? UNP P01116 CYS 118 conflict              118 10 
3 9BFZ SER C 1   ? UNP P62937 ?   ?   'expression tag'      0   11 
3 9BFZ SER C 53  ? UNP P62937 CYS 52  conflict              52  12 
4 9BFZ SER D 1   ? UNP P62937 ?   ?   'expression tag'      0   13 
4 9BFZ SER D 53  ? UNP P62937 CYS 52  conflict              52  14 
# 
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_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 B 15  ASN B 26  1 ? 12 
HELX_P HELX_P2  AA2 TYR A 65  ? GLY A 76  ? TYR B 64  GLY B 75  1 ? 12 
HELX_P HELX_P3  AA3 ASN A 87  ? ASP A 93  ? ASN B 86  ASP B 92  1 ? 7  
HELX_P HELX_P4  AA4 ASP A 93  ? ASP A 106 ? ASP B 92  ASP B 105 1 ? 14 
HELX_P HELX_P5  AA5 ASP A 127 ? GLY A 139 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P6  AA6 GLY A 152 ? LYS A 170 ? GLY B 151 LYS B 169 1 ? 19 
HELX_P HELX_P7  AA7 GLY B 16  ? ASN B 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P8  AA8 TYR B 65  ? GLY B 76  ? TYR A 64  GLY A 75  1 ? 12 
HELX_P HELX_P9  AA9 ASN B 87  ? ASP B 93  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P10 AB1 ASP B 93  ? ASP B 106 ? ASP A 92  ASP A 105 1 ? 14 
HELX_P HELX_P11 AB2 ASP B 127 ? GLY B 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P12 AB3 GLY B 152 ? GLU B 169 ? GLY A 151 GLU A 168 1 ? 18 
HELX_P HELX_P13 AB4 VAL C 30  ? GLY C 43  ? VAL C 29  GLY C 42  1 ? 14 
HELX_P HELX_P14 AB5 THR C 120 ? ASP C 124 ? THR C 119 ASP C 123 5 ? 5  
HELX_P HELX_P15 AB6 GLY C 136 ? PHE C 146 ? GLY C 135 PHE C 145 1 ? 11 
HELX_P HELX_P16 AB7 VAL D 30  ? GLY D 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P17 AB8 THR D 120 ? ASP D 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P18 AB9 GLY D 136 ? ARG D 145 ? GLY D 135 ARG D 144 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale none ? A CYS 13 SG  ? ? ? 1_555 G A1AOK . C51 ? ? B CYS 12  B A1AOK 203 1_555 ? ? ? ? ? ? ? 1.681 ? ? 
covale2  covale none ? B CYS 13 SG  ? ? ? 1_555 J A1AOK . C51 A ? A CYS 12  A A1AOK 203 1_555 ? ? ? ? ? ? ? 1.679 ? ? 
metalc1  metalc ?    ? A SER 18 OG  ? ? ? 1_555 F MG    . MG  ? ? B SER 17  B MG    202 1_555 ? ? ? ? ? ? ? 2.077 ? ? 
metalc2  metalc ?    ? A THR 36 OG1 ? ? ? 1_555 F MG    . MG  ? ? B THR 35  B MG    202 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc3  metalc ?    ? E GNP .  O1G ? ? ? 1_555 F MG    . MG  ? ? B GNP 201 B MG    202 1_555 ? ? ? ? ? ? ? 2.042 ? ? 
metalc4  metalc ?    ? E GNP .  O2B ? ? ? 1_555 F MG    . MG  ? ? B GNP 201 B MG    202 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc5  metalc ?    ? F MG  .  MG  ? ? ? 1_555 K HOH   . O   ? ? B MG  202 B HOH   309 1_555 ? ? ? ? ? ? ? 2.162 ? ? 
metalc6  metalc ?    ? F MG  .  MG  ? ? ? 1_555 K HOH   . O   ? ? B MG  202 B HOH   343 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
metalc7  metalc ?    ? B SER 18 OG  ? ? ? 1_555 I MG    . MG  ? ? A SER 17  A MG    202 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
metalc8  metalc ?    ? B THR 36 OG1 ? ? ? 1_555 I MG    . MG  ? ? A THR 35  A MG    202 1_555 ? ? ? ? ? ? ? 1.902 ? ? 
metalc9  metalc ?    ? H GNP .  O1G ? ? ? 1_555 I MG    . MG  ? ? A GNP 201 A MG    202 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
metalc10 metalc ?    ? H GNP .  O2B ? ? ? 1_555 I MG    . MG  ? ? A GNP 201 A MG    202 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc11 metalc ?    ? I MG  .  MG  ? ? ? 1_555 L HOH   . O   ? ? A MG  202 A HOH   319 1_555 ? ? ? ? ? ? ? 2.188 ? ? 
metalc12 metalc ?    ? I MG  .  MG  ? ? ? 1_555 L HOH   . O   ? ? A MG  202 A HOH   321 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
# 
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 ? B SER 17  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 OG1 ? A THR 36 ? B THR 35  ? 1_555 78.4  ? 
2  OG  ? A SER 18 ? B SER 17  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O1G ? E GNP .  ? B GNP 201 ? 1_555 166.4 ? 
3  OG1 ? A THR 36 ? B THR 35  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O1G ? E GNP .  ? B GNP 201 ? 1_555 89.9  ? 
4  OG  ? A SER 18 ? B SER 17  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O2B ? E GNP .  ? B GNP 201 ? 1_555 98.1  ? 
5  OG1 ? A THR 36 ? B THR 35  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O2B ? E GNP .  ? B GNP 201 ? 1_555 174.4 ? 
6  O1G ? E GNP .  ? B GNP 201 ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O2B ? E GNP .  ? B GNP 201 ? 1_555 94.0  ? 
7  OG  ? A SER 18 ? B SER 17  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 309 ? 1_555 84.7  ? 
8  OG1 ? A THR 36 ? B THR 35  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 309 ? 1_555 88.3  ? 
9  O1G ? E GNP .  ? B GNP 201 ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 309 ? 1_555 88.1  ? 
10 O2B ? E GNP .  ? B GNP 201 ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 309 ? 1_555 95.8  ? 
11 OG  ? A SER 18 ? B SER 17  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 343 ? 1_555 91.7  ? 
12 OG1 ? A THR 36 ? B THR 35  ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 343 ? 1_555 86.4  ? 
13 O1G ? E GNP .  ? B GNP 201 ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 343 ? 1_555 94.4  ? 
14 O2B ? E GNP .  ? B GNP 201 ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 343 ? 1_555 89.3  ? 
15 O   ? K HOH .  ? B HOH 309 ? 1_555 MG ? F MG . ? B MG 202 ? 1_555 O   ? K HOH .  ? B HOH 343 ? 1_555 174.1 ? 
16 OG  ? B SER 18 ? A SER 17  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 OG1 ? B THR 36 ? A THR 35  ? 1_555 84.3  ? 
17 OG  ? B SER 18 ? A SER 17  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O1G ? H GNP .  ? A GNP 201 ? 1_555 170.5 ? 
18 OG1 ? B THR 36 ? A THR 35  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O1G ? H GNP .  ? A GNP 201 ? 1_555 93.7  ? 
19 OG  ? B SER 18 ? A SER 17  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O2B ? H GNP .  ? A GNP 201 ? 1_555 94.4  ? 
20 OG1 ? B THR 36 ? A THR 35  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O2B ? H GNP .  ? A GNP 201 ? 1_555 178.6 ? 
21 O1G ? H GNP .  ? A GNP 201 ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O2B ? H GNP .  ? A GNP 201 ? 1_555 87.6  ? 
22 OG  ? B SER 18 ? A SER 17  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 319 ? 1_555 82.0  ? 
23 OG1 ? B THR 36 ? A THR 35  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 319 ? 1_555 94.2  ? 
24 O1G ? H GNP .  ? A GNP 201 ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 319 ? 1_555 88.9  ? 
25 O2B ? H GNP .  ? A GNP 201 ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 319 ? 1_555 85.9  ? 
26 OG  ? B SER 18 ? A SER 17  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 321 ? 1_555 95.3  ? 
27 OG1 ? B THR 36 ? A THR 35  ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 321 ? 1_555 96.6  ? 
28 O1G ? H GNP .  ? A GNP 201 ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 321 ? 1_555 94.1  ? 
29 O2B ? H GNP .  ? A GNP 201 ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 321 ? 1_555 83.2  ? 
30 O   ? L HOH .  ? A HOH 319 ? 1_555 MG ? I MG . ? A MG 202 ? 1_555 O   ? L HOH .  ? A HOH 321 ? 1_555 168.6 ? 
# 
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 A1AOK G . ? CYS A 13 ? A1AOK B 203 ? 1_555 CYS B 12 ? 1_555 C51 SG CYS 1 A1AOK None 'Covalent chemical modification' 
2 A1AOK J . A CYS B 13 ? A1AOK A 203 ? 1_555 CYS A 12 ? 1_555 C51 SG CYS 1 A1AOK 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 B 37  ILE B 46  
AA1 2 GLU A 50  ? THR A 59  ? GLU B 49  THR B 58  
AA1 3 THR A 3   ? VAL A 10  ? THR B 2   VAL B 9   
AA1 4 GLY A 78  ? ALA A 84  ? GLY B 77  ALA B 83  
AA1 5 MET A 112 ? ASN A 117 ? MET B 111 ASN B 116 
AA1 6 PHE A 142 ? GLU A 144 ? PHE B 141 GLU B 143 
AA2 1 GLU B 38  ? ILE B 47  ? GLU A 37  ILE A 46  
AA2 2 GLU B 50  ? THR B 59  ? GLU A 49  THR A 58  
AA2 3 MET B 2   ? VAL B 10  ? MET A 1   VAL A 9   
AA2 4 GLY B 78  ? ALA B 84  ? GLY A 77  ALA A 83  
AA2 5 MET B 112 ? ASN B 117 ? MET A 111 ASN A 116 
AA2 6 PHE B 142 ? GLU B 144 ? PHE A 141 GLU A 143 
AA3 1 ARG C 56  ? ILE C 58  ? ARG C 55  ILE C 57  
AA3 2 MET C 62  ? GLY C 65  ? MET C 61  GLY C 64  
AA3 3 PHE C 113 ? CYS C 116 ? PHE C 112 CYS C 115 
AA3 4 ILE C 98  ? MET C 101 ? ILE C 97  MET C 100 
AA3 5 VAL C 129 ? VAL C 133 ? VAL C 128 VAL C 132 
AA3 6 GLU C 16  ? LEU C 25  ? GLU C 15  LEU C 24  
AA3 7 THR C 6   ? VAL C 13  ? THR C 5   VAL C 12  
AA3 8 ILE C 157 ? LEU C 165 ? ILE C 156 LEU C 164 
AA4 1 ARG D 56  ? ILE D 58  ? ARG D 55  ILE D 57  
AA4 2 MET D 62  ? GLY D 65  ? MET D 61  GLY D 64  
AA4 3 PHE D 113 ? CYS D 116 ? PHE D 112 CYS D 115 
AA4 4 ILE D 98  ? MET D 101 ? ILE D 97  MET D 100 
AA4 5 VAL D 129 ? VAL D 133 ? VAL D 128 VAL D 132 
AA4 6 GLU D 16  ? LEU D 25  ? GLU D 15  LEU D 24  
AA4 7 THR D 6   ? VAL D 13  ? THR D 5   VAL D 12  
AA4 8 ILE D 157 ? LEU D 165 ? ILE D 156 LEU D 164 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 45  ? N VAL B 44  O SER A 52  ? O SER B 51  
AA1 2 3 O ASP A 55  ? O ASP B 54  N TYR A 5   ? N TYR B 4   
AA1 3 4 N VAL A 10  ? N VAL B 9   O LEU A 80  ? O LEU B 79  
AA1 4 5 N LEU A 81  ? N LEU B 80  O VAL A 115 ? O VAL B 114 
AA1 5 6 N LEU A 114 ? N LEU B 113 O ILE A 143 ? O ILE B 142 
AA2 1 2 N LYS B 43  ? N LYS A 42  O LEU B 54  ? O LEU A 53  
AA2 2 3 O ASP B 55  ? O ASP A 54  N TYR B 5   ? N TYR A 4   
AA2 3 4 N VAL B 10  ? N VAL A 9   O VAL B 82  ? O VAL A 81  
AA2 4 5 N PHE B 83  ? N PHE A 82  O ASN B 117 ? O ASN A 116 
AA2 5 6 N LEU B 114 ? N LEU A 113 O ILE B 143 ? O ILE A 142 
AA3 1 2 N ARG C 56  ? N ARG C 55  O GLN C 64  ? O GLN C 63  
AA3 2 3 N CYS C 63  ? N CYS C 62  O ILE C 115 ? O ILE C 114 
AA3 3 4 O CYS C 116 ? O CYS C 115 N ILE C 98  ? N ILE C 97  
AA3 4 5 N LEU C 99  ? N LEU C 98  O GLY C 131 ? O GLY C 130 
AA3 5 6 O LYS C 132 ? O LYS C 131 N GLU C 24  ? N GLU C 23  
AA3 6 7 O LEU C 18  ? O LEU C 17  N ILE C 11  ? N ILE C 10  
AA3 7 8 N ASP C 10  ? N ASP C 9   O ASP C 161 ? O ASP C 160 
AA4 1 2 N ARG D 56  ? N ARG D 55  O GLN D 64  ? O GLN D 63  
AA4 2 3 N CYS D 63  ? N CYS D 62  O ILE D 115 ? O ILE D 114 
AA4 3 4 O CYS D 116 ? O CYS D 115 N ILE D 98  ? N ILE D 97  
AA4 4 5 N LEU D 99  ? N LEU D 98  O GLY D 131 ? O GLY D 130 
AA4 5 6 O LYS D 132 ? O LYS D 131 N GLU D 24  ? N GLU D 23  
AA4 6 7 O LEU D 18  ? O LEU D 17  N ILE D 11  ? N ILE D 10  
AA4 7 8 N ASP D 10  ? N ASP D 9   O ASP D 161 ? O ASP D 160 
# 
_pdbx_entry_details.entry_id                   9BFZ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 B 36  ? ? -96.31  -62.96 
2  1 ARG B 149 ? ? 75.30   -0.47  
3  1 ILE A 36  ? ? -95.38  -64.41 
4  1 LYS A 117 ? ? 70.60   32.75  
5  1 PHE C 60  ? ? -129.13 -67.80 
6  1 ASN C 71  ? ? -144.87 11.05  
7  1 LYS C 133 ? ? -102.03 -67.71 
8  1 PHE D 60  ? ? -134.03 -70.24 
9  1 ASN D 71  ? ? -146.92 16.21  
10 1 LYS D 133 ? ? -101.95 -72.33 
# 
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 N2 ? B A1AOK 203 ? PLANAR . 
2 1 N2 A A A1AOK 203 ? PLANAR . 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     525 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   K 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z   
2 -x,y,-z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 52.9307850033 -21.8848118267 -8.97282688885 0.0630085638409 ? -0.0127604474195 ? 0.0018893803973   
? 0.0897109457803 ? 0.00800059484093 ? 0.0787243380019 ? 1.6936524761  ? 0.631383015861  ? 0.066417996872  ? 1.99461295835 ? 
-0.126375200448 ? 1.39866202093 ? -0.0879708830742 ? 0.107241967669   ? 0.0349983986865  ? -0.052150815058  ? 0.100912692639    ? 
0.0909243745508 ? -0.0138563126323 ? -0.0528700097534 ? -0.00296608117   ? 
2 'X-RAY DIFFRACTION' ? refined 83.0207591644 -28.4522258996 59.9703371916  0.0706080029894 ? 0.00329962614357 ? -0.00991347726858 
? 0.0653840187116 ? 0.0019284516318  ? 0.0985397335765 ? 1.67109357965 ? -0.651378866557 ? -0.124804401104 ? 1.54447128946 ? 
-0.229869062645 ? 1.60493379897 ? -0.0883888874178 ? -0.0486167295474 ? -0.0723250201398 ? 0.0832489651368  ? 0.058020933601    ? 
0.021457635393  ? 0.0162382172248  ? 0.00483357950867 ? 0.0232170894427  ? 
3 'X-RAY DIFFRACTION' ? refined 46.8091632466 -44.908373956  15.0277332123  0.0619665623285 ? 0.00388954098372 ? 0.0065410381451   
? 0.066246803542  ? 0.0171043637442  ? 0.0815406994    ? 1.53394184975 ? -0.165303654008 ? 0.0674439613558 ? 1.80943624958 ? 
0.151447471182  ? 1.51929727324 ? -0.0333363852658 ? -0.0695642229198 ? -0.0799829266972 ? 0.118850560191   ? 0.0326506510095   ? 
0.0420919813808 ? 0.0274569863761  ? -0.0642522127796 ? 0.00216229347586 ? 
4 'X-RAY DIFFRACTION' ? refined 76.8137211981 -5.7221125696  35.8058146739  0.0547084175771 ? 0.00228502341753 ? -0.0031809741318  
? 0.0623620850037 ? 0.00577290836476 ? 0.083303939471  ? 1.66995765993 ? 0.376449308877  ? 0.398457027195  ? 1.36700257469 ? 
-0.132773087934 ? 1.57063001478 ? -0.0172688419516 ? 0.0370238850952  ? 0.0337127572541  ? -0.0223662752596 ? -0.00853997772755 ? 
-0.082304168137 ? 0.0104896422894  ? 0.0316932879353  ? 0.0220905356873  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1 B 0 ? B ?   B 170 ? ? 
;(chain 'B' and resid 0 through 170)
;
2 'X-RAY DIFFRACTION' 2 D 1 A 0 ? E ?   A 170 ? ? 
;(chain 'A' and resid 0 through 170)
;
3 'X-RAY DIFFRACTION' 3 G 1 C 2 ? G 164 C 165 ? ? 
;(chain 'C' and resid 2 through 165)
;
4 'X-RAY DIFFRACTION' 4 I 1 D 0 ? I 165 D 164 ? ? 
;(chain 'D' and resid 0 through 164)
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      C 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       445 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.38 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A LYS 169 ? B LYS 170 
2 1 Y 1 C SER 0   ? C SER 1   
3 1 Y 1 C MET 1   ? C MET 2   
4 1 Y 1 D GLU 165 ? D GLU 166 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AOK C1     C  N N 1   
A1AOK C10    C  N N 2   
A1AOK C11    C  N N 3   
A1AOK C12    C  N N 4   
A1AOK C13    C  N N 5   
A1AOK C14    C  Y N 6   
A1AOK C15    C  Y N 7   
A1AOK C16    C  Y N 8   
A1AOK C17    C  Y N 9   
A1AOK C18    C  N N 10  
A1AOK C19    C  N N 11  
A1AOK C2     C  N S 12  
A1AOK C20    C  N N 13  
A1AOK C21    C  Y N 14  
A1AOK C22    C  Y N 15  
A1AOK C23    C  Y N 16  
A1AOK C24    C  Y N 17  
A1AOK C25    C  N N 18  
A1AOK C26    C  N N 19  
A1AOK C27    C  N N 20  
A1AOK C28    C  Y N 21  
A1AOK C29    C  Y N 22  
A1AOK C3     C  N N 23  
A1AOK C30    C  Y N 24  
A1AOK C31    C  Y N 25  
A1AOK C32    C  Y N 26  
A1AOK C33    C  Y N 27  
A1AOK C34    C  Y N 28  
A1AOK C35    C  Y N 29  
A1AOK C36    C  Y N 30  
A1AOK C37    C  Y N 31  
A1AOK C38    C  Y N 32  
A1AOK C39    C  Y N 33  
A1AOK C4     C  N N 34  
A1AOK C40    C  N S 35  
A1AOK C41    C  N N 36  
A1AOK C42    C  N N 37  
A1AOK C43    C  N N 38  
A1AOK C44    C  N N 39  
A1AOK C45    C  N N 40  
A1AOK C46    C  N S 41  
A1AOK C47    C  N N 42  
A1AOK C48    C  N N 43  
A1AOK C49    C  N N 44  
A1AOK C5     C  N N 45  
A1AOK C50    C  N N 46  
A1AOK C51    C  N N 47  
A1AOK C52    C  N N 48  
A1AOK C6     C  N N 49  
A1AOK C7     C  N S 50  
A1AOK C8     C  N N 51  
A1AOK C9     C  N N 52  
A1AOK N1     N  N N 53  
A1AOK N2     N  N S 54  
A1AOK N3     N  Y N 55  
A1AOK N4     N  N N 56  
A1AOK N5     N  N N 57  
A1AOK N6     N  N N 58  
A1AOK O1     O  N N 59  
A1AOK O2     O  N N 60  
A1AOK O3     O  N N 61  
A1AOK O4     O  N N 62  
A1AOK O5     O  N N 63  
A1AOK O6     O  N N 64  
A1AOK O7     O  N N 65  
A1AOK O8     O  N N 66  
A1AOK H14    H  N N 67  
A1AOK H12    H  N N 68  
A1AOK H13    H  N N 69  
A1AOK H17    H  N N 70  
A1AOK H15    H  N N 71  
A1AOK H16    H  N N 72  
A1AOK H19    H  N N 73  
A1AOK H18    H  N N 74  
A1AOK H20    H  N N 75  
A1AOK H21    H  N N 76  
A1AOK H22    H  N N 77  
A1AOK H23    H  N N 78  
A1AOK H2     H  N N 79  
A1AOK H26    H  N N 80  
A1AOK H25    H  N N 81  
A1AOK H24    H  N N 82  
A1AOK H27    H  N N 83  
A1AOK H28    H  N N 84  
A1AOK H29    H  N N 85  
A1AOK H30    H  N N 86  
A1AOK H31    H  N N 87  
A1AOK H32    H  N N 88  
A1AOK H33    H  N N 89  
A1AOK H35    H  N N 90  
A1AOK H34    H  N N 91  
A1AOK H38    H  N N 92  
A1AOK H37    H  N N 93  
A1AOK H39    H  N N 94  
A1AOK H40    H  N N 95  
A1AOK H41    H  N N 96  
A1AOK H42    H  N N 97  
A1AOK H43    H  N N 98  
A1AOK H45    H  N N 99  
A1AOK H4     H  N N 100 
A1AOK H3     H  N N 101 
A1AOK H46    H  N N 102 
A1AOK H47    H  N N 103 
A1AOK H48    H  N N 104 
A1AOK H49    H  N N 105 
A1AOK H50    H  N N 106 
A1AOK H51    H  N N 107 
A1AOK H53    H  N N 108 
A1AOK H52    H  N N 109 
A1AOK H56    H  N N 110 
A1AOK H55    H  N N 111 
A1AOK H54    H  N N 112 
A1AOK H57    H  N N 113 
A1AOK H59    H  N N 114 
A1AOK H58    H  N N 115 
A1AOK H61    H  N N 116 
A1AOK H60    H  N N 117 
A1AOK H6     H  N N 118 
A1AOK H5     H  N N 119 
A1AOK H63    H  N N 120 
A1AOK H62    H  N N 121 
A1AOK H66    H  N N 122 
A1AOK H65    H  N N 123 
A1AOK H64    H  N N 124 
A1AOK H67    H  N N 125 
A1AOK H68    H  N N 126 
A1AOK H8     H  N N 127 
A1AOK H7     H  N N 128 
A1AOK H9     H  N N 129 
A1AOK H10    H  N N 130 
A1AOK H11    H  N N 131 
A1AOK H1     H  N N 132 
A1AOK H36    H  N N 133 
A1AOK H44    H  N N 134 
ALA   N      N  N N 135 
ALA   CA     C  N S 136 
ALA   C      C  N N 137 
ALA   O      O  N N 138 
ALA   CB     C  N N 139 
ALA   OXT    O  N N 140 
ALA   H      H  N N 141 
ALA   H2     H  N N 142 
ALA   HA     H  N N 143 
ALA   HB1    H  N N 144 
ALA   HB2    H  N N 145 
ALA   HB3    H  N N 146 
ALA   HXT    H  N N 147 
ARG   N      N  N N 148 
ARG   CA     C  N S 149 
ARG   C      C  N N 150 
ARG   O      O  N N 151 
ARG   CB     C  N N 152 
ARG   CG     C  N N 153 
ARG   CD     C  N N 154 
ARG   NE     N  N N 155 
ARG   CZ     C  N N 156 
ARG   NH1    N  N N 157 
ARG   NH2    N  N N 158 
ARG   OXT    O  N N 159 
ARG   H      H  N N 160 
ARG   H2     H  N N 161 
ARG   HA     H  N N 162 
ARG   HB2    H  N N 163 
ARG   HB3    H  N N 164 
ARG   HG2    H  N N 165 
ARG   HG3    H  N N 166 
ARG   HD2    H  N N 167 
ARG   HD3    H  N N 168 
ARG   HE     H  N N 169 
ARG   HH11   H  N N 170 
ARG   HH12   H  N N 171 
ARG   HH21   H  N N 172 
ARG   HH22   H  N N 173 
ARG   HXT    H  N N 174 
ASN   N      N  N N 175 
ASN   CA     C  N S 176 
ASN   C      C  N N 177 
ASN   O      O  N N 178 
ASN   CB     C  N N 179 
ASN   CG     C  N N 180 
ASN   OD1    O  N N 181 
ASN   ND2    N  N N 182 
ASN   OXT    O  N N 183 
ASN   H      H  N N 184 
ASN   H2     H  N N 185 
ASN   HA     H  N N 186 
ASN   HB2    H  N N 187 
ASN   HB3    H  N N 188 
ASN   HD21   H  N N 189 
ASN   HD22   H  N N 190 
ASN   HXT    H  N N 191 
ASP   N      N  N N 192 
ASP   CA     C  N S 193 
ASP   C      C  N N 194 
ASP   O      O  N N 195 
ASP   CB     C  N N 196 
ASP   CG     C  N N 197 
ASP   OD1    O  N N 198 
ASP   OD2    O  N N 199 
ASP   OXT    O  N N 200 
ASP   H      H  N N 201 
ASP   H2     H  N N 202 
ASP   HA     H  N N 203 
ASP   HB2    H  N N 204 
ASP   HB3    H  N N 205 
ASP   HD2    H  N N 206 
ASP   HXT    H  N N 207 
CYS   N      N  N N 208 
CYS   CA     C  N R 209 
CYS   C      C  N N 210 
CYS   O      O  N N 211 
CYS   CB     C  N N 212 
CYS   SG     S  N N 213 
CYS   OXT    O  N N 214 
CYS   H      H  N N 215 
CYS   H2     H  N N 216 
CYS   HA     H  N N 217 
CYS   HB2    H  N N 218 
CYS   HB3    H  N N 219 
CYS   HG     H  N N 220 
CYS   HXT    H  N N 221 
GLN   N      N  N N 222 
GLN   CA     C  N S 223 
GLN   C      C  N N 224 
GLN   O      O  N N 225 
GLN   CB     C  N N 226 
GLN   CG     C  N N 227 
GLN   CD     C  N N 228 
GLN   OE1    O  N N 229 
GLN   NE2    N  N N 230 
GLN   OXT    O  N N 231 
GLN   H      H  N N 232 
GLN   H2     H  N N 233 
GLN   HA     H  N N 234 
GLN   HB2    H  N N 235 
GLN   HB3    H  N N 236 
GLN   HG2    H  N N 237 
GLN   HG3    H  N N 238 
GLN   HE21   H  N N 239 
GLN   HE22   H  N N 240 
GLN   HXT    H  N N 241 
GLU   N      N  N N 242 
GLU   CA     C  N S 243 
GLU   C      C  N N 244 
GLU   O      O  N N 245 
GLU   CB     C  N N 246 
GLU   CG     C  N N 247 
GLU   CD     C  N N 248 
GLU   OE1    O  N N 249 
GLU   OE2    O  N N 250 
GLU   OXT    O  N N 251 
GLU   H      H  N N 252 
GLU   H2     H  N N 253 
GLU   HA     H  N N 254 
GLU   HB2    H  N N 255 
GLU   HB3    H  N N 256 
GLU   HG2    H  N N 257 
GLU   HG3    H  N N 258 
GLU   HE2    H  N N 259 
GLU   HXT    H  N N 260 
GLY   N      N  N N 261 
GLY   CA     C  N N 262 
GLY   C      C  N N 263 
GLY   O      O  N N 264 
GLY   OXT    O  N N 265 
GLY   H      H  N N 266 
GLY   H2     H  N N 267 
GLY   HA2    H  N N 268 
GLY   HA3    H  N N 269 
GLY   HXT    H  N N 270 
GNP   PG     P  N N 271 
GNP   O1G    O  N N 272 
GNP   O2G    O  N N 273 
GNP   O3G    O  N N 274 
GNP   N3B    N  N N 275 
GNP   PB     P  N R 276 
GNP   O1B    O  N N 277 
GNP   O2B    O  N N 278 
GNP   O3A    O  N N 279 
GNP   PA     P  N S 280 
GNP   O1A    O  N N 281 
GNP   O2A    O  N N 282 
GNP   "O5'"  O  N N 283 
GNP   "C5'"  C  N N 284 
GNP   "C4'"  C  N R 285 
GNP   "O4'"  O  N N 286 
GNP   "C3'"  C  N S 287 
GNP   "O3'"  O  N N 288 
GNP   "C2'"  C  N R 289 
GNP   "O2'"  O  N N 290 
GNP   "C1'"  C  N R 291 
GNP   N9     N  Y N 292 
GNP   C8     C  Y N 293 
GNP   N7     N  Y N 294 
GNP   C5     C  Y N 295 
GNP   C6     C  Y N 296 
GNP   O6     O  N N 297 
GNP   N1     N  Y N 298 
GNP   C2     C  Y N 299 
GNP   N2     N  N N 300 
GNP   N3     N  Y N 301 
GNP   C4     C  Y N 302 
GNP   HOG2   H  N N 303 
GNP   HOG3   H  N N 304 
GNP   HNB3   H  N N 305 
GNP   HOB2   H  N N 306 
GNP   HOA2   H  N N 307 
GNP   "H5'2" H  N N 308 
GNP   "H5'1" H  N N 309 
GNP   "H4'"  H  N N 310 
GNP   "H3'"  H  N N 311 
GNP   "HO3'" H  N N 312 
GNP   "H2'"  H  N N 313 
GNP   "HO2'" H  N N 314 
GNP   "H1'"  H  N N 315 
GNP   H8     H  N N 316 
GNP   HN1    H  N N 317 
GNP   HN21   H  N N 318 
GNP   HN22   H  N N 319 
HIS   N      N  N N 320 
HIS   CA     C  N S 321 
HIS   C      C  N N 322 
HIS   O      O  N N 323 
HIS   CB     C  N N 324 
HIS   CG     C  Y N 325 
HIS   ND1    N  Y N 326 
HIS   CD2    C  Y N 327 
HIS   CE1    C  Y N 328 
HIS   NE2    N  Y N 329 
HIS   OXT    O  N N 330 
HIS   H      H  N N 331 
HIS   H2     H  N N 332 
HIS   HA     H  N N 333 
HIS   HB2    H  N N 334 
HIS   HB3    H  N N 335 
HIS   HD1    H  N N 336 
HIS   HD2    H  N N 337 
HIS   HE1    H  N N 338 
HIS   HE2    H  N N 339 
HIS   HXT    H  N N 340 
HOH   O      O  N N 341 
HOH   H1     H  N N 342 
HOH   H2     H  N N 343 
ILE   N      N  N N 344 
ILE   CA     C  N S 345 
ILE   C      C  N N 346 
ILE   O      O  N N 347 
ILE   CB     C  N S 348 
ILE   CG1    C  N N 349 
ILE   CG2    C  N N 350 
ILE   CD1    C  N N 351 
ILE   OXT    O  N N 352 
ILE   H      H  N N 353 
ILE   H2     H  N N 354 
ILE   HA     H  N N 355 
ILE   HB     H  N N 356 
ILE   HG12   H  N N 357 
ILE   HG13   H  N N 358 
ILE   HG21   H  N N 359 
ILE   HG22   H  N N 360 
ILE   HG23   H  N N 361 
ILE   HD11   H  N N 362 
ILE   HD12   H  N N 363 
ILE   HD13   H  N N 364 
ILE   HXT    H  N N 365 
LEU   N      N  N N 366 
LEU   CA     C  N S 367 
LEU   C      C  N N 368 
LEU   O      O  N N 369 
LEU   CB     C  N N 370 
LEU   CG     C  N N 371 
LEU   CD1    C  N N 372 
LEU   CD2    C  N N 373 
LEU   OXT    O  N N 374 
LEU   H      H  N N 375 
LEU   H2     H  N N 376 
LEU   HA     H  N N 377 
LEU   HB2    H  N N 378 
LEU   HB3    H  N N 379 
LEU   HG     H  N N 380 
LEU   HD11   H  N N 381 
LEU   HD12   H  N N 382 
LEU   HD13   H  N N 383 
LEU   HD21   H  N N 384 
LEU   HD22   H  N N 385 
LEU   HD23   H  N N 386 
LEU   HXT    H  N N 387 
LYS   N      N  N N 388 
LYS   CA     C  N S 389 
LYS   C      C  N N 390 
LYS   O      O  N N 391 
LYS   CB     C  N N 392 
LYS   CG     C  N N 393 
LYS   CD     C  N N 394 
LYS   CE     C  N N 395 
LYS   NZ     N  N N 396 
LYS   OXT    O  N N 397 
LYS   H      H  N N 398 
LYS   H2     H  N N 399 
LYS   HA     H  N N 400 
LYS   HB2    H  N N 401 
LYS   HB3    H  N N 402 
LYS   HG2    H  N N 403 
LYS   HG3    H  N N 404 
LYS   HD2    H  N N 405 
LYS   HD3    H  N N 406 
LYS   HE2    H  N N 407 
LYS   HE3    H  N N 408 
LYS   HZ1    H  N N 409 
LYS   HZ2    H  N N 410 
LYS   HZ3    H  N N 411 
LYS   HXT    H  N N 412 
MET   N      N  N N 413 
MET   CA     C  N S 414 
MET   C      C  N N 415 
MET   O      O  N N 416 
MET   CB     C  N N 417 
MET   CG     C  N N 418 
MET   SD     S  N N 419 
MET   CE     C  N N 420 
MET   OXT    O  N N 421 
MET   H      H  N N 422 
MET   H2     H  N N 423 
MET   HA     H  N N 424 
MET   HB2    H  N N 425 
MET   HB3    H  N N 426 
MET   HG2    H  N N 427 
MET   HG3    H  N N 428 
MET   HE1    H  N N 429 
MET   HE2    H  N N 430 
MET   HE3    H  N N 431 
MET   HXT    H  N N 432 
MG    MG     MG N N 433 
PHE   N      N  N N 434 
PHE   CA     C  N S 435 
PHE   C      C  N N 436 
PHE   O      O  N N 437 
PHE   CB     C  N N 438 
PHE   CG     C  Y N 439 
PHE   CD1    C  Y N 440 
PHE   CD2    C  Y N 441 
PHE   CE1    C  Y N 442 
PHE   CE2    C  Y N 443 
PHE   CZ     C  Y N 444 
PHE   OXT    O  N N 445 
PHE   H      H  N N 446 
PHE   H2     H  N N 447 
PHE   HA     H  N N 448 
PHE   HB2    H  N N 449 
PHE   HB3    H  N N 450 
PHE   HD1    H  N N 451 
PHE   HD2    H  N N 452 
PHE   HE1    H  N N 453 
PHE   HE2    H  N N 454 
PHE   HZ     H  N N 455 
PHE   HXT    H  N N 456 
PRO   N      N  N N 457 
PRO   CA     C  N S 458 
PRO   C      C  N N 459 
PRO   O      O  N N 460 
PRO   CB     C  N N 461 
PRO   CG     C  N N 462 
PRO   CD     C  N N 463 
PRO   OXT    O  N N 464 
PRO   H      H  N N 465 
PRO   HA     H  N N 466 
PRO   HB2    H  N N 467 
PRO   HB3    H  N N 468 
PRO   HG2    H  N N 469 
PRO   HG3    H  N N 470 
PRO   HD2    H  N N 471 
PRO   HD3    H  N N 472 
PRO   HXT    H  N N 473 
SER   N      N  N N 474 
SER   CA     C  N S 475 
SER   C      C  N N 476 
SER   O      O  N N 477 
SER   CB     C  N N 478 
SER   OG     O  N N 479 
SER   OXT    O  N N 480 
SER   H      H  N N 481 
SER   H2     H  N N 482 
SER   HA     H  N N 483 
SER   HB2    H  N N 484 
SER   HB3    H  N N 485 
SER   HG     H  N N 486 
SER   HXT    H  N N 487 
THR   N      N  N N 488 
THR   CA     C  N S 489 
THR   C      C  N N 490 
THR   O      O  N N 491 
THR   CB     C  N R 492 
THR   OG1    O  N N 493 
THR   CG2    C  N N 494 
THR   OXT    O  N N 495 
THR   H      H  N N 496 
THR   H2     H  N N 497 
THR   HA     H  N N 498 
THR   HB     H  N N 499 
THR   HG1    H  N N 500 
THR   HG21   H  N N 501 
THR   HG22   H  N N 502 
THR   HG23   H  N N 503 
THR   HXT    H  N N 504 
TRP   N      N  N N 505 
TRP   CA     C  N S 506 
TRP   C      C  N N 507 
TRP   O      O  N N 508 
TRP   CB     C  N N 509 
TRP   CG     C  Y N 510 
TRP   CD1    C  Y N 511 
TRP   CD2    C  Y N 512 
TRP   NE1    N  Y N 513 
TRP   CE2    C  Y N 514 
TRP   CE3    C  Y N 515 
TRP   CZ2    C  Y N 516 
TRP   CZ3    C  Y N 517 
TRP   CH2    C  Y N 518 
TRP   OXT    O  N N 519 
TRP   H      H  N N 520 
TRP   H2     H  N N 521 
TRP   HA     H  N N 522 
TRP   HB2    H  N N 523 
TRP   HB3    H  N N 524 
TRP   HD1    H  N N 525 
TRP   HE1    H  N N 526 
TRP   HE3    H  N N 527 
TRP   HZ2    H  N N 528 
TRP   HZ3    H  N N 529 
TRP   HH2    H  N N 530 
TRP   HXT    H  N N 531 
TYR   N      N  N N 532 
TYR   CA     C  N S 533 
TYR   C      C  N N 534 
TYR   O      O  N N 535 
TYR   CB     C  N N 536 
TYR   CG     C  Y N 537 
TYR   CD1    C  Y N 538 
TYR   CD2    C  Y N 539 
TYR   CE1    C  Y N 540 
TYR   CE2    C  Y N 541 
TYR   CZ     C  Y N 542 
TYR   OH     O  N N 543 
TYR   OXT    O  N N 544 
TYR   H      H  N N 545 
TYR   H2     H  N N 546 
TYR   HA     H  N N 547 
TYR   HB2    H  N N 548 
TYR   HB3    H  N N 549 
TYR   HD1    H  N N 550 
TYR   HD2    H  N N 551 
TYR   HE1    H  N N 552 
TYR   HE2    H  N N 553 
TYR   HH     H  N N 554 
TYR   HXT    H  N N 555 
VAL   N      N  N N 556 
VAL   CA     C  N S 557 
VAL   C      C  N N 558 
VAL   O      O  N N 559 
VAL   CB     C  N N 560 
VAL   CG1    C  N N 561 
VAL   CG2    C  N N 562 
VAL   OXT    O  N N 563 
VAL   H      H  N N 564 
VAL   H2     H  N N 565 
VAL   HA     H  N N 566 
VAL   HB     H  N N 567 
VAL   HG11   H  N N 568 
VAL   HG12   H  N N 569 
VAL   HG13   H  N N 570 
VAL   HG21   H  N N 571 
VAL   HG22   H  N N 572 
VAL   HG23   H  N N 573 
VAL   HXT    H  N N 574 
# 
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 
A1AOK O1    C1     doub N N 1   
A1AOK C1    N1     sing N N 2   
A1AOK N1    C2     sing N N 3   
A1AOK C2    C3     sing N N 4   
A1AOK C3    N2     sing N N 5   
A1AOK N2    C4     sing N N 6   
A1AOK C4    C5     sing N N 7   
A1AOK C5    C6     sing N N 8   
A1AOK C6    C7     sing N N 9   
A1AOK C7    C8     sing N N 10  
A1AOK C8    O2     sing N N 11  
A1AOK O2    C9     sing N N 12  
A1AOK C9    C10    sing N N 13  
A1AOK C10   C11    sing N N 14  
A1AOK C10   C12    sing N N 15  
A1AOK C10   C13    sing N N 16  
A1AOK C13   C14    sing N N 17  
A1AOK C14   C15    doub Y N 18  
A1AOK C15   C16    sing N N 19  
A1AOK C16   C17    doub Y N 20  
A1AOK C17   C18    sing N N 21  
A1AOK C18   C19    sing N N 22  
A1AOK C19   O3     sing N N 23  
A1AOK O3    C20    sing N N 24  
A1AOK C17   C21    sing Y N 25  
A1AOK C21   C22    doub Y N 26  
A1AOK C22   C23    sing Y N 27  
A1AOK C23   C24    doub Y N 28  
A1AOK C15   N3     sing Y N 29  
A1AOK N3    C25    sing N N 30  
A1AOK C25   C26    sing N N 31  
A1AOK C8    O4     doub N N 32  
A1AOK C7    N4     sing N N 33  
A1AOK C3    O5     doub N N 34  
A1AOK C2    C27    sing N N 35  
A1AOK C27   C28    sing N N 36  
A1AOK C28   C29    sing Y N 37  
A1AOK C29   C30    doub Y N 38  
A1AOK C30   C31    sing N N 39  
A1AOK C31   C32    sing Y N 40  
A1AOK C32   C33    doub Y N 41  
A1AOK C33   C34    sing Y N 42  
A1AOK C34   C35    doub Y N 43  
A1AOK C35   C36    sing Y N 44  
A1AOK C30   C37    sing Y N 45  
A1AOK C37   C38    doub Y N 46  
A1AOK C38   O6     sing N N 47  
A1AOK C38   C39    sing Y N 48  
A1AOK C1    C40    sing N N 49  
A1AOK C40   C41    sing N N 50  
A1AOK C41   C42    sing N N 51  
A1AOK C41   C43    sing N N 52  
A1AOK C40   N5     sing N N 53  
A1AOK N5    C44    sing N N 54  
A1AOK N5    C45    sing N N 55  
A1AOK C45   C46    sing N N 56  
A1AOK C46   C47    sing N N 57  
A1AOK C47   C48    sing N N 58  
A1AOK C48   N6     sing N N 59  
A1AOK N6    C49    sing N N 60  
A1AOK C49   C50    sing N N 61  
A1AOK C50   C51    sing N N 62  
A1AOK C49   O7     doub N N 63  
A1AOK N6    C52    sing N N 64  
A1AOK C45   O8     doub N N 65  
A1AOK N2    N4     sing N N 66  
A1AOK C14   C33    sing Y N 67  
A1AOK C16   C24    sing Y N 68  
A1AOK N3    C34    sing Y N 69  
A1AOK C28   C39    doub Y N 70  
A1AOK C31   C36    doub Y N 71  
A1AOK C46   C52    sing N N 72  
A1AOK C11   H14    sing N N 73  
A1AOK C11   H12    sing N N 74  
A1AOK C11   H13    sing N N 75  
A1AOK C12   H17    sing N N 76  
A1AOK C12   H15    sing N N 77  
A1AOK C12   H16    sing N N 78  
A1AOK C13   H19    sing N N 79  
A1AOK C13   H18    sing N N 80  
A1AOK C18   H20    sing N N 81  
A1AOK C18   H21    sing N N 82  
A1AOK C19   H22    sing N N 83  
A1AOK C19   H23    sing N N 84  
A1AOK C2    H2     sing N N 85  
A1AOK C20   H26    sing N N 86  
A1AOK C20   H25    sing N N 87  
A1AOK C20   H24    sing N N 88  
A1AOK C21   H27    sing N N 89  
A1AOK C22   H28    sing N N 90  
A1AOK C23   H29    sing N N 91  
A1AOK C24   H30    sing N N 92  
A1AOK C25   H31    sing N N 93  
A1AOK C25   H32    sing N N 94  
A1AOK C26   H33    sing N N 95  
A1AOK C26   H35    sing N N 96  
A1AOK C26   H34    sing N N 97  
A1AOK C27   H38    sing N N 98  
A1AOK C27   H37    sing N N 99  
A1AOK C29   H39    sing N N 100 
A1AOK C32   H40    sing N N 101 
A1AOK C35   H41    sing N N 102 
A1AOK C36   H42    sing N N 103 
A1AOK C37   H43    sing N N 104 
A1AOK C39   H45    sing N N 105 
A1AOK C4    H4     sing N N 106 
A1AOK C4    H3     sing N N 107 
A1AOK C40   H46    sing N N 108 
A1AOK C41   H47    sing N N 109 
A1AOK C42   H48    sing N N 110 
A1AOK C42   H49    sing N N 111 
A1AOK C42   H50    sing N N 112 
A1AOK C43   H51    sing N N 113 
A1AOK C43   H53    sing N N 114 
A1AOK C43   H52    sing N N 115 
A1AOK C44   H56    sing N N 116 
A1AOK C44   H55    sing N N 117 
A1AOK C44   H54    sing N N 118 
A1AOK C46   H57    sing N N 119 
A1AOK C47   H59    sing N N 120 
A1AOK C47   H58    sing N N 121 
A1AOK C48   H61    sing N N 122 
A1AOK C48   H60    sing N N 123 
A1AOK C5    H6     sing N N 124 
A1AOK C5    H5     sing N N 125 
A1AOK C50   H63    sing N N 126 
A1AOK C50   H62    sing N N 127 
A1AOK C51   H66    sing N N 128 
A1AOK C51   H65    sing N N 129 
A1AOK C51   H64    sing N N 130 
A1AOK C52   H67    sing N N 131 
A1AOK C52   H68    sing N N 132 
A1AOK C6    H8     sing N N 133 
A1AOK C6    H7     sing N N 134 
A1AOK C7    H9     sing N N 135 
A1AOK C9    H10    sing N N 136 
A1AOK C9    H11    sing N N 137 
A1AOK N1    H1     sing N N 138 
A1AOK N4    H36    sing N N 139 
A1AOK O6    H44    sing N N 140 
ALA   N     CA     sing N N 141 
ALA   N     H      sing N N 142 
ALA   N     H2     sing N N 143 
ALA   CA    C      sing N N 144 
ALA   CA    CB     sing N N 145 
ALA   CA    HA     sing N N 146 
ALA   C     O      doub N N 147 
ALA   C     OXT    sing N N 148 
ALA   CB    HB1    sing N N 149 
ALA   CB    HB2    sing N N 150 
ALA   CB    HB3    sing N N 151 
ALA   OXT   HXT    sing N N 152 
ARG   N     CA     sing N N 153 
ARG   N     H      sing N N 154 
ARG   N     H2     sing N N 155 
ARG   CA    C      sing N N 156 
ARG   CA    CB     sing N N 157 
ARG   CA    HA     sing N N 158 
ARG   C     O      doub N N 159 
ARG   C     OXT    sing N N 160 
ARG   CB    CG     sing N N 161 
ARG   CB    HB2    sing N N 162 
ARG   CB    HB3    sing N N 163 
ARG   CG    CD     sing N N 164 
ARG   CG    HG2    sing N N 165 
ARG   CG    HG3    sing N N 166 
ARG   CD    NE     sing N N 167 
ARG   CD    HD2    sing N N 168 
ARG   CD    HD3    sing N N 169 
ARG   NE    CZ     sing N N 170 
ARG   NE    HE     sing N N 171 
ARG   CZ    NH1    sing N N 172 
ARG   CZ    NH2    doub N N 173 
ARG   NH1   HH11   sing N N 174 
ARG   NH1   HH12   sing N N 175 
ARG   NH2   HH21   sing N N 176 
ARG   NH2   HH22   sing N N 177 
ARG   OXT   HXT    sing N N 178 
ASN   N     CA     sing N N 179 
ASN   N     H      sing N N 180 
ASN   N     H2     sing N N 181 
ASN   CA    C      sing N N 182 
ASN   CA    CB     sing N N 183 
ASN   CA    HA     sing N N 184 
ASN   C     O      doub N N 185 
ASN   C     OXT    sing N N 186 
ASN   CB    CG     sing N N 187 
ASN   CB    HB2    sing N N 188 
ASN   CB    HB3    sing N N 189 
ASN   CG    OD1    doub N N 190 
ASN   CG    ND2    sing N N 191 
ASN   ND2   HD21   sing N N 192 
ASN   ND2   HD22   sing N N 193 
ASN   OXT   HXT    sing N N 194 
ASP   N     CA     sing N N 195 
ASP   N     H      sing N N 196 
ASP   N     H2     sing N N 197 
ASP   CA    C      sing N N 198 
ASP   CA    CB     sing N N 199 
ASP   CA    HA     sing N N 200 
ASP   C     O      doub N N 201 
ASP   C     OXT    sing N N 202 
ASP   CB    CG     sing N N 203 
ASP   CB    HB2    sing N N 204 
ASP   CB    HB3    sing N N 205 
ASP   CG    OD1    doub N N 206 
ASP   CG    OD2    sing N N 207 
ASP   OD2   HD2    sing N N 208 
ASP   OXT   HXT    sing N N 209 
CYS   N     CA     sing N N 210 
CYS   N     H      sing N N 211 
CYS   N     H2     sing N N 212 
CYS   CA    C      sing N N 213 
CYS   CA    CB     sing N N 214 
CYS   CA    HA     sing N N 215 
CYS   C     O      doub N N 216 
CYS   C     OXT    sing N N 217 
CYS   CB    SG     sing N N 218 
CYS   CB    HB2    sing N N 219 
CYS   CB    HB3    sing N N 220 
CYS   SG    HG     sing N N 221 
CYS   OXT   HXT    sing N N 222 
GLN   N     CA     sing N N 223 
GLN   N     H      sing N N 224 
GLN   N     H2     sing N N 225 
GLN   CA    C      sing N N 226 
GLN   CA    CB     sing N N 227 
GLN   CA    HA     sing N N 228 
GLN   C     O      doub N N 229 
GLN   C     OXT    sing N N 230 
GLN   CB    CG     sing N N 231 
GLN   CB    HB2    sing N N 232 
GLN   CB    HB3    sing N N 233 
GLN   CG    CD     sing N N 234 
GLN   CG    HG2    sing N N 235 
GLN   CG    HG3    sing N N 236 
GLN   CD    OE1    doub N N 237 
GLN   CD    NE2    sing N N 238 
GLN   NE2   HE21   sing N N 239 
GLN   NE2   HE22   sing N N 240 
GLN   OXT   HXT    sing N N 241 
GLU   N     CA     sing N N 242 
GLU   N     H      sing N N 243 
GLU   N     H2     sing N N 244 
GLU   CA    C      sing N N 245 
GLU   CA    CB     sing N N 246 
GLU   CA    HA     sing N N 247 
GLU   C     O      doub N N 248 
GLU   C     OXT    sing N N 249 
GLU   CB    CG     sing N N 250 
GLU   CB    HB2    sing N N 251 
GLU   CB    HB3    sing N N 252 
GLU   CG    CD     sing N N 253 
GLU   CG    HG2    sing N N 254 
GLU   CG    HG3    sing N N 255 
GLU   CD    OE1    doub N N 256 
GLU   CD    OE2    sing N N 257 
GLU   OE2   HE2    sing N N 258 
GLU   OXT   HXT    sing N N 259 
GLY   N     CA     sing N N 260 
GLY   N     H      sing N N 261 
GLY   N     H2     sing N N 262 
GLY   CA    C      sing N N 263 
GLY   CA    HA2    sing N N 264 
GLY   CA    HA3    sing N N 265 
GLY   C     O      doub N N 266 
GLY   C     OXT    sing N N 267 
GLY   OXT   HXT    sing N N 268 
GNP   PG    O1G    doub N N 269 
GNP   PG    O2G    sing N N 270 
GNP   PG    O3G    sing N N 271 
GNP   PG    N3B    sing N N 272 
GNP   O2G   HOG2   sing N N 273 
GNP   O3G   HOG3   sing N N 274 
GNP   N3B   PB     sing N N 275 
GNP   N3B   HNB3   sing N N 276 
GNP   PB    O1B    doub N N 277 
GNP   PB    O2B    sing N N 278 
GNP   PB    O3A    sing N N 279 
GNP   O2B   HOB2   sing N N 280 
GNP   O3A   PA     sing N N 281 
GNP   PA    O1A    doub N N 282 
GNP   PA    O2A    sing N N 283 
GNP   PA    "O5'"  sing N N 284 
GNP   O2A   HOA2   sing N N 285 
GNP   "O5'" "C5'"  sing N N 286 
GNP   "C5'" "C4'"  sing N N 287 
GNP   "C5'" "H5'2" sing N N 288 
GNP   "C5'" "H5'1" sing N N 289 
GNP   "C4'" "O4'"  sing N N 290 
GNP   "C4'" "C3'"  sing N N 291 
GNP   "C4'" "H4'"  sing N N 292 
GNP   "O4'" "C1'"  sing N N 293 
GNP   "C3'" "O3'"  sing N N 294 
GNP   "C3'" "C2'"  sing N N 295 
GNP   "C3'" "H3'"  sing N N 296 
GNP   "O3'" "HO3'" sing N N 297 
GNP   "C2'" "O2'"  sing N N 298 
GNP   "C2'" "C1'"  sing N N 299 
GNP   "C2'" "H2'"  sing N N 300 
GNP   "O2'" "HO2'" sing N N 301 
GNP   "C1'" N9     sing N N 302 
GNP   "C1'" "H1'"  sing N N 303 
GNP   N9    C8     sing Y N 304 
GNP   N9    C4     sing Y N 305 
GNP   C8    N7     doub Y N 306 
GNP   C8    H8     sing N N 307 
GNP   N7    C5     sing Y N 308 
GNP   C5    C6     sing Y N 309 
GNP   C5    C4     doub Y N 310 
GNP   C6    O6     doub N N 311 
GNP   C6    N1     sing Y N 312 
GNP   N1    C2     sing Y N 313 
GNP   N1    HN1    sing N N 314 
GNP   C2    N2     sing N N 315 
GNP   C2    N3     doub Y N 316 
GNP   N2    HN21   sing N N 317 
GNP   N2    HN22   sing N N 318 
GNP   N3    C4     sing Y N 319 
HIS   N     CA     sing N N 320 
HIS   N     H      sing N N 321 
HIS   N     H2     sing N N 322 
HIS   CA    C      sing N N 323 
HIS   CA    CB     sing N N 324 
HIS   CA    HA     sing N N 325 
HIS   C     O      doub N N 326 
HIS   C     OXT    sing N N 327 
HIS   CB    CG     sing N N 328 
HIS   CB    HB2    sing N N 329 
HIS   CB    HB3    sing N N 330 
HIS   CG    ND1    sing Y N 331 
HIS   CG    CD2    doub Y N 332 
HIS   ND1   CE1    doub Y N 333 
HIS   ND1   HD1    sing N N 334 
HIS   CD2   NE2    sing Y N 335 
HIS   CD2   HD2    sing N N 336 
HIS   CE1   NE2    sing Y N 337 
HIS   CE1   HE1    sing N N 338 
HIS   NE2   HE2    sing N N 339 
HIS   OXT   HXT    sing N N 340 
HOH   O     H1     sing N N 341 
HOH   O     H2     sing N N 342 
ILE   N     CA     sing N N 343 
ILE   N     H      sing N N 344 
ILE   N     H2     sing N N 345 
ILE   CA    C      sing N N 346 
ILE   CA    CB     sing N N 347 
ILE   CA    HA     sing N N 348 
ILE   C     O      doub N N 349 
ILE   C     OXT    sing N N 350 
ILE   CB    CG1    sing N N 351 
ILE   CB    CG2    sing N N 352 
ILE   CB    HB     sing N N 353 
ILE   CG1   CD1    sing N N 354 
ILE   CG1   HG12   sing N N 355 
ILE   CG1   HG13   sing N N 356 
ILE   CG2   HG21   sing N N 357 
ILE   CG2   HG22   sing N N 358 
ILE   CG2   HG23   sing N N 359 
ILE   CD1   HD11   sing N N 360 
ILE   CD1   HD12   sing N N 361 
ILE   CD1   HD13   sing N N 362 
ILE   OXT   HXT    sing N N 363 
LEU   N     CA     sing N N 364 
LEU   N     H      sing N N 365 
LEU   N     H2     sing N N 366 
LEU   CA    C      sing N N 367 
LEU   CA    CB     sing N N 368 
LEU   CA    HA     sing N N 369 
LEU   C     O      doub N N 370 
LEU   C     OXT    sing N N 371 
LEU   CB    CG     sing N N 372 
LEU   CB    HB2    sing N N 373 
LEU   CB    HB3    sing N N 374 
LEU   CG    CD1    sing N N 375 
LEU   CG    CD2    sing N N 376 
LEU   CG    HG     sing N N 377 
LEU   CD1   HD11   sing N N 378 
LEU   CD1   HD12   sing N N 379 
LEU   CD1   HD13   sing N N 380 
LEU   CD2   HD21   sing N N 381 
LEU   CD2   HD22   sing N N 382 
LEU   CD2   HD23   sing N N 383 
LEU   OXT   HXT    sing N N 384 
LYS   N     CA     sing N N 385 
LYS   N     H      sing N N 386 
LYS   N     H2     sing N N 387 
LYS   CA    C      sing N N 388 
LYS   CA    CB     sing N N 389 
LYS   CA    HA     sing N N 390 
LYS   C     O      doub N N 391 
LYS   C     OXT    sing N N 392 
LYS   CB    CG     sing N N 393 
LYS   CB    HB2    sing N N 394 
LYS   CB    HB3    sing N N 395 
LYS   CG    CD     sing N N 396 
LYS   CG    HG2    sing N N 397 
LYS   CG    HG3    sing N N 398 
LYS   CD    CE     sing N N 399 
LYS   CD    HD2    sing N N 400 
LYS   CD    HD3    sing N N 401 
LYS   CE    NZ     sing N N 402 
LYS   CE    HE2    sing N N 403 
LYS   CE    HE3    sing N N 404 
LYS   NZ    HZ1    sing N N 405 
LYS   NZ    HZ2    sing N N 406 
LYS   NZ    HZ3    sing N N 407 
LYS   OXT   HXT    sing N N 408 
MET   N     CA     sing N N 409 
MET   N     H      sing N N 410 
MET   N     H2     sing N N 411 
MET   CA    C      sing N N 412 
MET   CA    CB     sing N N 413 
MET   CA    HA     sing N N 414 
MET   C     O      doub N N 415 
MET   C     OXT    sing N N 416 
MET   CB    CG     sing N N 417 
MET   CB    HB2    sing N N 418 
MET   CB    HB3    sing N N 419 
MET   CG    SD     sing N N 420 
MET   CG    HG2    sing N N 421 
MET   CG    HG3    sing N N 422 
MET   SD    CE     sing N N 423 
MET   CE    HE1    sing N N 424 
MET   CE    HE2    sing N N 425 
MET   CE    HE3    sing N N 426 
MET   OXT   HXT    sing N N 427 
PHE   N     CA     sing N N 428 
PHE   N     H      sing N N 429 
PHE   N     H2     sing N N 430 
PHE   CA    C      sing N N 431 
PHE   CA    CB     sing N N 432 
PHE   CA    HA     sing N N 433 
PHE   C     O      doub N N 434 
PHE   C     OXT    sing N N 435 
PHE   CB    CG     sing N N 436 
PHE   CB    HB2    sing N N 437 
PHE   CB    HB3    sing N N 438 
PHE   CG    CD1    doub Y N 439 
PHE   CG    CD2    sing Y N 440 
PHE   CD1   CE1    sing Y N 441 
PHE   CD1   HD1    sing N N 442 
PHE   CD2   CE2    doub Y N 443 
PHE   CD2   HD2    sing N N 444 
PHE   CE1   CZ     doub Y N 445 
PHE   CE1   HE1    sing N N 446 
PHE   CE2   CZ     sing Y N 447 
PHE   CE2   HE2    sing N N 448 
PHE   CZ    HZ     sing N N 449 
PHE   OXT   HXT    sing N N 450 
PRO   N     CA     sing N N 451 
PRO   N     CD     sing N N 452 
PRO   N     H      sing N N 453 
PRO   CA    C      sing N N 454 
PRO   CA    CB     sing N N 455 
PRO   CA    HA     sing N N 456 
PRO   C     O      doub N N 457 
PRO   C     OXT    sing N N 458 
PRO   CB    CG     sing N N 459 
PRO   CB    HB2    sing N N 460 
PRO   CB    HB3    sing N N 461 
PRO   CG    CD     sing N N 462 
PRO   CG    HG2    sing N N 463 
PRO   CG    HG3    sing N N 464 
PRO   CD    HD2    sing N N 465 
PRO   CD    HD3    sing N N 466 
PRO   OXT   HXT    sing N N 467 
SER   N     CA     sing N N 468 
SER   N     H      sing N N 469 
SER   N     H2     sing N N 470 
SER   CA    C      sing N N 471 
SER   CA    CB     sing N N 472 
SER   CA    HA     sing N N 473 
SER   C     O      doub N N 474 
SER   C     OXT    sing N N 475 
SER   CB    OG     sing N N 476 
SER   CB    HB2    sing N N 477 
SER   CB    HB3    sing N N 478 
SER   OG    HG     sing N N 479 
SER   OXT   HXT    sing N N 480 
THR   N     CA     sing N N 481 
THR   N     H      sing N N 482 
THR   N     H2     sing N N 483 
THR   CA    C      sing N N 484 
THR   CA    CB     sing N N 485 
THR   CA    HA     sing N N 486 
THR   C     O      doub N N 487 
THR   C     OXT    sing N N 488 
THR   CB    OG1    sing N N 489 
THR   CB    CG2    sing N N 490 
THR   CB    HB     sing N N 491 
THR   OG1   HG1    sing N N 492 
THR   CG2   HG21   sing N N 493 
THR   CG2   HG22   sing N N 494 
THR   CG2   HG23   sing N N 495 
THR   OXT   HXT    sing N N 496 
TRP   N     CA     sing N N 497 
TRP   N     H      sing N N 498 
TRP   N     H2     sing N N 499 
TRP   CA    C      sing N N 500 
TRP   CA    CB     sing N N 501 
TRP   CA    HA     sing N N 502 
TRP   C     O      doub N N 503 
TRP   C     OXT    sing N N 504 
TRP   CB    CG     sing N N 505 
TRP   CB    HB2    sing N N 506 
TRP   CB    HB3    sing N N 507 
TRP   CG    CD1    doub Y N 508 
TRP   CG    CD2    sing Y N 509 
TRP   CD1   NE1    sing Y N 510 
TRP   CD1   HD1    sing N N 511 
TRP   CD2   CE2    doub Y N 512 
TRP   CD2   CE3    sing Y N 513 
TRP   NE1   CE2    sing Y N 514 
TRP   NE1   HE1    sing N N 515 
TRP   CE2   CZ2    sing Y N 516 
TRP   CE3   CZ3    doub Y N 517 
TRP   CE3   HE3    sing N N 518 
TRP   CZ2   CH2    doub Y N 519 
TRP   CZ2   HZ2    sing N N 520 
TRP   CZ3   CH2    sing Y N 521 
TRP   CZ3   HZ3    sing N N 522 
TRP   CH2   HH2    sing N N 523 
TRP   OXT   HXT    sing N N 524 
TYR   N     CA     sing N N 525 
TYR   N     H      sing N N 526 
TYR   N     H2     sing N N 527 
TYR   CA    C      sing N N 528 
TYR   CA    CB     sing N N 529 
TYR   CA    HA     sing N N 530 
TYR   C     O      doub N N 531 
TYR   C     OXT    sing N N 532 
TYR   CB    CG     sing N N 533 
TYR   CB    HB2    sing N N 534 
TYR   CB    HB3    sing N N 535 
TYR   CG    CD1    doub Y N 536 
TYR   CG    CD2    sing Y N 537 
TYR   CD1   CE1    sing Y N 538 
TYR   CD1   HD1    sing N N 539 
TYR   CD2   CE2    doub Y N 540 
TYR   CD2   HD2    sing N N 541 
TYR   CE1   CZ     doub Y N 542 
TYR   CE1   HE1    sing N N 543 
TYR   CE2   CZ     sing Y N 544 
TYR   CE2   HE2    sing N N 545 
TYR   CZ    OH     sing N N 546 
TYR   OH    HH     sing N N 547 
TYR   OXT   HXT    sing N N 548 
VAL   N     CA     sing N N 549 
VAL   N     H      sing N N 550 
VAL   N     H2     sing N N 551 
VAL   CA    C      sing N N 552 
VAL   CA    CB     sing N N 553 
VAL   CA    HA     sing N N 554 
VAL   C     O      doub N N 555 
VAL   C     OXT    sing N N 556 
VAL   CB    CG1    sing N N 557 
VAL   CB    CG2    sing N N 558 
VAL   CB    HB     sing N N 559 
VAL   CG1   HG11   sing N N 560 
VAL   CG1   HG12   sing N N 561 
VAL   CG1   HG13   sing N N 562 
VAL   CG2   HG21   sing N N 563 
VAL   CG2   HG22   sing N N 564 
VAL   CG2   HG23   sing N N 565 
VAL   OXT   HXT    sing N N 566 
# 
_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 2 1' 
_space_group.name_Hall        'P 2y' 
_space_group.IT_number        3 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BFZ 
_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]   0.014949 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001014 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020761 
_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]   0.009816 
_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   ? 78.25000  -14.07600 -14.92700 1.000 35.54470 ? 0   SER   B N     1 
ATOM   2    C  CA    . SER   A 1 1   ? 77.65300  -14.14600 -13.59500 1.000 25.20920 ? 0   SER   B CA    1 
ATOM   3    C  C     . SER   A 1 1   ? 76.30800  -14.85600 -13.65200 1.000 33.27950 ? 0   SER   B C     1 
ATOM   4    O  O     . SER   A 1 1   ? 75.80900  -15.19100 -14.72500 1.000 39.24210 ? 0   SER   B O     1 
ATOM   5    C  CB    . SER   A 1 1   ? 77.49000  -12.74000 -13.00600 1.000 26.84087 ? 0   SER   B CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? 76.96800  -12.76700 -11.68400 1.000 20.39745 ? 0   SER   B OG    1 
ATOM   7    N  N     . MET   A 1 2   ? 75.71700  -15.09700 -12.49000 1.000 23.70950 ? 1   MET   B N     1 
ATOM   8    C  CA    . MET   A 1 2   ? 74.42400  -15.74200 -12.43700 1.000 22.49659 ? 1   MET   B CA    1 
ATOM   9    C  C     . MET   A 1 2   ? 73.60800  -15.09900 -11.33300 1.000 17.63077 ? 1   MET   B C     1 
ATOM   10   O  O     . MET   A 1 2   ? 74.09900  -14.27000 -10.56200 1.000 20.68036 ? 1   MET   B O     1 
ATOM   11   C  CB    . MET   A 1 2   ? 74.55300  -17.25900 -12.24100 1.000 22.19612 ? 1   MET   B CB    1 
ATOM   12   C  CG    . MET   A 1 2   ? 75.25600  -17.70600 -10.98500 1.000 21.58297 ? 1   MET   B CG    1 
ATOM   13   S  SD    . MET   A 1 2   ? 75.18500  -19.51600 -10.81400 1.000 39.58934 ? 1   MET   B SD    1 
ATOM   14   C  CE    . MET   A 1 2   ? 76.66400  -19.97900 -11.71500 1.000 31.25336 ? 1   MET   B CE    1 
ATOM   15   N  N     . THR   A 1 3   ? 72.33700  -15.47000 -11.29200 1.000 14.52770 ? 2   THR   B N     1 
ATOM   16   C  CA    . THR   A 1 3   ? 71.41200  -14.98000 -10.29600 1.000 13.79858 ? 2   THR   B CA    1 
ATOM   17   C  C     . THR   A 1 3   ? 70.73000  -16.18300 -9.67100  1.000 14.27774 ? 2   THR   B C     1 
ATOM   18   O  O     . THR   A 1 3   ? 70.94600  -17.33000 -10.07800 1.000 18.69065 ? 2   THR   B O     1 
ATOM   19   C  CB    . THR   A 1 3   ? 70.38000  -14.02500 -10.90800 1.000 14.67993 ? 2   THR   B CB    1 
ATOM   20   O  OG1   . THR   A 1 3   ? 69.77800  -14.66500 -12.03900 1.000 20.27525 ? 2   THR   B OG1   1 
ATOM   21   C  CG2   . THR   A 1 3   ? 71.04300  -12.70800 -11.36000 1.000 14.07503 ? 2   THR   B CG2   1 
ATOM   22   N  N     . GLU   A 1 4   ? 69.92300  -15.91300 -8.66200  1.000 13.14550 ? 3   GLU   B N     1 
ATOM   23   C  CA    . GLU   A 1 4   ? 69.23200  -16.95600 -7.91900  1.000 16.70855 ? 3   GLU   B CA    1 
ATOM   24   C  C     . GLU   A 1 4   ? 67.87600  -16.40900 -7.49700  1.000 15.80844 ? 3   GLU   B C     1 
ATOM   25   O  O     . GLU   A 1 4   ? 67.75500  -15.22600 -7.16300  1.000 16.01437 ? 3   GLU   B O     1 
ATOM   26   C  CB    . GLU   A 1 4   ? 70.07700  -17.40000 -6.71100  1.000 17.97795 ? 3   GLU   B CB    1 
ATOM   27   C  CG    . GLU   A 1 4   ? 69.51800  -18.55000 -5.88900  1.000 15.84266 ? 3   GLU   B CG    1 
ATOM   28   C  CD    . GLU   A 1 4   ? 70.53700  -19.07000 -4.86700  1.000 20.53843 ? 3   GLU   B CD    1 
ATOM   29   O  OE1   . GLU   A 1 4   ? 71.73200  -18.70700 -4.95300  1.000 20.42458 ? 3   GLU   B OE1   1 
ATOM   30   O  OE2   . GLU   A 1 4   ? 70.15300  -19.84400 -3.97800  1.000 23.19500 ? 3   GLU   B OE2   1 
ATOM   31   N  N     . TYR   A 1 5   ? 66.85800  -17.26700 -7.52600  1.000 9.57039  ? 4   TYR   B N     1 
ATOM   32   C  CA    . TYR   A 1 5   ? 65.48200  -16.86300 -7.26000  1.000 12.28550 ? 4   TYR   B CA    1 
ATOM   33   C  C     . TYR   A 1 5   ? 64.77700  -17.88100 -6.38000  1.000 9.96388  ? 4   TYR   B C     1 
ATOM   34   O  O     . TYR   A 1 5   ? 64.89700  -19.09700 -6.59100  1.000 11.95508 ? 4   TYR   B O     1 
ATOM   35   C  CB    . TYR   A 1 5   ? 64.68100  -16.70900 -8.55400  1.000 9.14018  ? 4   TYR   B CB    1 
ATOM   36   C  CG    . TYR   A 1 5   ? 65.31600  -15.78400 -9.55400  1.000 13.27493 ? 4   TYR   B CG    1 
ATOM   37   C  CD1   . TYR   A 1 5   ? 65.25700  -14.39600 -9.38500  1.000 16.07280 ? 4   TYR   B CD1   1 
ATOM   38   C  CD2   . TYR   A 1 5   ? 65.97900  -16.28200 -10.66400 1.000 9.74063  ? 4   TYR   B CD2   1 
ATOM   39   C  CE1   . TYR   A 1 5   ? 65.85500  -13.53300 -10.30100 1.000 15.78905 ? 4   TYR   B CE1   1 
ATOM   40   C  CE2   . TYR   A 1 5   ? 66.57700  -15.43300 -11.58500 1.000 10.48810 ? 4   TYR   B CE2   1 
ATOM   41   C  CZ    . TYR   A 1 5   ? 66.50000  -14.06300 -11.40700 1.000 11.91625 ? 4   TYR   B CZ    1 
ATOM   42   O  OH    . TYR   A 1 5   ? 67.09100  -13.21800 -12.30700 1.000 13.57369 ? 4   TYR   B OH    1 
ATOM   43   N  N     . LYS   A 1 6   ? 64.01700  -17.38800 -5.40500  1.000 9.45959  ? 5   LYS   B N     1 
ATOM   44   C  CA    . LYS   A 1 6   ? 63.20600  -18.25600 -4.55400  1.000 12.60852 ? 5   LYS   B CA    1 
ATOM   45   C  C     . LYS   A 1 6   ? 61.79300  -18.24900 -5.11800  1.000 10.12124 ? 5   LYS   B C     1 
ATOM   46   O  O     . LYS   A 1 6   ? 61.09300  -17.23000 -5.05000  1.000 8.54247  ? 5   LYS   B O     1 
ATOM   47   C  CB    . LYS   A 1 6   ? 63.23000  -17.79900 -3.09500  1.000 12.82223 ? 5   LYS   B CB    1 
ATOM   48   C  CG    . LYS   A 1 6   ? 64.62600  -17.73600 -2.49700  1.000 20.04408 ? 5   LYS   B CG    1 
ATOM   49   C  CD    . LYS   A 1 6   ? 64.60600  -17.13000 -1.08700  1.000 32.18753 ? 5   LYS   B CD    1 
ATOM   50   C  CE    . LYS   A 1 6   ? 64.54200  -15.60100 -1.11100  1.000 23.92798 ? 5   LYS   B CE    1 
ATOM   51   N  NZ    . LYS   A 1 6   ? 65.83400  -15.00000 -1.53400  1.000 33.43382 ? 5   LYS   B NZ    1 
ATOM   52   N  N     . LEU   A 1 7   ? 61.39400  -19.37100 -5.70800  1.000 11.60731 ? 6   LEU   B N     1 
ATOM   53   C  CA    . LEU   A 1 7   ? 60.05000  -19.54600 -6.23700  1.000 11.20800 ? 6   LEU   B CA    1 
ATOM   54   C  C     . LEU   A 1 7   ? 59.23900  -20.40700 -5.27900  1.000 9.55645  ? 6   LEU   B C     1 
ATOM   55   O  O     . LEU   A 1 7   ? 59.76000  -21.36500 -4.70000  1.000 9.11384  ? 6   LEU   B O     1 
ATOM   56   C  CB    . LEU   A 1 7   ? 60.10100  -20.19100 -7.62600  1.000 12.52795 ? 6   LEU   B CB    1 
ATOM   57   C  CG    . LEU   A 1 7   ? 61.15200  -19.61700 -8.59200  1.000 8.99726  ? 6   LEU   B CG    1 
ATOM   58   C  CD1   . LEU   A 1 7   ? 61.13100  -20.33000 -9.92500  1.000 11.66338 ? 6   LEU   B CD1   1 
ATOM   59   C  CD2   . LEU   A 1 7   ? 60.90500  -18.14100 -8.80600  1.000 9.67284  ? 6   LEU   B CD2   1 
ATOM   60   N  N     . VAL   A 1 8   ? 57.95800  -20.07500 -5.11600  1.000 7.67571  ? 7   VAL   B N     1 
ATOM   61   C  CA    . VAL   A 1 8   ? 57.08000  -20.79000 -4.20200  1.000 6.29619  ? 7   VAL   B CA    1 
ATOM   62   C  C     . VAL   A 1 8   ? 55.84200  -21.23200 -4.96800  1.000 5.95379  ? 7   VAL   B C     1 
ATOM   63   O  O     . VAL   A 1 8   ? 55.21100  -20.42000 -5.65100  1.000 9.22898  ? 7   VAL   B O     1 
ATOM   64   C  CB    . VAL   A 1 8   ? 56.69400  -19.92500 -2.99000  1.000 6.46039  ? 7   VAL   B CB    1 
ATOM   65   C  CG1   . VAL   A 1 8   ? 55.86600  -20.75000 -2.01800  1.000 6.93682  ? 7   VAL   B CG1   1 
ATOM   66   C  CG2   . VAL   A 1 8   ? 57.96000  -19.39000 -2.33200  1.000 8.23335  ? 7   VAL   B CG2   1 
ATOM   67   N  N     . VAL   A 1 9   ? 55.51700  -22.51900 -4.87700  1.000 8.72481  ? 8   VAL   B N     1 
ATOM   68   C  CA    . VAL   A 1 9   ? 54.37100  -23.09100 -5.57600  1.000 8.01123  ? 8   VAL   B CA    1 
ATOM   69   C  C     . VAL   A 1 9   ? 53.24400  -23.30200 -4.57500  1.000 7.58434  ? 8   VAL   B C     1 
ATOM   70   O  O     . VAL   A 1 9   ? 53.37600  -24.09900 -3.63600  1.000 7.97243  ? 8   VAL   B O     1 
ATOM   71   C  CB    . VAL   A 1 9   ? 54.74300  -24.41400 -6.26700  1.000 9.14279  ? 8   VAL   B CB    1 
ATOM   72   C  CG1   . VAL   A 1 9   ? 53.61300  -24.85300 -7.16900  1.000 8.72431  ? 8   VAL   B CG1   1 
ATOM   73   C  CG2   . VAL   A 1 9   ? 56.03900  -24.26000 -7.05300  1.000 5.97897  ? 8   VAL   B CG2   1 
ATOM   74   N  N     . VAL   A 1 10  ? 52.11100  -22.62900 -4.80400  1.000 9.44401  ? 9   VAL   B N     1 
ATOM   75   C  CA    . VAL   A 1 10  ? 50.96700  -22.65700 -3.90000  1.000 10.80644 ? 9   VAL   B CA    1 
ATOM   76   C  C     . VAL   A 1 10  ? 49.71200  -23.00900 -4.69900  1.000 7.51981  ? 9   VAL   B C     1 
ATOM   77   O  O     . VAL   A 1 10  ? 49.69200  -22.96400 -5.93100  1.000 7.74730  ? 9   VAL   B O     1 
ATOM   78   C  CB    . VAL   A 1 10  ? 50.78600  -21.31900 -3.14800  1.000 7.33705  ? 9   VAL   B CB    1 
ATOM   79   C  CG1   . VAL   A 1 10  ? 52.08100  -20.95500 -2.42000  1.000 6.75110  ? 9   VAL   B CG1   1 
ATOM   80   C  CG2   . VAL   A 1 10  ? 50.39300  -20.21500 -4.11600  1.000 7.62191  ? 9   VAL   B CG2   1 
ATOM   81   N  N     . GLY   A 1 11  ? 48.66800  -23.39200 -3.97100  1.000 11.88822 ? 10  GLY   B N     1 
ATOM   82   C  CA    . GLY   A 1 11  ? 47.40800  -23.79100 -4.57300  1.000 9.44189  ? 10  GLY   B CA    1 
ATOM   83   C  C     . GLY   A 1 11  ? 46.75900  -24.95900 -3.85000  1.000 10.76676 ? 10  GLY   B C     1 
ATOM   84   O  O     . GLY   A 1 11  ? 47.39800  -25.61600 -3.02600  1.000 10.92744 ? 10  GLY   B O     1 
ATOM   85   N  N     . ALA   A 1 12  ? 45.49600  -25.24000 -4.16800  1.000 11.18358 ? 11  ALA   B N     1 
ATOM   86   C  CA    . ALA   A 1 12  ? 44.73600  -26.24100 -3.43600  1.000 13.68916 ? 11  ALA   B CA    1 
ATOM   87   C  C     . ALA   A 1 12  ? 45.37500  -27.62500 -3.53300  1.000 9.95959  ? 11  ALA   B C     1 
ATOM   88   O  O     . ALA   A 1 12  ? 46.06900  -27.96100 -4.48900  1.000 8.52983  ? 11  ALA   B O     1 
ATOM   89   C  CB    . ALA   A 1 12  ? 43.29400  -26.30900 -3.95000  1.000 11.80057 ? 11  ALA   B CB    1 
ATOM   90   N  N     . CYS   A 1 13  ? 45.09800  -28.44800 -2.52700  1.000 10.20612 ? 12  CYS   B N     1 
ATOM   91   C  CA    . CYS   A 1 13  ? 45.58400  -29.82000 -2.54300  1.000 9.48798  ? 12  CYS   B CA    1 
ATOM   92   C  C     . CYS   A 1 13  ? 45.09100  -30.56400 -3.78200  1.000 10.57581 ? 12  CYS   B C     1 
ATOM   93   O  O     . CYS   A 1 13  ? 43.91300  -30.47400 -4.16600  1.000 10.21124 ? 12  CYS   B O     1 
ATOM   94   C  CB    . CYS   A 1 13  ? 45.12600  -30.55000 -1.27100  1.000 10.65530 ? 12  CYS   B CB    1 
ATOM   95   S  SG    . CYS   A 1 13  ? 43.31600  -30.60700 -1.05900  1.000 14.11056 ? 12  CYS   B SG    1 
ATOM   96   N  N     . GLY   A 1 14  ? 46.00000  -31.32200 -4.39400  1.000 9.44678  ? 13  GLY   B N     1 
ATOM   97   C  CA    . GLY   A 1 14  ? 45.66700  -32.17600 -5.51200  1.000 9.81041  ? 13  GLY   B CA    1 
ATOM   98   C  C     . GLY   A 1 14  ? 45.78200  -31.53700 -6.88000  1.000 9.87693  ? 13  GLY   B C     1 
ATOM   99   O  O     . GLY   A 1 14  ? 45.55100  -32.22300 -7.87700  1.000 9.93699  ? 13  GLY   B O     1 
ATOM   100  N  N     . VAL   A 1 15  ? 46.13800  -30.25100 -6.96900  1.000 10.16786 ? 14  VAL   B N     1 
ATOM   101  C  CA    . VAL   A 1 15  ? 46.08900  -29.59800 -8.27400  1.000 8.88455  ? 14  VAL   B CA    1 
ATOM   102  C  C     . VAL   A 1 15  ? 47.29800  -29.92300 -9.13500  1.000 12.62938 ? 14  VAL   B C     1 
ATOM   103  O  O     . VAL   A 1 15  ? 47.23000  -29.76600 -10.36500 1.000 9.84934  ? 14  VAL   B O     1 
ATOM   104  C  CB    . VAL   A 1 15  ? 45.96000  -28.07000 -8.17000  1.000 9.46385  ? 14  VAL   B CB    1 
ATOM   105  C  CG1   . VAL   A 1 15  ? 44.66900  -27.69100 -7.49300  1.000 9.08803  ? 14  VAL   B CG1   1 
ATOM   106  C  CG2   . VAL   A 1 15  ? 47.18100  -27.43900 -7.44800  1.000 7.89529  ? 14  VAL   B CG2   1 
ATOM   107  N  N     . GLY   A 1 16  ? 48.41400  -30.33700 -8.53300  1.000 13.69619 ? 15  GLY   B N     1 
ATOM   108  C  CA    . GLY   A 1 16  ? 49.56000  -30.76100 -9.32400  1.000 8.27299  ? 15  GLY   B CA    1 
ATOM   109  C  C     . GLY   A 1 16  ? 50.80400  -29.93100 -9.09100  1.000 7.70055  ? 15  GLY   B C     1 
ATOM   110  O  O     . GLY   A 1 16  ? 51.68300  -29.89000 -9.95000  1.000 7.78717  ? 15  GLY   B O     1 
ATOM   111  N  N     . LYS   A 1 17  ? 50.88200  -29.27900 -7.93200  1.000 7.32786  ? 16  LYS   B N     1 
ATOM   112  C  CA    . LYS   A 1 17  ? 52.06100  -28.48300 -7.58200  1.000 8.09864  ? 16  LYS   B CA    1 
ATOM   113  C  C     . LYS   A 1 17  ? 53.32300  -29.33400 -7.58900  1.000 9.93085  ? 16  LYS   B C     1 
ATOM   114  O  O     . LYS   A 1 17  ? 54.35800  -28.93500 -8.14200  1.000 7.07381  ? 16  LYS   B O     1 
ATOM   115  C  CB    . LYS   A 1 17  ? 51.86500  -27.85100 -6.20700  1.000 6.71940  ? 16  LYS   B CB    1 
ATOM   116  C  CG    . LYS   A 1 17  ? 50.64800  -26.90700 -6.09400  1.000 7.25428  ? 16  LYS   B CG    1 
ATOM   117  C  CD    . LYS   A 1 17  ? 50.60000  -26.26700 -4.70100  1.000 9.06591  ? 16  LYS   B CD    1 
ATOM   118  C  CE    . LYS   A 1 17  ? 50.19400  -27.26700 -3.60800  1.000 7.12185  ? 16  LYS   B CE    1 
ATOM   119  N  NZ    . LYS   A 1 17  ? 48.87000  -27.93900 -3.87600  1.000 7.56093  ? 16  LYS   B NZ    1 
ATOM   120  N  N     . SER   A 1 18  ? 53.26000  -30.50000 -6.94600  1.000 9.76021  ? 17  SER   B N     1 
ATOM   121  C  CA    . SER   A 1 18  ? 54.42500  -31.37800 -6.87600  1.000 12.82510 ? 17  SER   B CA    1 
ATOM   122  C  C     . SER   A 1 18  ? 54.74800  -31.98300 -8.23700  1.000 11.18713 ? 17  SER   B C     1 
ATOM   123  O  O     . SER   A 1 18  ? 55.91800  -32.01600 -8.63700  1.000 10.89786 ? 17  SER   B O     1 
ATOM   124  C  CB    . SER   A 1 18  ? 54.19800  -32.47800 -5.83500  1.000 9.58015  ? 17  SER   B CB    1 
ATOM   125  O  OG    . SER   A 1 18  ? 54.12500  -31.94300 -4.52500  1.000 9.21903  ? 17  SER   B OG    1 
ATOM   126  N  N     . ALA   A 1 19  ? 53.72700  -32.47600 -8.95200  1.000 9.96396  ? 18  ALA   B N     1 
ATOM   127  C  CA    . ALA   A 1 19  ? 53.94900  -33.04500 -10.27700 1.000 12.80513 ? 18  ALA   B CA    1 
ATOM   128  C  C     . ALA   A 1 19  ? 54.60400  -32.03300 -11.21200 1.000 10.58366 ? 18  ALA   B C     1 
ATOM   129  O  O     . ALA   A 1 19  ? 55.54200  -32.37100 -11.94500 1.000 14.17859 ? 18  ALA   B O     1 
ATOM   130  C  CB    . ALA   A 1 19  ? 52.62300  -33.54500 -10.86200 1.000 9.48693  ? 18  ALA   B CB    1 
ATOM   131  N  N     . LEU   A 1 20  ? 54.15600  -30.77600 -11.16600 1.000 8.26233  ? 19  LEU   B N     1 
ATOM   132  C  CA    . LEU   A 1 20  ? 54.79600  -29.73200 -11.96200 1.000 8.13274  ? 19  LEU   B CA    1 
ATOM   133  C  C     . LEU   A 1 20  ? 56.24800  -29.54800 -11.55300 1.000 12.37375 ? 19  LEU   B C     1 
ATOM   134  O  O     . LEU   A 1 20  ? 57.14000  -29.49600 -12.40400 1.000 11.61257 ? 19  LEU   B O     1 
ATOM   135  C  CB    . LEU   A 1 20  ? 54.03200  -28.41200 -11.84000 1.000 9.12364  ? 19  LEU   B CB    1 
ATOM   136  C  CG    . LEU   A 1 20  ? 52.67200  -28.37700 -12.55700 1.000 8.64874  ? 19  LEU   B CG    1 
ATOM   137  C  CD1   . LEU   A 1 20  ? 51.85100  -27.18300 -12.11800 1.000 8.66249  ? 19  LEU   B CD1   1 
ATOM   138  C  CD2   . LEU   A 1 20  ? 52.84900  -28.39400 -14.10300 1.000 13.71838 ? 19  LEU   B CD2   1 
ATOM   139  N  N     . THR   A 1 21  ? 56.51300  -29.50000 -10.24900 1.000 10.62878 ? 20  THR   B N     1 
ATOM   140  C  CA    . THR   A 1 21  ? 57.89300  -29.31800 -9.80400  1.000 12.80858 ? 20  THR   B CA    1 
ATOM   141  C  C     . THR   A 1 21  ? 58.75500  -30.50900 -10.20900 1.000 11.58023 ? 20  THR   B C     1 
ATOM   142  O  O     . THR   A 1 21  ? 59.88100  -30.33900 -10.68800 1.000 11.25273 ? 20  THR   B O     1 
ATOM   143  C  CB    . THR   A 1 21  ? 57.93000  -29.10000 -8.29000  1.000 9.20533  ? 20  THR   B CB    1 
ATOM   144  O  OG1   . THR   A 1 21  ? 57.17100  -27.92900 -7.95600  1.000 16.29852 ? 20  THR   B OG1   1 
ATOM   145  C  CG2   . THR   A 1 21  ? 59.37800  -28.89400 -7.79400  1.000 10.48145 ? 20  THR   B CG2   1 
ATOM   146  N  N     . ILE   A 1 22  ? 58.23000  -31.72700 -10.05000 1.000 11.81916 ? 21  ILE   B N     1 
ATOM   147  C  CA    . ILE   A 1 22  ? 59.02900  -32.91200 -10.32800 1.000 14.33981 ? 21  ILE   B CA    1 
ATOM   148  C  C     . ILE   A 1 22  ? 59.30100  -33.04500 -11.82500 1.000 14.30538 ? 21  ILE   B C     1 
ATOM   149  O  O     . ILE   A 1 22  ? 60.37300  -33.52400 -12.22500 1.000 16.54550 ? 21  ILE   B O     1 
ATOM   150  C  CB    . ILE   A 1 22  ? 58.33100  -34.14500 -9.72300  1.000 16.16423 ? 21  ILE   B CB    1 
ATOM   151  C  CG1   . ILE   A 1 22  ? 58.41500  -34.07500 -8.19400  1.000 14.92387 ? 21  ILE   B CG1   1 
ATOM   152  C  CG2   . ILE   A 1 22  ? 58.93400  -35.42800 -10.22200 1.000 14.68720 ? 21  ILE   B CG2   1 
ATOM   153  C  CD1   . ILE   A 1 22  ? 57.35900  -34.85900 -7.49500  1.000 21.06690 ? 21  ILE   B CD1   1 
ATOM   154  N  N     . GLN   A 1 23  ? 58.38100  -32.57700 -12.67300 1.000 12.14090 ? 22  GLN   B N     1 
ATOM   155  C  CA    . GLN   A 1 23  ? 58.67100  -32.50200 -14.10700 1.000 16.41438 ? 22  GLN   B CA    1 
ATOM   156  C  C     . GLN   A 1 23  ? 59.80000  -31.52000 -14.39000 1.000 19.30124 ? 22  GLN   B C     1 
ATOM   157  O  O     . GLN   A 1 23  ? 60.72600  -31.82500 -15.15000 1.000 18.51610 ? 22  GLN   B O     1 
ATOM   158  C  CB    . GLN   A 1 23  ? 57.42700  -32.10000 -14.90100 1.000 13.66472 ? 22  GLN   B CB    1 
ATOM   159  C  CG    . GLN   A 1 23  ? 56.61500  -33.25400 -15.39600 1.000 16.80417 ? 22  GLN   B CG    1 
ATOM   160  C  CD    . GLN   A 1 23  ? 57.25800  -34.01300 -16.54600 1.000 17.80810 ? 22  GLN   B CD    1 
ATOM   161  O  OE1   . GLN   A 1 23  ? 58.43100  -33.81500 -16.89000 1.000 16.18108 ? 22  GLN   B OE1   1 
ATOM   162  N  NE2   . GLN   A 1 23  ? 56.48400  -34.89300 -17.14900 1.000 13.58019 ? 22  GLN   B NE2   1 
ATOM   163  N  N     . LEU   A 1 24  ? 59.74700  -30.33500 -13.78000 1.000 13.95832 ? 23  LEU   B N     1 
ATOM   164  C  CA    . LEU   A 1 24  ? 60.81700  -29.37400 -14.01900 1.000 14.74683 ? 23  LEU   B CA    1 
ATOM   165  C  C     . LEU   A 1 24  ? 62.15900  -29.91300 -13.53900 1.000 18.61034 ? 23  LEU   B C     1 
ATOM   166  O  O     . LEU   A 1 24  ? 63.16500  -29.78800 -14.24600 1.000 20.59520 ? 23  LEU   B O     1 
ATOM   167  C  CB    . LEU   A 1 24  ? 60.50000  -28.03700 -13.34800 1.000 17.59600 ? 23  LEU   B CB    1 
ATOM   168  C  CG    . LEU   A 1 24  ? 61.56000  -26.95500 -13.58100 1.000 13.79482 ? 23  LEU   B CG    1 
ATOM   169  C  CD1   . LEU   A 1 24  ? 61.36900  -26.23100 -14.90600 1.000 14.66676 ? 23  LEU   B CD1   1 
ATOM   170  C  CD2   . LEU   A 1 24  ? 61.54200  -25.98300 -12.44700 1.000 14.28068 ? 23  LEU   B CD2   1 
ATOM   171  N  N     . ILE   A 1 25  ? 62.18800  -30.53900 -12.35800 1.000 13.09500 ? 24  ILE   B N     1 
ATOM   172  C  CA    . ILE   A 1 25  ? 63.44600  -30.95400 -11.73900 1.000 19.67667 ? 24  ILE   B CA    1 
ATOM   173  C  C     . ILE   A 1 25  ? 63.92700  -32.28700 -12.30700 1.000 20.99339 ? 24  ILE   B C     1 
ATOM   174  O  O     . ILE   A 1 25  ? 65.11000  -32.45200 -12.61600 1.000 20.61152 ? 24  ILE   B O     1 
ATOM   175  C  CB    . ILE   A 1 25  ? 63.29500  -31.03900 -10.20400 1.000 17.23886 ? 24  ILE   B CB    1 
ATOM   176  C  CG1   . ILE   A 1 25  ? 62.93700  -29.68700 -9.58800  1.000 16.25288 ? 24  ILE   B CG1   1 
ATOM   177  C  CG2   . ILE   A 1 25  ? 64.55900  -31.65000 -9.55900  1.000 18.60028 ? 24  ILE   B CG2   1 
ATOM   178  C  CD1   . ILE   A 1 25  ? 63.99700  -28.60000 -9.78100  1.000 20.69320 ? 24  ILE   B CD1   1 
ATOM   179  N  N     . GLN   A 1 26  ? 63.03900  -33.27400 -12.41000 1.000 19.13790 ? 25  GLN   B N     1 
ATOM   180  C  CA    . GLN   A 1 26  ? 63.44400  -34.64900 -12.67500 1.000 19.02791 ? 25  GLN   B CA    1 
ATOM   181  C  C     . GLN   A 1 26  ? 62.98600  -35.18500 -14.02600 1.000 19.75787 ? 25  GLN   B C     1 
ATOM   182  O  O     . GLN   A 1 26  ? 63.35100  -36.30900 -14.37000 1.000 22.51377 ? 25  GLN   B O     1 
ATOM   183  C  CB    . GLN   A 1 26  ? 62.93600  -35.55900 -11.54900 1.000 16.92408 ? 25  GLN   B CB    1 
ATOM   184  C  CG    . GLN   A 1 26  ? 63.47700  -35.16500 -10.17800 1.000 18.81436 ? 25  GLN   B CG    1 
ATOM   185  C  CD    . GLN   A 1 26  ? 62.90200  -35.98300 -9.03700  1.000 25.34455 ? 25  GLN   B CD    1 
ATOM   186  O  OE1   . GLN   A 1 26  ? 62.06800  -36.86400 -9.24200  1.000 30.41936 ? 25  GLN   B OE1   1 
ATOM   187  N  NE2   . GLN   A 1 26  ? 63.33900  -35.68200 -7.81700  1.000 27.31285 ? 25  GLN   B NE2   1 
ATOM   188  N  N     . ASN   A 1 27  ? 62.21400  -34.41600 -14.79700 1.000 16.05051 ? 26  ASN   B N     1 
ATOM   189  C  CA    . ASN   A 1 27  ? 61.76100  -34.79100 -16.14500 1.000 22.05281 ? 26  ASN   B CA    1 
ATOM   190  C  C     . ASN   A 1 27  ? 61.05200  -36.14000 -16.16500 1.000 17.99642 ? 26  ASN   B C     1 
ATOM   191  O  O     . ASN   A 1 27  ? 61.29900  -36.97400 -17.03600 1.000 22.57608 ? 26  ASN   B O     1 
ATOM   192  C  CB    . ASN   A 1 27  ? 62.91500  -34.80700 -17.15400 1.000 19.25057 ? 26  ASN   B CB    1 
ATOM   193  C  CG    . ASN   A 1 27  ? 63.57000  -33.45900 -17.31900 1.000 35.68891 ? 26  ASN   B CG    1 
ATOM   194  O  OD1   . ASN   A 1 27  ? 63.12400  -32.63100 -18.12000 1.000 40.85191 ? 26  ASN   B OD1   1 
ATOM   195  N  ND2   . ASN   A 1 27  ? 64.65100  -33.23000 -16.56600 1.000 36.04279 ? 26  ASN   B ND2   1 
ATOM   196  N  N     . HIS   A 1 28  ? 60.16200  -36.35700 -15.19900 1.000 19.92834 ? 27  HIS   B N     1 
ATOM   197  C  CA    . HIS   A 1 28  ? 59.24500  -37.48800 -15.28000 1.000 20.78754 ? 27  HIS   B CA    1 
ATOM   198  C  C     . HIS   A 1 28  ? 57.97200  -37.16300 -14.51000 1.000 16.81570 ? 27  HIS   B C     1 
ATOM   199  O  O     . HIS   A 1 28  ? 57.89500  -36.16800 -13.78600 1.000 18.84996 ? 27  HIS   B O     1 
ATOM   200  C  CB    . HIS   A 1 28  ? 59.89100  -38.78600 -14.77800 1.000 23.62052 ? 27  HIS   B CB    1 
ATOM   201  C  CG    . HIS   A 1 28  ? 60.29100  -38.75400 -13.33600 1.000 24.40721 ? 27  HIS   B CG    1 
ATOM   202  N  ND1   . HIS   A 1 28  ? 59.42300  -39.07800 -12.31400 1.000 31.37364 ? 27  HIS   B ND1   1 
ATOM   203  C  CD2   . HIS   A 1 28  ? 61.47600  -38.46700 -12.74500 1.000 32.36306 ? 27  HIS   B CD2   1 
ATOM   204  C  CE1   . HIS   A 1 28  ? 60.04800  -38.96700 -11.15500 1.000 33.56235 ? 27  HIS   B CE1   1 
ATOM   205  N  NE2   . HIS   A 1 28  ? 61.29600  -38.59900 -11.38900 1.000 33.64138 ? 27  HIS   B NE2   1 
ATOM   206  N  N     . PHE   A 1 29  ? 56.96300  -38.01600 -14.68700 1.000 17.22414 ? 28  PHE   B N     1 
ATOM   207  C  CA    . PHE   A 1 29  ? 55.64700  -37.84500 -14.07900 1.000 16.79790 ? 28  PHE   B CA    1 
ATOM   208  C  C     . PHE   A 1 29  ? 55.12600  -39.21100 -13.66000 1.000 21.08855 ? 28  PHE   B C     1 
ATOM   209  O  O     . PHE   A 1 29  ? 55.32100  -40.19300 -14.37900 1.000 23.54528 ? 28  PHE   B O     1 
ATOM   210  C  CB    . PHE   A 1 29  ? 54.67000  -37.19000 -15.06700 1.000 18.50348 ? 28  PHE   B CB    1 
ATOM   211  C  CG    . PHE   A 1 29  ? 53.20600  -37.29300 -14.66900 1.000 16.61856 ? 28  PHE   B CG    1 
ATOM   212  C  CD1   . PHE   A 1 29  ? 52.63500  -36.34900 -13.83400 1.000 15.51412 ? 28  PHE   B CD1   1 
ATOM   213  C  CD2   . PHE   A 1 29  ? 52.40100  -38.31600 -15.15400 1.000 21.23817 ? 28  PHE   B CD2   1 
ATOM   214  C  CE1   . PHE   A 1 29  ? 51.29800  -36.42900 -13.48300 1.000 15.67654 ? 28  PHE   B CE1   1 
ATOM   215  C  CE2   . PHE   A 1 29  ? 51.06800  -38.40100 -14.80200 1.000 18.20976 ? 28  PHE   B CE2   1 
ATOM   216  C  CZ    . PHE   A 1 29  ? 50.51600  -37.45500 -13.96600 1.000 15.52896 ? 28  PHE   B CZ    1 
ATOM   217  N  N     . VAL   A 1 30  ? 54.46700  -39.27500 -12.50100 1.000 24.22642 ? 29  VAL   B N     1 
ATOM   218  C  CA    . VAL   A 1 30  ? 53.81900  -40.50000 -12.04600 1.000 24.48854 ? 29  VAL   B CA    1 
ATOM   219  C  C     . VAL   A 1 30  ? 52.39200  -40.18800 -11.62700 1.000 20.86195 ? 29  VAL   B C     1 
ATOM   220  O  O     . VAL   A 1 30  ? 52.09500  -39.10700 -11.11000 1.000 20.70637 ? 29  VAL   B O     1 
ATOM   221  C  CB    . VAL   A 1 30  ? 54.55500  -41.19400 -10.87300 1.000 29.92557 ? 29  VAL   B CB    1 
ATOM   222  C  CG1   . VAL   A 1 30  ? 55.86000  -41.85600 -11.34400 1.000 28.91006 ? 29  VAL   B CG1   1 
ATOM   223  C  CG2   . VAL   A 1 30  ? 54.77300  -40.20600 -9.71400  1.000 27.01135 ? 29  VAL   B CG2   1 
ATOM   224  N  N     . ASP   A 1 31  ? 51.51700  -41.17700 -11.82400 1.000 23.34481 ? 30  ASP   B N     1 
ATOM   225  C  CA    . ASP   A 1 31  ? 50.11200  -41.05300 -11.45200 1.000 23.59386 ? 30  ASP   B CA    1 
ATOM   226  C  C     . ASP   A 1 31  ? 49.90000  -41.09200 -9.94500  1.000 23.00587 ? 30  ASP   B C     1 
ATOM   227  O  O     . ASP   A 1 31  ? 48.89700  -40.55700 -9.45200  1.000 19.55894 ? 30  ASP   B O     1 
ATOM   228  C  CB    . ASP   A 1 31  ? 49.31500  -42.18200 -12.10200 1.000 29.57523 ? 30  ASP   B CB    1 
ATOM   229  C  CG    . ASP   A 1 31  ? 48.99300  -41.90000 -13.54300 1.000 34.61867 ? 30  ASP   B CG    1 
ATOM   230  O  OD1   . ASP   A 1 31  ? 48.55000  -40.76500 -13.83400 1.000 32.06233 ? 30  ASP   B OD1   1 
ATOM   231  O  OD2   . ASP   A 1 31  ? 49.18900  -42.80600 -14.38200 1.000 34.46635 ? 30  ASP   B OD2   1 
ATOM   232  N  N     . GLU   A 1 32  ? 50.78500  -41.76800 -9.21000  1.000 21.96267 ? 31  GLU   B N     1 
ATOM   233  C  CA    . GLU   A 1 32  ? 50.58000  -41.95700 -7.77900  1.000 21.83633 ? 31  GLU   B CA    1 
ATOM   234  C  C     . GLU   A 1 32  ? 50.63900  -40.61200 -7.06300  1.000 18.06101 ? 31  GLU   B C     1 
ATOM   235  O  O     . GLU   A 1 32  ? 51.50500  -39.78000 -7.34000  1.000 20.90044 ? 31  GLU   B O     1 
ATOM   236  C  CB    . GLU   A 1 32  ? 51.63600  -42.91700 -7.21800  1.000 29.84316 ? 31  GLU   B CB    1 
ATOM   237  C  CG    . GLU   A 1 32  ? 51.45600  -43.30800 -5.74800  1.000 28.33105 ? 31  GLU   B CG    1 
ATOM   238  C  CD    . GLU   A 1 32  ? 52.28300  -44.53600 -5.36000  1.000 34.65127 ? 31  GLU   B CD    1 
ATOM   239  O  OE1   . GLU   A 1 32  ? 53.40900  -44.69300 -5.88100  1.000 43.99998 ? 31  GLU   B OE1   1 
ATOM   240  O  OE2   . GLU   A 1 32  ? 51.80000  -45.34900 -4.54300  1.000 34.12854 ? 31  GLU   B OE2   1 
ATOM   241  N  N     . TYR   A 1 33  ? 49.69800  -40.39400 -6.15700  1.000 18.56133 ? 32  TYR   B N     1 
ATOM   242  C  CA    . TYR   A 1 33  ? 49.61300  -39.14800 -5.40500  1.000 14.30707 ? 32  TYR   B CA    1 
ATOM   243  C  C     . TYR   A 1 33  ? 50.39700  -39.31300 -4.11200  1.000 14.82401 ? 32  TYR   B C     1 
ATOM   244  O  O     . TYR   A 1 33  ? 50.08700  -40.19400 -3.30200  1.000 13.96521 ? 32  TYR   B O     1 
ATOM   245  C  CB    . TYR   A 1 33  ? 48.14500  -38.81100 -5.13300  1.000 14.15446 ? 32  TYR   B CB    1 
ATOM   246  C  CG    . TYR   A 1 33  ? 47.82900  -37.57300 -4.30200  1.000 15.68298 ? 32  TYR   B CG    1 
ATOM   247  C  CD1   . TYR   A 1 33  ? 48.76800  -36.56400 -4.06100  1.000 11.16226 ? 32  TYR   B CD1   1 
ATOM   248  C  CD2   . TYR   A 1 33  ? 46.55400  -37.42300 -3.76200  1.000 15.47880 ? 32  TYR   B CD2   1 
ATOM   249  C  CE1   . TYR   A 1 33  ? 48.41600  -35.43900 -3.28700  1.000 11.59038 ? 32  TYR   B CE1   1 
ATOM   250  C  CE2   . TYR   A 1 33  ? 46.19900  -36.32900 -3.01400  1.000 11.91402 ? 32  TYR   B CE2   1 
ATOM   251  C  CZ    . TYR   A 1 33  ? 47.12200  -35.34300 -2.76500  1.000 12.96848 ? 32  TYR   B CZ    1 
ATOM   252  O  OH    . TYR   A 1 33  ? 46.69200  -34.27700 -2.00400  1.000 10.84468 ? 32  TYR   B OH    1 
ATOM   253  N  N     . ASP   A 1 34  ? 51.42500  -38.48300 -3.92900  1.000 12.15132 ? 33  ASP   B N     1 
ATOM   254  C  CA    . ASP   A 1 34  ? 52.18200  -38.47300 -2.68300  1.000 12.50230 ? 33  ASP   B CA    1 
ATOM   255  C  C     . ASP   A 1 34  ? 51.96000  -37.12300 -2.02100  1.000 11.48695 ? 33  ASP   B C     1 
ATOM   256  O  O     . ASP   A 1 34  ? 52.67000  -36.15400 -2.34400  1.000 10.75133 ? 33  ASP   B O     1 
ATOM   257  C  CB    . ASP   A 1 34  ? 53.67600  -38.71300 -2.94700  1.000 12.54333 ? 33  ASP   B CB    1 
ATOM   258  C  CG    . ASP   A 1 34  ? 54.48400  -38.90500 -1.67100  1.000 15.67038 ? 33  ASP   B CG    1 
ATOM   259  O  OD1   . ASP   A 1 34  ? 53.89600  -38.97000 -0.56900  1.000 13.29938 ? 33  ASP   B OD1   1 
ATOM   260  O  OD2   . ASP   A 1 34  ? 55.72800  -38.97300 -1.77400  1.000 19.74020 ? 33  ASP   B OD2   1 
ATOM   261  N  N     . PRO   A 1 35  ? 51.01400  -37.01000 -1.08100  1.000 11.71914 ? 34  PRO   B N     1 
ATOM   262  C  CA    . PRO   A 1 35  ? 50.63900  -35.69000 -0.53600  1.000 11.09100 ? 34  PRO   B CA    1 
ATOM   263  C  C     . PRO   A 1 35  ? 51.79700  -35.02000 0.19200   1.000 11.46770 ? 34  PRO   B C     1 
ATOM   264  O  O     . PRO   A 1 35  ? 52.47500  -35.63300 1.01300   1.000 12.12197 ? 34  PRO   B O     1 
ATOM   265  C  CB    . PRO   A 1 35  ? 49.48600  -36.00800 0.42400   1.000 11.80356 ? 34  PRO   B CB    1 
ATOM   266  C  CG    . PRO   A 1 35  ? 48.94800  -37.34600 -0.04200  1.000 12.58199 ? 34  PRO   B CG    1 
ATOM   267  C  CD    . PRO   A 1 35  ? 50.18500  -38.09000 -0.53100  1.000 12.72559 ? 34  PRO   B CD    1 
ATOM   268  N  N     . THR   A 1 36  ? 51.99200  -33.74200 -0.10800  1.000 10.01663 ? 35  THR   B N     1 
ATOM   269  C  CA    . THR   A 1 36  ? 53.18000  -33.00100 0.30700   1.000 9.74389  ? 35  THR   B CA    1 
ATOM   270  C  C     . THR   A 1 36  ? 53.05200  -32.49900 1.74400   1.000 11.95289 ? 35  THR   B C     1 
ATOM   271  O  O     . THR   A 1 36  ? 51.98000  -32.07300 2.17000   1.000 10.29883 ? 35  THR   B O     1 
ATOM   272  C  CB    . THR   A 1 36  ? 53.38800  -31.82000 -0.65200  1.000 9.13489  ? 35  THR   B CB    1 
ATOM   273  O  OG1   . THR   A 1 36  ? 53.62200  -32.31600 -1.98100  1.000 8.69932  ? 35  THR   B OG1   1 
ATOM   274  C  CG2   . THR   A 1 36  ? 54.55500  -30.90700 -0.22800  1.000 8.63085  ? 35  THR   B CG2   1 
ATOM   275  N  N     . ILE   A 1 37  ? 54.15900  -32.54900 2.50100   1.000 11.19669 ? 36  ILE   B N     1 
ATOM   276  C  CA    . ILE   A 1 37  ? 54.24700  -31.76400 3.73100   1.000 10.82736 ? 36  ILE   B CA    1 
ATOM   277  C  C     . ILE   A 1 37  ? 54.98400  -30.48400 3.35700   1.000 10.52268 ? 36  ILE   B C     1 
ATOM   278  O  O     . ILE   A 1 37  ? 54.42300  -29.38700 3.40300   1.000 10.33893 ? 36  ILE   B O     1 
ATOM   279  C  CB    . ILE   A 1 37  ? 54.95800  -32.52300 4.87300   1.000 11.90987 ? 36  ILE   B CB    1 
ATOM   280  C  CG1   . ILE   A 1 37  ? 54.14900  -33.74600 5.31200   1.000 13.67950 ? 36  ILE   B CG1   1 
ATOM   281  C  CG2   . ILE   A 1 37  ? 55.24400  -31.59200 6.06600   1.000 12.32681 ? 36  ILE   B CG2   1 
ATOM   282  C  CD1   . ILE   A 1 37  ? 52.89600  -33.42600 6.12600   1.000 13.16886 ? 36  ILE   B CD1   1 
ATOM   283  N  N     . GLU   A 1 38  ? 56.23500  -30.63400 2.93200   1.000 10.05927 ? 37  GLU   B N     1 
ATOM   284  C  CA    . GLU   A 1 38  ? 57.02200  -29.53400 2.40800   1.000 10.15070 ? 37  GLU   B CA    1 
ATOM   285  C  C     . GLU   A 1 38  ? 58.24500  -30.10500 1.70900   1.000 10.68788 ? 37  GLU   B C     1 
ATOM   286  O  O     . GLU   A 1 38  ? 58.87800  -31.01300 2.24900   1.000 12.56421 ? 37  GLU   B O     1 
ATOM   287  C  CB    . GLU   A 1 38  ? 57.45300  -28.58800 3.52600   1.000 10.84099 ? 37  GLU   B CB    1 
ATOM   288  C  CG    . GLU   A 1 38  ? 58.13000  -27.34200 2.99300   1.000 11.17199 ? 37  GLU   B CG    1 
ATOM   289  C  CD    . GLU   A 1 38  ? 58.90900  -26.63000 4.06000   1.000 16.51588 ? 37  GLU   B CD    1 
ATOM   290  O  OE1   . GLU   A 1 38  ? 58.27600  -25.98200 4.91200   1.000 14.91374 ? 37  GLU   B OE1   1 
ATOM   291  O  OE2   . GLU   A 1 38  ? 60.15200  -26.76400 4.06600   1.000 15.93935 ? 37  GLU   B OE2   1 
ATOM   292  N  N     . ASP   A 1 39  ? 58.59200  -29.59700 0.52800   1.000 12.16686 ? 38  ASP   B N     1 
ATOM   293  C  CA    . ASP   A 1 39  ? 59.79500  -30.05500 -0.15600  1.000 14.71573 ? 38  ASP   B CA    1 
ATOM   294  C  C     . ASP   A 1 39  ? 60.49000  -28.89800 -0.85300  1.000 11.00785 ? 38  ASP   B C     1 
ATOM   295  O  O     . ASP   A 1 39  ? 59.85800  -27.91500 -1.24200  1.000 11.54639 ? 38  ASP   B O     1 
ATOM   296  C  CB    . ASP   A 1 39  ? 59.48100  -31.17000 -1.16100  1.000 13.89684 ? 38  ASP   B CB    1 
ATOM   297  C  CG    . ASP   A 1 39  ? 59.14500  -32.48500 -0.47800  1.000 13.08417 ? 38  ASP   B CG    1 
ATOM   298  O  OD1   . ASP   A 1 39  ? 60.03600  -33.11200 0.12200   1.000 13.29311 ? 38  ASP   B OD1   1 
ATOM   299  O  OD2   . ASP   A 1 39  ? 57.97300  -32.88900 -0.51300  1.000 17.34513 ? 38  ASP   B OD2   1 
ATOM   300  N  N     . SER   A 1 40  ? 61.81500  -29.01900 -0.98500  1.000 12.85898 ? 39  SER   B N     1 
ATOM   301  C  CA    . SER   A 1 40  ? 62.63800  -27.99900 -1.61900  1.000 16.67718 ? 39  SER   B CA    1 
ATOM   302  C  C     . SER   A 1 40  ? 63.53300  -28.62900 -2.67500  1.000 16.00561 ? 39  SER   B C     1 
ATOM   303  O  O     . SER   A 1 40  ? 63.94500  -29.78700 -2.56100  1.000 21.56004 ? 39  SER   B O     1 
ATOM   304  C  CB    . SER   A 1 40  ? 63.50500  -27.25300 -0.59800  1.000 17.05941 ? 39  SER   B CB    1 
ATOM   305  O  OG    . SER   A 1 40  ? 62.69700  -26.54500 0.32100   1.000 22.35945 ? 39  SER   B OG    1 
ATOM   306  N  N     . TYR   A 1 41  ? 63.83400  -27.84000 -3.70500  1.000 15.45881 ? 40  TYR   B N     1 
ATOM   307  C  CA    . TYR   A 1 41  ? 64.63100  -28.28400 -4.83600  1.000 14.56933 ? 40  TYR   B CA    1 
ATOM   308  C  C     . TYR   A 1 41  ? 65.44700  -27.11000 -5.34900  1.000 13.82884 ? 40  TYR   B C     1 
ATOM   309  O  O     . TYR   A 1 41  ? 65.02200  -25.95600 -5.25700  1.000 12.47213 ? 40  TYR   B O     1 
ATOM   310  C  CB    . TYR   A 1 41  ? 63.75600  -28.82900 -5.96400  1.000 13.23571 ? 40  TYR   B CB    1 
ATOM   311  C  CG    . TYR   A 1 41  ? 62.79800  -29.91200 -5.51200  1.000 18.03650 ? 40  TYR   B CG    1 
ATOM   312  C  CD1   . TYR   A 1 41  ? 63.19200  -31.23800 -5.47300  1.000 17.14021 ? 40  TYR   B CD1   1 
ATOM   313  C  CD2   . TYR   A 1 41  ? 61.50500  -29.59700 -5.11000  1.000 13.76490 ? 40  TYR   B CD2   1 
ATOM   314  C  CE1   . TYR   A 1 41  ? 62.31900  -32.22900 -5.04500  1.000 21.84251 ? 40  TYR   B CE1   1 
ATOM   315  C  CE2   . TYR   A 1 41  ? 60.63500  -30.57000 -4.69100  1.000 12.81225 ? 40  TYR   B CE2   1 
ATOM   316  C  CZ    . TYR   A 1 41  ? 61.04300  -31.88600 -4.65900  1.000 18.93366 ? 40  TYR   B CZ    1 
ATOM   317  O  OH    . TYR   A 1 41  ? 60.15800  -32.85300 -4.23300  1.000 17.73116 ? 40  TYR   B OH    1 
ATOM   318  N  N     . ARG   A 1 42  ? 66.62600  -27.41800 -5.88100  1.000 13.94542 ? 41  ARG   B N     1 
ATOM   319  C  CA    . ARG   A 1 42  ? 67.48600  -26.46000 -6.56400  1.000 13.25794 ? 41  ARG   B CA    1 
ATOM   320  C  C     . ARG   A 1 42  ? 67.76100  -26.97200 -7.97000  1.000 16.84040 ? 41  ARG   B C     1 
ATOM   321  O  O     . ARG   A 1 42  ? 67.97900  -28.17300 -8.16200  1.000 18.31301 ? 41  ARG   B O     1 
ATOM   322  C  CB    . ARG   A 1 42  ? 68.82100  -26.26100 -5.80800  1.000 18.59697 ? 41  ARG   B CB    1 
ATOM   323  C  CG    . ARG   A 1 42  ? 68.66400  -25.49700 -4.50800  1.000 20.19887 ? 41  ARG   B CG    1 
ATOM   324  C  CD    . ARG   A 1 42  ? 69.88200  -25.61700 -3.61500  1.000 18.46852 ? 41  ARG   B CD    1 
ATOM   325  N  NE    . ARG   A 1 42  ? 71.12500  -25.15300 -4.22200  1.000 21.94743 ? 41  ARG   B NE    1 
ATOM   326  C  CZ    . ARG   A 1 42  ? 71.57800  -23.90400 -4.17400  1.000 23.34867 ? 41  ARG   B CZ    1 
ATOM   327  N  NH1   . ARG   A 1 42  ? 70.84700  -22.91200 -3.68200  1.000 22.75402 ? 41  ARG   B NH1   1 
ATOM   328  N  NH2   . ARG   A 1 42  ? 72.79700  -23.64000 -4.62700  1.000 26.64566 ? 41  ARG   B NH2   1 
ATOM   329  N  N     . LYS   A 1 43  ? 67.72900  -26.06800 -8.95000  1.000 13.63442 ? 42  LYS   B N     1 
ATOM   330  C  CA    . LYS   A 1 43  ? 68.04600  -26.41000 -10.33300 1.000 16.50066 ? 42  LYS   B CA    1 
ATOM   331  C  C     . LYS   A 1 43  ? 68.66200  -25.20800 -11.03100 1.000 16.22388 ? 42  LYS   B C     1 
ATOM   332  O  O     . LYS   A 1 43  ? 68.13100  -24.09800 -10.93600 1.000 18.94791 ? 42  LYS   B O     1 
ATOM   333  C  CB    . LYS   A 1 43  ? 66.80200  -26.86000 -11.11000 1.000 18.97532 ? 42  LYS   B CB    1 
ATOM   334  C  CG    . LYS   A 1 43  ? 67.12800  -27.26700 -12.54900 1.000 22.60677 ? 42  LYS   B CG    1 
ATOM   335  C  CD    . LYS   A 1 43  ? 65.92100  -27.79500 -13.29900 1.000 26.76448 ? 42  LYS   B CD    1 
ATOM   336  C  CE    . LYS   A 1 43  ? 66.34600  -28.53700 -14.55600 1.000 24.79841 ? 42  LYS   B CE    1 
ATOM   337  N  NZ    . LYS   A 1 43  ? 67.06200  -29.82600 -14.24300 1.000 31.83094 ? 42  LYS   B NZ    1 
ATOM   338  N  N     . GLN   A 1 44  ? 69.75900  -25.43100 -11.75000 1.000 13.14867 ? 43  GLN   B N     1 
ATOM   339  C  CA    . GLN   A 1 44  ? 70.38600  -24.36900 -12.52400 1.000 16.01553 ? 43  GLN   B CA    1 
ATOM   340  C  C     . GLN   A 1 44  ? 69.85300  -24.40100 -13.95100 1.000 18.85411 ? 43  GLN   B C     1 
ATOM   341  O  O     . GLN   A 1 44  ? 69.89000  -25.44900 -14.61200 1.000 15.73612 ? 43  GLN   B O     1 
ATOM   342  C  CB    . GLN   A 1 44  ? 71.91100  -24.50700 -12.51200 1.000 16.19281 ? 43  GLN   B CB    1 
ATOM   343  C  CG    . GLN   A 1 44  ? 72.63100  -23.52100 -13.42600 1.000 16.36986 ? 43  GLN   B CG    1 
ATOM   344  C  CD    . GLN   A 1 44  ? 74.14500  -23.59600 -13.30200 1.000 27.36556 ? 43  GLN   B CD    1 
ATOM   345  O  OE1   . GLN   A 1 44  ? 74.68300  -23.71300 -12.19900 1.000 35.70667 ? 43  GLN   B OE1   1 
ATOM   346  N  NE2   . GLN   A 1 44  ? 74.84000  -23.52700 -14.43300 1.000 26.43542 ? 43  GLN   B NE2   1 
ATOM   347  N  N     . VAL   A 1 45  ? 69.34600  -23.25100 -14.41100 1.000 13.36144 ? 44  VAL   B N     1 
ATOM   348  C  CA    . VAL   A 1 45  ? 68.74600  -23.10100 -15.72800 1.000 15.11326 ? 44  VAL   B CA    1 
ATOM   349  C  C     . VAL   A 1 45  ? 69.35800  -21.88800 -16.40700 1.000 14.47876 ? 44  VAL   B C     1 
ATOM   350  O  O     . VAL   A 1 45  ? 70.06100  -21.08800 -15.79000 1.000 16.35937 ? 44  VAL   B O     1 
ATOM   351  C  CB    . VAL   A 1 45  ? 67.21500  -22.94000 -15.65400 1.000 18.01868 ? 44  VAL   B CB    1 
ATOM   352  C  CG1   . VAL   A 1 45  ? 66.58400  -24.20100 -15.06500 1.000 21.93571 ? 44  VAL   B CG1   1 
ATOM   353  C  CG2   . VAL   A 1 45  ? 66.87000  -21.72800 -14.80700 1.000 15.75273 ? 44  VAL   B CG2   1 
ATOM   354  N  N     . VAL   A 1 46  ? 69.10200  -21.77700 -17.70400 1.000 16.25475 ? 45  VAL   B N     1 
ATOM   355  C  CA    . VAL   A 1 46  ? 69.43200  -20.58300 -18.47500 1.000 15.52722 ? 45  VAL   B CA    1 
ATOM   356  C  C     . VAL   A 1 46  ? 68.11700  -20.05300 -19.02700 1.000 17.72488 ? 45  VAL   B C     1 
ATOM   357  O  O     . VAL   A 1 46  ? 67.40500  -20.77300 -19.73900 1.000 16.02175 ? 45  VAL   B O     1 
ATOM   358  C  CB    . VAL   A 1 46  ? 70.44400  -20.86800 -19.59500 1.000 17.19594 ? 45  VAL   B CB    1 
ATOM   359  C  CG1   . VAL   A 1 46  ? 70.60200  -19.64300 -20.48300 1.000 17.95875 ? 45  VAL   B CG1   1 
ATOM   360  C  CG2   . VAL   A 1 46  ? 71.79500  -21.30000 -19.01000 1.000 17.95700 ? 45  VAL   B CG2   1 
ATOM   361  N  N     . ILE   A 1 47  ? 67.76400  -18.82700 -18.64900 1.000 14.42087 ? 46  ILE   B N     1 
ATOM   362  C  CA    . ILE   A 1 47  ? 66.52000  -18.19200 -19.07800 1.000 14.33506 ? 46  ILE   B CA    1 
ATOM   363  C  C     . ILE   A 1 47  ? 66.87600  -16.88000 -19.75500 1.000 16.74246 ? 46  ILE   B C     1 
ATOM   364  O  O     . ILE   A 1 47  ? 67.47300  -16.00000 -19.12300 1.000 16.46387 ? 46  ILE   B O     1 
ATOM   365  C  CB    . ILE   A 1 47  ? 65.57300  -17.94300 -17.90000 1.000 13.88711 ? 46  ILE   B CB    1 
ATOM   366  C  CG1   . ILE   A 1 47  ? 65.28800  -19.24300 -17.16000 1.000 11.93416 ? 46  ILE   B CG1   1 
ATOM   367  C  CG2   . ILE   A 1 47  ? 64.25800  -17.31600 -18.37900 1.000 13.01705 ? 46  ILE   B CG2   1 
ATOM   368  C  CD1   . ILE   A 1 47  ? 64.47100  -19.02600 -15.93700 1.000 11.33076 ? 46  ILE   B CD1   1 
ATOM   369  N  N     . ASP   A 1 48  ? 66.50800  -16.74700 -21.02800 1.000 15.71799 ? 47  ASP   B N     1 
ATOM   370  C  CA    . ASP   A 1 48  ? 66.81100  -15.55000 -21.81300 1.000 17.66290 ? 47  ASP   B CA    1 
ATOM   371  C  C     . ASP   A 1 48  ? 68.30700  -15.24600 -21.79200 1.000 17.73820 ? 47  ASP   B C     1 
ATOM   372  O  O     . ASP   A 1 48  ? 68.73300  -14.10400 -21.62600 1.000 18.11807 ? 47  ASP   B O     1 
ATOM   373  C  CB    . ASP   A 1 48  ? 66.00500  -14.34400 -21.32700 1.000 16.18504 ? 47  ASP   B CB    1 
ATOM   374  C  CG    . ASP   A 1 48  ? 64.51300  -14.56500 -21.44700 1.000 15.52111 ? 47  ASP   B CG    1 
ATOM   375  O  OD1   . ASP   A 1 48  ? 64.12200  -15.47200 -22.20800 1.000 21.81539 ? 47  ASP   B OD1   1 
ATOM   376  O  OD2   . ASP   A 1 48  ? 63.73500  -13.85000 -20.78700 1.000 16.94647 ? 47  ASP   B OD2   1 
ATOM   377  N  N     . GLY   A 1 49  ? 69.10900  -16.29600 -21.96700 1.000 18.27181 ? 48  GLY   B N     1 
ATOM   378  C  CA    . GLY   A 1 49  ? 70.54700  -16.14300 -21.98800 1.000 19.38033 ? 48  GLY   B CA    1 
ATOM   379  C  C     . GLY   A 1 49  ? 71.19500  -15.88700 -20.64800 1.000 18.74616 ? 48  GLY   B C     1 
ATOM   380  O  O     . GLY   A 1 49  ? 72.42400  -15.77000 -20.59500 1.000 19.91179 ? 48  GLY   B O     1 
ATOM   381  N  N     . GLU   A 1 50  ? 70.42000  -15.78200 -19.56600 1.000 17.26962 ? 49  GLU   B N     1 
ATOM   382  C  CA    . GLU   A 1 50  ? 70.95300  -15.52000 -18.23100 1.000 20.47824 ? 49  GLU   B CA    1 
ATOM   383  C  C     . GLU   A 1 50  ? 70.84300  -16.78700 -17.38500 1.000 15.91527 ? 49  GLU   B C     1 
ATOM   384  O  O     . GLU   A 1 50  ? 69.76000  -17.35300 -17.24900 1.000 15.01042 ? 49  GLU   B O     1 
ATOM   385  C  CB    . GLU   A 1 50  ? 70.21500  -14.35500 -17.56700 1.000 16.26314 ? 49  GLU   B CB    1 
ATOM   386  C  CG    . GLU   A 1 50  ? 70.30100  -13.06700 -18.38900 1.000 22.42500 ? 49  GLU   B CG    1 
ATOM   387  C  CD    . GLU   A 1 50  ? 69.45400  -11.91700 -17.84500 1.000 27.42268 ? 49  GLU   B CD    1 
ATOM   388  O  OE1   . GLU   A 1 50  ? 68.70200  -12.12200 -16.86300 1.000 19.79945 ? 49  GLU   B OE1   1 
ATOM   389  O  OE2   . GLU   A 1 50  ? 69.55200  -10.80400 -18.42100 1.000 26.88427 ? 49  GLU   B OE2   1 
ATOM   390  N  N     . THR   A 1 51  ? 71.97000  -17.22400 -16.82700 1.000 16.71236 ? 50  THR   B N     1 
ATOM   391  C  CA    . THR   A 1 51  ? 72.02000  -18.42000 -15.99700 1.000 15.96256 ? 50  THR   B CA    1 
ATOM   392  C  C     . THR   A 1 51  ? 71.49000  -18.11900 -14.60300 1.000 17.40168 ? 50  THR   B C     1 
ATOM   393  O  O     . THR   A 1 51  ? 71.86400  -17.11100 -13.99600 1.000 14.85586 ? 50  THR   B O     1 
ATOM   394  C  CB    . THR   A 1 51  ? 73.45900  -18.92600 -15.90600 1.000 20.11114 ? 50  THR   B CB    1 
ATOM   395  O  OG1   . THR   A 1 51  ? 73.93100  -19.25000 -17.21900 1.000 24.50580 ? 50  THR   B OG1   1 
ATOM   396  C  CG2   . THR   A 1 51  ? 73.55100  -20.14900 -15.00200 1.000 17.83281 ? 50  THR   B CG2   1 
ATOM   397  N  N     . SER   A 1 52  ? 70.63100  -18.99700 -14.08100 1.000 13.79622 ? 51  SER   B N     1 
ATOM   398  C  CA    . SER   A 1 52  ? 70.05800  -18.75400 -12.76500 1.000 16.13908 ? 51  SER   B CA    1 
ATOM   399  C  C     . SER   A 1 52  ? 69.90000  -20.05500 -11.99300 1.000 15.66704 ? 51  SER   B C     1 
ATOM   400  O  O     . SER   A 1 52  ? 69.69500  -21.12200 -12.58100 1.000 15.44737 ? 51  SER   B O     1 
ATOM   401  C  CB    . SER   A 1 52  ? 68.70800  -18.04100 -12.88000 1.000 17.84267 ? 51  SER   B CB    1 
ATOM   402  O  OG    . SER   A 1 52  ? 68.87700  -16.73100 -13.40600 1.000 17.57634 ? 51  SER   B OG    1 
ATOM   403  N  N     . LEU   A 1 53  ? 69.99800  -19.95200 -10.66600 1.000 12.12485 ? 52  LEU   B N     1 
ATOM   404  C  CA    . LEU   A 1 53  ? 69.64700  -21.03900 -9.75600  1.000 13.55005 ? 52  LEU   B CA    1 
ATOM   405  C  C     . LEU   A 1 53  ? 68.22500  -20.81400 -9.26700  1.000 13.25664 ? 52  LEU   B C     1 
ATOM   406  O  O     . LEU   A 1 53  ? 67.92600  -19.76700 -8.68300  1.000 15.37185 ? 52  LEU   B O     1 
ATOM   407  C  CB    . LEU   A 1 53  ? 70.59700  -21.11200 -8.55700  1.000 18.59384 ? 52  LEU   B CB    1 
ATOM   408  C  CG    . LEU   A 1 53  ? 71.75700  -22.11200 -8.54600  1.000 30.79167 ? 52  LEU   B CG    1 
ATOM   409  C  CD1   . LEU   A 1 53  ? 71.24300  -23.55200 -8.61100  1.000 29.29159 ? 52  LEU   B CD1   1 
ATOM   410  C  CD2   . LEU   A 1 53  ? 72.74300  -21.83400 -9.66700  1.000 34.44763 ? 52  LEU   B CD2   1 
ATOM   411  N  N     . LEU   A 1 54  ? 67.35100  -21.77700 -9.51100  1.000 11.44767 ? 53  LEU   B N     1 
ATOM   412  C  CA    . LEU   A 1 54  ? 65.98700  -21.72200 -9.00800  1.000 9.11124  ? 53  LEU   B CA    1 
ATOM   413  C  C     . LEU   A 1 54  ? 65.92700  -22.51800 -7.71400  1.000 11.64831 ? 53  LEU   B C     1 
ATOM   414  O  O     . LEU   A 1 54  ? 66.27000  -23.70600 -7.69900  1.000 13.06603 ? 53  LEU   B O     1 
ATOM   415  C  CB    . LEU   A 1 54  ? 64.98300  -22.26600 -10.02800 1.000 10.63783 ? 53  LEU   B CB    1 
ATOM   416  C  CG    . LEU   A 1 54  ? 65.17900  -21.73500 -11.44700 1.000 13.86640 ? 53  LEU   B CG    1 
ATOM   417  C  CD1   . LEU   A 1 54  ? 64.12500  -22.27100 -12.41100 1.000 16.26531 ? 53  LEU   B CD1   1 
ATOM   418  C  CD2   . LEU   A 1 54  ? 65.21900  -20.20700 -11.43900 1.000 12.47221 ? 53  LEU   B CD2   1 
ATOM   419  N  N     . ASP   A 1 55  ? 65.55500  -21.84500 -6.62000  1.000 8.65885  ? 54  ASP   B N     1 
ATOM   420  C  CA    . ASP   A 1 55  ? 65.27500  -22.49300 -5.34400  1.000 8.58489  ? 54  ASP   B CA    1 
ATOM   421  C  C     . ASP   A 1 55  ? 63.77000  -22.63100 -5.25800  1.000 9.23306  ? 54  ASP   B C     1 
ATOM   422  O  O     . ASP   A 1 55  ? 63.07000  -21.63800 -5.04700  1.000 11.79081 ? 54  ASP   B O     1 
ATOM   423  C  CB    . ASP   A 1 55  ? 65.77000  -21.68000 -4.15900  1.000 13.06089 ? 54  ASP   B CB    1 
ATOM   424  C  CG    . ASP   A 1 55  ? 67.23600  -21.38800 -4.22600  1.000 14.86054 ? 54  ASP   B CG    1 
ATOM   425  O  OD1   . ASP   A 1 55  ? 67.99700  -22.29100 -4.62300  1.000 20.67858 ? 54  ASP   B OD1   1 
ATOM   426  O  OD2   . ASP   A 1 55  ? 67.62600  -20.25300 -3.87400  1.000 18.63701 ? 54  ASP   B OD2   1 
ATOM   427  N  N     . ILE   A 1 56  ? 63.26900  -23.84000 -5.43100  1.000 9.65483  ? 55  ILE   B N     1 
ATOM   428  C  CA    . ILE   A 1 56  ? 61.83000  -24.04500 -5.55100  1.000 9.05265  ? 55  ILE   B CA    1 
ATOM   429  C  C     . ILE   A 1 56  ? 61.29900  -24.64400 -4.25700  1.000 11.29339 ? 55  ILE   B C     1 
ATOM   430  O  O     . ILE   A 1 56  ? 61.76100  -25.70300 -3.81100  1.000 9.37456  ? 55  ILE   B O     1 
ATOM   431  C  CB    . ILE   A 1 56  ? 61.49200  -24.92400 -6.76200  1.000 10.92259 ? 55  ILE   B CB    1 
ATOM   432  C  CG1   . ILE   A 1 56  ? 61.97700  -24.21600 -8.03000  1.000 10.81129 ? 55  ILE   B CG1   1 
ATOM   433  C  CG2   . ILE   A 1 56  ? 59.96900  -25.15300 -6.84400  1.000 11.32820 ? 55  ILE   B CG2   1 
ATOM   434  C  CD1   . ILE   A 1 56  ? 62.30900  -25.16900 -9.13700  1.000 18.03635 ? 55  ILE   B CD1   1 
ATOM   435  N  N     . LEU   A 1 57  ? 60.32500  -23.95900 -3.65900  1.000 8.70531  ? 56  LEU   B N     1 
ATOM   436  C  CA    . LEU   A 1 57  ? 59.64700  -24.42500 -2.45800  1.000 8.76790  ? 56  LEU   B CA    1 
ATOM   437  C  C     . LEU   A 1 57  ? 58.28600  -24.97100 -2.87200  1.000 10.08917 ? 56  LEU   B C     1 
ATOM   438  O  O     . LEU   A 1 57  ? 57.42300  -24.21200 -3.32200  1.000 8.65358  ? 56  LEU   B O     1 
ATOM   439  C  CB    . LEU   A 1 57  ? 59.50500  -23.28400 -1.45100  1.000 7.09020  ? 56  LEU   B CB    1 
ATOM   440  C  CG    . LEU   A 1 57  ? 58.80300  -23.60100 -0.13800  1.000 10.13616 ? 56  LEU   B CG    1 
ATOM   441  C  CD1   . LEU   A 1 57  ? 59.58300  -24.70400 0.57100   1.000 11.56990 ? 56  LEU   B CD1   1 
ATOM   442  C  CD2   . LEU   A 1 57  ? 58.71400  -22.35300 0.72500   1.000 12.42973 ? 56  LEU   B CD2   1 
ATOM   443  N  N     . ASP   A 1 58  ? 58.11000  -26.28600 -2.73400  1.000 8.24532  ? 57  ASP   B N     1 
ATOM   444  C  CA    . ASP   A 1 58  ? 56.85600  -26.97100 -3.05900  1.000 10.46324 ? 57  ASP   B CA    1 
ATOM   445  C  C     . ASP   A 1 58  ? 56.03900  -27.07900 -1.77400  1.000 9.07727  ? 57  ASP   B C     1 
ATOM   446  O  O     . ASP   A 1 58  ? 56.39700  -27.84300 -0.86800  1.000 9.38143  ? 57  ASP   B O     1 
ATOM   447  C  CB    . ASP   A 1 58  ? 57.18100  -28.34000 -3.66400  1.000 9.19236  ? 57  ASP   B CB    1 
ATOM   448  C  CG    . ASP   A 1 58  ? 55.96100  -29.15000 -4.04100  1.000 11.84724 ? 57  ASP   B CG    1 
ATOM   449  O  OD1   . ASP   A 1 58  ? 54.85800  -28.57600 -4.16500  1.000 13.46999 ? 57  ASP   B OD1   1 
ATOM   450  O  OD2   . ASP   A 1 58  ? 56.11800  -30.38900 -4.20900  1.000 10.74726 ? 57  ASP   B OD2   1 
ATOM   451  N  N     . THR   A 1 59  ? 54.95700  -26.30000 -1.67600  1.000 8.89031  ? 58  THR   B N     1 
ATOM   452  C  CA    . THR   A 1 59  ? 54.17400  -26.26100 -0.44900  1.000 7.23110  ? 58  THR   B CA    1 
ATOM   453  C  C     . THR   A 1 59  ? 52.99900  -27.23000 -0.53700  1.000 7.44670  ? 58  THR   B C     1 
ATOM   454  O  O     . THR   A 1 59  ? 52.59100  -27.66100 -1.61300  1.000 7.79493  ? 58  THR   B O     1 
ATOM   455  C  CB    . THR   A 1 59  ? 53.63100  -24.85300 -0.13300  1.000 8.58962  ? 58  THR   B CB    1 
ATOM   456  O  OG1   . THR   A 1 59  ? 52.58400  -24.48700 -1.05800  1.000 6.95208  ? 58  THR   B OG1   1 
ATOM   457  C  CG2   . THR   A 1 59  ? 54.75200  -23.78400 -0.14600  1.000 10.00110 ? 58  THR   B CG2   1 
ATOM   458  N  N     . ALA   A 1 60  ? 52.45300  -27.55100 0.61800   1.000 8.00031  ? 59  ALA   B N     1 
ATOM   459  C  CA    . ALA   A 1 60  ? 51.25200  -28.35900 0.69800   1.000 8.38324  ? 59  ALA   B CA    1 
ATOM   460  C  C     . ALA   A 1 60  ? 50.02700  -27.47700 0.49000   1.000 8.36355  ? 59  ALA   B C     1 
ATOM   461  O  O     . ALA   A 1 60  ? 49.98000  -26.34000 0.96700   1.000 8.88300  ? 59  ALA   B O     1 
ATOM   462  C  CB    . ALA   A 1 60  ? 51.16300  -29.04900 2.05700   1.000 9.19057  ? 59  ALA   B CB    1 
ATOM   463  N  N     . GLY   A 1 61  ? 49.01900  -28.02000 -0.19500  1.000 8.47479  ? 60  GLY   B N     1 
ATOM   464  C  CA    . GLY   A 1 61  ? 47.72800  -27.36100 -0.23300  1.000 10.37179 ? 60  GLY   B CA    1 
ATOM   465  C  C     . GLY   A 1 61  ? 46.97700  -27.59000 1.06300   1.000 10.25689 ? 60  GLY   B C     1 
ATOM   466  O  O     . GLY   A 1 61  ? 46.26700  -28.58600 1.21300   1.000 10.16559 ? 60  GLY   B O     1 
ATOM   467  N  N     . GLN   A 1 62  ? 47.16100  -26.69600 2.02900   1.000 11.02752 ? 61  GLN   B N     1 
ATOM   468  C  CA    . GLN   A 1 62  ? 46.50200  -26.82400 3.31500   1.000 10.86829 ? 61  GLN   B CA    1 
ATOM   469  C  C     . GLN   A 1 62  ? 46.15900  -25.42800 3.80000   1.000 18.00979 ? 61  GLN   B C     1 
ATOM   470  O  O     . GLN   A 1 62  ? 46.81500  -24.44800 3.42600   1.000 20.30487 ? 61  GLN   B O     1 
ATOM   471  C  CB    . GLN   A 1 62  ? 47.38400  -27.56000 4.33900   1.000 14.26319 ? 61  GLN   B CB    1 
ATOM   472  C  CG    . GLN   A 1 62  ? 48.78100  -26.97900 4.50100   1.000 15.16623 ? 61  GLN   B CG    1 
ATOM   473  C  CD    . GLN   A 1 62  ? 48.82900  -25.75300 5.41200   1.000 15.01255 ? 61  GLN   B CD    1 
ATOM   474  O  OE1   . GLN   A 1 62  ? 47.98100  -25.58200 6.28600   1.000 23.02927 ? 61  GLN   B OE1   1 
ATOM   475  N  NE2   . GLN   A 1 62  ? 49.82600  -24.89800 5.20800   1.000 15.55916 ? 61  GLN   B NE2   1 
ATOM   476  N  N     . GLU   A 1 63  ? 45.14500  -25.34700 4.65600   1.000 22.95560 ? 62  GLU   B N     1 
ATOM   477  C  CA    . GLU   A 1 63  ? 44.69900  -24.05700 5.16400   1.000 26.24543 ? 62  GLU   B CA    1 
ATOM   478  C  C     . GLU   A 1 63  ? 44.58100  -24.06600 6.68000   1.000 26.48421 ? 62  GLU   B C     1 
ATOM   479  O  O     . GLU   A 1 63  ? 43.71900  -23.38400 7.24400   1.000 30.79466 ? 62  GLU   B O     1 
ATOM   480  C  CB    . GLU   A 1 63  ? 43.37900  -23.64600 4.51600   1.000 27.58319 ? 62  GLU   B CB    1 
ATOM   481  C  CG    . GLU   A 1 63  ? 43.56800  -22.97200 3.16400   1.000 29.87990 ? 62  GLU   B CG    1 
ATOM   482  C  CD    . GLU   A 1 63  ? 42.31000  -22.99400 2.32500   1.000 38.15960 ? 62  GLU   B CD    1 
ATOM   483  O  OE1   . GLU   A 1 63  ? 41.24500  -23.39300 2.85200   1.000 42.31724 ? 62  GLU   B OE1   1 
ATOM   484  O  OE2   . GLU   A 1 63  ? 42.38900  -22.62500 1.13600   1.000 41.16535 ? 62  GLU   B OE2   1 
ATOM   485  N  N     . GLU   A 1 64  ? 45.44500  -24.82500 7.35900   1.000 20.95723 ? 63  GLU   B N     1 
ATOM   486  C  CA    . GLU   A 1 64  ? 45.42600  -24.88300 8.81600   1.000 24.07862 ? 63  GLU   B CA    1 
ATOM   487  C  C     . GLU   A 1 64  ? 46.62300  -24.23100 9.49700   1.000 20.49331 ? 63  GLU   B C     1 
ATOM   488  O  O     . GLU   A 1 64  ? 46.56000  -23.99500 10.71000  1.000 25.26205 ? 63  GLU   B O     1 
ATOM   489  C  CB    . GLU   A 1 64  ? 45.33900  -26.33600 9.29300   1.000 20.90530 ? 63  GLU   B CB    1 
ATOM   490  C  CG    . GLU   A 1 64  ? 43.95800  -26.92400 9.22000   1.000 30.57815 ? 63  GLU   B CG    1 
ATOM   491  C  CD    . GLU   A 1 64  ? 43.79600  -27.86500 8.05300   1.000 34.72886 ? 63  GLU   B CD    1 
ATOM   492  O  OE1   . GLU   A 1 64  ? 43.89900  -27.41800 6.88100   1.000 35.14907 ? 63  GLU   B OE1   1 
ATOM   493  O  OE2   . GLU   A 1 64  ? 43.57600  -29.06500 8.32100   1.000 36.40994 ? 63  GLU   B OE2   1 
ATOM   494  N  N     . TYR   A 1 65  ? 47.70900  -23.95400 8.77400   1.000 21.46162 ? 64  TYR   B N     1 
ATOM   495  C  CA    . TYR   A 1 65  ? 48.98000  -23.51100 9.36100   1.000 21.49136 ? 64  TYR   B CA    1 
ATOM   496  C  C     . TYR   A 1 65  ? 49.37300  -22.16600 8.76100   1.000 22.15157 ? 64  TYR   B C     1 
ATOM   497  O  O     . TYR   A 1 65  ? 50.17300  -22.09100 7.82900   1.000 19.75790 ? 64  TYR   B O     1 
ATOM   498  C  CB    . TYR   A 1 65  ? 50.06700  -24.57100 9.15500   1.000 19.44375 ? 64  TYR   B CB    1 
ATOM   499  C  CG    . TYR   A 1 65  ? 49.65400  -25.87400 9.77900   1.000 17.61802 ? 64  TYR   B CG    1 
ATOM   500  C  CD1   . TYR   A 1 65  ? 49.72100  -26.04700 11.14600  1.000 15.94002 ? 64  TYR   B CD1   1 
ATOM   501  C  CD2   . TYR   A 1 65  ? 49.14300  -26.91300 9.00500   1.000 16.93911 ? 64  TYR   B CD2   1 
ATOM   502  C  CE1   . TYR   A 1 65  ? 49.31600  -27.22100 11.73300  1.000 19.85211 ? 64  TYR   B CE1   1 
ATOM   503  C  CE2   . TYR   A 1 65  ? 48.73100  -28.10200 9.58900   1.000 14.97507 ? 64  TYR   B CE2   1 
ATOM   504  C  CZ    . TYR   A 1 65  ? 48.82500  -28.24700 10.95400  1.000 16.31469 ? 64  TYR   B CZ    1 
ATOM   505  O  OH    . TYR   A 1 65  ? 48.41600  -29.40600 11.55900  1.000 17.32298 ? 64  TYR   B OH    1 
ATOM   506  N  N     . SER   A 1 66  ? 48.81800  -21.10100 9.33300   1.000 22.07494 ? 65  SER   B N     1 
ATOM   507  C  CA    . SER   A 1 66  ? 48.97300  -19.76800 8.76800   1.000 22.20729 ? 65  SER   B CA    1 
ATOM   508  C  C     . SER   A 1 66  ? 50.35000  -19.17600 9.03700   1.000 20.79552 ? 65  SER   B C     1 
ATOM   509  O  O     . SER   A 1 66  ? 50.84000  -18.38800 8.22400   1.000 21.83066 ? 65  SER   B O     1 
ATOM   510  C  CB    . SER   A 1 66  ? 47.89100  -18.84500 9.32800   1.000 23.99256 ? 65  SER   B CB    1 
ATOM   511  O  OG    . SER   A 1 66  ? 46.59600  -19.33800 9.01500   1.000 31.40054 ? 65  SER   B OG    1 
ATOM   512  N  N     . ALA   A 1 67  ? 50.98500  -19.52900 10.15900  1.000 18.20631 ? 66  ALA   B N     1 
ATOM   513  C  CA    . ALA   A 1 67  ? 52.29900  -18.96900 10.46800  1.000 18.17625 ? 66  ALA   B CA    1 
ATOM   514  C  C     . ALA   A 1 67  ? 53.38000  -19.53700 9.56000   1.000 19.00776 ? 66  ALA   B C     1 
ATOM   515  O  O     . ALA   A 1 67  ? 54.32500  -18.82500 9.19800   1.000 18.31568 ? 66  ALA   B O     1 
ATOM   516  C  CB    . ALA   A 1 67  ? 52.65900  -19.22400 11.93300  1.000 22.22305 ? 66  ALA   B CB    1 
ATOM   517  N  N     . MET   A 1 68  ? 53.27100  -20.81400 9.19700   1.000 17.72179 ? 67  MET   B N     1 
ATOM   518  C  CA    . MET   A 1 68  ? 54.17600  -21.35200 8.19100   1.000 17.86348 ? 67  MET   B CA    1 
ATOM   519  C  C     . MET   A 1 68  ? 53.86900  -20.75600 6.82500   1.000 12.29758 ? 67  MET   B C     1 
ATOM   520  O  O     . MET   A 1 68  ? 54.78500  -20.36900 6.09200   1.000 15.30451 ? 67  MET   B O     1 
ATOM   521  C  CB    . MET   A 1 68  ? 54.07800  -22.88200 8.15300   1.000 13.85117 ? 67  MET   B CB    1 
ATOM   522  C  CG    . MET   A 1 68  ? 54.72500  -23.55300 9.33500   1.000 17.99614 ? 67  MET   B CG    1 
ATOM   523  S  SD    . MET   A 1 68  ? 56.51800  -23.36200 9.31100   1.000 30.53045 ? 67  MET   B SD    1 
ATOM   524  C  CE    . MET   A 1 68  ? 56.90000  -23.98800 7.68100   1.000 25.16417 ? 67  MET   B CE    1 
ATOM   525  N  N     . ARG   A 1 69  ? 52.58400  -20.67800 6.46800   1.000 14.78608 ? 68  ARG   B N     1 
ATOM   526  C  CA    . ARG   A 1 69  ? 52.19500  -20.05400 5.20700   1.000 11.93779 ? 68  ARG   B CA    1 
ATOM   527  C  C     . ARG   A 1 69  ? 52.78900  -18.65200 5.08500   1.000 12.67171 ? 68  ARG   B C     1 
ATOM   528  O  O     . ARG   A 1 69  ? 53.39200  -18.30600 4.06400   1.000 10.49595 ? 68  ARG   B O     1 
ATOM   529  C  CB    . ARG   A 1 69  ? 50.67000  -20.00600 5.09300   1.000 11.39839 ? 68  ARG   B CB    1 
ATOM   530  C  CG    . ARG   A 1 69  ? 50.16600  -19.17200 3.90900   1.000 17.12427 ? 68  ARG   B CG    1 
ATOM   531  C  CD    . ARG   A 1 69  ? 48.72200  -18.76000 4.08700   1.000 20.51897 ? 68  ARG   B CD    1 
ATOM   532  N  NE    . ARG   A 1 69  ? 48.59300  -17.71900 5.10300   1.000 23.49377 ? 68  ARG   B NE    1 
ATOM   533  C  CZ    . ARG   A 1 69  ? 47.46600  -17.41300 5.73300   1.000 28.57441 ? 68  ARG   B CZ    1 
ATOM   534  N  NH1   . ARG   A 1 69  ? 46.32900  -18.03800 5.46400   1.000 26.75522 ? 68  ARG   B NH1   1 
ATOM   535  N  NH2   . ARG   A 1 69  ? 47.48200  -16.46400 6.66500   1.000 26.47496 ? 68  ARG   B NH2   1 
ATOM   536  N  N     . ASP   A 1 70  ? 52.63400  -17.83400 6.13000   1.000 13.04110 ? 69  ASP   B N     1 
ATOM   537  C  CA    . ASP   A 1 70  ? 53.11900  -16.45700 6.06700   1.000 15.77903 ? 69  ASP   B CA    1 
ATOM   538  C  C     . ASP   A 1 70  ? 54.62800  -16.40100 5.82900   1.000 12.51599 ? 69  ASP   B C     1 
ATOM   539  O  O     . ASP   A 1 70  ? 55.10900  -15.56800 5.05000   1.000 13.65067 ? 69  ASP   B O     1 
ATOM   540  C  CB    . ASP   A 1 70  ? 52.74600  -15.71400 7.35000   1.000 13.39746 ? 69  ASP   B CB    1 
ATOM   541  C  CG    . ASP   A 1 70  ? 51.24000  -15.44600 7.46700   1.000 20.17662 ? 69  ASP   B CG    1 
ATOM   542  O  OD1   . ASP   A 1 70  ? 50.48400  -15.79900 6.54000   1.000 18.46254 ? 69  ASP   B OD1   1 
ATOM   543  O  OD2   . ASP   A 1 70  ? 50.81400  -14.87700 8.49900   1.000 20.10888 ? 69  ASP   B OD2   1 
ATOM   544  N  N     . GLN   A 1 71  ? 55.39800  -17.27500 6.48400   1.000 11.56968 ? 70  GLN   B N     1 
ATOM   545  C  CA    . GLN   A 1 71  ? 56.84700  -17.23300 6.27900   1.000 15.98330 ? 70  GLN   B CA    1 
ATOM   546  C  C     . GLN   A 1 71  ? 57.21200  -17.63900 4.85400   1.000 13.41204 ? 70  GLN   B C     1 
ATOM   547  O  O     . GLN   A 1 71  ? 58.13500  -17.07100 4.25800   1.000 13.95848 ? 70  GLN   B O     1 
ATOM   548  C  CB    . GLN   A 1 71  ? 57.57100  -18.11600 7.29700   1.000 19.63579 ? 70  GLN   B CB    1 
ATOM   549  C  CG    . GLN   A 1 71  ? 59.09600  -18.05600 7.17600   1.000 18.60931 ? 70  GLN   B CG    1 
ATOM   550  C  CD    . GLN   A 1 71  ? 59.64700  -16.62900 7.19200   1.000 22.67368 ? 70  GLN   B CD    1 
ATOM   551  O  OE1   . GLN   A 1 71  ? 59.23500  -15.78900 7.99800   1.000 23.82903 ? 70  GLN   B OE1   1 
ATOM   552  N  NE2   . GLN   A 1 71  ? 60.57800  -16.34900 6.28700   1.000 24.53232 ? 70  GLN   B NE2   1 
ATOM   553  N  N     . TYR   A 1 72  ? 56.48800  -18.60800 4.28800   1.000 11.81020 ? 71  TYR   B N     1 
ATOM   554  C  CA    . TYR   A 1 72  ? 56.67900  -18.96300 2.88800   1.000 10.56805 ? 71  TYR   B CA    1 
ATOM   555  C  C     . TYR   A 1 72  ? 56.49700  -17.75000 1.99200   1.000 9.39291  ? 71  TYR   B C     1 
ATOM   556  O  O     . TYR   A 1 72  ? 57.23600  -17.55500 1.02400   1.000 10.17235 ? 71  TYR   B O     1 
ATOM   557  C  CB    . TYR   A 1 72  ? 55.65800  -20.02400 2.47400   1.000 14.24734 ? 71  TYR   B CB    1 
ATOM   558  C  CG    . TYR   A 1 72  ? 55.76100  -21.40100 3.09700   1.000 9.81218  ? 71  TYR   B CG    1 
ATOM   559  C  CD1   . TYR   A 1 72  ? 56.93200  -21.86100 3.69500   1.000 14.79476 ? 71  TYR   B CD1   1 
ATOM   560  C  CD2   . TYR   A 1 72  ? 54.67600  -22.25600 3.04700   1.000 10.18596 ? 71  TYR   B CD2   1 
ATOM   561  C  CE1   . TYR   A 1 72  ? 56.99700  -23.14100 4.24800   1.000 11.43316 ? 71  TYR   B CE1   1 
ATOM   562  C  CE2   . TYR   A 1 72  ? 54.72800  -23.51600 3.59300   1.000 12.71011 ? 71  TYR   B CE2   1 
ATOM   563  C  CZ    . TYR   A 1 72  ? 55.88500  -23.96700 4.17800   1.000 13.50989 ? 71  TYR   B CZ    1 
ATOM   564  O  OH    . TYR   A 1 72  ? 55.89700  -25.24900 4.69800   1.000 11.55099 ? 71  TYR   B OH    1 
ATOM   565  N  N     . MET   A 1 73  ? 55.46000  -16.96100 2.26200   1.000 11.67587 ? 72  MET   B N     1 
ATOM   566  C  CA    . MET   A 1 73  ? 55.17600  -15.80800 1.43100   1.000 8.97245  ? 72  MET   B CA    1 
ATOM   567  C  C     . MET   A 1 73  ? 56.16300  -14.67600 1.69100   1.000 12.46485 ? 72  MET   B C     1 
ATOM   568  O  O     . MET   A 1 73  ? 56.52400  -13.96100 0.75200   1.000 11.32211 ? 72  MET   B O     1 
ATOM   569  C  CB    . MET   A 1 73  ? 53.71800  -15.38300 1.64700   1.000 9.31818  ? 72  MET   B CB    1 
ATOM   570  C  CG    . MET   A 1 73  ? 52.74200  -16.45400 1.16300   1.000 10.85147 ? 72  MET   B CG    1 
ATOM   571  S  SD    . MET   A 1 73  ? 50.99000  -16.17500 1.54000   1.000 14.56458 ? 72  MET   B SD    1 
ATOM   572  C  CE    . MET   A 1 73  ? 50.22900  -17.49500 0.60300   1.000 14.60383 ? 72  MET   B CE    1 
ATOM   573  N  N     . ARG   A 1 74  ? 56.62900  -14.50500 2.93200   1.000 10.07375 ? 73  ARG   B N     1 
ATOM   574  C  CA    . ARG   A 1 74  ? 57.63900  -13.47600 3.19500   1.000 15.05980 ? 73  ARG   B CA    1 
ATOM   575  C  C     . ARG   A 1 74  ? 58.92500  -13.73900 2.41300   1.000 17.12076 ? 73  ARG   B C     1 
ATOM   576  O  O     . ARG   A 1 74  ? 59.48100  -12.82900 1.78300   1.000 16.94001 ? 73  ARG   B O     1 
ATOM   577  C  CB    . ARG   A 1 74  ? 57.94100  -13.38600 4.69300   1.000 13.43179 ? 73  ARG   B CB    1 
ATOM   578  C  CG    . ARG   A 1 74  ? 57.18800  -12.27600 5.38900   1.000 18.30457 ? 73  ARG   B CG    1 
ATOM   579  C  CD    . ARG   A 1 74  ? 57.66400  -12.08100 6.81800   1.000 22.21305 ? 73  ARG   B CD    1 
ATOM   580  N  NE    . ARG   A 1 74  ? 57.58300  -13.31800 7.57800   1.000 24.48389 ? 73  ARG   B NE    1 
ATOM   581  C  CZ    . ARG   A 1 74  ? 56.52100  -13.71000 8.27100   1.000 27.23113 ? 73  ARG   B CZ    1 
ATOM   582  N  NH1   . ARG   A 1 74  ? 55.41200  -12.97700 8.32400   1.000 19.40157 ? 73  ARG   B NH1   1 
ATOM   583  N  NH2   . ARG   A 1 74  ? 56.56900  -14.86600 8.92600   1.000 18.75068 ? 73  ARG   B NH2   1 
ATOM   584  N  N     . THR   A 1 75  ? 59.40800  -14.98500 2.43400   1.000 11.13615 ? 74  THR   B N     1 
ATOM   585  C  CA    . THR   A 1 75  ? 60.67500  -15.33600 1.79700   1.000 13.38090 ? 74  THR   B CA    1 
ATOM   586  C  C     . THR   A 1 75  ? 60.57000  -15.45300 0.27900   1.000 15.65061 ? 74  THR   B C     1 
ATOM   587  O  O     . THR   A 1 75  ? 61.54400  -15.17200 -0.42700  1.000 13.20302 ? 74  THR   B O     1 
ATOM   588  C  CB    . THR   A 1 75  ? 61.17700  -16.66300 2.37100   1.000 14.42440 ? 74  THR   B CB    1 
ATOM   589  O  OG1   . THR   A 1 75  ? 61.20700  -16.58300 3.79400   1.000 26.94371 ? 74  THR   B OG1   1 
ATOM   590  C  CG2   . THR   A 1 75  ? 62.56500  -16.99600 1.86800   1.000 20.92658 ? 74  THR   B CG2   1 
ATOM   591  N  N     . GLY   A 1 76  ? 59.42700  -15.88300 -0.24700  1.000 11.19119 ? 75  GLY   B N     1 
ATOM   592  C  CA    . GLY   A 1 76  ? 59.34000  -16.10900 -1.68100  1.000 8.69761  ? 75  GLY   B CA    1 
ATOM   593  C  C     . GLY   A 1 76  ? 59.45300  -14.81200 -2.46600  1.000 11.47545 ? 75  GLY   B C     1 
ATOM   594  O  O     . GLY   A 1 76  ? 58.92000  -13.77300 -2.07100  1.000 11.84328 ? 75  GLY   B O     1 
ATOM   595  N  N     . GLU   A 1 77  ? 60.15900  -14.87700 -3.60000  1.000 7.79396  ? 76  GLU   B N     1 
ATOM   596  C  CA    . GLU   A 1 77  ? 60.22400  -13.73400 -4.50600  1.000 10.19981 ? 76  GLU   B CA    1 
ATOM   597  C  C     . GLU   A 1 77  ? 59.17600  -13.79000 -5.60700  1.000 11.44220 ? 76  GLU   B C     1 
ATOM   598  O  O     . GLU   A 1 77  ? 58.84500  -12.74300 -6.18600  1.000 15.71766 ? 76  GLU   B O     1 
ATOM   599  C  CB    . GLU   A 1 77  ? 61.61100  -13.64900 -5.14800  1.000 12.73356 ? 76  GLU   B CB    1 
ATOM   600  C  CG    . GLU   A 1 77  ? 62.75300  -13.58400 -4.16100  1.000 13.05308 ? 76  GLU   B CG    1 
ATOM   601  C  CD    . GLU   A 1 77  ? 64.11300  -13.64000 -4.85600  1.000 17.89225 ? 76  GLU   B CD    1 
ATOM   602  O  OE1   . GLU   A 1 77  ? 64.51000  -12.62000 -5.46300  1.000 18.46276 ? 76  GLU   B OE1   1 
ATOM   603  O  OE2   . GLU   A 1 77  ? 64.77200  -14.70100 -4.79700  1.000 14.28075 ? 76  GLU   B OE2   1 
ATOM   604  N  N     . GLY   A 1 78  ? 58.68100  -14.97900 -5.93100  1.000 10.49944 ? 77  GLY   B N     1 
ATOM   605  C  CA    . GLY   A 1 78  ? 57.62700  -15.12600 -6.92100  1.000 8.31564  ? 77  GLY   B CA    1 
ATOM   606  C  C     . GLY   A 1 78  ? 56.85000  -16.38400 -6.61900  1.000 9.60569  ? 77  GLY   B C     1 
ATOM   607  O  O     . GLY   A 1 78  ? 57.36700  -17.31400 -5.99800  1.000 8.03172  ? 77  GLY   B O     1 
ATOM   608  N  N     . PHE   A 1 79  ? 55.60100  -16.42100 -7.07500  1.000 6.79140  ? 78  PHE   B N     1 
ATOM   609  C  CA    . PHE   A 1 79  ? 54.66100  -17.46300 -6.69100  1.000 9.24169  ? 78  PHE   B CA    1 
ATOM   610  C  C     . PHE   A 1 79  ? 53.94000  -17.98700 -7.91900  1.000 7.84141  ? 78  PHE   B C     1 
ATOM   611  O  O     . PHE   A 1 79  ? 53.48100  -17.19800 -8.75100  1.000 8.73851  ? 78  PHE   B O     1 
ATOM   612  C  CB    . PHE   A 1 79  ? 53.63500  -16.92000 -5.68200  1.000 9.04761  ? 78  PHE   B CB    1 
ATOM   613  C  CG    . PHE   A 1 79  ? 54.27000  -16.38600 -4.44900  1.000 13.14243 ? 78  PHE   B CG    1 
ATOM   614  C  CD1   . PHE   A 1 79  ? 54.75200  -15.08200 -4.41300  1.000 10.11603 ? 78  PHE   B CD1   1 
ATOM   615  C  CD2   . PHE   A 1 79  ? 54.46100  -17.20900 -3.34200  1.000 9.87305  ? 78  PHE   B CD2   1 
ATOM   616  C  CE1   . PHE   A 1 79  ? 55.39200  -14.60500 -3.28400  1.000 10.12810 ? 78  PHE   B CE1   1 
ATOM   617  C  CE2   . PHE   A 1 79  ? 55.08300  -16.73500 -2.21400  1.000 11.08569 ? 78  PHE   B CE2   1 
ATOM   618  C  CZ    . PHE   A 1 79  ? 55.56300  -15.43000 -2.18700  1.000 8.16640  ? 78  PHE   B CZ    1 
ATOM   619  N  N     . LEU   A 1 80  ? 53.88100  -19.31300 -8.04600  1.000 6.81038  ? 79  LEU   B N     1 
ATOM   620  C  CA    . LEU   A 1 80  ? 52.97800  -19.95600 -8.99000  1.000 10.16427 ? 79  LEU   B CA    1 
ATOM   621  C  C     . LEU   A 1 80  ? 51.66800  -20.21400 -8.27200  1.000 7.72146  ? 79  LEU   B C     1 
ATOM   622  O  O     . LEU   A 1 80  ? 51.65400  -20.87000 -7.22900  1.000 8.34459  ? 79  LEU   B O     1 
ATOM   623  C  CB    . LEU   A 1 80  ? 53.54300  -21.27600 -9.51800  1.000 7.70951  ? 79  LEU   B CB    1 
ATOM   624  C  CG    . LEU   A 1 80  ? 54.74600  -21.24700 -10.45400 1.000 10.09989 ? 79  LEU   B CG    1 
ATOM   625  C  CD1   . LEU   A 1 80  ? 54.98700  -22.65700 -10.99500 1.000 8.74692  ? 79  LEU   B CD1   1 
ATOM   626  C  CD2   . LEU   A 1 80  ? 54.54800  -20.24200 -11.58500 1.000 11.57279 ? 79  LEU   B CD2   1 
ATOM   627  N  N     . LEU   A 1 81  ? 50.58000  -19.67700 -8.82000  1.000 8.15674  ? 80  LEU   B N     1 
ATOM   628  C  CA    . LEU   A 1 81  ? 49.23600  -19.89300 -8.31800  1.000 7.84761  ? 80  LEU   B CA    1 
ATOM   629  C  C     . LEU   A 1 81  ? 48.62200  -20.99400 -9.18100  1.000 7.88241  ? 80  LEU   B C     1 
ATOM   630  O  O     . LEU   A 1 81  ? 48.18000  -20.73300 -10.30200 1.000 8.77252  ? 80  LEU   B O     1 
ATOM   631  C  CB    . LEU   A 1 81  ? 48.42500  -18.59900 -8.39800  1.000 8.58641  ? 80  LEU   B CB    1 
ATOM   632  C  CG    . LEU   A 1 81  ? 48.61800  -17.48900 -7.35200  1.000 14.24101 ? 80  LEU   B CG    1 
ATOM   633  C  CD1   . LEU   A 1 81  ? 50.05400  -17.27800 -6.96600  1.000 9.76555  ? 80  LEU   B CD1   1 
ATOM   634  C  CD2   . LEU   A 1 81  ? 47.99600  -16.18900 -7.84500  1.000 11.54585 ? 80  LEU   B CD2   1 
ATOM   635  N  N     . VAL   A 1 82  ? 48.60900  -22.22800 -8.67200  1.000 9.17305  ? 81  VAL   B N     1 
ATOM   636  C  CA    . VAL   A 1 82  ? 48.21000  -23.39000 -9.46300  1.000 9.48325  ? 81  VAL   B CA    1 
ATOM   637  C  C     . VAL   A 1 82  ? 46.78500  -23.79300 -9.11000  1.000 8.58688  ? 81  VAL   B C     1 
ATOM   638  O  O     . VAL   A 1 82  ? 46.43800  -23.93700 -7.92900  1.000 8.04318  ? 81  VAL   B O     1 
ATOM   639  C  CB    . VAL   A 1 82  ? 49.17500  -24.56900 -9.25800  1.000 7.08706  ? 81  VAL   B CB    1 
ATOM   640  C  CG1   . VAL   A 1 82  ? 48.84800  -25.71600 -10.22700 1.000 7.46736  ? 81  VAL   B CG1   1 
ATOM   641  C  CG2   . VAL   A 1 82  ? 50.60300  -24.10700 -9.44300  1.000 7.51213  ? 81  VAL   B CG2   1 
ATOM   642  N  N     . PHE   A 1 83  ? 45.94700  -23.93800 -10.12900 1.000 9.10883  ? 82  PHE   B N     1 
ATOM   643  C  CA    . PHE   A 1 83  ? 44.65400  -24.60200 -9.99300  1.000 9.41658  ? 82  PHE   B CA    1 
ATOM   644  C  C     . PHE   A 1 83  ? 44.60200  -25.69400 -11.04500 1.000 10.14102 ? 82  PHE   B C     1 
ATOM   645  O  O     . PHE   A 1 83  ? 45.49000  -25.79000 -11.89800 1.000 10.84579 ? 82  PHE   B O     1 
ATOM   646  C  CB    . PHE   A 1 83  ? 43.46100  -23.63900 -10.16000 1.000 11.77293 ? 82  PHE   B CB    1 
ATOM   647  C  CG    . PHE   A 1 83  ? 43.25700  -23.16400 -11.57400 1.000 10.44910 ? 82  PHE   B CG    1 
ATOM   648  C  CD1   . PHE   A 1 83  ? 43.99300  -22.09400 -12.08000 1.000 11.51598 ? 82  PHE   B CD1   1 
ATOM   649  C  CD2   . PHE   A 1 83  ? 42.33500  -23.78100 -12.39300 1.000 11.54977 ? 82  PHE   B CD2   1 
ATOM   650  C  CE1   . PHE   A 1 83  ? 43.81300  -21.66500 -13.38900 1.000 10.88249 ? 82  PHE   B CE1   1 
ATOM   651  C  CE2   . PHE   A 1 83  ? 42.14000  -23.35100 -13.70400 1.000 13.60708 ? 82  PHE   B CE2   1 
ATOM   652  C  CZ    . PHE   A 1 83  ? 42.87300  -22.29600 -14.20000 1.000 11.75278 ? 82  PHE   B CZ    1 
ATOM   653  N  N     . ALA   A 1 84  ? 43.57000  -26.53700 -10.96000 1.000 10.12045 ? 83  ALA   B N     1 
ATOM   654  C  CA    . ALA   A 1 84  ? 43.37700  -27.64300 -11.89000 1.000 13.23525 ? 83  ALA   B CA    1 
ATOM   655  C  C     . ALA   A 1 84  ? 42.13500  -27.38500 -12.72800 1.000 15.03781 ? 83  ALA   B C     1 
ATOM   656  O  O     . ALA   A 1 84  ? 41.10800  -26.93700 -12.20800 1.000 12.14790 ? 83  ALA   B O     1 
ATOM   657  C  CB    . ALA   A 1 84  ? 43.25200  -28.97300 -11.15100 1.000 11.63639 ? 83  ALA   B CB    1 
ATOM   658  N  N     . ILE   A 1 85  ? 42.23500  -27.65400 -14.03400 1.000 12.17326 ? 84  ILE   B N     1 
ATOM   659  C  CA    . ILE   A 1 85  ? 41.16600  -27.25800 -14.94000 1.000 13.27759 ? 84  ILE   B CA    1 
ATOM   660  C  C     . ILE   A 1 85  ? 39.92900  -28.12100 -14.76700 1.000 14.42096 ? 84  ILE   B C     1 
ATOM   661  O  O     . ILE   A 1 85  ? 38.87300  -27.78100 -15.29500 1.000 15.28647 ? 84  ILE   B O     1 
ATOM   662  C  CB    . ILE   A 1 85  ? 41.64300  -27.28300 -16.40700 1.000 15.48455 ? 84  ILE   B CB    1 
ATOM   663  C  CG1   . ILE   A 1 85  ? 41.94800  -28.71700 -16.84400 1.000 15.38256 ? 84  ILE   B CG1   1 
ATOM   664  C  CG2   . ILE   A 1 85  ? 42.86600  -26.38100 -16.56900 1.000 14.08594 ? 84  ILE   B CG2   1 
ATOM   665  C  CD1   . ILE   A 1 85  ? 41.53800  -29.02100 -18.27100 1.000 23.14586 ? 84  ILE   B CD1   1 
ATOM   666  N  N     . ASN   A 1 86  ? 40.03300  -29.20200 -13.99800 1.000 15.59375 ? 85  ASN   B N     1 
ATOM   667  C  CA    . ASN   A 1 86  ? 38.89700  -30.04100 -13.64500 1.000 14.87969 ? 85  ASN   B CA    1 
ATOM   668  C  C     . ASN   A 1 86  ? 38.55500  -29.94800 -12.16200 1.000 14.57526 ? 85  ASN   B C     1 
ATOM   669  O  O     . ASN   A 1 86  ? 37.91800  -30.85500 -11.62200 1.000 15.92560 ? 85  ASN   B O     1 
ATOM   670  C  CB    . ASN   A 1 86  ? 39.16100  -31.49700 -14.03800 1.000 15.22768 ? 85  ASN   B CB    1 
ATOM   671  C  CG    . ASN   A 1 86  ? 40.32400  -32.12300 -13.26400 1.000 15.89692 ? 85  ASN   B CG    1 
ATOM   672  O  OD1   . ASN   A 1 86  ? 41.20500  -31.42800 -12.76600 1.000 14.56886 ? 85  ASN   B OD1   1 
ATOM   673  N  ND2   . ASN   A 1 86  ? 40.32100  -33.44300 -13.16800 1.000 16.93783 ? 85  ASN   B ND2   1 
ATOM   674  N  N     . ASN   A 1 87  ? 38.98100  -28.87900 -11.48800 1.000 14.74168 ? 86  ASN   B N     1 
ATOM   675  C  CA    . ASN   A 1 87  ? 38.66900  -28.64100 -10.07700 1.000 16.18222 ? 86  ASN   B CA    1 
ATOM   676  C  C     . ASN   A 1 87  ? 38.21000  -27.19000 -9.95900  1.000 17.34923 ? 86  ASN   B C     1 
ATOM   677  O  O     . ASN   A 1 87  ? 39.02500  -26.28000 -9.80900  1.000 14.64186 ? 86  ASN   B O     1 
ATOM   678  C  CB    . ASN   A 1 87  ? 39.86600  -28.93200 -9.18700  1.000 14.96982 ? 86  ASN   B CB    1 
ATOM   679  C  CG    . ASN   A 1 87  ? 39.57000  -28.70800 -7.70800  1.000 17.38040 ? 86  ASN   B CG    1 
ATOM   680  O  OD1   . ASN   A 1 87  ? 38.60100  -28.04200 -7.34300  1.000 15.45860 ? 86  ASN   B OD1   1 
ATOM   681  N  ND2   . ASN   A 1 87  ? 40.41600  -29.26000 -6.85200  1.000 18.09842 ? 86  ASN   B ND2   1 
ATOM   682  N  N     . THR   A 1 88  ? 36.89300  -26.98300 -10.00600 1.000 15.50181 ? 87  THR   B N     1 
ATOM   683  C  CA    . THR   A 1 88  ? 36.35400  -25.62600 -9.96500  1.000 17.99426 ? 87  THR   B CA    1 
ATOM   684  C  C     . THR   A 1 88  ? 36.68900  -24.92800 -8.65100  1.000 18.27174 ? 87  THR   B C     1 
ATOM   685  O  O     . THR   A 1 88  ? 37.03200  -23.73700 -8.64400  1.000 18.38181 ? 87  THR   B O     1 
ATOM   686  C  CB    . THR   A 1 88  ? 34.84200  -25.67700 -10.20700 1.000 17.83185 ? 87  THR   B CB    1 
ATOM   687  O  OG1   . THR   A 1 88  ? 34.61200  -25.87700 -11.60800 1.000 17.79243 ? 87  THR   B OG1   1 
ATOM   688  C  CG2   . THR   A 1 88  ? 34.14000  -24.38700 -9.73800  1.000 17.97945 ? 87  THR   B CG2   1 
ATOM   689  N  N     . LYS   A 1 89  ? 36.62200  -25.65100 -7.53200  1.000 15.19578 ? 88  LYS   B N     1 
ATOM   690  C  CA    . LYS   A 1 89  ? 36.96200  -25.03500 -6.25300  1.000 18.78263 ? 88  LYS   B CA    1 
ATOM   691  C  C     . LYS   A 1 89  ? 38.40500  -24.54800 -6.23600  1.000 19.77994 ? 88  LYS   B C     1 
ATOM   692  O  O     . LYS   A 1 89  ? 38.70300  -23.49100 -5.66200  1.000 19.45983 ? 88  LYS   B O     1 
ATOM   693  C  CB    . LYS   A 1 89  ? 36.72600  -26.01300 -5.10300  1.000 19.46829 ? 88  LYS   B CB    1 
ATOM   694  C  CG    . LYS   A 1 89  ? 37.05300  -25.39200 -3.74900  1.000 25.89483 ? 88  LYS   B CG    1 
ATOM   695  C  CD    . LYS   A 1 89  ? 37.18000  -26.41700 -2.63800  1.000 39.59586 ? 88  LYS   B CD    1 
ATOM   696  C  CE    . LYS   A 1 89  ? 37.67900  -25.76700 -1.34300  1.000 28.72127 ? 88  LYS   B CE    1 
ATOM   697  N  NZ    . LYS   A 1 89  ? 39.18000  -25.67500 -1.24700  1.000 31.61442 ? 88  LYS   B NZ    1 
ATOM   698  N  N     . SER   A 1 90  ? 39.32400  -25.29800 -6.85100  1.000 14.60051 ? 89  SER   B N     1 
ATOM   699  C  CA    . SER   A 1 90  ? 40.71600  -24.85400 -6.82100  1.000 13.52484 ? 89  SER   B CA    1 
ATOM   700  C  C     . SER   A 1 90  ? 40.88300  -23.53600 -7.56300  1.000 16.52375 ? 89  SER   B C     1 
ATOM   701  O  O     . SER   A 1 90  ? 41.74700  -22.72300 -7.20200  1.000 12.87771 ? 89  SER   B O     1 
ATOM   702  C  CB    . SER   A 1 90  ? 41.64800  -25.92700 -7.39000  1.000 11.64482 ? 89  SER   B CB    1 
ATOM   703  O  OG    . SER   A 1 90  ? 41.55800  -26.03000 -8.79700  1.000 13.25945 ? 89  SER   B OG    1 
ATOM   704  N  N     . PHE   A 1 91  ? 40.04000  -23.29000 -8.56800  1.000 12.18255 ? 90  PHE   B N     1 
ATOM   705  C  CA    . PHE   A 1 91  ? 40.06700  -22.00300 -9.25500  1.000 14.22916 ? 90  PHE   B CA    1 
ATOM   706  C  C     . PHE   A 1 91  ? 39.42300  -20.91800 -8.40000  1.000 14.36801 ? 90  PHE   B C     1 
ATOM   707  O  O     . PHE   A 1 91  ? 39.92200  -19.78700 -8.34500  1.000 14.60611 ? 90  PHE   B O     1 
ATOM   708  C  CB    . PHE   A 1 91  ? 39.38300  -22.13500 -10.61400 1.000 13.24255 ? 90  PHE   B CB    1 
ATOM   709  C  CG    . PHE   A 1 91  ? 39.27000  -20.84500 -11.37500 1.000 17.68191 ? 90  PHE   B CG    1 
ATOM   710  C  CD1   . PHE   A 1 91  ? 40.38000  -20.28600 -12.00200 1.000 13.28667 ? 90  PHE   B CD1   1 
ATOM   711  C  CD2   . PHE   A 1 91  ? 38.04300  -20.20600 -11.49200 1.000 19.33338 ? 90  PHE   B CD2   1 
ATOM   712  C  CE1   . PHE   A 1 91  ? 40.27100  -19.08800 -12.71000 1.000 16.07248 ? 90  PHE   B CE1   1 
ATOM   713  C  CE2   . PHE   A 1 91  ? 37.92300  -19.01800 -12.20400 1.000 18.94824 ? 90  PHE   B CE2   1 
ATOM   714  C  CZ    . PHE   A 1 91  ? 39.04100  -18.46000 -12.81100 1.000 21.93623 ? 90  PHE   B CZ    1 
ATOM   715  N  N     . GLU   A 1 92  ? 38.32400  -21.24800 -7.71200  1.000 16.92427 ? 91  GLU   B N     1 
ATOM   716  C  CA    . GLU   A 1 92  ? 37.71600  -20.31000 -6.76900  1.000 15.57342 ? 91  GLU   B CA    1 
ATOM   717  C  C     . GLU   A 1 92  ? 38.63500  -19.99300 -5.58800  1.000 20.75477 ? 91  GLU   B C     1 
ATOM   718  O  O     . GLU   A 1 92  ? 38.44600  -18.96700 -4.92800  1.000 18.30559 ? 91  GLU   B O     1 
ATOM   719  C  CB    . GLU   A 1 92  ? 36.38500  -20.87400 -6.27500  1.000 20.39481 ? 91  GLU   B CB    1 
ATOM   720  C  CG    . GLU   A 1 92  ? 35.39600  -21.08500 -7.41000  1.000 19.73394 ? 91  GLU   B CG    1 
ATOM   721  C  CD    . GLU   A 1 92  ? 34.10800  -21.77100 -6.97000  1.000 35.73600 ? 91  GLU   B CD    1 
ATOM   722  O  OE1   . GLU   A 1 92  ? 34.11100  -22.46200 -5.92500  1.000 32.51374 ? 91  GLU   B OE1   1 
ATOM   723  O  OE2   . GLU   A 1 92  ? 33.09200  -21.60500 -7.67800  1.000 30.95955 ? 91  GLU   B OE2   1 
ATOM   724  N  N     . ASP   A 1 93  ? 39.62100  -20.84800 -5.30600  1.000 15.72830 ? 92  ASP   B N     1 
ATOM   725  C  CA    . ASP   A 1 93  ? 40.58900  -20.58700 -4.24100  1.000 19.05027 ? 92  ASP   B CA    1 
ATOM   726  C  C     . ASP   A 1 93  ? 41.64700  -19.56800 -4.61600  1.000 17.82472 ? 92  ASP   B C     1 
ATOM   727  O  O     . ASP   A 1 93  ? 42.29400  -19.01600 -3.71600  1.000 18.40019 ? 92  ASP   B O     1 
ATOM   728  C  CB    . ASP   A 1 93  ? 41.32400  -21.86700 -3.84000  1.000 18.26557 ? 92  ASP   B CB    1 
ATOM   729  C  CG    . ASP   A 1 93  ? 40.56500  -22.67900 -2.82600  1.000 25.24898 ? 92  ASP   B CG    1 
ATOM   730  O  OD1   . ASP   A 1 93  ? 39.51600  -22.20100 -2.35400  1.000 23.26262 ? 92  ASP   B OD1   1 
ATOM   731  O  OD2   . ASP   A 1 93  ? 41.02900  -23.79100 -2.50000  1.000 23.80816 ? 92  ASP   B OD2   1 
ATOM   732  N  N     . ILE   A 1 94  ? 41.87000  -19.34000 -5.91100  1.000 13.06626 ? 93  ILE   B N     1 
ATOM   733  C  CA    . ILE   A 1 94  ? 43.05300  -18.59900 -6.34500  1.000 18.44519 ? 93  ILE   B CA    1 
ATOM   734  C  C     . ILE   A 1 94  ? 43.09600  -17.21500 -5.70300  1.000 14.26396 ? 93  ILE   B C     1 
ATOM   735  O  O     . ILE   A 1 94  ? 44.14600  -16.76400 -5.22000  1.000 12.94105 ? 93  ILE   B O     1 
ATOM   736  C  CB    . ILE   A 1 94  ? 43.09600  -18.51100 -7.88100  1.000 15.10580 ? 93  ILE   B CB    1 
ATOM   737  C  CG1   . ILE   A 1 94  ? 43.40600  -19.88200 -8.48300  1.000 13.69533 ? 93  ILE   B CG1   1 
ATOM   738  C  CG2   . ILE   A 1 94  ? 44.11500  -17.42200 -8.33200  1.000 15.01747 ? 93  ILE   B CG2   1 
ATOM   739  C  CD1   . ILE   A 1 94  ? 44.87400  -20.37400 -8.25400  1.000 12.19431 ? 93  ILE   B CD1   1 
ATOM   740  N  N     . HIS   A 1 95  ? 41.95600  -16.51600 -5.68900  1.000 12.61817 ? 94  HIS   B N     1 
ATOM   741  C  CA    . HIS   A 1 95  ? 41.96800  -15.14100 -5.20100  1.000 14.98712 ? 94  HIS   B CA    1 
ATOM   742  C  C     . HIS   A 1 95  ? 42.40100  -15.07700 -3.74500  1.000 14.57258 ? 94  HIS   B C     1 
ATOM   743  O  O     . HIS   A 1 95  ? 43.04300  -14.10400 -3.33400  1.000 13.06425 ? 94  HIS   B O     1 
ATOM   744  C  CB    . HIS   A 1 95  ? 40.59700  -14.47800 -5.41600  1.000 16.66932 ? 94  HIS   B CB    1 
ATOM   745  C  CG    . HIS   A 1 95  ? 39.50200  -14.99900 -4.53800  1.000 17.41742 ? 94  HIS   B CG    1 
ATOM   746  N  ND1   . HIS   A 1 95  ? 39.08400  -14.34400 -3.40000  1.000 19.58221 ? 94  HIS   B ND1   1 
ATOM   747  C  CD2   . HIS   A 1 95  ? 38.70800  -16.09300 -4.65300  1.000 20.71496 ? 94  HIS   B CD2   1 
ATOM   748  C  CE1   . HIS   A 1 95  ? 38.09400  -15.02000 -2.84000  1.000 22.99962 ? 94  HIS   B CE1   1 
ATOM   749  N  NE2   . HIS   A 1 95  ? 37.84400  -16.08400 -3.58200  1.000 23.71395 ? 94  HIS   B NE2   1 
ATOM   750  N  N     . HIS   A 1 96  ? 42.09600  -16.11800 -2.96400  1.000 16.81479 ? 95  HIS   B N     1 
ATOM   751  C  CA    . HIS   A 1 96  ? 42.55300  -16.16000 -1.57900  1.000 16.81083 ? 95  HIS   B CA    1 
ATOM   752  C  C     . HIS   A 1 96  ? 44.07100  -16.16600 -1.50600  1.000 13.77162 ? 95  HIS   B C     1 
ATOM   753  O  O     . HIS   A 1 96  ? 44.66200  -15.49100 -0.65200  1.000 12.22319 ? 95  HIS   B O     1 
ATOM   754  C  CB    . HIS   A 1 96  ? 42.00000  -17.39300 -0.86400  1.000 14.20753 ? 95  HIS   B CB    1 
ATOM   755  C  CG    . HIS   A 1 96  ? 40.52200  -17.34800 -0.61700  1.000 20.78670 ? 95  HIS   B CG    1 
ATOM   756  N  ND1   . HIS   A 1 96  ? 39.90300  -16.29500 0.02300   1.000 21.02940 ? 95  HIS   B ND1   1 
ATOM   757  C  CD2   . HIS   A 1 96  ? 39.54500  -18.24200 -0.90100  1.000 24.20944 ? 95  HIS   B CD2   1 
ATOM   758  C  CE1   . HIS   A 1 96  ? 38.60600  -16.53700 0.11000   1.000 25.11448 ? 95  HIS   B CE1   1 
ATOM   759  N  NE2   . HIS   A 1 96  ? 38.36300  -17.70900 -0.44700  1.000 22.25186 ? 95  HIS   B NE2   1 
ATOM   760  N  N     . TYR   A 1 97  ? 44.72200  -16.93300 -2.38600  1.000 10.93963 ? 96  TYR   B N     1 
ATOM   761  C  CA    . TYR   A 1 97  ? 46.18000  -16.97200 -2.36300  1.000 13.39612 ? 96  TYR   B CA    1 
ATOM   762  C  C     . TYR   A 1 97  ? 46.77100  -15.61100 -2.70400  1.000 13.91079 ? 96  TYR   B C     1 
ATOM   763  O  O     . TYR   A 1 97  ? 47.68200  -15.14600 -2.01200  1.000 14.42422 ? 96  TYR   B O     1 
ATOM   764  C  CB    . TYR   A 1 97  ? 46.71800  -18.04500 -3.31500  1.000 13.69444 ? 96  TYR   B CB    1 
ATOM   765  C  CG    . TYR   A 1 97  ? 46.48900  -19.44300 -2.79700  1.000 16.66816 ? 96  TYR   B CG    1 
ATOM   766  C  CD1   . TYR   A 1 97  ? 47.36900  -20.02300 -1.88400  1.000 14.99607 ? 96  TYR   B CD1   1 
ATOM   767  C  CD2   . TYR   A 1 97  ? 45.37700  -20.17400 -3.20100  1.000 14.61112 ? 96  TYR   B CD2   1 
ATOM   768  C  CE1   . TYR   A 1 97  ? 47.15000  -21.30000 -1.39000  1.000 9.71153  ? 96  TYR   B CE1   1 
ATOM   769  C  CE2   . TYR   A 1 97  ? 45.14400  -21.44100 -2.72600  1.000 13.85783 ? 96  TYR   B CE2   1 
ATOM   770  C  CZ    . TYR   A 1 97  ? 46.02800  -22.00700 -1.82000  1.000 14.71628 ? 96  TYR   B CZ    1 
ATOM   771  O  OH    . TYR   A 1 97  ? 45.76800  -23.27700 -1.35200  1.000 13.43722 ? 96  TYR   B OH    1 
ATOM   772  N  N     . ARG   A 1 98  ? 46.26300  -14.95100 -3.75700  1.000 10.41902 ? 97  ARG   B N     1 
ATOM   773  C  CA    . ARG   A 1 98  ? 46.81200  -13.64400 -4.11400  1.000 11.60251 ? 97  ARG   B CA    1 
ATOM   774  C  C     . ARG   A 1 98  ? 46.57300  -12.62900 -3.00500  1.000 14.20340 ? 97  ARG   B C     1 
ATOM   775  O  O     . ARG   A 1 98  ? 47.43900  -11.78100 -2.73300  1.000 11.70045 ? 97  ARG   B O     1 
ATOM   776  C  CB    . ARG   A 1 98  ? 46.22000  -13.14300 -5.42900  1.000 17.11570 ? 97  ARG   B CB    1 
ATOM   777  C  CG    . ARG   A 1 98  ? 46.68500  -11.74400 -5.82900  1.000 19.74565 ? 97  ARG   B CG    1 
ATOM   778  C  CD    . ARG   A 1 98  ? 46.15400  -11.36300 -7.19900  1.000 21.61314 ? 97  ARG   B CD    1 
ATOM   779  N  NE    . ARG   A 1 98  ? 46.27800  -9.93800  -7.48000  1.000 21.28156 ? 97  ARG   B NE    1 
ATOM   780  C  CZ    . ARG   A 1 98  ? 47.31700  -9.37500  -8.08200  1.000 29.31426 ? 97  ARG   B CZ    1 
ATOM   781  N  NH1   . ARG   A 1 98  ? 48.37800  -10.08400 -8.43900  1.000 21.27702 ? 97  ARG   B NH1   1 
ATOM   782  N  NH2   . ARG   A 1 98  ? 47.28700  -8.06900  -8.34300  1.000 28.64426 ? 97  ARG   B NH2   1 
ATOM   783  N  N     . GLU   A 1 99  ? 45.40600  -12.70300 -2.35400  1.000 12.44498 ? 98  GLU   B N     1 
ATOM   784  C  CA    . GLU   A 1 99  ? 45.10900  -11.78900 -1.25600  1.000 13.98489 ? 98  GLU   B CA    1 
ATOM   785  C  C     . GLU   A 1 99  ? 46.09300  -11.96600 -0.10400  1.000 17.26548 ? 98  GLU   B C     1 
ATOM   786  O  O     . GLU   A 1 99  ? 46.60700  -10.97800 0.44000   1.000 14.53277 ? 98  GLU   B O     1 
ATOM   787  C  CB    . GLU   A 1 99  ? 43.66600  -12.00000 -0.77300  1.000 16.82920 ? 98  GLU   B CB    1 
ATOM   788  C  CG    . GLU   A 1 99  ? 42.61800  -11.46000 -1.74100  1.000 26.89941 ? 98  GLU   B CG    1 
ATOM   789  C  CD    . GLU   A 1 99  ? 41.21700  -12.05700 -1.54700  1.000 28.00939 ? 98  GLU   B CD    1 
ATOM   790  O  OE1   . GLU   A 1 99  ? 41.00200  -12.83300 -0.58200  1.000 22.08863 ? 98  GLU   B OE1   1 
ATOM   791  O  OE2   . GLU   A 1 99  ? 40.32600  -11.73300 -2.37300  1.000 27.07893 ? 98  GLU   B OE2   1 
ATOM   792  N  N     . GLN   A 1 100 ? 46.36500  -13.22100 0.28600   1.000 12.47865 ? 99  GLN   B N     1 
ATOM   793  C  CA    . GLN   A 1 100 ? 47.28900  -13.48900 1.38100   1.000 15.01057 ? 99  GLN   B CA    1 
ATOM   794  C  C     . GLN   A 1 100 ? 48.71000  -13.06600 1.02800   1.000 14.27399 ? 99  GLN   B C     1 
ATOM   795  O  O     . GLN   A 1 100 ? 49.43100  -12.52700 1.87700   1.000 15.00695 ? 99  GLN   B O     1 
ATOM   796  C  CB    . GLN   A 1 100 ? 47.24500  -14.97900 1.75200   1.000 16.26088 ? 99  GLN   B CB    1 
ATOM   797  C  CG    . GLN   A 1 100 ? 45.89000  -15.47200 2.27300   1.000 24.32643 ? 99  GLN   B CG    1 
ATOM   798  C  CD    . GLN   A 1 100 ? 45.53200  -14.97300 3.68200   1.000 35.84423 ? 99  GLN   B CD    1 
ATOM   799  O  OE1   . GLN   A 1 100 ? 46.19700  -14.09600 4.24900   1.000 34.67861 ? 99  GLN   B OE1   1 
ATOM   800  N  NE2   . GLN   A 1 100 ? 44.45800  -15.53100 4.24400   1.000 43.41623 ? 99  GLN   B NE2   1 
ATOM   801  N  N     . ILE   A 1 101 ? 49.12900  -13.30500 -0.21500  1.000 11.97981 ? 100 ILE   B N     1 
ATOM   802  C  CA    . ILE   A 1 101 ? 50.48600  -12.94100 -0.62800  1.000 13.74334 ? 100 ILE   B CA    1 
ATOM   803  C  C     . ILE   A 1 101 ? 50.67500  -11.43200 -0.56600  1.000 11.22757 ? 100 ILE   B C     1 
ATOM   804  O  O     . ILE   A 1 101 ? 51.67700  -10.94100 -0.03600  1.000 12.18679 ? 100 ILE   B O     1 
ATOM   805  C  CB    . ILE   A 1 101 ? 50.79100  -13.48200 -2.03500  1.000 10.52002 ? 100 ILE   B CB    1 
ATOM   806  C  CG1   . ILE   A 1 101 ? 50.85400  -15.00100 -2.04100  1.000 11.09426 ? 100 ILE   B CG1   1 
ATOM   807  C  CG2   . ILE   A 1 101 ? 52.13800  -12.99000 -2.52200  1.000 12.78507 ? 100 ILE   B CG2   1 
ATOM   808  C  CD1   . ILE   A 1 101 ? 50.82600  -15.55500 -3.42700  1.000 10.34290 ? 100 ILE   B CD1   1 
ATOM   809  N  N     . LYS   A 1 102 ? 49.71300  -10.68000 -1.10200  1.000 11.77867 ? 101 LYS   B N     1 
ATOM   810  C  CA    . LYS   A 1 102 ? 49.77500  -9.22200  -1.05200  1.000 13.66288 ? 101 LYS   B CA    1 
ATOM   811  C  C     . LYS   A 1 102 ? 49.77500  -8.71200  0.38300   1.000 13.70777 ? 101 LYS   B C     1 
ATOM   812  O  O     . LYS   A 1 102 ? 50.44300  -7.72200  0.69400   1.000 14.31943 ? 101 LYS   B O     1 
ATOM   813  C  CB    . LYS   A 1 102 ? 48.59300  -8.60900  -1.82100  1.000 14.97395 ? 101 LYS   B CB    1 
ATOM   814  C  CG    . LYS   A 1 102 ? 48.59500  -8.90300  -3.31400  1.000 16.91826 ? 101 LYS   B CG    1 
ATOM   815  C  CD    . LYS   A 1 102 ? 47.82100  -7.84500  -4.09500  1.000 20.87197 ? 101 LYS   B CD    1 
ATOM   816  C  CE    . LYS   A 1 102 ? 46.36300  -7.86400  -3.74700  1.000 20.52680 ? 101 LYS   B CE    1 
ATOM   817  N  NZ    . LYS   A 1 102 ? 45.67300  -6.60400  -4.16900  1.000 23.72823 ? 101 LYS   B NZ    1 
ATOM   818  N  N     . ARG   A 1 103 ? 49.01100  -9.36000  1.26400   1.000 13.99278 ? 102 ARG   B N     1 
ATOM   819  C  CA    . ARG   A 1 103 ? 48.95000  -8.93300  2.65800   1.000 15.07702 ? 102 ARG   B CA    1 
ATOM   820  C  C     . ARG   A 1 103 ? 50.27500  -9.16400  3.37200   1.000 14.72563 ? 102 ARG   B C     1 
ATOM   821  O  O     . ARG   A 1 103 ? 50.79000  -8.26100  4.03900   1.000 15.61213 ? 102 ARG   B O     1 
ATOM   822  C  CB    . ARG   A 1 103 ? 47.83300  -9.66900  3.38600   1.000 15.54495 ? 102 ARG   B CB    1 
ATOM   823  C  CG    . ARG   A 1 103 ? 47.71600  -9.28300  4.85300   1.000 19.18012 ? 102 ARG   B CG    1 
ATOM   824  C  CD    . ARG   A 1 103 ? 46.69300  -10.14900 5.59700   1.000 21.91180 ? 102 ARG   B CD    1 
ATOM   825  N  NE    . ARG   A 1 103 ? 47.07200  -11.56000 5.61800   1.000 26.93238 ? 102 ARG   B NE    1 
ATOM   826  C  CZ    . ARG   A 1 103 ? 48.02600  -12.06800 6.38900   1.000 24.03732 ? 102 ARG   B CZ    1 
ATOM   827  N  NH1   . ARG   A 1 103 ? 48.77700  -11.29600 7.16200   1.000 25.67184 ? 102 ARG   B NH1   1 
ATOM   828  N  NH2   . ARG   A 1 103 ? 48.24000  -13.38100 6.37900   1.000 31.55915 ? 102 ARG   B NH2   1 
ATOM   829  N  N     . VAL   A 1 104 ? 50.81300  -10.38100 3.27600   1.000 13.60807 ? 103 VAL   B N     1 
ATOM   830  C  CA    . VAL   A 1 104 ? 52.06100  -10.71800 3.96600   1.000 14.23834 ? 103 VAL   B CA    1 
ATOM   831  C  C     . VAL   A 1 104 ? 53.19900  -9.85000  3.45400   1.000 13.31735 ? 103 VAL   B C     1 
ATOM   832  O  O     . VAL   A 1 104 ? 54.02900  -9.35300  4.22400   1.000 13.94775 ? 103 VAL   B O     1 
ATOM   833  C  CB    . VAL   A 1 104 ? 52.37600  -12.21800 3.79700   1.000 13.32984 ? 103 VAL   B CB    1 
ATOM   834  C  CG1   . VAL   A 1 104 ? 53.78100  -12.53300 4.29400   1.000 12.12246 ? 103 VAL   B CG1   1 
ATOM   835  C  CG2   . VAL   A 1 104 ? 51.35500  -13.05800 4.53300   1.000 16.83704 ? 103 VAL   B CG2   1 
ATOM   836  N  N     . LYS   A 1 105 ? 53.24200  -9.64300  2.14700   1.000 12.69436 ? 104 LYS   B N     1 
ATOM   837  C  CA    . LYS   A 1 105 ? 54.26900  -8.85000  1.50200   1.000 15.97046 ? 104 LYS   B CA    1 
ATOM   838  C  C     . LYS   A 1 105 ? 54.00800  -7.35300  1.58400   1.000 13.87317 ? 104 LYS   B C     1 
ATOM   839  O  O     . LYS   A 1 105 ? 54.90500  -6.57200  1.25100   1.000 14.13560 ? 104 LYS   B O     1 
ATOM   840  C  CB    . LYS   A 1 105 ? 54.38200  -9.28900  0.04300   1.000 13.68438 ? 104 LYS   B CB    1 
ATOM   841  C  CG    . LYS   A 1 105 ? 55.05300  -10.62600 -0.11300  1.000 15.38090 ? 104 LYS   B CG    1 
ATOM   842  C  CD    . LYS   A 1 105 ? 56.34200  -10.36200 -0.87200  1.000 27.40612 ? 104 LYS   B CD    1 
ATOM   843  C  CE    . LYS   A 1 105 ? 57.06400  -11.61100 -1.19300  1.000 16.42871 ? 104 LYS   B CE    1 
ATOM   844  N  NZ    . LYS   A 1 105 ? 58.15000  -11.84400 -0.21600  1.000 9.79229  ? 104 LYS   B NZ    1 
ATOM   845  N  N     . ASP   A 1 106 ? 52.81300  -6.94400  2.02200   1.000 14.74382 ? 105 ASP   B N     1 
ATOM   846  C  CA    . ASP   A 1 106 ? 52.42600  -5.53500  2.11100   1.000 16.10750 ? 105 ASP   B CA    1 
ATOM   847  C  C     . ASP   A 1 106 ? 52.70800  -4.81400  0.79300   1.000 16.32004 ? 105 ASP   B C     1 
ATOM   848  O  O     . ASP   A 1 106 ? 53.38800  -3.77900  0.74200   1.000 16.72767 ? 105 ASP   B O     1 
ATOM   849  C  CB    . ASP   A 1 106 ? 53.12400  -4.84400  3.29400   1.000 17.18700 ? 105 ASP   B CB    1 
ATOM   850  C  CG    . ASP   A 1 106 ? 52.67300  -3.39800  3.49400   1.000 18.83385 ? 105 ASP   B CG    1 
ATOM   851  O  OD1   . ASP   A 1 106 ? 51.45200  -3.14400  3.55000   1.000 19.58900 ? 105 ASP   B OD1   1 
ATOM   852  O  OD2   . ASP   A 1 106 ? 53.54900  -2.50900  3.61200   1.000 20.00937 ? 105 ASP   B OD2   1 
ATOM   853  N  N     . SER   A 1 107 ? 52.16900  -5.37400  -0.29100  1.000 15.20467 ? 106 SER   B N     1 
ATOM   854  C  CA    . SER   A 1 107 ? 52.41000  -4.82300  -1.61400  1.000 18.14976 ? 106 SER   B CA    1 
ATOM   855  C  C     . SER   A 1 107 ? 51.25900  -5.13700  -2.55900  1.000 18.67338 ? 106 SER   B C     1 
ATOM   856  O  O     . SER   A 1 107 ? 50.61800  -6.18500  -2.45800  1.000 18.47267 ? 106 SER   B O     1 
ATOM   857  C  CB    . SER   A 1 107 ? 53.71000  -5.35700  -2.21000  1.000 17.40958 ? 106 SER   B CB    1 
ATOM   858  O  OG    . SER   A 1 107 ? 53.90000  -4.82300  -3.50800  1.000 23.04161 ? 106 SER   B OG    1 
ATOM   859  N  N     . GLU   A 1 108 ? 51.01300  -4.20900  -3.49000  1.000 19.79925 ? 107 GLU   B N     1 
ATOM   860  C  CA    . GLU   A 1 108 ? 50.08000  -4.44800  -4.58400  1.000 21.91145 ? 107 GLU   B CA    1 
ATOM   861  C  C     . GLU   A 1 108 ? 50.71600  -5.22000  -5.72900  1.000 24.71066 ? 107 GLU   B C     1 
ATOM   862  O  O     . GLU   A 1 108 ? 49.99700  -5.73900  -6.58800  1.000 25.47774 ? 107 GLU   B O     1 
ATOM   863  C  CB    . GLU   A 1 108 ? 49.54800  -3.11900  -5.12900  1.000 26.42889 ? 107 GLU   B CB    1 
ATOM   864  C  CG    . GLU   A 1 108 ? 48.74500  -2.31900  -4.13400  1.000 26.87501 ? 107 GLU   B CG    1 
ATOM   865  C  CD    . GLU   A 1 108 ? 47.28500  -2.73000  -4.10800  1.000 28.04784 ? 107 GLU   B CD    1 
ATOM   866  O  OE1   . GLU   A 1 108 ? 46.98700  -3.83600  -3.60300  1.000 32.01237 ? 107 GLU   B OE1   1 
ATOM   867  O  OE2   . GLU   A 1 108 ? 46.44600  -1.93800  -4.59700  1.000 30.62957 ? 107 GLU   B OE2   1 
ATOM   868  N  N     . ASP   A 1 109 ? 52.04600  -5.30200  -5.76200  1.000 21.12623 ? 108 ASP   B N     1 
ATOM   869  C  CA    . ASP   A 1 109 ? 52.79000  -5.76800  -6.93200  1.000 24.45048 ? 108 ASP   B CA    1 
ATOM   870  C  C     . ASP   A 1 109 ? 53.77700  -6.85100  -6.48900  1.000 21.73113 ? 108 ASP   B C     1 
ATOM   871  O  O     . ASP   A 1 109 ? 54.89400  -6.55200  -6.05500  1.000 21.35423 ? 108 ASP   B O     1 
ATOM   872  C  CB    . ASP   A 1 109 ? 53.47900  -4.56800  -7.59800  1.000 21.70653 ? 108 ASP   B CB    1 
ATOM   873  C  CG    . ASP   A 1 109 ? 54.29900  -4.95200  -8.79800  1.000 29.82003 ? 108 ASP   B CG    1 
ATOM   874  O  OD1   . ASP   A 1 109 ? 53.84600  -5.79900  -9.60500  1.000 26.67206 ? 108 ASP   B OD1   1 
ATOM   875  O  OD2   . ASP   A 1 109 ? 55.40100  -4.38700  -8.93600  1.000 33.18473 ? 108 ASP   B OD2   1 
ATOM   876  N  N     . VAL   A 1 110 ? 53.36300  -8.11100  -6.58600  1.000 16.17887 ? 109 VAL   B N     1 
ATOM   877  C  CA    . VAL   A 1 110 ? 54.19000  -9.25700  -6.21600  1.000 13.02408 ? 109 VAL   B CA    1 
ATOM   878  C  C     . VAL   A 1 110 ? 54.28000  -10.17300 -7.41400  1.000 14.59603 ? 109 VAL   B C     1 
ATOM   879  O  O     . VAL   A 1 110 ? 53.24500  -10.53000 -7.98500  1.000 10.83594 ? 109 VAL   B O     1 
ATOM   880  C  CB    . VAL   A 1 110 ? 53.62500  -10.03200 -5.00700  1.000 18.02920 ? 109 VAL   B CB    1 
ATOM   881  C  CG1   . VAL   A 1 110 ? 54.53900  -11.21800 -4.69100  1.000 9.88316  ? 109 VAL   B CG1   1 
ATOM   882  C  CG2   . VAL   A 1 110 ? 53.45000  -9.14200  -3.78500  1.000 10.84309 ? 109 VAL   B CG2   1 
ATOM   883  N  N     . PRO   A 1 111 ? 55.47500  -10.62200 -7.82000  1.000 11.85555 ? 110 PRO   B N     1 
ATOM   884  C  CA    . PRO   A 1 111 ? 55.59200  -11.53300 -8.97300  1.000 10.07579 ? 110 PRO   B CA    1 
ATOM   885  C  C     . PRO   A 1 111 ? 54.77100  -12.80000 -8.77500  1.000 10.60301 ? 110 PRO   B C     1 
ATOM   886  O  O     . PRO   A 1 111 ? 54.93400  -13.52600 -7.79200  1.000 7.87467  ? 110 PRO   B O     1 
ATOM   887  C  CB    . PRO   A 1 111 ? 57.10000  -11.82700 -9.03700  1.000 11.73242 ? 110 PRO   B CB    1 
ATOM   888  C  CG    . PRO   A 1 111 ? 57.74100  -10.65900 -8.36000  1.000 14.35769 ? 110 PRO   B CG    1 
ATOM   889  C  CD    . PRO   A 1 111 ? 56.79400  -10.25600 -7.27000  1.000 10.60686 ? 110 PRO   B CD    1 
ATOM   890  N  N     . MET   A 1 112 ? 53.85500  -13.04300 -9.71400  1.000 12.65045 ? 111 MET   B N     1 
ATOM   891  C  CA    . MET   A 1 112 ? 52.96400  -14.20000 -9.66500  1.000 12.53632 ? 111 MET   B CA    1 
ATOM   892  C  C     . MET   A 1 112 ? 52.61600  -14.63200 -11.07900 1.000 10.71337 ? 111 MET   B C     1 
ATOM   893  O  O     . MET   A 1 112 ? 52.54700  -13.80700 -11.99300 1.000 9.50727  ? 111 MET   B O     1 
ATOM   894  C  CB    . MET   A 1 112 ? 51.64500  -13.89200 -8.94700  1.000 14.56281 ? 111 MET   B CB    1 
ATOM   895  C  CG    . MET   A 1 112 ? 51.71700  -13.57700 -7.47500  1.000 16.98073 ? 111 MET   B CG    1 
ATOM   896  S  SD    . MET   A 1 112 ? 50.04000  -13.12600 -6.93400  1.000 16.69826 ? 111 MET   B SD    1 
ATOM   897  C  CE    . MET   A 1 112 ? 50.46400  -11.94500 -5.66500  1.000 16.07376 ? 111 MET   B CE    1 
ATOM   898  N  N     . VAL   A 1 113 ? 52.32300  -15.92100 -11.24000 1.000 11.01993 ? 112 VAL   B N     1 
ATOM   899  C  CA    . VAL   A 1 113 ? 51.85300  -16.46400 -12.51100 1.000 10.68705 ? 112 VAL   B CA    1 
ATOM   900  C  C     . VAL   A 1 113 ? 50.69100  -17.39500 -12.20000 1.000 8.76177  ? 112 VAL   B C     1 
ATOM   901  O  O     . VAL   A 1 113 ? 50.74000  -18.14000 -11.21900 1.000 8.75299  ? 112 VAL   B O     1 
ATOM   902  C  CB    . VAL   A 1 113 ? 52.97200  -17.19600 -13.28200 1.000 12.58697 ? 112 VAL   B CB    1 
ATOM   903  C  CG1   . VAL   A 1 113 ? 52.41100  -17.93900 -14.48500 1.000 10.30363 ? 112 VAL   B CG1   1 
ATOM   904  C  CG2   . VAL   A 1 113 ? 54.04400  -16.17900 -13.75000 1.000 12.39713 ? 112 VAL   B CG2   1 
ATOM   905  N  N     . LEU   A 1 114 ? 49.61700  -17.28800 -12.97500 1.000 8.83568  ? 113 LEU   B N     1 
ATOM   906  C  CA    . LEU   A 1 114 ? 48.47600  -18.18500 -12.82900 1.000 8.96433  ? 113 LEU   B CA    1 
ATOM   907  C  C     . LEU   A 1 114 ? 48.70700  -19.42200 -13.67700 1.000 9.86703  ? 113 LEU   B C     1 
ATOM   908  O  O     . LEU   A 1 114 ? 48.99200  -19.31600 -14.87400 1.000 11.22182 ? 113 LEU   B O     1 
ATOM   909  C  CB    . LEU   A 1 114 ? 47.17200  -17.49700 -13.24100 1.000 10.14241 ? 113 LEU   B CB    1 
ATOM   910  C  CG    . LEU   A 1 114 ? 45.88400  -18.30100 -13.06400 1.000 10.25686 ? 113 LEU   B CG    1 
ATOM   911  C  CD1   . LEU   A 1 114 ? 45.59600  -18.51700 -11.58900 1.000 9.98698  ? 113 LEU   B CD1   1 
ATOM   912  C  CD2   . LEU   A 1 114 ? 44.73400  -17.59100 -13.71900 1.000 11.40161 ? 113 LEU   B CD2   1 
ATOM   913  N  N     . VAL   A 1 115 ? 48.57500  -20.59100 -13.06300 1.000 8.51862  ? 114 VAL   B N     1 
ATOM   914  C  CA    . VAL   A 1 115 ? 48.86200  -21.86200 -13.71400 1.000 8.53455  ? 114 VAL   B CA    1 
ATOM   915  C  C     . VAL   A 1 115 ? 47.58800  -22.70300 -13.72500 1.000 9.00248  ? 114 VAL   B C     1 
ATOM   916  O  O     . VAL   A 1 115 ? 47.09400  -23.09500 -12.66100 1.000 8.95256  ? 114 VAL   B O     1 
ATOM   917  C  CB    . VAL   A 1 115 ? 49.99600  -22.60500 -12.99600 1.000 7.84868  ? 114 VAL   B CB    1 
ATOM   918  C  CG1   . VAL   A 1 115 ? 50.27100  -23.94800 -13.65300 1.000 8.37187  ? 114 VAL   B CG1   1 
ATOM   919  C  CG2   . VAL   A 1 115 ? 51.24400  -21.75100 -12.98000 1.000 7.65770  ? 114 VAL   B CG2   1 
ATOM   920  N  N     . GLY   A 1 116 ? 47.08800  -23.00300 -14.92000 1.000 9.71492  ? 115 GLY   B N     1 
ATOM   921  C  CA    . GLY   A 1 116 ? 45.96300  -23.90600 -15.09400 1.000 10.29968 ? 115 GLY   B CA    1 
ATOM   922  C  C     . GLY   A 1 116 ? 46.43900  -25.29200 -15.48400 1.000 10.71826 ? 115 GLY   B C     1 
ATOM   923  O  O     . GLY   A 1 116 ? 46.76100  -25.53300 -16.64800 1.000 10.86759 ? 115 GLY   B O     1 
ATOM   924  N  N     . ASN   A 1 117 ? 46.50100  -26.20800 -14.51800 1.000 10.96369 ? 116 ASN   B N     1 
ATOM   925  C  CA    . ASN   A 1 117 ? 47.17200  -27.49100 -14.69800 1.000 12.79804 ? 116 ASN   B CA    1 
ATOM   926  C  C     . ASN   A 1 117 ? 46.16400  -28.61000 -14.99900 1.000 13.66413 ? 116 ASN   B C     1 
ATOM   927  O  O     . ASN   A 1 117 ? 44.94600  -28.43700 -14.88400 1.000 13.71897 ? 116 ASN   B O     1 
ATOM   928  C  CB    . ASN   A 1 117 ? 48.00700  -27.82000 -13.45600 1.000 10.89419 ? 116 ASN   B CB    1 
ATOM   929  C  CG    . ASN   A 1 117 ? 48.85200  -29.07200 -13.62900 1.000 12.49041 ? 116 ASN   B CG    1 
ATOM   930  O  OD1   . ASN   A 1 117 ? 49.46900  -29.27700 -14.67100 1.000 11.26352 ? 116 ASN   B OD1   1 
ATOM   931  N  ND2   . ASN   A 1 117 ? 48.86000  -29.92400 -12.61200 1.000 9.07321  ? 116 ASN   B ND2   1 
ATOM   932  N  N     . LYS   A 1 118 ? 46.70700  -29.77300 -15.40100 1.000 10.99734 ? 117 LYS   B N     1 
ATOM   933  C  CA    . LYS   A 1 118 ? 45.93900  -30.94400 -15.85900 1.000 11.93250 ? 117 LYS   B CA    1 
ATOM   934  C  C     . LYS   A 1 118 ? 45.18000  -30.66100 -17.15300 1.000 15.56236 ? 117 LYS   B C     1 
ATOM   935  O  O     . LYS   A 1 118 ? 44.07600  -31.18700 -17.36900 1.000 16.31991 ? 117 LYS   B O     1 
ATOM   936  C  CB    . LYS   A 1 118 ? 44.98700  -31.45800 -14.77000 1.000 14.74480 ? 117 LYS   B CB    1 
ATOM   937  C  CG    . LYS   A 1 118 ? 45.64300  -31.60200 -13.39000 1.000 11.07845 ? 117 LYS   B CG    1 
ATOM   938  C  CD    . LYS   A 1 118 ? 44.85400  -32.55400 -12.51700 1.000 11.77758 ? 117 LYS   B CD    1 
ATOM   939  C  CE    . LYS   A 1 118 ? 45.48400  -32.67500 -11.12400 1.000 11.10165 ? 117 LYS   B CE    1 
ATOM   940  N  NZ    . LYS   A 1 118 ? 44.67800  -33.59400 -10.27000 1.000 11.30390 ? 117 LYS   B NZ    1 
ATOM   941  N  N     . SER   A 1 119 ? 45.77400  -29.84200 -18.03300 1.000 13.01243 ? 118 SER   B N     1 
ATOM   942  C  CA    . SER   A 1 119 ? 45.16300  -29.48500 -19.30800 1.000 14.25986 ? 118 SER   B CA    1 
ATOM   943  C  C     . SER   A 1 119 ? 45.04600  -30.67300 -20.26000 1.000 19.22004 ? 118 SER   B C     1 
ATOM   944  O  O     . SER   A 1 119 ? 44.41100  -30.54400 -21.31400 1.000 17.09143 ? 118 SER   B O     1 
ATOM   945  C  CB    . SER   A 1 119 ? 45.96200  -28.36300 -19.97600 1.000 17.64144 ? 118 SER   B CB    1 
ATOM   946  O  OG    . SER   A 1 119 ? 46.16500  -27.27100 -19.08900 1.000 20.11117 ? 118 SER   B OG    1 
ATOM   947  N  N     . ASP   A 1 120 ? 45.63600  -31.81800 -19.91800 1.000 15.16495 ? 119 ASP   B N     1 
ATOM   948  C  CA    . ASP   A 1 120 ? 45.48900  -33.03600 -20.70200 1.000 16.39602 ? 119 ASP   B CA    1 
ATOM   949  C  C     . ASP   A 1 120 ? 44.16500  -33.74900 -20.46200 1.000 17.11375 ? 119 ASP   B C     1 
ATOM   950  O  O     . ASP   A 1 120 ? 43.84700  -34.69600 -21.19200 1.000 19.39269 ? 119 ASP   B O     1 
ATOM   951  C  CB    . ASP   A 1 120 ? 46.62900  -34.00300 -20.38200 1.000 17.10138 ? 119 ASP   B CB    1 
ATOM   952  C  CG    . ASP   A 1 120 ? 46.68500  -34.36800 -18.91500 1.000 16.94759 ? 119 ASP   B CG    1 
ATOM   953  O  OD1   . ASP   A 1 120 ? 47.19400  -33.54500 -18.11300 1.000 13.99869 ? 119 ASP   B OD1   1 
ATOM   954  O  OD2   . ASP   A 1 120 ? 46.18900  -35.46600 -18.55700 1.000 15.68445 ? 119 ASP   B OD2   1 
ATOM   955  N  N     . LEU   A 1 121 ? 43.42800  -33.35900 -19.47400 1.000 17.56144 ? 120 LEU   B N     1 
ATOM   956  C  CA    . LEU   A 1 121 ? 42.33500  -34.23700 -19.08900 1.000 17.21021 ? 120 LEU   B CA    1 
ATOM   957  C  C     . LEU   A 1 121 ? 41.05400  -33.87600 -19.83100 1.000 19.14421 ? 120 LEU   B C     1 
ATOM   958  O  O     . LEU   A 1 121 ? 40.82100  -32.71000 -20.16000 1.000 18.32796 ? 120 LEU   B O     1 
ATOM   959  C  CB    . LEU   A 1 121 ? 42.09500  -34.16000 -17.58300 1.000 17.37661 ? 120 LEU   B CB    1 
ATOM   960  C  CG    . LEU   A 1 121 ? 43.13200  -34.95700 -16.77900 1.000 19.95612 ? 120 LEU   B CG    1 
ATOM   961  C  CD1   . LEU   A 1 121 ? 42.86900  -34.91200 -15.27700 1.000 23.90522 ? 120 LEU   B CD1   1 
ATOM   962  C  CD2   . LEU   A 1 121 ? 43.22900  -36.39100 -17.26900 1.000 17.54693 ? 120 LEU   B CD2   1 
ATOM   963  N  N     . PRO   A 1 122 ? 40.20900  -34.87000 -20.10100 1.000 19.64842 ? 121 PRO   B N     1 
ATOM   964  C  CA    . PRO   A 1 122 ? 38.94800  -34.61600 -20.80000 1.000 21.33788 ? 121 PRO   B CA    1 
ATOM   965  C  C     . PRO   A 1 122 ? 37.81300  -34.13800 -19.91000 1.000 20.95232 ? 121 PRO   B C     1 
ATOM   966  O  O     . PRO   A 1 122 ? 36.67400  -34.09500 -20.37600 1.000 22.28191 ? 121 PRO   B O     1 
ATOM   967  C  CB    . PRO   A 1 122 ? 38.61500  -35.99700 -21.37900 1.000 22.46518 ? 121 PRO   B CB    1 
ATOM   968  C  CG    . PRO   A 1 122 ? 39.11700  -36.93000 -20.32600 1.000 21.70799 ? 121 PRO   B CG    1 
ATOM   969  C  CD    . PRO   A 1 122 ? 40.39000  -36.29700 -19.79200 1.000 21.14239 ? 121 PRO   B CD    1 
ATOM   970  N  N     . SER   A 1 123 ? 38.07900  -33.78100 -18.65900 1.000 20.54893 ? 122 SER   B N     1 
ATOM   971  C  CA    . SER   A 1 123 ? 37.03300  -33.54800 -17.66700 1.000 21.38090 ? 122 SER   B CA    1 
ATOM   972  C  C     . SER   A 1 123 ? 36.97200  -32.08500 -17.23000 1.000 18.97244 ? 122 SER   B C     1 
ATOM   973  O  O     . SER   A 1 123 ? 36.65600  -31.77400 -16.08500 1.000 18.46985 ? 122 SER   B O     1 
ATOM   974  C  CB    . SER   A 1 123 ? 37.24100  -34.45700 -16.46300 1.000 19.15486 ? 122 SER   B CB    1 
ATOM   975  O  OG    . SER   A 1 123 ? 38.54600  -34.27700 -15.94000 1.000 17.75011 ? 122 SER   B OG    1 
ATOM   976  N  N     . ARG   A 1 124 ? 37.23900  -31.17300 -18.15900 1.000 21.34478 ? 123 ARG   B N     1 
ATOM   977  C  CA    . ARG   A 1 124 ? 37.35400  -29.75600 -17.82600 1.000 21.28371 ? 123 ARG   B CA    1 
ATOM   978  C  C     . ARG   A 1 124 ? 36.07800  -29.22400 -17.18900 1.000 21.75108 ? 123 ARG   B C     1 
ATOM   979  O  O     . ARG   A 1 124 ? 34.96800  -29.50100 -17.65300 1.000 20.53548 ? 123 ARG   B O     1 
ATOM   980  C  CB    . ARG   A 1 124 ? 37.67500  -28.94400 -19.08700 1.000 19.47335 ? 123 ARG   B CB    1 
ATOM   981  C  CG    . ARG   A 1 124 ? 37.56200  -27.44500 -18.90000 1.000 19.46517 ? 123 ARG   B CG    1 
ATOM   982  C  CD    . ARG   A 1 124 ? 37.90000  -26.69400 -20.18100 1.000 19.24975 ? 123 ARG   B CD    1 
ATOM   983  N  NE    . ARG   A 1 124 ? 39.29300  -26.85600 -20.58900 1.000 20.36160 ? 123 ARG   B NE    1 
ATOM   984  C  CZ    . ARG   A 1 124 ? 40.29900  -26.10200 -20.15600 1.000 24.14351 ? 123 ARG   B CZ    1 
ATOM   985  N  NH1   . ARG   A 1 124 ? 40.12000  -25.16400 -19.23800 1.000 20.46667 ? 123 ARG   B NH1   1 
ATOM   986  N  NH2   . ARG   A 1 124 ? 41.51600  -26.29300 -20.65500 1.000 16.80982 ? 123 ARG   B NH2   1 
ATOM   987  N  N     . THR   A 1 125 ? 36.25000  -28.44500 -16.11200 1.000 20.51027 ? 124 THR   B N     1 
ATOM   988  C  CA    . THR   A 1 125 ? 35.15600  -27.70500 -15.49500 1.000 18.84735 ? 124 THR   B CA    1 
ATOM   989  C  C     . THR   A 1 125 ? 35.40700  -26.20700 -15.43100 1.000 18.49292 ? 124 THR   B C     1 
ATOM   990  O  O     . THR   A 1 125 ? 34.47500  -25.46100 -15.12800 1.000 19.34451 ? 124 THR   B O     1 
ATOM   991  C  CB    . THR   A 1 125 ? 34.88200  -28.20000 -14.06400 1.000 18.48357 ? 124 THR   B CB    1 
ATOM   992  O  OG1   . THR   A 1 125 ? 35.98100  -27.83500 -13.22000 1.000 16.98090 ? 124 THR   B OG1   1 
ATOM   993  C  CG2   . THR   A 1 125 ? 34.69500  -29.68800 -14.03600 1.000 18.86217 ? 124 THR   B CG2   1 
ATOM   994  N  N     . VAL   A 1 126 ? 36.63300  -25.75100 -15.67000 1.000 17.38786 ? 125 VAL   B N     1 
ATOM   995  C  CA    . VAL   A 1 126 ? 36.96900  -24.33100 -15.66700 1.000 21.96053 ? 125 VAL   B CA    1 
ATOM   996  C  C     . VAL   A 1 126 ? 37.31600  -23.95200 -17.09700 1.000 18.47365 ? 125 VAL   B C     1 
ATOM   997  O  O     . VAL   A 1 126 ? 38.25600  -24.50700 -17.67200 1.000 22.33497 ? 125 VAL   B O     1 
ATOM   998  C  CB    . VAL   A 1 126 ? 38.15100  -24.02000 -14.73000 1.000 17.60950 ? 125 VAL   B CB    1 
ATOM   999  C  CG1   . VAL   A 1 126 ? 38.41000  -22.51500 -14.69100 1.000 18.71658 ? 125 VAL   B CG1   1 
ATOM   1000 C  CG2   . VAL   A 1 126 ? 37.91900  -24.57400 -13.32300 1.000 17.46739 ? 125 VAL   B CG2   1 
ATOM   1001 N  N     . ASP   A 1 127 ? 36.57800  -23.02000 -17.69100 1.000 23.76874 ? 126 ASP   B N     1 
ATOM   1002 C  CA    . ASP   A 1 127 ? 36.95800  -22.66600 -19.05200 1.000 24.86939 ? 126 ASP   B CA    1 
ATOM   1003 C  C     . ASP   A 1 127 ? 38.09700  -21.65700 -19.01300 1.000 25.71354 ? 126 ASP   B C     1 
ATOM   1004 O  O     . ASP   A 1 127 ? 38.24500  -20.89100 -18.05400 1.000 23.98047 ? 126 ASP   B O     1 
ATOM   1005 C  CB    . ASP   A 1 127 ? 35.77100  -22.14200 -19.86300 1.000 40.97015 ? 126 ASP   B CB    1 
ATOM   1006 C  CG    . ASP   A 1 127 ? 35.24700  -20.82200 -19.36400 1.000 42.45100 ? 126 ASP   B CG    1 
ATOM   1007 O  OD1   . ASP   A 1 127 ? 35.89200  -19.78600 -19.63500 1.000 40.57442 ? 126 ASP   B OD1   1 
ATOM   1008 O  OD2   . ASP   A 1 127 ? 34.16900  -20.82400 -18.72900 1.000 51.73767 ? 126 ASP   B OD2   1 
ATOM   1009 N  N     . THR   A 1 128 ? 38.93600  -21.69300 -20.05300 1.000 22.51437 ? 127 THR   B N     1 
ATOM   1010 C  CA    . THR   A 1 128 ? 40.16800  -20.91400 -20.00600 1.000 23.66430 ? 127 THR   B CA    1 
ATOM   1011 C  C     . THR   A 1 128 ? 39.88900  -19.42000 -20.10700 1.000 25.05934 ? 127 THR   B C     1 
ATOM   1012 O  O     . THR   A 1 128 ? 40.65200  -18.61700 -19.55700 1.000 20.42127 ? 127 THR   B O     1 
ATOM   1013 C  CB    . THR   A 1 128 ? 41.13700  -21.37400 -21.09800 1.000 27.00607 ? 127 THR   B CB    1 
ATOM   1014 O  OG1   . THR   A 1 128 ? 40.88000  -20.66900 -22.31200 1.000 40.04333 ? 127 THR   B OG1   1 
ATOM   1015 C  CG2   . THR   A 1 128 ? 40.97800  -22.85700 -21.36000 1.000 19.88479 ? 127 THR   B CG2   1 
ATOM   1016 N  N     . LYS   A 1 129 ? 38.78200  -19.02500 -20.74900 1.000 23.76721 ? 128 LYS   B N     1 
ATOM   1017 C  CA    . LYS   A 1 129 ? 38.43200  -17.60600 -20.77500 1.000 29.72497 ? 128 LYS   B CA    1 
ATOM   1018 C  C     . LYS   A 1 129 ? 38.27300  -17.05000 -19.36400 1.000 25.96421 ? 128 LYS   B C     1 
ATOM   1019 O  O     . LYS   A 1 129 ? 38.69600  -15.92100 -19.08300 1.000 23.15545 ? 128 LYS   B O     1 
ATOM   1020 C  CB    . LYS   A 1 129 ? 37.15200  -17.38200 -21.58000 1.000 23.01335 ? 128 LYS   B CB    1 
ATOM   1021 C  CG    . LYS   A 1 129 ? 36.78200  -15.91600 -21.73300 1.000 28.65911 ? 128 LYS   B CG    1 
ATOM   1022 C  CD    . LYS   A 1 129 ? 35.32000  -15.74600 -22.14700 1.000 26.70809 ? 128 LYS   B CD    1 
ATOM   1023 C  CE    . LYS   A 1 129 ? 35.07900  -14.38900 -22.77700 1.000 41.65352 ? 128 LYS   B CE    1 
ATOM   1024 N  NZ    . LYS   A 1 129 ? 35.72200  -14.29300 -24.12200 1.000 54.74309 ? 128 LYS   B NZ    1 
ATOM   1025 N  N     . GLN   A 1 130 ? 37.66800  -17.82800 -18.46100 1.000 24.01094 ? 129 GLN   B N     1 
ATOM   1026 C  CA    . GLN   A 1 130 ? 37.58500  -17.42400 -17.05900 1.000 24.75447 ? 129 GLN   B CA    1 
ATOM   1027 C  C     . GLN   A 1 130 ? 38.96400  -17.14000 -16.49000 1.000 18.02152 ? 129 GLN   B C     1 
ATOM   1028 O  O     . GLN   A 1 130 ? 39.18400  -16.11200 -15.84200 1.000 17.96997 ? 129 GLN   B O     1 
ATOM   1029 C  CB    . GLN   A 1 130 ? 36.91600  -18.51900 -16.22900 1.000 27.63471 ? 129 GLN   B CB    1 
ATOM   1030 C  CG    . GLN   A 1 130 ? 35.43000  -18.37600 -16.04700 1.000 31.74804 ? 129 GLN   B CG    1 
ATOM   1031 C  CD    . GLN   A 1 130 ? 34.85500  -19.56700 -15.29900 1.000 45.00945 ? 129 GLN   B CD    1 
ATOM   1032 O  OE1   . GLN   A 1 130 ? 34.68800  -20.65100 -15.86500 1.000 44.37278 ? 129 GLN   B OE1   1 
ATOM   1033 N  NE2   . GLN   A 1 130 ? 34.58900  -19.38300 -14.00900 1.000 42.47609 ? 129 GLN   B NE2   1 
ATOM   1034 N  N     . ALA   A 1 131 ? 39.89300  -18.07800 -16.68800 1.000 16.30903 ? 130 ALA   B N     1 
ATOM   1035 C  CA    . ALA   A 1 131 ? 41.23300  -17.93100 -16.13800 1.000 18.86986 ? 130 ALA   B CA    1 
ATOM   1036 C  C     . ALA   A 1 131 ? 42.00000  -16.81400 -16.83900 1.000 15.13633 ? 130 ALA   B C     1 
ATOM   1037 O  O     . ALA   A 1 131 ? 42.75200  -16.07100 -16.19500 1.000 16.72460 ? 130 ALA   B O     1 
ATOM   1038 C  CB    . ALA   A 1 131 ? 41.97800  -19.26200 -16.24900 1.000 16.45850 ? 130 ALA   B CB    1 
ATOM   1039 N  N     . GLN   A 1 132 ? 41.83700  -16.69100 -18.15800 1.000 16.89505 ? 131 GLN   B N     1 
ATOM   1040 C  CA    . GLN   A 1 132 ? 42.46500  -15.58800 -18.88100 1.000 16.64164 ? 131 GLN   B CA    1 
ATOM   1041 C  C     . GLN   A 1 132 ? 41.98400  -14.24600 -18.34400 1.000 19.19639 ? 131 GLN   B C     1 
ATOM   1042 O  O     . GLN   A 1 132 ? 42.78600  -13.33500 -18.10900 1.000 19.56895 ? 131 GLN   B O     1 
ATOM   1043 C  CB    . GLN   A 1 132 ? 42.17500  -15.71200 -20.37700 1.000 19.36696 ? 131 GLN   B CB    1 
ATOM   1044 C  CG    . GLN   A 1 132 ? 42.82200  -16.92500 -21.04300 1.000 20.69962 ? 131 GLN   B CG    1 
ATOM   1045 C  CD    . GLN   A 1 132 ? 42.48900  -17.02900 -22.52200 1.000 30.44420 ? 131 GLN   B CD    1 
ATOM   1046 O  OE1   . GLN   A 1 132 ? 41.52100  -16.43300 -22.99400 1.000 29.59753 ? 131 GLN   B OE1   1 
ATOM   1047 N  NE2   . GLN   A 1 132 ? 43.28300  -17.79700 -23.25700 1.000 29.80117 ? 131 GLN   B NE2   1 
ATOM   1048 N  N     . ASP   A 1 133 ? 40.67200  -14.12100 -18.11500 1.000 18.59200 ? 132 ASP   B N     1 
ATOM   1049 C  CA    . ASP   A 1 133 ? 40.10700  -12.87100 -17.61900 1.000 20.24752 ? 132 ASP   B CA    1 
ATOM   1050 C  C     . ASP   A 1 133 ? 40.56600  -12.56800 -16.20200 1.000 18.10789 ? 132 ASP   B C     1 
ATOM   1051 O  O     . ASP   A 1 133 ? 40.77200  -11.40100 -15.84100 1.000 19.29978 ? 132 ASP   B O     1 
ATOM   1052 C  CB    . ASP   A 1 133 ? 38.58400  -12.93000 -17.66000 1.000 20.60514 ? 132 ASP   B CB    1 
ATOM   1053 C  CG    . ASP   A 1 133 ? 38.04400  -12.99500 -19.06200 1.000 28.61001 ? 132 ASP   B CG    1 
ATOM   1054 O  OD1   . ASP   A 1 133 ? 38.83200  -12.77300 -20.00400 1.000 26.69223 ? 132 ASP   B OD1   1 
ATOM   1055 O  OD2   . ASP   A 1 133 ? 36.83100  -13.27400 -19.21800 1.000 25.93193 ? 132 ASP   B OD2   1 
ATOM   1056 N  N     . LEU   A 1 134 ? 40.69100  -13.59700 -15.36700 1.000 16.95542 ? 133 LEU   B N     1 
ATOM   1057 C  CA    . LEU   A 1 134 ? 41.15300  -13.35800 -14.01200 1.000 16.07656 ? 133 LEU   B CA    1 
ATOM   1058 C  C     . LEU   A 1 134 ? 42.59000  -12.85700 -14.02300 1.000 17.01513 ? 133 LEU   B C     1 
ATOM   1059 O  O     . LEU   A 1 134 ? 42.90100  -11.83400 -13.40800 1.000 18.39695 ? 133 LEU   B O     1 
ATOM   1060 C  CB    . LEU   A 1 134 ? 41.02200  -14.62700 -13.17300 1.000 15.56559 ? 133 LEU   B CB    1 
ATOM   1061 C  CG    . LEU   A 1 134 ? 41.42000  -14.41400 -11.71900 1.000 20.05837 ? 133 LEU   B CG    1 
ATOM   1062 C  CD1   . LEU   A 1 134 ? 40.35800  -13.59000 -11.01600 1.000 24.69173 ? 133 LEU   B CD1   1 
ATOM   1063 C  CD2   . LEU   A 1 134 ? 41.68000  -15.73800 -11.00600 1.000 16.57108 ? 133 LEU   B CD2   1 
ATOM   1064 N  N     . ALA   A 1 135 ? 43.47400  -13.56000 -14.74600 1.000 17.35296 ? 134 ALA   B N     1 
ATOM   1065 C  CA    . ALA   A 1 135 ? 44.87700  -13.15600 -14.82300 1.000 19.09980 ? 134 ALA   B CA    1 
ATOM   1066 C  C     . ALA   A 1 135 ? 45.01200  -11.74000 -15.36100 1.000 21.08408 ? 134 ALA   B C     1 
ATOM   1067 O  O     . ALA   A 1 135 ? 45.85100  -10.96200 -14.89000 1.000 17.38574 ? 134 ALA   B O     1 
ATOM   1068 C  CB    . ALA   A 1 135 ? 45.65700  -14.13800 -15.69700 1.000 16.40356 ? 134 ALA   B CB    1 
ATOM   1069 N  N     . ARG   A 1 136 ? 44.19500  -11.39000 -16.35300 1.000 19.37735 ? 135 ARG   B N     1 
ATOM   1070 C  CA    . ARG   A 1 136 ? 44.19100  -10.02600 -16.86400 1.000 22.89009 ? 135 ARG   B CA    1 
ATOM   1071 C  C     . ARG   A 1 136 ? 43.79700  -9.04200  -15.77300 1.000 21.87335 ? 135 ARG   B C     1 
ATOM   1072 O  O     . ARG   A 1 136 ? 44.41700  -7.98400  -15.62500 1.000 19.64627 ? 135 ARG   B O     1 
ATOM   1073 C  CB    . ARG   A 1 136 ? 43.24800  -9.91900  -18.06200 1.000 21.84447 ? 135 ARG   B CB    1 
ATOM   1074 C  CG    . ARG   A 1 136 ? 43.04400  -8.49400  -18.55300 1.000 26.94074 ? 135 ARG   B CG    1 
ATOM   1075 C  CD    . ARG   A 1 136 ? 42.25300  -8.42900  -19.85000 1.000 37.12567 ? 135 ARG   B CD    1 
ATOM   1076 N  NE    . ARG   A 1 136 ? 42.64800  -9.47400  -20.78700 1.000 41.91317 ? 135 ARG   B NE    1 
ATOM   1077 C  CZ    . ARG   A 1 136 ? 41.86800  -10.48100 -21.15400 1.000 35.31311 ? 135 ARG   B CZ    1 
ATOM   1078 N  NH1   . ARG   A 1 136 ? 40.61700  -10.57900 -20.72900 1.000 37.07389 ? 135 ARG   B NH1   1 
ATOM   1079 N  NH2   . ARG   A 1 136 ? 42.35200  -11.41100 -21.97300 1.000 36.60201 ? 135 ARG   B NH2   1 
ATOM   1080 N  N     . SER   A 1 137 ? 42.76800  -9.38100  -14.98800 1.000 21.02516 ? 136 SER   B N     1 
ATOM   1081 C  CA    . SER   A 1 137 ? 42.35700  -8.50500  -13.89400 1.000 24.21307 ? 136 SER   B CA    1 
ATOM   1082 C  C     . SER   A 1 137 ? 43.45600  -8.33500  -12.85600 1.000 21.10873 ? 136 SER   B C     1 
ATOM   1083 O  O     . SER   A 1 137 ? 43.48900  -7.31200  -12.16100 1.000 23.51067 ? 136 SER   B O     1 
ATOM   1084 C  CB    . SER   A 1 137 ? 41.09400  -9.04600  -13.23200 1.000 23.32907 ? 136 SER   B CB    1 
ATOM   1085 O  OG    . SER   A 1 137 ? 41.39100  -10.20500 -12.47800 1.000 20.46130 ? 136 SER   B OG    1 
ATOM   1086 N  N     . TYR   A 1 138 ? 44.35700  -9.30700  -12.74700 1.000 20.52605 ? 137 TYR   B N     1 
ATOM   1087 C  CA    . TYR   A 1 138 ? 45.51200  -9.21100  -11.87500 1.000 17.65176 ? 137 TYR   B CA    1 
ATOM   1088 C  C     . TYR   A 1 138 ? 46.71500  -8.56700  -12.55000 1.000 17.65337 ? 137 TYR   B C     1 
ATOM   1089 O  O     . TYR   A 1 138 ? 47.66600  -8.19900  -11.85500 1.000 16.37745 ? 137 TYR   B O     1 
ATOM   1090 C  CB    . TYR   A 1 138 ? 45.90900  -10.60600 -11.37400 1.000 15.43300 ? 137 TYR   B CB    1 
ATOM   1091 C  CG    . TYR   A 1 138 ? 44.90500  -11.26300 -10.46000 1.000 17.21914 ? 137 TYR   B CG    1 
ATOM   1092 C  CD1   . TYR   A 1 138 ? 43.89300  -10.52500 -9.85500  1.000 19.86036 ? 137 TYR   B CD1   1 
ATOM   1093 C  CD2   . TYR   A 1 138 ? 44.97500  -12.62700 -10.19200 1.000 17.78128 ? 137 TYR   B CD2   1 
ATOM   1094 C  CE1   . TYR   A 1 138 ? 42.97300  -11.13500 -9.00400  1.000 23.21051 ? 137 TYR   B CE1   1 
ATOM   1095 C  CE2   . TYR   A 1 138 ? 44.05700  -13.24300 -9.34100  1.000 20.17942 ? 137 TYR   B CE2   1 
ATOM   1096 C  CZ    . TYR   A 1 138 ? 43.06300  -12.49200 -8.75300  1.000 20.99858 ? 137 TYR   B CZ    1 
ATOM   1097 O  OH    . TYR   A 1 138 ? 42.15100  -13.09600 -7.91400  1.000 20.34957 ? 137 TYR   B OH    1 
ATOM   1098 N  N     . GLY   A 1 139 ? 46.70700  -8.44300  -13.87400 1.000 15.27418 ? 138 GLY   B N     1 
ATOM   1099 C  CA    . GLY   A 1 139 ? 47.91000  -8.04100  -14.58100 1.000 19.54587 ? 138 GLY   B CA    1 
ATOM   1100 C  C     . GLY   A 1 139 ? 49.04300  -9.04700  -14.52800 1.000 17.34782 ? 138 GLY   B C     1 
ATOM   1101 O  O     . GLY   A 1 139 ? 50.20800  -8.64600  -14.56000 1.000 18.20465 ? 138 GLY   B O     1 
ATOM   1102 N  N     . ILE   A 1 140 ? 48.74000  -10.33800 -14.45400 1.000 16.95385 ? 139 ILE   B N     1 
ATOM   1103 C  CA    . ILE   A 1 140 ? 49.76800  -11.37600 -14.39700 1.000 11.97298 ? 139 ILE   B CA    1 
ATOM   1104 C  C     . ILE   A 1 140 ? 49.56800  -12.31700 -15.57400 1.000 16.74256 ? 139 ILE   B C     1 
ATOM   1105 O  O     . ILE   A 1 140 ? 48.47600  -12.38300 -16.17200 1.000 15.71530 ? 139 ILE   B O     1 
ATOM   1106 C  CB    . ILE   A 1 140 ? 49.73200  -12.15200 -13.05900 1.000 12.40297 ? 139 ILE   B CB    1 
ATOM   1107 C  CG1   . ILE   A 1 140 ? 48.40500  -12.92400 -12.91000 1.000 12.06235 ? 139 ILE   B CG1   1 
ATOM   1108 C  CG2   . ILE   A 1 140 ? 49.98000  -11.22200 -11.88800 1.000 18.81133 ? 139 ILE   B CG2   1 
ATOM   1109 C  CD1   . ILE   A 1 140 ? 48.33700  -13.74700 -11.64200 1.000 12.33324 ? 139 ILE   B CD1   1 
ATOM   1110 N  N     . PRO   A 1 141 ? 50.60400  -13.07700 -15.93300 1.000 14.10283 ? 140 PRO   B N     1 
ATOM   1111 C  CA    . PRO   A 1 141 ? 50.45300  -14.08400 -16.98300 1.000 12.39410 ? 140 PRO   B CA    1 
ATOM   1112 C  C     . PRO   A 1 141 ? 49.59600  -15.25800 -16.53600 1.000 11.22997 ? 140 PRO   B C     1 
ATOM   1113 O  O     . PRO   A 1 141 ? 49.48800  -15.57100 -15.34500 1.000 10.60714 ? 140 PRO   B O     1 
ATOM   1114 C  CB    . PRO   A 1 141 ? 51.89600  -14.53800 -17.24800 1.000 14.21060 ? 140 PRO   B CB    1 
ATOM   1115 C  CG    . PRO   A 1 141 ? 52.73800  -13.39700 -16.78200 1.000 12.38732 ? 140 PRO   B CG    1 
ATOM   1116 C  CD    . PRO   A 1 141 ? 52.01800  -12.92600 -15.54600 1.000 11.61782 ? 140 PRO   B CD    1 
ATOM   1117 N  N     . PHE   A 1 142 ? 49.00600  -15.91800 -17.52700 1.000 12.81675 ? 141 PHE   B N     1 
ATOM   1118 C  CA    . PHE   A 1 142 ? 48.28500  -17.17000 -17.35600 1.000 11.57596 ? 141 PHE   B CA    1 
ATOM   1119 C  C     . PHE   A 1 142 ? 48.91200  -18.20200 -18.28200 1.000 13.28572 ? 141 PHE   B C     1 
ATOM   1120 O  O     . PHE   A 1 142 ? 49.10300  -17.93400 -19.47000 1.000 14.01486 ? 141 PHE   B O     1 
ATOM   1121 C  CB    . PHE   A 1 142 ? 46.79700  -17.01100 -17.65900 1.000 13.58139 ? 141 PHE   B CB    1 
ATOM   1122 C  CG    . PHE   A 1 142 ? 46.07800  -18.32400 -17.78700 1.000 12.57056 ? 141 PHE   B CG    1 
ATOM   1123 C  CD1   . PHE   A 1 142 ? 46.05200  -19.21200 -16.72600 1.000 11.69970 ? 141 PHE   B CD1   1 
ATOM   1124 C  CD2   . PHE   A 1 142 ? 45.47600  -18.68500 -18.97600 1.000 17.03489 ? 141 PHE   B CD2   1 
ATOM   1125 C  CE1   . PHE   A 1 142 ? 45.39900  -20.43900 -16.84300 1.000 11.86951 ? 141 PHE   B CE1   1 
ATOM   1126 C  CE2   . PHE   A 1 142 ? 44.82100  -19.89200 -19.10300 1.000 14.29303 ? 141 PHE   B CE2   1 
ATOM   1127 C  CZ    . PHE   A 1 142 ? 44.78400  -20.77400 -18.03600 1.000 14.89340 ? 141 PHE   B CZ    1 
ATOM   1128 N  N     . ILE   A 1 143 ? 49.26000  -19.36400 -17.73200 1.000 10.92514 ? 142 ILE   B N     1 
ATOM   1129 C  CA    . ILE   A 1 143 ? 49.96700  -20.41100 -18.46100 1.000 12.29825 ? 142 ILE   B CA    1 
ATOM   1130 C  C     . ILE   A 1 143 ? 49.18400  -21.69900 -18.30300 1.000 10.99923 ? 142 ILE   B C     1 
ATOM   1131 O  O     . ILE   A 1 143 ? 48.92100  -22.12300 -17.17700 1.000 12.73256 ? 142 ILE   B O     1 
ATOM   1132 C  CB    . ILE   A 1 143 ? 51.40400  -20.62300 -17.94300 1.000 13.70102 ? 142 ILE   B CB    1 
ATOM   1133 C  CG1   . ILE   A 1 143 ? 52.24200  -19.34000 -18.05300 1.000 15.76389 ? 142 ILE   B CG1   1 
ATOM   1134 C  CG2   . ILE   A 1 143 ? 52.06700  -21.78700 -18.67300 1.000 16.29043 ? 142 ILE   B CG2   1 
ATOM   1135 C  CD1   . ILE   A 1 143 ? 52.47500  -18.85800 -19.46600 1.000 16.93794 ? 142 ILE   B CD1   1 
ATOM   1136 N  N     . GLU   A 1 144 ? 48.86300  -22.34800 -19.41500 1.000 14.61969 ? 143 GLU   B N     1 
ATOM   1137 C  CA    . GLU   A 1 144 ? 48.21700  -23.65300 -19.37400 1.000 16.92925 ? 143 GLU   B CA    1 
ATOM   1138 C  C     . GLU   A 1 144 ? 49.27500  -24.74700 -19.32700 1.000 20.89947 ? 143 GLU   B C     1 
ATOM   1139 O  O     . GLU   A 1 144 ? 50.18700  -24.76500 -20.16000 1.000 15.01894 ? 143 GLU   B O     1 
ATOM   1140 C  CB    . GLU   A 1 144 ? 47.32100  -23.84600 -20.59000 1.000 18.50433 ? 143 GLU   B CB    1 
ATOM   1141 C  CG    . GLU   A 1 144 ? 46.22000  -22.81100 -20.70300 1.000 25.56867 ? 143 GLU   B CG    1 
ATOM   1142 C  CD    . GLU   A 1 144 ? 45.38100  -23.00600 -21.94600 1.000 35.43214 ? 143 GLU   B CD    1 
ATOM   1143 O  OE1   . GLU   A 1 144 ? 44.73100  -24.07500 -22.06100 1.000 32.56387 ? 143 GLU   B OE1   1 
ATOM   1144 O  OE2   . GLU   A 1 144 ? 45.38900  -22.09800 -22.81200 1.000 30.28676 ? 143 GLU   B OE2   1 
ATOM   1145 N  N     . THR   A 1 145 ? 49.15000  -25.66100 -18.35800 1.000 12.25619 ? 144 THR   B N     1 
ATOM   1146 C  CA    . THR   A 1 145 ? 50.16600  -26.67900 -18.14200 1.000 14.61509 ? 144 THR   B CA    1 
ATOM   1147 C  C     . THR   A 1 145 ? 49.52700  -28.05800 -18.08300 1.000 16.60995 ? 144 THR   B C     1 
ATOM   1148 O  O     . THR   A 1 145 ? 48.33900  -28.20700 -17.78600 1.000 14.46626 ? 144 THR   B O     1 
ATOM   1149 C  CB    . THR   A 1 145 ? 50.97700  -26.44100 -16.84300 1.000 15.15331 ? 144 THR   B CB    1 
ATOM   1150 O  OG1   . THR   A 1 145 ? 50.14700  -26.61200 -15.69000 1.000 9.35593  ? 144 THR   B OG1   1 
ATOM   1151 C  CG2   . THR   A 1 145 ? 51.58400  -25.04000 -16.80200 1.000 10.47905 ? 144 THR   B CG2   1 
ATOM   1152 N  N     . SER   A 1 146 ? 50.34500  -29.06800 -18.36500 1.000 11.59336 ? 145 SER   B N     1 
ATOM   1153 C  CA    . SER   A 1 146 ? 50.05400  -30.44100 -17.96800 1.000 13.49388 ? 145 SER   B CA    1 
ATOM   1154 C  C     . SER   A 1 146 ? 51.34800  -31.04900 -17.45200 1.000 12.89242 ? 145 SER   B C     1 
ATOM   1155 O  O     . SER   A 1 146 ? 52.28600  -31.24100 -18.22900 1.000 13.81962 ? 145 SER   B O     1 
ATOM   1156 C  CB    . SER   A 1 146 ? 49.50200  -31.27100 -19.12900 1.000 13.10969 ? 145 SER   B CB    1 
ATOM   1157 O  OG    . SER   A 1 146 ? 49.60400  -32.65900 -18.83600 1.000 14.16083 ? 145 SER   B OG    1 
ATOM   1158 N  N     . ALA   A 1 147 ? 51.39900  -31.36400 -16.15500 1.000 11.18832 ? 146 ALA   B N     1 
ATOM   1159 C  CA    . ALA   A 1 147 ? 52.53700  -32.12700 -15.63700 1.000 11.44195 ? 146 ALA   B CA    1 
ATOM   1160 C  C     . ALA   A 1 147 ? 52.67600  -33.49200 -16.31000 1.000 14.90406 ? 146 ALA   B C     1 
ATOM   1161 O  O     . ALA   A 1 147 ? 53.77200  -34.06200 -16.33600 1.000 14.69432 ? 146 ALA   B O     1 
ATOM   1162 C  CB    . ALA   A 1 147 ? 52.40100  -32.29800 -14.12900 1.000 11.13374 ? 146 ALA   B CB    1 
ATOM   1163 N  N     . LYS   A 1 148 ? 51.59600  -34.02900 -16.87200 1.000 12.56336 ? 147 LYS   B N     1 
ATOM   1164 C  CA    . LYS   A 1 148 ? 51.69100  -35.36100 -17.44900 1.000 14.92572 ? 147 LYS   B CA    1 
ATOM   1165 C  C     . LYS   A 1 148 ? 52.32500  -35.34800 -18.83500 1.000 18.76345 ? 147 LYS   B C     1 
ATOM   1166 O  O     . LYS   A 1 148 ? 53.09700  -36.25300 -19.17200 1.000 20.80216 ? 147 LYS   B O     1 
ATOM   1167 C  CB    . LYS   A 1 148 ? 50.30700  -35.99300 -17.50500 1.000 15.87252 ? 147 LYS   B CB    1 
ATOM   1168 C  CG    . LYS   A 1 148 ? 50.33200  -37.40600 -18.03800 1.000 17.50737 ? 147 LYS   B CG    1 
ATOM   1169 C  CD    . LYS   A 1 148 ? 48.93500  -37.94800 -18.11300 1.000 20.08647 ? 147 LYS   B CD    1 
ATOM   1170 C  CE    . LYS   A 1 148 ? 48.94100  -39.37100 -18.63700 1.000 24.38530 ? 147 LYS   B CE    1 
ATOM   1171 N  NZ    . LYS   A 1 148 ? 47.55300  -39.80100 -18.93000 1.000 27.79839 ? 147 LYS   B NZ    1 
ATOM   1172 N  N     . THR   A 1 149 ? 51.99900  -34.35500 -19.66100 1.000 17.96612 ? 148 THR   B N     1 
ATOM   1173 C  CA    . THR   A 1 149 ? 52.57100  -34.26000 -20.99800 1.000 15.78752 ? 148 THR   B CA    1 
ATOM   1174 C  C     . THR   A 1 149 ? 53.76800  -33.31200 -21.06400 1.000 17.91309 ? 148 THR   B C     1 
ATOM   1175 O  O     . THR   A 1 149 ? 54.43100  -33.25100 -22.09900 1.000 19.70994 ? 148 THR   B O     1 
ATOM   1176 C  CB    . THR   A 1 149 ? 51.50600  -33.79100 -21.98600 1.000 16.46541 ? 148 THR   B CB    1 
ATOM   1177 O  OG1   . THR   A 1 149 ? 51.19300  -32.41600 -21.72100 1.000 17.35703 ? 148 THR   B OG1   1 
ATOM   1178 C  CG2   . THR   A 1 149 ? 50.24100  -34.63700 -21.82500 1.000 16.93218 ? 148 THR   B CG2   1 
ATOM   1179 N  N     . ARG   A 1 150 ? 54.04600  -32.57900 -19.98800 1.000 14.02167 ? 149 ARG   B N     1 
ATOM   1180 C  CA    . ARG   A 1 150 ? 55.08900  -31.56600 -19.84400 1.000 16.09160 ? 149 ARG   B CA    1 
ATOM   1181 C  C     . ARG   A 1 150 ? 54.71600  -30.27300 -20.55800 1.000 18.21468 ? 149 ARG   B C     1 
ATOM   1182 O  O     . ARG   A 1 150 ? 55.47800  -29.30800 -20.49700 1.000 13.17458 ? 149 ARG   B O     1 
ATOM   1183 C  CB    . ARG   A 1 150 ? 56.47800  -32.04200 -20.31900 1.000 16.47904 ? 149 ARG   B CB    1 
ATOM   1184 C  CG    . ARG   A 1 150 ? 57.62800  -31.48300 -19.46800 1.000 27.75012 ? 149 ARG   B CG    1 
ATOM   1185 C  CD    . ARG   A 1 150 ? 58.90900  -31.23500 -20.28300 1.000 32.11464 ? 149 ARG   B CD    1 
ATOM   1186 N  NE    . ARG   A 1 150 ? 59.78400  -30.26600 -19.62200 1.000 34.77757 ? 149 ARG   B NE    1 
ATOM   1187 C  CZ    . ARG   A 1 150 ? 60.49300  -30.53600 -18.53400 1.000 32.32815 ? 149 ARG   B CZ    1 
ATOM   1188 N  NH1   . ARG   A 1 150 ? 60.47900  -31.74100 -17.98600 1.000 31.67700 ? 149 ARG   B NH1   1 
ATOM   1189 N  NH2   . ARG   A 1 150 ? 61.23200  -29.57400 -17.98300 1.000 34.27090 ? 149 ARG   B NH2   1 
ATOM   1190 N  N     . GLN   A 1 151 ? 53.55200  -30.21000 -21.20800 1.000 14.46305 ? 150 GLN   B N     1 
ATOM   1191 C  CA    . GLN   A 1 151 ? 53.12100  -28.96600 -21.83500 1.000 14.08380 ? 150 GLN   B CA    1 
ATOM   1192 C  C     . GLN   A 1 151 ? 53.14000  -27.82300 -20.82400 1.000 16.82967 ? 150 GLN   B C     1 
ATOM   1193 O  O     . GLN   A 1 151 ? 52.58700  -27.94100 -19.72600 1.000 14.76345 ? 150 GLN   B O     1 
ATOM   1194 C  CB    . GLN   A 1 151 ? 51.72000  -29.12400 -22.41200 1.000 14.78029 ? 150 GLN   B CB    1 
ATOM   1195 C  CG    . GLN   A 1 151 ? 51.01300  -27.82100 -22.67800 1.000 21.00264 ? 150 GLN   B CG    1 
ATOM   1196 C  CD    . GLN   A 1 151 ? 49.51400  -27.94800 -22.50000 1.000 28.70828 ? 150 GLN   B CD    1 
ATOM   1197 O  OE1   . GLN   A 1 151 ? 48.98000  -29.05700 -22.42600 1.000 30.86921 ? 150 GLN   B OE1   1 
ATOM   1198 N  NE2   . GLN   A 1 151 ? 48.82800  -26.81500 -22.41800 1.000 31.11396 ? 150 GLN   B NE2   1 
ATOM   1199 N  N     . GLY   A 1 152 ? 53.80600  -26.72400 -21.18800 1.000 16.70578 ? 151 GLY   B N     1 
ATOM   1200 C  CA    . GLY   A 1 152 ? 53.76000  -25.50800 -20.40200 1.000 11.93910 ? 151 GLY   B CA    1 
ATOM   1201 C  C     . GLY   A 1 152 ? 54.58500  -25.50000 -19.13600 1.000 16.82194 ? 151 GLY   B C     1 
ATOM   1202 O  O     . GLY   A 1 152 ? 54.64700  -24.45700 -18.47100 1.000 14.61662 ? 151 GLY   B O     1 
ATOM   1203 N  N     . VAL   A 1 153 ? 55.25800  -26.60200 -18.79900 1.000 13.40106 ? 152 VAL   B N     1 
ATOM   1204 C  CA    . VAL   A 1 153 ? 55.94200  -26.69700 -17.50600 1.000 13.14283 ? 152 VAL   B CA    1 
ATOM   1205 C  C     . VAL   A 1 153 ? 57.11300  -25.71200 -17.42100 1.000 11.53832 ? 152 VAL   B C     1 
ATOM   1206 O  O     . VAL   A 1 153 ? 57.18500  -24.89200 -16.50200 1.000 10.82313 ? 152 VAL   B O     1 
ATOM   1207 C  CB    . VAL   A 1 153 ? 56.40300  -28.13900 -17.24500 1.000 15.02815 ? 152 VAL   B CB    1 
ATOM   1208 C  CG1   . VAL   A 1 153 ? 57.26000  -28.18600 -15.98500 1.000 17.06385 ? 152 VAL   B CG1   1 
ATOM   1209 C  CG2   . VAL   A 1 153 ? 55.19300  -29.06100 -17.10700 1.000 12.06142 ? 152 VAL   B CG2   1 
ATOM   1210 N  N     . ASP   A 1 154 ? 58.07000  -25.81100 -18.34300 1.000 15.39700 ? 153 ASP   B N     1 
ATOM   1211 C  CA    . ASP   A 1 154 ? 59.15500  -24.82700 -18.36400 1.000 15.70140 ? 153 ASP   B CA    1 
ATOM   1212 C  C     . ASP   A 1 154 ? 58.59500  -23.42000 -18.47400 1.000 14.39169 ? 153 ASP   B C     1 
ATOM   1213 O  O     . ASP   A 1 154 ? 59.08700  -22.48800 -17.82800 1.000 14.25583 ? 153 ASP   B O     1 
ATOM   1214 C  CB    . ASP   A 1 154 ? 60.09900  -25.08300 -19.53300 1.000 19.22713 ? 153 ASP   B CB    1 
ATOM   1215 C  CG    . ASP   A 1 154 ? 60.93500  -26.33000 -19.36100 1.000 16.80657 ? 153 ASP   B CG    1 
ATOM   1216 O  OD1   . ASP   A 1 154 ? 61.02600  -26.85700 -18.23900 1.000 20.90624 ? 153 ASP   B OD1   1 
ATOM   1217 O  OD2   . ASP   A 1 154 ? 61.50100  -26.78200 -20.36700 1.000 24.47915 ? 153 ASP   B OD2   1 
ATOM   1218 N  N     . ASP   A 1 155 ? 57.56600  -23.25700 -19.30000 1.000 14.55772 ? 154 ASP   B N     1 
ATOM   1219 C  CA    . ASP   A 1 155 ? 56.96200  -21.95000 -19.53100 1.000 19.02954 ? 154 ASP   B CA    1 
ATOM   1220 C  C     . ASP   A 1 155 ? 56.50700  -21.31200 -18.22300 1.000 16.89890 ? 154 ASP   B C     1 
ATOM   1221 O  O     . ASP   A 1 155 ? 56.73200  -20.11800 -17.98400 1.000 12.05897 ? 154 ASP   B O     1 
ATOM   1222 C  CB    . ASP   A 1 155 ? 55.78500  -22.10600 -20.49300 1.000 17.08617 ? 154 ASP   B CB    1 
ATOM   1223 C  CG    . ASP   A 1 155 ? 55.36800  -20.80300 -21.13100 1.000 23.41298 ? 154 ASP   B CG    1 
ATOM   1224 O  OD1   . ASP   A 1 155 ? 56.00200  -19.75700 -20.85600 1.000 22.56769 ? 154 ASP   B OD1   1 
ATOM   1225 O  OD2   . ASP   A 1 155 ? 54.41100  -20.83600 -21.93200 1.000 32.96714 ? 154 ASP   B OD2   1 
ATOM   1226 N  N     . ALA   A 1 156 ? 55.86200  -22.09900 -17.36100 1.000 12.97447 ? 155 ALA   B N     1 
ATOM   1227 C  CA    . ALA   A 1 156 ? 55.34000  -21.55800 -16.11200 1.000 10.22491 ? 155 ALA   B CA    1 
ATOM   1228 C  C     . ALA   A 1 156 ? 56.45900  -21.02000 -15.22500 1.000 13.12420 ? 155 ALA   B C     1 
ATOM   1229 O  O     . ALA   A 1 156 ? 56.39000  -19.89000 -14.71500 1.000 11.09153 ? 155 ALA   B O     1 
ATOM   1230 C  CB    . ALA   A 1 156 ? 54.54800  -22.64900 -15.39100 1.000 11.37957 ? 155 ALA   B CB    1 
ATOM   1231 N  N     . PHE   A 1 157 ? 57.50300  -21.82000 -15.02500 1.000 11.70144 ? 156 PHE   B N     1 
ATOM   1232 C  CA    . PHE   A 1 157 ? 58.58100  -21.40500 -14.14000 1.000 8.71908  ? 156 PHE   B CA    1 
ATOM   1233 C  C     . PHE   A 1 157 ? 59.40700  -20.27800 -14.75500 1.000 8.91647  ? 156 PHE   B C     1 
ATOM   1234 O  O     . PHE   A 1 157 ? 59.76500  -19.31900 -14.06400 1.000 8.35040  ? 156 PHE   B O     1 
ATOM   1235 C  CB    . PHE   A 1 157 ? 59.45800  -22.60600 -13.80600 1.000 8.34284  ? 156 PHE   B CB    1 
ATOM   1236 C  CG    . PHE   A 1 157 ? 58.82400  -23.56600 -12.84900 1.000 10.27249 ? 156 PHE   B CG    1 
ATOM   1237 C  CD1   . PHE   A 1 157 ? 58.87900  -23.33900 -11.48000 1.000 7.03425  ? 156 PHE   B CD1   1 
ATOM   1238 C  CD2   . PHE   A 1 157 ? 58.15900  -24.69400 -13.31500 1.000 9.84293  ? 156 PHE   B CD2   1 
ATOM   1239 C  CE1   . PHE   A 1 157 ? 58.29200  -24.22100 -10.59800 1.000 11.45630 ? 156 PHE   B CE1   1 
ATOM   1240 C  CE2   . PHE   A 1 157 ? 57.57800  -25.57400 -12.44800 1.000 11.93537 ? 156 PHE   B CE2   1 
ATOM   1241 C  CZ    . PHE   A 1 157 ? 57.63400  -25.33800 -11.07600 1.000 14.61286 ? 156 PHE   B CZ    1 
ATOM   1242 N  N     . TYR   A 1 158 ? 59.72200  -20.37800 -16.04800 1.000 11.44660 ? 157 TYR   B N     1 
ATOM   1243 C  CA    . TYR   A 1 158 ? 60.52100  -19.33800 -16.69200 1.000 9.76534  ? 157 TYR   B CA    1 
ATOM   1244 C  C     . TYR   A 1 158 ? 59.77300  -18.01800 -16.72000 1.000 11.91582 ? 157 TYR   B C     1 
ATOM   1245 O  O     . TYR   A 1 158 ? 60.36500  -16.95000 -16.50300 1.000 11.86749 ? 157 TYR   B O     1 
ATOM   1246 C  CB    . TYR   A 1 158 ? 60.88200  -19.73800 -18.11900 1.000 11.19898 ? 157 TYR   B CB    1 
ATOM   1247 C  CG    . TYR   A 1 158 ? 61.82900  -20.90700 -18.25900 1.000 11.50704 ? 157 TYR   B CG    1 
ATOM   1248 C  CD1   . TYR   A 1 158 ? 62.24100  -21.64200 -17.15600 1.000 12.73791 ? 157 TYR   B CD1   1 
ATOM   1249 C  CD2   . TYR   A 1 158 ? 62.31100  -21.26900 -19.51100 1.000 16.93647 ? 157 TYR   B CD2   1 
ATOM   1250 C  CE1   . TYR   A 1 158 ? 63.11500  -22.71200 -17.29800 1.000 12.17498 ? 157 TYR   B CE1   1 
ATOM   1251 C  CE2   . TYR   A 1 158 ? 63.17500  -22.33100 -19.66100 1.000 21.18926 ? 157 TYR   B CE2   1 
ATOM   1252 C  CZ    . TYR   A 1 158 ? 63.56700  -23.05300 -18.55200 1.000 17.55755 ? 157 TYR   B CZ    1 
ATOM   1253 O  OH    . TYR   A 1 158 ? 64.43200  -24.10900 -18.72000 1.000 29.03368 ? 157 TYR   B OH    1 
ATOM   1254 N  N     . THR   A 1 159 ? 58.47200  -18.06800 -17.02300 1.000 10.91489 ? 158 THR   B N     1 
ATOM   1255 C  CA    . THR   A 1 159 ? 57.66700  -16.85400 -17.00200 1.000 9.84378  ? 158 THR   B CA    1 
ATOM   1256 C  C     . THR   A 1 159 ? 57.67600  -16.23000 -15.61400 1.000 9.20124  ? 158 THR   B C     1 
ATOM   1257 O  O     . THR   A 1 159 ? 57.77700  -15.00300 -15.47600 1.000 9.49627  ? 158 THR   B O     1 
ATOM   1258 C  CB    . THR   A 1 159 ? 56.23500  -17.16900 -17.45500 1.000 13.90782 ? 158 THR   B CB    1 
ATOM   1259 O  OG1   . THR   A 1 159 ? 56.24700  -17.54600 -18.83800 1.000 16.20401 ? 158 THR   B OG1   1 
ATOM   1260 C  CG2   . THR   A 1 159 ? 55.31400  -15.96900 -17.28000 1.000 13.76798 ? 158 THR   B CG2   1 
ATOM   1261 N  N     . LEU   A 1 160 ? 57.59300  -17.05500 -14.56900 1.000 8.75769  ? 159 LEU   B N     1 
ATOM   1262 C  CA    . LEU   A 1 160 ? 57.67800  -16.51900 -13.21100 1.000 8.01630  ? 159 LEU   B CA    1 
ATOM   1263 C  C     . LEU   A 1 160 ? 59.01000  -15.81200 -12.97600 1.000 10.56735 ? 159 LEU   B C     1 
ATOM   1264 O  O     . LEU   A 1 160 ? 59.06100  -14.78400 -12.29300 1.000 8.33311  ? 159 LEU   B O     1 
ATOM   1265 C  CB    . LEU   A 1 160 ? 57.48000  -17.62800 -12.17900 1.000 7.37411  ? 159 LEU   B CB    1 
ATOM   1266 C  CG    . LEU   A 1 160 ? 57.44700  -17.09300 -10.73600 1.000 7.35050  ? 159 LEU   B CG    1 
ATOM   1267 C  CD1   . LEU   A 1 160 ? 56.39600  -16.00000 -10.55800 1.000 7.63486  ? 159 LEU   B CD1   1 
ATOM   1268 C  CD2   . LEU   A 1 160 ? 57.23000  -18.21800 -9.72900  1.000 8.09962  ? 159 LEU   B CD2   1 
ATOM   1269 N  N     . VAL   A 1 161 ? 60.10000  -16.35200 -13.52300 1.000 8.52559  ? 160 VAL   B N     1 
ATOM   1270 C  CA    . VAL   A 1 161 ? 61.39100  -15.68700 -13.36500 1.000 10.91148 ? 160 VAL   B CA    1 
ATOM   1271 C  C     . VAL   A 1 161 ? 61.39400  -14.35000 -14.10000 1.000 11.63934 ? 160 VAL   B C     1 
ATOM   1272 O  O     . VAL   A 1 161 ? 61.90300  -13.34600 -13.58600 1.000 11.05717 ? 160 VAL   B O     1 
ATOM   1273 C  CB    . VAL   A 1 161 ? 62.53900  -16.60800 -13.82900 1.000 10.73663 ? 160 VAL   B CB    1 
ATOM   1274 C  CG1   . VAL   A 1 161 ? 63.85700  -15.81300 -13.97500 1.000 9.99475  ? 160 VAL   B CG1   1 
ATOM   1275 C  CG2   . VAL   A 1 161 ? 62.72200  -17.74800 -12.84300 1.000 8.73850  ? 160 VAL   B CG2   1 
ATOM   1276 N  N     . ARG   A 1 162 ? 60.81000  -14.30200 -15.30300 1.000 10.08320 ? 161 ARG   B N     1 
ATOM   1277 C  CA    . ARG   A 1 162 ? 60.73700  -13.02800 -16.02000 1.000 11.63184 ? 161 ARG   B CA    1 
ATOM   1278 C  C     . ARG   A 1 162 ? 59.91700  -11.99700 -15.24900 1.000 15.96649 ? 161 ARG   B C     1 
ATOM   1279 O  O     . ARG   A 1 162 ? 60.25700  -10.80600 -15.22700 1.000 12.09149 ? 161 ARG   B O     1 
ATOM   1280 C  CB    . ARG   A 1 162 ? 60.14600  -13.23100 -17.41400 1.000 12.95832 ? 161 ARG   B CB    1 
ATOM   1281 C  CG    . ARG   A 1 162 ? 60.96000  -14.13700 -18.29500 1.000 13.11295 ? 161 ARG   B CG    1 
ATOM   1282 C  CD    . ARG   A 1 162 ? 60.54400  -14.00500 -19.74700 1.000 14.41697 ? 161 ARG   B CD    1 
ATOM   1283 N  NE    . ARG   A 1 162 ? 61.21200  -15.01300 -20.55300 1.000 18.59938 ? 161 ARG   B NE    1 
ATOM   1284 C  CZ    . ARG   A 1 162 ? 60.77100  -16.25400 -20.71300 1.000 15.75187 ? 161 ARG   B CZ    1 
ATOM   1285 N  NH1   . ARG   A 1 162 ? 59.61100  -16.65100 -20.20900 1.000 13.67159 ? 161 ARG   B NH1   1 
ATOM   1286 N  NH2   . ARG   A 1 162 ? 61.50300  -17.11600 -21.40800 1.000 19.14673 ? 161 ARG   B NH2   1 
ATOM   1287 N  N     . GLU   A 1 163 ? 58.82300  -12.43000 -14.62400 1.000 10.75315 ? 162 GLU   B N     1 
ATOM   1288 C  CA    . GLU   A 1 163 ? 58.04800  -11.51600 -13.79200 1.000 11.41950 ? 162 GLU   B CA    1 
ATOM   1289 C  C     . GLU   A 1 163 ? 58.86700  -11.00400 -12.60900 1.000 16.72935 ? 162 GLU   B C     1 
ATOM   1290 O  O     . GLU   A 1 163 ? 58.75500  -9.83300  -12.22500 1.000 10.52085 ? 162 GLU   B O     1 
ATOM   1291 C  CB    . GLU   A 1 163 ? 56.77900  -12.21200 -13.32200 1.000 10.97998 ? 162 GLU   B CB    1 
ATOM   1292 C  CG    . GLU   A 1 163 ? 55.86200  -12.58700 -14.48700 1.000 14.85446 ? 162 GLU   B CG    1 
ATOM   1293 C  CD    . GLU   A 1 163 ? 55.25000  -11.36800 -15.15500 1.000 16.54698 ? 162 GLU   B CD    1 
ATOM   1294 O  OE1   . GLU   A 1 163 ? 54.56100  -10.60400 -14.46200 1.000 17.03502 ? 162 GLU   B OE1   1 
ATOM   1295 O  OE2   . GLU   A 1 163 ? 55.45900  -11.16400 -16.36500 1.000 17.83152 ? 162 GLU   B OE2   1 
ATOM   1296 N  N     . ILE   A 1 164 ? 59.68800  -11.86800 -12.00400 1.000 12.75260 ? 163 ILE   B N     1 
ATOM   1297 C  CA    . ILE   A 1 164 ? 60.56600  -11.40300 -10.92800 1.000 10.82511 ? 163 ILE   B CA    1 
ATOM   1298 C  C     . ILE   A 1 164 ? 61.54400  -10.37200 -11.46900 1.000 15.80249 ? 163 ILE   B C     1 
ATOM   1299 O  O     . ILE   A 1 164 ? 61.73400  -9.29300  -10.89000 1.000 16.35307 ? 163 ILE   B O     1 
ATOM   1300 C  CB    . ILE   A 1 164 ? 61.29400  -12.59100 -10.27100 1.000 13.04564 ? 163 ILE   B CB    1 
ATOM   1301 C  CG1   . ILE   A 1 164 ? 60.30100  -13.38600 -9.44100  1.000 8.31928  ? 163 ILE   B CG1   1 
ATOM   1302 C  CG2   . ILE   A 1 164 ? 62.45400  -12.09700 -9.40000  1.000 13.39414 ? 163 ILE   B CG2   1 
ATOM   1303 C  CD1   . ILE   A 1 164 ? 60.82300  -14.72600 -8.90400  1.000 7.86874  ? 163 ILE   B CD1   1 
ATOM   1304 N  N     . ARG   A 1 165 ? 62.15800  -10.67600 -12.61000 1.000 13.12937 ? 164 ARG   B N     1 
ATOM   1305 C  CA    . ARG   A 1 165 ? 63.09900  -9.72800  -13.19800 1.000 19.30268 ? 164 ARG   B CA    1 
ATOM   1306 C  C     . ARG   A 1 165 ? 62.40900  -8.40700  -13.54700 1.000 18.38000 ? 164 ARG   B C     1 
ATOM   1307 O  O     . ARG   A 1 165 ? 62.96400  -7.32800  -13.29600 1.000 18.45161 ? 164 ARG   B O     1 
ATOM   1308 C  CB    . ARG   A 1 165 ? 63.78000  -10.36100 -14.41900 1.000 12.89060 ? 164 ARG   B CB    1 
ATOM   1309 C  CG    . ARG   A 1 165 ? 64.67100  -11.56600 -14.08000 1.000 14.52569 ? 164 ARG   B CG    1 
ATOM   1310 C  CD    . ARG   A 1 165 ? 65.13900  -12.33100 -15.33900 1.000 15.65770 ? 164 ARG   B CD    1 
ATOM   1311 N  NE    . ARG   A 1 165 ? 66.13800  -13.36200 -15.06000 1.000 16.77627 ? 164 ARG   B NE    1 
ATOM   1312 C  CZ    . ARG   A 1 165 ? 66.56400  -14.25800 -15.94700 1.000 16.20801 ? 164 ARG   B CZ    1 
ATOM   1313 N  NH1   . ARG   A 1 165 ? 66.08400  -14.29400 -17.17900 1.000 13.11554 ? 164 ARG   B NH1   1 
ATOM   1314 N  NH2   . ARG   A 1 165 ? 67.48900  -15.14800 -15.58700 1.000 12.75809 ? 164 ARG   B NH2   1 
ATOM   1315 N  N     . LYS   A 1 166 ? 61.18500  -8.46300  -14.09300 1.000 16.51440 ? 165 LYS   B N     1 
ATOM   1316 C  CA    . LYS   A 1 166 ? 60.47900  -7.22400  -14.42600 1.000 17.18975 ? 165 LYS   B CA    1 
ATOM   1317 C  C     . LYS   A 1 166 ? 60.17300  -6.41600  -13.17500 1.000 16.62705 ? 165 LYS   B C     1 
ATOM   1318 O  O     . LYS   A 1 166 ? 60.22700  -5.18200  -13.19600 1.000 20.96763 ? 165 LYS   B O     1 
ATOM   1319 C  CB    . LYS   A 1 166 ? 59.17600  -7.51300  -15.17200 1.000 17.26482 ? 165 LYS   B CB    1 
ATOM   1320 C  CG    . LYS   A 1 166 ? 59.33600  -8.14400  -16.55000 1.000 22.33615 ? 165 LYS   B CG    1 
ATOM   1321 C  CD    . LYS   A 1 166 ? 58.10000  -8.98500  -16.92400 1.000 22.94504 ? 165 LYS   B CD    1 
ATOM   1322 C  CE    . LYS   A 1 166 ? 56.94500  -8.10200  -17.38500 1.000 21.37340 ? 165 LYS   B CE    1 
ATOM   1323 N  NZ    . LYS   A 1 166 ? 55.68700  -8.90200  -17.50100 1.000 22.62459 ? 165 LYS   B NZ    1 
ATOM   1324 N  N     . HIS   A 1 167 ? 59.83300  -7.10000  -12.08100 1.000 16.86165 ? 166 HIS   B N     1 
ATOM   1325 C  CA    . HIS   A 1 167 ? 59.54900  -6.42100  -10.82500 1.000 17.15897 ? 166 HIS   B CA    1 
ATOM   1326 C  C     . HIS   A 1 167 ? 60.79300  -5.72900  -10.27900 1.000 20.99654 ? 166 HIS   B C     1 
ATOM   1327 O  O     . HIS   A 1 167 ? 60.70900  -4.61400  -9.75000  1.000 19.17470 ? 166 HIS   B O     1 
ATOM   1328 C  CB    . HIS   A 1 167 ? 58.99100  -7.43100  -9.81700  1.000 17.03890 ? 166 HIS   B CB    1 
ATOM   1329 C  CG    . HIS   A 1 167 ? 58.91900  -6.91800  -8.41200  1.000 20.72901 ? 166 HIS   B CG    1 
ATOM   1330 N  ND1   . HIS   A 1 167 ? 57.94300  -6.04200  -7.98700  1.000 30.18540 ? 166 HIS   B ND1   1 
ATOM   1331 C  CD2   . HIS   A 1 167 ? 59.69900  -7.16500  -7.33000  1.000 21.59300 ? 166 HIS   B CD2   1 
ATOM   1332 C  CE1   . HIS   A 1 167 ? 58.13000  -5.76300  -6.70900  1.000 22.03022 ? 166 HIS   B CE1   1 
ATOM   1333 N  NE2   . HIS   A 1 167 ? 59.18900  -6.43100  -6.28700  1.000 23.92745 ? 166 HIS   B NE2   1 
ATOM   1334 N  N     . LYS   A 1 168 ? 61.96100  -6.37200  -10.41400 1.000 18.44405 ? 167 LYS   B N     1 
ATOM   1335 C  CA    . LYS   A 1 168 ? 63.19600  -5.79400  -9.88600  1.000 19.46183 ? 167 LYS   B CA    1 
ATOM   1336 C  C     . LYS   A 1 168 ? 63.59100  -4.50200  -10.59100 1.000 23.09545 ? 167 LYS   B C     1 
ATOM   1337 O  O     . LYS   A 1 168 ? 64.31900  -3.69300  -10.00500 1.000 28.18439 ? 167 LYS   B O     1 
ATOM   1338 C  CB    . LYS   A 1 168 ? 64.34300  -6.79800  -9.99200  1.000 16.69052 ? 167 LYS   B CB    1 
ATOM   1339 C  CG    . LYS   A 1 168 ? 64.32600  -7.92600  -8.96000  1.000 19.65023 ? 167 LYS   B CG    1 
ATOM   1340 C  CD    . LYS   A 1 168 ? 65.44400  -8.89400  -9.27300  1.000 17.58362 ? 167 LYS   B CD    1 
ATOM   1341 C  CE    . LYS   A 1 168 ? 65.82800  -9.77500  -8.09800  1.000 19.73453 ? 167 LYS   B CE    1 
ATOM   1342 N  NZ    . LYS   A 1 168 ? 67.16200  -10.44600 -8.36600  1.000 16.14376 ? 167 LYS   B NZ    1 
ATOM   1343 N  N     . GLU   A 1 169 ? 63.13600  -4.28600  -11.82700 1.000 21.64156 ? 168 GLU   B N     1 
ATOM   1344 C  CA    . GLU   A 1 169 ? 63.44600  -3.04800  -12.53700 1.000 24.93492 ? 168 GLU   B CA    1 
ATOM   1345 C  C     . GLU   A 1 169 ? 62.74900  -1.83400  -11.94200 1.000 29.06755 ? 168 GLU   B C     1 
ATOM   1346 O  O     . GLU   A 1 169 ? 63.22700  -0.70900  -12.12200 1.000 26.91655 ? 168 GLU   B O     1 
ATOM   1347 C  CB    . GLU   A 1 169 ? 63.04200  -3.15000  -14.00800 1.000 28.65507 ? 168 GLU   B CB    1 
ATOM   1348 C  CG    . GLU   A 1 169 ? 63.81700  -4.15100  -14.83800 1.000 32.01950 ? 168 GLU   B CG    1 
ATOM   1349 C  CD    . GLU   A 1 169 ? 63.37300  -4.13700  -16.29400 1.000 33.67334 ? 168 GLU   B CD    1 
ATOM   1350 O  OE1   . GLU   A 1 169 ? 62.17700  -3.89100  -16.54200 1.000 42.39366 ? 168 GLU   B OE1   1 
ATOM   1351 O  OE2   . GLU   A 1 169 ? 64.21500  -4.35300  -17.19100 1.000 44.05710 ? 168 GLU   B OE2   1 
ATOM   1352 N  N     . LYS   A 1 170 ? 61.62100  -2.02700  -11.27300 1.000 27.37801 ? 169 LYS   B N     1 
ATOM   1353 C  CA    . LYS   A 1 170 ? 60.82300  -0.90600  -10.81600 1.000 28.09272 ? 169 LYS   B CA    1 
ATOM   1354 C  C     . LYS   A 1 170 ? 61.55400  -0.08400  -9.75200  1.000 33.15778 ? 169 LYS   B C     1 
ATOM   1355 O  O     . LYS   A 1 170 ? 62.28800  -0.60400  -8.91200  1.000 26.61616 ? 169 LYS   B O     1 
ATOM   1356 C  CB    . LYS   A 1 170 ? 59.47900  -1.40600  -10.29000 1.000 34.49487 ? 169 LYS   B CB    1 
ATOM   1357 C  CG    . LYS   A 1 170 ? 58.59500  -2.03800  -11.35700 1.000 33.23341 ? 169 LYS   B CG    1 
ATOM   1358 C  CD    . LYS   A 1 170 ? 57.39500  -2.73700  -10.73700 1.000 39.63290 ? 169 LYS   B CD    1 
ATOM   1359 C  CE    . LYS   A 1 170 ? 56.47300  -3.30400  -11.80500 1.000 40.56093 ? 169 LYS   B CE    1 
ATOM   1360 N  NZ    . LYS   A 1 170 ? 55.96800  -2.22000  -12.68500 1.000 41.18634 ? 169 LYS   B NZ    1 
ATOM   1361 O  OXT   . LYS   A 1 170 ? 61.44400  1.14500   -9.72600  1.000 38.24919 ? 169 LYS   B OXT   1 
ATOM   1362 N  N     . SER   B 1 1   ? 108.07300 -36.46500 66.36200  1.000 35.20669 ? 0   SER   A N     1 
ATOM   1363 C  CA    . SER   B 1 1   ? 107.65300 -36.23700 64.98400  1.000 23.27098 ? 0   SER   A CA    1 
ATOM   1364 C  C     . SER   B 1 1   ? 106.37300 -35.40600 64.95400  1.000 30.37195 ? 0   SER   A C     1 
ATOM   1365 O  O     . SER   B 1 1   ? 105.92800 -34.88600 65.98200  1.000 31.21707 ? 0   SER   A O     1 
ATOM   1366 C  CB    . SER   B 1 1   ? 107.44300 -37.57300 64.26100  1.000 27.87018 ? 0   SER   A CB    1 
ATOM   1367 O  OG    . SER   B 1 1   ? 107.21700 -37.39200 62.86700  1.000 27.09715 ? 0   SER   A OG    1 
ATOM   1368 N  N     . MET   B 1 2   ? 105.78800 -35.26300 63.77200  1.000 20.91882 ? 1   MET   A N     1 
ATOM   1369 C  CA    . MET   B 1 2   ? 104.48200 -34.63900 63.67800  1.000 21.00964 ? 1   MET   A CA    1 
ATOM   1370 C  C     . MET   B 1 2   ? 103.68100 -35.33000 62.58700  1.000 20.18221 ? 1   MET   A C     1 
ATOM   1371 O  O     . MET   B 1 2   ? 104.17100 -36.21700 61.88600  1.000 19.78845 ? 1   MET   A O     1 
ATOM   1372 C  CB    . MET   B 1 2   ? 104.59500 -33.13200 63.42300  1.000 25.33738 ? 1   MET   A CB    1 
ATOM   1373 C  CG    . MET   B 1 2   ? 104.98600 -32.75600 62.02000  1.000 25.94340 ? 1   MET   A CG    1 
ATOM   1374 S  SD    . MET   B 1 2   ? 104.86700 -30.96300 61.79600  1.000 46.67856 ? 1   MET   A SD    1 
ATOM   1375 C  CE    . MET   B 1 2   ? 106.58000 -30.53700 61.97500  1.000 24.54557 ? 1   MET   A CE    1 
ATOM   1376 N  N     . THR   B 1 3   ? 102.42400 -34.91800 62.47400  1.000 17.73265 ? 2   THR   A N     1 
ATOM   1377 C  CA    . THR   B 1 3   ? 101.46800 -35.46400 61.53300  1.000 17.92914 ? 2   THR   A CA    1 
ATOM   1378 C  C     . THR   B 1 3   ? 100.78000 -34.29000 60.84600  1.000 19.61605 ? 2   THR   A C     1 
ATOM   1379 O  O     . THR   B 1 3   ? 100.92800 -33.13300 61.25300  1.000 18.40496 ? 2   THR   A O     1 
ATOM   1380 C  CB    . THR   B 1 3   ? 100.44500 -36.35700 62.25000  1.000 20.74467 ? 2   THR   A CB    1 
ATOM   1381 O  OG1   . THR   B 1 3   ? 99.85200  -35.60400 63.31900  1.000 17.49839 ? 2   THR   A OG1   1 
ATOM   1382 C  CG2   . THR   B 1 3   ? 101.13600 -37.60100 62.84000  1.000 17.96696 ? 2   THR   A CG2   1 
ATOM   1383 N  N     . GLU   B 1 4   ? 100.03800 -34.59000 59.79000  1.000 13.71463 ? 3   GLU   A N     1 
ATOM   1384 C  CA    . GLU   B 1 4   ? 99.32500  -33.57100 59.03400  1.000 12.88005 ? 3   GLU   A CA    1 
ATOM   1385 C  C     . GLU   B 1 4   ? 97.93400  -34.09300 58.69900  1.000 13.50333 ? 3   GLU   A C     1 
ATOM   1386 O  O     . GLU   B 1 4   ? 97.77100  -35.28000 58.41500  1.000 15.90285 ? 3   GLU   A O     1 
ATOM   1387 C  CB    . GLU   B 1 4   ? 100.10600 -33.20600 57.76000  1.000 18.60924 ? 3   GLU   A CB    1 
ATOM   1388 C  CG    . GLU   B 1 4   ? 99.59700  -31.97600 57.03300  1.000 17.12646 ? 3   GLU   A CG    1 
ATOM   1389 C  CD    . GLU   B 1 4   ? 100.53200 -31.52500 55.91800  1.000 24.86100 ? 3   GLU   A CD    1 
ATOM   1390 O  OE1   . GLU   B 1 4   ? 101.74300 -31.85600 55.95600  1.000 26.76227 ? 3   GLU   A OE1   1 
ATOM   1391 O  OE2   . GLU   B 1 4   ? 100.06500 -30.82300 55.00400  1.000 20.34683 ? 3   GLU   A OE2   1 
ATOM   1392 N  N     . TYR   B 1 5   ? 96.93100  -33.21300 58.74600  1.000 11.34013 ? 4   TYR   A N     1 
ATOM   1393 C  CA    . TYR   B 1 5   ? 95.54600  -33.59900 58.49600  1.000 11.22209 ? 4   TYR   A CA    1 
ATOM   1394 C  C     . TYR   B 1 5   ? 94.87600  -32.57800 57.58100  1.000 14.54246 ? 4   TYR   A C     1 
ATOM   1395 O  O     . TYR   B 1 5   ? 95.00500  -31.36600 57.79500  1.000 11.87802 ? 4   TYR   A O     1 
ATOM   1396 C  CB    . TYR   B 1 5   ? 94.75500  -33.72000 59.80300  1.000 13.03414 ? 4   TYR   A CB    1 
ATOM   1397 C  CG    . TYR   B 1 5   ? 95.39200  -34.64000 60.81400  1.000 11.52967 ? 4   TYR   A CG    1 
ATOM   1398 C  CD1   . TYR   B 1 5   ? 95.35000  -36.02300 60.64700  1.000 20.21004 ? 4   TYR   A CD1   1 
ATOM   1399 C  CD2   . TYR   B 1 5   ? 96.05300  -34.13400 61.92800  1.000 18.18507 ? 4   TYR   A CD2   1 
ATOM   1400 C  CE1   . TYR   B 1 5   ? 95.96300  -36.88200 61.56800  1.000 17.73968 ? 4   TYR   A CE1   1 
ATOM   1401 C  CE2   . TYR   B 1 5   ? 96.66200  -34.98800 62.86000  1.000 15.62273 ? 4   TYR   A CE2   1 
ATOM   1402 C  CZ    . TYR   B 1 5   ? 96.60400  -36.35700 62.67000  1.000 12.94006 ? 4   TYR   A CZ    1 
ATOM   1403 O  OH    . TYR   B 1 5   ? 97.19600  -37.20200 63.57400  1.000 15.21633 ? 4   TYR   A OH    1 
ATOM   1404 N  N     . LYS   B 1 6   ? 94.17400  -33.06900 56.55400  1.000 12.47221 ? 5   LYS   A N     1 
ATOM   1405 C  CA    . LYS   B 1 6   ? 93.39900  -32.22100 55.65200  1.000 12.76386 ? 5   LYS   A CA    1 
ATOM   1406 C  C     . LYS   B 1 6   ? 91.96100  -32.22900 56.15200  1.000 11.72695 ? 5   LYS   A C     1 
ATOM   1407 O  O     . LYS   B 1 6   ? 91.24300  -33.22400 55.97600  1.000 11.91334 ? 5   LYS   A O     1 
ATOM   1408 C  CB    . LYS   B 1 6   ? 93.48400  -32.70900 54.20700  1.000 15.18956 ? 5   LYS   A CB    1 
ATOM   1409 C  CG    . LYS   B 1 6   ? 94.88300  -32.75700 53.64200  1.000 22.35522 ? 5   LYS   A CG    1 
ATOM   1410 C  CD    . LYS   B 1 6   ? 94.84500  -33.28100 52.21400  1.000 27.40105 ? 5   LYS   A CD    1 
ATOM   1411 C  CE    . LYS   B 1 6   ? 95.01200  -34.78900 52.17400  1.000 28.86761 ? 5   LYS   A CE    1 
ATOM   1412 N  NZ    . LYS   B 1 6   ? 96.44000  -35.19600 52.41800  1.000 36.85061 ? 5   LYS   A NZ    1 
ATOM   1413 N  N     . LEU   B 1 7   ? 91.55500  -31.12900 56.78600  1.000 8.93054  ? 6   LEU   A N     1 
ATOM   1414 C  CA    . LEU   B 1 7   ? 90.20700  -30.95600 57.31500  1.000 10.82519 ? 6   LEU   A CA    1 
ATOM   1415 C  C     . LEU   B 1 7   ? 89.40200  -30.08900 56.36300  1.000 10.30079 ? 6   LEU   A C     1 
ATOM   1416 O  O     . LEU   B 1 7   ? 89.91200  -29.08400 55.86600  1.000 8.10723  ? 6   LEU   A O     1 
ATOM   1417 C  CB    . LEU   B 1 7   ? 90.25500  -30.30300 58.69900  1.000 14.76754 ? 6   LEU   A CB    1 
ATOM   1418 C  CG    . LEU   B 1 7   ? 91.33400  -30.81900 59.65100  1.000 9.78974  ? 6   LEU   A CG    1 
ATOM   1419 C  CD1   . LEU   B 1 7   ? 91.39600  -30.00100 60.94300  1.000 12.06956 ? 6   LEU   A CD1   1 
ATOM   1420 C  CD2   . LEU   B 1 7   ? 91.12000  -32.28300 59.95400  1.000 11.47903 ? 6   LEU   A CD2   1 
ATOM   1421 N  N     . VAL   B 1 8   ? 88.14100  -30.46100 56.12600  1.000 8.76810  ? 7   VAL   A N     1 
ATOM   1422 C  CA    . VAL   B 1 8   ? 87.26900  -29.72700 55.21500  1.000 11.83483 ? 7   VAL   A CA    1 
ATOM   1423 C  C     . VAL   B 1 8   ? 86.03900  -29.27700 55.98700  1.000 9.37600  ? 7   VAL   A C     1 
ATOM   1424 O  O     . VAL   B 1 8   ? 85.36400  -30.09900 56.61500  1.000 7.78392  ? 7   VAL   A O     1 
ATOM   1425 C  CB    . VAL   B 1 8   ? 86.86700  -30.58400 54.00200  1.000 8.42427  ? 7   VAL   A CB    1 
ATOM   1426 C  CG1   . VAL   B 1 8   ? 85.97700  -29.79400 53.05800  1.000 10.70401 ? 7   VAL   A CG1   1 
ATOM   1427 C  CG2   . VAL   B 1 8   ? 88.10900  -31.08700 53.30500  1.000 8.06358  ? 7   VAL   A CG2   1 
ATOM   1428 N  N     . VAL   B 1 9   ? 85.74200  -27.97800 55.92700  1.000 8.02978  ? 8   VAL   A N     1 
ATOM   1429 C  CA    . VAL   B 1 9   ? 84.59300  -27.40300 56.62000  1.000 7.89204  ? 8   VAL   A CA    1 
ATOM   1430 C  C     . VAL   B 1 9   ? 83.46500  -27.23000 55.61100  1.000 7.37558  ? 8   VAL   A C     1 
ATOM   1431 O  O     . VAL   B 1 9   ? 83.62600  -26.50000 54.62900  1.000 8.53645  ? 8   VAL   A O     1 
ATOM   1432 C  CB    . VAL   B 1 9   ? 84.96600  -26.06200 57.27400  1.000 8.16510  ? 8   VAL   A CB    1 
ATOM   1433 C  CG1   . VAL   B 1 9   ? 83.81900  -25.52100 58.16700  1.000 6.31182  ? 8   VAL   A CG1   1 
ATOM   1434 C  CG2   . VAL   B 1 9   ? 86.25800  -26.20300 58.04000  1.000 10.77384 ? 8   VAL   A CG2   1 
ATOM   1435 N  N     . VAL   B 1 10  ? 82.31600  -27.89600 55.84100  1.000 7.38972  ? 9   VAL   A N     1 
ATOM   1436 C  CA    . VAL   B 1 10  ? 81.17200  -27.84300 54.93600  1.000 9.90876  ? 9   VAL   A CA    1 
ATOM   1437 C  C     . VAL   B 1 10  ? 79.88300  -27.51400 55.69900  1.000 7.77763  ? 9   VAL   A C     1 
ATOM   1438 O  O     . VAL   B 1 10  ? 79.80200  -27.61500 56.91900  1.000 7.91945  ? 9   VAL   A O     1 
ATOM   1439 C  CB    . VAL   B 1 10  ? 80.97700  -29.16400 54.16200  1.000 8.02117  ? 9   VAL   A CB    1 
ATOM   1440 C  CG1   . VAL   B 1 10  ? 82.21500  -29.47000 53.32000  1.000 11.58826 ? 9   VAL   A CG1   1 
ATOM   1441 C  CG2   . VAL   B 1 10  ? 80.66300  -30.28300 55.13100  1.000 9.33990  ? 9   VAL   A CG2   1 
ATOM   1442 N  N     . GLY   B 1 11  ? 78.86400  -27.13600 54.95200  1.000 8.24903  ? 10  GLY   A N     1 
ATOM   1443 C  CA    . GLY   B 1 11  ? 77.58100  -26.74900 55.51600  1.000 7.89120  ? 10  GLY   A CA    1 
ATOM   1444 C  C     . GLY   B 1 11  ? 76.96700  -25.56900 54.77600  1.000 10.80117 ? 10  GLY   A C     1 
ATOM   1445 O  O     . GLY   B 1 11  ? 77.61500  -24.87000 53.99300  1.000 7.39038  ? 10  GLY   A O     1 
ATOM   1446 N  N     . ALA   B 1 12  ? 75.67500  -25.34000 55.03700  1.000 8.12419  ? 11  ALA   A N     1 
ATOM   1447 C  CA    . ALA   B 1 12  ? 74.90900  -24.36200 54.28100  1.000 9.21346  ? 11  ALA   A CA    1 
ATOM   1448 C  C     . ALA   B 1 12  ? 75.52600  -22.97200 54.39900  1.000 7.83073  ? 11  ALA   A C     1 
ATOM   1449 O  O     . ALA   B 1 12  ? 76.32400  -22.68500 55.29200  1.000 8.40040  ? 11  ALA   A O     1 
ATOM   1450 C  CB    . ALA   B 1 12  ? 73.45100  -24.32100 54.75800  1.000 9.82177  ? 11  ALA   A CB    1 
ATOM   1451 N  N     . CYS   B 1 13  ? 75.14800  -22.09800 53.47100  1.000 8.24573  ? 12  CYS   A N     1 
ATOM   1452 C  CA    . CYS   B 1 13  ? 75.70500  -20.75700 53.47700  1.000 8.30327  ? 12  CYS   A CA    1 
ATOM   1453 C  C     . CYS   B 1 13  ? 75.29400  -20.00000 54.73300  1.000 9.36282  ? 12  CYS   A C     1 
ATOM   1454 O  O     . CYS   B 1 13  ? 74.17200  -20.14100 55.22200  1.000 9.51421  ? 12  CYS   A O     1 
ATOM   1455 C  CB    . CYS   B 1 13  ? 75.27000  -19.99900 52.22500  1.000 8.91472  ? 12  CYS   A CB    1 
ATOM   1456 S  SG    . CYS   B 1 13  ? 73.49500  -19.83900 52.04100  1.000 13.38137 ? 12  CYS   A SG    1 
ATOM   1457 N  N     . GLY   B 1 14  ? 76.21900  -19.18700 55.24900  1.000 8.30811  ? 13  GLY   A N     1 
ATOM   1458 C  CA    . GLY   B 1 14  ? 75.95700  -18.33400 56.39200  1.000 8.61983  ? 13  GLY   A CA    1 
ATOM   1459 C  C     . GLY   B 1 14  ? 76.00300  -18.98500 57.76000  1.000 8.48362  ? 13  GLY   A C     1 
ATOM   1460 O  O     . GLY   B 1 14  ? 75.76000  -18.29800 58.76000  1.000 11.46090 ? 13  GLY   A O     1 
ATOM   1461 N  N     . VAL   B 1 15  ? 76.29200  -20.28300 57.85700  1.000 10.30681 ? 14  VAL   A N     1 
ATOM   1462 C  CA    . VAL   B 1 15  ? 76.21400  -20.92400 59.17200  1.000 8.08951  ? 14  VAL   A CA    1 
ATOM   1463 C  C     . VAL   B 1 15  ? 77.39300  -20.56400 60.06700  1.000 9.41818  ? 14  VAL   A C     1 
ATOM   1464 O  O     . VAL   B 1 15  ? 77.31700  -20.74200 61.29100  1.000 9.35252  ? 14  VAL   A O     1 
ATOM   1465 C  CB    . VAL   B 1 15  ? 76.12300  -22.45500 59.04500  1.000 8.05523  ? 14  VAL   A CB    1 
ATOM   1466 C  CG1   . VAL   B 1 15  ? 74.82000  -22.84600 58.36400  1.000 7.99455  ? 14  VAL   A CG1   1 
ATOM   1467 C  CG2   . VAL   B 1 15  ? 77.33600  -22.99700 58.27400  1.000 8.22781  ? 14  VAL   A CG2   1 
ATOM   1468 N  N     . GLY   B 1 16  ? 78.46800  -20.04300 59.50700  1.000 12.00534 ? 15  GLY   A N     1 
ATOM   1469 C  CA    . GLY   B 1 16  ? 79.63800  -19.68600 60.28000  1.000 9.07742  ? 15  GLY   A CA    1 
ATOM   1470 C  C     . GLY   B 1 16  ? 80.84500  -20.58000 60.04300  1.000 12.21958 ? 15  GLY   A C     1 
ATOM   1471 O  O     . GLY   B 1 16  ? 81.72500  -20.63800 60.91600  1.000 12.16888 ? 15  GLY   A O     1 
ATOM   1472 N  N     . LYS   B 1 17  ? 80.90900  -21.27100 58.89900  1.000 7.66284  ? 16  LYS   A N     1 
ATOM   1473 C  CA    . LYS   B 1 17  ? 82.08600  -22.07100 58.56500  1.000 10.27513 ? 16  LYS   A CA    1 
ATOM   1474 C  C     . LYS   B 1 17  ? 83.34600  -21.22200 58.60700  1.000 8.36223  ? 16  LYS   A C     1 
ATOM   1475 O  O     . LYS   B 1 17  ? 84.35900  -21.61900 59.19400  1.000 8.86614  ? 16  LYS   A O     1 
ATOM   1476 C  CB    . LYS   B 1 17  ? 81.92300  -22.70000 57.17300  1.000 7.43471  ? 16  LYS   A CB    1 
ATOM   1477 C  CG    . LYS   B 1 17  ? 80.75000  -23.68700 57.04600  1.000 9.08025  ? 16  LYS   A CG    1 
ATOM   1478 C  CD    . LYS   B 1 17  ? 80.60200  -24.18400 55.59200  1.000 6.41190  ? 16  LYS   A CD    1 
ATOM   1479 C  CE    . LYS   B 1 17  ? 80.39100  -23.02900 54.63000  1.000 7.55114  ? 16  LYS   A CE    1 
ATOM   1480 N  NZ    . LYS   B 1 17  ? 79.02800  -22.39700 54.68800  1.000 7.85652  ? 16  LYS   A NZ    1 
ATOM   1481 N  N     . SER   B 1 18  ? 83.29600  -20.04400 57.97800  1.000 9.07987  ? 17  SER   A N     1 
ATOM   1482 C  CA    . SER   B 1 18  ? 84.46300  -19.16600 57.90300  1.000 10.00359 ? 17  SER   A CA    1 
ATOM   1483 C  C     . SER   B 1 18  ? 84.79900  -18.53700 59.25000  1.000 11.51566 ? 17  SER   A C     1 
ATOM   1484 O  O     . SER   B 1 18  ? 85.97700  -18.43600 59.61600  1.000 10.76698 ? 17  SER   A O     1 
ATOM   1485 C  CB    . SER   B 1 18  ? 84.22900  -18.07000 56.86500  1.000 10.57226 ? 17  SER   A CB    1 
ATOM   1486 O  OG    . SER   B 1 18  ? 84.31400  -18.59600 55.55500  1.000 11.10748 ? 17  SER   A OG    1 
ATOM   1487 N  N     . ALA   B 1 19  ? 83.79400  -18.07200 59.98900  1.000 11.35782 ? 18  ALA   A N     1 
ATOM   1488 C  CA    . ALA   B 1 19  ? 84.09200  -17.46100 61.28000  1.000 13.41687 ? 18  ALA   A CA    1 
ATOM   1489 C  C     . ALA   B 1 19  ? 84.69600  -18.47600 62.25200  1.000 11.28999 ? 18  ALA   A C     1 
ATOM   1490 O  O     . ALA   B 1 19  ? 85.51600  -18.11600 63.10300  1.000 13.36351 ? 18  ALA   A O     1 
ATOM   1491 C  CB    . ALA   B 1 19  ? 82.83200  -16.83100 61.86300  1.000 11.47830 ? 18  ALA   A CB    1 
ATOM   1492 N  N     . LEU   B 1 20  ? 84.29200  -19.73500 62.14900  1.000 12.67361 ? 19  LEU   A N     1 
ATOM   1493 C  CA    . LEU   B 1 20  ? 84.90500  -20.77600 62.96900  1.000 11.16569 ? 19  LEU   A CA    1 
ATOM   1494 C  C     . LEU   B 1 20  ? 86.36800  -20.96700 62.59500  1.000 11.54765 ? 19  LEU   A C     1 
ATOM   1495 O  O     . LEU   B 1 20  ? 87.23700  -21.01100 63.46800  1.000 12.24461 ? 19  LEU   A O     1 
ATOM   1496 C  CB    . LEU   B 1 20  ? 84.13600  -22.09000 62.81300  1.000 9.84452  ? 19  LEU   A CB    1 
ATOM   1497 C  CG    . LEU   B 1 20  ? 82.79500  -22.21600 63.54000  1.000 11.17964 ? 19  LEU   A CG    1 
ATOM   1498 C  CD1   . LEU   B 1 20  ? 82.05500  -23.49900 63.14000  1.000 8.73285  ? 19  LEU   A CD1   1 
ATOM   1499 C  CD2   . LEU   B 1 20  ? 82.99700  -22.13100 65.05800  1.000 8.72607  ? 19  LEU   A CD2   1 
ATOM   1500 N  N     . THR   B 1 21  ? 86.65500  -21.05400 61.29600  1.000 12.84542 ? 20  THR   A N     1 
ATOM   1501 C  CA    . THR   B 1 21  ? 88.02900  -21.21800 60.83500  1.000 8.16468  ? 20  THR   A CA    1 
ATOM   1502 C  C     . THR   B 1 21  ? 88.89700  -20.02800 61.22900  1.000 13.70573 ? 20  THR   A C     1 
ATOM   1503 O  O     . THR   B 1 21  ? 90.02800  -20.20800 61.69800  1.000 13.55520 ? 20  THR   A O     1 
ATOM   1504 C  CB    . THR   B 1 21  ? 88.02200  -21.41900 59.32400  1.000 10.85891 ? 20  THR   A CB    1 
ATOM   1505 O  OG1   . THR   B 1 21  ? 87.17300  -22.53500 59.01700  1.000 13.29721 ? 20  THR   A OG1   1 
ATOM   1506 C  CG2   . THR   B 1 21  ? 89.43100  -21.69300 58.80200  1.000 13.60246 ? 20  THR   A CG2   1 
ATOM   1507 N  N     . ILE   B 1 22  ? 88.37900  -18.80400 61.07900  1.000 11.63545 ? 21  ILE   A N     1 
ATOM   1508 C  CA    . ILE   B 1 22  ? 89.19400  -17.62800 61.37000  1.000 13.47251 ? 21  ILE   A CA    1 
ATOM   1509 C  C     . ILE   B 1 22  ? 89.47600  -17.51300 62.86400  1.000 13.87917 ? 21  ILE   A C     1 
ATOM   1510 O  O     . ILE   B 1 22  ? 90.54900  -17.04200 63.27200  1.000 15.42519 ? 21  ILE   A O     1 
ATOM   1511 C  CB    . ILE   B 1 22  ? 88.52900  -16.35900 60.81400  1.000 12.43776 ? 21  ILE   A CB    1 
ATOM   1512 C  CG1   . ILE   B 1 22  ? 88.69200  -16.33100 59.29700  1.000 16.54051 ? 21  ILE   A CG1   1 
ATOM   1513 C  CG2   . ILE   B 1 22  ? 89.15100  -15.09700 61.43900  1.000 14.06410 ? 21  ILE   A CG2   1 
ATOM   1514 C  CD1   . ILE   B 1 22  ? 87.91100  -15.26300 58.63400  1.000 26.22197 ? 21  ILE   A CD1   1 
ATOM   1515 N  N     . GLN   B 1 23  ? 88.52900  -17.92300 63.70400  1.000 10.70209 ? 22  GLN   A N     1 
ATOM   1516 C  CA    . GLN   B 1 23  ? 88.80400  -17.97300 65.13600  1.000 12.39643 ? 22  GLN   A CA    1 
ATOM   1517 C  C     . GLN   B 1 23  ? 89.90200  -18.98000 65.44100  1.000 15.11563 ? 22  GLN   A C     1 
ATOM   1518 O  O     . GLN   B 1 23  ? 90.82400  -18.69900 66.21600  1.000 14.99030 ? 22  GLN   A O     1 
ATOM   1519 C  CB    . GLN   B 1 23  ? 87.53700  -18.31600 65.91200  1.000 15.13629 ? 22  GLN   A CB    1 
ATOM   1520 C  CG    . GLN   B 1 23  ? 86.73100  -17.10500 66.30000  1.000 15.79957 ? 22  GLN   A CG    1 
ATOM   1521 C  CD    . GLN   B 1 23  ? 87.31500  -16.36800 67.49600  1.000 16.91228 ? 22  GLN   A CD    1 
ATOM   1522 O  OE1   . GLN   B 1 23  ? 88.51200  -16.45400 67.78500  1.000 17.99309 ? 22  GLN   A OE1   1 
ATOM   1523 N  NE2   . GLN   B 1 23  ? 86.46300  -15.64500 68.20500  1.000 15.00530 ? 22  GLN   A NE2   1 
ATOM   1524 N  N     . LEU   B 1 24  ? 89.82600  -20.16400 64.83200  1.000 10.48517 ? 23  LEU   A N     1 
ATOM   1525 C  CA    . LEU   B 1 24  ? 90.88700  -21.13700 65.05800  1.000 11.27844 ? 23  LEU   A CA    1 
ATOM   1526 C  C     . LEU   B 1 24  ? 92.22500  -20.59900 64.57500  1.000 15.85733 ? 23  LEU   A C     1 
ATOM   1527 O  O     . LEU   B 1 24  ? 93.23700  -20.71100 65.27600  1.000 17.91264 ? 23  LEU   A O     1 
ATOM   1528 C  CB    . LEU   B 1 24  ? 90.56900  -22.44700 64.35300  1.000 15.04221 ? 23  LEU   A CB    1 
ATOM   1529 C  CG    . LEU   B 1 24  ? 91.63100  -23.50000 64.65400  1.000 17.11584 ? 23  LEU   A CG    1 
ATOM   1530 C  CD1   . LEU   B 1 24  ? 91.28000  -24.21100 65.93700  1.000 14.40238 ? 23  LEU   A CD1   1 
ATOM   1531 C  CD2   . LEU   B 1 24  ? 91.73900  -24.46000 63.48900  1.000 13.97292 ? 23  LEU   A CD2   1 
ATOM   1532 N  N     . ILE   B 1 25  ? 92.23900  -19.99300 63.38700  1.000 15.54590 ? 24  ILE   A N     1 
ATOM   1533 C  CA    . ILE   B 1 25  ? 93.48600  -19.56500 62.75600  1.000 17.43275 ? 24  ILE   A CA    1 
ATOM   1534 C  C     . ILE   B 1 25  ? 93.95300  -18.22400 63.31400  1.000 19.41172 ? 24  ILE   A C     1 
ATOM   1535 O  O     . ILE   B 1 25  ? 95.11100  -18.07400 63.72600  1.000 21.97263 ? 24  ILE   A O     1 
ATOM   1536 C  CB    . ILE   B 1 25  ? 93.30100  -19.49100 61.22900  1.000 18.99361 ? 24  ILE   A CB    1 
ATOM   1537 C  CG1   . ILE   B 1 25  ? 92.95500  -20.86600 60.66200  1.000 20.26437 ? 24  ILE   A CG1   1 
ATOM   1538 C  CG2   . ILE   B 1 25  ? 94.55900  -18.92600 60.56600  1.000 16.62450 ? 24  ILE   A CG2   1 
ATOM   1539 C  CD1   . ILE   B 1 25  ? 94.11400  -21.81600 60.64300  1.000 19.03208 ? 24  ILE   A CD1   1 
ATOM   1540 N  N     . GLN   B 1 26  ? 93.07400  -17.22200 63.31400  1.000 16.64287 ? 25  GLN   A N     1 
ATOM   1541 C  CA    . GLN   B 1 26  ? 93.46600  -15.84000 63.56400  1.000 18.72603 ? 25  GLN   A CA    1 
ATOM   1542 C  C     . GLN   B 1 26  ? 93.02600  -15.30600 64.91800  1.000 18.66411 ? 25  GLN   A C     1 
ATOM   1543 O  O     . GLN   B 1 26  ? 93.33900  -14.15700 65.23100  1.000 20.41889 ? 25  GLN   A O     1 
ATOM   1544 C  CB    . GLN   B 1 26  ? 92.92000  -14.92300 62.46100  1.000 18.85848 ? 25  GLN   A CB    1 
ATOM   1545 C  CG    . GLN   B 1 26  ? 93.46600  -15.24000 61.08700  1.000 19.07270 ? 25  GLN   A CG    1 
ATOM   1546 C  CD    . GLN   B 1 26  ? 92.89600  -14.34300 60.01700  1.000 25.92834 ? 25  GLN   A CD    1 
ATOM   1547 O  OE1   . GLN   B 1 26  ? 92.15300  -13.40600 60.30700  1.000 26.55731 ? 25  GLN   A OE1   1 
ATOM   1548 N  NE2   . GLN   B 1 26  ? 93.23800  -14.62600 58.76300  1.000 29.07996 ? 25  GLN   A NE2   1 
ATOM   1549 N  N     . ASN   B 1 27  ? 92.30400  -16.09100 65.71700  1.000 15.10585 ? 26  ASN   A N     1 
ATOM   1550 C  CA    . ASN   B 1 27  ? 91.94100  -15.71800 67.08600  1.000 18.98466 ? 26  ASN   A CA    1 
ATOM   1551 C  C     . ASN   B 1 27  ? 91.17200  -14.40000 67.15000  1.000 19.47173 ? 26  ASN   A C     1 
ATOM   1552 O  O     . ASN   B 1 27  ? 91.44300  -13.55400 68.00400  1.000 21.01832 ? 26  ASN   A O     1 
ATOM   1553 C  CB    . ASN   B 1 27  ? 93.18100  -15.65400 67.98700  1.000 18.58792 ? 26  ASN   A CB    1 
ATOM   1554 C  CG    . ASN   B 1 27  ? 93.68800  -17.02200 68.35000  1.000 27.37246 ? 26  ASN   A CG    1 
ATOM   1555 O  OD1   . ASN   B 1 27  ? 93.11500  -17.69500 69.21200  1.000 27.39763 ? 26  ASN   A OD1   1 
ATOM   1556 N  ND2   . ASN   B 1 27  ? 94.74200  -17.46600 67.66800  1.000 28.64508 ? 26  ASN   A ND2   1 
ATOM   1557 N  N     . HIS   B 1 28  ? 90.19800  -14.22200 66.25700  1.000 19.57969 ? 27  HIS   A N     1 
ATOM   1558 C  CA    . HIS   B 1 28  ? 89.30200  -13.07600 66.36300  1.000 17.62104 ? 27  HIS   A CA    1 
ATOM   1559 C  C     . HIS   B 1 28  ? 88.02900  -13.35300 65.56900  1.000 20.43688 ? 27  HIS   A C     1 
ATOM   1560 O  O     . HIS   B 1 28  ? 87.95700  -14.29100 64.76600  1.000 17.88711 ? 27  HIS   A O     1 
ATOM   1561 C  CB    . HIS   B 1 28  ? 89.97700  -11.78500 65.88900  1.000 24.12356 ? 27  HIS   A CB    1 
ATOM   1562 C  CG    . HIS   B 1 28  ? 90.28500  -11.77300 64.42600  1.000 27.92242 ? 27  HIS   A CG    1 
ATOM   1563 N  ND1   . HIS   B 1 28  ? 89.37900  -11.34100 63.48100  1.000 30.70242 ? 27  HIS   A ND1   1 
ATOM   1564 C  CD2   . HIS   B 1 28  ? 91.39200  -12.14700 63.74400  1.000 29.15403 ? 27  HIS   A CD2   1 
ATOM   1565 C  CE1   . HIS   B 1 28  ? 89.91400  -11.45200 62.27900  1.000 30.17292 ? 27  HIS   A CE1   1 
ATOM   1566 N  NE2   . HIS   B 1 28  ? 91.13500  -11.94100 62.40900  1.000 24.95542 ? 27  HIS   A NE2   1 
ATOM   1567 N  N     . PHE   B 1 29  ? 87.02200  -12.51400 65.81300  1.000 17.39989 ? 28  PHE   A N     1 
ATOM   1568 C  CA    . PHE   B 1 29  ? 85.70000  -12.62900 65.21000  1.000 17.56368 ? 28  PHE   A CA    1 
ATOM   1569 C  C     . PHE   B 1 29  ? 85.24600  -11.25000 64.75400  1.000 15.32110 ? 28  PHE   A C     1 
ATOM   1570 O  O     . PHE   B 1 29  ? 85.44500  -10.26300 65.47100  1.000 21.76071 ? 28  PHE   A O     1 
ATOM   1571 C  CB    . PHE   B 1 29  ? 84.69600  -13.21800 66.22000  1.000 16.32812 ? 28  PHE   A CB    1 
ATOM   1572 C  CG    . PHE   B 1 29  ? 83.25500  -13.20200 65.74900  1.000 19.80366 ? 28  PHE   A CG    1 
ATOM   1573 C  CD1   . PHE   B 1 29  ? 82.73500  -14.24500 64.99900  1.000 14.48120 ? 28  PHE   A CD1   1 
ATOM   1574 C  CD2   . PHE   B 1 29  ? 82.41700  -12.15800 66.08900  1.000 14.73128 ? 28  PHE   A CD2   1 
ATOM   1575 C  CE1   . PHE   B 1 29  ? 81.41700  -14.20700 64.57200  1.000 14.77990 ? 28  PHE   A CE1   1 
ATOM   1576 C  CE2   . PHE   B 1 29  ? 81.11300  -12.12900 65.67800  1.000 16.68329 ? 28  PHE   A CE2   1 
ATOM   1577 C  CZ    . PHE   B 1 29  ? 80.60500  -13.14800 64.91800  1.000 15.47930 ? 28  PHE   A CZ    1 
ATOM   1578 N  N     . VAL   B 1 30  ? 84.64000  -11.17500 63.56800  1.000 22.91412 ? 29  VAL   A N     1 
ATOM   1579 C  CA    . VAL   B 1 30  ? 83.98400  -9.94900  63.11900  1.000 26.03805 ? 29  VAL   A CA    1 
ATOM   1580 C  C     . VAL   B 1 30  ? 82.57500  -10.27900 62.65300  1.000 18.54871 ? 29  VAL   A C     1 
ATOM   1581 O  O     . VAL   B 1 30  ? 82.31300  -11.35900 62.11200  1.000 22.86000 ? 29  VAL   A O     1 
ATOM   1582 C  CB    . VAL   B 1 30  ? 84.74100  -9.21500  61.98600  1.000 27.30270 ? 29  VAL   A CB    1 
ATOM   1583 C  CG1   . VAL   B 1 30  ? 86.15400  -8.80000  62.43100  1.000 27.28691 ? 29  VAL   A CG1   1 
ATOM   1584 C  CG2   . VAL   B 1 30  ? 84.76400  -10.06700 60.71900  1.000 26.18702 ? 29  VAL   A CG2   1 
ATOM   1585 N  N     . ASP   B 1 31  ? 81.66900  -9.31700  62.84800  1.000 22.88659 ? 30  ASP   A N     1 
ATOM   1586 C  CA    . ASP   B 1 31  ? 80.27300  -9.49700  62.46600  1.000 27.33257 ? 30  ASP   A CA    1 
ATOM   1587 C  C     . ASP   B 1 31  ? 80.05700  -9.43500  60.96300  1.000 21.89985 ? 30  ASP   A C     1 
ATOM   1588 O  O     . ASP   B 1 31  ? 79.06000  -9.98500  60.47600  1.000 20.32512 ? 30  ASP   A O     1 
ATOM   1589 C  CB    . ASP   B 1 31  ? 79.40100  -8.43400  63.14300  1.000 30.47892 ? 30  ASP   A CB    1 
ATOM   1590 C  CG    . ASP   B 1 31  ? 79.19900  -8.70400  64.61600  1.000 30.68145 ? 30  ASP   A CG    1 
ATOM   1591 O  OD1   . ASP   B 1 31  ? 78.56200  -9.72500  64.95900  1.000 30.47963 ? 30  ASP   A OD1   1 
ATOM   1592 O  OD2   . ASP   B 1 31  ? 79.70200  -7.90900  65.43500  1.000 38.67537 ? 30  ASP   A OD2   1 
ATOM   1593 N  N     . GLU   B 1 32  ? 80.94700  -8.77200  60.22200  1.000 22.52069 ? 31  GLU   A N     1 
ATOM   1594 C  CA    . GLU   B 1 32  ? 80.70800  -8.55300  58.80100  1.000 20.89163 ? 31  GLU   A CA    1 
ATOM   1595 C  C     . GLU   B 1 32  ? 80.78600  -9.87100  58.03900  1.000 20.32724 ? 31  GLU   A C     1 
ATOM   1596 O  O     . GLU   B 1 32  ? 81.66400  -10.70600 58.28100  1.000 20.72789 ? 31  GLU   A O     1 
ATOM   1597 C  CB    . GLU   B 1 32  ? 81.70200  -7.53300  58.23300  1.000 24.89614 ? 31  GLU   A CB    1 
ATOM   1598 C  CG    . GLU   B 1 32  ? 81.35600  -7.04600  56.83500  1.000 25.25129 ? 31  GLU   A CG    1 
ATOM   1599 C  CD    . GLU   B 1 32  ? 82.27100  -5.93200  56.31700  1.000 30.64024 ? 31  GLU   A CD    1 
ATOM   1600 O  OE1   . GLU   B 1 32  ? 83.48400  -5.92100  56.62500  1.000 30.38365 ? 31  GLU   A OE1   1 
ATOM   1601 O  OE2   . GLU   B 1 32  ? 81.75900  -5.05300  55.58800  1.000 32.17047 ? 31  GLU   A OE2   1 
ATOM   1602 N  N     . TYR   B 1 33  ? 79.83700  -10.07100 57.13300  1.000 15.23842 ? 32  TYR   A N     1 
ATOM   1603 C  CA    . TYR   B 1 33  ? 79.74500  -11.31500 56.37300  1.000 15.70117 ? 32  TYR   A CA    1 
ATOM   1604 C  C     . TYR   B 1 33  ? 80.52800  -11.15300 55.07500  1.000 16.01954 ? 32  TYR   A C     1 
ATOM   1605 O  O     . TYR   B 1 33  ? 80.22100  -10.27100 54.27200  1.000 14.04580 ? 32  TYR   A O     1 
ATOM   1606 C  CB    . TYR   B 1 33  ? 78.27200  -11.64800 56.12400  1.000 14.35328 ? 32  TYR   A CB    1 
ATOM   1607 C  CG    . TYR   B 1 33  ? 77.95700  -12.88000 55.29400  1.000 13.26818 ? 32  TYR   A CG    1 
ATOM   1608 C  CD1   . TYR   B 1 33  ? 78.89900  -13.89300 55.07500  1.000 10.33808 ? 32  TYR   A CD1   1 
ATOM   1609 C  CD2   . TYR   B 1 33  ? 76.69200  -13.03200 54.74400  1.000 16.68448 ? 32  TYR   A CD2   1 
ATOM   1610 C  CE1   . TYR   B 1 33  ? 78.57900  -15.00800 54.30200  1.000 9.79455  ? 32  TYR   A CE1   1 
ATOM   1611 C  CE2   . TYR   B 1 33  ? 76.36400  -14.15000 53.98300  1.000 17.74839 ? 32  TYR   A CE2   1 
ATOM   1612 C  CZ    . TYR   B 1 33  ? 77.30100  -15.12900 53.76500  1.000 10.88509 ? 32  TYR   A CZ    1 
ATOM   1613 O  OH    . TYR   B 1 33  ? 76.94400  -16.22400 53.01200  1.000 10.99482 ? 32  TYR   A OH    1 
ATOM   1614 N  N     . ASP   B 1 34  ? 81.56300  -11.97400 54.89200  1.000 11.65976 ? 33  ASP   A N     1 
ATOM   1615 C  CA    . ASP   B 1 34  ? 82.36400  -12.00000 53.66600  1.000 13.42571 ? 33  ASP   A CA    1 
ATOM   1616 C  C     . ASP   B 1 34  ? 82.14600  -13.35700 53.00900  1.000 12.18952 ? 33  ASP   A C     1 
ATOM   1617 O  O     . ASP   B 1 34  ? 82.85800  -14.32600 53.32400  1.000 13.27063 ? 33  ASP   A O     1 
ATOM   1618 C  CB    . ASP   B 1 34  ? 83.85100  -11.76600 53.96300  1.000 13.70016 ? 33  ASP   A CB    1 
ATOM   1619 C  CG    . ASP   B 1 34  ? 84.68700  -11.56700 52.70200  1.000 18.98118 ? 33  ASP   A CG    1 
ATOM   1620 O  OD1   . ASP   B 1 34  ? 84.11000  -11.53700 51.59600  1.000 12.88525 ? 33  ASP   A OD1   1 
ATOM   1621 O  OD2   . ASP   B 1 34  ? 85.93200  -11.42900 52.82000  1.000 20.58000 ? 33  ASP   A OD2   1 
ATOM   1622 N  N     . PRO   B 1 35  ? 81.17500  -13.47700 52.09900  1.000 11.02317 ? 34  PRO   A N     1 
ATOM   1623 C  CA    . PRO   B 1 35  ? 80.82100  -14.80100 51.55900  1.000 10.33250 ? 34  PRO   A CA    1 
ATOM   1624 C  C     . PRO   B 1 35  ? 81.98600  -15.46700 50.84100  1.000 10.99132 ? 34  PRO   A C     1 
ATOM   1625 O  O     . PRO   B 1 35  ? 82.66100  -14.85000 50.02200  1.000 14.07389 ? 34  PRO   A O     1 
ATOM   1626 C  CB    . PRO   B 1 35  ? 79.65800  -14.49000 50.60600  1.000 12.80002 ? 34  PRO   A CB    1 
ATOM   1627 C  CG    . PRO   B 1 35  ? 79.07200  -13.21300 51.12900  1.000 11.49025 ? 34  PRO   A CG    1 
ATOM   1628 C  CD    . PRO   B 1 35  ? 80.29500  -12.42300 51.57500  1.000 11.85452 ? 34  PRO   A CD    1 
ATOM   1629 N  N     . THR   B 1 36  ? 82.18300  -16.74600 51.13700  1.000 10.22620 ? 35  THR   A N     1 
ATOM   1630 C  CA    . THR   B 1 36  ? 83.34400  -17.49000 50.67200  1.000 10.25077 ? 35  THR   A CA    1 
ATOM   1631 C  C     . THR   B 1 36  ? 83.17600  -17.96900 49.23300  1.000 12.09802 ? 35  THR   A C     1 
ATOM   1632 O  O     . THR   B 1 36  ? 82.09000  -18.38000 48.81800  1.000 9.53302  ? 35  THR   A O     1 
ATOM   1633 C  CB    . THR   B 1 36  ? 83.58100  -18.68200 51.60300  1.000 8.53706  ? 35  THR   A CB    1 
ATOM   1634 O  OG1   . THR   B 1 36  ? 83.71100  -18.21100 52.94400  1.000 8.43112  ? 35  THR   A OG1   1 
ATOM   1635 C  CG2   . THR   B 1 36  ? 84.86200  -19.47500 51.22500  1.000 9.61514  ? 35  THR   A CG2   1 
ATOM   1636 N  N     . ILE   B 1 37  ? 84.26700  -17.91000 48.46900  1.000 12.02014 ? 36  ILE   A N     1 
ATOM   1637 C  CA    . ILE   B 1 37  ? 84.38600  -18.69800 47.25000  1.000 10.29664 ? 36  ILE   A CA    1 
ATOM   1638 C  C     . ILE   B 1 37  ? 85.13800  -19.97000 47.62300  1.000 9.75188  ? 36  ILE   A C     1 
ATOM   1639 O  O     . ILE   B 1 37  ? 84.58400  -21.07300 47.56500  1.000 10.56743 ? 36  ILE   A O     1 
ATOM   1640 C  CB    . ILE   B 1 37  ? 85.10900  -17.92800 46.13000  1.000 11.31513 ? 36  ILE   A CB    1 
ATOM   1641 C  CG1   . ILE   B 1 37  ? 84.25700  -16.75200 45.64400  1.000 12.00440 ? 36  ILE   A CG1   1 
ATOM   1642 C  CG2   . ILE   B 1 37  ? 85.41100  -18.86000 44.97100  1.000 11.65196 ? 36  ILE   A CG2   1 
ATOM   1643 C  CD1   . ILE   B 1 37  ? 83.04300  -17.16800 44.85800  1.000 12.14397 ? 36  ILE   A CD1   1 
ATOM   1644 N  N     . GLU   B 1 38  ? 86.39700  -19.81400 48.03300  1.000 10.68351 ? 37  GLU   A N     1 
ATOM   1645 C  CA    . GLU   B 1 38  ? 87.17500  -20.91600 48.59200  1.000 12.83995 ? 37  GLU   A CA    1 
ATOM   1646 C  C     . GLU   B 1 38  ? 88.40600  -20.33800 49.28300  1.000 9.67827  ? 37  GLU   A C     1 
ATOM   1647 O  O     . GLU   B 1 38  ? 89.02100  -19.41200 48.76300  1.000 12.79091 ? 37  GLU   A O     1 
ATOM   1648 C  CB    . GLU   B 1 38  ? 87.59200  -21.91800 47.50800  1.000 13.29924 ? 37  GLU   A CB    1 
ATOM   1649 C  CG    . GLU   B 1 38  ? 88.37400  -23.12500 48.03000  1.000 10.55390 ? 37  GLU   A CG    1 
ATOM   1650 C  CD    . GLU   B 1 38  ? 89.12700  -23.85500 46.92900  1.000 17.54068 ? 37  GLU   A CD    1 
ATOM   1651 O  OE1   . GLU   B 1 38  ? 88.50700  -24.58300 46.12700  1.000 15.55881 ? 37  GLU   A OE1   1 
ATOM   1652 O  OE2   . GLU   B 1 38  ? 90.35700  -23.68500 46.85400  1.000 17.66722 ? 37  GLU   A OE2   1 
ATOM   1653 N  N     . ASP   B 1 39  ? 88.75200  -20.87700 50.45200  1.000 9.88821  ? 38  ASP   A N     1 
ATOM   1654 C  CA    . ASP   B 1 39  ? 89.92500  -20.41900 51.18500  1.000 13.58291 ? 38  ASP   A CA    1 
ATOM   1655 C  C     . ASP   B 1 39  ? 90.59000  -21.58200 51.89000  1.000 12.94974 ? 38  ASP   A C     1 
ATOM   1656 O  O     . ASP   B 1 39  ? 89.93200  -22.54600 52.28700  1.000 10.62537 ? 38  ASP   A O     1 
ATOM   1657 C  CB    . ASP   B 1 39  ? 89.57400  -19.34400 52.21600  1.000 11.45465 ? 38  ASP   A CB    1 
ATOM   1658 C  CG    . ASP   B 1 39  ? 89.20700  -18.03100 51.57200  1.000 17.36669 ? 38  ASP   A CG    1 
ATOM   1659 O  OD1   . ASP   B 1 39  ? 90.10500  -17.36800 51.02100  1.000 16.00896 ? 38  ASP   A OD1   1 
ATOM   1660 O  OD2   . ASP   B 1 39  ? 88.01100  -17.68300 51.59000  1.000 17.51593 ? 38  ASP   A OD2   1 
ATOM   1661 N  N     . SER   B 1 40  ? 91.91100  -21.46300 52.06500  1.000 14.95146 ? 39  SER   A N     1 
ATOM   1662 C  CA    . SER   B 1 40  ? 92.74300  -22.50900 52.64500  1.000 16.05298 ? 39  SER   A CA    1 
ATOM   1663 C  C     . SER   B 1 40  ? 93.64200  -21.92300 53.72200  1.000 15.99816 ? 39  SER   A C     1 
ATOM   1664 O  O     . SER   B 1 40  ? 94.15300  -20.80300 53.58000  1.000 14.84429 ? 39  SER   A O     1 
ATOM   1665 C  CB    . SER   B 1 40  ? 93.61800  -23.19100 51.58300  1.000 16.88726 ? 39  SER   A CB    1 
ATOM   1666 O  OG    . SER   B 1 40  ? 92.84600  -24.06000 50.78600  1.000 19.07411 ? 39  SER   A OG    1 
ATOM   1667 N  N     . TYR   B 1 41  ? 93.84300  -22.68300 54.79800  1.000 11.55813 ? 40  TYR   A N     1 
ATOM   1668 C  CA    . TYR   B 1 41  ? 94.70900  -22.21800 55.87000  1.000 14.50581 ? 40  TYR   A CA    1 
ATOM   1669 C  C     . TYR   B 1 41  ? 95.55800  -23.37400 56.36700  1.000 13.11029 ? 40  TYR   A C     1 
ATOM   1670 O  O     . TYR   B 1 41  ? 95.22700  -24.54300 56.17700  1.000 12.83141 ? 40  TYR   A O     1 
ATOM   1671 C  CB    . TYR   B 1 41  ? 93.90700  -21.60700 57.01900  1.000 11.97888 ? 40  TYR   A CB    1 
ATOM   1672 C  CG    . TYR   B 1 41  ? 92.98900  -20.48700 56.56800  1.000 15.52335 ? 40  TYR   A CG    1 
ATOM   1673 C  CD1   . TYR   B 1 41  ? 93.43700  -19.17500 56.50600  1.000 18.11202 ? 40  TYR   A CD1   1 
ATOM   1674 C  CD2   . TYR   B 1 41  ? 91.68200  -20.76000 56.17900  1.000 14.63523 ? 40  TYR   A CD2   1 
ATOM   1675 C  CE1   . TYR   B 1 41  ? 92.58800  -18.15000 56.07900  1.000 19.77626 ? 40  TYR   A CE1   1 
ATOM   1676 C  CE2   . TYR   B 1 41  ? 90.83700  -19.76300 55.76200  1.000 14.41557 ? 40  TYR   A CE2   1 
ATOM   1677 C  CZ    . TYR   B 1 41  ? 91.29000  -18.45800 55.71100  1.000 19.02406 ? 40  TYR   A CZ    1 
ATOM   1678 O  OH    . TYR   B 1 41  ? 90.42200  -17.47700 55.28600  1.000 18.11794 ? 40  TYR   A OH    1 
ATOM   1679 N  N     . ARG   B 1 42  ? 96.68300  -23.02600 56.98100  1.000 11.66030 ? 41  ARG   A N     1 
ATOM   1680 C  CA    . ARG   B 1 42  ? 97.57600  -24.00200 57.59100  1.000 13.99170 ? 41  ARG   A CA    1 
ATOM   1681 C  C     . ARG   B 1 42  ? 97.85300  -23.52500 59.00700  1.000 15.17490 ? 41  ARG   A C     1 
ATOM   1682 O  O     . ARG   B 1 42  ? 98.12200  -22.33700 59.21500  1.000 19.61616 ? 41  ARG   A O     1 
ATOM   1683 C  CB    . ARG   B 1 42  ? 98.88900  -24.16700 56.78800  1.000 18.49181 ? 41  ARG   A CB    1 
ATOM   1684 C  CG    . ARG   B 1 42  ? 98.76700  -25.03500 55.52300  1.000 18.00554 ? 41  ARG   A CG    1 
ATOM   1685 C  CD    . ARG   B 1 42  ? 99.95600  -24.93400 54.53400  1.000 22.45450 ? 41  ARG   A CD    1 
ATOM   1686 N  NE    . ARG   B 1 42  ? 101.24500 -25.46300 54.98600  1.000 18.97961 ? 41  ARG   A NE    1 
ATOM   1687 C  CZ    . ARG   B 1 42  ? 101.65700 -26.72100 54.84300  1.000 17.62076 ? 41  ARG   A CZ    1 
ATOM   1688 N  NH1   . ARG   B 1 42  ? 100.85100 -27.67200 54.40400  1.000 26.90974 ? 41  ARG   A NH1   1 
ATOM   1689 N  NH2   . ARG   B 1 42  ? 102.91100 -27.03700 55.15900  1.000 17.19511 ? 41  ARG   A NH2   1 
ATOM   1690 N  N     . LYS   B 1 43  ? 97.76200  -24.42900 59.97900  1.000 12.26809 ? 42  LYS   A N     1 
ATOM   1691 C  CA    . LYS   B 1 43  ? 98.10100  -24.06900 61.35000  1.000 17.18805 ? 42  LYS   A CA    1 
ATOM   1692 C  C     . LYS   B 1 43  ? 98.75800  -25.24700 62.05000  1.000 16.21409 ? 42  LYS   A C     1 
ATOM   1693 O  O     . LYS   B 1 43  ? 98.29500  -26.38400 61.91900  1.000 16.54465 ? 42  LYS   A O     1 
ATOM   1694 C  CB    . LYS   B 1 43  ? 96.86800  -23.64100 62.15300  1.000 18.08129 ? 42  LYS   A CB    1 
ATOM   1695 C  CG    . LYS   B 1 43  ? 97.22400  -23.09200 63.52600  1.000 19.53013 ? 42  LYS   A CG    1 
ATOM   1696 C  CD    . LYS   B 1 43  ? 95.98900  -22.68000 64.30800  1.000 23.51277 ? 42  LYS   A CD    1 
ATOM   1697 C  CE    . LYS   B 1 43  ? 96.38500  -21.98600 65.60500  1.000 23.10237 ? 42  LYS   A CE    1 
ATOM   1698 N  NZ    . LYS   B 1 43  ? 97.09500  -20.69300 65.31600  1.000 23.65877 ? 42  LYS   A NZ    1 
ATOM   1699 N  N     . GLN   B 1 44  ? 99.82400  -24.97100 62.80200  1.000 19.60328 ? 43  GLN   A N     1 
ATOM   1700 C  CA    . GLN   B 1 44  ? 100.44000 -25.99100 63.64000  1.000 18.01925 ? 43  GLN   A CA    1 
ATOM   1701 C  C     . GLN   B 1 44  ? 99.83500  -25.92800 65.03800  1.000 22.29553 ? 43  GLN   A C     1 
ATOM   1702 O  O     . GLN   B 1 44  ? 99.71000  -24.84400 65.62400  1.000 21.53922 ? 43  GLN   A O     1 
ATOM   1703 C  CB    . GLN   B 1 44  ? 101.96100 -25.82800 63.70300  1.000 17.81387 ? 43  GLN   A CB    1 
ATOM   1704 C  CG    . GLN   B 1 44  ? 102.63900 -26.88900 64.54400  1.000 17.26260 ? 43  GLN   A CG    1 
ATOM   1705 C  CD    . GLN   B 1 44  ? 104.15900 -26.78100 64.54900  1.000 33.43959 ? 43  GLN   A CD    1 
ATOM   1706 O  OE1   . GLN   B 1 44  ? 104.80100 -26.69700 63.49600  1.000 31.58735 ? 43  GLN   A OE1   1 
ATOM   1707 N  NE2   . GLN   B 1 44  ? 104.74200 -26.77500 65.74600  1.000 30.01330 ? 43  GLN   A NE2   1 
ATOM   1708 N  N     . VAL   B 1 45  ? 99.42800  -27.09700 65.54600  1.000 18.30959 ? 44  VAL   A N     1 
ATOM   1709 C  CA    . VAL   B 1 45  ? 98.80800  -27.24400 66.85600  1.000 15.11133 ? 44  VAL   A CA    1 
ATOM   1710 C  C     . VAL   B 1 45  ? 99.43800  -28.43500 67.56400  1.000 19.96114 ? 44  VAL   A C     1 
ATOM   1711 O  O     . VAL   B 1 45  ? 100.06000 -29.30300 66.94200  1.000 18.85799 ? 44  VAL   A O     1 
ATOM   1712 C  CB    . VAL   B 1 45  ? 97.28500  -27.44900 66.75500  1.000 16.81404 ? 44  VAL   A CB    1 
ATOM   1713 C  CG1   . VAL   B 1 45  ? 96.61300  -26.23300 66.11800  1.000 19.56417 ? 44  VAL   A CG1   1 
ATOM   1714 C  CG2   . VAL   B 1 45  ? 96.98800  -28.68300 65.92600  1.000 15.62292 ? 44  VAL   A CG2   1 
ATOM   1715 N  N     . VAL   B 1 46  ? 99.26900  -28.45900 68.88600  1.000 21.47239 ? 45  VAL   A N     1 
ATOM   1716 C  CA    . VAL   B 1 46  ? 99.56500  -29.61800 69.72300  1.000 22.26850 ? 45  VAL   A CA    1 
ATOM   1717 C  C     . VAL   B 1 46  ? 98.23600  -30.13900 70.26400  1.000 21.63823 ? 45  VAL   A C     1 
ATOM   1718 O  O     . VAL   B 1 46  ? 97.52700  -29.42300 70.98200  1.000 19.20087 ? 45  VAL   A O     1 
ATOM   1719 C  CB    . VAL   B 1 46  ? 100.52900 -29.27300 70.86900  1.000 22.15897 ? 45  VAL   A CB    1 
ATOM   1720 C  CG1   . VAL   B 1 46  ? 100.84900 -30.51600 71.67700  1.000 26.25983 ? 45  VAL   A CG1   1 
ATOM   1721 C  CG2   . VAL   B 1 46  ? 101.81000 -28.67600 70.33200  1.000 26.46765 ? 45  VAL   A CG2   1 
ATOM   1722 N  N     . ILE   B 1 47  ? 97.88900  -31.37500 69.90700  1.000 18.45939 ? 46  ILE   A N     1 
ATOM   1723 C  CA    . ILE   B 1 47  ? 96.66100  -32.01500 70.36800  1.000 20.71681 ? 46  ILE   A CA    1 
ATOM   1724 C  C     . ILE   B 1 47  ? 97.03700  -33.28900 71.11100  1.000 19.14600 ? 46  ILE   A C     1 
ATOM   1725 O  O     . ILE   B 1 47  ? 97.58100  -34.22500 70.51200  1.000 19.58856 ? 46  ILE   A O     1 
ATOM   1726 C  CB    . ILE   B 1 47  ? 95.70600  -32.33000 69.20800  1.000 15.67274 ? 46  ILE   A CB    1 
ATOM   1727 C  CG1   . ILE   B 1 47  ? 95.27800  -31.05200 68.49300  1.000 12.98267 ? 46  ILE   A CG1   1 
ATOM   1728 C  CG2   . ILE   B 1 47  ? 94.48600  -33.08100 69.71800  1.000 14.41855 ? 46  ILE   A CG2   1 
ATOM   1729 C  CD1   . ILE   B 1 47  ? 94.67000  -31.32600 67.15800  1.000 13.14833 ? 46  ILE   A CD1   1 
ATOM   1730 N  N     . ASP   B 1 48  ? 96.73100  -33.32700 72.40800  1.000 18.67044 ? 47  ASP   A N     1 
ATOM   1731 C  CA    . ASP   B 1 48  ? 97.05300  -34.46700 73.26900  1.000 21.83077 ? 47  ASP   A CA    1 
ATOM   1732 C  C     . ASP   B 1 48  ? 98.54300  -34.78400 73.22900  1.000 20.39881 ? 47  ASP   A C     1 
ATOM   1733 O  O     . ASP   B 1 48  ? 98.94400  -35.94500 73.13400  1.000 23.89594 ? 47  ASP   A O     1 
ATOM   1734 C  CB    . ASP   B 1 48  ? 96.23800  -35.71100 72.89800  1.000 21.00533 ? 47  ASP   A CB    1 
ATOM   1735 C  CG    . ASP   B 1 48  ? 94.73800  -35.47600 72.95500  1.000 21.00425 ? 47  ASP   A CG    1 
ATOM   1736 O  OD1   . ASP   B 1 48  ? 94.30500  -34.49100 73.58900  1.000 20.26111 ? 47  ASP   A OD1   1 
ATOM   1737 O  OD2   . ASP   B 1 48  ? 93.99300  -36.28800 72.36100  1.000 20.01138 ? 47  ASP   A OD2   1 
ATOM   1738 N  N     . GLY   B 1 49  ? 99.37200  -33.74600 73.29000  1.000 19.41475 ? 48  GLY   A N     1 
ATOM   1739 C  CA    . GLY   B 1 49  ? 100.80400 -33.93600 73.29400  1.000 20.61400 ? 48  GLY   A CA    1 
ATOM   1740 C  C     . GLY   B 1 49  ? 101.43500 -34.26100 71.95800  1.000 20.40429 ? 48  GLY   A C     1 
ATOM   1741 O  O     . GLY   B 1 49  ? 102.66800 -34.35200 71.88700  1.000 21.40636 ? 48  GLY   A O     1 
ATOM   1742 N  N     . GLU   B 1 50  ? 100.64800 -34.43400 70.89700  1.000 21.62423 ? 49  GLU   A N     1 
ATOM   1743 C  CA    . GLU   B 1 50  ? 101.16000 -34.76700 69.56800  1.000 18.34581 ? 49  GLU   A CA    1 
ATOM   1744 C  C     . GLU   B 1 50  ? 101.04700 -33.54100 68.66700  1.000 19.23406 ? 49  GLU   A C     1 
ATOM   1745 O  O     . GLU   B 1 50  ? 99.95800  -32.98300 68.51200  1.000 18.04830 ? 49  GLU   A O     1 
ATOM   1746 C  CB    . GLU   B 1 50  ? 100.38600 -35.94700 68.96700  1.000 22.12166 ? 49  GLU   A CB    1 
ATOM   1747 C  CG    . GLU   B 1 50  ? 100.49000 -37.24300 69.78000  1.000 20.48437 ? 49  GLU   A CG    1 
ATOM   1748 C  CD    . GLU   B 1 50  ? 99.48600  -38.33700 69.36200  1.000 33.16722 ? 49  GLU   A CD    1 
ATOM   1749 O  OE1   . GLU   B 1 50  ? 98.92200  -38.28100 68.23500  1.000 27.70280 ? 49  GLU   A OE1   1 
ATOM   1750 O  OE2   . GLU   B 1 50  ? 99.26600  -39.25800 70.18400  1.000 30.23592 ? 49  GLU   A OE2   1 
ATOM   1751 N  N     . THR   B 1 51  ? 102.16200 -33.13400 68.06200  1.000 18.64776 ? 50  THR   A N     1 
ATOM   1752 C  CA    . THR   B 1 51  ? 102.16400 -31.96300 67.19400  1.000 19.75334 ? 50  THR   A CA    1 
ATOM   1753 C  C     . THR   B 1 51  ? 101.60000 -32.32400 65.82800  1.000 20.56011 ? 50  THR   A C     1 
ATOM   1754 O  O     . THR   B 1 51  ? 101.98000 -33.34400 65.24500  1.000 20.34207 ? 50  THR   A O     1 
ATOM   1755 C  CB    . THR   B 1 51  ? 103.58200 -31.41300 67.03200  1.000 26.55818 ? 50  THR   A CB    1 
ATOM   1756 O  OG1   . THR   B 1 51  ? 104.17400 -31.22900 68.32100  1.000 26.30992 ? 50  THR   A OG1   1 
ATOM   1757 C  CG2   . THR   B 1 51  ? 103.55000 -30.08200 66.29100  1.000 22.66640 ? 50  THR   A CG2   1 
ATOM   1758 N  N     . SER   B 1 52  ? 100.70200 -31.48700 65.30500  1.000 15.34876 ? 51  SER   A N     1 
ATOM   1759 C  CA    . SER   B 1 52  ? 100.15400 -31.74700 63.98700  1.000 16.18923 ? 51  SER   A CA    1 
ATOM   1760 C  C     . SER   B 1 52  ? 100.00400 -30.45600 63.20000  1.000 17.49234 ? 51  SER   A C     1 
ATOM   1761 O  O     . SER   B 1 52  ? 99.76300  -29.38900 63.76700  1.000 15.71396 ? 51  SER   A O     1 
ATOM   1762 C  CB    . SER   B 1 52  ? 98.79800  -32.44600 64.07900  1.000 18.23476 ? 51  SER   A CB    1 
ATOM   1763 O  OG    . SER   B 1 52  ? 98.93300  -33.66400 64.78800  1.000 21.48207 ? 51  SER   A OG    1 
ATOM   1764 N  N     . LEU   B 1 53  ? 100.11500 -30.57600 61.88100  1.000 13.69298 ? 52  LEU   A N     1 
ATOM   1765 C  CA    . LEU   B 1 53  ? 99.81400  -29.48300 60.96700  1.000 14.00226 ? 52  LEU   A CA    1 
ATOM   1766 C  C     . LEU   B 1 53  ? 98.40500  -29.67500 60.42200  1.000 12.04284 ? 52  LEU   A C     1 
ATOM   1767 O  O     . LEU   B 1 53  ? 98.10300  -30.71600 59.83000  1.000 11.74364 ? 52  LEU   A O     1 
ATOM   1768 C  CB    . LEU   B 1 53  ? 100.82100 -29.43800 59.82400  1.000 15.70669 ? 52  LEU   A CB    1 
ATOM   1769 C  CG    . LEU   B 1 53  ? 100.80100 -28.09500 59.11600  1.000 25.79399 ? 52  LEU   A CG    1 
ATOM   1770 C  CD1   . LEU   B 1 53  ? 102.11800 -27.39200 59.38200  1.000 31.14858 ? 52  LEU   A CD1   1 
ATOM   1771 C  CD2   . LEU   B 1 53  ? 100.57300 -28.32200 57.64500  1.000 24.77850 ? 52  LEU   A CD2   1 
ATOM   1772 N  N     . LEU   B 1 54  ? 97.54200  -28.69400 60.64800  1.000 11.48781 ? 53  LEU   A N     1 
ATOM   1773 C  CA    . LEU   B 1 54  ? 96.17100  -28.73500 60.15700  1.000 11.00389 ? 53  LEU   A CA    1 
ATOM   1774 C  C     . LEU   B 1 54  ? 96.08300  -27.94800 58.85500  1.000 12.88147 ? 53  LEU   A C     1 
ATOM   1775 O  O     . LEU   B 1 54  ? 96.45300  -26.76900 58.81500  1.000 14.96091 ? 53  LEU   A O     1 
ATOM   1776 C  CB    . LEU   B 1 54  ? 95.20200  -28.17700 61.19600  1.000 10.74997 ? 53  LEU   A CB    1 
ATOM   1777 C  CG    . LEU   B 1 54  ? 95.35200  -28.73300 62.62000  1.000 13.70152 ? 53  LEU   A CG    1 
ATOM   1778 C  CD1   . LEU   B 1 54  ? 94.27800  -28.16300 63.54000  1.000 13.25100 ? 53  LEU   A CD1   1 
ATOM   1779 C  CD2   . LEU   B 1 54  ? 95.35100  -30.26700 62.64100  1.000 10.94479 ? 53  LEU   A CD2   1 
ATOM   1780 N  N     . ASP   B 1 55  ? 95.64600  -28.61500 57.78600  1.000 10.59975 ? 54  ASP   A N     1 
ATOM   1781 C  CA    . ASP   B 1 55  ? 95.36100  -27.96900 56.50900  1.000 11.60642 ? 54  ASP   A CA    1 
ATOM   1782 C  C     . ASP   B 1 55  ? 93.85600  -27.84000 56.45100  1.000 10.44192 ? 54  ASP   A C     1 
ATOM   1783 O  O     . ASP   B 1 55  ? 93.15300  -28.85600 56.41800  1.000 14.72740 ? 54  ASP   A O     1 
ATOM   1784 C  CB    . ASP   B 1 55  ? 95.85200  -28.78200 55.31500  1.000 12.14324 ? 54  ASP   A CB    1 
ATOM   1785 C  CG    . ASP   B 1 55  ? 97.32700  -29.05500 55.35100  1.000 16.31340 ? 54  ASP   A CG    1 
ATOM   1786 O  OD1   . ASP   B 1 55  ? 98.10900  -28.12800 55.61800  1.000 28.48492 ? 54  ASP   A OD1   1 
ATOM   1787 O  OD2   . ASP   B 1 55  ? 97.68800  -30.20700 55.08000  1.000 19.03187 ? 54  ASP   A OD2   1 
ATOM   1788 N  N     . ILE   B 1 56  ? 93.35800  -26.61100 56.46000  1.000 10.35261 ? 55  ILE   A N     1 
ATOM   1789 C  CA    . ILE   B 1 56  ? 91.92300  -26.37200 56.58500  1.000 11.60243 ? 55  ILE   A CA    1 
ATOM   1790 C  C     . ILE   B 1 56  ? 91.39000  -25.82600 55.27400  1.000 9.19049  ? 55  ILE   A C     1 
ATOM   1791 O  O     . ILE   B 1 56  ? 91.83300  -24.77600 54.79600  1.000 9.68403  ? 55  ILE   A O     1 
ATOM   1792 C  CB    . ILE   B 1 56  ? 91.59800  -25.42400 57.74300  1.000 10.63008 ? 55  ILE   A CB    1 
ATOM   1793 C  CG1   . ILE   B 1 56  ? 92.14300  -26.01300 59.03900  1.000 16.46793 ? 55  ILE   A CG1   1 
ATOM   1794 C  CG2   . ILE   B 1 56  ? 90.08200  -25.26100 57.86100  1.000 11.95950 ? 55  ILE   A CG2   1 
ATOM   1795 C  CD1   . ILE   B 1 56  ? 92.30200  -24.98500 60.10200  1.000 21.67402 ? 55  ILE   A CD1   1 
ATOM   1796 N  N     . LEU   B 1 57  ? 90.41400  -26.52900 54.71400  1.000 10.82514 ? 56  LEU   A N     1 
ATOM   1797 C  CA    . LEU   B 1 57  ? 89.70800  -26.07700 53.52400  1.000 9.80964  ? 56  LEU   A CA    1 
ATOM   1798 C  C     . LEU   B 1 57  ? 88.36300  -25.52100 53.97300  1.000 9.93828  ? 56  LEU   A C     1 
ATOM   1799 O  O     . LEU   B 1 57  ? 87.51600  -26.26500 54.48200  1.000 6.79774  ? 56  LEU   A O     1 
ATOM   1800 C  CB    . LEU   B 1 57  ? 89.53500  -27.21600 52.52700  1.000 11.24231 ? 56  LEU   A CB    1 
ATOM   1801 C  CG    . LEU   B 1 57  ? 88.96200  -26.84100 51.16100  1.000 13.99272 ? 56  LEU   A CG    1 
ATOM   1802 C  CD1   . LEU   B 1 57  ? 89.82000  -25.82000 50.45400  1.000 8.46590  ? 56  LEU   A CD1   1 
ATOM   1803 C  CD2   . LEU   B 1 57  ? 88.84700  -28.09800 50.33000  1.000 14.08932 ? 56  LEU   A CD2   1 
ATOM   1804 N  N     . ASP   B 1 58  ? 88.19600  -24.20600 53.79700  1.000 9.01407  ? 57  ASP   A N     1 
ATOM   1805 C  CA    . ASP   B 1 58  ? 86.96400  -23.47700 54.09000  1.000 9.12642  ? 57  ASP   A CA    1 
ATOM   1806 C  C     . ASP   B 1 58  ? 86.16700  -23.39600 52.79700  1.000 11.85292 ? 57  ASP   A C     1 
ATOM   1807 O  O     . ASP   B 1 58  ? 86.52000  -22.61600 51.90000  1.000 10.33572 ? 57  ASP   A O     1 
ATOM   1808 C  CB    . ASP   B 1 58  ? 87.31600  -22.08100 54.61500  1.000 9.13965  ? 57  ASP   A CB    1 
ATOM   1809 C  CG    . ASP   B 1 58  ? 86.10700  -21.27200 55.04000  1.000 9.08039  ? 57  ASP   A CG    1 
ATOM   1810 O  OD1   . ASP   B 1 58  ? 85.03000  -21.85200 55.28700  1.000 9.10106  ? 57  ASP   A OD1   1 
ATOM   1811 O  OD2   . ASP   B 1 58  ? 86.25700  -20.03200 55.12400  1.000 13.11571 ? 57  ASP   A OD2   1 
ATOM   1812 N  N     . THR   B 1 59  ? 85.10700  -24.20400 52.69300  1.000 10.29059 ? 58  THR   A N     1 
ATOM   1813 C  CA    . THR   B 1 59  ? 84.30200  -24.28300 51.48400  1.000 7.38671  ? 58  THR   A CA    1 
ATOM   1814 C  C     . THR   B 1 59  ? 83.11600  -23.33600 51.56100  1.000 7.20699  ? 58  THR   A C     1 
ATOM   1815 O  O     . THR   B 1 59  ? 82.69200  -22.92600 52.63900  1.000 7.14090  ? 58  THR   A O     1 
ATOM   1816 C  CB    . THR   B 1 59  ? 83.78200  -25.71000 51.24400  1.000 9.07904  ? 58  THR   A CB    1 
ATOM   1817 O  OG1   . THR   B 1 59  ? 82.74600  -26.01400 52.18700  1.000 8.14179  ? 58  THR   A OG1   1 
ATOM   1818 C  CG2   . THR   B 1 59  ? 84.92500  -26.73700 51.38100  1.000 9.71989  ? 58  THR   A CG2   1 
ATOM   1819 N  N     . ALA   B 1 60  ? 82.57600  -23.00400 50.39500  1.000 7.63048  ? 59  ALA   A N     1 
ATOM   1820 C  CA    . ALA   B 1 60  ? 81.36200  -22.20100 50.31900  1.000 7.83381  ? 59  ALA   A CA    1 
ATOM   1821 C  C     . ALA   B 1 60  ? 80.13500  -23.08400 50.48500  1.000 9.34782  ? 59  ALA   A C     1 
ATOM   1822 O  O     . ALA   B 1 60  ? 80.10200  -24.22300 50.00700  1.000 12.26984 ? 59  ALA   A O     1 
ATOM   1823 C  CB    . ALA   B 1 60  ? 81.27900  -21.47100 48.98000  1.000 8.51398  ? 59  ALA   A CB    1 
ATOM   1824 N  N     . GLY   B 1 61  ? 79.12700  -22.54700 51.16100  1.000 7.73564  ? 60  GLY   A N     1 
ATOM   1825 C  CA    . GLY   B 1 61  ? 77.82200  -23.17400 51.19900  1.000 8.99813  ? 60  GLY   A CA    1 
ATOM   1826 C  C     . GLY   B 1 61  ? 77.09900  -22.91100 49.90000  1.000 11.48907 ? 60  GLY   A C     1 
ATOM   1827 O  O     . GLY   B 1 61  ? 76.50900  -21.84900 49.72500  1.000 12.16990 ? 60  GLY   A O     1 
ATOM   1828 N  N     . GLN   B 1 62  ? 77.19000  -23.85100 48.96100  1.000 12.84273 ? 61  GLN   A N     1 
ATOM   1829 C  CA    . GLN   B 1 62  ? 76.55900  -23.73100 47.65300  1.000 14.07659 ? 61  GLN   A CA    1 
ATOM   1830 C  C     . GLN   B 1 62  ? 76.23500  -25.13300 47.17400  1.000 18.28354 ? 61  GLN   A C     1 
ATOM   1831 O  O     . GLN   B 1 62  ? 76.89000  -26.09800 47.57300  1.000 16.92055 ? 61  GLN   A O     1 
ATOM   1832 C  CB    . GLN   B 1 62  ? 77.45900  -23.01100 46.62900  1.000 15.43084 ? 61  GLN   A CB    1 
ATOM   1833 C  CG    . GLN   B 1 62  ? 78.88300  -23.60000 46.46100  1.000 13.28301 ? 61  GLN   A CG    1 
ATOM   1834 C  CD    . GLN   B 1 62  ? 78.95500  -24.81800 45.54600  1.000 19.55465 ? 61  GLN   A CD    1 
ATOM   1835 O  OE1   . GLN   B 1 62  ? 78.04500  -25.07300 44.74800  1.000 20.46972 ? 61  GLN   A OE1   1 
ATOM   1836 N  NE2   . GLN   B 1 62  ? 80.04300  -25.57700 45.65600  1.000 15.37083 ? 61  GLN   A NE2   1 
ATOM   1837 N  N     . GLU   B 1 63  ? 75.24100  -25.23900 46.29800  1.000 23.49006 ? 62  GLU   A N     1 
ATOM   1838 C  CA    . GLU   B 1 63  ? 74.82700  -26.53300 45.76700  1.000 25.52649 ? 62  GLU   A CA    1 
ATOM   1839 C  C     . GLU   B 1 63  ? 74.73200  -26.49900 44.25100  1.000 28.70176 ? 62  GLU   A C     1 
ATOM   1840 O  O     . GLU   B 1 63  ? 73.87200  -27.14600 43.64500  1.000 29.51395 ? 62  GLU   A O     1 
ATOM   1841 C  CB    . GLU   B 1 63  ? 73.50600  -26.96900 46.39300  1.000 29.80820 ? 62  GLU   A CB    1 
ATOM   1842 C  CG    . GLU   B 1 63  ? 73.59900  -27.13600 47.90700  1.000 27.59875 ? 62  GLU   A CG    1 
ATOM   1843 C  CD    . GLU   B 1 63  ? 72.25800  -27.44700 48.54300  1.000 41.12316 ? 62  GLU   A CD    1 
ATOM   1844 O  OE1   . GLU   B 1 63  ? 71.24400  -27.47900 47.81000  1.000 46.32452 ? 62  GLU   A OE1   1 
ATOM   1845 O  OE2   . GLU   B 1 63  ? 72.21800  -27.66200 49.77300  1.000 41.43576 ? 62  GLU   A OE2   1 
ATOM   1846 N  N     . GLU   B 1 64  ? 75.61800  -25.74000 43.60700  1.000 19.17976 ? 63  GLU   A N     1 
ATOM   1847 C  CA    . GLU   B 1 64  ? 75.63300  -25.64100 42.15500  1.000 21.63110 ? 63  GLU   A CA    1 
ATOM   1848 C  C     . GLU   B 1 64  ? 76.85800  -26.26900 41.50500  1.000 23.49418 ? 63  GLU   A C     1 
ATOM   1849 O  O     . GLU   B 1 64  ? 76.85300  -26.45800 40.28300  1.000 22.73948 ? 63  GLU   A O     1 
ATOM   1850 C  CB    . GLU   B 1 64  ? 75.55100  -24.17500 41.70700  1.000 18.22593 ? 63  GLU   A CB    1 
ATOM   1851 C  CG    . GLU   B 1 64  ? 74.17600  -23.53600 41.81800  1.000 29.24660 ? 63  GLU   A CG    1 
ATOM   1852 C  CD    . GLU   B 1 64  ? 73.94100  -22.86900 43.16000  1.000 36.06737 ? 63  GLU   A CD    1 
ATOM   1853 O  OE1   . GLU   B 1 64  ? 73.99500  -23.55400 44.21000  1.000 38.21408 ? 63  GLU   A OE1   1 
ATOM   1854 O  OE2   . GLU   B 1 64  ? 73.70300  -21.64400 43.16000  1.000 39.70290 ? 63  GLU   A OE2   1 
ATOM   1855 N  N     . TYR   B 1 65  ? 77.91400  -26.58900 42.27600  1.000 20.17059 ? 64  TYR   A N     1 
ATOM   1856 C  CA    . TYR   B 1 65  ? 79.19700  -26.99500 41.70000  1.000 19.39280 ? 64  TYR   A CA    1 
ATOM   1857 C  C     . TYR   B 1 65  ? 79.60700  -28.34500 42.30400  1.000 19.99527 ? 64  TYR   A C     1 
ATOM   1858 O  O     . TYR   B 1 65  ? 80.43900  -28.41600 43.20700  1.000 15.43583 ? 64  TYR   A O     1 
ATOM   1859 C  CB    . TYR   B 1 65  ? 80.26100  -25.89400 41.91200  1.000 16.12136 ? 64  TYR   A CB    1 
ATOM   1860 C  CG    . TYR   B 1 65  ? 79.83600  -24.59700 41.24800  1.000 15.08749 ? 64  TYR   A CG    1 
ATOM   1861 C  CD1   . TYR   B 1 65  ? 79.87300  -24.46700 39.87300  1.000 14.35713 ? 64  TYR   A CD1   1 
ATOM   1862 C  CD2   . TYR   B 1 65  ? 79.37900  -23.51900 41.99700  1.000 15.38438 ? 64  TYR   A CD2   1 
ATOM   1863 C  CE1   . TYR   B 1 65  ? 79.45500  -23.29900 39.24700  1.000 17.94007 ? 64  TYR   A CE1   1 
ATOM   1864 C  CE2   . TYR   B 1 65  ? 78.97300  -22.33900 41.38100  1.000 13.37727 ? 64  TYR   A CE2   1 
ATOM   1865 C  CZ    . TYR   B 1 65  ? 79.01400  -22.24400 40.00600  1.000 14.56154 ? 64  TYR   A CZ    1 
ATOM   1866 O  OH    . TYR   B 1 65  ? 78.61000  -21.10300 39.37500  1.000 15.39227 ? 64  TYR   A OH    1 
ATOM   1867 N  N     . SER   B 1 66  ? 79.03600  -29.42200 41.75700  1.000 16.45560 ? 65  SER   A N     1 
ATOM   1868 C  CA    . SER   B 1 66  ? 79.18700  -30.74100 42.35000  1.000 17.32050 ? 65  SER   A CA    1 
ATOM   1869 C  C     . SER   B 1 66  ? 80.54300  -31.36900 42.04500  1.000 13.58861 ? 65  SER   A C     1 
ATOM   1870 O  O     . SER   B 1 66  ? 81.04900  -32.14100 42.86300  1.000 18.78106 ? 65  SER   A O     1 
ATOM   1871 C  CB    . SER   B 1 66  ? 78.05800  -31.64700 41.86800  1.000 18.69510 ? 65  SER   A CB    1 
ATOM   1872 O  OG    . SER   B 1 66  ? 78.07800  -31.75000 40.45700  1.000 28.22482 ? 65  SER   A OG    1 
ATOM   1873 N  N     . ALA   B 1 67  ? 81.14700  -31.06600 40.89300  1.000 14.52885 ? 66  ALA   A N     1 
ATOM   1874 C  CA    . ALA   B 1 67  ? 82.46300  -31.62600 40.59000  1.000 16.28105 ? 66  ALA   A CA    1 
ATOM   1875 C  C     . ALA   B 1 67  ? 83.53700  -31.06300 41.51700  1.000 16.69927 ? 66  ALA   A C     1 
ATOM   1876 O  O     . ALA   B 1 67  ? 84.45800  -31.78400 41.92800  1.000 16.73694 ? 66  ALA   A O     1 
ATOM   1877 C  CB    . ALA   B 1 67  ? 82.82300  -31.36400 39.12800  1.000 21.71013 ? 66  ALA   A CB    1 
ATOM   1878 N  N     . MET   B 1 68  ? 83.43700  -29.77800 41.86200  1.000 18.48446 ? 67  MET   A N     1 
ATOM   1879 C  CA    . MET   B 1 68  ? 84.36500  -29.19700 42.83100  1.000 13.55973 ? 67  MET   A CA    1 
ATOM   1880 C  C     . MET   B 1 68  ? 84.10600  -29.74400 44.22300  1.000 11.76103 ? 67  MET   A C     1 
ATOM   1881 O  O     . MET   B 1 68  ? 85.04200  -30.12900 44.93900  1.000 12.06549 ? 67  MET   A O     1 
ATOM   1882 C  CB    . MET   B 1 68  ? 84.24300  -27.67100 42.82600  1.000 11.67843 ? 67  MET   A CB    1 
ATOM   1883 C  CG    . MET   B 1 68  ? 84.90200  -27.01800 41.61900  1.000 16.35387 ? 67  MET   A CG    1 
ATOM   1884 S  SD    . MET   B 1 68  ? 86.70000  -27.09800 41.68100  1.000 27.42947 ? 67  MET   A SD    1 
ATOM   1885 C  CE    . MET   B 1 68  ? 87.05900  -26.17000 43.15600  1.000 24.33078 ? 67  MET   A CE    1 
ATOM   1886 N  N     . ARG   B 1 69  ? 82.83800  -29.75700 44.63300  1.000 10.73038 ? 68  ARG   A N     1 
ATOM   1887 C  CA    . ARG   B 1 69  ? 82.44800  -30.36400 45.89700  1.000 11.47202 ? 68  ARG   A CA    1 
ATOM   1888 C  C     . ARG   B 1 69  ? 82.98800  -31.78300 46.00100  1.000 10.36265 ? 68  ARG   A C     1 
ATOM   1889 O  O     . ARG   B 1 69  ? 83.55000  -32.17200 47.02900  1.000 11.14803 ? 68  ARG   A O     1 
ATOM   1890 C  CB    . ARG   B 1 69  ? 80.92200  -30.35600 46.01600  1.000 12.39035 ? 68  ARG   A CB    1 
ATOM   1891 C  CG    . ARG   B 1 69  ? 80.35700  -31.15100 47.18200  1.000 18.19791 ? 68  ARG   A CG    1 
ATOM   1892 C  CD    . ARG   B 1 69  ? 78.92100  -31.61800 46.90700  1.000 20.33978 ? 68  ARG   A CD    1 
ATOM   1893 N  NE    . ARG   B 1 69  ? 78.86800  -32.61800 45.84100  1.000 20.49042 ? 68  ARG   A NE    1 
ATOM   1894 C  CZ    . ARG   B 1 69  ? 77.74900  -33.09500 45.31600  1.000 26.87229 ? 68  ARG   A CZ    1 
ATOM   1895 N  NH1   . ARG   B 1 69  ? 76.56000  -32.68300 45.72900  1.000 25.08640 ? 68  ARG   A NH1   1 
ATOM   1896 N  NH2   . ARG   B 1 69  ? 77.82300  -34.00100 44.34100  1.000 28.26306 ? 68  ARG   A NH2   1 
ATOM   1897 N  N     . ASP   B 1 70  ? 82.81800  -32.56800 44.92900  1.000 11.32497 ? 69  ASP   A N     1 
ATOM   1898 C  CA    . ASP   B 1 70  ? 83.26900  -33.95800 44.93000  1.000 12.26799 ? 69  ASP   A CA    1 
ATOM   1899 C  C     . ASP   B 1 70  ? 84.77500  -34.04300 45.12800  1.000 11.64691 ? 69  ASP   A C     1 
ATOM   1900 O  O     . ASP   B 1 70  ? 85.26500  -34.91200 45.85600  1.000 11.54932 ? 69  ASP   A O     1 
ATOM   1901 C  CB    . ASP   B 1 70  ? 82.87700  -34.65400 43.62300  1.000 13.10184 ? 69  ASP   A CB    1 
ATOM   1902 C  CG    . ASP   B 1 70  ? 81.41800  -35.10100 43.60200  1.000 17.70634 ? 69  ASP   A CG    1 
ATOM   1903 O  OD1   . ASP   B 1 70  ? 80.71600  -34.90700 44.60900  1.000 13.40043 ? 69  ASP   A OD1   1 
ATOM   1904 O  OD2   . ASP   B 1 70  ? 80.98200  -35.65000 42.56800  1.000 19.30113 ? 69  ASP   A OD2   1 
ATOM   1905 N  N     . GLN   B 1 71  ? 85.52700  -33.14400 44.49900  1.000 11.73156 ? 70  GLN   A N     1 
ATOM   1906 C  CA    . GLN   B 1 71  ? 86.97400  -33.21800 44.66600  1.000 12.57551 ? 70  GLN   A CA    1 
ATOM   1907 C  C     . GLN   B 1 71  ? 87.37500  -32.81200 46.07500  1.000 10.75210 ? 70  GLN   A C     1 
ATOM   1908 O  O     . GLN   B 1 71  ? 88.31900  -33.38000 46.63100  1.000 11.68092 ? 70  GLN   A O     1 
ATOM   1909 C  CB    . GLN   B 1 71  ? 87.69800  -32.37600 43.62100  1.000 17.10766 ? 70  GLN   A CB    1 
ATOM   1910 C  CG    . GLN   B 1 71  ? 89.23500  -32.51600 43.71700  1.000 18.03779 ? 70  GLN   A CG    1 
ATOM   1911 C  CD    . GLN   B 1 71  ? 89.72800  -33.96000 43.55900  1.000 19.68159 ? 70  GLN   A CD    1 
ATOM   1912 O  OE1   . GLN   B 1 71  ? 89.35000  -34.66200 42.61900  1.000 19.40162 ? 70  GLN   A OE1   1 
ATOM   1913 N  NE2   . GLN   B 1 71  ? 90.56600  -34.41100 44.49400  1.000 20.36216 ? 70  GLN   A NE2   1 
ATOM   1914 N  N     . TYR   B 1 72  ? 86.65200  -31.85400 46.68200  1.000 10.02937 ? 71  TYR   A N     1 
ATOM   1915 C  CA    . TYR   B 1 72  ? 86.88400  -31.53400 48.09000  1.000 11.94269 ? 71  TYR   A CA    1 
ATOM   1916 C  C     . TYR   B 1 72  ? 86.73700  -32.78000 48.94700  1.000 11.08111 ? 71  TYR   A C     1 
ATOM   1917 O  O     . TYR   B 1 72  ? 87.55000  -33.04300 49.83800  1.000 10.98180 ? 71  TYR   A O     1 
ATOM   1918 C  CB    . TYR   B 1 72  ? 85.89400  -30.48200 48.59400  1.000 12.33711 ? 71  TYR   A CB    1 
ATOM   1919 C  CG    . TYR   B 1 72  ? 85.95200  -29.11700 47.94400  1.000 9.12919  ? 71  TYR   A CG    1 
ATOM   1920 C  CD1   . TYR   B 1 72  ? 87.13100  -28.62100 47.38600  1.000 9.90114  ? 71  TYR   A CD1   1 
ATOM   1921 C  CD2   . TYR   B 1 72  ? 84.82600  -28.30100 47.92700  1.000 8.78152  ? 71  TYR   A CD2   1 
ATOM   1922 C  CE1   . TYR   B 1 72  ? 87.17200  -27.34600 46.80400  1.000 10.47919 ? 71  TYR   A CE1   1 
ATOM   1923 C  CE2   . TYR   B 1 72  ? 84.86000  -27.04200 47.35700  1.000 11.80230 ? 71  TYR   A CE2   1 
ATOM   1924 C  CZ    . TYR   B 1 72  ? 86.02800  -26.56300 46.79700  1.000 14.58618 ? 71  TYR   A CZ    1 
ATOM   1925 O  OH    . TYR   B 1 72  ? 86.03400  -25.29300 46.22700  1.000 11.46324 ? 71  TYR   A OH    1 
ATOM   1926 N  N     . MET   B 1 73  ? 85.68800  -33.55100 48.69800  1.000 9.44410  ? 72  MET   A N     1 
ATOM   1927 C  CA    . MET   B 1 73  ? 85.41600  -34.70400 49.53200  1.000 10.71597 ? 72  MET   A CA    1 
ATOM   1928 C  C     . MET   B 1 73  ? 86.39900  -35.84200 49.27200  1.000 14.32602 ? 72  MET   A C     1 
ATOM   1929 O  O     . MET   B 1 73  ? 86.71100  -36.60900 50.19200  1.000 13.48243 ? 72  MET   A O     1 
ATOM   1930 C  CB    . MET   B 1 73  ? 83.95700  -35.11800 49.31400  1.000 10.17445 ? 72  MET   A CB    1 
ATOM   1931 C  CG    . MET   B 1 73  ? 82.98700  -34.03400 49.77100  1.000 9.52810  ? 72  MET   A CG    1 
ATOM   1932 S  SD    . MET   B 1 73  ? 81.25300  -34.43600 49.42800  1.000 15.23445 ? 72  MET   A SD    1 
ATOM   1933 C  CE    . MET   B 1 73  ? 80.40500  -33.04100 50.17700  1.000 13.64618 ? 72  MET   A CE    1 
ATOM   1934 N  N     . ARG   B 1 74  ? 86.92900  -35.95900 48.05200  1.000 14.32591 ? 73  ARG   A N     1 
ATOM   1935 C  CA    . ARG   B 1 74  ? 87.88500  -37.03200 47.79700  1.000 15.25755 ? 73  ARG   A CA    1 
ATOM   1936 C  C     . ARG   B 1 74  ? 89.18700  -36.79400 48.54500  1.000 17.25820 ? 73  ARG   A C     1 
ATOM   1937 O  O     . ARG   B 1 74  ? 89.78100  -37.74200 49.07000  1.000 19.57157 ? 73  ARG   A O     1 
ATOM   1938 C  CB    . ARG   B 1 74  ? 88.15200  -37.18700 46.29500  1.000 15.67821 ? 73  ARG   A CB    1 
ATOM   1939 C  CG    . ARG   B 1 74  ? 87.28700  -38.24700 45.63500  1.000 21.03088 ? 73  ARG   A CG    1 
ATOM   1940 C  CD    . ARG   B 1 74  ? 87.68200  -38.54000 44.19100  1.000 24.57100 ? 73  ARG   A CD    1 
ATOM   1941 N  NE    . ARG   B 1 74  ? 87.70100  -37.33800 43.37000  1.000 19.97144 ? 73  ARG   A NE    1 
ATOM   1942 C  CZ    . ARG   B 1 74  ? 86.68300  -36.89300 42.64500  1.000 19.73834 ? 73  ARG   A CZ    1 
ATOM   1943 N  NH1   . ARG   B 1 74  ? 85.51500  -37.52000 42.62700  1.000 20.93914 ? 73  ARG   A NH1   1 
ATOM   1944 N  NH2   . ARG   B 1 74  ? 86.84000  -35.78800 41.92200  1.000 19.58257 ? 73  ARG   A NH2   1 
ATOM   1945 N  N     . THR   B 1 75  ? 89.62400  -35.53000 48.62800  1.000 10.77980 ? 74  THR   A N     1 
ATOM   1946 C  CA    . THR   B 1 75  ? 90.90700  -35.17400 49.22400  1.000 11.89170 ? 74  THR   A CA    1 
ATOM   1947 C  C     . THR   B 1 75  ? 90.82000  -35.04400 50.74000  1.000 14.21465 ? 74  THR   A C     1 
ATOM   1948 O  O     . THR   B 1 75  ? 91.81100  -35.28000 51.44100  1.000 11.73733 ? 74  THR   A O     1 
ATOM   1949 C  CB    . THR   B 1 75  ? 91.39300  -33.86000 48.60700  1.000 15.23402 ? 74  THR   A CB    1 
ATOM   1950 O  OG1   . THR   B 1 75  ? 91.56200  -34.03400 47.19800  1.000 24.43306 ? 74  THR   A OG1   1 
ATOM   1951 C  CG2   . THR   B 1 75  ? 92.70000  -33.41700 49.21000  1.000 19.23874 ? 74  THR   A CG2   1 
ATOM   1952 N  N     . GLY   B 1 76  ? 89.65000  -34.69400 51.25900  1.000 10.30708 ? 75  GLY   A N     1 
ATOM   1953 C  CA    . GLY   B 1 76  ? 89.52800  -34.43900 52.67900  1.000 8.83231  ? 75  GLY   A CA    1 
ATOM   1954 C  C     . GLY   B 1 76  ? 89.67500  -35.71700 53.48300  1.000 10.75743 ? 75  GLY   A C     1 
ATOM   1955 O  O     . GLY   B 1 76  ? 89.19100  -36.78300 53.09900  1.000 11.27796 ? 75  GLY   A O     1 
ATOM   1956 N  N     . GLU   B 1 77  ? 90.35600  -35.60400 54.61800  1.000 10.44284 ? 76  GLU   A N     1 
ATOM   1957 C  CA    . GLU   B 1 77  ? 90.45500  -36.71200 55.56000  1.000 10.46324 ? 76  GLU   A CA    1 
ATOM   1958 C  C     . GLU   B 1 77  ? 89.41000  -36.65900 56.66000  1.000 12.92177 ? 76  GLU   A C     1 
ATOM   1959 O  O     . GLU   B 1 77  ? 89.07500  -37.70400 57.23200  1.000 10.44540 ? 76  GLU   A O     1 
ATOM   1960 C  CB    . GLU   B 1 77  ? 91.83500  -36.72200 56.21700  1.000 12.97960 ? 76  GLU   A CB    1 
ATOM   1961 C  CG    . GLU   B 1 77  ? 92.98200  -36.90800 55.25800  1.000 16.83814 ? 76  GLU   A CG    1 
ATOM   1962 C  CD    . GLU   B 1 77  ? 94.31300  -36.80100 55.96900  1.000 21.76985 ? 76  GLU   A CD    1 
ATOM   1963 O  OE1   . GLU   B 1 77  ? 94.66600  -37.74300 56.72200  1.000 21.99657 ? 76  GLU   A OE1   1 
ATOM   1964 O  OE2   . GLU   B 1 77  ? 94.98600  -35.76600 55.78700  1.000 16.56540 ? 76  GLU   A OE2   1 
ATOM   1965 N  N     . GLY   B 1 78  ? 88.94100  -35.46500 57.00300  1.000 10.42166 ? 77  GLY   A N     1 
ATOM   1966 C  CA    . GLY   B 1 78  ? 87.93400  -35.30400 58.04100  1.000 8.45450  ? 77  GLY   A CA    1 
ATOM   1967 C  C     . GLY   B 1 78  ? 87.06900  -34.12300 57.67500  1.000 10.02724 ? 77  GLY   A C     1 
ATOM   1968 O  O     . GLY   B 1 78  ? 87.50900  -33.21600 56.96400  1.000 8.96436  ? 77  GLY   A O     1 
ATOM   1969 N  N     . PHE   B 1 79  ? 85.83300  -34.12500 58.16700  1.000 8.12317  ? 78  PHE   A N     1 
ATOM   1970 C  CA    . PHE   B 1 79  ? 84.87300  -33.09800 57.77400  1.000 10.60767 ? 78  PHE   A CA    1 
ATOM   1971 C  C     . PHE   B 1 79  ? 84.13800  -32.54200 58.98200  1.000 11.49235 ? 78  PHE   A C     1 
ATOM   1972 O  O     . PHE   B 1 79  ? 83.59100  -33.31300 59.77800  1.000 7.25524  ? 78  PHE   A O     1 
ATOM   1973 C  CB    . PHE   B 1 79  ? 83.86000  -33.66200 56.76700  1.000 7.58269  ? 78  PHE   A CB    1 
ATOM   1974 C  CG    . PHE   B 1 79  ? 84.49200  -34.17900 55.53000  1.000 14.41098 ? 78  PHE   A CG    1 
ATOM   1975 C  CD1   . PHE   B 1 79  ? 84.98800  -35.47700 55.48100  1.000 12.13643 ? 78  PHE   A CD1   1 
ATOM   1976 C  CD2   . PHE   B 1 79  ? 84.62900  -33.36400 54.41100  1.000 9.84641  ? 78  PHE   A CD2   1 
ATOM   1977 C  CE1   . PHE   B 1 79  ? 85.60200  -35.95100 54.33700  1.000 12.71795 ? 78  PHE   A CE1   1 
ATOM   1978 C  CE2   . PHE   B 1 79  ? 85.22100  -33.84300 53.27200  1.000 9.81995  ? 78  PHE   A CE2   1 
ATOM   1979 C  CZ    . PHE   B 1 79  ? 85.72800  -35.12300 53.23900  1.000 13.57862 ? 78  PHE   A CZ    1 
ATOM   1980 N  N     . LEU   B 1 80  ? 84.10200  -31.20700 59.10000  1.000 11.52768 ? 79  LEU   A N     1 
ATOM   1981 C  CA    . LEU   B 1 80  ? 83.20000  -30.53400 60.03300  1.000 9.25401  ? 79  LEU   A CA    1 
ATOM   1982 C  C     . LEU   B 1 80  ? 81.90100  -30.24200 59.29900  1.000 8.77830  ? 79  LEU   A C     1 
ATOM   1983 O  O     . LEU   B 1 80  ? 81.91000  -29.51200 58.30300  1.000 10.17008 ? 79  LEU   A O     1 
ATOM   1984 C  CB    . LEU   B 1 80  ? 83.79000  -29.22100 60.55900  1.000 8.11375  ? 79  LEU   A CB    1 
ATOM   1985 C  CG    . LEU   B 1 80  ? 84.96500  -29.18600 61.52500  1.000 12.85369 ? 79  LEU   A CG    1 
ATOM   1986 C  CD1   . LEU   B 1 80  ? 85.15300  -27.75000 61.98100  1.000 11.23405 ? 79  LEU   A CD1   1 
ATOM   1987 C  CD2   . LEU   B 1 80  ? 84.75200  -30.11100 62.72600  1.000 16.50818 ? 79  LEU   A CD2   1 
ATOM   1988 N  N     . LEU   B 1 81  ? 80.79700  -30.83300 59.77200  1.000 9.41788  ? 80  LEU   A N     1 
ATOM   1989 C  CA    . LEU   B 1 81  ? 79.46400  -30.60000 59.22600  1.000 9.65819  ? 80  LEU   A CA    1 
ATOM   1990 C  C     . LEU   B 1 81  ? 78.81800  -29.51900 60.09200  1.000 7.62913  ? 80  LEU   A C     1 
ATOM   1991 O  O     . LEU   B 1 81  ? 78.38500  -29.79700 61.21300  1.000 9.32472  ? 80  LEU   A O     1 
ATOM   1992 C  CB    . LEU   B 1 81  ? 78.63800  -31.88700 59.24000  1.000 11.43323 ? 80  LEU   A CB    1 
ATOM   1993 C  CG    . LEU   B 1 81  ? 79.24000  -33.20900 58.74300  1.000 13.31878 ? 80  LEU   A CG    1 
ATOM   1994 C  CD1   . LEU   B 1 81  ? 78.18600  -34.35400 58.71200  1.000 9.23485  ? 80  LEU   A CD1   1 
ATOM   1995 C  CD2   . LEU   B 1 81  ? 79.87700  -33.04600 57.37300  1.000 12.06576 ? 80  LEU   A CD2   1 
ATOM   1996 N  N     . VAL   B 1 82  ? 78.77000  -28.28300 59.59000  1.000 6.74904  ? 81  VAL   A N     1 
ATOM   1997 C  CA    . VAL   B 1 82  ? 78.33000  -27.14100 60.38900  1.000 9.39877  ? 81  VAL   A CA    1 
ATOM   1998 C  C     . VAL   B 1 82  ? 76.89400  -26.79400 60.03400  1.000 7.26477  ? 81  VAL   A C     1 
ATOM   1999 O  O     . VAL   B 1 82  ? 76.54800  -26.70600 58.85300  1.000 7.16855  ? 81  VAL   A O     1 
ATOM   2000 C  CB    . VAL   B 1 82  ? 79.23600  -25.91800 60.17700  1.000 6.59606  ? 81  VAL   A CB    1 
ATOM   2001 C  CG1   . VAL   B 1 82  ? 78.95700  -24.85200 61.24600  1.000 7.37919  ? 81  VAL   A CG1   1 
ATOM   2002 C  CG2   . VAL   B 1 82  ? 80.70100  -26.32000 60.19900  1.000 7.20043  ? 81  VAL   A CG2   1 
ATOM   2003 N  N     . PHE   B 1 83  ? 76.05700  -26.61500 61.05400  1.000 7.57790  ? 82  PHE   A N     1 
ATOM   2004 C  CA    . PHE   B 1 83  ? 74.76900  -25.93000 60.91600  1.000 10.18454 ? 82  PHE   A CA    1 
ATOM   2005 C  C     . PHE   B 1 83  ? 74.69600  -24.81700 61.95400  1.000 8.23525  ? 82  PHE   A C     1 
ATOM   2006 O  O     . PHE   B 1 83  ? 75.51200  -24.75600 62.87800  1.000 9.40725  ? 82  PHE   A O     1 
ATOM   2007 C  CB    . PHE   B 1 83  ? 73.56900  -26.87800 61.08600  1.000 8.62201  ? 82  PHE   A CB    1 
ATOM   2008 C  CG    . PHE   B 1 83  ? 73.38600  -27.40300 62.50000  1.000 11.28212 ? 82  PHE   A CG    1 
ATOM   2009 C  CD1   . PHE   B 1 83  ? 74.08100  -28.53500 62.92900  1.000 9.02806  ? 82  PHE   A CD1   1 
ATOM   2010 C  CD2   . PHE   B 1 83  ? 72.51400  -26.78500 63.39200  1.000 11.40605 ? 82  PHE   A CD2   1 
ATOM   2011 C  CE1   . PHE   B 1 83  ? 73.92300  -29.03400 64.21100  1.000 9.51914  ? 82  PHE   A CE1   1 
ATOM   2012 C  CE2   . PHE   B 1 83  ? 72.35100  -27.28000 64.68700  1.000 11.26674 ? 82  PHE   A CE2   1 
ATOM   2013 C  CZ    . PHE   B 1 83  ? 73.05800  -28.41300 65.09500  1.000 10.13530 ? 82  PHE   A CZ    1 
ATOM   2014 N  N     . ALA   B 1 84  ? 73.71300  -23.93200 61.79200  1.000 10.66573 ? 83  ALA   A N     1 
ATOM   2015 C  CA    . ALA   B 1 84  ? 73.47900  -22.85000 62.73800  1.000 10.45646 ? 83  ALA   A CA    1 
ATOM   2016 C  C     . ALA   B 1 84  ? 72.25200  -23.17000 63.57300  1.000 11.61960 ? 83  ALA   A C     1 
ATOM   2017 O  O     . ALA   B 1 84  ? 71.22400  -23.60300 63.04100  1.000 10.20479 ? 83  ALA   A O     1 
ATOM   2018 C  CB    . ALA   B 1 84  ? 73.28900  -21.50900 62.02400  1.000 11.57312 ? 83  ALA   A CB    1 
ATOM   2019 N  N     . ILE   B 1 85  ? 72.35600  -22.94100 64.88600  1.000 12.33730 ? 84  ILE   A N     1 
ATOM   2020 C  CA    . ILE   B 1 85  ? 71.26200  -23.32400 65.77000  1.000 11.14510 ? 84  ILE   A CA    1 
ATOM   2021 C  C     . ILE   B 1 85  ? 70.01900  -22.48000 65.51700  1.000 12.70388 ? 84  ILE   A C     1 
ATOM   2022 O  O     . ILE   B 1 85  ? 68.92000  -22.87200 65.92400  1.000 14.31592 ? 84  ILE   A O     1 
ATOM   2023 C  CB    . ILE   B 1 85  ? 71.68200  -23.25000 67.25500  1.000 12.21831 ? 84  ILE   A CB    1 
ATOM   2024 C  CG1   . ILE   B 1 85  ? 72.11600  -21.84000 67.63100  1.000 11.77455 ? 84  ILE   A CG1   1 
ATOM   2025 C  CG2   . ILE   B 1 85  ? 72.78700  -24.26100 67.56600  1.000 13.76370 ? 84  ILE   A CG2   1 
ATOM   2026 C  CD1   . ILE   B 1 85  ? 71.59700  -21.39200 68.99200  1.000 15.99243 ? 84  ILE   A CD1   1 
ATOM   2027 N  N     . ASN   B 1 86  ? 70.15100  -21.34800 64.82100  1.000 11.65531 ? 85  ASN   A N     1 
ATOM   2028 C  CA    . ASN   B 1 86  ? 69.00900  -20.50600 64.48400  1.000 13.45213 ? 85  ASN   A CA    1 
ATOM   2029 C  C     . ASN   B 1 86  ? 68.61600  -20.61400 63.01100  1.000 15.04914 ? 85  ASN   A C     1 
ATOM   2030 O  O     . ASN   B 1 86  ? 67.98300  -19.69600 62.47400  1.000 14.96433 ? 85  ASN   A O     1 
ATOM   2031 C  CB    . ASN   B 1 86  ? 69.29700  -19.04500 64.84500  1.000 16.41999 ? 85  ASN   A CB    1 
ATOM   2032 C  CG    . ASN   B 1 86  ? 70.38100  -18.42500 63.97900  1.000 17.06206 ? 85  ASN   A CG    1 
ATOM   2033 O  OD1   . ASN   B 1 86  ? 71.16000  -19.12600 63.31500  1.000 16.19270 ? 85  ASN   A OD1   1 
ATOM   2034 N  ND2   . ASN   B 1 86  ? 70.46400  -17.10300 64.01100  1.000 15.54596 ? 85  ASN   A ND2   1 
ATOM   2035 N  N     . ASN   B 1 87  ? 68.99400  -21.71600 62.34200  1.000 12.24678 ? 86  ASN   A N     1 
ATOM   2036 C  CA    . ASN   B 1 87  ? 68.74300  -21.91300 60.91200  1.000 11.40167 ? 86  ASN   A CA    1 
ATOM   2037 C  C     . ASN   B 1 87  ? 68.27600  -23.35000 60.72600  1.000 11.58342 ? 86  ASN   A C     1 
ATOM   2038 O  O     . ASN   B 1 87  ? 69.09400  -24.25900 60.56000  1.000 11.81904 ? 86  ASN   A O     1 
ATOM   2039 C  CB    . ASN   B 1 87  ? 69.99100  -21.61800 60.09000  1.000 12.35729 ? 86  ASN   A CB    1 
ATOM   2040 C  CG    . ASN   B 1 87  ? 69.77700  -21.78100 58.59000  1.000 10.72522 ? 86  ASN   A CG    1 
ATOM   2041 O  OD1   . ASN   B 1 87  ? 68.82200  -22.40900 58.13600  1.000 13.72617 ? 86  ASN   A OD1   1 
ATOM   2042 N  ND2   . ASN   B 1 87  ? 70.69200  -21.22900 57.81300  1.000 14.69333 ? 86  ASN   A ND2   1 
ATOM   2043 N  N     . THR   B 1 88  ? 66.95500  -23.54800 60.73700  1.000 13.01196 ? 87  THR   A N     1 
ATOM   2044 C  CA    . THR   B 1 88  ? 66.42800  -24.90800 60.64300  1.000 12.99978 ? 87  THR   A CA    1 
ATOM   2045 C  C     . THR   B 1 88  ? 66.83700  -25.56800 59.33500  1.000 12.71695 ? 87  THR   A C     1 
ATOM   2046 O  O     . THR   B 1 88  ? 67.18600  -26.75500 59.31000  1.000 15.17834 ? 87  THR   A O     1 
ATOM   2047 C  CB    . THR   B 1 88  ? 64.90400  -24.88500 60.79800  1.000 18.25092 ? 87  THR   A CB    1 
ATOM   2048 O  OG1   . THR   B 1 88  ? 64.58300  -24.53500 62.15100  1.000 16.01863 ? 87  THR   A OG1   1 
ATOM   2049 C  CG2   . THR   B 1 88  ? 64.28500  -26.25000 60.47800  1.000 23.19082 ? 87  THR   A CG2   1 
ATOM   2050 N  N     . LYS   B 1 89  ? 66.83300  -24.81200 58.23800  1.000 13.04608 ? 88  LYS   A N     1 
ATOM   2051 C  CA    . LYS   B 1 89  ? 67.16700  -25.41400 56.95600  1.000 13.48730 ? 88  LYS   A CA    1 
ATOM   2052 C  C     . LYS   B 1 89  ? 68.59500  -25.94700 56.95400  1.000 16.68103 ? 88  LYS   A C     1 
ATOM   2053 O  O     . LYS   B 1 89  ? 68.85600  -27.03800 56.43100  1.000 16.33466 ? 88  LYS   A O     1 
ATOM   2054 C  CB    . LYS   B 1 89  ? 66.96400  -24.40300 55.83200  1.000 17.73534 ? 88  LYS   A CB    1 
ATOM   2055 C  CG    . LYS   B 1 89  ? 66.98800  -25.03200 54.44900  1.000 21.99778 ? 88  LYS   A CG    1 
ATOM   2056 C  CD    . LYS   B 1 89  ? 68.18000  -24.52900 53.66300  1.000 25.56549 ? 88  LYS   A CD    1 
ATOM   2057 C  CE    . LYS   B 1 89  ? 68.35400  -25.29300 52.35000  1.000 26.86760 ? 88  LYS   A CE    1 
ATOM   2058 N  NZ    . LYS   B 1 89  ? 69.65800  -24.93200 51.69900  1.000 23.79808 ? 88  LYS   A NZ    1 
ATOM   2059 N  N     . SER   B 1 90  ? 69.52900  -25.20400 57.55700  1.000 10.90035 ? 89  SER   A N     1 
ATOM   2060 C  CA    . SER   B 1 90  ? 70.90800  -25.66600 57.60500  1.000 12.73353 ? 89  SER   A CA    1 
ATOM   2061 C  C     . SER   B 1 90  ? 71.02400  -26.97300 58.37300  1.000 16.62972 ? 89  SER   A C     1 
ATOM   2062 O  O     . SER   B 1 90  ? 71.85600  -27.82500 58.02900  1.000 13.93733 ? 89  SER   A O     1 
ATOM   2063 C  CB    . SER   B 1 90  ? 71.81000  -24.60400 58.23900  1.000 11.67136 ? 89  SER   A CB    1 
ATOM   2064 O  OG    . SER   B 1 90  ? 71.69300  -24.59200 59.65500  1.000 10.12892 ? 89  SER   A OG    1 
ATOM   2065 N  N     . PHE   B 1 91  ? 70.20100  -27.15900 59.40800  1.000 13.12297 ? 90  PHE   A N     1 
ATOM   2066 C  CA    . PHE   B 1 91  ? 70.18900  -28.45100 60.08400  1.000 15.25190 ? 90  PHE   A CA    1 
ATOM   2067 C  C     . PHE   B 1 91  ? 69.58300  -29.51900 59.18900  1.000 14.57764 ? 90  PHE   A C     1 
ATOM   2068 O  O     . PHE   B 1 91  ? 70.06900  -30.65200 59.16300  1.000 11.71009 ? 90  PHE   A O     1 
ATOM   2069 C  CB    . PHE   B 1 91  ? 69.42900  -28.36800 61.40500  1.000 12.20864 ? 90  PHE   A CB    1 
ATOM   2070 C  CG    . PHE   B 1 91  ? 69.40300  -29.66300 62.16100  1.000 16.89752 ? 90  PHE   A CG    1 
ATOM   2071 C  CD1   . PHE   B 1 91  ? 70.52700  -30.10500 62.84100  1.000 17.03576 ? 90  PHE   A CD1   1 
ATOM   2072 C  CD2   . PHE   B 1 91  ? 68.26000  -30.45000 62.18300  1.000 16.12603 ? 90  PHE   A CD2   1 
ATOM   2073 C  CE1   . PHE   B 1 91  ? 70.50100  -31.30800 63.54300  1.000 16.05726 ? 90  PHE   A CE1   1 
ATOM   2074 C  CE2   . PHE   B 1 91  ? 68.23500  -31.65500 62.87300  1.000 15.85455 ? 90  PHE   A CE2   1 
ATOM   2075 C  CZ    . PHE   B 1 91  ? 69.35100  -32.07400 63.55700  1.000 16.52955 ? 90  PHE   A CZ    1 
ATOM   2076 N  N     . GLU   B 1 92  ? 68.53300  -29.16600 58.43400  1.000 13.36965 ? 91  GLU   A N     1 
ATOM   2077 C  CA    . GLU   B 1 92  ? 67.90800  -30.10700 57.51300  1.000 15.74770 ? 91  GLU   A CA    1 
ATOM   2078 C  C     . GLU   B 1 92  ? 68.82700  -30.47200 56.35800  1.000 16.56127 ? 91  GLU   A C     1 
ATOM   2079 O  O     . GLU   B 1 92  ? 68.61100  -31.50000 55.71400  1.000 23.57660 ? 91  GLU   A O     1 
ATOM   2080 C  CB    . GLU   B 1 92  ? 66.59900  -29.52900 56.97700  1.000 16.11015 ? 91  GLU   A CB    1 
ATOM   2081 C  CG    . GLU   B 1 92  ? 65.53100  -29.39900 58.04400  1.000 17.45938 ? 91  GLU   A CG    1 
ATOM   2082 C  CD    . GLU   B 1 92  ? 64.31700  -28.61100 57.57900  1.000 27.14149 ? 91  GLU   A CD    1 
ATOM   2083 O  OE1   . GLU   B 1 92  ? 64.42200  -27.87700 56.56800  1.000 26.01795 ? 91  GLU   A OE1   1 
ATOM   2084 O  OE2   . GLU   B 1 92  ? 63.26400  -28.72700 58.24000  1.000 23.21529 ? 91  GLU   A OE2   1 
ATOM   2085 N  N     . ASP   B 1 93  ? 69.84700  -29.66300 56.08500  1.000 14.55062 ? 92  ASP   A N     1 
ATOM   2086 C  CA    . ASP   B 1 93  ? 70.80800  -29.96500 55.03400  1.000 13.95251 ? 92  ASP   A CA    1 
ATOM   2087 C  C     . ASP   B 1 93  ? 71.88600  -30.94900 55.46400  1.000 17.31272 ? 92  ASP   A C     1 
ATOM   2088 O  O     . ASP   B 1 93  ? 72.61200  -31.45100 54.60200  1.000 14.59411 ? 92  ASP   A O     1 
ATOM   2089 C  CB    . ASP   B 1 93  ? 71.51500  -28.69500 54.55700  1.000 16.05690 ? 92  ASP   A CB    1 
ATOM   2090 C  CG    . ASP   B 1 93  ? 70.64400  -27.81900 53.69200  1.000 21.63897 ? 92  ASP   A CG    1 
ATOM   2091 O  OD1   . ASP   B 1 93  ? 69.50500  -28.21300 53.39500  1.000 18.60589 ? 92  ASP   A OD1   1 
ATOM   2092 O  OD2   . ASP   B 1 93  ? 71.11200  -26.72400 53.32100  1.000 23.57224 ? 92  ASP   A OD2   1 
ATOM   2093 N  N     . ILE   B 1 94  ? 72.02900  -31.20700 56.76400  1.000 12.70998 ? 93  ILE   A N     1 
ATOM   2094 C  CA    . ILE   B 1 94  ? 73.17200  -31.97400 57.24800  1.000 13.20615 ? 93  ILE   A CA    1 
ATOM   2095 C  C     . ILE   B 1 94  ? 73.22600  -33.36100 56.60600  1.000 15.04535 ? 93  ILE   A C     1 
ATOM   2096 O  O     . ILE   B 1 94  ? 74.29300  -33.81000 56.16400  1.000 10.07671 ? 93  ILE   A O     1 
ATOM   2097 C  CB    . ILE   B 1 94  ? 73.14800  -32.04800 58.78700  1.000 12.61873 ? 93  ILE   A CB    1 
ATOM   2098 C  CG1   . ILE   B 1 94  ? 73.51400  -30.68700 59.37700  1.000 9.20323  ? 93  ILE   A CG1   1 
ATOM   2099 C  CG2   . ILE   B 1 94  ? 74.11600  -33.12400 59.29800  1.000 11.09463 ? 93  ILE   A CG2   1 
ATOM   2100 C  CD1   . ILE   B 1 94  ? 74.91700  -30.20900 58.96300  1.000 10.24308 ? 93  ILE   A CD1   1 
ATOM   2101 N  N     . HIS   B 1 95  ? 72.08700  -34.06200 56.54000  1.000 12.55839 ? 94  HIS   A N     1 
ATOM   2102 C  CA    . HIS   B 1 95  ? 72.12100  -35.43700 56.04800  1.000 16.25358 ? 94  HIS   A CA    1 
ATOM   2103 C  C     . HIS   B 1 95  ? 72.59700  -35.51400 54.60200  1.000 17.32555 ? 94  HIS   A C     1 
ATOM   2104 O  O     . HIS   B 1 95  ? 73.23500  -36.50500 54.22200  1.000 13.16849 ? 94  HIS   A O     1 
ATOM   2105 C  CB    . HIS   B 1 95  ? 70.75000  -36.10800 56.21400  1.000 15.21024 ? 94  HIS   A CB    1 
ATOM   2106 C  CG    . HIS   B 1 95  ? 69.68600  -35.57500 55.31700  1.000 18.39628 ? 94  HIS   A CG    1 
ATOM   2107 N  ND1   . HIS   B 1 95  ? 69.24800  -36.25000 54.19700  1.000 22.11957 ? 94  HIS   A ND1   1 
ATOM   2108 C  CD2   . HIS   B 1 95  ? 68.93400  -34.45200 55.39800  1.000 21.90610 ? 94  HIS   A CD2   1 
ATOM   2109 C  CE1   . HIS   B 1 95  ? 68.28600  -35.55700 53.61300  1.000 18.88913 ? 94  HIS   A CE1   1 
ATOM   2110 N  NE2   . HIS   B 1 95  ? 68.07000  -34.46500 54.32600  1.000 19.06743 ? 94  HIS   A NE2   1 
ATOM   2111 N  N     . HIS   B 1 96  ? 72.33400  -34.47600 53.79600  1.000 13.33782 ? 95  HIS   A N     1 
ATOM   2112 C  CA    . HIS   B 1 96  ? 72.83400  -34.45900 52.41900  1.000 13.98519 ? 95  HIS   A CA    1 
ATOM   2113 C  C     . HIS   B 1 96  ? 74.35900  -34.37600 52.37600  1.000 14.69982 ? 95  HIS   A C     1 
ATOM   2114 O  O     . HIS   B 1 96  ? 74.99400  -34.96900 51.49500  1.000 11.88098 ? 95  HIS   A O     1 
ATOM   2115 C  CB    . HIS   B 1 96  ? 72.23100  -33.29000 51.64300  1.000 14.69324 ? 95  HIS   A CB    1 
ATOM   2116 C  CG    . HIS   B 1 96  ? 70.77200  -33.44200 51.35000  1.000 16.08004 ? 95  HIS   A CG    1 
ATOM   2117 N  ND1   . HIS   B 1 96  ? 69.89100  -32.38200 51.36300  1.000 26.01285 ? 95  HIS   A ND1   1 
ATOM   2118 C  CD2   . HIS   B 1 96  ? 70.04300  -34.52700 51.00700  1.000 21.28865 ? 95  HIS   A CD2   1 
ATOM   2119 C  CE1   . HIS   B 1 96  ? 68.67700  -32.80900 51.06300  1.000 19.15268 ? 95  HIS   A CE1   1 
ATOM   2120 N  NE2   . HIS   B 1 96  ? 68.74200  -34.10700 50.83700  1.000 25.45822 ? 95  HIS   A NE2   1 
ATOM   2121 N  N     . TYR   B 1 97  ? 74.96800  -33.62600 53.29800  1.000 11.23384 ? 96  TYR   A N     1 
ATOM   2122 C  CA    . TYR   B 1 97  ? 76.42400  -33.57300 53.33400  1.000 9.48975  ? 96  TYR   A CA    1 
ATOM   2123 C  C     . TYR   B 1 97  ? 77.00700  -34.93400 53.69500  1.000 14.36730 ? 96  TYR   A C     1 
ATOM   2124 O  O     . TYR   B 1 97  ? 77.95100  -35.40500 53.04400  1.000 11.24582 ? 96  TYR   A O     1 
ATOM   2125 C  CB    . TYR   B 1 97  ? 76.90200  -32.50600 54.31900  1.000 10.84092 ? 96  TYR   A CB    1 
ATOM   2126 C  CG    . TYR   B 1 97  ? 76.65100  -31.09900 53.81300  1.000 10.20943 ? 96  TYR   A CG    1 
ATOM   2127 C  CD1   . TYR   B 1 97  ? 77.53700  -30.48900 52.94300  1.000 12.24872 ? 96  TYR   A CD1   1 
ATOM   2128 C  CD2   . TYR   B 1 97  ? 75.50300  -30.40100 54.17800  1.000 11.99429 ? 96  TYR   A CD2   1 
ATOM   2129 C  CE1   . TYR   B 1 97  ? 77.30500  -29.21000 52.46300  1.000 9.99749  ? 96  TYR   A CE1   1 
ATOM   2130 C  CE2   . TYR   B 1 97  ? 75.25800  -29.12300 53.71100  1.000 11.50511 ? 96  TYR   A CE2   1 
ATOM   2131 C  CZ    . TYR   B 1 97  ? 76.17300  -28.53300 52.85100  1.000 13.50358 ? 96  TYR   A CZ    1 
ATOM   2132 O  OH    . TYR   B 1 97  ? 75.92200  -27.28000 52.37000  1.000 15.98474 ? 96  TYR   A OH    1 
ATOM   2133 N  N     . ARG   B 1 98  ? 76.45200  -35.58600 54.72700  1.000 10.16439 ? 97  ARG   A N     1 
ATOM   2134 C  CA    . ARG   B 1 98  ? 76.95500  -36.90000 55.10000  1.000 10.63858 ? 97  ARG   A CA    1 
ATOM   2135 C  C     . ARG   B 1 98  ? 76.76600  -37.89100 53.96700  1.000 13.66475 ? 97  ARG   A C     1 
ATOM   2136 O  O     . ARG   B 1 98  ? 77.65200  -38.70800 53.70600  1.000 12.17740 ? 97  ARG   A O     1 
ATOM   2137 C  CB    . ARG   B 1 98  ? 76.26500  -37.41800 56.35900  1.000 14.91210 ? 97  ARG   A CB    1 
ATOM   2138 C  CG    . ARG   B 1 98  ? 76.73300  -38.82300 56.75600  1.000 11.80982 ? 97  ARG   A CG    1 
ATOM   2139 C  CD    . ARG   B 1 98  ? 76.28200  -39.23900 58.13600  1.000 21.63422 ? 97  ARG   A CD    1 
ATOM   2140 N  NE    . ARG   B 1 98  ? 76.46100  -40.67000 58.34800  1.000 22.81299 ? 97  ARG   A NE    1 
ATOM   2141 C  CZ    . ARG   B 1 98  ? 77.59900  -41.23900 58.72200  1.000 26.65866 ? 97  ARG   A CZ    1 
ATOM   2142 N  NH1   . ARG   B 1 98  ? 78.67400  -40.51900 59.00100  1.000 31.13553 ? 97  ARG   A NH1   1 
ATOM   2143 N  NH2   . ARG   B 1 98  ? 77.66000  -42.56500 58.81700  1.000 25.20378 ? 97  ARG   A NH2   1 
ATOM   2144 N  N     . GLU   B 1 99  ? 75.61000  -37.84300 53.29200  1.000 14.14400 ? 98  GLU   A N     1 
ATOM   2145 C  CA    . GLU   B 1 99  ? 75.35300  -38.80900 52.22800  1.000 15.14716 ? 98  GLU   A CA    1 
ATOM   2146 C  C     . GLU   B 1 99  ? 76.29800  -38.60600 51.05500  1.000 15.69513 ? 98  GLU   A C     1 
ATOM   2147 O  O     . GLU   B 1 99  ? 76.72400  -39.58300 50.43200  1.000 15.69381 ? 98  GLU   A O     1 
ATOM   2148 C  CB    . GLU   B 1 99  ? 73.90800  -38.70600 51.73700  1.000 15.90722 ? 98  GLU   A CB    1 
ATOM   2149 C  CG    . GLU   B 1 99  ? 72.86000  -39.13600 52.73800  1.000 22.32106 ? 98  GLU   A CG    1 
ATOM   2150 C  CD    . GLU   B 1 99  ? 71.49600  -38.48900 52.46800  1.000 26.67034 ? 98  GLU   A CD    1 
ATOM   2151 O  OE1   . GLU   B 1 99  ? 71.37600  -37.69300 51.50400  1.000 23.77986 ? 98  GLU   A OE1   1 
ATOM   2152 O  OE2   . GLU   B 1 99  ? 70.54300  -38.78700 53.22100  1.000 26.98468 ? 98  GLU   A OE2   1 
ATOM   2153 N  N     . GLN   B 1 100 ? 76.63900  -37.35000 50.74100  1.000 12.97853 ? 99  GLN   A N     1 
ATOM   2154 C  CA    . GLN   B 1 100 ? 77.52600  -37.10100 49.61100  1.000 14.76473 ? 99  GLN   A CA    1 
ATOM   2155 C  C     . GLN   B 1 100 ? 78.97000  -37.47300 49.92700  1.000 13.64396 ? 99  GLN   A C     1 
ATOM   2156 O  O     . GLN   B 1 100 ? 79.67900  -37.99400 49.06200  1.000 13.76066 ? 99  GLN   A O     1 
ATOM   2157 C  CB    . GLN   B 1 100 ? 77.41800  -35.63700 49.16900  1.000 15.36438 ? 99  GLN   A CB    1 
ATOM   2158 C  CG    . GLN   B 1 100 ? 76.10500  -35.32300 48.43200  1.000 22.23505 ? 99  GLN   A CG    1 
ATOM   2159 C  CD    . GLN   B 1 100 ? 75.88000  -36.21300 47.20300  1.000 24.88922 ? 99  GLN   A CD    1 
ATOM   2160 O  OE1   . GLN   B 1 100 ? 76.83100  -36.68400 46.57800  1.000 29.32854 ? 99  GLN   A OE1   1 
ATOM   2161 N  NE2   . GLN   B 1 100 ? 74.61700  -36.44200 46.85700  1.000 38.63431 ? 99  GLN   A NE2   1 
ATOM   2162 N  N     . ILE   B 1 101 ? 79.42400  -37.20100 51.15100  1.000 11.93725 ? 100 ILE   A N     1 
ATOM   2163 C  CA    . ILE   B 1 101 ? 80.76600  -37.60900 51.56300  1.000 12.90706 ? 100 ILE   A CA    1 
ATOM   2164 C  C     . ILE   B 1 101 ? 80.91000  -39.12600 51.51300  1.000 11.71640 ? 100 ILE   A C     1 
ATOM   2165 O  O     . ILE   B 1 101 ? 81.95600  -39.65100 51.11000  1.000 13.60832 ? 100 ILE   A O     1 
ATOM   2166 C  CB    . ILE   B 1 101 ? 81.07200  -37.08700 52.97500  1.000 9.91398  ? 100 ILE   A CB    1 
ATOM   2167 C  CG1   . ILE   B 1 101 ? 81.06500  -35.56300 53.03100  1.000 9.07582  ? 100 ILE   A CG1   1 
ATOM   2168 C  CG2   . ILE   B 1 101 ? 82.41300  -37.63100 53.45300  1.000 11.30954 ? 100 ILE   A CG2   1 
ATOM   2169 C  CD1   . ILE   B 1 101 ? 80.95100  -35.08300 54.43900  1.000 9.56160  ? 100 ILE   A CD1   1 
ATOM   2170 N  N     . LYS   B 1 102 ? 79.87600  -39.85800 51.95000  1.000 12.47854 ? 101 LYS   A N     1 
ATOM   2171 C  CA    . LYS   B 1 102 ? 79.93000  -41.32100 51.88700  1.000 13.52681 ? 101 LYS   A CA    1 
ATOM   2172 C  C     . LYS   B 1 102 ? 79.93000  -41.82200 50.44600  1.000 14.50339 ? 101 LYS   A C     1 
ATOM   2173 O  O     . LYS   B 1 102 ? 80.60900  -42.80500 50.12500  1.000 15.28585 ? 101 LYS   A O     1 
ATOM   2174 C  CB    . LYS   B 1 102 ? 78.75600  -41.93500 52.66100  1.000 15.83450 ? 101 LYS   A CB    1 
ATOM   2175 C  CG    . LYS   B 1 102 ? 78.84200  -41.75000 54.17500  1.000 16.80372 ? 101 LYS   A CG    1 
ATOM   2176 C  CD    . LYS   B 1 102 ? 77.55200  -42.13900 54.87600  1.000 17.52129 ? 101 LYS   A CD    1 
ATOM   2177 C  CE    . LYS   B 1 102 ? 77.25100  -43.59400 54.73000  1.000 22.50271 ? 101 LYS   A CE    1 
ATOM   2178 N  NZ    . LYS   B 1 102 ? 75.80700  -43.86800 55.00100  1.000 22.33901 ? 101 LYS   A NZ    1 
ATOM   2179 N  N     . ARG   B 1 103 ? 79.16600  -41.17100 49.56800  1.000 14.61479 ? 102 ARG   A N     1 
ATOM   2180 C  CA    . ARG   B 1 103 ? 79.12400  -41.60100 48.17700  1.000 15.69690 ? 102 ARG   A CA    1 
ATOM   2181 C  C     . ARG   B 1 103 ? 80.47000  -41.37000 47.50500  1.000 15.42174 ? 102 ARG   A C     1 
ATOM   2182 O  O     . ARG   B 1 103 ? 80.97700  -42.23800 46.78700  1.000 16.43913 ? 102 ARG   A O     1 
ATOM   2183 C  CB    . ARG   B 1 103 ? 78.01000  -40.86300 47.42800  1.000 16.38776 ? 102 ARG   A CB    1 
ATOM   2184 C  CG    . ARG   B 1 103 ? 77.86900  -41.27000 45.95800  1.000 17.25501 ? 102 ARG   A CG    1 
ATOM   2185 C  CD    . ARG   B 1 103 ? 76.87400  -40.38400 45.20200  1.000 17.47639 ? 102 ARG   A CD    1 
ATOM   2186 N  NE    . ARG   B 1 103 ? 77.27800  -38.98000 45.20800  1.000 23.02656 ? 102 ARG   A NE    1 
ATOM   2187 C  CZ    . ARG   B 1 103 ? 78.26900  -38.46600 44.48600  1.000 28.36527 ? 102 ARG   A CZ    1 
ATOM   2188 N  NH1   . ARG   B 1 103 ? 79.01600  -39.22100 43.69200  1.000 22.17366 ? 102 ARG   A NH1   1 
ATOM   2189 N  NH2   . ARG   B 1 103 ? 78.52900  -37.16200 44.57400  1.000 23.34268 ? 102 ARG   A NH2   1 
ATOM   2190 N  N     . VAL   B 1 104 ? 81.06500  -40.19900 47.74900  1.000 14.18101 ? 103 VAL   A N     1 
ATOM   2191 C  CA    . VAL   B 1 104 ? 82.31300  -39.81400 47.09400  1.000 14.05892 ? 103 VAL   A CA    1 
ATOM   2192 C  C     . VAL   B 1 104 ? 83.47500  -40.66100 47.60000  1.000 14.12808 ? 103 VAL   A C     1 
ATOM   2193 O  O     . VAL   B 1 104 ? 84.31500  -41.12200 46.82000  1.000 18.62772 ? 103 VAL   A O     1 
ATOM   2194 C  CB    . VAL   B 1 104 ? 82.56800  -38.31400 47.31200  1.000 13.97024 ? 103 VAL   A CB    1 
ATOM   2195 C  CG1   . VAL   B 1 104 ? 84.03200  -37.95100 47.03400  1.000 16.65020 ? 103 VAL   A CG1   1 
ATOM   2196 C  CG2   . VAL   B 1 104 ? 81.63900  -37.49900 46.44500  1.000 13.42295 ? 103 VAL   A CG2   1 
ATOM   2197 N  N     . LYS   B 1 105 ? 83.54100  -40.88000 48.90200  1.000 13.59969 ? 104 LYS   A N     1 
ATOM   2198 C  CA    . LYS   B 1 105 ? 84.60300  -41.68600 49.47400  1.000 15.14954 ? 104 LYS   A CA    1 
ATOM   2199 C  C     . LYS   B 1 105 ? 84.28500  -43.17700 49.42300  1.000 16.10104 ? 104 LYS   A C     1 
ATOM   2200 O  O     . LYS   B 1 105 ? 85.13500  -43.98800 49.80200  1.000 16.04463 ? 104 LYS   A O     1 
ATOM   2201 C  CB    . LYS   B 1 105 ? 84.86900  -41.22200 50.90600  1.000 20.28328 ? 104 LYS   A CB    1 
ATOM   2202 C  CG    . LYS   B 1 105 ? 85.10500  -39.70000 50.97700  1.000 19.13010 ? 104 LYS   A CG    1 
ATOM   2203 C  CD    . LYS   B 1 105 ? 85.78500  -39.25100 52.26300  1.000 21.83978 ? 104 LYS   A CD    1 
ATOM   2204 C  CE    . LYS   B 1 105 ? 87.28500  -39.60500 52.27900  1.000 17.03632 ? 104 LYS   A CE    1 
ATOM   2205 N  NZ    . LYS   B 1 105 ? 88.13900  -38.68700 51.46500  1.000 15.35844 ? 104 LYS   A NZ    1 
ATOM   2206 N  N     . ASP   B 1 106 ? 83.09400  -43.54500 48.94400  1.000 15.89639 ? 105 ASP   A N     1 
ATOM   2207 C  CA    . ASP   B 1 106 ? 82.67300  -44.94600 48.82700  1.000 17.37958 ? 105 ASP   A CA    1 
ATOM   2208 C  C     . ASP   B 1 106 ? 82.91300  -45.69700 50.13600  1.000 17.45192 ? 105 ASP   A C     1 
ATOM   2209 O  O     . ASP   B 1 106 ? 83.52000  -46.77300 50.17200  1.000 18.43717 ? 105 ASP   A O     1 
ATOM   2210 C  CB    . ASP   B 1 106 ? 83.37900  -45.62200 47.65200  1.000 18.55141 ? 105 ASP   A CB    1 
ATOM   2211 C  CG    . ASP   B 1 106 ? 82.86700  -47.01900 47.37500  1.000 20.31498 ? 105 ASP   A CG    1 
ATOM   2212 O  OD1   . ASP   B 1 106 ? 81.64100  -47.24200 47.45100  1.000 20.85486 ? 105 ASP   A OD1   1 
ATOM   2213 O  OD2   . ASP   B 1 106 ? 83.69500  -47.89100 47.04400  1.000 21.30845 ? 105 ASP   A OD2   1 
ATOM   2214 N  N     . SER   B 1 107 ? 82.42900  -45.10300 51.22900  1.000 16.50285 ? 106 SER   A N     1 
ATOM   2215 C  CA    . SER   B 1 107 ? 82.69800  -45.61300 52.56600  1.000 18.56595 ? 106 SER   A CA    1 
ATOM   2216 C  C     . SER   B 1 107 ? 81.56400  -45.22200 53.49900  1.000 16.08397 ? 106 SER   A C     1 
ATOM   2217 O  O     . SER   B 1 107 ? 81.02600  -44.11900 53.39300  1.000 17.81675 ? 106 SER   A O     1 
ATOM   2218 C  CB    . SER   B 1 107 ? 84.01900  -45.07300 53.13100  1.000 19.83679 ? 106 SER   A CB    1 
ATOM   2219 O  OG    . SER   B 1 107 ? 84.36700  -45.78700 54.30400  1.000 22.95647 ? 106 SER   A OG    1 
ATOM   2220 N  N     . GLU   B 1 108 ? 81.21400  -46.12000 54.42100  1.000 16.87025 ? 107 GLU   A N     1 
ATOM   2221 C  CA    . GLU   B 1 108 ? 80.25700  -45.76500 55.46500  1.000 22.24179 ? 107 GLU   A CA    1 
ATOM   2222 C  C     . GLU   B 1 108 ? 80.92700  -45.20800 56.71500  1.000 21.04751 ? 107 GLU   A C     1 
ATOM   2223 O  O     . GLU   B 1 108 ? 80.22500  -44.76600 57.63100  1.000 20.73553 ? 107 GLU   A O     1 
ATOM   2224 C  CB    . GLU   B 1 108 ? 79.38000  -46.97300 55.83000  1.000 24.04173 ? 107 GLU   A CB    1 
ATOM   2225 C  CG    . GLU   B 1 108 ? 78.50400  -47.44400 54.67300  1.000 25.03667 ? 107 GLU   A CG    1 
ATOM   2226 C  CD    . GLU   B 1 108 ? 77.07500  -47.79200 55.08800  1.000 27.84164 ? 107 GLU   A CD    1 
ATOM   2227 O  OE1   . GLU   B 1 108 ? 76.84100  -48.91400 55.60400  1.000 25.30441 ? 107 GLU   A OE1   1 
ATOM   2228 O  OE2   . GLU   B 1 108 ? 76.17700  -46.94200 54.88600  1.000 28.61043 ? 107 GLU   A OE2   1 
ATOM   2229 N  N     . ASP   B 1 109 ? 82.26300  -45.18300 56.75300  1.000 16.97845 ? 108 ASP   A N     1 
ATOM   2230 C  CA    . ASP   B 1 109 ? 83.04700  -44.81500 57.93200  1.000 16.37725 ? 108 ASP   A CA    1 
ATOM   2231 C  C     . ASP   B 1 109 ? 84.05300  -43.72800 57.53800  1.000 14.62148 ? 108 ASP   A C     1 
ATOM   2232 O  O     . ASP   B 1 109 ? 85.20400  -44.02800 57.20700  1.000 21.08334 ? 108 ASP   A O     1 
ATOM   2233 C  CB    . ASP   B 1 109 ? 83.74000  -46.06400 58.50200  1.000 22.01575 ? 108 ASP   A CB    1 
ATOM   2234 C  CG    . ASP   B 1 109 ? 84.62000  -45.75700 59.69100  1.000 26.48732 ? 108 ASP   A CG    1 
ATOM   2235 O  OD1   . ASP   B 1 109 ? 84.34900  -44.74800 60.38500  1.000 36.72501 ? 108 ASP   A OD1   1 
ATOM   2236 O  OD2   . ASP   B 1 109 ? 85.58600  -46.51600 59.92400  1.000 27.07610 ? 108 ASP   A OD2   1 
ATOM   2237 N  N     . VAL   B 1 110 ? 83.62700  -42.47500 57.56400  1.000 14.49219 ? 109 VAL   A N     1 
ATOM   2238 C  CA    . VAL   B 1 110 ? 84.47100  -41.32900 57.23800  1.000 11.71351 ? 109 VAL   A CA    1 
ATOM   2239 C  C     . VAL   B 1 110 ? 84.52900  -40.41900 58.44900  1.000 13.49158 ? 109 VAL   A C     1 
ATOM   2240 O  O     . VAL   B 1 110 ? 83.47500  -40.09900 59.01500  1.000 10.68906 ? 109 VAL   A O     1 
ATOM   2241 C  CB    . VAL   B 1 110 ? 83.96200  -40.54800 56.01200  1.000 11.09713 ? 109 VAL   A CB    1 
ATOM   2242 C  CG1   . VAL   B 1 110 ? 84.89400  -39.37700 55.71600  1.000 10.26415 ? 109 VAL   A CG1   1 
ATOM   2243 C  CG2   . VAL   B 1 110 ? 83.86700  -41.44300 54.80500  1.000 13.07264 ? 109 VAL   A CG2   1 
ATOM   2244 N  N     . PRO   B 1 111 ? 85.70600  -39.96400 58.88600  1.000 10.46234 ? 110 PRO   A N     1 
ATOM   2245 C  CA    . PRO   B 1 111 ? 85.78700  -39.06500 60.05300  1.000 10.22263 ? 110 PRO   A CA    1 
ATOM   2246 C  C     . PRO   B 1 111 ? 84.99500  -37.78300 59.83500  1.000 10.83394 ? 110 PRO   A C     1 
ATOM   2247 O  O     . PRO   B 1 111 ? 85.22100  -37.05400 58.87100  1.000 9.47860  ? 110 PRO   A O     1 
ATOM   2248 C  CB    . PRO   B 1 111 ? 87.29100  -38.77800 60.17500  1.000 12.81194 ? 110 PRO   A CB    1 
ATOM   2249 C  CG    . PRO   B 1 111 ? 87.94000  -39.97300 59.57200  1.000 14.12847 ? 110 PRO   A CG    1 
ATOM   2250 C  CD    . PRO   B 1 111 ? 87.03300  -40.45100 58.47200  1.000 11.84953 ? 110 PRO   A CD    1 
ATOM   2251 N  N     . MET   B 1 112 ? 84.07200  -37.50500 60.76100  1.000 14.17938 ? 111 MET   A N     1 
ATOM   2252 C  CA    . MET   B 1 112 ? 83.16600  -36.36500 60.67800  1.000 8.64057  ? 111 MET   A CA    1 
ATOM   2253 C  C     . MET   B 1 112 ? 82.76600  -35.93200 62.07000  1.000 8.70027  ? 111 MET   A C     1 
ATOM   2254 O  O     . MET   B 1 112 ? 82.69700  -36.74600 62.99000  1.000 11.99182 ? 111 MET   A O     1 
ATOM   2255 C  CB    . MET   B 1 112 ? 81.85200  -36.69400 59.96700  1.000 15.71268 ? 111 MET   A CB    1 
ATOM   2256 C  CG    . MET   B 1 112 ? 81.91500  -36.95900 58.52100  1.000 17.32240 ? 111 MET   A CG    1 
ATOM   2257 S  SD    . MET   B 1 112 ? 80.25100  -37.51100 58.12300  1.000 16.99208 ? 111 MET   A SD    1 
ATOM   2258 C  CE    . MET   B 1 112 ? 80.65400  -38.35000 56.59900  1.000 13.88474 ? 111 MET   A CE    1 
ATOM   2259 N  N     . VAL   B 1 113 ? 82.43500  -34.65200 62.19300  1.000 10.47576 ? 112 VAL   A N     1 
ATOM   2260 C  CA    . VAL   B 1 113 ? 81.97900  -34.06700 63.44500  1.000 9.71830  ? 112 VAL   A CA    1 
ATOM   2261 C  C     . VAL   B 1 113 ? 80.82700  -33.14600 63.10200  1.000 11.55914 ? 112 VAL   A C     1 
ATOM   2262 O  O     . VAL   B 1 113 ? 80.90800  -32.37500 62.14100  1.000 9.37188  ? 112 VAL   A O     1 
ATOM   2263 C  CB    . VAL   B 1 113 ? 83.09400  -33.29300 64.17600  1.000 9.34944  ? 112 VAL   A CB    1 
ATOM   2264 C  CG1   . VAL   B 1 113 ? 82.51200  -32.45500 65.32000  1.000 11.75082 ? 112 VAL   A CG1   1 
ATOM   2265 C  CG2   . VAL   B 1 113 ? 84.14300  -34.27600 64.69500  1.000 11.94576 ? 112 VAL   A CG2   1 
ATOM   2266 N  N     . LEU   B 1 114 ? 79.74700  -33.25500 63.85600  1.000 10.25258 ? 113 LEU   A N     1 
ATOM   2267 C  CA    . LEU   B 1 114 ? 78.61300  -32.36700 63.69200  1.000 8.46830  ? 113 LEU   A CA    1 
ATOM   2268 C  C     . LEU   B 1 114 ? 78.78900  -31.14400 64.58100  1.000 9.48327  ? 113 LEU   A C     1 
ATOM   2269 O  O     . LEU   B 1 114 ? 78.99800  -31.27800 65.79100  1.000 9.57587  ? 113 LEU   A O     1 
ATOM   2270 C  CB    . LEU   B 1 114 ? 77.32600  -33.11000 64.03400  1.000 9.22134  ? 113 LEU   A CB    1 
ATOM   2271 C  CG    . LEU   B 1 114 ? 76.05500  -32.27300 63.98000  1.000 9.37943  ? 113 LEU   A CG    1 
ATOM   2272 C  CD1   . LEU   B 1 114 ? 75.74000  -31.95100 62.52500  1.000 11.34729 ? 113 LEU   A CD1   1 
ATOM   2273 C  CD2   . LEU   B 1 114 ? 74.91300  -33.02500 64.66700  1.000 11.54089 ? 113 LEU   A CD2   1 
ATOM   2274 N  N     . VAL   B 1 115 ? 78.68700  -29.95800 63.98400  1.000 8.48032  ? 114 VAL   A N     1 
ATOM   2275 C  CA    . VAL   B 1 115 ? 78.93000  -28.69900 64.67600  1.000 8.92171  ? 114 VAL   A CA    1 
ATOM   2276 C  C     . VAL   B 1 115 ? 77.65400  -27.87300 64.63900  1.000 11.48785 ? 114 VAL   A C     1 
ATOM   2277 O  O     . VAL   B 1 115 ? 77.17300  -27.51800 63.55400  1.000 7.86599  ? 114 VAL   A O     1 
ATOM   2278 C  CB    . VAL   B 1 115 ? 80.08100  -27.91100 64.03500  1.000 7.40045  ? 114 VAL   A CB    1 
ATOM   2279 C  CG1   . VAL   B 1 115 ? 80.35900  -26.62700 64.84300  1.000 7.60477  ? 114 VAL   A CG1   1 
ATOM   2280 C  CG2   . VAL   B 1 115 ? 81.31600  -28.77300 63.89600  1.000 7.78570  ? 114 VAL   A CG2   1 
ATOM   2281 N  N     . GLY   B 1 116 ? 77.11900  -27.56600 65.81500  1.000 8.69001  ? 115 GLY   A N     1 
ATOM   2282 C  CA    . GLY   B 1 116 ? 76.01000  -26.63400 65.94700  1.000 9.04274  ? 115 GLY   A CA    1 
ATOM   2283 C  C     . GLY   B 1 116 ? 76.52800  -25.27400 66.36700  1.000 10.02759 ? 115 GLY   A C     1 
ATOM   2284 O  O     . GLY   B 1 116 ? 76.83900  -25.04500 67.53900  1.000 11.27301 ? 115 GLY   A O     1 
ATOM   2285 N  N     . ASN   B 1 117 ? 76.61200  -24.36100 65.41600  1.000 9.22077  ? 116 ASN   A N     1 
ATOM   2286 C  CA    . ASN   B 1 117 ? 77.23400  -23.06400 65.62600  1.000 11.38214 ? 116 ASN   A CA    1 
ATOM   2287 C  C     . ASN   B 1 117 ? 76.20800  -21.96400 65.93800  1.000 9.38222  ? 116 ASN   A C     1 
ATOM   2288 O  O     . ASN   B 1 117 ? 74.98700  -22.14500 65.83400  1.000 11.17093 ? 116 ASN   A O     1 
ATOM   2289 C  CB    . ASN   B 1 117 ? 78.06900  -22.69400 64.39900  1.000 8.50313  ? 116 ASN   A CB    1 
ATOM   2290 C  CG    . ASN   B 1 117 ? 78.95600  -21.51800 64.66400  1.000 8.95299  ? 116 ASN   A CG    1 
ATOM   2291 O  OD1   . ASN   B 1 117 ? 79.61300  -21.47400 65.69500  1.000 10.59385 ? 116 ASN   A OD1   1 
ATOM   2292 N  ND2   . ASN   B 1 117 ? 78.92700  -20.51900 63.77400  1.000 8.35559  ? 116 ASN   A ND2   1 
ATOM   2293 N  N     . LYS   B 1 118 ? 76.74000  -20.80800 66.35800  1.000 9.71646  ? 117 LYS   A N     1 
ATOM   2294 C  CA    . LYS   B 1 118 ? 75.96900  -19.62900 66.76700  1.000 10.46739 ? 117 LYS   A CA    1 
ATOM   2295 C  C     . LYS   B 1 118 ? 75.24600  -19.84600 68.10000  1.000 11.87710 ? 117 LYS   A C     1 
ATOM   2296 O  O     . LYS   B 1 118 ? 74.15700  -19.29600 68.32500  1.000 15.86328 ? 117 LYS   A O     1 
ATOM   2297 C  CB    . LYS   B 1 118 ? 74.98300  -19.18600 65.67300  1.000 12.85887 ? 117 LYS   A CB    1 
ATOM   2298 C  CG    . LYS   B 1 118 ? 75.62200  -18.96200 64.26900  1.000 11.35103 ? 117 LYS   A CG    1 
ATOM   2299 C  CD    . LYS   B 1 118 ? 74.81600  -17.98300 63.38400  1.000 14.09646 ? 117 LYS   A CD    1 
ATOM   2300 C  CE    . LYS   B 1 118 ? 75.43300  -17.87000 61.98400  1.000 9.49536  ? 117 LYS   A CE    1 
ATOM   2301 N  NZ    . LYS   B 1 118 ? 74.79000  -16.89400 61.04600  1.000 9.88698  ? 117 LYS   A NZ    1 
ATOM   2302 N  N     . SER   B 1 119 ? 75.85500  -20.63500 68.99600  1.000 11.40176 ? 118 SER   A N     1 
ATOM   2303 C  CA    . SER   B 1 119 ? 75.25000  -20.97100 70.28000  1.000 12.29829 ? 118 SER   A CA    1 
ATOM   2304 C  C     . SER   B 1 119 ? 75.06200  -19.76200 71.19300  1.000 13.34995 ? 118 SER   A C     1 
ATOM   2305 O  O     . SER   B 1 119 ? 74.32600  -19.86500 72.17800  1.000 17.33130 ? 118 SER   A O     1 
ATOM   2306 C  CB    . SER   B 1 119 ? 76.09500  -22.02700 71.00000  1.000 12.28214 ? 118 SER   A CB    1 
ATOM   2307 O  OG    . SER   B 1 119 ? 76.41100  -23.10000 70.12900  1.000 19.83808 ? 118 SER   A OG    1 
ATOM   2308 N  N     . ASP   B 1 120 ? 75.70300  -18.62600 70.90200  1.000 13.75508 ? 119 ASP   A N     1 
ATOM   2309 C  CA    . ASP   B 1 120 ? 75.52000  -17.41500 71.70000  1.000 14.52878 ? 119 ASP   A CA    1 
ATOM   2310 C  C     . ASP   B 1 120 ? 74.20000  -16.71200 71.42800  1.000 15.11267 ? 119 ASP   A C     1 
ATOM   2311 O  O     . ASP   B 1 120 ? 73.81700  -15.82900 72.20900  1.000 16.19993 ? 119 ASP   A O     1 
ATOM   2312 C  CB    . ASP   B 1 120 ? 76.65100  -16.43000 71.42400  1.000 18.95979 ? 119 ASP   A CB    1 
ATOM   2313 C  CG    . ASP   B 1 120 ? 76.74100  -16.05300 69.95700  1.000 16.02040 ? 119 ASP   A CG    1 
ATOM   2314 O  OD1   . ASP   B 1 120 ? 77.21300  -16.89100 69.15100  1.000 14.68395 ? 119 ASP   A OD1   1 
ATOM   2315 O  OD2   . ASP   B 1 120 ? 76.31200  -14.92700 69.60700  1.000 18.16212 ? 119 ASP   A OD2   1 
ATOM   2316 N  N     . LEU   B 1 121 ? 73.52500  -17.05800 70.38800  1.000 14.36171 ? 120 LEU   A N     1 
ATOM   2317 C  CA    . LEU   B 1 121 ? 72.38700  -16.24300 69.97600  1.000 15.69719 ? 120 LEU   A CA    1 
ATOM   2318 C  C     . LEU   B 1 121 ? 71.10800  -16.63300 70.71400  1.000 16.38801 ? 120 LEU   A C     1 
ATOM   2319 O  O     . LEU   B 1 121 ? 70.94600  -17.78800 71.13100  1.000 16.65704 ? 120 LEU   A O     1 
ATOM   2320 C  CB    . LEU   B 1 121 ? 72.16600  -16.36600 68.47300  1.000 14.97997 ? 120 LEU   A CB    1 
ATOM   2321 C  CG    . LEU   B 1 121 ? 73.19500  -15.62700 67.62000  1.000 18.85212 ? 120 LEU   A CG    1 
ATOM   2322 C  CD1   . LEU   B 1 121 ? 73.00200  -15.92900 66.14400  1.000 16.86961 ? 120 LEU   A CD1   1 
ATOM   2323 C  CD2   . LEU   B 1 121 ? 73.09400  -14.12000 67.88500  1.000 18.62291 ? 120 LEU   A CD2   1 
ATOM   2324 N  N     . PRO   B 1 122 ? 70.19500  -15.68400 70.87500  1.000 16.78964 ? 121 PRO   A N     1 
ATOM   2325 C  CA    . PRO   B 1 122 ? 68.92900  -15.94800 71.57700  1.000 17.85245 ? 121 PRO   A CA    1 
ATOM   2326 C  C     . PRO   B 1 122 ? 67.80300  -16.43600 70.68200  1.000 17.67608 ? 121 PRO   A C     1 
ATOM   2327 O  O     . PRO   B 1 122 ? 66.66000  -16.48100 71.14000  1.000 18.73722 ? 121 PRO   A O     1 
ATOM   2328 C  CB    . PRO   B 1 122 ? 68.58100  -14.56500 72.13900  1.000 19.17671 ? 121 PRO   A CB    1 
ATOM   2329 C  CG    . PRO   B 1 122 ? 69.02100  -13.65000 71.04200  1.000 18.63157 ? 121 PRO   A CG    1 
ATOM   2330 C  CD    . PRO   B 1 122 ? 70.32300  -14.26200 70.50700  1.000 17.22689 ? 121 PRO   A CD    1 
ATOM   2331 N  N     . SER   B 1 123 ? 68.09700  -16.79100 69.43800  1.000 16.52630 ? 122 SER   A N     1 
ATOM   2332 C  CA    . SER   B 1 123 ? 67.09200  -17.02600 68.40400  1.000 18.86918 ? 122 SER   A CA    1 
ATOM   2333 C  C     . SER   B 1 123 ? 67.04700  -18.48900 67.96100  1.000 18.80492 ? 122 SER   A C     1 
ATOM   2334 O  O     . SER   B 1 123 ? 66.79000  -18.79900 66.79400  1.000 15.26109 ? 122 SER   A O     1 
ATOM   2335 C  CB    . SER   B 1 123 ? 67.36000  -16.12300 67.20500  1.000 16.02007 ? 122 SER   A CB    1 
ATOM   2336 O  OG    . SER   B 1 123 ? 68.71500  -16.22200 66.80800  1.000 17.85623 ? 122 SER   A OG    1 
ATOM   2337 N  N     . ARG   B 1 124 ? 67.25900  -19.40300 68.90100  1.000 15.88027 ? 123 ARG   A N     1 
ATOM   2338 C  CA    . ARG   B 1 124 ? 67.40800  -20.81900 68.57100  1.000 15.26768 ? 123 ARG   A CA    1 
ATOM   2339 C  C     . ARG   B 1 124 ? 66.14800  -21.38900 67.92300  1.000 17.64214 ? 123 ARG   A C     1 
ATOM   2340 O  O     . ARG   B 1 124 ? 65.03000  -21.13500 68.37800  1.000 16.93587 ? 123 ARG   A O     1 
ATOM   2341 C  CB    . ARG   B 1 124 ? 67.74100  -21.61900 69.83800  1.000 15.64846 ? 123 ARG   A CB    1 
ATOM   2342 C  CG    . ARG   B 1 124 ? 67.73200  -23.12200 69.60600  1.000 15.85459 ? 123 ARG   A CG    1 
ATOM   2343 C  CD    . ARG   B 1 124 ? 67.99300  -23.89700 70.89600  1.000 19.29061 ? 123 ARG   A CD    1 
ATOM   2344 N  NE    . ARG   B 1 124 ? 69.35200  -23.70700 71.39900  1.000 18.53601 ? 123 ARG   A NE    1 
ATOM   2345 C  CZ    . ARG   B 1 124 ? 70.40400  -24.42600 71.02300  1.000 17.63968 ? 123 ARG   A CZ    1 
ATOM   2346 N  NH1   . ARG   B 1 124 ? 70.31800  -25.33800 70.06700  1.000 13.85465 ? 123 ARG   A NH1   1 
ATOM   2347 N  NH2   . ARG   B 1 124 ? 71.57100  -24.23500 71.63100  1.000 22.40379 ? 123 ARG   A NH2   1 
ATOM   2348 N  N     . THR   B 1 125 ? 66.34200  -22.16400 66.84700  1.000 14.97994 ? 124 THR   A N     1 
ATOM   2349 C  CA    . THR   B 1 125 ? 65.27400  -22.92300 66.22100  1.000 15.50915 ? 124 THR   A CA    1 
ATOM   2350 C  C     . THR   B 1 125 ? 65.53300  -24.42900 66.19800  1.000 16.41346 ? 124 THR   A C     1 
ATOM   2351 O  O     . THR   B 1 125 ? 64.58700  -25.19000 65.98500  1.000 16.04686 ? 124 THR   A O     1 
ATOM   2352 C  CB    . THR   B 1 125 ? 65.02400  -22.43900 64.77700  1.000 15.18200 ? 124 THR   A CB    1 
ATOM   2353 O  OG1   . THR   B 1 125 ? 66.16900  -22.71900 63.96400  1.000 13.94796 ? 124 THR   A OG1   1 
ATOM   2354 C  CG2   . THR   B 1 125 ? 64.70500  -20.92500 64.72900  1.000 15.59147 ? 124 THR   A CG2   1 
ATOM   2355 N  N     . VAL   B 1 126 ? 66.77100  -24.87300 66.41500  1.000 14.67193 ? 125 VAL   A N     1 
ATOM   2356 C  CA    . VAL   B 1 126 ? 67.13500  -26.29100 66.42600  1.000 17.60304 ? 125 VAL   A CA    1 
ATOM   2357 C  C     . VAL   B 1 126 ? 67.41800  -26.70000 67.86600  1.000 18.13376 ? 125 VAL   A C     1 
ATOM   2358 O  O     . VAL   B 1 126 ? 68.31500  -26.14200 68.50900  1.000 14.95314 ? 125 VAL   A O     1 
ATOM   2359 C  CB    . VAL   B 1 126 ? 68.35800  -26.58300 65.53800  1.000 14.17319 ? 125 VAL   A CB    1 
ATOM   2360 C  CG1   . VAL   B 1 126 ? 68.61800  -28.08200 65.46400  1.000 17.16736 ? 125 VAL   A CG1   1 
ATOM   2361 C  CG2   . VAL   B 1 126 ? 68.17600  -25.99700 64.13300  1.000 13.33945 ? 125 VAL   A CG2   1 
ATOM   2362 N  N     . ASP   B 1 127 ? 66.66500  -27.67600 68.37200  1.000 17.59520 ? 126 ASP   A N     1 
ATOM   2363 C  CA    . ASP   B 1 127 ? 66.89500  -28.17400 69.72500  1.000 16.36244 ? 126 ASP   A CA    1 
ATOM   2364 C  C     . ASP   B 1 127 ? 68.22500  -28.92100 69.82000  1.000 16.21772 ? 126 ASP   A C     1 
ATOM   2365 O  O     . ASP   B 1 127 ? 68.60800  -29.64600 68.90300  1.000 16.63316 ? 126 ASP   A O     1 
ATOM   2366 C  CB    . ASP   B 1 127 ? 65.75600  -29.10100 70.15400  1.000 21.97048 ? 126 ASP   A CB    1 
ATOM   2367 C  CG    . ASP   B 1 127 ? 64.49000  -28.34600 70.49000  1.000 36.40335 ? 126 ASP   A CG    1 
ATOM   2368 O  OD1   . ASP   B 1 127 ? 64.57200  -27.11200 70.71900  1.000 34.39487 ? 126 ASP   A OD1   1 
ATOM   2369 O  OD2   . ASP   B 1 127 ? 63.41600  -28.98400 70.52600  1.000 39.81919 ? 126 ASP   A OD2   1 
ATOM   2370 N  N     . THR   B 1 128 ? 68.91800  -28.75200 70.95200  1.000 16.94985 ? 127 THR   A N     1 
ATOM   2371 C  CA    . THR   B 1 128 ? 70.17500  -29.46800 71.17200  1.000 20.14984 ? 127 THR   A CA    1 
ATOM   2372 C  C     . THR   B 1 128 ? 69.96800  -30.97600 71.12900  1.000 18.72275 ? 127 THR   A C     1 
ATOM   2373 O  O     . THR   B 1 128 ? 70.77700  -31.69900 70.53500  1.000 18.88445 ? 127 THR   A O     1 
ATOM   2374 C  CB    . THR   B 1 128 ? 70.79700  -29.05100 72.50400  1.000 17.72507 ? 127 THR   A CB    1 
ATOM   2375 O  OG1   . THR   B 1 128 ? 71.26700  -27.70700 72.39900  1.000 18.80022 ? 127 THR   A OG1   1 
ATOM   2376 C  CG2   . THR   B 1 128 ? 71.97900  -29.96200 72.86800  1.000 18.37438 ? 127 THR   A CG2   1 
ATOM   2377 N  N     . LYS   B 1 129 ? 68.87500  -31.46500 71.72800  1.000 21.70911 ? 128 LYS   A N     1 
ATOM   2378 C  CA    . LYS   B 1 129 ? 68.59400  -32.89900 71.69800  1.000 19.81056 ? 128 LYS   A CA    1 
ATOM   2379 C  C     . LYS   B 1 129 ? 68.46700  -33.42100 70.26900  1.000 18.84524 ? 128 LYS   A C     1 
ATOM   2380 O  O     . LYS   B 1 129 ? 68.95300  -34.51500 69.96600  1.000 17.95793 ? 128 LYS   A O     1 
ATOM   2381 C  CB    . LYS   B 1 129 ? 67.32500  -33.21900 72.48400  1.000 19.47014 ? 128 LYS   A CB    1 
ATOM   2382 C  CG    . LYS   B 1 129 ? 67.15200  -34.72200 72.75600  1.000 24.23062 ? 128 LYS   A CG    1 
ATOM   2383 C  CD    . LYS   B 1 129 ? 65.68200  -35.11700 72.95400  1.000 27.32587 ? 128 LYS   A CD    1 
ATOM   2384 C  CE    . LYS   B 1 129 ? 65.54600  -36.46400 73.68800  1.000 24.06773 ? 128 LYS   A CE    1 
ATOM   2385 N  NZ    . LYS   B 1 129 ? 66.55200  -37.49400 73.25200  1.000 27.67532 ? 128 LYS   A NZ    1 
ATOM   2386 N  N     . GLN   B 1 130 ? 67.80400  -32.66800 69.38000  1.000 20.71032 ? 129 GLN   A N     1 
ATOM   2387 C  CA    . GLN   B 1 130 ? 67.70500  -33.10300 67.98500  1.000 20.56572 ? 129 GLN   A CA    1 
ATOM   2388 C  C     . GLN   B 1 130 ? 69.08700  -33.33400 67.38100  1.000 17.43073 ? 129 GLN   A C     1 
ATOM   2389 O  O     . GLN   B 1 130 ? 69.31900  -34.34200 66.69900  1.000 15.12226 ? 129 GLN   A O     1 
ATOM   2390 C  CB    . GLN   B 1 130 ? 66.92600  -32.07700 67.14800  1.000 19.64595 ? 129 GLN   A CB    1 
ATOM   2391 C  CG    . GLN   B 1 130 ? 65.51200  -31.80100 67.64800  1.000 24.22237 ? 129 GLN   A CG    1 
ATOM   2392 C  CD    . GLN   B 1 130 ? 64.79000  -30.68800 66.88700  1.000 35.96867 ? 129 GLN   A CD    1 
ATOM   2393 O  OE1   . GLN   B 1 130 ? 65.36400  -29.63600 66.59300  1.000 28.32910 ? 129 GLN   A OE1   1 
ATOM   2394 N  NE2   . GLN   B 1 130 ? 63.50800  -30.91700 66.58000  1.000 40.99650 ? 129 GLN   A NE2   1 
ATOM   2395 N  N     . ALA   B 1 131 ? 70.01600  -32.40300 67.62400  1.000 17.12656 ? 130 ALA   A N     1 
ATOM   2396 C  CA    . ALA   B 1 131 ? 71.36500  -32.52200 67.08400  1.000 18.38838 ? 130 ALA   A CA    1 
ATOM   2397 C  C     . ALA   B 1 131 ? 72.13700  -33.65100 67.75500  1.000 13.50367 ? 130 ALA   A C     1 
ATOM   2398 O  O     . ALA   B 1 131 ? 72.86200  -34.39600 67.08600  1.000 17.43680 ? 130 ALA   A O     1 
ATOM   2399 C  CB    . ALA   B 1 131 ? 72.11100  -31.19900 67.24300  1.000 13.35737 ? 130 ALA   A CB    1 
ATOM   2400 N  N     . GLN   B 1 132 ? 72.00400  -33.78600 69.07500  1.000 14.17572 ? 131 GLN   A N     1 
ATOM   2401 C  CA    . GLN   B 1 132 ? 72.62500  -34.90700 69.77300  1.000 14.72326 ? 131 GLN   A CA    1 
ATOM   2402 C  C     . GLN   B 1 132 ? 72.13000  -36.23900 69.21600  1.000 15.41765 ? 131 GLN   A C     1 
ATOM   2403 O  O     . GLN   B 1 132 ? 72.93000  -37.11800 68.87600  1.000 15.26282 ? 131 GLN   A O     1 
ATOM   2404 C  CB    . GLN   B 1 132 ? 72.33800  -34.81400 71.27300  1.000 17.65776 ? 131 GLN   A CB    1 
ATOM   2405 C  CG    . GLN   B 1 132 ? 72.98200  -33.61500 71.94400  1.000 18.45309 ? 131 GLN   A CG    1 
ATOM   2406 C  CD    . GLN   B 1 132 ? 72.61900  -33.47900 73.41400  1.000 22.15486 ? 131 GLN   A CD    1 
ATOM   2407 O  OE1   . GLN   B 1 132 ? 71.60400  -33.99700 73.87200  1.000 18.79615 ? 131 GLN   A OE1   1 
ATOM   2408 N  NE2   . GLN   B 1 132 ? 73.46000  -32.77300 74.15900  1.000 24.46902 ? 131 GLN   A NE2   1 
ATOM   2409 N  N     . ASP   B 1 133 ? 70.81000  -36.38900 69.07700  1.000 16.30372 ? 132 ASP   A N     1 
ATOM   2410 C  CA    . ASP   B 1 133 ? 70.24700  -37.64600 68.59100  1.000 17.24515 ? 132 ASP   A CA    1 
ATOM   2411 C  C     . ASP   B 1 133 ? 70.70900  -37.96500 67.17100  1.000 16.45621 ? 132 ASP   A C     1 
ATOM   2412 O  O     . ASP   B 1 133 ? 70.99800  -39.13000 66.85300  1.000 18.68735 ? 132 ASP   A O     1 
ATOM   2413 C  CB    . ASP   B 1 133 ? 68.71600  -37.59700 68.66200  1.000 18.43842 ? 132 ASP   A CB    1 
ATOM   2414 C  CG    . ASP   B 1 133 ? 68.19700  -37.54100 70.09400  1.000 21.73862 ? 132 ASP   A CG    1 
ATOM   2415 O  OD1   . ASP   B 1 133 ? 69.00900  -37.72400 71.02300  1.000 23.87860 ? 132 ASP   A OD1   1 
ATOM   2416 O  OD2   . ASP   B 1 133 ? 66.98500  -37.29400 70.29900  1.000 20.61245 ? 132 ASP   A OD2   1 
ATOM   2417 N  N     . LEU   B 1 134 ? 70.78400  -36.95200 66.30200  1.000 15.65735 ? 133 LEU   A N     1 
ATOM   2418 C  CA    . LEU   B 1 134 ? 71.25200  -37.17500 64.93800  1.000 15.44486 ? 133 LEU   A CA    1 
ATOM   2419 C  C     . LEU   B 1 134 ? 72.69500  -37.67400 64.93200  1.000 17.33417 ? 133 LEU   A C     1 
ATOM   2420 O  O     . LEU   B 1 134 ? 73.01400  -38.70900 64.33000  1.000 15.28969 ? 133 LEU   A O     1 
ATOM   2421 C  CB    . LEU   B 1 134 ? 71.13600  -35.88100 64.12000  1.000 14.10755 ? 133 LEU   A CB    1 
ATOM   2422 C  CG    . LEU   B 1 134 ? 71.58600  -36.06400 62.66600  1.000 14.47474 ? 133 LEU   A CG    1 
ATOM   2423 C  CD1   . LEU   B 1 134 ? 70.73000  -37.10300 61.97800  1.000 18.96551 ? 133 LEU   A CD1   1 
ATOM   2424 C  CD2   . LEU   B 1 134 ? 71.55400  -34.77000 61.89100  1.000 16.84917 ? 133 LEU   A CD2   1 
ATOM   2425 N  N     . ALA   B 1 135 ? 73.57600  -36.94800 65.61800  1.000 13.68554 ? 134 ALA   A N     1 
ATOM   2426 C  CA    . ALA   B 1 135 ? 74.97200  -37.35000 65.70500  1.000 12.85983 ? 134 ALA   A CA    1 
ATOM   2427 C  C     . ALA   B 1 135 ? 75.10700  -38.76600 66.24400  1.000 16.40878 ? 134 ALA   A C     1 
ATOM   2428 O  O     . ALA   B 1 135 ? 75.86800  -39.57400 65.69700  1.000 14.42818 ? 134 ALA   A O     1 
ATOM   2429 C  CB    . ALA   B 1 135 ? 75.74000  -36.36100 66.58300  1.000 14.46926 ? 134 ALA   A CB    1 
ATOM   2430 N  N     . ARG   B 1 136 ? 74.37000  -39.09200 67.30900  1.000 14.97235 ? 135 ARG   A N     1 
ATOM   2431 C  CA    . ARG   B 1 136 ? 74.37300  -40.46000 67.81000  1.000 16.20818 ? 135 ARG   A CA    1 
ATOM   2432 C  C     . ARG   B 1 136 ? 73.97800  -41.44000 66.71100  1.000 20.04930 ? 135 ARG   A C     1 
ATOM   2433 O  O     . ARG   B 1 136 ? 74.63900  -42.46400 66.51900  1.000 19.43478 ? 135 ARG   A O     1 
ATOM   2434 C  CB    . ARG   B 1 136 ? 73.44000  -40.58600 69.02200  1.000 18.15086 ? 135 ARG   A CB    1 
ATOM   2435 C  CG    . ARG   B 1 136 ? 73.60900  -41.88000 69.78800  1.000 26.06827 ? 135 ARG   A CG    1 
ATOM   2436 C  CD    . ARG   B 1 136 ? 72.65400  -42.00400 70.96400  1.000 23.55595 ? 135 ARG   A CD    1 
ATOM   2437 N  NE    . ARG   B 1 136 ? 73.04400  -41.19600 72.11400  1.000 26.83232 ? 135 ARG   A NE    1 
ATOM   2438 C  CZ    . ARG   B 1 136 ? 74.00400  -41.52200 72.97200  1.000 32.00899 ? 135 ARG   A CZ    1 
ATOM   2439 N  NH1   . ARG   B 1 136 ? 74.74500  -42.61000 72.80500  1.000 22.81198 ? 135 ARG   A NH1   1 
ATOM   2440 N  NH2   . ARG   B 1 136 ? 74.23400  -40.73200 74.01800  1.000 28.06940 ? 135 ARG   A NH2   1 
ATOM   2441 N  N     . SER   B 1 137 ? 72.90800  -41.13200 65.96000  1.000 17.18546 ? 136 SER   A N     1 
ATOM   2442 C  CA    . SER   B 1 137 ? 72.46900  -42.04100 64.90000  1.000 20.55224 ? 136 SER   A CA    1 
ATOM   2443 C  C     . SER   B 1 137 ? 73.55300  -42.24400 63.85100  1.000 20.45168 ? 136 SER   A C     1 
ATOM   2444 O  O     . SER   B 1 137 ? 73.62800  -43.31900 63.23900  1.000 25.45084 ? 136 SER   A O     1 
ATOM   2445 C  CB    . SER   B 1 137 ? 71.18800  -41.51800 64.24400  1.000 21.13060 ? 136 SER   A CB    1 
ATOM   2446 O  OG    . SER   B 1 137 ? 71.45000  -40.38000 63.44200  1.000 21.51408 ? 136 SER   A OG    1 
ATOM   2447 N  N     . TYR   B 1 138 ? 74.41400  -41.24000 63.66000  1.000 15.33505 ? 137 TYR   A N     1 
ATOM   2448 C  CA    . TYR   B 1 138 ? 75.53500  -41.30800 62.72700  1.000 16.85967 ? 137 TYR   A CA    1 
ATOM   2449 C  C     . TYR   B 1 138 ? 76.77300  -41.94600 63.34100  1.000 20.34981 ? 137 TYR   A C     1 
ATOM   2450 O  O     . TYR   B 1 138 ? 77.69400  -42.31400 62.60000  1.000 14.36577 ? 137 TYR   A O     1 
ATOM   2451 C  CB    . TYR   B 1 138 ? 75.91400  -39.90400 62.24300  1.000 15.25024 ? 137 TYR   A CB    1 
ATOM   2452 C  CG    . TYR   B 1 138 ? 74.93500  -39.24600 61.30700  1.000 17.64557 ? 137 TYR   A CG    1 
ATOM   2453 C  CD1   . TYR   B 1 138 ? 73.95000  -39.98300 60.66700  1.000 17.93481 ? 137 TYR   A CD1   1 
ATOM   2454 C  CD2   . TYR   B 1 138 ? 75.00900  -37.87800 61.05700  1.000 13.97692 ? 137 TYR   A CD2   1 
ATOM   2455 C  CE1   . TYR   B 1 138 ? 73.05700  -39.37600 59.80500  1.000 20.09269 ? 137 TYR   A CE1   1 
ATOM   2456 C  CE2   . TYR   B 1 138 ? 74.13200  -37.26300 60.19400  1.000 15.72637 ? 137 TYR   A CE2   1 
ATOM   2457 C  CZ    . TYR   B 1 138 ? 73.14500  -38.02000 59.57500  1.000 20.17102 ? 137 TYR   A CZ    1 
ATOM   2458 O  OH    . TYR   B 1 138 ? 72.25900  -37.41200 58.71500  1.000 21.68506 ? 137 TYR   A OH    1 
ATOM   2459 N  N     . GLY   B 1 139 ? 76.81600  -42.06900 64.66800  1.000 15.05876 ? 138 GLY   A N     1 
ATOM   2460 C  CA    . GLY   B 1 139 ? 78.00100  -42.55200 65.33900  1.000 16.68626 ? 138 GLY   A CA    1 
ATOM   2461 C  C     . GLY   B 1 139 ? 79.13400  -41.55400 65.40900  1.000 15.90355 ? 138 GLY   A C     1 
ATOM   2462 O  O     . GLY   B 1 139 ? 80.30100  -41.96200 65.48800  1.000 13.94122 ? 138 GLY   A O     1 
ATOM   2463 N  N     . ILE   B 1 140 ? 78.83200  -40.26100 65.38000  1.000 13.06370 ? 139 ILE   A N     1 
ATOM   2464 C  CA    . ILE   B 1 140 ? 79.87400  -39.23700 65.32200  1.000 14.21776 ? 139 ILE   A CA    1 
ATOM   2465 C  C     . ILE   B 1 140 ? 79.67000  -38.24500 66.45800  1.000 13.27456 ? 139 ILE   A C     1 
ATOM   2466 O  O     . ILE   B 1 140 ? 78.58300  -38.16800 67.05000  1.000 14.73809 ? 139 ILE   A O     1 
ATOM   2467 C  CB    . ILE   B 1 140 ? 79.87800  -38.50700 63.96200  1.000 13.26499 ? 139 ILE   A CB    1 
ATOM   2468 C  CG1   . ILE   B 1 140 ? 78.57600  -37.71300 63.78800  1.000 13.52625 ? 139 ILE   A CG1   1 
ATOM   2469 C  CG2   . ILE   B 1 140 ? 80.09200  -39.50100 62.82400  1.000 19.03396 ? 139 ILE   A CG2   1 
ATOM   2470 C  CD1   . ILE   B 1 140 ? 78.53500  -36.92800 62.48300  1.000 12.00774 ? 139 ILE   A CD1   1 
ATOM   2471 N  N     . PRO   B 1 141 ? 80.69100  -37.45300 66.77600  1.000 14.69212 ? 140 PRO   A N     1 
ATOM   2472 C  CA    . PRO   B 1 141 ? 80.54500  -36.47100 67.85600  1.000 14.54189 ? 140 PRO   A CA    1 
ATOM   2473 C  C     . PRO   B 1 141 ? 79.67300  -35.28700 67.44300  1.000 13.73999 ? 140 PRO   A C     1 
ATOM   2474 O  O     . PRO   B 1 141 ? 79.51000  -34.96700 66.26300  1.000 11.07283 ? 140 PRO   A O     1 
ATOM   2475 C  CB    . PRO   B 1 141 ? 81.99000  -36.02500 68.13400  1.000 18.14554 ? 140 PRO   A CB    1 
ATOM   2476 C  CG    . PRO   B 1 141 ? 82.85300  -37.08800 67.54100  1.000 20.68231 ? 140 PRO   A CG    1 
ATOM   2477 C  CD    . PRO   B 1 141 ? 82.09500  -37.55400 66.33100  1.000 15.45395 ? 140 PRO   A CD    1 
ATOM   2478 N  N     . PHE   B 1 142 ? 79.10900  -34.63200 68.45500  1.000 11.11628 ? 141 PHE   A N     1 
ATOM   2479 C  CA    . PHE   B 1 142 ? 78.40800  -33.36600 68.27800  1.000 14.28717 ? 141 PHE   A CA    1 
ATOM   2480 C  C     . PHE   B 1 142 ? 78.99800  -32.34300 69.23800  1.000 16.07826 ? 141 PHE   A C     1 
ATOM   2481 O  O     . PHE   B 1 142 ? 79.18600  -32.63700 70.42000  1.000 16.33011 ? 141 PHE   A O     1 
ATOM   2482 C  CB    . PHE   B 1 142 ? 76.89700  -33.51000 68.53000  1.000 12.40733 ? 141 PHE   A CB    1 
ATOM   2483 C  CG    . PHE   B 1 142 ? 76.18100  -32.19300 68.60600  1.000 11.68069 ? 141 PHE   A CG    1 
ATOM   2484 C  CD1   . PHE   B 1 142 ? 76.11900  -31.37000 67.50000  1.000 10.45606 ? 141 PHE   A CD1   1 
ATOM   2485 C  CD2   . PHE   B 1 142 ? 75.56700  -31.78500 69.78000  1.000 16.19179 ? 141 PHE   A CD2   1 
ATOM   2486 C  CE1   . PHE   B 1 142 ? 75.47000  -30.14100 67.55900  1.000 10.43018 ? 141 PHE   A CE1   1 
ATOM   2487 C  CE2   . PHE   B 1 142 ? 74.91000  -30.56900 69.85500  1.000 13.97743 ? 141 PHE   A CE2   1 
ATOM   2488 C  CZ    . PHE   B 1 142 ? 74.86300  -29.73900 68.73800  1.000 13.20537 ? 141 PHE   A CZ    1 
ATOM   2489 N  N     . ILE   B 1 143 ? 79.28400  -31.14100 68.73900  1.000 12.28923 ? 142 ILE   A N     1 
ATOM   2490 C  CA    . ILE   B 1 143 ? 79.88200  -30.08900 69.54900  1.000 11.87775 ? 142 ILE   A CA    1 
ATOM   2491 C  C     . ILE   B 1 143 ? 79.14300  -28.79200 69.26300  1.000 15.13818 ? 142 ILE   A C     1 
ATOM   2492 O  O     . ILE   B 1 143 ? 78.95400  -28.43800 68.09400  1.000 11.06056 ? 142 ILE   A O     1 
ATOM   2493 C  CB    . ILE   B 1 143 ? 81.38200  -29.91700 69.24800  1.000 16.89920 ? 142 ILE   A CB    1 
ATOM   2494 C  CG1   . ILE   B 1 143 ? 82.09700  -31.23900 69.46000  1.000 19.28698 ? 142 ILE   A CG1   1 
ATOM   2495 C  CG2   . ILE   B 1 143 ? 81.99400  -28.86500 70.18100  1.000 19.19051 ? 142 ILE   A CG2   1 
ATOM   2496 C  CD1   . ILE   B 1 143 ? 83.44700  -31.28000 68.87500  1.000 22.15724 ? 142 ILE   A CD1   1 
ATOM   2497 N  N     . GLU   B 1 144 ? 78.74200  -28.08300 70.32100  1.000 10.71377 ? 143 GLU   A N     1 
ATOM   2498 C  CA    . GLU   B 1 144 ? 78.12300  -26.76700 70.18100  1.000 17.12684 ? 143 GLU   A CA    1 
ATOM   2499 C  C     . GLU   B 1 144 ? 79.20100  -25.69100 70.20600  1.000 14.35552 ? 143 GLU   A C     1 
ATOM   2500 O  O     . GLU   B 1 144 ? 80.08300  -25.71200 71.06600  1.000 16.47173 ? 143 GLU   A O     1 
ATOM   2501 C  CB    . GLU   B 1 144 ? 77.12500  -26.49500 71.30300  1.000 18.48386 ? 143 GLU   A CB    1 
ATOM   2502 C  CG    . GLU   B 1 144 ? 76.18800  -27.62700 71.66600  1.000 25.60220 ? 143 GLU   A CG    1 
ATOM   2503 C  CD    . GLU   B 1 144 ? 75.39800  -27.31100 72.93900  1.000 28.97090 ? 143 GLU   A CD    1 
ATOM   2504 O  OE1   . GLU   B 1 144 ? 74.80000  -26.20500 73.01400  1.000 28.77034 ? 143 GLU   A OE1   1 
ATOM   2505 O  OE2   . GLU   B 1 144 ? 75.39900  -28.15200 73.87100  1.000 27.51704 ? 143 GLU   A OE2   1 
ATOM   2506 N  N     . THR   B 1 145 ? 79.13300  -24.74700 69.26700  1.000 12.89475 ? 144 THR   A N     1 
ATOM   2507 C  CA    . THR   B 1 145 ? 80.16200  -23.72300 69.16300  1.000 11.58478 ? 144 THR   A CA    1 
ATOM   2508 C  C     . THR   B 1 145 ? 79.54400  -22.34000 69.04800  1.000 13.50913 ? 144 THR   A C     1 
ATOM   2509 O  O     . THR   B 1 145 ? 78.37500  -22.18500 68.69100  1.000 12.06152 ? 144 THR   A O     1 
ATOM   2510 C  CB    . THR   B 1 145 ? 81.06500  -23.94200 67.94800  1.000 11.43530 ? 144 THR   A CB    1 
ATOM   2511 O  OG1   . THR   B 1 145 ? 80.27900  -23.82200 66.75700  1.000 8.66136  ? 144 THR   A OG1   1 
ATOM   2512 C  CG2   . THR   B 1 145 ? 81.70300  -25.32600 68.00300  1.000 9.54451  ? 144 THR   A CG2   1 
ATOM   2513 N  N     . SER   B 1 146 ? 80.37600  -21.33800 69.32700  1.000 10.64502 ? 145 SER   A N     1 
ATOM   2514 C  CA    . SER   B 1 146 ? 80.11100  -19.96400 68.93100  1.000 11.28626 ? 145 SER   A CA    1 
ATOM   2515 C  C     . SER   B 1 146 ? 81.41900  -19.37600 68.43100  1.000 11.38330 ? 145 SER   A C     1 
ATOM   2516 O  O     . SER   B 1 146 ? 82.36100  -19.21700 69.21200  1.000 11.91638 ? 145 SER   A O     1 
ATOM   2517 C  CB    . SER   B 1 146 ? 79.55900  -19.14700 70.09600  1.000 12.79685 ? 145 SER   A CB    1 
ATOM   2518 O  OG    . SER   B 1 146 ? 79.60500  -17.77100 69.78000  1.000 12.36922 ? 145 SER   A OG    1 
ATOM   2519 N  N     . ALA   B 1 147 ? 81.49300  -19.06100 67.13600  1.000 12.08083 ? 146 ALA   A N     1 
ATOM   2520 C  CA    . ALA   B 1 147 ? 82.64300  -18.30600 66.63600  1.000 10.72363 ? 146 ALA   A CA    1 
ATOM   2521 C  C     . ALA   B 1 147 ? 82.73900  -16.92200 67.27400  1.000 13.71150 ? 146 ALA   A C     1 
ATOM   2522 O  O     . ALA   B 1 147 ? 83.83500  -16.34800 67.36500  1.000 15.37544 ? 146 ALA   A O     1 
ATOM   2523 C  CB    . ALA   B 1 147 ? 82.56000  -18.18300 65.11900  1.000 10.83050 ? 146 ALA   A CB    1 
ATOM   2524 N  N     . LYS   B 1 148 ? 81.62200  -16.38000 67.75300  1.000 12.46523 ? 147 LYS   A N     1 
ATOM   2525 C  CA    . LYS   B 1 148 ? 81.66500  -15.04600 68.34500  1.000 13.58470 ? 147 LYS   A CA    1 
ATOM   2526 C  C     . LYS   B 1 148 ? 82.35400  -15.05700 69.70300  1.000 19.06367 ? 147 LYS   A C     1 
ATOM   2527 O  O     . LYS   B 1 148 ? 83.14600  -14.15800 70.00600  1.000 19.44090 ? 147 LYS   A O     1 
ATOM   2528 C  CB    . LYS   B 1 148 ? 80.25200  -14.46700 68.46100  1.000 13.39604 ? 147 LYS   A CB    1 
ATOM   2529 C  CG    . LYS   B 1 148 ? 80.22200  -13.07900 69.11100  1.000 17.21869 ? 147 LYS   A CG    1 
ATOM   2530 C  CD    . LYS   B 1 148 ? 78.83700  -12.46200 69.05000  1.000 15.19377 ? 147 LYS   A CD    1 
ATOM   2531 C  CE    . LYS   B 1 148 ? 78.84200  -11.04400 69.61200  1.000 24.51211 ? 147 LYS   A CE    1 
ATOM   2532 N  NZ    . LYS   B 1 148 ? 77.47100  -10.57400 69.91900  1.000 26.00283 ? 147 LYS   A NZ    1 
ATOM   2533 N  N     . THR   B 1 149 ? 82.06500  -16.05500 70.54100  1.000 13.85363 ? 148 THR   A N     1 
ATOM   2534 C  CA    . THR   B 1 149 ? 82.65000  -16.11600 71.87400  1.000 18.43658 ? 148 THR   A CA    1 
ATOM   2535 C  C     . THR   B 1 149 ? 83.84000  -17.06100 71.96300  1.000 19.98471 ? 148 THR   A C     1 
ATOM   2536 O  O     . THR   B 1 149 ? 84.47400  -17.12900 73.02000  1.000 18.39847 ? 148 THR   A O     1 
ATOM   2537 C  CB    . THR   B 1 149 ? 81.61100  -16.57000 72.89700  1.000 15.32942 ? 148 THR   A CB    1 
ATOM   2538 O  OG1   . THR   B 1 149 ? 81.37100  -17.97100 72.70900  1.000 18.95787 ? 148 THR   A OG1   1 
ATOM   2539 C  CG2   . THR   B 1 149 ? 80.30000  -15.78500 72.72400  1.000 17.05758 ? 148 THR   A CG2   1 
ATOM   2540 N  N     . ARG   B 1 150 ? 84.12100  -17.80700 70.89700  1.000 14.07349 ? 149 ARG   A N     1 
ATOM   2541 C  CA    . ARG   B 1 150 ? 85.13100  -18.85000 70.78700  1.000 15.92818 ? 149 ARG   A CA    1 
ATOM   2542 C  C     . ARG   B 1 150 ? 84.76500  -20.11700 71.55900  1.000 17.32138 ? 149 ARG   A C     1 
ATOM   2543 O  O     . ARG   B 1 150 ? 85.55300  -21.07600 71.54600  1.000 15.17140 ? 149 ARG   A O     1 
ATOM   2544 C  CB    . ARG   B 1 150 ? 86.52800  -18.36900 71.21300  1.000 14.74403 ? 149 ARG   A CB    1 
ATOM   2545 C  CG    . ARG   B 1 150 ? 87.60200  -18.95200 70.32500  1.000 21.92722 ? 149 ARG   A CG    1 
ATOM   2546 C  CD    . ARG   B 1 150 ? 88.93700  -18.22500 70.41100  1.000 22.13882 ? 149 ARG   A CD    1 
ATOM   2547 N  NE    . ARG   B 1 150 ? 89.83400  -18.78900 69.41000  1.000 23.62615 ? 149 ARG   A NE    1 
ATOM   2548 C  CZ    . ARG   B 1 150 ? 90.40800  -19.97700 69.53500  1.000 24.29027 ? 149 ARG   A CZ    1 
ATOM   2549 N  NH1   . ARG   B 1 150 ? 90.28300  -20.68900 70.64600  1.000 24.50007 ? 149 ARG   A NH1   1 
ATOM   2550 N  NH2   . ARG   B 1 150 ? 91.12400  -20.46500 68.52500  1.000 25.24193 ? 149 ARG   A NH2   1 
ATOM   2551 N  N     . GLN   B 1 151 ? 83.59300  -20.17700 72.19300  1.000 16.04322 ? 150 GLN   A N     1 
ATOM   2552 C  CA    . GLN   B 1 151 ? 83.14000  -21.40400 72.84900  1.000 17.88952 ? 150 GLN   A CA    1 
ATOM   2553 C  C     . GLN   B 1 151 ? 83.19600  -22.58400 71.89500  1.000 13.44591 ? 150 GLN   A C     1 
ATOM   2554 O  O     . GLN   B 1 151 ? 82.58800  -22.54300 70.82000  1.000 12.91252 ? 150 GLN   A O     1 
ATOM   2555 C  CB    . GLN   B 1 151 ? 81.70600  -21.24100 73.36100  1.000 22.39220 ? 150 GLN   A CB    1 
ATOM   2556 C  CG    . GLN   B 1 151 ? 81.07800  -22.57100 73.81500  1.000 22.11520 ? 150 GLN   A CG    1 
ATOM   2557 C  CD    . GLN   B 1 151 ? 79.54800  -22.55000 73.80300  1.000 30.80974 ? 150 GLN   A CD    1 
ATOM   2558 O  OE1   . GLN   B 1 151 ? 78.89700  -23.59100 73.91600  1.000 28.02953 ? 150 GLN   A OE1   1 
ATOM   2559 N  NE2   . GLN   B 1 151 ? 78.97300  -21.36200 73.67200  1.000 35.11190 ? 150 GLN   A NE2   1 
ATOM   2560 N  N     . GLY   B 1 152 ? 83.93000  -23.63400 72.29100  1.000 13.51411 ? 151 GLY   A N     1 
ATOM   2561 C  CA    . GLY   B 1 152 ? 83.94700  -24.89600 71.57800  1.000 13.80527 ? 151 GLY   A CA    1 
ATOM   2562 C  C     . GLY   B 1 152 ? 84.71500  -24.93100 70.27200  1.000 11.69260 ? 151 GLY   A C     1 
ATOM   2563 O  O     . GLY   B 1 152 ? 84.73300  -25.98400 69.61600  1.000 10.02682 ? 151 GLY   A O     1 
ATOM   2564 N  N     . VAL   B 1 153 ? 85.37000  -23.83400 69.87800  1.000 14.22406 ? 152 VAL   A N     1 
ATOM   2565 C  CA    . VAL   B 1 153 ? 86.06300  -23.79400 68.59100  1.000 9.97461  ? 152 VAL   A CA    1 
ATOM   2566 C  C     . VAL   B 1 153 ? 87.22200  -24.78900 68.56100  1.000 10.01588 ? 152 VAL   A C     1 
ATOM   2567 O  O     . VAL   B 1 153 ? 87.29800  -25.65100 67.67600  1.000 11.39218 ? 152 VAL   A O     1 
ATOM   2568 C  CB    . VAL   B 1 153 ? 86.55600  -22.36900 68.28800  1.000 13.09218 ? 152 VAL   A CB    1 
ATOM   2569 C  CG1   . VAL   B 1 153 ? 87.42800  -22.37000 67.02700  1.000 11.09016 ? 152 VAL   A CG1   1 
ATOM   2570 C  CG2   . VAL   B 1 153 ? 85.37500  -21.42100 68.13500  1.000 11.91213 ? 152 VAL   A CG2   1 
ATOM   2571 N  N     . ASP   B 1 154 ? 88.16600  -24.66400 69.50000  1.000 13.09248 ? 153 ASP   A N     1 
ATOM   2572 C  CA    . ASP   B 1 154 ? 89.25800  -25.63800 69.56300  1.000 14.73940 ? 153 ASP   A CA    1 
ATOM   2573 C  C     . ASP   B 1 154 ? 88.71200  -27.06100 69.68300  1.000 15.97662 ? 153 ASP   A C     1 
ATOM   2574 O  O     . ASP   B 1 154 ? 89.15800  -27.97500 68.97600  1.000 13.66910 ? 153 ASP   A O     1 
ATOM   2575 C  CB    . ASP   B 1 154 ? 90.19700  -25.32000 70.73100  1.000 12.28354 ? 153 ASP   A CB    1 
ATOM   2576 C  CG    . ASP   B 1 154 ? 91.01200  -24.04400 70.51200  1.000 21.28234 ? 153 ASP   A CG    1 
ATOM   2577 O  OD1   . ASP   B 1 154 ? 90.99000  -23.47200 69.39700  1.000 17.79991 ? 153 ASP   A OD1   1 
ATOM   2578 O  OD2   . ASP   B 1 154 ? 91.68400  -23.60900 71.46600  1.000 23.88100 ? 153 ASP   A OD2   1 
ATOM   2579 N  N     . ASP   B 1 155 ? 87.72300  -27.26100 70.56500  1.000 13.84165 ? 154 ASP   A N     1 
ATOM   2580 C  CA    . ASP   B 1 155 ? 87.15300  -28.59300 70.76400  1.000 12.20173 ? 154 ASP   A CA    1 
ATOM   2581 C  C     . ASP   B 1 155 ? 86.62600  -29.17200 69.45900  1.000 12.20087 ? 154 ASP   A C     1 
ATOM   2582 O  O     . ASP   B 1 155 ? 86.77200  -30.37400 69.20500  1.000 12.05753 ? 154 ASP   A O     1 
ATOM   2583 C  CB    . ASP   B 1 155 ? 86.02300  -28.55100 71.79300  1.000 14.70302 ? 154 ASP   A CB    1 
ATOM   2584 C  CG    . ASP   B 1 155 ? 86.51100  -28.27400 73.20100  1.000 17.33830 ? 154 ASP   A CG    1 
ATOM   2585 O  OD1   . ASP   B 1 155 ? 87.71200  -28.48900 73.49600  1.000 18.83788 ? 154 ASP   A OD1   1 
ATOM   2586 O  OD2   . ASP   B 1 155 ? 85.67200  -27.86600 74.03200  1.000 26.02783 ? 154 ASP   A OD2   1 
ATOM   2587 N  N     . ALA   B 1 156 ? 86.00900  -28.32900 68.62100  1.000 9.74521  ? 155 ALA   A N     1 
ATOM   2588 C  CA    . ALA   B 1 156 ? 85.43500  -28.80300 67.36400  1.000 11.09375 ? 155 ALA   A CA    1 
ATOM   2589 C  C     . ALA   B 1 156 ? 86.51500  -29.36400 66.45300  1.000 9.28608  ? 155 ALA   A C     1 
ATOM   2590 O  O     . ALA   B 1 156 ? 86.44100  -30.51800 66.01500  1.000 8.87829  ? 155 ALA   A O     1 
ATOM   2591 C  CB    . ALA   B 1 156 ? 84.67100  -27.67400 66.66700  1.000 8.43623  ? 155 ALA   A CB    1 
ATOM   2592 N  N     . PHE   B 1 157 ? 87.54600  -28.57000 66.17400  1.000 9.47221  ? 156 PHE   A N     1 
ATOM   2593 C  CA    . PHE   B 1 157 ? 88.61200  -29.05000 65.29900  1.000 10.90720 ? 156 PHE   A CA    1 
ATOM   2594 C  C     . PHE   B 1 157 ? 89.42800  -30.15700 65.94800  1.000 9.06173  ? 156 PHE   A C     1 
ATOM   2595 O  O     . PHE   B 1 157 ? 89.85500  -31.09900 65.26700  1.000 11.66834 ? 156 PHE   A O     1 
ATOM   2596 C  CB    . PHE   B 1 157 ? 89.51700  -27.89600 64.89500  1.000 8.55066  ? 156 PHE   A CB    1 
ATOM   2597 C  CG    . PHE   B 1 157 ? 88.86700  -26.94300 63.95200  1.000 8.05045  ? 156 PHE   A CG    1 
ATOM   2598 C  CD1   . PHE   B 1 157 ? 88.13100  -25.88100 64.43800  1.000 8.11460  ? 156 PHE   A CD1   1 
ATOM   2599 C  CD2   . PHE   B 1 157 ? 88.98200  -27.10700 62.57700  1.000 9.66504  ? 156 PHE   A CD2   1 
ATOM   2600 C  CE1   . PHE   B 1 157 ? 87.52100  -24.98200 63.58100  1.000 10.70150 ? 156 PHE   A CE1   1 
ATOM   2601 C  CE2   . PHE   B 1 157 ? 88.37500  -26.21200 61.70800  1.000 13.47715 ? 156 PHE   A CE2   1 
ATOM   2602 C  CZ    . PHE   B 1 157 ? 87.64600  -25.14600 62.21300  1.000 13.40173 ? 156 PHE   A CZ    1 
ATOM   2603 N  N     . TYR   B 1 158 ? 89.69100  -30.05500 67.25000  1.000 9.69774  ? 157 TYR   A N     1 
ATOM   2604 C  CA    . TYR   B 1 158 ? 90.49600  -31.08800 67.89600  1.000 11.77614 ? 157 TYR   A CA    1 
ATOM   2605 C  C     . TYR   B 1 158 ? 89.75500  -32.41300 67.93900  1.000 11.04002 ? 157 TYR   A C     1 
ATOM   2606 O  O     . TYR   B 1 158 ? 90.36500  -33.47300 67.75800  1.000 10.70023 ? 157 TYR   A O     1 
ATOM   2607 C  CB    . TYR   B 1 158 ? 90.89900  -30.66500 69.30300  1.000 11.56987 ? 157 TYR   A CB    1 
ATOM   2608 C  CG    . TYR   B 1 158 ? 91.85900  -29.49600 69.36400  1.000 12.55394 ? 157 TYR   A CG    1 
ATOM   2609 C  CD1   . TYR   B 1 158 ? 92.26300  -28.82400 68.21000  1.000 11.19094 ? 157 TYR   A CD1   1 
ATOM   2610 C  CD2   . TYR   B 1 158 ? 92.34800  -29.05200 70.58500  1.000 12.70699 ? 157 TYR   A CD2   1 
ATOM   2611 C  CE1   . TYR   B 1 158 ? 93.13100  -27.75900 68.28200  1.000 12.34667 ? 157 TYR   A CE1   1 
ATOM   2612 C  CE2   . TYR   B 1 158 ? 93.21800  -27.98700 70.66000  1.000 16.78995 ? 157 TYR   A CE2   1 
ATOM   2613 C  CZ    . TYR   B 1 158 ? 93.59600  -27.34200 69.51700  1.000 17.94129 ? 157 TYR   A CZ    1 
ATOM   2614 O  OH    . TYR   B 1 158 ? 94.46400  -26.28000 69.60800  1.000 26.35481 ? 157 TYR   A OH    1 
ATOM   2615 N  N     . THR   B 1 159 ? 88.43400  -32.37400 68.16500  1.000 11.35646 ? 158 THR   A N     1 
ATOM   2616 C  CA    . THR   B 1 159 ? 87.65200  -33.60600 68.13000  1.000 10.25181 ? 158 THR   A CA    1 
ATOM   2617 C  C     . THR   B 1 159 ? 87.72100  -34.26100 66.75300  1.000 13.17648 ? 158 THR   A C     1 
ATOM   2618 O  O     . THR   B 1 159 ? 87.82400  -35.49000 66.64800  1.000 15.75316 ? 158 THR   A O     1 
ATOM   2619 C  CB    . THR   B 1 159 ? 86.20100  -33.32000 68.51100  1.000 10.16752 ? 158 THR   A CB    1 
ATOM   2620 O  OG1   . THR   B 1 159 ? 86.13200  -32.94700 69.89600  1.000 13.30712 ? 158 THR   A OG1   1 
ATOM   2621 C  CG2   . THR   B 1 159 ? 85.31400  -34.54300 68.28900  1.000 15.36664 ? 158 THR   A CG2   1 
ATOM   2622 N  N     . LEU   B 1 160 ? 87.65700  -33.45900 65.68400  1.000 9.06437  ? 159 LEU   A N     1 
ATOM   2623 C  CA    . LEU   B 1 160 ? 87.75800  -34.01500 64.33900  1.000 8.74527  ? 159 LEU   A CA    1 
ATOM   2624 C  C     . LEU   B 1 160 ? 89.11500  -34.67500 64.12400  1.000 11.35706 ? 159 LEU   A C     1 
ATOM   2625 O  O     . LEU   B 1 160 ? 89.18900  -35.77600 63.57500  1.000 10.40754 ? 159 LEU   A O     1 
ATOM   2626 C  CB    . LEU   B 1 160 ? 87.50900  -32.93900 63.29000  1.000 8.07250  ? 159 LEU   A CB    1 
ATOM   2627 C  CG    . LEU   B 1 160 ? 87.57000  -33.43200 61.84100  1.000 7.86024  ? 159 LEU   A CG    1 
ATOM   2628 C  CD1   . LEU   B 1 160 ? 86.56900  -34.58100 61.61300  1.000 8.05266  ? 159 LEU   A CD1   1 
ATOM   2629 C  CD2   . LEU   B 1 160 ? 87.32500  -32.28000 60.83300  1.000 9.59456  ? 159 LEU   A CD2   1 
ATOM   2630 N  N     . VAL   B 1 161 ? 90.19600  -34.02600 64.56100  1.000 12.15838 ? 160 VAL   A N     1 
ATOM   2631 C  CA    . VAL   B 1 161 ? 91.51800  -34.64500 64.46500  1.000 10.00052 ? 160 VAL   A CA    1 
ATOM   2632 C  C     . VAL   B 1 161 ? 91.52800  -35.97600 65.20800  1.000 10.93158 ? 160 VAL   A C     1 
ATOM   2633 O  O     . VAL   B 1 161 ? 91.99600  -36.99600 64.68700  1.000 13.08288 ? 160 VAL   A O     1 
ATOM   2634 C  CB    . VAL   B 1 161 ? 92.59500  -33.68200 64.99900  1.000 10.71638 ? 160 VAL   A CB    1 
ATOM   2635 C  CG1   . VAL   B 1 161 ? 93.94300  -34.43000 65.21700  1.000 11.22042 ? 160 VAL   A CG1   1 
ATOM   2636 C  CG2   . VAL   B 1 161 ? 92.76000  -32.52300 64.05600  1.000 9.82999  ? 160 VAL   A CG2   1 
ATOM   2637 N  N     . ARG   B 1 162 ? 90.98200  -35.99600 66.42600  1.000 12.52901 ? 161 ARG   A N     1 
ATOM   2638 C  CA    . ARG   B 1 162 ? 90.88900  -37.24700 67.16900  1.000 14.29660 ? 161 ARG   A CA    1 
ATOM   2639 C  C     . ARG   B 1 162 ? 90.08400  -38.29600 66.40200  1.000 19.41370 ? 161 ARG   A C     1 
ATOM   2640 O  O     . ARG   B 1 162 ? 90.41800  -39.49100 66.44500  1.000 20.19408 ? 161 ARG   A O     1 
ATOM   2641 C  CB    . ARG   B 1 162 ? 90.28300  -36.98900 68.55500  1.000 20.18358 ? 161 ARG   A CB    1 
ATOM   2642 C  CG    . ARG   B 1 162 ? 91.17300  -36.13700 69.47500  1.000 14.30330 ? 161 ARG   A CG    1 
ATOM   2643 C  CD    . ARG   B 1 162 ? 90.61200  -36.04200 70.90100  1.000 16.60591 ? 161 ARG   A CD    1 
ATOM   2644 N  NE    . ARG   B 1 162 ? 91.41300  -35.14900 71.73200  1.000 17.14012 ? 161 ARG   A NE    1 
ATOM   2645 C  CZ    . ARG   B 1 162 ? 91.08700  -33.89300 72.01500  1.000 20.06587 ? 161 ARG   A CZ    1 
ATOM   2646 N  NH1   . ARG   B 1 162 ? 89.92500  -33.38000 71.64400  1.000 14.81162 ? 161 ARG   A NH1   1 
ATOM   2647 N  NH2   . ARG   B 1 162 ? 91.95000  -33.13200 72.68100  1.000 21.32878 ? 161 ARG   A NH2   1 
ATOM   2648 N  N     . GLU   B 1 163 ? 89.04300  -37.87600 65.67400  1.000 13.34453 ? 162 GLU   A N     1 
ATOM   2649 C  CA    . GLU   B 1 163 ? 88.28500  -38.85300 64.90000  1.000 17.33442 ? 162 GLU   A CA    1 
ATOM   2650 C  C     . GLU   B 1 163 ? 89.11000  -39.42900 63.75600  1.000 18.56024 ? 162 GLU   A C     1 
ATOM   2651 O  O     . GLU   B 1 163 ? 88.96700  -40.60700 63.42700  1.000 16.24262 ? 162 GLU   A O     1 
ATOM   2652 C  CB    . GLU   B 1 163 ? 87.00300  -38.22900 64.36800  1.000 14.66344 ? 162 GLU   A CB    1 
ATOM   2653 C  CG    . GLU   B 1 163 ? 86.01200  -37.91900 65.46200  1.000 15.41498 ? 162 GLU   A CG    1 
ATOM   2654 C  CD    . GLU   B 1 163 ? 85.37900  -39.17200 66.05300  1.000 18.94898 ? 162 GLU   A CD    1 
ATOM   2655 O  OE1   . GLU   B 1 163 ? 84.70500  -39.91400 65.30200  1.000 16.51524 ? 162 GLU   A OE1   1 
ATOM   2656 O  OE2   . GLU   B 1 163 ? 85.55700  -39.41400 67.26500  1.000 18.50413 ? 162 GLU   A OE2   1 
ATOM   2657 N  N     . ILE   B 1 164 ? 89.95900  -38.61600 63.13000  1.000 16.82462 ? 163 ILE   A N     1 
ATOM   2658 C  CA    . ILE   B 1 164 ? 90.84600  -39.13800 62.09500  1.000 14.39973 ? 163 ILE   A CA    1 
ATOM   2659 C  C     . ILE   B 1 164 ? 91.83400  -40.12000 62.70500  1.000 21.78826 ? 163 ILE   A C     1 
ATOM   2660 O  O     . ILE   B 1 164 ? 92.13700  -41.17200 62.12100  1.000 20.95123 ? 163 ILE   A O     1 
ATOM   2661 C  CB    . ILE   B 1 164 ? 91.55800  -37.97300 61.37700  1.000 15.08364 ? 163 ILE   A CB    1 
ATOM   2662 C  CG1   . ILE   B 1 164 ? 90.53500  -37.11900 60.61800  1.000 12.56288 ? 163 ILE   A CG1   1 
ATOM   2663 C  CG2   . ILE   B 1 164 ? 92.61400  -38.48600 60.43100  1.000 17.85661 ? 163 ILE   A CG2   1 
ATOM   2664 C  CD1   . ILE   B 1 164 ? 91.07700  -35.83500 60.03500  1.000 9.95279  ? 163 ILE   A CD1   1 
ATOM   2665 N  N     . ARG   B 1 165 ? 92.33500  -39.80600 63.89900  1.000 19.46756 ? 164 ARG   A N     1 
ATOM   2666 C  CA    . ARG   B 1 165 ? 93.29000  -40.69500 64.54800  1.000 22.94821 ? 164 ARG   A CA    1 
ATOM   2667 C  C     . ARG   B 1 165 ? 92.62300  -42.00100 64.95300  1.000 24.53522 ? 164 ARG   A C     1 
ATOM   2668 O  O     . ARG   B 1 165 ? 93.18300  -43.07800 64.73600  1.000 29.76739 ? 164 ARG   A O     1 
ATOM   2669 C  CB    . ARG   B 1 165 ? 93.92900  -39.99200 65.74800  1.000 17.83585 ? 164 ARG   A CB    1 
ATOM   2670 C  CG    . ARG   B 1 165 ? 94.72300  -38.72600 65.38200  1.000 15.89583 ? 164 ARG   A CG    1 
ATOM   2671 C  CD    . ARG   B 1 165 ? 95.32500  -38.07200 66.61700  1.000 18.85655 ? 164 ARG   A CD    1 
ATOM   2672 N  NE    . ARG   B 1 165 ? 96.23100  -36.96300 66.32200  1.000 17.74847 ? 164 ARG   A NE    1 
ATOM   2673 C  CZ    . ARG   B 1 165 ? 96.66000  -36.10200 67.23900  1.000 19.44441 ? 164 ARG   A CZ    1 
ATOM   2674 N  NH1   . ARG   B 1 165 ? 96.25700  -36.17700 68.49800  1.000 19.85780 ? 164 ARG   A NH1   1 
ATOM   2675 N  NH2   . ARG   B 1 165 ? 97.50700  -35.13800 66.88500  1.000 19.09084 ? 164 ARG   A NH2   1 
ATOM   2676 N  N     . LYS   B 1 166 ? 91.40900  -41.93000 65.50700  1.000 26.83509 ? 165 LYS   A N     1 
ATOM   2677 C  CA    . LYS   B 1 166 ? 90.69000  -43.15700 65.84300  1.000 28.36930 ? 165 LYS   A CA    1 
ATOM   2678 C  C     . LYS   B 1 166 ? 90.32900  -43.95400 64.59700  1.000 31.36623 ? 165 LYS   A C     1 
ATOM   2679 O  O     . LYS   B 1 166 ? 90.31400  -45.19200 64.63400  1.000 30.68127 ? 165 LYS   A O     1 
ATOM   2680 C  CB    . LYS   B 1 166 ? 89.43200  -42.82600 66.64400  1.000 33.95844 ? 165 LYS   A CB    1 
ATOM   2681 C  CG    . LYS   B 1 166 ? 89.70400  -42.48600 68.09800  1.000 35.82322 ? 165 LYS   A CG    1 
ATOM   2682 C  CD    . LYS   B 1 166 ? 88.65400  -41.53000 68.65100  1.000 37.38242 ? 165 LYS   A CD    1 
ATOM   2683 C  CE    . LYS   B 1 166 ? 87.37600  -42.25400 69.06100  1.000 44.37887 ? 165 LYS   A CE    1 
ATOM   2684 N  NZ    . LYS   B 1 166 ? 86.53800  -42.69000 67.90200  1.000 45.80450 ? 165 LYS   A NZ    1 
ATOM   2685 N  N     . HIS   B 1 167 ? 90.03600  -43.26800 63.48900  1.000 31.83953 ? 166 HIS   A N     1 
ATOM   2686 C  CA    . HIS   B 1 167 ? 89.73000  -43.96700 62.24600  1.000 30.47125 ? 166 HIS   A CA    1 
ATOM   2687 C  C     . HIS   B 1 167 ? 90.93700  -44.74600 61.74600  1.000 30.43187 ? 166 HIS   A C     1 
ATOM   2688 O  O     . HIS   B 1 167 ? 90.80000  -45.88800 61.28300  1.000 27.06250 ? 166 HIS   A O     1 
ATOM   2689 C  CB    . HIS   B 1 167 ? 89.26000  -42.97100 61.19200  1.000 26.32102 ? 166 HIS   A CB    1 
ATOM   2690 C  CG    . HIS   B 1 167 ? 89.15600  -43.54600 59.81600  1.000 27.29628 ? 166 HIS   A CG    1 
ATOM   2691 N  ND1   . HIS   B 1 167 ? 90.14200  -43.38300 58.86600  1.000 29.27576 ? 166 HIS   A ND1   1 
ATOM   2692 C  CD2   . HIS   B 1 167 ? 88.17600  -44.26700 59.22300  1.000 29.37475 ? 166 HIS   A CD2   1 
ATOM   2693 C  CE1   . HIS   B 1 167 ? 89.77700  -43.98700 57.74900  1.000 27.08553 ? 166 HIS   A CE1   1 
ATOM   2694 N  NE2   . HIS   B 1 167 ? 88.58700  -44.52900 57.93800  1.000 29.81796 ? 166 HIS   A NE2   1 
ATOM   2695 N  N     . LYS   B 1 168 ? 92.12700  -44.15100 61.84400  1.000 28.15909 ? 167 LYS   A N     1 
ATOM   2696 C  CA    . LYS   B 1 168 ? 93.33200  -44.84200 61.41600  1.000 31.96277 ? 167 LYS   A CA    1 
ATOM   2697 C  C     . LYS   B 1 168 ? 93.68900  -46.00800 62.33000  1.000 36.18983 ? 167 LYS   A C     1 
ATOM   2698 O  O     . LYS   B 1 168 ? 94.41600  -46.91100 61.90000  1.000 37.11214 ? 167 LYS   A O     1 
ATOM   2699 C  CB    . LYS   B 1 168 ? 94.49300  -43.85600 61.31700  1.000 28.47133 ? 167 LYS   A CB    1 
ATOM   2700 C  CG    . LYS   B 1 168 ? 94.34000  -42.84200 60.19400  1.000 26.01365 ? 167 LYS   A CG    1 
ATOM   2701 C  CD    . LYS   B 1 168 ? 95.66800  -42.22500 59.87300  1.000 26.56050 ? 167 LYS   A CD    1 
ATOM   2702 C  CE    . LYS   B 1 168 ? 95.62100  -40.73300 59.93000  1.000 23.98904 ? 167 LYS   A CE    1 
ATOM   2703 N  NZ    . LYS   B 1 168 ? 97.00200  -40.17600 59.75900  1.000 22.16738 ? 167 LYS   A NZ    1 
ATOM   2704 N  N     . GLU   B 1 169 ? 93.18900  -46.03000 63.56500  1.000 34.59029 ? 168 GLU   A N     1 
ATOM   2705 C  CA    . GLU   B 1 169 ? 93.33400  -47.24200 64.38300  1.000 33.52278 ? 168 GLU   A CA    1 
ATOM   2706 C  C     . GLU   B 1 169 ? 92.53000  -48.38300 63.78000  1.000 26.50961 ? 168 GLU   A C     1 
ATOM   2707 O  O     . GLU   B 1 169 ? 92.84400  -49.55100 64.01200  1.000 30.27434 ? 168 GLU   A O     1 
ATOM   2708 C  CB    . GLU   B 1 169 ? 92.87700  -47.00600 65.82300  1.000 36.06585 ? 168 GLU   A CB    1 
ATOM   2709 C  CG    . GLU   B 1 169 ? 93.71400  -46.01300 66.60300  1.000 38.88901 ? 168 GLU   A CG    1 
ATOM   2710 C  CD    . GLU   B 1 169 ? 93.03800  -45.59700 67.89200  1.000 44.64937 ? 168 GLU   A CD    1 
ATOM   2711 O  OE1   . GLU   B 1 169 ? 91.82600  -45.87200 68.04000  1.000 50.27109 ? 168 GLU   A OE1   1 
ATOM   2712 O  OE2   . GLU   B 1 169 ? 93.71600  -44.99600 68.75500  1.000 48.01704 ? 168 GLU   A OE2   1 
ATOM   2713 N  N     . VAL   C 2 3   ? 37.09600  -51.73000 31.77200  1.000 37.27187 ? 2   VAL   C N     1 
ATOM   2714 C  CA    . VAL   C 2 3   ? 36.50200  -52.51800 30.70500  1.000 29.97770 ? 2   VAL   C CA    1 
ATOM   2715 C  C     . VAL   C 2 3   ? 36.84800  -51.98200 29.31900  1.000 27.03931 ? 2   VAL   C C     1 
ATOM   2716 O  O     . VAL   C 2 3   ? 36.41200  -52.55400 28.32200  1.000 28.32446 ? 2   VAL   C O     1 
ATOM   2717 C  CB    . VAL   C 2 3   ? 34.97400  -52.60200 30.86100  1.000 35.85695 ? 2   VAL   C CB    1 
ATOM   2718 C  CG1   . VAL   C 2 3   ? 34.60300  -53.38100 32.11800  1.000 47.13029 ? 2   VAL   C CG1   1 
ATOM   2719 C  CG2   . VAL   C 2 3   ? 34.37100  -51.20100 30.89000  1.000 39.91382 ? 2   VAL   C CG2   1 
ATOM   2720 N  N     . ASN   C 2 4   ? 37.60700  -50.88300 29.23200  1.000 25.28421 ? 3   ASN   C N     1 
ATOM   2721 C  CA    . ASN   C 2 4   ? 38.05500  -50.42800 27.92000  1.000 20.25505 ? 3   ASN   C CA    1 
ATOM   2722 C  C     . ASN   C 2 4   ? 38.99800  -51.46200 27.31200  1.000 18.75518 ? 3   ASN   C C     1 
ATOM   2723 O  O     . ASN   C 2 4   ? 39.87200  -51.98500 28.00400  1.000 18.24837 ? 3   ASN   C O     1 
ATOM   2724 C  CB    . ASN   C 2 4   ? 38.77200  -49.08300 28.00200  1.000 20.16711 ? 3   ASN   C CB    1 
ATOM   2725 C  CG    . ASN   C 2 4   ? 37.81800  -47.91600 28.10100  1.000 18.94094 ? 3   ASN   C CG    1 
ATOM   2726 O  OD1   . ASN   C 2 4   ? 36.69300  -47.95900 27.59600  1.000 19.57865 ? 3   ASN   C OD1   1 
ATOM   2727 N  ND2   . ASN   C 2 4   ? 38.25400  -46.87500 28.77500  1.000 16.39629 ? 3   ASN   C ND2   1 
ATOM   2728 N  N     . PRO   C 2 5   ? 38.85900  -51.76800 26.02600  1.000 18.78839 ? 4   PRO   C N     1 
ATOM   2729 C  CA    . PRO   C 2 5   ? 39.74100  -52.76900 25.41900  1.000 17.58558 ? 4   PRO   C CA    1 
ATOM   2730 C  C     . PRO   C 2 5   ? 41.17500  -52.26700 25.30200  1.000 16.93435 ? 4   PRO   C C     1 
ATOM   2731 O  O     . PRO   C 2 5   ? 41.43100  -51.06700 25.23400  1.000 15.46697 ? 4   PRO   C O     1 
ATOM   2732 C  CB    . PRO   C 2 5   ? 39.12400  -53.00600 24.03700  1.000 19.69858 ? 4   PRO   C CB    1 
ATOM   2733 C  CG    . PRO   C 2 5   ? 38.31800  -51.76800 23.73900  1.000 18.08897 ? 4   PRO   C CG    1 
ATOM   2734 C  CD    . PRO   C 2 5   ? 37.86200  -51.23000 25.08100  1.000 18.01212 ? 4   PRO   C CD    1 
ATOM   2735 N  N     . THR   C 2 6   ? 42.11400  -53.21500 25.29300  1.000 14.15559 ? 5   THR   C N     1 
ATOM   2736 C  CA    . THR   C 2 6   ? 43.52700  -52.97100 25.01400  1.000 13.63376 ? 5   THR   C CA    1 
ATOM   2737 C  C     . THR   C 2 6   ? 43.92200  -53.70700 23.73900  1.000 12.74090 ? 5   THR   C C     1 
ATOM   2738 O  O     . THR   C 2 6   ? 43.58600  -54.88200 23.56400  1.000 15.57288 ? 5   THR   C O     1 
ATOM   2739 C  CB    . THR   C 2 6   ? 44.42700  -53.44700 26.17600  1.000 15.30420 ? 5   THR   C CB    1 
ATOM   2740 O  OG1   . THR   C 2 6   ? 44.00000  -52.82400 27.39700  1.000 22.41593 ? 5   THR   C OG1   1 
ATOM   2741 C  CG2   . THR   C 2 6   ? 45.90000  -53.08500 25.90500  1.000 16.98630 ? 5   THR   C CG2   1 
ATOM   2742 N  N     . VAL   C 2 7   ? 44.63300  -53.02000 22.84300  1.000 11.59505 ? 6   VAL   C N     1 
ATOM   2743 C  CA    . VAL   C 2 7   ? 45.18300  -53.65500 21.65000  1.000 11.73597 ? 6   VAL   C CA    1 
ATOM   2744 C  C     . VAL   C 2 7   ? 46.69500  -53.46700 21.64900  1.000 12.09949 ? 6   VAL   C C     1 
ATOM   2745 O  O     . VAL   C 2 7   ? 47.23200  -52.55700 22.28000  1.000 13.44843 ? 6   VAL   C O     1 
ATOM   2746 C  CB    . VAL   C 2 7   ? 44.57500  -53.10600 20.34400  1.000 17.13124 ? 6   VAL   C CB    1 
ATOM   2747 C  CG1   . VAL   C 2 7   ? 43.13000  -53.57300 20.16800  1.000 16.33546 ? 6   VAL   C CG1   1 
ATOM   2748 C  CG2   . VAL   C 2 7   ? 44.66500  -51.60000 20.31700  1.000 15.29462 ? 6   VAL   C CG2   1 
ATOM   2749 N  N     . PHE   C 2 8   ? 47.38400  -54.33600 20.91700  1.000 11.92298 ? 7   PHE   C N     1 
ATOM   2750 C  CA    . PHE   C 2 8   ? 48.83700  -54.29600 20.82900  1.000 14.09670 ? 7   PHE   C CA    1 
ATOM   2751 C  C     . PHE   C 2 8   ? 49.25500  -54.18300 19.37100  1.000 12.77303 ? 7   PHE   C C     1 
ATOM   2752 O  O     . PHE   C 2 8   ? 48.60000  -54.74200 18.49000  1.000 13.40368 ? 7   PHE   C O     1 
ATOM   2753 C  CB    . PHE   C 2 8   ? 49.49000  -55.53700 21.47800  1.000 16.68137 ? 7   PHE   C CB    1 
ATOM   2754 C  CG    . PHE   C 2 8   ? 49.38400  -56.80500 20.65300  1.000 12.78252 ? 7   PHE   C CG    1 
ATOM   2755 C  CD1   . PHE   C 2 8   ? 50.36100  -57.13800 19.72800  1.000 16.03973 ? 7   PHE   C CD1   1 
ATOM   2756 C  CD2   . PHE   C 2 8   ? 48.31200  -57.66200 20.81000  1.000 13.78864 ? 7   PHE   C CD2   1 
ATOM   2757 C  CE1   . PHE   C 2 8   ? 50.26100  -58.29400 18.97400  1.000 12.41514 ? 7   PHE   C CE1   1 
ATOM   2758 C  CE2   . PHE   C 2 8   ? 48.21600  -58.82800 20.06000  1.000 18.33400 ? 7   PHE   C CE2   1 
ATOM   2759 C  CZ    . PHE   C 2 8   ? 49.18800  -59.13000 19.13400  1.000 16.67729 ? 7   PHE   C CZ    1 
ATOM   2760 N  N     . PHE   C 2 9   ? 50.32200  -53.42300 19.12900  1.000 12.39422 ? 8   PHE   C N     1 
ATOM   2761 C  CA    . PHE   C 2 9   ? 51.07300  -53.44900 17.87900  1.000 13.26403 ? 8   PHE   C CA    1 
ATOM   2762 C  C     . PHE   C 2 9   ? 52.47600  -53.95000 18.18500  1.000 12.54385 ? 8   PHE   C C     1 
ATOM   2763 O  O     . PHE   C 2 9   ? 53.13000  -53.43100 19.10000  1.000 10.65612 ? 8   PHE   C O     1 
ATOM   2764 C  CB    . PHE   C 2 9   ? 51.22800  -52.06300 17.23400  1.000 8.17331  ? 8   PHE   C CB    1 
ATOM   2765 C  CG    . PHE   C 2 9   ? 49.97900  -51.47200 16.65800  1.000 10.01209 ? 8   PHE   C CG    1 
ATOM   2766 C  CD1   . PHE   C 2 9   ? 48.80000  -52.19700 16.54900  1.000 13.47378 ? 8   PHE   C CD1   1 
ATOM   2767 C  CD2   . PHE   C 2 9   ? 50.00100  -50.16100 16.18900  1.000 13.33941 ? 8   PHE   C CD2   1 
ATOM   2768 C  CE1   . PHE   C 2 9   ? 47.66200  -51.60700 15.99400  1.000 10.53295 ? 8   PHE   C CE1   1 
ATOM   2769 C  CE2   . PHE   C 2 9   ? 48.87500  -49.57800 15.64200  1.000 13.17000 ? 8   PHE   C CE2   1 
ATOM   2770 C  CZ    . PHE   C 2 9   ? 47.70300  -50.31000 15.54100  1.000 10.05837 ? 8   PHE   C CZ    1 
ATOM   2771 N  N     . ASP   C 2 10  ? 52.96000  -54.89800 17.38400  1.000 11.69257 ? 9   ASP   C N     1 
ATOM   2772 C  CA    . ASP   C 2 10  ? 54.37400  -55.25700 17.36500  1.000 10.99859 ? 9   ASP   C CA    1 
ATOM   2773 C  C     . ASP   C 2 10  ? 54.98500  -54.57900 16.14900  1.000 11.57591 ? 9   ASP   C C     1 
ATOM   2774 O  O     . ASP   C 2 10  ? 54.62400  -54.89300 15.00600  1.000 12.33275 ? 9   ASP   C O     1 
ATOM   2775 C  CB    . ASP   C 2 10  ? 54.56100  -56.77500 17.33700  1.000 14.87335 ? 9   ASP   C CB    1 
ATOM   2776 C  CG    . ASP   C 2 10  ? 54.21700  -57.40900 18.65700  1.000 17.78302 ? 9   ASP   C CG    1 
ATOM   2777 O  OD1   . ASP   C 2 10  ? 54.59300  -56.80700 19.69800  1.000 15.81474 ? 9   ASP   C OD1   1 
ATOM   2778 O  OD2   . ASP   C 2 10  ? 53.53500  -58.47200 18.66800  1.000 18.16903 ? 9   ASP   C OD2   1 
ATOM   2779 N  N     . ILE   C 2 11  ? 55.86800  -53.61200 16.41100  1.000 9.75147  ? 10  ILE   C N     1 
ATOM   2780 C  CA    . ILE   C 2 11  ? 56.44700  -52.72800 15.40500  1.000 11.07362 ? 10  ILE   C CA    1 
ATOM   2781 C  C     . ILE   C 2 11  ? 57.71000  -53.36700 14.86700  1.000 10.05520 ? 10  ILE   C C     1 
ATOM   2782 O  O     . ILE   C 2 11  ? 58.47200  -53.97700 15.62200  1.000 10.87205 ? 10  ILE   C O     1 
ATOM   2783 C  CB    . ILE   C 2 11  ? 56.74900  -51.33900 16.00100  1.000 9.21266  ? 10  ILE   C CB    1 
ATOM   2784 C  CG1   . ILE   C 2 11  ? 55.48800  -50.75300 16.65200  1.000 13.28488 ? 10  ILE   C CG1   1 
ATOM   2785 C  CG2   . ILE   C 2 11  ? 57.31800  -50.40500 14.93400  1.000 11.48026 ? 10  ILE   C CG2   1 
ATOM   2786 C  CD1   . ILE   C 2 11  ? 54.30300  -50.56400 15.69700  1.000 11.52691 ? 10  ILE   C CD1   1 
ATOM   2787 N  N     . ALA   C 2 12  ? 57.92800  -53.23300 13.55600  1.000 11.40613 ? 11  ALA   C N     1 
ATOM   2788 C  CA    . ALA   C 2 12  ? 59.10000  -53.78300 12.88600  1.000 12.04691 ? 11  ALA   C CA    1 
ATOM   2789 C  C     . ALA   C 2 12  ? 59.79500  -52.68600 12.09100  1.000 10.77765 ? 11  ALA   C C     1 
ATOM   2790 O  O     . ALA   C 2 12  ? 59.16200  -51.73600 11.63300  1.000 11.66786 ? 11  ALA   C O     1 
ATOM   2791 C  CB    . ALA   C 2 12  ? 58.73300  -54.95500 11.95600  1.000 13.44062 ? 11  ALA   C CB    1 
ATOM   2792 N  N     . VAL   C 2 13  ? 61.11000  -52.81300 11.95200  1.000 11.41616 ? 12  VAL   C N     1 
ATOM   2793 C  CA    . VAL   C 2 13  ? 61.92500  -51.88900 11.16400  1.000 12.22276 ? 12  VAL   C CA    1 
ATOM   2794 C  C     . VAL   C 2 13  ? 62.56400  -52.73200 10.07900  1.000 13.76148 ? 12  VAL   C C     1 
ATOM   2795 O  O     . VAL   C 2 13  ? 63.40300  -53.59300 10.37600  1.000 13.99907 ? 12  VAL   C O     1 
ATOM   2796 C  CB    . VAL   C 2 13  ? 62.99500  -51.17500 12.00400  1.000 16.61241 ? 12  VAL   C CB    1 
ATOM   2797 C  CG1   . VAL   C 2 13  ? 63.83800  -50.24800 11.13900  1.000 19.30144 ? 12  VAL   C CG1   1 
ATOM   2798 C  CG2   . VAL   C 2 13  ? 62.37700  -50.41700 13.14100  1.000 13.31409 ? 12  VAL   C CG2   1 
ATOM   2799 N  N     . ASP   C 2 14  ? 62.16500  -52.50200 8.82700   1.000 14.30380 ? 13  ASP   C N     1 
ATOM   2800 C  CA    . ASP   C 2 14  ? 62.61800  -53.33000 7.71000   1.000 16.37244 ? 13  ASP   C CA    1 
ATOM   2801 C  C     . ASP   C 2 14  ? 62.47300  -54.80900 8.05300   1.000 13.99393 ? 13  ASP   C C     1 
ATOM   2802 O  O     . ASP   C 2 14  ? 63.34900  -55.62700 7.76300   1.000 19.10960 ? 13  ASP   C O     1 
ATOM   2803 C  CB    . ASP   C 2 14  ? 64.06200  -53.00300 7.31700   1.000 20.55205 ? 13  ASP   C CB    1 
ATOM   2804 C  CG    . ASP   C 2 14  ? 64.19100  -51.66100 6.62100   1.000 20.94191 ? 13  ASP   C CG    1 
ATOM   2805 O  OD1   . ASP   C 2 14  ? 63.17500  -51.15600 6.11400   1.000 21.46738 ? 13  ASP   C OD1   1 
ATOM   2806 O  OD2   . ASP   C 2 14  ? 65.31100  -51.11700 6.56900   1.000 20.56326 ? 13  ASP   C OD2   1 
ATOM   2807 N  N     . GLY   C 2 15  ? 61.37500  -55.14300 8.72600   1.000 13.47569 ? 14  GLY   C N     1 
ATOM   2808 C  CA    . GLY   C 2 15  ? 61.09400  -56.50700 9.11400   1.000 15.65364 ? 14  GLY   C CA    1 
ATOM   2809 C  C     . GLY   C 2 15  ? 61.67300  -56.94600 10.44300  1.000 16.84032 ? 14  GLY   C C     1 
ATOM   2810 O  O     . GLY   C 2 15  ? 61.28400  -58.01500 10.94000  1.000 18.71109 ? 14  GLY   C O     1 
ATOM   2811 N  N     . GLU   C 2 16  ? 62.59500  -56.17200 11.03500  1.000 14.18482 ? 15  GLU   C N     1 
ATOM   2812 C  CA    . GLU   C 2 16  ? 63.16200  -56.61100 12.31200  1.000 14.87323 ? 15  GLU   C CA    1 
ATOM   2813 C  C     . GLU   C 2 16  ? 62.35300  -56.06500 13.48400  1.000 14.03413 ? 15  GLU   C C     1 
ATOM   2814 O  O     . GLU   C 2 16  ? 61.99000  -54.89000 13.48900  1.000 17.19155 ? 15  GLU   C O     1 
ATOM   2815 C  CB    . GLU   C 2 16  ? 64.61600  -56.16100 12.45400  1.000 15.74837 ? 15  GLU   C CB    1 
ATOM   2816 C  CG    . GLU   C 2 16  ? 65.60400  -56.94300 11.58200  1.000 17.05130 ? 15  GLU   C CG    1 
ATOM   2817 C  CD    . GLU   C 2 16  ? 65.79800  -58.38500 12.04200  1.000 18.18662 ? 15  GLU   C CD    1 
ATOM   2818 O  OE1   . GLU   C 2 16  ? 65.52200  -58.70300 13.21900  1.000 18.23853 ? 15  GLU   C OE1   1 
ATOM   2819 O  OE2   . GLU   C 2 16  ? 66.24100  -59.20500 11.22300  1.000 19.16948 ? 15  GLU   C OE2   1 
ATOM   2820 N  N     . PRO   C 2 17  ? 62.10500  -56.88100 14.50900  1.000 16.74986 ? 16  PRO   C N     1 
ATOM   2821 C  CA    . PRO   C 2 17  ? 61.27700  -56.42300 15.63000  1.000 15.72798 ? 16  PRO   C CA    1 
ATOM   2822 C  C     . PRO   C 2 17  ? 61.91000  -55.22800 16.31500  1.000 17.21293 ? 16  PRO   C C     1 
ATOM   2823 O  O     . PRO   C 2 17  ? 63.09300  -55.23800 16.65400  1.000 17.53773 ? 16  PRO   C O     1 
ATOM   2824 C  CB    . PRO   C 2 17  ? 61.22600  -57.63800 16.56400  1.000 18.05779 ? 16  PRO   C CB    1 
ATOM   2825 C  CG    . PRO   C 2 17  ? 61.54700  -58.79400 15.69400  1.000 23.90927 ? 16  PRO   C CG    1 
ATOM   2826 C  CD    . PRO   C 2 17  ? 62.51500  -58.28400 14.66700  1.000 18.58965 ? 16  PRO   C CD    1 
ATOM   2827 N  N     . LEU   C 2 18  ? 61.10800  -54.18800 16.50300  1.000 13.01275 ? 17  LEU   C N     1 
ATOM   2828 C  CA    . LEU   C 2 18  ? 61.52300  -53.04800 17.30700  1.000 16.04427 ? 17  LEU   C CA    1 
ATOM   2829 C  C     . LEU   C 2 18  ? 61.00200  -53.17700 18.73600  1.000 16.28938 ? 17  LEU   C C     1 
ATOM   2830 O  O     . LEU   C 2 18  ? 61.77200  -53.09600 19.69100  1.000 15.63716 ? 17  LEU   C O     1 
ATOM   2831 C  CB    . LEU   C 2 18  ? 61.02700  -51.75100 16.66400  1.000 14.03980 ? 17  LEU   C CB    1 
ATOM   2832 C  CG    . LEU   C 2 18  ? 61.52600  -50.42800 17.21700  1.000 13.36960 ? 17  LEU   C CG    1 
ATOM   2833 C  CD1   . LEU   C 2 18  ? 63.02900  -50.27400 16.96200  1.000 12.50197 ? 17  LEU   C CD1   1 
ATOM   2834 C  CD2   . LEU   C 2 18  ? 60.75100  -49.26500 16.61500  1.000 12.15240 ? 17  LEU   C CD2   1 
ATOM   2835 N  N     . GLY   C 2 19  ? 59.70400  -53.40100 18.89100  1.000 14.38969 ? 18  GLY   C N     1 
ATOM   2836 C  CA    . GLY   C 2 19  ? 59.11400  -53.58600 20.20000  1.000 12.54348 ? 18  GLY   C CA    1 
ATOM   2837 C  C     . GLY   C 2 19  ? 57.60700  -53.51500 20.09100  1.000 13.20683 ? 18  GLY   C C     1 
ATOM   2838 O  O     . GLY   C 2 19  ? 57.04600  -53.36400 19.00500  1.000 11.50089 ? 18  GLY   C O     1 
ATOM   2839 N  N     . ARG   C 2 20  ? 56.96000  -53.61600 21.24700  1.000 12.05154 ? 19  ARG   C N     1 
ATOM   2840 C  CA    . ARG   C 2 20  ? 55.50400  -53.62900 21.31700  1.000 11.54805 ? 19  ARG   C CA    1 
ATOM   2841 C  C     . ARG   C 2 20  ? 55.00500  -52.29100 21.84600  1.000 14.31930 ? 19  ARG   C C     1 
ATOM   2842 O  O     . ARG   C 2 20  ? 55.63100  -51.69600 22.73200  1.000 13.60524 ? 19  ARG   C O     1 
ATOM   2843 C  CB    . ARG   C 2 20  ? 55.02200  -54.78400 22.20600  1.000 14.93970 ? 19  ARG   C CB    1 
ATOM   2844 C  CG    . ARG   C 2 20  ? 53.52000  -54.79800 22.47000  1.000 14.44457 ? 19  ARG   C CG    1 
ATOM   2845 C  CD    . ARG   C 2 20  ? 53.04900  -56.12200 23.07400  1.000 13.35753 ? 19  ARG   C CD    1 
ATOM   2846 N  NE    . ARG   C 2 20  ? 53.07400  -57.20100 22.09400  1.000 15.67253 ? 19  ARG   C NE    1 
ATOM   2847 C  CZ    . ARG   C 2 20  ? 52.42500  -58.34700 22.24100  1.000 17.98734 ? 19  ARG   C CZ    1 
ATOM   2848 N  NH1   . ARG   C 2 20  ? 51.71000  -58.59800 23.33000  1.000 15.44956 ? 19  ARG   C NH1   1 
ATOM   2849 N  NH2   . ARG   C 2 20  ? 52.50800  -59.27200 21.28400  1.000 14.50839 ? 19  ARG   C NH2   1 
ATOM   2850 N  N     . VAL   C 2 21  ? 53.90500  -51.80500 21.26500  1.000 10.18046 ? 20  VAL   C N     1 
ATOM   2851 C  CA    . VAL   C 2 21  ? 53.14900  -50.66100 21.76600  1.000 10.53510 ? 20  VAL   C CA    1 
ATOM   2852 C  C     . VAL   C 2 21  ? 51.74700  -51.17200 22.05000  1.000 14.46673 ? 20  VAL   C C     1 
ATOM   2853 O  O     . VAL   C 2 21  ? 51.15100  -51.83100 21.19300  1.000 14.10277 ? 20  VAL   C O     1 
ATOM   2854 C  CB    . VAL   C 2 21  ? 53.08300  -49.50900 20.74300  1.000 10.92052 ? 20  VAL   C CB    1 
ATOM   2855 C  CG1   . VAL   C 2 21  ? 52.26700  -48.34500 21.29700  1.000 12.89045 ? 20  VAL   C CG1   1 
ATOM   2856 C  CG2   . VAL   C 2 21  ? 54.48800  -49.04100 20.31100  1.000 10.85630 ? 20  VAL   C CG2   1 
ATOM   2857 N  N     . SER   C 2 22  ? 51.22800  -50.90200 23.24400  1.000 10.43782 ? 21  SER   C N     1 
ATOM   2858 C  CA    . SER   C 2 22  ? 49.83400  -51.21700 23.52600  1.000 10.63989 ? 21  SER   C CA    1 
ATOM   2859 C  C     . SER   C 2 22  ? 49.02300  -49.93800 23.71800  1.000 10.25022 ? 21  SER   C C     1 
ATOM   2860 O  O     . SER   C 2 22  ? 49.55800  -48.88800 24.07400  1.000 12.85480 ? 21  SER   C O     1 
ATOM   2861 C  CB    . SER   C 2 22  ? 49.70000  -52.14000 24.75000  1.000 12.93059 ? 21  SER   C CB    1 
ATOM   2862 O  OG    . SER   C 2 22  ? 50.05800  -51.50900 25.96200  1.000 16.85459 ? 21  SER   C OG    1 
ATOM   2863 N  N     . PHE   C 2 23  ? 47.72500  -50.03100 23.47400  1.000 10.17505 ? 22  PHE   C N     1 
ATOM   2864 C  CA    . PHE   C 2 23  ? 46.83300  -48.88100 23.54300  1.000 9.91100  ? 22  PHE   C CA    1 
ATOM   2865 C  C     . PHE   C 2 23  ? 45.62600  -49.23300 24.39600  1.000 12.15634 ? 22  PHE   C C     1 
ATOM   2866 O  O     . PHE   C 2 23  ? 45.09900  -50.34500 24.29500  1.000 14.26865 ? 22  PHE   C O     1 
ATOM   2867 C  CB    . PHE   C 2 23  ? 46.34800  -48.45700 22.15600  1.000 9.68768  ? 22  PHE   C CB    1 
ATOM   2868 C  CG    . PHE   C 2 23  ? 47.44500  -48.28600 21.14000  1.000 11.44213 ? 22  PHE   C CG    1 
ATOM   2869 C  CD1   . PHE   C 2 23  ? 48.08100  -47.05900 20.98300  1.000 13.39183 ? 22  PHE   C CD1   1 
ATOM   2870 C  CD2   . PHE   C 2 23  ? 47.81000  -49.34100 20.31700  1.000 15.30289 ? 22  PHE   C CD2   1 
ATOM   2871 C  CE1   . PHE   C 2 23  ? 49.07600  -46.88400 20.03600  1.000 12.56919 ? 22  PHE   C CE1   1 
ATOM   2872 C  CE2   . PHE   C 2 23  ? 48.80400  -49.18600 19.35300  1.000 12.11681 ? 22  PHE   C CE2   1 
ATOM   2873 C  CZ    . PHE   C 2 23  ? 49.44600  -47.95700 19.21700  1.000 14.10139 ? 22  PHE   C CZ    1 
ATOM   2874 N  N     . GLU   C 2 24  ? 45.20900  -48.30400 25.25500  1.000 11.16814 ? 23  GLU   C N     1 
ATOM   2875 C  CA    . GLU   C 2 24  ? 43.85600  -48.32100 25.79500  1.000 12.29431 ? 23  GLU   C CA    1 
ATOM   2876 C  C     . GLU   C 2 24  ? 42.93200  -47.60100 24.81800  1.000 14.29045 ? 23  GLU   C C     1 
ATOM   2877 O  O     . GLU   C 2 24  ? 43.24300  -46.49600 24.36900  1.000 11.77738 ? 23  GLU   C O     1 
ATOM   2878 C  CB    . GLU   C 2 24  ? 43.78700  -47.64700 27.16600  1.000 18.46873 ? 23  GLU   C CB    1 
ATOM   2879 C  CG    . GLU   C 2 24  ? 42.38800  -47.67200 27.77300  1.000 16.23005 ? 23  GLU   C CG    1 
ATOM   2880 C  CD    . GLU   C 2 24  ? 42.28000  -46.82600 29.03400  1.000 19.58580 ? 23  GLU   C CD    1 
ATOM   2881 O  OE1   . GLU   C 2 24  ? 43.32700  -46.33400 29.51700  1.000 19.28205 ? 23  GLU   C OE1   1 
ATOM   2882 O  OE2   . GLU   C 2 24  ? 41.14800  -46.65100 29.53700  1.000 19.04818 ? 23  GLU   C OE2   1 
ATOM   2883 N  N     . LEU   C 2 25  ? 41.81900  -48.23900 24.46300  1.000 11.57879 ? 24  LEU   C N     1 
ATOM   2884 C  CA    . LEU   C 2 25  ? 40.83300  -47.64600 23.56400  1.000 16.13808 ? 24  LEU   C CA    1 
ATOM   2885 C  C     . LEU   C 2 25  ? 39.64600  -47.14300 24.37600  1.000 13.44148 ? 24  LEU   C C     1 
ATOM   2886 O  O     . LEU   C 2 25  ? 39.06600  -47.89400 25.16600  1.000 15.27978 ? 24  LEU   C O     1 
ATOM   2887 C  CB    . LEU   C 2 25  ? 40.36000  -48.65200 22.51300  1.000 12.60199 ? 24  LEU   C CB    1 
ATOM   2888 C  CG    . LEU   C 2 25  ? 41.45100  -49.35100 21.69500  1.000 14.06870 ? 24  LEU   C CG    1 
ATOM   2889 C  CD1   . LEU   C 2 25  ? 40.84300  -50.18100 20.56000  1.000 10.45084 ? 24  LEU   C CD1   1 
ATOM   2890 C  CD2   . LEU   C 2 25  ? 42.46400  -48.36100 21.16300  1.000 10.78119 ? 24  LEU   C CD2   1 
ATOM   2891 N  N     . PHE   C 2 26  ? 39.28200  -45.87500 24.17500  1.000 13.73686 ? 25  PHE   C N     1 
ATOM   2892 C  CA    . PHE   C 2 26  ? 38.26300  -45.22700 25.00000  1.000 12.95256 ? 25  PHE   C CA    1 
ATOM   2893 C  C     . PHE   C 2 26  ? 36.85000  -45.56100 24.52100  1.000 15.54586 ? 25  PHE   C C     1 
ATOM   2894 O  O     . PHE   C 2 26  ? 36.07500  -44.69200 24.12700  1.000 15.96212 ? 25  PHE   C O     1 
ATOM   2895 C  CB    . PHE   C 2 26  ? 38.48100  -43.72400 25.00800  1.000 13.81053 ? 25  PHE   C CB    1 
ATOM   2896 C  CG    . PHE   C 2 26  ? 39.81800  -43.31000 25.53100  1.000 12.31197 ? 25  PHE   C CG    1 
ATOM   2897 C  CD1   . PHE   C 2 26  ? 40.43000  -44.01400 26.55100  1.000 13.88789 ? 25  PHE   C CD1   1 
ATOM   2898 C  CD2   . PHE   C 2 26  ? 40.45800  -42.19300 25.01400  1.000 12.29125 ? 25  PHE   C CD2   1 
ATOM   2899 C  CE1   . PHE   C 2 26  ? 41.66400  -43.61900 27.03700  1.000 17.19071 ? 25  PHE   C CE1   1 
ATOM   2900 C  CE2   . PHE   C 2 26  ? 41.68100  -41.78300 25.50400  1.000 14.28880 ? 25  PHE   C CE2   1 
ATOM   2901 C  CZ    . PHE   C 2 26  ? 42.29300  -42.50600 26.50800  1.000 15.41395 ? 25  PHE   C CZ    1 
ATOM   2902 N  N     . ALA   C 2 27  ? 36.51200  -46.85000 24.57600  1.000 16.51686 ? 26  ALA   C N     1 
ATOM   2903 C  CA    . ALA   C 2 27  ? 35.15200  -47.24300 24.22200  1.000 17.16893 ? 26  ALA   C CA    1 
ATOM   2904 C  C     . ALA   C 2 27  ? 34.12700  -46.65200 25.17000  1.000 17.48305 ? 26  ALA   C C     1 
ATOM   2905 O  O     . ALA   C 2 27  ? 32.96700  -46.50400 24.77800  1.000 16.79950 ? 26  ALA   C O     1 
ATOM   2906 C  CB    . ALA   C 2 27  ? 35.00200  -48.76200 24.20200  1.000 15.96443 ? 26  ALA   C CB    1 
ATOM   2907 N  N     . ASP   C 2 28  ? 34.52700  -46.31000 26.40000  1.000 16.71832 ? 27  ASP   C N     1 
ATOM   2908 C  CA    . ASP   C 2 28  ? 33.58100  -45.71100 27.33400  1.000 21.29136 ? 27  ASP   C CA    1 
ATOM   2909 C  C     . ASP   C 2 28  ? 33.10400  -44.34100 26.85700  1.000 24.01930 ? 27  ASP   C C     1 
ATOM   2910 O  O     . ASP   C 2 28  ? 31.96500  -43.95400 27.13300  1.000 26.86936 ? 27  ASP   C O     1 
ATOM   2911 C  CB    . ASP   C 2 28  ? 34.18900  -45.63200 28.74500  1.000 18.85687 ? 27  ASP   C CB    1 
ATOM   2912 C  CG    . ASP   C 2 28  ? 35.49800  -44.83800 28.80200  1.000 20.43479 ? 27  ASP   C CG    1 
ATOM   2913 O  OD1   . ASP   C 2 28  ? 36.16300  -44.66300 27.75900  1.000 17.71975 ? 27  ASP   C OD1   1 
ATOM   2914 O  OD2   . ASP   C 2 28  ? 35.87200  -44.40300 29.91700  1.000 22.62366 ? 27  ASP   C OD2   1 
ATOM   2915 N  N     . LYS   C 2 29  ? 33.92900  -43.60900 26.10700  1.000 19.68750 ? 28  LYS   C N     1 
ATOM   2916 C  CA    . LYS   C 2 29  ? 33.55200  -42.27000 25.68100  1.000 23.39470 ? 28  LYS   C CA    1 
ATOM   2917 C  C     . LYS   C 2 29  ? 33.41300  -42.11800 24.17400  1.000 17.17831 ? 28  LYS   C C     1 
ATOM   2918 O  O     . LYS   C 2 29  ? 32.73900  -41.18700 23.72500  1.000 20.45185 ? 28  LYS   C O     1 
ATOM   2919 C  CB    . LYS   C 2 29  ? 34.57400  -41.23800 26.18800  1.000 24.15281 ? 28  LYS   C CB    1 
ATOM   2920 C  CG    . LYS   C 2 29  ? 34.05100  -40.32700 27.31100  1.000 28.17215 ? 28  LYS   C CG    1 
ATOM   2921 C  CD    . LYS   C 2 29  ? 34.50200  -40.76800 28.69900  1.000 34.33092 ? 28  LYS   C CD    1 
ATOM   2922 C  CE    . LYS   C 2 29  ? 34.13200  -39.71800 29.76900  1.000 38.95312 ? 28  LYS   C CE    1 
ATOM   2923 N  NZ    . LYS   C 2 29  ? 34.74000  -39.99200 31.11900  1.000 38.65628 ? 28  LYS   C NZ    1 
ATOM   2924 N  N     . VAL   C 2 30  ? 34.04200  -42.98600 23.39000  1.000 14.46694 ? 29  VAL   C N     1 
ATOM   2925 C  CA    . VAL   C 2 30  ? 34.06300  -42.88100 21.93100  1.000 13.58214 ? 29  VAL   C CA    1 
ATOM   2926 C  C     . VAL   C 2 30  ? 33.82900  -44.27700 21.35500  1.000 17.01661 ? 29  VAL   C C     1 
ATOM   2927 O  O     . VAL   C 2 30  ? 34.71300  -44.82900 20.67600  1.000 15.12443 ? 29  VAL   C O     1 
ATOM   2928 C  CB    . VAL   C 2 30  ? 35.39000  -42.27000 21.44000  1.000 19.44414 ? 29  VAL   C CB    1 
ATOM   2929 C  CG1   . VAL   C 2 30  ? 35.18600  -41.52200 20.15600  1.000 19.78864 ? 29  VAL   C CG1   1 
ATOM   2930 C  CG2   . VAL   C 2 30  ? 36.00800  -41.34200 22.49900  1.000 16.59596 ? 29  VAL   C CG2   1 
ATOM   2931 N  N     . PRO   C 2 31  ? 32.65000  -44.87600 21.58300  1.000 16.82554 ? 30  PRO   C N     1 
ATOM   2932 C  CA    . PRO   C 2 31  ? 32.49200  -46.32300 21.31900  1.000 16.30652 ? 30  PRO   C CA    1 
ATOM   2933 C  C     . PRO   C 2 31  ? 32.66900  -46.73600 19.87100  1.000 14.24640 ? 30  PRO   C C     1 
ATOM   2934 O  O     . PRO   C 2 31  ? 33.29200  -47.77200 19.62500  1.000 15.67317 ? 30  PRO   C O     1 
ATOM   2935 C  CB    . PRO   C 2 31  ? 31.06100  -46.61200 21.79500  1.000 16.64525 ? 30  PRO   C CB    1 
ATOM   2936 C  CG    . PRO   C 2 31  ? 30.36600  -45.25300 21.75200  1.000 17.01082 ? 30  PRO   C CG    1 
ATOM   2937 C  CD    . PRO   C 2 31  ? 31.44000  -44.30000 22.19200  1.000 16.47208 ? 30  PRO   C CD    1 
ATOM   2938 N  N     . LYS   C 2 32  ? 32.10500  -45.99800 18.90900  1.000 15.44905 ? 31  LYS   C N     1 
ATOM   2939 C  CA    . LYS   C 2 32  ? 32.16700  -46.43700 17.51500  1.000 14.32727 ? 31  LYS   C CA    1 
ATOM   2940 C  C     . LYS   C 2 32  ? 33.57200  -46.30000 16.94500  1.000 17.86839 ? 31  LYS   C C     1 
ATOM   2941 O  O     . LYS   C 2 32  ? 34.01200  -47.14900 16.16300  1.000 13.40541 ? 31  LYS   C O     1 
ATOM   2942 C  CB    . LYS   C 2 32  ? 31.18500  -45.63800 16.65200  1.000 17.25708 ? 31  LYS   C CB    1 
ATOM   2943 C  CG    . LYS   C 2 32  ? 29.78400  -45.52000 17.20600  1.000 22.69256 ? 31  LYS   C CG    1 
ATOM   2944 C  CD    . LYS   C 2 32  ? 28.98300  -44.48600 16.41000  1.000 26.72050 ? 31  LYS   C CD    1 
ATOM   2945 C  CE    . LYS   C 2 32  ? 27.58100  -44.31900 16.94500  1.000 30.32362 ? 31  LYS   C CE    1 
ATOM   2946 N  NZ    . LYS   C 2 32  ? 26.76500  -45.53700 16.72000  1.000 39.40994 ? 31  LYS   C NZ    1 
ATOM   2947 N  N     . THR   C 2 33  ? 34.27300  -45.22100 17.29300  1.000 11.66017 ? 32  THR   C N     1 
ATOM   2948 C  CA    . THR   C 2 33  ? 35.63200  -45.02900 16.80000  1.000 11.93893 ? 32  THR   C CA    1 
ATOM   2949 C  C     . THR   C 2 33  ? 36.58700  -46.03400 17.43900  1.000 11.51187 ? 32  THR   C C     1 
ATOM   2950 O  O     . THR   C 2 33  ? 37.43900  -46.60900 16.75500  1.000 10.70466 ? 32  THR   C O     1 
ATOM   2951 C  CB    . THR   C 2 33  ? 36.07400  -43.58700 17.06200  1.000 12.19117 ? 32  THR   C CB    1 
ATOM   2952 O  OG1   . THR   C 2 33  ? 35.07500  -42.68100 16.56000  1.000 12.50274 ? 32  THR   C OG1   1 
ATOM   2953 C  CG2   . THR   C 2 33  ? 37.40400  -43.28300 16.37400  1.000 11.76672 ? 32  THR   C CG2   1 
ATOM   2954 N  N     . ALA   C 2 34  ? 36.42400  -46.30700 18.73700  1.000 11.76637 ? 33  ALA   C N     1 
ATOM   2955 C  CA    . ALA   C 2 34  ? 37.26800  -47.31600 19.37900  1.000 10.76870 ? 33  ALA   C CA    1 
ATOM   2956 C  C     . ALA   C 2 34  ? 37.03000  -48.70600 18.79000  1.000 14.62973 ? 33  ALA   C C     1 
ATOM   2957 O  O     . ALA   C 2 34  ? 37.97100  -49.50300 18.66100  1.000 10.71965 ? 33  ALA   C O     1 
ATOM   2958 C  CB    . ALA   C 2 34  ? 37.01700  -47.32600 20.88500  1.000 11.62561 ? 33  ALA   C CB    1 
ATOM   2959 N  N     . GLU   C 2 35  ? 35.77500  -49.01000 18.42400  1.000 12.85088 ? 34  GLU   C N     1 
ATOM   2960 C  CA    . GLU   C 2 35  ? 35.44300  -50.33400 17.90200  1.000 14.34577 ? 34  GLU   C CA    1 
ATOM   2961 C  C     . GLU   C 2 35  ? 36.03900  -50.55300 16.51900  1.000 13.86429 ? 34  GLU   C C     1 
ATOM   2962 O  O     . GLU   C 2 35  ? 36.47300  -51.66700 16.19300  1.000 13.42139 ? 34  GLU   C O     1 
ATOM   2963 C  CB    . GLU   C 2 35  ? 33.92100  -50.52000 17.87100  1.000 13.67299 ? 34  GLU   C CB    1 
ATOM   2964 C  CG    . GLU   C 2 35  ? 33.44000  -51.76400 17.12200  1.000 16.25113 ? 34  GLU   C CG    1 
ATOM   2965 C  CD    . GLU   C 2 35  ? 33.94400  -53.07900 17.72200  1.000 16.38972 ? 34  GLU   C CD    1 
ATOM   2966 O  OE1   . GLU   C 2 35  ? 34.46300  -53.08100 18.85600  1.000 18.21793 ? 34  GLU   C OE1   1 
ATOM   2967 O  OE2   . GLU   C 2 35  ? 33.79000  -54.12200 17.05700  1.000 15.58724 ? 34  GLU   C OE2   1 
ATOM   2968 N  N     . ASN   C 2 36  ? 36.04400  -49.50600 15.69100  1.000 11.02428 ? 35  ASN   C N     1 
ATOM   2969 C  CA    . ASN   C 2 36  ? 36.74200  -49.55000 14.41100  1.000 12.36777 ? 35  ASN   C CA    1 
ATOM   2970 C  C     . ASN   C 2 36  ? 38.20200  -49.95200 14.60600  1.000 12.89890 ? 35  ASN   C C     1 
ATOM   2971 O  O     . ASN   C 2 36  ? 38.66800  -50.95800 14.05000  1.000 9.65676  ? 35  ASN   C O     1 
ATOM   2972 C  CB    . ASN   C 2 36  ? 36.62800  -48.17600 13.73200  1.000 10.04575 ? 35  ASN   C CB    1 
ATOM   2973 C  CG    . ASN   C 2 36  ? 37.27000  -48.13900 12.35500  1.000 9.88169  ? 35  ASN   C CG    1 
ATOM   2974 O  OD1   . ASN   C 2 36  ? 36.98500  -48.96600 11.50000  1.000 9.73103  ? 35  ASN   C OD1   1 
ATOM   2975 N  ND2   . ASN   C 2 36  ? 38.18700  -47.19900 12.16100  1.000 12.73639 ? 35  ASN   C ND2   1 
ATOM   2976 N  N     . PHE   C 2 37  ? 38.92000  -49.20100 15.44100  1.000 9.11585  ? 36  PHE   C N     1 
ATOM   2977 C  CA    . PHE   C 2 37  ? 40.33800  -49.47000 15.65700  1.000 8.64031  ? 36  PHE   C CA    1 
ATOM   2978 C  C     . PHE   C 2 37  ? 40.55700  -50.84800 16.27100  1.000 9.12092  ? 36  PHE   C C     1 
ATOM   2979 O  O     . PHE   C 2 37  ? 41.49700  -51.56100 15.89500  1.000 10.26004 ? 36  PHE   C O     1 
ATOM   2980 C  CB    . PHE   C 2 37  ? 40.91900  -48.37600 16.54300  1.000 10.09629 ? 36  PHE   C CB    1 
ATOM   2981 C  CG    . PHE   C 2 37  ? 42.41300  -48.34400 16.56100  1.000 9.34802  ? 36  PHE   C CG    1 
ATOM   2982 C  CD1   . PHE   C 2 37  ? 43.11800  -49.10300 17.47300  1.000 10.78514 ? 36  PHE   C CD1   1 
ATOM   2983 C  CD2   . PHE   C 2 37  ? 43.10600  -47.54000 15.67700  1.000 10.63362 ? 36  PHE   C CD2   1 
ATOM   2984 C  CE1   . PHE   C 2 37  ? 44.50900  -49.06800 17.50500  1.000 11.26932 ? 36  PHE   C CE1   1 
ATOM   2985 C  CE2   . PHE   C 2 37  ? 44.49000  -47.49700 15.69500  1.000 11.71034 ? 36  PHE   C CE2   1 
ATOM   2986 C  CZ    . PHE   C 2 37  ? 45.19500  -48.26500 16.61500  1.000 9.39842  ? 36  PHE   C CZ    1 
ATOM   2987 N  N     . ARG   C 2 38  ? 39.69600  -51.24400 17.21400  1.000 11.34779 ? 37  ARG   C N     1 
ATOM   2988 C  CA    . ARG   C 2 38  ? 39.77800  -52.58500 17.78900  1.000 11.90850 ? 37  ARG   C CA    1 
ATOM   2989 C  C     . ARG   C 2 38  ? 39.68200  -53.65200 16.70600  1.000 14.69016 ? 37  ARG   C C     1 
ATOM   2990 O  O     . ARG   C 2 38  ? 40.53600  -54.55000 16.61100  1.000 11.27677 ? 37  ARG   C O     1 
ATOM   2991 C  CB    . ARG   C 2 38  ? 38.65700  -52.78400 18.81200  1.000 12.23904 ? 37  ARG   C CB    1 
ATOM   2992 C  CG    . ARG   C 2 38  ? 38.84100  -54.03500 19.67700  1.000 14.01128 ? 37  ARG   C CG    1 
ATOM   2993 C  CD    . ARG   C 2 38  ? 37.53600  -54.51500 20.33800  1.000 14.13208 ? 37  ARG   C CD    1 
ATOM   2994 N  NE    . ARG   C 2 38  ? 36.50800  -54.83500 19.34700  1.000 15.65985 ? 37  ARG   C NE    1 
ATOM   2995 C  CZ    . ARG   C 2 38  ? 36.51500  -55.91800 18.57800  1.000 16.74673 ? 37  ARG   C CZ    1 
ATOM   2996 N  NH1   . ARG   C 2 38  ? 37.47400  -56.82500 18.66700  1.000 16.90481 ? 37  ARG   C NH1   1 
ATOM   2997 N  NH2   . ARG   C 2 38  ? 35.53700  -56.09500 17.69300  1.000 15.38615 ? 37  ARG   C NH2   1 
ATOM   2998 N  N     . ALA   C 2 39  ? 38.63500  -53.56700 15.87800  1.000 11.99316 ? 38  ALA   C N     1 
ATOM   2999 C  CA    . ALA   C 2 39  ? 38.39400  -54.59600 14.87300  1.000 12.70536 ? 38  ALA   C CA    1 
ATOM   3000 C  C     . ALA   C 2 39  ? 39.47700  -54.58500 13.79900  1.000 11.31906 ? 38  ALA   C C     1 
ATOM   3001 O  O     . ALA   C 2 39  ? 39.89600  -55.64900 13.32500  1.000 13.25086 ? 38  ALA   C O     1 
ATOM   3002 C  CB    . ALA   C 2 39  ? 37.00100  -54.40800 14.25500  1.000 12.41105 ? 38  ALA   C CB    1 
ATOM   3003 N  N     . LEU   C 2 40  ? 39.95800  -53.39600 13.41700  1.000 11.18150 ? 39  LEU   C N     1 
ATOM   3004 C  CA    . LEU   C 2 40  ? 41.06600  -53.33100 12.46600  1.000 12.24647 ? 39  LEU   C CA    1 
ATOM   3005 C  C     . LEU   C 2 40  ? 42.32300  -53.95900 13.05200  1.000 10.38540 ? 39  LEU   C C     1 
ATOM   3006 O  O     . LEU   C 2 40  ? 43.14000  -54.51600 12.30700  1.000 12.51363 ? 39  LEU   C O     1 
ATOM   3007 C  CB    . LEU   C 2 40  ? 41.32400  -51.87900 12.03300  1.000 9.70743  ? 39  LEU   C CB    1 
ATOM   3008 C  CG    . LEU   C 2 40  ? 40.17000  -51.20400 11.25600  1.000 10.95027 ? 39  LEU   C CG    1 
ATOM   3009 C  CD1   . LEU   C 2 40  ? 40.44400  -49.75000 10.95900  1.000 12.62418 ? 39  LEU   C CD1   1 
ATOM   3010 C  CD2   . LEU   C 2 40  ? 39.84900  -51.97000 9.95000   1.000 15.93683 ? 39  LEU   C CD2   1 
ATOM   3011 N  N     . SER   C 2 41  ? 42.47000  -53.92100 14.38400  1.000 10.72691 ? 40  SER   C N     1 
ATOM   3012 C  CA    . SER   C 2 41  ? 43.66300  -54.46900 15.01900  1.000 13.00268 ? 40  SER   C CA    1 
ATOM   3013 C  C     . SER   C 2 41  ? 43.60500  -55.98800 15.08800  1.000 11.23367 ? 40  SER   C C     1 
ATOM   3014 O  O     . SER   C 2 41  ? 44.63500  -56.65700 14.94700  1.000 12.55544 ? 40  SER   C O     1 
ATOM   3015 C  CB    . SER   C 2 41  ? 43.84300  -53.87700 16.41600  1.000 13.75846 ? 40  SER   C CB    1 
ATOM   3016 O  OG    . SER   C 2 41  ? 44.09700  -52.49900 16.33900  1.000 9.51459  ? 40  SER   C OG    1 
ATOM   3017 N  N     . THR   C 2 42  ? 42.41000  -56.55400 15.28800  1.000 11.24243 ? 41  THR   C N     1 
ATOM   3018 C  CA    . THR   C 2 42  ? 42.26600  -58.01000 15.28800  1.000 15.29655 ? 41  THR   C CA    1 
ATOM   3019 C  C     . THR   C 2 42  ? 42.22400  -58.60400 13.88700  1.000 14.72499 ? 41  THR   C C     1 
ATOM   3020 O  O     . THR   C 2 42  ? 42.52100  -59.79700 13.72600  1.000 17.54309 ? 41  THR   C O     1 
ATOM   3021 C  CB    . THR   C 2 42  ? 40.99600  -58.44800 16.02300  1.000 16.11553 ? 41  THR   C CB    1 
ATOM   3022 O  OG1   . THR   C 2 42  ? 39.84300  -58.01900 15.28800  1.000 14.66532 ? 41  THR   C OG1   1 
ATOM   3023 C  CG2   . THR   C 2 42  ? 40.93800  -57.89400 17.44300  1.000 15.11196 ? 41  THR   C CG2   1 
ATOM   3024 N  N     . GLY   C 2 43  ? 41.84900  -57.81800 12.88300  1.000 11.97366 ? 42  GLY   C N     1 
ATOM   3025 C  CA    . GLY   C 2 43  ? 41.62100  -58.35300 11.55700  1.000 12.38680 ? 42  GLY   C CA    1 
ATOM   3026 C  C     . GLY   C 2 43  ? 40.35100  -59.17100 11.40300  1.000 14.61025 ? 42  GLY   C C     1 
ATOM   3027 O  O     . GLY   C 2 43  ? 40.20600  -59.88200 10.40100  1.000 19.63670 ? 42  GLY   C O     1 
ATOM   3028 N  N     . GLU   C 2 44  ? 39.41700  -59.09500 12.35900  1.000 14.03663 ? 43  GLU   C N     1 
ATOM   3029 C  CA    . GLU   C 2 44  ? 38.30900  -60.05400 12.38400  1.000 15.45381 ? 43  GLU   C CA    1 
ATOM   3030 C  C     . GLU   C 2 44  ? 37.31700  -59.85900 11.24400  1.000 17.30683 ? 43  GLU   C C     1 
ATOM   3031 O  O     . GLU   C 2 44  ? 36.49600  -60.75300 10.99400  1.000 17.16187 ? 43  GLU   C O     1 
ATOM   3032 C  CB    . GLU   C 2 44  ? 37.57600  -59.97700 13.71900  1.000 18.80053 ? 43  GLU   C CB    1 
ATOM   3033 C  CG    . GLU   C 2 44  ? 36.95900  -58.62100 13.99100  1.000 15.30548 ? 43  GLU   C CG    1 
ATOM   3034 C  CD    . GLU   C 2 44  ? 36.52900  -58.48200 15.43400  1.000 22.86100 ? 43  GLU   C CD    1 
ATOM   3035 O  OE1   . GLU   C 2 44  ? 37.41500  -58.54000 16.32100  1.000 17.91693 ? 43  GLU   C OE1   1 
ATOM   3036 O  OE2   . GLU   C 2 44  ? 35.30800  -58.34400 15.67900  1.000 16.59734 ? 43  GLU   C OE2   1 
ATOM   3037 N  N     . LYS   C 2 45  ? 37.35600  -58.71200 10.57000  1.000 15.05808 ? 44  LYS   C N     1 
ATOM   3038 C  CA    . LYS   C 2 45  ? 36.50100  -58.44700 9.42200   1.000 15.29666 ? 44  LYS   C CA    1 
ATOM   3039 C  C     . LYS   C 2 45  ? 37.11900  -58.92100 8.11400   1.000 19.66987 ? 44  LYS   C C     1 
ATOM   3040 O  O     . LYS   C 2 45  ? 36.48400  -58.78200 7.06500   1.000 16.66811 ? 44  LYS   C O     1 
ATOM   3041 C  CB    . LYS   C 2 45  ? 36.19400  -56.94900 9.32400   1.000 17.20603 ? 44  LYS   C CB    1 
ATOM   3042 C  CG    . LYS   C 2 45  ? 35.58100  -56.34600 10.57700  1.000 16.25367 ? 44  LYS   C CG    1 
ATOM   3043 C  CD    . LYS   C 2 45  ? 34.22500  -56.96200 10.89300  1.000 18.72969 ? 44  LYS   C CD    1 
ATOM   3044 C  CE    . LYS   C 2 45  ? 33.54700  -56.24300 12.06300  1.000 23.42743 ? 44  LYS   C CE    1 
ATOM   3045 N  NZ    . LYS   C 2 45  ? 32.28400  -56.91500 12.50000  1.000 27.38387 ? 44  LYS   C NZ    1 
ATOM   3046 N  N     . GLY   C 2 46  ? 38.33700  -59.46600 8.15200   1.000 17.92334 ? 45  GLY   C N     1 
ATOM   3047 C  CA    . GLY   C 2 46  ? 39.02500  -59.88300 6.94500   1.000 21.70684 ? 45  GLY   C CA    1 
ATOM   3048 C  C     . GLY   C 2 46  ? 39.96500  -58.85700 6.35000   1.000 21.70428 ? 45  GLY   C C     1 
ATOM   3049 O  O     . GLY   C 2 46  ? 40.48500  -59.08600 5.25100   1.000 25.10043 ? 45  GLY   C O     1 
ATOM   3050 N  N     . PHE   C 2 47  ? 40.17200  -57.72700 7.02300   1.000 14.88643 ? 46  PHE   C N     1 
ATOM   3051 C  CA    . PHE   C 2 47  ? 41.14400  -56.71500 6.63100   1.000 12.37420 ? 46  PHE   C CA    1 
ATOM   3052 C  C     . PHE   C 2 47  ? 41.57300  -55.96800 7.88700   1.000 12.23602 ? 46  PHE   C C     1 
ATOM   3053 O  O     . PHE   C 2 47  ? 40.91600  -56.04800 8.92800   1.000 13.58035 ? 46  PHE   C O     1 
ATOM   3054 C  CB    . PHE   C 2 47  ? 40.57100  -55.75800 5.57200   1.000 11.88962 ? 46  PHE   C CB    1 
ATOM   3055 C  CG    . PHE   C 2 47  ? 39.21600  -55.18800 5.92800   1.000 16.41900 ? 46  PHE   C CG    1 
ATOM   3056 C  CD1   . PHE   C 2 47  ? 39.10600  -54.03600 6.68700   1.000 16.12627 ? 46  PHE   C CD1   1 
ATOM   3057 C  CD2   . PHE   C 2 47  ? 38.06000  -55.81200 5.50400   1.000 16.61954 ? 46  PHE   C CD2   1 
ATOM   3058 C  CE1   . PHE   C 2 47  ? 37.85400  -53.50800 7.01400   1.000 14.51457 ? 46  PHE   C CE1   1 
ATOM   3059 C  CE2   . PHE   C 2 47  ? 36.80000  -55.28800 5.82100   1.000 20.02589 ? 46  PHE   C CE2   1 
ATOM   3060 C  CZ    . PHE   C 2 47  ? 36.71000  -54.14100 6.58300   1.000 15.22580 ? 46  PHE   C CZ    1 
ATOM   3061 N  N     . GLY   C 2 48  ? 42.68700  -55.25100 7.79500   1.000 12.38335 ? 47  GLY   C N     1 
ATOM   3062 C  CA    . GLY   C 2 48  ? 43.07300  -54.42100 8.92200   1.000 9.94768  ? 47  GLY   C CA    1 
ATOM   3063 C  C     . GLY   C 2 48  ? 44.54500  -54.04100 8.86400   1.000 11.88107 ? 47  GLY   C C     1 
ATOM   3064 O  O     . GLY   C 2 48  ? 45.16700  -54.05900 7.80200   1.000 11.17507 ? 47  GLY   C O     1 
ATOM   3065 N  N     . TYR   C 2 49  ? 45.07400  -53.70100 10.04000  1.000 11.53519 ? 48  TYR   C N     1 
ATOM   3066 C  CA    . TYR   C 2 49  ? 46.36100  -53.01300 10.15700  1.000 9.41345  ? 48  TYR   C CA    1 
ATOM   3067 C  C     . TYR   C 2 49  ? 47.56300  -53.92200 9.98200   1.000 10.40940 ? 48  TYR   C C     1 
ATOM   3068 O  O     . TYR   C 2 49  ? 48.66400  -53.42500 9.71200   1.000 8.17609  ? 48  TYR   C O     1 
ATOM   3069 C  CB    . TYR   C 2 49  ? 46.47700  -52.35200 11.52600  1.000 8.56485  ? 48  TYR   C CB    1 
ATOM   3070 C  CG    . TYR   C 2 49  ? 45.54200  -51.19500 11.74500  1.000 9.47827  ? 48  TYR   C CG    1 
ATOM   3071 C  CD1   . TYR   C 2 49  ? 45.37300  -50.21300 10.77700  1.000 12.10506 ? 48  TYR   C CD1   1 
ATOM   3072 C  CD2   . TYR   C 2 49  ? 44.82500  -51.08300 12.92700  1.000 12.65264 ? 48  TYR   C CD2   1 
ATOM   3073 C  CE1   . TYR   C 2 49  ? 44.51100  -49.14500 10.98700  1.000 11.08582 ? 48  TYR   C CE1   1 
ATOM   3074 C  CE2   . TYR   C 2 49  ? 43.97500  -50.03200 13.14200  1.000 11.55913 ? 48  TYR   C CE2   1 
ATOM   3075 C  CZ    . TYR   C 2 49  ? 43.81600  -49.06800 12.18200  1.000 8.99801  ? 48  TYR   C CZ    1 
ATOM   3076 O  OH    . TYR   C 2 49  ? 42.96000  -48.02000 12.43600  1.000 9.14018  ? 48  TYR   C OH    1 
ATOM   3077 N  N     . LYS   C 2 50  ? 47.39900  -55.22400 10.16400  1.000 13.12122 ? 49  LYS   C N     1 
ATOM   3078 C  CA    . LYS   C 2 50  ? 48.55500  -56.10800 10.19500  1.000 9.33761  ? 49  LYS   C CA    1 
ATOM   3079 C  C     . LYS   C 2 50  ? 49.26700  -56.09700 8.85100   1.000 11.76072 ? 49  LYS   C C     1 
ATOM   3080 O  O     . LYS   C 2 50  ? 48.67600  -56.42500 7.81200   1.000 9.83204  ? 49  LYS   C O     1 
ATOM   3081 C  CB    . LYS   C 2 50  ? 48.13700  -57.52700 10.56800  1.000 11.87367 ? 49  LYS   C CB    1 
ATOM   3082 C  CG    . LYS   C 2 50  ? 49.33600  -58.48100 10.76600  1.000 16.96299 ? 49  LYS   C CG    1 
ATOM   3083 C  CD    . LYS   C 2 50  ? 48.85400  -59.82100 11.26500  1.000 16.00282 ? 49  LYS   C CD    1 
ATOM   3084 C  CE    . LYS   C 2 50  ? 49.99800  -60.76900 11.51800  1.000 25.80892 ? 49  LYS   C CE    1 
ATOM   3085 N  NZ    . LYS   C 2 50  ? 49.47800  -61.99200 12.20100  1.000 28.79959 ? 49  LYS   C NZ    1 
ATOM   3086 N  N     . GLY   C 2 51  ? 50.54300  -55.70900 8.87800   1.000 12.84669 ? 50  GLY   C N     1 
ATOM   3087 C  CA    . GLY   C 2 51  ? 51.34800  -55.56800 7.69000   1.000 12.69433 ? 50  GLY   C CA    1 
ATOM   3088 C  C     . GLY   C 2 51  ? 51.53500  -54.13300 7.22700   1.000 11.68491 ? 50  GLY   C C     1 
ATOM   3089 O  O     . GLY   C 2 51  ? 52.51400  -53.84500 6.54400   1.000 12.78543 ? 50  GLY   C O     1 
ATOM   3090 N  N     . SER   C 2 52  ? 50.62500  -53.23000 7.57800   1.000 11.28528 ? 51  SER   C N     1 
ATOM   3091 C  CA    . SER   C 2 52  ? 50.68700  -51.87100 7.06500   1.000 10.87838 ? 51  SER   C CA    1 
ATOM   3092 C  C     . SER   C 2 52  ? 51.77500  -51.06700 7.78300   1.000 10.00677 ? 51  SER   C C     1 
ATOM   3093 O  O     . SER   C 2 52  ? 52.37600  -51.50200 8.76500   1.000 12.25025 ? 51  SER   C O     1 
ATOM   3094 C  CB    . SER   C 2 52  ? 49.32600  -51.18800 7.20000   1.000 9.59564  ? 51  SER   C CB    1 
ATOM   3095 O  OG    . SER   C 2 52  ? 48.93900  -51.05800 8.55900   1.000 9.26991  ? 51  SER   C OG    1 
ATOM   3096 N  N     . SER   C 2 53  ? 52.03300  -49.87200 7.27600   1.000 9.68617  ? 52  SER   C N     1 
ATOM   3097 C  CA    . SER   C 2 53  ? 53.19700  -49.10700 7.68800   1.000 10.94905 ? 52  SER   C CA    1 
ATOM   3098 C  C     . SER   C 2 53  ? 52.79700  -47.82500 8.41200   1.000 9.38811  ? 52  SER   C C     1 
ATOM   3099 O  O     . SER   C 2 53  ? 51.65500  -47.35700 8.33200   1.000 10.17024 ? 52  SER   C O     1 
ATOM   3100 C  CB    . SER   C 2 53  ? 54.06100  -48.74800 6.48100   1.000 14.77088 ? 52  SER   C CB    1 
ATOM   3101 O  OG    . SER   C 2 53  ? 53.38400  -47.76000 5.74300   1.000 17.98986 ? 52  SER   C OG    1 
ATOM   3102 N  N     . PHE   C 2 54  ? 53.75700  -47.28100 9.15300   1.000 9.90798  ? 53  PHE   C N     1 
ATOM   3103 C  CA    . PHE   C 2 54  ? 53.71700  -45.88700 9.59600   1.000 10.34030 ? 53  PHE   C CA    1 
ATOM   3104 C  C     . PHE   C 2 54  ? 54.43900  -45.10300 8.52000   1.000 9.26236  ? 53  PHE   C C     1 
ATOM   3105 O  O     . PHE   C 2 54  ? 55.66800  -45.07600 8.49000   1.000 9.59628  ? 53  PHE   C O     1 
ATOM   3106 C  CB    . PHE   C 2 54  ? 54.37500  -45.69700 10.96000  1.000 9.54247  ? 53  PHE   C CB    1 
ATOM   3107 C  CG    . PHE   C 2 54  ? 53.52800  -46.15200 12.10700  1.000 10.19701 ? 53  PHE   C CG    1 
ATOM   3108 C  CD1   . PHE   C 2 54  ? 53.44900  -47.49700 12.43300  1.000 9.78317  ? 53  PHE   C CD1   1 
ATOM   3109 C  CD2   . PHE   C 2 54  ? 52.79300  -45.23600 12.86000  1.000 10.55958 ? 53  PHE   C CD2   1 
ATOM   3110 C  CE1   . PHE   C 2 54  ? 52.65100  -47.92900 13.48300  1.000 10.40925 ? 53  PHE   C CE1   1 
ATOM   3111 C  CE2   . PHE   C 2 54  ? 51.99700  -45.66400 13.91400  1.000 11.12794 ? 53  PHE   C CE2   1 
ATOM   3112 C  CZ    . PHE   C 2 54  ? 51.92200  -47.01500 14.22400  1.000 9.62616  ? 53  PHE   C CZ    1 
ATOM   3113 N  N     . HIS   C 2 55  ? 53.66700  -44.49700 7.62000   1.000 10.54409 ? 54  HIS   C N     1 
ATOM   3114 C  CA    . HIS   C 2 55  ? 54.17400  -43.88000 6.40400   1.000 11.05571 ? 54  HIS   C CA    1 
ATOM   3115 C  C     . HIS   C 2 55  ? 54.58600  -42.42400 6.59000   1.000 9.58885  ? 54  HIS   C C     1 
ATOM   3116 O  O     . HIS   C 2 55  ? 55.30500  -41.88600 5.73300   1.000 14.24454 ? 54  HIS   C O     1 
ATOM   3117 C  CB    . HIS   C 2 55  ? 53.10500  -43.94400 5.31100   1.000 11.00783 ? 54  HIS   C CB    1 
ATOM   3118 C  CG    . HIS   C 2 55  ? 51.87800  -43.15800 5.64400   1.000 11.32381 ? 54  HIS   C CG    1 
ATOM   3119 N  ND1   . HIS   C 2 55  ? 50.87300  -43.65900 6.44200   1.000 9.91829  ? 54  HIS   C ND1   1 
ATOM   3120 C  CD2   . HIS   C 2 55  ? 51.49900  -41.90100 5.30400   1.000 10.41092 ? 54  HIS   C CD2   1 
ATOM   3121 C  CE1   . HIS   C 2 55  ? 49.92800  -42.74600 6.58500   1.000 10.33124 ? 54  HIS   C CE1   1 
ATOM   3122 N  NE2   . HIS   C 2 55  ? 50.27700  -41.67400 5.89500   1.000 7.53739  ? 54  HIS   C NE2   1 
ATOM   3123 N  N     . ARG   C 2 56  ? 54.15800  -41.78000 7.67700   1.000 8.10218  ? 55  ARG   C N     1 
ATOM   3124 C  CA    . ARG   C 2 56  ? 54.42300  -40.35700 7.90200   1.000 7.35490  ? 55  ARG   C CA    1 
ATOM   3125 C  C     . ARG   C 2 56  ? 54.77200  -40.15700 9.37400   1.000 7.44769  ? 55  ARG   C C     1 
ATOM   3126 O  O     . ARG   C 2 56  ? 53.90500  -40.28900 10.24300  1.000 6.66334  ? 55  ARG   C O     1 
ATOM   3127 C  CB    . ARG   C 2 56  ? 53.21900  -39.48500 7.51000   1.000 6.74740  ? 55  ARG   C CB    1 
ATOM   3128 C  CG    . ARG   C 2 56  ? 53.45200  -37.99800 7.79400   1.000 9.60046  ? 55  ARG   C CG    1 
ATOM   3129 C  CD    . ARG   C 2 56  ? 52.18300  -37.17600 7.53300   1.000 7.08437  ? 55  ARG   C CD    1 
ATOM   3130 N  NE    . ARG   C 2 56  ? 51.88000  -37.03700 6.11400   1.000 7.47801  ? 55  ARG   C NE    1 
ATOM   3131 C  CZ    . ARG   C 2 56  ? 50.84600  -36.33800 5.66100   1.000 10.66792 ? 55  ARG   C CZ    1 
ATOM   3132 N  NH1   . ARG   C 2 56  ? 50.04100  -35.69300 6.49100   1.000 8.16058  ? 55  ARG   C NH1   1 
ATOM   3133 N  NH2   . ARG   C 2 56  ? 50.63000  -36.26300 4.34600   1.000 8.19353  ? 55  ARG   C NH2   1 
ATOM   3134 N  N     . ILE   C 2 57  ? 56.03400  -39.83300 9.65400   1.000 7.22277  ? 56  ILE   C N     1 
ATOM   3135 C  CA    . ILE   C 2 57  ? 56.53300  -39.68600 11.02100  1.000 7.48218  ? 56  ILE   C CA    1 
ATOM   3136 C  C     . ILE   C 2 57  ? 57.28800  -38.36800 11.06000  1.000 8.14728  ? 56  ILE   C C     1 
ATOM   3137 O  O     . ILE   C 2 57  ? 58.34600  -38.23800 10.43800  1.000 8.93038  ? 56  ILE   C O     1 
ATOM   3138 C  CB    . ILE   C 2 57  ? 57.44200  -40.85000 11.44900  1.000 7.53121  ? 56  ILE   C CB    1 
ATOM   3139 C  CG1   . ILE   C 2 57  ? 56.65700  -42.17900 11.43900  1.000 7.03185  ? 56  ILE   C CG1   1 
ATOM   3140 C  CG2   . ILE   C 2 57  ? 58.00500  -40.61100 12.84200  1.000 7.84136  ? 56  ILE   C CG2   1 
ATOM   3141 C  CD1   . ILE   C 2 57  ? 57.39700  -43.31400 12.11100  1.000 8.83574  ? 56  ILE   C CD1   1 
ATOM   3142 N  N     . ILE   C 2 58  ? 56.74400  -37.39100 11.77300  1.000 7.95326  ? 57  ILE   C N     1 
ATOM   3143 C  CA    . ILE   C 2 58  ? 57.34000  -36.06500 11.84100  1.000 8.67997  ? 57  ILE   C CA    1 
ATOM   3144 C  C     . ILE   C 2 58  ? 57.80800  -35.84900 13.28000  1.000 11.76952 ? 57  ILE   C C     1 
ATOM   3145 O  O     . ILE   C 2 58  ? 56.97200  -35.76500 14.19400  1.000 8.96594  ? 57  ILE   C O     1 
ATOM   3146 C  CB    . ILE   C 2 58  ? 56.35800  -34.98000 11.38300  1.000 10.32977 ? 57  ILE   C CB    1 
ATOM   3147 C  CG1   . ILE   C 2 58  ? 56.00600  -35.22700 9.90500   1.000 12.76174 ? 57  ILE   C CG1   1 
ATOM   3148 C  CG2   . ILE   C 2 58  ? 56.95800  -33.59500 11.58200  1.000 11.84626 ? 57  ILE   C CG2   1 
ATOM   3149 C  CD1   . ILE   C 2 58  ? 55.12600  -34.16200 9.27000   1.000 12.64537 ? 57  ILE   C CD1   1 
ATOM   3150 N  N     . PRO   C 2 59  ? 59.12100  -35.76800 13.52600  1.000 10.43401 ? 58  PRO   C N     1 
ATOM   3151 C  CA    . PRO   C 2 59  ? 59.61600  -35.63200 14.90300  1.000 12.18203 ? 58  PRO   C CA    1 
ATOM   3152 C  C     . PRO   C 2 59  ? 59.04300  -34.40900 15.60300  1.000 12.74617 ? 58  PRO   C C     1 
ATOM   3153 O  O     . PRO   C 2 59  ? 59.02400  -33.30200 15.05300  1.000 12.93839 ? 58  PRO   C O     1 
ATOM   3154 C  CB    . PRO   C 2 59  ? 61.13900  -35.51500 14.72700  1.000 14.58878 ? 58  PRO   C CB    1 
ATOM   3155 C  CG    . PRO   C 2 59  ? 61.42900  -36.20400 13.39400  1.000 12.32016 ? 58  PRO   C CG    1 
ATOM   3156 C  CD    . PRO   C 2 59  ? 60.21600  -35.84900 12.54200  1.000 10.38544 ? 58  PRO   C CD    1 
ATOM   3157 N  N     . GLY   C 2 60  ? 58.60500  -34.61300 16.84600  1.000 11.98468 ? 59  GLY   C N     1 
ATOM   3158 C  CA    . GLY   C 2 60  ? 58.01300  -33.54300 17.62100  1.000 15.65653 ? 59  GLY   C CA    1 
ATOM   3159 C  C     . GLY   C 2 60  ? 56.52200  -33.40100 17.45100  1.000 10.63422 ? 59  GLY   C C     1 
ATOM   3160 O  O     . GLY   C 2 60  ? 55.91000  -32.55200 18.11700  1.000 13.23975 ? 59  GLY   C O     1 
ATOM   3161 N  N     . PHE   C 2 61  ? 55.91600  -34.19600 16.58100  1.000 10.71545 ? 60  PHE   C N     1 
ATOM   3162 C  CA    . PHE   C 2 61  ? 54.48300  -34.10300 16.37800  1.000 9.07800  ? 60  PHE   C CA    1 
ATOM   3163 C  C     . PHE   C 2 61  ? 53.81100  -35.46900 16.48500  1.000 8.62474  ? 60  PHE   C C     1 
ATOM   3164 O  O     . PHE   C 2 61  ? 53.06600  -35.69600 17.43900  1.000 11.97798 ? 60  PHE   C O     1 
ATOM   3165 C  CB    . PHE   C 2 61  ? 54.19300  -33.45100 15.03100  1.000 8.67636  ? 60  PHE   C CB    1 
ATOM   3166 C  CG    . PHE   C 2 61  ? 54.67000  -32.02900 14.93900  1.000 9.91942  ? 60  PHE   C CG    1 
ATOM   3167 C  CD1   . PHE   C 2 61  ? 53.84200  -30.97800 15.31700  1.000 11.59885 ? 60  PHE   C CD1   1 
ATOM   3168 C  CD2   . PHE   C 2 61  ? 55.94400  -31.74400 14.47100  1.000 10.16681 ? 60  PHE   C CD2   1 
ATOM   3169 C  CE1   . PHE   C 2 61  ? 54.27500  -29.66300 15.22400  1.000 14.54699 ? 60  PHE   C CE1   1 
ATOM   3170 C  CE2   . PHE   C 2 61  ? 56.38600  -30.43100 14.37100  1.000 15.21955 ? 60  PHE   C CE2   1 
ATOM   3171 C  CZ    . PHE   C 2 61  ? 55.55000  -29.38900 14.74600  1.000 14.00715 ? 60  PHE   C CZ    1 
ATOM   3172 N  N     . MET   C 2 62  ? 54.05800  -36.38800 15.54800  1.000 8.89788  ? 61  MET   C N     1 
ATOM   3173 C  CA    . MET   C 2 62  ? 53.26100  -37.61000 15.56600  1.000 9.97810  ? 61  MET   C CA    1 
ATOM   3174 C  C     . MET   C 2 62  ? 53.85000  -38.69500 14.67300  1.000 10.08002 ? 61  MET   C C     1 
ATOM   3175 O  O     . MET   C 2 62  ? 54.68300  -38.43200 13.80200  1.000 8.33541  ? 61  MET   C O     1 
ATOM   3176 C  CB    . MET   C 2 62  ? 51.82100  -37.32200 15.12200  1.000 9.94054  ? 61  MET   C CB    1 
ATOM   3177 C  CG    . MET   C 2 62  ? 51.62700  -37.33500 13.60900  1.000 7.60296  ? 61  MET   C CG    1 
ATOM   3178 S  SD    . MET   C 2 62  ? 52.47500  -35.99500 12.74800  1.000 9.76730  ? 61  MET   C SD    1 
ATOM   3179 C  CE    . MET   C 2 62  ? 52.50600  -36.71500 11.10700  1.000 10.07205 ? 61  MET   C CE    1 
ATOM   3180 N  N     . CYS   C 2 63  ? 53.37200  -39.92600 14.89500  1.000 6.32648  ? 62  CYS   C N     1 
ATOM   3181 C  CA    . CYS   C 2 63  ? 53.63000  -41.07700 14.03100  1.000 6.13199  ? 62  CYS   C CA    1 
ATOM   3182 C  C     . CYS   C 2 63  ? 52.28700  -41.48600 13.44800  1.000 6.22086  ? 62  CYS   C C     1 
ATOM   3183 O  O     . CYS   C 2 63  ? 51.37400  -41.80700 14.20400  1.000 8.05850  ? 62  CYS   C O     1 
ATOM   3184 C  CB    . CYS   C 2 63  ? 54.21500  -42.25900 14.80600  1.000 7.96389  ? 62  CYS   C CB    1 
ATOM   3185 S  SG    . CYS   C 2 63  ? 55.72800  -41.90900 15.70600  1.000 8.63997  ? 62  CYS   C SG    1 
ATOM   3186 N  N     . GLN   C 2 64  ? 52.17900  -41.49900 12.12300  1.000 7.17381  ? 63  GLN   C N     1 
ATOM   3187 C  CA    . GLN   C 2 64  ? 50.91900  -41.68600 11.42200  1.000 7.80128  ? 63  GLN   C CA    1 
ATOM   3188 C  C     . GLN   C 2 64  ? 50.99400  -42.94500 10.56500  1.000 9.63179  ? 63  GLN   C C     1 
ATOM   3189 O  O     . GLN   C 2 64  ? 51.97500  -43.15700 9.84100   1.000 9.19955  ? 63  GLN   C O     1 
ATOM   3190 C  CB    . GLN   C 2 64  ? 50.58000  -40.44700 10.56500  1.000 8.19034  ? 63  GLN   C CB    1 
ATOM   3191 C  CG    . GLN   C 2 64  ? 49.28500  -40.57400 9.77700   1.000 7.82341  ? 63  GLN   C CG    1 
ATOM   3192 C  CD    . GLN   C 2 64  ? 48.89000  -39.29700 9.05800   1.000 8.29230  ? 63  GLN   C CD    1 
ATOM   3193 O  OE1   . GLN   C 2 64  ? 49.32200  -38.20900 9.44000   1.000 9.47352  ? 63  GLN   C OE1   1 
ATOM   3194 N  NE2   . GLN   C 2 64  ? 48.07900  -39.42100 7.99000   1.000 6.70484  ? 63  GLN   C NE2   1 
ATOM   3195 N  N     . GLY   C 2 65  ? 49.95700  -43.77800 10.64800  1.000 8.80514  ? 64  GLY   C N     1 
ATOM   3196 C  CA    . GLY   C 2 65  ? 49.91700  -45.02300 9.90100   1.000 7.88788  ? 64  GLY   C CA    1 
ATOM   3197 C  C     . GLY   C 2 65  ? 48.50600  -45.44600 9.55600   1.000 8.68624  ? 64  GLY   C C     1 
ATOM   3198 O  O     . GLY   C 2 65  ? 47.56400  -44.66600 9.74000   1.000 8.55307  ? 64  GLY   C O     1 
ATOM   3199 N  N     . GLY   C 2 66  ? 48.35000  -46.66400 9.02900   1.000 9.11428  ? 65  GLY   C N     1 
ATOM   3200 C  CA    . GLY   C 2 66  ? 47.03800  -47.27700 8.89100   1.000 10.46384 ? 65  GLY   C CA    1 
ATOM   3201 C  C     . GLY   C 2 66  ? 46.49700  -47.41000 7.48500   1.000 9.80140  ? 65  GLY   C C     1 
ATOM   3202 O  O     . GLY   C 2 66  ? 45.34200  -47.83400 7.33200   1.000 12.38477 ? 65  GLY   C O     1 
ATOM   3203 N  N     . ASP   C 2 67  ? 47.27100  -47.07000 6.45200   1.000 9.86140  ? 66  ASP   C N     1 
ATOM   3204 C  CA    . ASP   C 2 67  ? 46.82100  -47.24800 5.06900   1.000 10.89892 ? 66  ASP   C CA    1 
ATOM   3205 C  C     . ASP   C 2 67  ? 47.11400  -48.67800 4.62900   1.000 10.62865 ? 66  ASP   C C     1 
ATOM   3206 O  O     . ASP   C 2 67  ? 48.17500  -48.97300 4.07500   1.000 11.64043 ? 66  ASP   C O     1 
ATOM   3207 C  CB    . ASP   C 2 67  ? 47.48100  -46.23600 4.14100   1.000 8.15814  ? 66  ASP   C CB    1 
ATOM   3208 C  CG    . ASP   C 2 67  ? 47.05700  -46.41900 2.68100   1.000 7.72401  ? 66  ASP   C CG    1 
ATOM   3209 O  OD1   . ASP   C 2 67  ? 46.24200  -47.32000 2.38700   1.000 11.82854 ? 66  ASP   C OD1   1 
ATOM   3210 O  OD2   . ASP   C 2 67  ? 47.52300  -45.65500 1.81900   1.000 9.81164  ? 66  ASP   C OD2   1 
ATOM   3211 N  N     . PHE   C 2 68  ? 46.14200  -49.57200 4.82400   1.000 8.65901  ? 67  PHE   C N     1 
ATOM   3212 C  CA    . PHE   C 2 68  ? 46.27600  -50.93600 4.33300   1.000 10.54037 ? 67  PHE   C CA    1 
ATOM   3213 C  C     . PHE   C 2 68  ? 45.56700  -51.18600 3.00300   1.000 11.90111 ? 67  PHE   C C     1 
ATOM   3214 O  O     . PHE   C 2 68  ? 45.55900  -52.33200 2.52900   1.000 11.06334 ? 67  PHE   C O     1 
ATOM   3215 C  CB    . PHE   C 2 68  ? 45.77300  -51.93900 5.38500   1.000 10.21647 ? 67  PHE   C CB    1 
ATOM   3216 C  CG    . PHE   C 2 68  ? 44.33600  -51.74900 5.77100   1.000 10.94476 ? 67  PHE   C CG    1 
ATOM   3217 C  CD1   . PHE   C 2 68  ? 43.31200  -52.29800 5.01100   1.000 10.04899 ? 67  PHE   C CD1   1 
ATOM   3218 C  CD2   . PHE   C 2 68  ? 44.01000  -51.03400 6.90200   1.000 8.30199  ? 67  PHE   C CD2   1 
ATOM   3219 C  CE1   . PHE   C 2 68  ? 41.98900  -52.11400 5.37700   1.000 9.40765  ? 67  PHE   C CE1   1 
ATOM   3220 C  CE2   . PHE   C 2 68  ? 42.70100  -50.86000 7.28000   1.000 10.58795 ? 67  PHE   C CE2   1 
ATOM   3221 C  CZ    . PHE   C 2 68  ? 41.68500  -51.40600 6.52400   1.000 11.92099 ? 67  PHE   C CZ    1 
ATOM   3222 N  N     . THR   C 2 69  ? 44.98300  -50.16400 2.37200   1.000 10.87966 ? 68  THR   C N     1 
ATOM   3223 C  CA    . THR   C 2 69  ? 44.34600  -50.38600 1.08000   1.000 9.92664  ? 68  THR   C CA    1 
ATOM   3224 C  C     . THR   C 2 69  ? 45.17200  -49.88800 -0.09400  1.000 12.36903 ? 68  THR   C C     1 
ATOM   3225 O  O     . THR   C 2 69  ? 45.21200  -50.55300 -1.13200  1.000 12.45746 ? 68  THR   C O     1 
ATOM   3226 C  CB    . THR   C 2 69  ? 42.96600  -49.71900 1.02600   1.000 13.91302 ? 68  THR   C CB    1 
ATOM   3227 O  OG1   . THR   C 2 69  ? 43.11800  -48.30300 1.17900   1.000 13.03717 ? 68  THR   C OG1   1 
ATOM   3228 C  CG2   . THR   C 2 69  ? 42.06700  -50.25600 2.13100   1.000 11.90942 ? 68  THR   C CG2   1 
ATOM   3229 N  N     . ARG   C 2 70  ? 45.80500  -48.71700 0.02500   1.000 11.25352 ? 69  ARG   C N     1 
ATOM   3230 C  CA    . ARG   C 2 70  ? 46.64200  -48.19500 -1.05000  1.000 12.29793 ? 69  ARG   C CA    1 
ATOM   3231 C  C     . ARG   C 2 70  ? 48.13000  -48.30700 -0.74400  1.000 12.52388 ? 69  ARG   C C     1 
ATOM   3232 O  O     . ARG   C 2 70  ? 48.94100  -48.29100 -1.67700  1.000 10.63302 ? 69  ARG   C O     1 
ATOM   3233 C  CB    . ARG   C 2 70  ? 46.28200  -46.72900 -1.35900  1.000 10.23735 ? 69  ARG   C CB    1 
ATOM   3234 C  CG    . ARG   C 2 70  ? 44.87100  -46.51000 -1.94800  1.000 10.83871 ? 69  ARG   C CG    1 
ATOM   3235 C  CD    . ARG   C 2 70  ? 44.78300  -46.95800 -3.40200  1.000 18.40382 ? 69  ARG   C CD    1 
ATOM   3236 N  NE    . ARG   C 2 70  ? 44.50100  -48.38500 -3.53600  1.000 26.12177 ? 69  ARG   C NE    1 
ATOM   3237 C  CZ    . ARG   C 2 70  ? 43.29500  -48.93400 -3.41200  1.000 27.72743 ? 69  ARG   C CZ    1 
ATOM   3238 N  NH1   . ARG   C 2 70  ? 42.22700  -48.20500 -3.11300  1.000 27.62734 ? 69  ARG   C NH1   1 
ATOM   3239 N  NH2   . ARG   C 2 70  ? 43.15500  -50.24800 -3.59200  1.000 23.73346 ? 69  ARG   C NH2   1 
ATOM   3240 N  N     . HIS   C 2 71  ? 48.49100  -48.46300 0.53100   1.000 9.21613  ? 70  HIS   C N     1 
ATOM   3241 C  CA    . HIS   C 2 71  ? 49.87400  -48.67300 0.95300   1.000 11.28982 ? 70  HIS   C CA    1 
ATOM   3242 C  C     . HIS   C 2 71  ? 50.75700  -47.49700 0.55000   1.000 14.94250 ? 70  HIS   C C     1 
ATOM   3243 O  O     . HIS   C 2 71  ? 51.93800  -47.68000 0.26500   1.000 10.85282 ? 70  HIS   C O     1 
ATOM   3244 C  CB    . HIS   C 2 71  ? 50.45000  -49.99000 0.39300   1.000 14.51085 ? 70  HIS   C CB    1 
ATOM   3245 C  CG    . HIS   C 2 71  ? 49.54800  -51.17800 0.55600   1.000 15.56013 ? 70  HIS   C CG    1 
ATOM   3246 N  ND1   . HIS   C 2 71  ? 49.53300  -51.95700 1.69500   1.000 11.65233 ? 70  HIS   C ND1   1 
ATOM   3247 C  CD2   . HIS   C 2 71  ? 48.63100  -51.71800 -0.28100  1.000 15.62955 ? 70  HIS   C CD2   1 
ATOM   3248 C  CE1   . HIS   C 2 71  ? 48.63500  -52.91800 1.55700   1.000 14.57611 ? 70  HIS   C CE1   1 
ATOM   3249 N  NE2   . HIS   C 2 71  ? 48.07700  -52.79800 0.36400   1.000 12.61938 ? 70  HIS   C NE2   1 
ATOM   3250 N  N     . ASN   C 2 72  ? 50.19100  -46.26600 0.51300   1.000 9.04184  ? 71  ASN   C N     1 
ATOM   3251 C  CA    . ASN   C 2 72  ? 50.99400  -45.10900 0.12700   1.000 13.65457 ? 71  ASN   C CA    1 
ATOM   3252 C  C     . ASN   C 2 72  ? 50.63300  -43.82200 0.86500   1.000 14.33111 ? 71  ASN   C C     1 
ATOM   3253 O  O     . ASN   C 2 72  ? 51.12200  -42.75500 0.46700   1.000 9.23920  ? 71  ASN   C O     1 
ATOM   3254 C  CB    . ASN   C 2 72  ? 50.92000  -44.86200 -1.39400  1.000 13.37824 ? 71  ASN   C CB    1 
ATOM   3255 C  CG    . ASN   C 2 72  ? 49.52700  -44.46100 -1.87700  1.000 12.66523 ? 71  ASN   C CG    1 
ATOM   3256 O  OD1   . ASN   C 2 72  ? 48.62600  -44.23100 -1.09000  1.000 11.76863 ? 71  ASN   C OD1   1 
ATOM   3257 N  ND2   . ASN   C 2 72  ? 49.35800  -44.39000 -3.19400  1.000 18.96603 ? 71  ASN   C ND2   1 
ATOM   3258 N  N     . GLY   C 2 73  ? 49.81700  -43.87400 1.92000   1.000 11.88978 ? 72  GLY   C N     1 
ATOM   3259 C  CA    . GLY   C 2 73  ? 49.42600  -42.68500 2.64200   1.000 7.74683  ? 72  GLY   C CA    1 
ATOM   3260 C  C     . GLY   C 2 73  ? 48.10800  -42.07100 2.21800   1.000 9.60185  ? 72  GLY   C C     1 
ATOM   3261 O  O     . GLY   C 2 73  ? 47.63900  -41.12900 2.87800   1.000 9.37508  ? 72  GLY   C O     1 
ATOM   3262 N  N     . THR   C 2 74  ? 47.48500  -42.56400 1.15100   1.000 8.33784  ? 73  THR   C N     1 
ATOM   3263 C  CA    . THR   C 2 74  ? 46.27100  -41.93600 0.63700   1.000 8.77013  ? 73  THR   C CA    1 
ATOM   3264 C  C     . THR   C 2 74  ? 45.00400  -42.73100 0.90400   1.000 10.06940 ? 73  THR   C C     1 
ATOM   3265 O  O     . THR   C 2 74  ? 43.90100  -42.20400 0.68800   1.000 10.15619 ? 73  THR   C O     1 
ATOM   3266 C  CB    . THR   C 2 74  ? 46.37300  -41.70400 -0.87500  1.000 10.33849 ? 73  THR   C CB    1 
ATOM   3267 O  OG1   . THR   C 2 74  ? 46.31600  -42.97000 -1.55200  1.000 10.80264 ? 73  THR   C OG1   1 
ATOM   3268 C  CG2   . THR   C 2 74  ? 47.69300  -40.99100 -1.23400  1.000 13.05879 ? 73  THR   C CG2   1 
ATOM   3269 N  N     . GLY   C 2 75  ? 45.11500  -43.97700 1.35800   1.000 11.82571 ? 74  GLY   C N     1 
ATOM   3270 C  CA    . GLY   C 2 75  ? 43.97900  -44.84500 1.44900   1.000 11.47166 ? 74  GLY   C CA    1 
ATOM   3271 C  C     . GLY   C 2 75  ? 43.60200  -45.21300 2.86500   1.000 13.51275 ? 74  GLY   C C     1 
ATOM   3272 O  O     . GLY   C 2 75  ? 43.95700  -44.53900 3.84400   1.000 10.83662 ? 74  GLY   C O     1 
ATOM   3273 N  N     . GLY   C 2 76  ? 42.86400  -46.30600 2.97600   1.000 19.54129 ? 75  GLY   C N     1 
ATOM   3274 C  CA    . GLY   C 2 76  ? 42.37900  -46.81100 4.23300   1.000 13.23511 ? 75  GLY   C CA    1 
ATOM   3275 C  C     . GLY   C 2 76  ? 40.87300  -46.94500 4.16200   1.000 15.25159 ? 75  GLY   C C     1 
ATOM   3276 O  O     . GLY   C 2 76  ? 40.23500  -46.40900 3.25400   1.000 17.80543 ? 75  GLY   C O     1 
ATOM   3277 N  N     . LYS   C 2 77  ? 40.29700  -47.67100 5.10900   1.000 14.64411 ? 76  LYS   C N     1 
ATOM   3278 C  CA    . LYS   C 2 77  ? 38.85600  -47.83100 5.14200   1.000 12.50537 ? 76  LYS   C CA    1 
ATOM   3279 C  C     . LYS   C 2 77  ? 38.47500  -48.31800 6.52500   1.000 13.90976 ? 76  LYS   C C     1 
ATOM   3280 O  O     . LYS   C 2 77  ? 39.29000  -48.91600 7.23800   1.000 13.21652 ? 76  LYS   C O     1 
ATOM   3281 C  CB    . LYS   C 2 77  ? 38.34900  -48.78900 4.05700   1.000 17.37084 ? 76  LYS   C CB    1 
ATOM   3282 C  CG    . LYS   C 2 77  ? 38.76400  -50.22600 4.21400   1.000 14.39731 ? 76  LYS   C CG    1 
ATOM   3283 C  CD    . LYS   C 2 77  ? 37.96700  -51.09800 3.25800   1.000 18.52850 ? 76  LYS   C CD    1 
ATOM   3284 C  CE    . LYS   C 2 77  ? 38.56000  -52.47900 3.10400   1.000 21.60747 ? 76  LYS   C CE    1 
ATOM   3285 N  NZ    . LYS   C 2 77  ? 37.64000  -53.42200 2.38900   1.000 22.20853 ? 76  LYS   C NZ    1 
ATOM   3286 N  N     . SER   C 2 78  ? 37.24800  -48.00500 6.91600   1.000 13.14209 ? 77  SER   C N     1 
ATOM   3287 C  CA    . SER   C 2 78  ? 36.78200  -48.36200 8.24000   1.000 13.26625 ? 77  SER   C CA    1 
ATOM   3288 C  C     . SER   C 2 78  ? 35.97900  -49.64900 8.15200   1.000 10.89542 ? 77  SER   C C     1 
ATOM   3289 O  O     . SER   C 2 78  ? 35.72800  -50.19000 7.07300   1.000 11.89917 ? 77  SER   C O     1 
ATOM   3290 C  CB    . SER   C 2 78  ? 35.94200  -47.23600 8.84300   1.000 13.35685 ? 77  SER   C CB    1 
ATOM   3291 O  OG    . SER   C 2 78  ? 34.65300  -47.24300 8.27000   1.000 11.13318 ? 77  SER   C OG    1 
ATOM   3292 N  N     . ILE   C 2 79  ? 35.55100  -50.14900 9.31000   1.000 11.20819 ? 78  ILE   C N     1 
ATOM   3293 C  CA    . ILE   C 2 79  ? 34.68600  -51.32200 9.29100   1.000 12.31293 ? 78  ILE   C CA    1 
ATOM   3294 C  C     . ILE   C 2 79  ? 33.25500  -50.95900 8.93400   1.000 14.40382 ? 78  ILE   C C     1 
ATOM   3295 O  O     . ILE   C 2 79  ? 32.42500  -51.85500 8.73500   1.000 14.46251 ? 78  ILE   C O     1 
ATOM   3296 C  CB    . ILE   C 2 79  ? 34.73000  -52.06400 10.63800  1.000 12.52140 ? 78  ILE   C CB    1 
ATOM   3297 C  CG1   . ILE   C 2 79  ? 34.19700  -51.17300 11.75600  1.000 14.67724 ? 78  ILE   C CG1   1 
ATOM   3298 C  CG2   . ILE   C 2 79  ? 36.16300  -52.49400 10.97100  1.000 12.54953 ? 78  ILE   C CG2   1 
ATOM   3299 C  CD1   . ILE   C 2 79  ? 33.86100  -51.95000 13.01400  1.000 14.13471 ? 78  ILE   C CD1   1 
ATOM   3300 N  N     . TYR   C 2 80  ? 32.94300  -49.67200 8.82100   1.000 15.75288 ? 79  TYR   C N     1 
ATOM   3301 C  CA    . TYR   C 2 80  ? 31.58200  -49.24300 8.51300   1.000 14.89057 ? 79  TYR   C CA    1 
ATOM   3302 C  C     . TYR   C 2 80  ? 31.40200  -48.84700 7.05800   1.000 16.53505 ? 79  TYR   C C     1 
ATOM   3303 O  O     . TYR   C 2 80  ? 30.29600  -48.48300 6.66000   1.000 20.38374 ? 79  TYR   C O     1 
ATOM   3304 C  CB    . TYR   C 2 80  ? 31.18200  -48.06100 9.39700   1.000 16.00007 ? 79  TYR   C CB    1 
ATOM   3305 C  CG    . TYR   C 2 80  ? 31.49900  -48.25900 10.85100  1.000 15.04747 ? 79  TYR   C CG    1 
ATOM   3306 C  CD1   . TYR   C 2 80  ? 30.72300  -49.09500 11.64400  1.000 14.76166 ? 79  TYR   C CD1   1 
ATOM   3307 C  CD2   . TYR   C 2 80  ? 32.57600  -47.60000 11.43400  1.000 14.34330 ? 79  TYR   C CD2   1 
ATOM   3308 C  CE1   . TYR   C 2 80  ? 31.00700  -49.26700 12.98100  1.000 14.62268 ? 79  TYR   C CE1   1 
ATOM   3309 C  CE2   . TYR   C 2 80  ? 32.88100  -47.77100 12.76200  1.000 17.92025 ? 79  TYR   C CE2   1 
ATOM   3310 C  CZ    . TYR   C 2 80  ? 32.09600  -48.60900 13.53800  1.000 17.42475 ? 79  TYR   C CZ    1 
ATOM   3311 O  OH    . TYR   C 2 80  ? 32.41100  -48.77000 14.87000  1.000 15.11389 ? 79  TYR   C OH    1 
ATOM   3312 N  N     . GLY   C 2 81  ? 32.45800  -48.89800 6.26900   1.000 19.65526 ? 80  GLY   C N     1 
ATOM   3313 C  CA    . GLY   C 2 81  ? 32.49700  -48.32700 4.94600   1.000 19.72969 ? 80  GLY   C CA    1 
ATOM   3314 C  C     . GLY   C 2 81  ? 33.77800  -47.54900 4.77500   1.000 18.16153 ? 80  GLY   C C     1 
ATOM   3315 O  O     . GLY   C 2 81  ? 34.67300  -47.57600 5.62900   1.000 16.96880 ? 80  GLY   C O     1 
ATOM   3316 N  N     . GLU   C 2 82  ? 33.87300  -46.83500 3.65200   1.000 16.80471 ? 81  GLU   C N     1 
ATOM   3317 C  CA    . GLU   C 2 82  ? 35.11300  -46.13600 3.33800   1.000 17.42475 ? 81  GLU   C CA    1 
ATOM   3318 C  C     . GLU   C 2 82  ? 35.37100  -44.99800 4.31500   1.000 18.32170 ? 81  GLU   C C     1 
ATOM   3319 O  O     . GLU   C 2 82  ? 36.52600  -44.72800 4.66200   1.000 19.03895 ? 81  GLU   C O     1 
ATOM   3320 C  CB    . GLU   C 2 82  ? 35.07700  -45.62300 1.89800   1.000 22.31059 ? 81  GLU   C CB    1 
ATOM   3321 C  CG    . GLU   C 2 82  ? 35.15400  -46.72300 0.83100   1.000 18.15236 ? 81  GLU   C CG    1 
ATOM   3322 C  CD    . GLU   C 2 82  ? 35.14600  -46.18100 -0.59800  1.000 21.47489 ? 81  GLU   C CD    1 
ATOM   3323 O  OE1   . GLU   C 2 82  ? 35.20000  -44.94200 -0.77700  1.000 21.51842 ? 81  GLU   C OE1   1 
ATOM   3324 O  OE2   . GLU   C 2 82  ? 35.09900  -47.00500 -1.54800  1.000 16.22606 ? 81  GLU   C OE2   1 
ATOM   3325 N  N     . LYS   C 2 83  ? 34.31600  -44.31400 4.76200   1.000 18.20708 ? 82  LYS   C N     1 
ATOM   3326 C  CA    . LYS   C 2 83  ? 34.46100  -43.22300 5.71300   1.000 17.15653 ? 82  LYS   C CA    1 
ATOM   3327 C  C     . LYS   C 2 83  ? 33.33400  -43.27000 6.73800   1.000 15.64966 ? 82  LYS   C C     1 
ATOM   3328 O  O     . LYS   C 2 83  ? 32.28400  -43.87500 6.50700   1.000 14.80744 ? 82  LYS   C O     1 
ATOM   3329 C  CB    . LYS   C 2 83  ? 34.47300  -41.87100 4.99500   1.000 17.49367 ? 82  LYS   C CB    1 
ATOM   3330 C  CG    . LYS   C 2 83  ? 33.14600  -41.52300 4.34700   1.000 24.89051 ? 82  LYS   C CG    1 
ATOM   3331 C  CD    . LYS   C 2 83  ? 33.32600  -40.67800 3.09600   1.000 27.61894 ? 82  LYS   C CD    1 
ATOM   3332 C  CE    . LYS   C 2 83  ? 34.19600  -39.47200 3.36700   1.000 29.91181 ? 82  LYS   C CE    1 
ATOM   3333 N  NZ    . LYS   C 2 83  ? 34.38400  -38.61700 2.15300   1.000 42.76560 ? 82  LYS   C NZ    1 
ATOM   3334 N  N     . PHE   C 2 84  ? 33.55700  -42.62600 7.88600   1.000 15.89495 ? 83  PHE   C N     1 
ATOM   3335 C  CA    . PHE   C 2 84  ? 32.47000  -42.44100 8.84500   1.000 16.69509 ? 83  PHE   C CA    1 
ATOM   3336 C  C     . PHE   C 2 84  ? 32.63600  -41.09900 9.54700   1.000 15.73892 ? 83  PHE   C C     1 
ATOM   3337 O  O     . PHE   C 2 84  ? 33.71200  -40.49500 9.53900   1.000 11.23439 ? 83  PHE   C O     1 
ATOM   3338 C  CB    . PHE   C 2 84  ? 32.35800  -43.61100 9.84900   1.000 13.73859 ? 83  PHE   C CB    1 
ATOM   3339 C  CG    . PHE   C 2 84  ? 33.55700  -43.80100 10.75100  1.000 14.34687 ? 83  PHE   C CG    1 
ATOM   3340 C  CD1   . PHE   C 2 84  ? 34.71500  -44.40900 10.28500  1.000 15.50801 ? 83  PHE   C CD1   1 
ATOM   3341 C  CD2   . PHE   C 2 84  ? 33.48700  -43.45700 12.08800  1.000 11.79751 ? 83  PHE   C CD2   1 
ATOM   3342 C  CE1   . PHE   C 2 84  ? 35.79800  -44.61500 11.12900  1.000 12.36984 ? 83  PHE   C CE1   1 
ATOM   3343 C  CE2   . PHE   C 2 84  ? 34.55800  -43.66100 12.93500  1.000 16.69830 ? 83  PHE   C CE2   1 
ATOM   3344 C  CZ    . PHE   C 2 84  ? 35.71700  -44.24900 12.45300  1.000 14.39399 ? 83  PHE   C CZ    1 
ATOM   3345 N  N     . GLU   C 2 85  ? 31.53800  -40.62500 10.13600  1.000 13.71430 ? 84  GLU   C N     1 
ATOM   3346 C  CA    . GLU   C 2 85  ? 31.52300  -39.26600 10.64500  1.000 15.26689 ? 84  GLU   C CA    1 
ATOM   3347 C  C     . GLU   C 2 85  ? 32.29400  -39.14800 11.95900  1.000 17.69522 ? 84  GLU   C C     1 
ATOM   3348 O  O     . GLU   C 2 85  ? 32.60600  -40.13600 12.63600  1.000 16.80549 ? 84  GLU   C O     1 
ATOM   3349 C  CB    . GLU   C 2 85  ? 30.08600  -38.78100 10.81200  1.000 17.24378 ? 84  GLU   C CB    1 
ATOM   3350 C  CG    . GLU   C 2 85  ? 29.25900  -39.61200 11.73800  1.000 24.48441 ? 84  GLU   C CG    1 
ATOM   3351 C  CD    . GLU   C 2 85  ? 27.83200  -39.13200 11.78000  1.000 32.64677 ? 84  GLU   C CD    1 
ATOM   3352 O  OE1   . GLU   C 2 85  ? 27.42900  -38.41800 10.83900  1.000 35.27934 ? 84  GLU   C OE1   1 
ATOM   3353 O  OE2   . GLU   C 2 85  ? 27.12100  -39.46200 12.75100  1.000 35.55356 ? 84  GLU   C OE2   1 
ATOM   3354 N  N     . ASP   C 2 86  ? 32.64000  -37.90600 12.29300  1.000 12.58082 ? 85  ASP   C N     1 
ATOM   3355 C  CA    . ASP   C 2 86  ? 33.31600  -37.62000 13.54500  1.000 11.93984 ? 85  ASP   C CA    1 
ATOM   3356 C  C     . ASP   C 2 86  ? 32.35300  -37.86300 14.69600  1.000 12.82078 ? 85  ASP   C C     1 
ATOM   3357 O  O     . ASP   C 2 86  ? 31.29600  -37.21900 14.77800  1.000 13.90483 ? 85  ASP   C O     1 
ATOM   3358 C  CB    . ASP   C 2 86  ? 33.81500  -36.17600 13.54300  1.000 11.92784 ? 85  ASP   C CB    1 
ATOM   3359 C  CG    . ASP   C 2 86  ? 34.80200  -35.91600 12.43200  1.000 11.70282 ? 85  ASP   C CG    1 
ATOM   3360 O  OD1   . ASP   C 2 86  ? 35.80100  -36.67200 12.36500  1.000 11.47219 ? 85  ASP   C OD1   1 
ATOM   3361 O  OD2   . ASP   C 2 86  ? 34.58100  -34.97600 11.62800  1.000 11.69171 ? 85  ASP   C OD2   1 
ATOM   3362 N  N     . GLU   C 2 87  ? 32.71500  -38.78800 15.58200  1.000 12.50248 ? 86  GLU   C N     1 
ATOM   3363 C  CA    . GLU   C 2 87  ? 31.77900  -39.25900 16.60000  1.000 17.46069 ? 86  GLU   C CA    1 
ATOM   3364 C  C     . GLU   C 2 87  ? 31.51600  -38.18200 17.64700  1.000 15.23768 ? 86  GLU   C C     1 
ATOM   3365 O  O     . GLU   C 2 87  ? 30.36600  -37.79500 17.89000  1.000 16.62843 ? 86  GLU   C O     1 
ATOM   3366 C  CB    . GLU   C 2 87  ? 32.32300  -40.53400 17.24800  1.000 14.41279 ? 86  GLU   C CB    1 
ATOM   3367 C  CG    . GLU   C 2 87  ? 31.37200  -41.17900 18.24100  1.000 14.18080 ? 86  GLU   C CG    1 
ATOM   3368 C  CD    . GLU   C 2 87  ? 31.84300  -42.55500 18.65000  1.000 15.82826 ? 86  GLU   C CD    1 
ATOM   3369 O  OE1   . GLU   C 2 87  ? 32.99700  -42.91800 18.31500  1.000 15.31393 ? 86  GLU   C OE1   1 
ATOM   3370 O  OE2   . GLU   C 2 87  ? 31.06300  -43.27200 19.29900  1.000 16.05296 ? 86  GLU   C OE2   1 
ATOM   3371 N  N     . ASN   C 2 88  ? 32.57400  -37.68800 18.27400  1.000 13.56276 ? 87  ASN   C N     1 
ATOM   3372 C  CA    . ASN   C 2 88  ? 32.47800  -36.58300 19.21900  1.000 15.73331 ? 87  ASN   C CA    1 
ATOM   3373 C  C     . ASN   C 2 88  ? 33.86700  -35.99000 19.34800  1.000 13.95205 ? 87  ASN   C C     1 
ATOM   3374 O  O     . ASN   C 2 88  ? 34.83500  -36.53700 18.83000  1.000 13.83248 ? 87  ASN   C O     1 
ATOM   3375 C  CB    . ASN   C 2 88  ? 31.93800  -37.02000 20.58500  1.000 15.19677 ? 87  ASN   C CB    1 
ATOM   3376 C  CG    . ASN   C 2 88  ? 32.85100  -37.98800 21.30900  1.000 16.84352 ? 87  ASN   C CG    1 
ATOM   3377 O  OD1   . ASN   C 2 88  ? 33.99400  -37.66300 21.62700  1.000 15.79403 ? 87  ASN   C OD1   1 
ATOM   3378 N  ND2   . ASN   C 2 88  ? 32.33400  -39.17700 21.61000  1.000 15.63069 ? 87  ASN   C ND2   1 
ATOM   3379 N  N     . PHE   C 2 89  ? 33.96200  -34.87400 20.05800  1.000 13.92436 ? 88  PHE   C N     1 
ATOM   3380 C  CA    . PHE   C 2 89  ? 35.26100  -34.28400 20.34000  1.000 15.21131 ? 88  PHE   C CA    1 
ATOM   3381 C  C     . PHE   C 2 89  ? 35.48600  -34.13000 21.83800  1.000 15.83024 ? 88  PHE   C C     1 
ATOM   3382 O  O     . PHE   C 2 89  ? 36.11200  -33.16800 22.28000  1.000 16.35330 ? 88  PHE   C O     1 
ATOM   3383 C  CB    . PHE   C 2 89  ? 35.41100  -32.94800 19.61800  1.000 13.45875 ? 88  PHE   C CB    1 
ATOM   3384 C  CG    . PHE   C 2 89  ? 35.34300  -33.07100 18.12400  1.000 12.90866 ? 88  PHE   C CG    1 
ATOM   3385 C  CD1   . PHE   C 2 89  ? 36.34500  -33.72100 17.41900  1.000 12.66020 ? 88  PHE   C CD1   1 
ATOM   3386 C  CD2   . PHE   C 2 89  ? 34.27100  -32.55100 17.42100  1.000 17.92644 ? 88  PHE   C CD2   1 
ATOM   3387 C  CE1   . PHE   C 2 89  ? 36.27400  -33.84200 16.05300  1.000 11.41311 ? 88  PHE   C CE1   1 
ATOM   3388 C  CE2   . PHE   C 2 89  ? 34.19900  -32.67800 16.03300  1.000 14.40187 ? 88  PHE   C CE2   1 
ATOM   3389 C  CZ    . PHE   C 2 89  ? 35.19400  -33.31400 15.35900  1.000 12.21521 ? 88  PHE   C CZ    1 
ATOM   3390 N  N     . ILE   C 2 90  ? 34.99700  -35.09100 22.62700  1.000 15.05623 ? 89  ILE   C N     1 
ATOM   3391 C  CA    . ILE   C 2 90  ? 35.09400  -34.97600 24.08100  1.000 15.52430 ? 89  ILE   C CA    1 
ATOM   3392 C  C     . ILE   C 2 90  ? 36.55000  -34.90000 24.50100  1.000 14.55888 ? 89  ILE   C C     1 
ATOM   3393 O  O     . ILE   C 2 90  ? 36.92100  -34.09600 25.36000  1.000 18.90909 ? 89  ILE   C O     1 
ATOM   3394 C  CB    . ILE   C 2 90  ? 34.38400  -36.15300 24.77700  1.000 17.96107 ? 89  ILE   C CB    1 
ATOM   3395 C  CG1   . ILE   C 2 90  ? 32.87600  -36.11900 24.54100  1.000 20.72039 ? 89  ILE   C CG1   1 
ATOM   3396 C  CG2   . ILE   C 2 90  ? 34.64500  -36.12300 26.28100  1.000 16.76207 ? 89  ILE   C CG2   1 
ATOM   3397 C  CD1   . ILE   C 2 90  ? 32.17800  -37.36000 25.10000  1.000 17.57253 ? 89  ILE   C CD1   1 
ATOM   3398 N  N     . LEU   C 2 91  ? 37.39300  -35.73000 23.89300  1.000 14.75303 ? 90  LEU   C N     1 
ATOM   3399 C  CA    . LEU   C 2 91  ? 38.76900  -35.89900 24.32900  1.000 14.32175 ? 90  LEU   C CA    1 
ATOM   3400 C  C     . LEU   C 2 91  ? 39.70800  -35.07000 23.46000  1.000 14.97517 ? 90  LEU   C C     1 
ATOM   3401 O  O     . LEU   C 2 91  ? 39.48100  -34.88700 22.26200  1.000 14.38079 ? 90  LEU   C O     1 
ATOM   3402 C  CB    . LEU   C 2 91  ? 39.14100  -37.38300 24.30400  1.000 15.03777 ? 90  LEU   C CB    1 
ATOM   3403 C  CG    . LEU   C 2 91  ? 38.20300  -38.13200 25.26100  1.000 18.64932 ? 90  LEU   C CG    1 
ATOM   3404 C  CD1   . LEU   C 2 91  ? 38.32800  -39.62100 25.14600  1.000 20.80960 ? 90  LEU   C CD1   1 
ATOM   3405 C  CD2   . LEU   C 2 91  ? 38.44700  -37.67800 26.70500  1.000 21.02358 ? 90  LEU   C CD2   1 
ATOM   3406 N  N     . LYS   C 2 92  ? 40.76600  -34.55300 24.08000  1.000 15.87239 ? 91  LYS   C N     1 
ATOM   3407 C  CA    . LYS   C 2 92  ? 41.64700  -33.61100 23.41100  1.000 11.85738 ? 91  LYS   C CA    1 
ATOM   3408 C  C     . LYS   C 2 92  ? 43.05300  -34.18700 23.26800  1.000 11.89231 ? 91  LYS   C C     1 
ATOM   3409 O  O     . LYS   C 2 92  ? 43.39600  -35.23400 23.83100  1.000 12.42535 ? 91  LYS   C O     1 
ATOM   3410 C  CB    . LYS   C 2 92  ? 41.67800  -32.27100 24.15800  1.000 12.91500 ? 91  LYS   C CB    1 
ATOM   3411 C  CG    . LYS   C 2 92  ? 40.31100  -31.57100 24.24200  1.000 16.14614 ? 91  LYS   C CG    1 
ATOM   3412 C  CD    . LYS   C 2 92  ? 40.43000  -30.25000 24.98000  1.000 16.40925 ? 91  LYS   C CD    1 
ATOM   3413 C  CE    . LYS   C 2 92  ? 39.19900  -29.37400 24.80100  1.000 20.42901 ? 91  LYS   C CE    1 
ATOM   3414 N  NZ    . LYS   C 2 92  ? 39.40900  -28.05100 25.46100  1.000 22.74478 ? 91  LYS   C NZ    1 
ATOM   3415 N  N     . HIS   C 2 93  ? 43.85200  -33.49300 22.45700  1.000 11.10190 ? 92  HIS   C N     1 
ATOM   3416 C  CA    . HIS   C 2 93  ? 45.23300  -33.88100 22.15600  1.000 10.46195 ? 92  HIS   C CA    1 
ATOM   3417 C  C     . HIS   C 2 93  ? 46.12800  -33.29600 23.23900  1.000 15.85078 ? 92  HIS   C C     1 
ATOM   3418 O  O     . HIS   C 2 93  ? 46.76700  -32.25500 23.07100  1.000 17.41593 ? 92  HIS   C O     1 
ATOM   3419 C  CB    . HIS   C 2 93  ? 45.62900  -33.38700 20.77200  1.000 12.40796 ? 92  HIS   C CB    1 
ATOM   3420 C  CG    . HIS   C 2 93  ? 44.77100  -33.93600 19.67800  1.000 11.81581 ? 92  HIS   C CG    1 
ATOM   3421 N  ND1   . HIS   C 2 93  ? 43.54400  -33.40100 19.36000  1.000 12.79599 ? 92  HIS   C ND1   1 
ATOM   3422 C  CD2   . HIS   C 2 93  ? 44.94000  -35.00500 18.86400  1.000 11.34808 ? 92  HIS   C CD2   1 
ATOM   3423 C  CE1   . HIS   C 2 93  ? 43.00300  -34.10000 18.37800  1.000 11.57548 ? 92  HIS   C CE1   1 
ATOM   3424 N  NE2   . HIS   C 2 93  ? 43.83500  -35.07400 18.05300  1.000 11.77554 ? 92  HIS   C NE2   1 
ATOM   3425 N  N     . THR   C 2 94  ? 46.14900  -33.97600 24.38100  1.000 13.05128 ? 93  THR   C N     1 
ATOM   3426 C  CA    . THR   C 2 94  ? 46.69300  -33.40000 25.60300  1.000 14.31757 ? 93  THR   C CA    1 
ATOM   3427 C  C     . THR   C 2 94  ? 48.18400  -33.64200 25.79600  1.000 15.80640 ? 93  THR   C C     1 
ATOM   3428 O  O     . THR   C 2 94  ? 48.76700  -33.04700 26.70200  1.000 17.22623 ? 93  THR   C O     1 
ATOM   3429 C  CB    . THR   C 2 94  ? 45.94000  -33.95300 26.81700  1.000 18.77438 ? 93  THR   C CB    1 
ATOM   3430 O  OG1   . THR   C 2 94  ? 45.97600  -35.38800 26.79200  1.000 14.56334 ? 93  THR   C OG1   1 
ATOM   3431 C  CG2   . THR   C 2 94  ? 44.49900  -33.47700 26.79500  1.000 16.29066 ? 93  THR   C CG2   1 
ATOM   3432 N  N     . GLY   C 2 95  ? 48.81900  -34.48200 24.98800  1.000 12.39084 ? 94  GLY   C N     1 
ATOM   3433 C  CA    . GLY   C 2 95  ? 50.21900  -34.77100 25.17800  1.000 11.88243 ? 94  GLY   C CA    1 
ATOM   3434 C  C     . GLY   C 2 95  ? 50.66600  -36.06000 24.51900  1.000 12.90629 ? 94  GLY   C C     1 
ATOM   3435 O  O     . GLY   C 2 95  ? 49.93000  -36.68600 23.74400  1.000 15.07817 ? 94  GLY   C O     1 
ATOM   3436 N  N     . PRO   C 2 96  ? 51.90000  -36.47700 24.80000  1.000 11.64645 ? 95  PRO   C N     1 
ATOM   3437 C  CA    . PRO   C 2 96  ? 52.46500  -37.63200 24.08600  1.000 12.58237 ? 95  PRO   C CA    1 
ATOM   3438 C  C     . PRO   C 2 96  ? 51.69900  -38.92100 24.37700  1.000 12.83986 ? 95  PRO   C C     1 
ATOM   3439 O  O     . PRO   C 2 96  ? 51.30200  -39.18800 25.51100  1.000 11.82086 ? 95  PRO   C O     1 
ATOM   3440 C  CB    . PRO   C 2 96  ? 53.90300  -37.70400 24.61900  1.000 13.40098 ? 95  PRO   C CB    1 
ATOM   3441 C  CG    . PRO   C 2 96  ? 54.21800  -36.31500 25.04600  1.000 13.51271 ? 95  PRO   C CG    1 
ATOM   3442 C  CD    . PRO   C 2 96  ? 52.91600  -35.76800 25.59800  1.000 15.37189 ? 95  PRO   C CD    1 
ATOM   3443 N  N     . GLY   C 2 97  ? 51.51900  -39.73600 23.34300  1.000 10.26610 ? 96  GLY   C N     1 
ATOM   3444 C  CA    . GLY   C 2 97  ? 50.82800  -41.00700 23.47100  1.000 12.67253 ? 96  GLY   C CA    1 
ATOM   3445 C  C     . GLY   C 2 97  ? 49.35500  -40.98100 23.12000  1.000 12.72312 ? 96  GLY   C C     1 
ATOM   3446 O  O     . GLY   C 2 97  ? 48.71800  -42.04100 23.12500  1.000 10.12658 ? 96  GLY   C O     1 
ATOM   3447 N  N     . ILE   C 2 98  ? 48.79000  -39.80500 22.83200  1.000 9.94228  ? 97  ILE   C N     1 
ATOM   3448 C  CA    . ILE   C 2 98  ? 47.38100  -39.72600 22.45800  1.000 11.51594 ? 97  ILE   C CA    1 
ATOM   3449 C  C     . ILE   C 2 98  ? 47.17900  -40.40400 21.11100  1.000 9.61235  ? 97  ILE   C C     1 
ATOM   3450 O  O     . ILE   C 2 98  ? 47.96200  -40.20700 20.17600  1.000 9.48812  ? 97  ILE   C O     1 
ATOM   3451 C  CB    . ILE   C 2 98  ? 46.92300  -38.25900 22.41300  1.000 10.12613 ? 97  ILE   C CB    1 
ATOM   3452 C  CG1   . ILE   C 2 98  ? 46.85200  -37.69300 23.83200  1.000 12.09755 ? 97  ILE   C CG1   1 
ATOM   3453 C  CG2   . ILE   C 2 98  ? 45.59500  -38.12200 21.62800  1.000 13.16963 ? 97  ILE   C CG2   1 
ATOM   3454 C  CD1   . ILE   C 2 98  ? 45.62800  -38.09100 24.62800  1.000 11.30648 ? 97  ILE   C CD1   1 
ATOM   3455 N  N     . LEU   C 2 99  ? 46.11500  -41.20100 21.00400  1.000 8.65604  ? 98  LEU   C N     1 
ATOM   3456 C  CA    . LEU   C 2 99  ? 45.78200  -41.92300 19.78300  1.000 8.47300  ? 98  LEU   C CA    1 
ATOM   3457 C  C     . LEU   C 2 99  ? 44.54700  -41.27400 19.16800  1.000 10.63072 ? 98  LEU   C C     1 
ATOM   3458 O  O     . LEU   C 2 99  ? 43.49900  -41.19800 19.81400  1.000 7.60621  ? 98  LEU   C O     1 
ATOM   3459 C  CB    . LEU   C 2 99  ? 45.53300  -43.40400 20.08600  1.000 8.19520  ? 98  LEU   C CB    1 
ATOM   3460 C  CG    . LEU   C 2 99  ? 45.15900  -44.32300 18.93500  1.000 11.28311 ? 98  LEU   C CG    1 
ATOM   3461 C  CD1   . LEU   C 2 99  ? 46.30000  -44.36000 17.90700  1.000 8.12046  ? 98  LEU   C CD1   1 
ATOM   3462 C  CD2   . LEU   C 2 99  ? 44.83800  -45.72900 19.46000  1.000 11.08543 ? 98  LEU   C CD2   1 
ATOM   3463 N  N     . SER   C 2 100 ? 44.67700  -40.80700 17.92800  1.000 8.87404  ? 99  SER   C N     1 
ATOM   3464 C  CA    . SER   C 2 100 ? 43.67200  -39.95800 17.30600  1.000 10.59712 ? 99  SER   C CA    1 
ATOM   3465 C  C     . SER   C 2 100 ? 43.52400  -40.35000 15.83800  1.000 10.63532 ? 99  SER   C C     1 
ATOM   3466 O  O     . SER   C 2 100 ? 44.43800  -40.91100 15.23900  1.000 8.88168  ? 99  SER   C O     1 
ATOM   3467 C  CB    . SER   C 2 100 ? 44.06100  -38.48100 17.44700  1.000 9.09938  ? 99  SER   C CB    1 
ATOM   3468 O  OG    . SER   C 2 100 ? 43.03000  -37.60800 16.99800  1.000 9.25520  ? 99  SER   C OG    1 
ATOM   3469 N  N     . MET   C 2 101 ? 42.35600  -40.04600 15.26200  1.000 8.78093  ? 100 MET   C N     1 
ATOM   3470 C  CA    . MET   C 2 101 ? 42.05800  -40.41500 13.87700  1.000 11.75357 ? 100 MET   C CA    1 
ATOM   3471 C  C     . MET   C 2 101 ? 42.60200  -39.37300 12.89900  1.000 11.07739 ? 100 MET   C C     1 
ATOM   3472 O  O     . MET   C 2 101 ? 42.36800  -38.16700 13.06100  1.000 8.11247  ? 100 MET   C O     1 
ATOM   3473 C  CB    . MET   C 2 101 ? 40.54500  -40.54900 13.65700  1.000 10.90796 ? 100 MET   C CB    1 
ATOM   3474 C  CG    . MET   C 2 101 ? 39.89100  -41.73900 14.31600  1.000 9.66245  ? 100 MET   C CG    1 
ATOM   3475 S  SD    . MET   C 2 101 ? 40.63000  -43.29400 13.73800  1.000 10.88424 ? 100 MET   C SD    1 
ATOM   3476 C  CE    . MET   C 2 101 ? 40.06700  -43.34600 12.03700  1.000 11.35440 ? 100 MET   C CE    1 
ATOM   3477 N  N     . ALA   C 2 102 ? 43.28700  -39.84200 11.85700  1.000 7.48412  ? 101 ALA   C N     1 
ATOM   3478 C  CA    . ALA   C 2 102 ? 43.61000  -38.96200 10.74200  1.000 9.64806  ? 101 ALA   C CA    1 
ATOM   3479 C  C     . ALA   C 2 102 ? 42.37600  -38.81200 9.86000   1.000 11.17162 ? 101 ALA   C C     1 
ATOM   3480 O  O     . ALA   C 2 102 ? 41.43600  -39.61000 9.93900   1.000 8.76828  ? 101 ALA   C O     1 
ATOM   3481 C  CB    . ALA   C 2 102 ? 44.77400  -39.52000 9.91600   1.000 8.31355  ? 101 ALA   C CB    1 
ATOM   3482 N  N     . ASN   C 2 103 ? 42.37800  -37.78200 9.01200   1.000 8.59310  ? 102 ASN   C N     1 
ATOM   3483 C  CA    . ASN   C 2 103 ? 41.22300  -37.55500 8.15000   1.000 9.30821  ? 102 ASN   C CA    1 
ATOM   3484 C  C     . ASN   C 2 103 ? 41.59600  -36.53900 7.07800   1.000 9.76317  ? 102 ASN   C C     1 
ATOM   3485 O  O     . ASN   C 2 103 ? 42.66800  -35.92900 7.11300   1.000 9.15700  ? 102 ASN   C O     1 
ATOM   3486 C  CB    . ASN   C 2 103 ? 39.98900  -37.08900 8.95600   1.000 11.93524 ? 102 ASN   C CB    1 
ATOM   3487 C  CG    . ASN   C 2 103 ? 40.18000  -35.73000 9.62200   1.000 10.36274 ? 102 ASN   C CG    1 
ATOM   3488 O  OD1   . ASN   C 2 103 ? 40.64000  -34.76900 9.00500   1.000 14.70110 ? 102 ASN   C OD1   1 
ATOM   3489 N  ND2   . ASN   C 2 103 ? 39.82400  -35.64800 10.90100  1.000 9.44839  ? 102 ASN   C ND2   1 
ATOM   3490 N  N     . ALA   C 2 104 ? 40.69800  -36.36900 6.11900   1.000 10.87194 ? 103 ALA   C N     1 
ATOM   3491 C  CA    . ALA   C 2 104 ? 40.86500  -35.35900 5.08100   1.000 13.64627 ? 103 ALA   C CA    1 
ATOM   3492 C  C     . ALA   C 2 104 ? 39.78500  -34.28800 5.18600   1.000 12.19090 ? 103 ALA   C C     1 
ATOM   3493 O  O     . ALA   C 2 104 ? 39.24100  -33.83100 4.18000   1.000 14.86180 ? 103 ALA   C O     1 
ATOM   3494 C  CB    . ALA   C 2 104 ? 40.87000  -36.00000 3.69500   1.000 12.22806 ? 103 ALA   C CB    1 
ATOM   3495 N  N     . GLY   C 2 105 ? 39.49600  -33.85000 6.41300   1.000 11.67549 ? 104 GLY   C N     1 
ATOM   3496 C  CA    . GLY   C 2 105 ? 38.41100  -32.92400 6.66900   1.000 11.92779 ? 104 GLY   C CA    1 
ATOM   3497 C  C     . GLY   C 2 105 ? 37.26500  -33.56700 7.44000   1.000 12.65898 ? 104 GLY   C C     1 
ATOM   3498 O  O     . GLY   C 2 105 ? 37.33300  -34.73400 7.84000   1.000 12.33278 ? 104 GLY   C O     1 
ATOM   3499 N  N     . PRO   C 2 106 ? 36.18600  -32.81400 7.64800   1.000 12.04577 ? 105 PRO   C N     1 
ATOM   3500 C  CA    . PRO   C 2 106 ? 35.07500  -33.30400 8.48300   1.000 16.64668 ? 105 PRO   C CA    1 
ATOM   3501 C  C     . PRO   C 2 106 ? 34.49200  -34.61600 7.97700   1.000 12.32331 ? 105 PRO   C C     1 
ATOM   3502 O  O     . PRO   C 2 106 ? 34.24000  -34.78400 6.78100   1.000 12.73837 ? 105 PRO   C O     1 
ATOM   3503 C  CB    . PRO   C 2 106 ? 34.04300  -32.17800 8.38800   1.000 13.65792 ? 105 PRO   C CB    1 
ATOM   3504 C  CG    . PRO   C 2 106 ? 34.84400  -30.95800 8.08200   1.000 17.10407 ? 105 PRO   C CG    1 
ATOM   3505 C  CD    . PRO   C 2 106 ? 35.99200  -31.41400 7.22500   1.000 13.01290 ? 105 PRO   C CD    1 
ATOM   3506 N  N     . ASN   C 2 107 ? 34.25800  -35.53500 8.91000   1.000 11.98005 ? 106 ASN   C N     1 
ATOM   3507 C  CA    . ASN   C 2 107 ? 33.49800  -36.75900 8.64400   1.000 12.22027 ? 106 ASN   C CA    1 
ATOM   3508 C  C     . ASN   C 2 107 ? 34.14500  -37.60800 7.55500   1.000 13.96006 ? 106 ASN   C C     1 
ATOM   3509 O  O     . ASN   C 2 107 ? 33.48200  -38.10700 6.64000   1.000 13.18530 ? 106 ASN   C O     1 
ATOM   3510 C  CB    . ASN   C 2 107 ? 32.05400  -36.41200 8.29000   1.000 13.56560 ? 106 ASN   C CB    1 
ATOM   3511 C  CG    . ASN   C 2 107 ? 31.39500  -35.61900 9.37200   1.000 14.57443 ? 106 ASN   C CG    1 
ATOM   3512 O  OD1   . ASN   C 2 107 ? 31.50200  -35.96600 10.54400  1.000 13.88205 ? 106 ASN   C OD1   1 
ATOM   3513 N  ND2   . ASN   C 2 107 ? 30.72000  -34.52900 8.99800   1.000 20.24247 ? 106 ASN   C ND2   1 
ATOM   3514 N  N     . THR   C 2 108 ? 35.45900  -37.76900 7.65000   1.000 10.73003 ? 107 THR   C N     1 
ATOM   3515 C  CA    . THR   C 2 108 ? 36.16200  -38.60100 6.68200   1.000 12.05379 ? 107 THR   C CA    1 
ATOM   3516 C  C     . THR   C 2 108 ? 37.03300  -39.64400 7.37300   1.000 12.00329 ? 107 THR   C C     1 
ATOM   3517 O  O     . THR   C 2 108 ? 38.03600  -40.07600 6.81000   1.000 13.92473 ? 107 THR   C O     1 
ATOM   3518 C  CB    . THR   C 2 108 ? 37.00600  -37.75400 5.71900   1.000 10.29335 ? 107 THR   C CB    1 
ATOM   3519 O  OG1   . THR   C 2 108 ? 37.96100  -36.97100 6.44700   1.000 10.90823 ? 107 THR   C OG1   1 
ATOM   3520 C  CG2   . THR   C 2 108 ? 36.11100  -36.82900 4.88000   1.000 16.49304 ? 107 THR   C CG2   1 
ATOM   3521 N  N     . ASN   C 2 109 ? 36.67200  -40.06500 8.58300   1.000 10.98544 ? 108 ASN   C N     1 
ATOM   3522 C  CA    . ASN   C 2 109 ? 37.46000  -41.09400 9.26000   1.000 8.65524  ? 108 ASN   C CA    1 
ATOM   3523 C  C     . ASN   C 2 109 ? 37.42100  -42.39800 8.47900   1.000 11.70465 ? 108 ASN   C C     1 
ATOM   3524 O  O     . ASN   C 2 109 ? 36.37500  -42.80300 7.97400   1.000 11.02709 ? 108 ASN   C O     1 
ATOM   3525 C  CB    . ASN   C 2 109 ? 36.94100  -41.34100 10.67300  1.000 10.93398 ? 108 ASN   C CB    1 
ATOM   3526 C  CG    . ASN   C 2 109 ? 36.99800  -40.09500 11.54500  1.000 11.70292 ? 108 ASN   C CG    1 
ATOM   3527 O  OD1   . ASN   C 2 109 ? 38.07400  -39.63300 11.90400  1.000 12.08346 ? 108 ASN   C OD1   1 
ATOM   3528 N  ND2   . ASN   C 2 109 ? 35.83800  -39.55800 11.89000  1.000 10.65635 ? 108 ASN   C ND2   1 
ATOM   3529 N  N     . GLY   C 2 110 ? 38.56900  -43.07000 8.41200   1.000 8.61959  ? 109 GLY   C N     1 
ATOM   3530 C  CA    . GLY   C 2 110 ? 38.69500  -44.33500 7.72100   1.000 10.08239 ? 109 GLY   C CA    1 
ATOM   3531 C  C     . GLY   C 2 110 ? 39.45600  -45.31900 8.58600   1.000 9.05940  ? 109 GLY   C C     1 
ATOM   3532 O  O     . GLY   C 2 110 ? 38.92800  -45.79300 9.59200   1.000 11.91036 ? 109 GLY   C O     1 
ATOM   3533 N  N     . SER   C 2 111 ? 40.69900  -45.63100 8.22100   1.000 9.24953  ? 110 SER   C N     1 
ATOM   3534 C  CA    . SER   C 2 111 ? 41.57600  -46.40500 9.09000   1.000 9.00772  ? 110 SER   C CA    1 
ATOM   3535 C  C     . SER   C 2 111 ? 42.81100  -45.64900 9.55400   1.000 8.60497  ? 110 SER   C C     1 
ATOM   3536 O  O     . SER   C 2 111 ? 43.39600  -46.04000 10.56900  1.000 7.69099  ? 110 SER   C O     1 
ATOM   3537 C  CB    . SER   C 2 111 ? 42.04100  -47.69200 8.39100   1.000 9.48719  ? 110 SER   C CB    1 
ATOM   3538 O  OG    . SER   C 2 111 ? 42.57600  -47.40400 7.12700   1.000 10.57928 ? 110 SER   C OG    1 
ATOM   3539 N  N     . GLN   C 2 112 ? 43.23600  -44.60100 8.85000   1.000 6.22890  ? 111 GLN   C N     1 
ATOM   3540 C  CA    . GLN   C 2 112 ? 44.47400  -43.94700 9.25400   1.000 5.82413  ? 111 GLN   C CA    1 
ATOM   3541 C  C     . GLN   C 2 112 ? 44.31100  -43.26300 10.61000  1.000 7.76377  ? 111 GLN   C C     1 
ATOM   3542 O  O     . GLN   C 2 112 ? 43.24400  -42.75800 10.96100  1.000 7.57219  ? 111 GLN   C O     1 
ATOM   3543 C  CB    . GLN   C 2 112 ? 44.93400  -42.93700 8.20400   1.000 7.67278  ? 111 GLN   C CB    1 
ATOM   3544 C  CG    . GLN   C 2 112 ? 45.42100  -43.56200 6.89600   1.000 8.18279  ? 111 GLN   C CG    1 
ATOM   3545 C  CD    . GLN   C 2 112 ? 46.15900  -42.56000 6.04300   1.000 8.69055  ? 111 GLN   C CD    1 
ATOM   3546 O  OE1   . GLN   C 2 112 ? 46.89100  -41.71200 6.55700   1.000 8.56316  ? 111 GLN   C OE1   1 
ATOM   3547 N  NE2   . GLN   C 2 112 ? 45.95300  -42.62900 4.73300   1.000 9.36555  ? 111 GLN   C NE2   1 
ATOM   3548 N  N     . PHE   C 2 113 ? 45.39800  -43.24700 11.36800  1.000 6.79056  ? 112 PHE   C N     1 
ATOM   3549 C  CA    . PHE   C 2 113 ? 45.41800  -42.78500 12.74400  1.000 6.62556  ? 112 PHE   C CA    1 
ATOM   3550 C  C     . PHE   C 2 113 ? 46.79300  -42.17900 12.97400  1.000 6.58118  ? 112 PHE   C C     1 
ATOM   3551 O  O     . PHE   C 2 113 ? 47.69900  -42.35500 12.16700  1.000 7.67784  ? 112 PHE   C O     1 
ATOM   3552 C  CB    . PHE   C 2 113 ? 45.16300  -43.94300 13.71800  1.000 6.88112  ? 112 PHE   C CB    1 
ATOM   3553 C  CG    . PHE   C 2 113 ? 46.23200  -45.01800 13.63300  1.000 10.07808 ? 112 PHE   C CG    1 
ATOM   3554 C  CD1   . PHE   C 2 113 ? 46.10300  -46.07500 12.74200  1.000 11.14545 ? 112 PHE   C CD1   1 
ATOM   3555 C  CD2   . PHE   C 2 113 ? 47.37700  -44.92300 14.39500  1.000 5.80148  ? 112 PHE   C CD2   1 
ATOM   3556 C  CE1   . PHE   C 2 113 ? 47.11800  -47.04600 12.62800  1.000 8.79698  ? 112 PHE   C CE1   1 
ATOM   3557 C  CE2   . PHE   C 2 113 ? 48.39600  -45.86200 14.29500  1.000 8.15010  ? 112 PHE   C CE2   1 
ATOM   3558 C  CZ    . PHE   C 2 113 ? 48.26900  -46.93000 13.41500  1.000 12.44766 ? 112 PHE   C CZ    1 
ATOM   3559 N  N     . PHE   C 2 114 ? 46.94800  -41.46600 14.08300  1.000 6.81324  ? 113 PHE   C N     1 
ATOM   3560 C  CA    . PHE   C 2 114 ? 48.26700  -41.01800 14.49200  1.000 8.46501  ? 113 PHE   C CA    1 
ATOM   3561 C  C     . PHE   C 2 114 ? 48.40100  -41.12400 16.00000  1.000 7.35563  ? 113 PHE   C C     1 
ATOM   3562 O  O     . PHE   C 2 114 ? 47.41800  -41.03500 16.73700  1.000 8.62986  ? 113 PHE   C O     1 
ATOM   3563 C  CB    . PHE   C 2 114 ? 48.59000  -39.59300 14.01400  1.000 6.78456  ? 113 PHE   C CB    1 
ATOM   3564 C  CG    . PHE   C 2 114 ? 47.64500  -38.53100 14.50800  1.000 11.06650 ? 113 PHE   C CG    1 
ATOM   3565 C  CD1   . PHE   C 2 114 ? 46.38600  -38.39400 13.95400  1.000 8.98235  ? 113 PHE   C CD1   1 
ATOM   3566 C  CD2   . PHE   C 2 114 ? 48.04600  -37.63800 15.48100  1.000 7.58955  ? 113 PHE   C CD2   1 
ATOM   3567 C  CE1   . PHE   C 2 114 ? 45.51300  -37.39000 14.37700  1.000 9.05280  ? 113 PHE   C CE1   1 
ATOM   3568 C  CE2   . PHE   C 2 114 ? 47.18600  -36.61700 15.91400  1.000 9.42150  ? 113 PHE   C CE2   1 
ATOM   3569 C  CZ    . PHE   C 2 114 ? 45.91400  -36.50700 15.36400  1.000 9.57632  ? 113 PHE   C CZ    1 
ATOM   3570 N  N     . ILE   C 2 115 ? 49.63400  -41.39100 16.43800  1.000 7.78645  ? 114 ILE   C N     1 
ATOM   3571 C  CA    . ILE   C 2 115 ? 50.03200  -41.31200 17.83900  1.000 6.25442  ? 114 ILE   C CA    1 
ATOM   3572 C  C     . ILE   C 2 115 ? 50.76300  -39.98300 18.02700  1.000 7.69208  ? 114 ILE   C C     1 
ATOM   3573 O  O     . ILE   C 2 115 ? 51.78300  -39.74000 17.37500  1.000 7.41561  ? 114 ILE   C O     1 
ATOM   3574 C  CB    . ILE   C 2 115 ? 50.94300  -42.49200 18.22800  1.000 8.02671  ? 114 ILE   C CB    1 
ATOM   3575 C  CG1   . ILE   C 2 115 ? 50.31700  -43.84200 17.86300  1.000 9.91560  ? 114 ILE   C CG1   1 
ATOM   3576 C  CG2   . ILE   C 2 115 ? 51.28700  -42.45600 19.70500  1.000 8.34241  ? 114 ILE   C CG2   1 
ATOM   3577 C  CD1   . ILE   C 2 115 ? 51.34600  -44.98400 17.87800  1.000 7.69562  ? 114 ILE   C CD1   1 
ATOM   3578 N  N     . CYS   C 2 116 ? 50.27300  -39.12600 18.92200  1.000 8.38071  ? 115 CYS   C N     1 
ATOM   3579 C  CA    . CYS   C 2 116 ? 51.00000  -37.89600 19.22500  1.000 9.48684  ? 115 CYS   C CA    1 
ATOM   3580 C  C     . CYS   C 2 116 ? 52.28800  -38.18900 19.98100  1.000 12.48032 ? 115 CYS   C C     1 
ATOM   3581 O  O     . CYS   C 2 116 ? 52.31500  -39.04100 20.87100  1.000 8.53705  ? 115 CYS   C O     1 
ATOM   3582 C  CB    . CYS   C 2 116 ? 50.15100  -36.96300 20.07700  1.000 7.88034  ? 115 CYS   C CB    1 
ATOM   3583 S  SG    . CYS   C 2 116 ? 48.56900  -36.55500 19.34500  1.000 12.60602 ? 115 CYS   C SG    1 
ATOM   3584 N  N     . THR   C 2 117 ? 53.35200  -37.44000 19.65800  1.000 10.11556 ? 116 THR   C N     1 
ATOM   3585 C  CA    . THR   C 2 117 ? 54.55400  -37.42300 20.47800  1.000 9.68000  ? 116 THR   C CA    1 
ATOM   3586 C  C     . THR   C 2 117 ? 54.72100  -36.10100 21.21400  1.000 14.57011 ? 116 THR   C C     1 
ATOM   3587 O  O     . THR   C 2 117 ? 55.71600  -35.91400 21.92400  1.000 10.95442 ? 116 THR   C O     1 
ATOM   3588 C  CB    . THR   C 2 117 ? 55.79300  -37.72400 19.63100  1.000 10.82596 ? 116 THR   C CB    1 
ATOM   3589 O  OG1   . THR   C 2 117 ? 55.90000  -36.76700 18.57600  1.000 13.77123 ? 116 THR   C OG1   1 
ATOM   3590 C  CG2   . THR   C 2 117 ? 55.69300  -39.13300 19.03700  1.000 11.61396 ? 116 THR   C CG2   1 
ATOM   3591 N  N     . ALA   C 2 118 ? 53.75000  -35.20200 21.08000  1.000 10.45355 ? 117 ALA   C N     1 
ATOM   3592 C  CA    . ALA   C 2 118 ? 53.68900  -33.94200 21.79300  1.000 12.27234 ? 117 ALA   C CA    1 
ATOM   3593 C  C     . ALA   C 2 118 ? 52.22000  -33.56100 21.92100  1.000 14.13427 ? 117 ALA   C C     1 
ATOM   3594 O  O     . ALA   C 2 118 ? 51.35200  -34.12900 21.26000  1.000 14.91329 ? 117 ALA   C O     1 
ATOM   3595 C  CB    . ALA   C 2 118 ? 54.46300  -32.83900 21.06700  1.000 15.03209 ? 117 ALA   C CB    1 
ATOM   3596 N  N     . LYS   C 2 119 ? 51.94900  -32.60300 22.79300  1.000 11.18336 ? 118 LYS   C N     1 
ATOM   3597 C  CA    . LYS   C 2 119 ? 50.65100  -31.94100 22.78300  1.000 16.01136 ? 118 LYS   C CA    1 
ATOM   3598 C  C     . LYS   C 2 119 ? 50.41900  -31.30800 21.41100  1.000 14.66226 ? 118 LYS   C C     1 
ATOM   3599 O  O     . LYS   C 2 119 ? 51.29200  -30.61000 20.88600  1.000 17.59570 ? 118 LYS   C O     1 
ATOM   3600 C  CB    . LYS   C 2 119 ? 50.61200  -30.88600 23.90000  1.000 14.78952 ? 118 LYS   C CB    1 
ATOM   3601 C  CG    . LYS   C 2 119 ? 49.27000  -30.18900 24.15700  1.000 16.73301 ? 118 LYS   C CG    1 
ATOM   3602 C  CD    . LYS   C 2 119 ? 49.42500  -29.21900 25.33200  1.000 20.39824 ? 118 LYS   C CD    1 
ATOM   3603 C  CE    . LYS   C 2 119 ? 48.10300  -28.66800 25.83900  1.000 26.41855 ? 118 LYS   C CE    1 
ATOM   3604 N  NZ    . LYS   C 2 119 ? 47.61000  -27.57700 24.98100  1.000 32.31635 ? 118 LYS   C NZ    1 
ATOM   3605 N  N     . THR   C 2 120 ? 49.24900  -31.58900 20.80200  1.000 14.33880 ? 119 THR   C N     1 
ATOM   3606 C  CA    . THR   C 2 120 ? 48.88100  -31.04300 19.48800  1.000 15.79210 ? 119 THR   C CA    1 
ATOM   3607 C  C     . THR   C 2 120 ? 47.48200  -30.41600 19.57500  1.000 12.96439 ? 119 THR   C C     1 
ATOM   3608 O  O     . THR   C 2 120 ? 46.55700  -30.87600 18.91100  1.000 12.94544 ? 119 THR   C O     1 
ATOM   3609 C  CB    . THR   C 2 120 ? 48.93700  -32.12500 18.37700  1.000 13.65030 ? 119 THR   C CB    1 
ATOM   3610 O  OG1   . THR   C 2 120 ? 48.04800  -33.20900 18.68400  1.000 12.31176 ? 119 THR   C OG1   1 
ATOM   3611 C  CG2   . THR   C 2 120 ? 50.35600  -32.67600 18.20500  1.000 12.32245 ? 119 THR   C CG2   1 
ATOM   3612 N  N     . GLU   C 2 121 ? 47.35000  -29.35500 20.37700  1.000 13.48925 ? 120 GLU   C N     1 
ATOM   3613 C  CA    . GLU   C 2 121 ? 46.03100  -28.81400 20.73300  1.000 15.18901 ? 120 GLU   C CA    1 
ATOM   3614 C  C     . GLU   C 2 121 ? 45.31500  -28.14600 19.56300  1.000 15.71993 ? 120 GLU   C C     1 
ATOM   3615 O  O     . GLU   C 2 121 ? 44.08300  -27.98600 19.60100  1.000 13.91400 ? 120 GLU   C O     1 
ATOM   3616 C  CB    . GLU   C 2 121 ? 46.16800  -27.81600 21.88300  1.000 17.95643 ? 120 GLU   C CB    1 
ATOM   3617 C  CG    . GLU   C 2 121 ? 46.79600  -26.46700 21.51700  1.000 22.46196 ? 120 GLU   C CG    1 
ATOM   3618 C  CD    . GLU   C 2 121 ? 48.32100  -26.47700 21.49700  1.000 25.12135 ? 120 GLU   C CD    1 
ATOM   3619 O  OE1   . GLU   C 2 121 ? 48.94000  -27.52700 21.77000  1.000 26.47122 ? 120 GLU   C OE1   1 
ATOM   3620 O  OE2   . GLU   C 2 121 ? 48.91000  -25.41500 21.20400  1.000 37.53422 ? 120 GLU   C OE2   1 
ATOM   3621 N  N     . TRP   C 2 122 ? 46.04400  -27.76300 18.51900  1.000 11.98327 ? 121 TRP   C N     1 
ATOM   3622 C  CA    . TRP   C 2 122 ? 45.38900  -27.18100 17.35100  1.000 13.34144 ? 121 TRP   C CA    1 
ATOM   3623 C  C     . TRP   C 2 122 ? 44.55700  -28.19700 16.58200  1.000 12.43907 ? 121 TRP   C C     1 
ATOM   3624 O  O     . TRP   C 2 122 ? 43.80100  -27.80700 15.68400  1.000 11.60560 ? 121 TRP   C O     1 
ATOM   3625 C  CB    . TRP   C 2 122 ? 46.44000  -26.55400 16.43400  1.000 14.99414 ? 121 TRP   C CB    1 
ATOM   3626 C  CG    . TRP   C 2 122 ? 47.44700  -27.56000 15.92000  1.000 14.13195 ? 121 TRP   C CG    1 
ATOM   3627 C  CD1   . TRP   C 2 122 ? 47.38600  -28.25600 14.74600  1.000 14.73765 ? 121 TRP   C CD1   1 
ATOM   3628 C  CD2   . TRP   C 2 122 ? 48.66900  -27.96400 16.56100  1.000 13.52366 ? 121 TRP   C CD2   1 
ATOM   3629 N  NE1   . TRP   C 2 122 ? 48.48400  -29.07700 14.62500  1.000 14.53266 ? 121 TRP   C NE1   1 
ATOM   3630 C  CE2   . TRP   C 2 122 ? 49.29300  -28.90100 15.71600  1.000 15.29066 ? 121 TRP   C CE2   1 
ATOM   3631 C  CE3   . TRP   C 2 122 ? 49.30500  -27.60500 17.76100  1.000 13.49012 ? 121 TRP   C CE3   1 
ATOM   3632 C  CZ2   . TRP   C 2 122 ? 50.51600  -29.51300 16.04400  1.000 14.01344 ? 121 TRP   C CZ2   1 
ATOM   3633 C  CZ3   . TRP   C 2 122 ? 50.52300  -28.20600 18.08100  1.000 18.93760 ? 121 TRP   C CZ3   1 
ATOM   3634 C  CH2   . TRP   C 2 122 ? 51.11500  -29.14200 17.22400  1.000 11.48860 ? 121 TRP   C CH2   1 
ATOM   3635 N  N     . LEU   C 2 123 ? 44.68400  -29.48200 16.90600  1.000 10.53309 ? 122 LEU   C N     1 
ATOM   3636 C  CA    . LEU   C 2 123 ? 43.89300  -30.52100 16.27300  1.000 14.06213 ? 122 LEU   C CA    1 
ATOM   3637 C  C     . LEU   C 2 123 ? 42.60000  -30.80300 17.02700  1.000 11.84570 ? 122 LEU   C C     1 
ATOM   3638 O  O     . LEU   C 2 123 ? 41.71900  -31.48400 16.48200  1.000 12.20850 ? 122 LEU   C O     1 
ATOM   3639 C  CB    . LEU   C 2 123 ? 44.73800  -31.79700 16.14400  1.000 8.98796  ? 122 LEU   C CB    1 
ATOM   3640 C  CG    . LEU   C 2 123 ? 45.99600  -31.68900 15.26300  1.000 8.94983  ? 122 LEU   C CG    1 
ATOM   3641 C  CD1   . LEU   C 2 123 ? 46.82100  -32.97000 15.30900  1.000 10.01281 ? 122 LEU   C CD1   1 
ATOM   3642 C  CD2   . LEU   C 2 123 ? 45.67400  -31.34600 13.81100  1.000 9.65860  ? 122 LEU   C CD2   1 
ATOM   3643 N  N     . ASP   C 2 124 ? 42.47700  -30.28800 18.25100  1.000 10.91824 ? 123 ASP   C N     1 
ATOM   3644 C  CA    . ASP   C 2 124 ? 41.24600  -30.41300 19.02500  1.000 12.82337 ? 123 ASP   C CA    1 
ATOM   3645 C  C     . ASP   C 2 124 ? 40.03600  -29.92100 18.24200  1.000 12.01153 ? 123 ASP   C C     1 
ATOM   3646 O  O     . ASP   C 2 124 ? 40.03600  -28.81600 17.69200  1.000 13.65537 ? 123 ASP   C O     1 
ATOM   3647 C  CB    . ASP   C 2 124 ? 41.33800  -29.59900 20.31200  1.000 12.47105 ? 123 ASP   C CB    1 
ATOM   3648 C  CG    . ASP   C 2 124 ? 42.36900  -30.13200 21.28000  1.000 17.42643 ? 123 ASP   C CG    1 
ATOM   3649 O  OD1   . ASP   C 2 124 ? 42.91100  -31.24400 21.05900  1.000 12.87750 ? 123 ASP   C OD1   1 
ATOM   3650 O  OD2   . ASP   C 2 124 ? 42.64000  -29.41100 22.26700  1.000 15.31941 ? 123 ASP   C OD2   1 
ATOM   3651 N  N     . GLY   C 2 125 ? 38.96700  -30.70700 18.26600  1.000 13.99411 ? 124 GLY   C N     1 
ATOM   3652 C  CA    . GLY   C 2 125 ? 37.76700  -30.31800 17.57200  1.000 13.66781 ? 124 GLY   C CA    1 
ATOM   3653 C  C     . GLY   C 2 125 ? 37.77700  -30.62900 16.10100  1.000 17.52454 ? 124 GLY   C C     1 
ATOM   3654 O  O     . GLY   C 2 125 ? 36.74500  -30.44000 15.44200  1.000 14.83633 ? 124 GLY   C O     1 
ATOM   3655 N  N     . LYS   C 2 126 ? 38.89500  -31.13600 15.57300  1.000 12.63491 ? 125 LYS   C N     1 
ATOM   3656 C  CA    . LYS   C 2 126 ? 39.02000  -31.47600 14.16400  1.000 10.72061 ? 125 LYS   C CA    1 
ATOM   3657 C  C     . LYS   C 2 126 ? 39.42500  -32.91900 13.91800  1.000 10.01237 ? 125 LYS   C C     1 
ATOM   3658 O  O     . LYS   C 2 126 ? 39.14500  -33.43800 12.83700  1.000 13.91101 ? 125 LYS   C O     1 
ATOM   3659 C  CB    . LYS   C 2 126 ? 40.04300  -30.55300 13.48400  1.000 12.62570 ? 125 LYS   C CB    1 
ATOM   3660 C  CG    . LYS   C 2 126 ? 39.68600  -29.08400 13.55900  1.000 23.04142 ? 125 LYS   C CG    1 
ATOM   3661 C  CD    . LYS   C 2 126 ? 40.64900  -28.23900 12.73400  1.000 31.20488 ? 125 LYS   C CD    1 
ATOM   3662 C  CE    . LYS   C 2 126 ? 40.10700  -26.83200 12.54700  1.000 33.14475 ? 125 LYS   C CE    1 
ATOM   3663 N  NZ    . LYS   C 2 126 ? 38.73900  -26.88700 11.97800  1.000 33.98927 ? 125 LYS   C NZ    1 
ATOM   3664 N  N     . HIS   C 2 127 ? 40.07700  -33.57100 14.86700  1.000 9.30401  ? 126 HIS   C N     1 
ATOM   3665 C  CA    . HIS   C 2 127 ? 40.40100  -34.98700 14.80800  1.000 8.58633  ? 126 HIS   C CA    1 
ATOM   3666 C  C     . HIS   C 2 127 ? 39.85200  -35.64200 16.06700  1.000 10.27268 ? 126 HIS   C C     1 
ATOM   3667 O  O     . HIS   C 2 127 ? 39.99400  -35.09200 17.16500  1.000 9.21072  ? 126 HIS   C O     1 
ATOM   3668 C  CB    . HIS   C 2 127 ? 41.94300  -35.19500 14.68300  1.000 8.87711  ? 126 HIS   C CB    1 
ATOM   3669 C  CG    . HIS   C 2 127 ? 42.50800  -34.67800 13.39200  1.000 8.72126  ? 126 HIS   C CG    1 
ATOM   3670 N  ND1   . HIS   C 2 127 ? 42.81500  -35.49800 12.32600  1.000 7.90627  ? 126 HIS   C ND1   1 
ATOM   3671 C  CD2   . HIS   C 2 127 ? 42.78300  -33.41200 12.98300  1.000 8.24570  ? 126 HIS   C CD2   1 
ATOM   3672 C  CE1   . HIS   C 2 127 ? 43.25300  -34.76300 11.32000  1.000 8.38004  ? 126 HIS   C CE1   1 
ATOM   3673 N  NE2   . HIS   C 2 127 ? 43.25300  -33.49500 11.69500  1.000 8.44505  ? 126 HIS   C NE2   1 
ATOM   3674 N  N     . VAL   C 2 128 ? 39.20000  -36.79200 15.90400  1.000 9.46458  ? 127 VAL   C N     1 
ATOM   3675 C  CA    . VAL   C 2 128 ? 38.60000  -37.50800 17.02900  1.000 9.12079  ? 127 VAL   C CA    1 
ATOM   3676 C  C     . VAL   C 2 128 ? 39.67600  -38.29000 17.78100  1.000 10.04913 ? 127 VAL   C C     1 
ATOM   3677 O  O     . VAL   C 2 128 ? 40.30700  -39.19400 17.22300  1.000 10.52739 ? 127 VAL   C O     1 
ATOM   3678 C  CB    . VAL   C 2 128 ? 37.47700  -38.43200 16.53700  1.000 10.46253 ? 127 VAL   C CB    1 
ATOM   3679 C  CG1   . VAL   C 2 128 ? 36.93400  -39.34100 17.65800  1.000 9.89967  ? 127 VAL   C CG1   1 
ATOM   3680 C  CG2   . VAL   C 2 128 ? 36.34900  -37.58300 15.91900  1.000 10.13475 ? 127 VAL   C CG2   1 
ATOM   3681 N  N     . VAL   C 2 129 ? 39.86100  -37.95800 19.06700  1.000 10.21221 ? 128 VAL   C N     1 
ATOM   3682 C  CA    . VAL   C 2 129 ? 40.71800  -38.71900 19.97300  1.000 10.05174 ? 128 VAL   C CA    1 
ATOM   3683 C  C     . VAL   C 2 129 ? 39.94300  -39.91200 20.52800  1.000 12.81816 ? 128 VAL   C C     1 
ATOM   3684 O  O     . VAL   C 2 129 ? 38.78900  -39.78000 20.95600  1.000 11.28275 ? 128 VAL   C O     1 
ATOM   3685 C  CB    . VAL   C 2 129 ? 41.22800  -37.80800 21.10600  1.000 9.86265  ? 128 VAL   C CB    1 
ATOM   3686 C  CG1   . VAL   C 2 129 ? 42.02200  -38.60600 22.13300  1.000 13.32736 ? 128 VAL   C CG1   1 
ATOM   3687 C  CG2   . VAL   C 2 129 ? 42.07000  -36.67400 20.54400  1.000 9.18577  ? 128 VAL   C CG2   1 
ATOM   3688 N  N     . PHE   C 2 130 ? 40.57600  -41.09200 20.55100  1.000 9.01449  ? 129 PHE   C N     1 
ATOM   3689 C  CA    . PHE   C 2 130 ? 39.84200  -42.28500 20.94000  1.000 12.52004 ? 129 PHE   C CA    1 
ATOM   3690 C  C     . PHE   C 2 130 ? 40.65500  -43.28200 21.74800  1.000 9.57632  ? 129 PHE   C C     1 
ATOM   3691 O  O     . PHE   C 2 130 ? 40.12800  -44.35400 22.06500  1.000 13.28578 ? 129 PHE   C O     1 
ATOM   3692 C  CB    . PHE   C 2 130 ? 39.27300  -42.99400 19.69900  1.000 12.55338 ? 129 PHE   C CB    1 
ATOM   3693 C  CG    . PHE   C 2 130 ? 40.33000  -43.54100 18.77200  1.000 13.24137 ? 129 PHE   C CG    1 
ATOM   3694 C  CD1   . PHE   C 2 130 ? 40.93300  -42.72200 17.82500  1.000 11.79635 ? 129 PHE   C CD1   1 
ATOM   3695 C  CD2   . PHE   C 2 130 ? 40.70200  -44.88500 18.83600  1.000 11.37952 ? 129 PHE   C CD2   1 
ATOM   3696 C  CE1   . PHE   C 2 130 ? 41.91800  -43.21800 16.96100  1.000 12.29839 ? 129 PHE   C CE1   1 
ATOM   3697 C  CE2   . PHE   C 2 130 ? 41.66400  -45.40000 17.98700  1.000 10.11365 ? 129 PHE   C CE2   1 
ATOM   3698 C  CZ    . PHE   C 2 130 ? 42.29200  -44.56600 17.03400  1.000 10.10553 ? 129 PHE   C CZ    1 
ATOM   3699 N  N     . GLY   C 2 131 ? 41.90600  -42.98000 22.07400  1.000 9.76163  ? 130 GLY   C N     1 
ATOM   3700 C  CA    . GLY   C 2 131 ? 42.68900  -43.89100 22.87100  1.000 12.18921 ? 130 GLY   C CA    1 
ATOM   3701 C  C     . GLY   C 2 131 ? 43.97600  -43.23800 23.32300  1.000 12.25119 ? 130 GLY   C C     1 
ATOM   3702 O  O     . GLY   C 2 131 ? 44.22500  -42.05800 23.06800  1.000 10.78542 ? 130 GLY   C O     1 
ATOM   3703 N  N     . LYS   C 2 132 ? 44.80700  -44.03100 23.98500  1.000 9.56721  ? 131 LYS   C N     1 
ATOM   3704 C  CA    . LYS   C 2 132 ? 46.11000  -43.51900 24.37800  1.000 9.56202  ? 131 LYS   C CA    1 
ATOM   3705 C  C     . LYS   C 2 132 ? 47.07500  -44.67900 24.49700  1.000 9.62496  ? 131 LYS   C C     1 
ATOM   3706 O  O     . LYS   C 2 132 ? 46.66800  -45.82400 24.72100  1.000 10.91690 ? 131 LYS   C O     1 
ATOM   3707 C  CB    . LYS   C 2 132 ? 46.04500  -42.73900 25.69600  1.000 10.47251 ? 131 LYS   C CB    1 
ATOM   3708 C  CG    . LYS   C 2 132 ? 45.75100  -43.61000 26.91800  1.000 11.50225 ? 131 LYS   C CG    1 
ATOM   3709 C  CD    . LYS   C 2 132 ? 45.89300  -42.81000 28.21000  1.000 15.63308 ? 131 LYS   C CD    1 
ATOM   3710 C  CE    . LYS   C 2 132 ? 45.69600  -43.69900 29.43400  1.000 14.50270 ? 131 LYS   C CE    1 
ATOM   3711 N  NZ    . LYS   C 2 132 ? 45.39300  -42.91300 30.66800  1.000 22.94176 ? 131 LYS   C NZ    1 
ATOM   3712 N  N     . VAL   C 2 133 ? 48.36200  -44.37500 24.34100  1.000 9.41414  ? 132 VAL   C N     1 
ATOM   3713 C  CA    . VAL   C 2 133 ? 49.37400  -45.40700 24.54700  1.000 9.67435  ? 132 VAL   C CA    1 
ATOM   3714 C  C     . VAL   C 2 133 ? 49.35300  -45.84500 25.99900  1.000 12.55849 ? 132 VAL   C C     1 
ATOM   3715 O  O     . VAL   C 2 133 ? 49.28200  -45.02000 26.92500  1.000 12.09442 ? 132 VAL   C O     1 
ATOM   3716 C  CB    . VAL   C 2 133 ? 50.76800  -44.90700 24.14200  1.000 9.43226  ? 132 VAL   C CB    1 
ATOM   3717 C  CG1   . VAL   C 2 133 ? 51.84100  -45.83600 24.70900  1.000 11.32551 ? 132 VAL   C CG1   1 
ATOM   3718 C  CG2   . VAL   C 2 133 ? 50.86400  -44.82900 22.63500  1.000 8.50461  ? 132 VAL   C CG2   1 
ATOM   3719 N  N     . LYS   C 2 134 ? 49.42700  -47.15100 26.20500  1.000 11.20440 ? 133 LYS   C N     1 
ATOM   3720 C  CA    . LYS   C 2 134 ? 49.44400  -47.71800 27.54400  1.000 12.42982 ? 133 LYS   C CA    1 
ATOM   3721 C  C     . LYS   C 2 134 ? 50.87900  -48.10000 27.88700  1.000 13.65643 ? 133 LYS   C C     1 
ATOM   3722 O  O     . LYS   C 2 134 ? 51.51300  -47.48300 28.75100  1.000 17.84137 ? 133 LYS   C O     1 
ATOM   3723 C  CB    . LYS   C 2 134 ? 48.50600  -48.92800 27.60200  1.000 12.83526 ? 133 LYS   C CB    1 
ATOM   3724 C  CG    . LYS   C 2 134 ? 48.30600  -49.55300 28.96500  1.000 17.64881 ? 133 LYS   C CG    1 
ATOM   3725 C  CD    . LYS   C 2 134 ? 47.71800  -50.95400 28.80100  1.000 21.63511 ? 133 LYS   C CD    1 
ATOM   3726 C  CE    . LYS   C 2 134 ? 46.36600  -51.06700 29.45200  1.000 18.04146 ? 133 LYS   C CE    1 
ATOM   3727 N  NZ    . LYS   C 2 134 ? 46.51600  -51.30900 30.90800  1.000 33.32914 ? 133 LYS   C NZ    1 
ATOM   3728 N  N     . GLU   C 2 135 ? 51.41700  -49.09800 27.20400  1.000 12.68910 ? 134 GLU   C N     1 
ATOM   3729 C  CA    . GLU   C 2 135 ? 52.81900  -49.46000 27.37100  1.000 14.47849 ? 134 GLU   C CA    1 
ATOM   3730 C  C     . GLU   C 2 135 ? 53.57300  -49.23000 26.07100  1.000 14.69395 ? 134 GLU   C C     1 
ATOM   3731 O  O     . GLU   C 2 135 ? 53.00100  -49.31800 24.98500  1.000 12.35834 ? 134 GLU   C O     1 
ATOM   3732 C  CB    . GLU   C 2 135 ? 52.97100  -50.91400 27.81900  1.000 15.85776 ? 134 GLU   C CB    1 
ATOM   3733 C  CG    . GLU   C 2 135 ? 52.62500  -51.10900 29.28400  1.000 23.09013 ? 134 GLU   C CG    1 
ATOM   3734 C  CD    . GLU   C 2 135 ? 52.26700  -52.53500 29.60800  1.000 38.67118 ? 134 GLU   C CD    1 
ATOM   3735 O  OE1   . GLU   C 2 135 ? 51.42100  -53.11100 28.88400  1.000 43.28731 ? 134 GLU   C OE1   1 
ATOM   3736 O  OE2   . GLU   C 2 135 ? 52.83300  -53.07600 30.58200  1.000 42.02642 ? 134 GLU   C OE2   1 
ATOM   3737 N  N     . GLY   C 2 136 ? 54.86700  -48.93100 26.19000  1.000 13.39648 ? 135 GLY   C N     1 
ATOM   3738 C  CA    . GLY   C 2 136 ? 55.69900  -48.78600 25.01200  1.000 13.55257 ? 135 GLY   C CA    1 
ATOM   3739 C  C     . GLY   C 2 136 ? 55.82400  -47.39300 24.43900  1.000 11.22892 ? 135 GLY   C C     1 
ATOM   3740 O  O     . GLY   C 2 136 ? 56.10300  -47.24900 23.24300  1.000 12.85100 ? 135 GLY   C O     1 
ATOM   3741 N  N     . MET   C 2 137 ? 55.64500  -46.34900 25.24900  1.000 12.12390 ? 136 MET   C N     1 
ATOM   3742 C  CA    . MET   C 2 137 ? 55.98000  -45.01600 24.75600  1.000 13.06947 ? 136 MET   C CA    1 
ATOM   3743 C  C     . MET   C 2 137 ? 57.44000  -44.94500 24.33300  1.000 14.51920 ? 136 MET   C C     1 
ATOM   3744 O  O     . MET   C 2 137 ? 57.80200  -44.10700 23.50300  1.000 13.02932 ? 136 MET   C O     1 
ATOM   3745 C  CB    . MET   C 2 137 ? 55.69400  -43.95800 25.82000  1.000 17.26775 ? 136 MET   C CB    1 
ATOM   3746 C  CG    . MET   C 2 137 ? 54.29000  -43.36700 25.78000  1.000 17.48320 ? 136 MET   C CG    1 
ATOM   3747 S  SD    . MET   C 2 137 ? 53.89800  -42.68400 24.17200  1.000 17.11641 ? 136 MET   C SD    1 
ATOM   3748 C  CE    . MET   C 2 137 ? 55.10600  -41.38600 23.95500  1.000 23.38319 ? 136 MET   C CE    1 
ATOM   3749 N  N     . ASN   C 2 138 ? 58.29500  -45.80600 24.89800  1.000 12.33397 ? 137 ASN   C N     1 
ATOM   3750 C  CA    . ASN   C 2 138 ? 59.70200  -45.79500 24.51000  1.000 12.82822 ? 137 ASN   C CA    1 
ATOM   3751 C  C     . ASN   C 2 138 ? 59.87700  -46.34500 23.10300  1.000 13.09641 ? 137 ASN   C C     1 
ATOM   3752 O  O     . ASN   C 2 138 ? 60.77000  -45.90100 22.36900  1.000 13.39110 ? 137 ASN   C O     1 
ATOM   3753 C  CB    . ASN   C 2 138 ? 60.55500  -46.55100 25.53200  1.000 15.52551 ? 137 ASN   C CB    1 
ATOM   3754 C  CG    . ASN   C 2 138 ? 60.30600  -48.06400 25.54500  1.000 15.06711 ? 137 ASN   C CG    1 
ATOM   3755 O  OD1   . ASN   C 2 138 ? 59.16700  -48.52800 25.58200  1.000 13.82775 ? 137 ASN   C OD1   1 
ATOM   3756 N  ND2   . ASN   C 2 138 ? 61.38700  -48.83300 25.55200  1.000 15.22054 ? 137 ASN   C ND2   1 
ATOM   3757 N  N     . ILE   C 2 139 ? 58.99700  -47.26100 22.69200  1.000 14.02333 ? 138 ILE   C N     1 
ATOM   3758 C  CA    . ILE   C 2 139 ? 58.99700  -47.74900 21.31900  1.000 10.90565 ? 138 ILE   C CA    1 
ATOM   3759 C  C     . ILE   C 2 139 ? 58.48200  -46.67200 20.37200  1.000 11.17098 ? 138 ILE   C C     1 
ATOM   3760 O  O     . ILE   C 2 139 ? 59.00100  -46.49800 19.26400  1.000 11.90356 ? 138 ILE   C O     1 
ATOM   3761 C  CB    . ILE   C 2 139 ? 58.16800  -49.04600 21.22400  1.000 11.83738 ? 138 ILE   C CB    1 
ATOM   3762 C  CG1   . ILE   C 2 139 ? 58.67400  -50.09800 22.22000  1.000 11.87151 ? 138 ILE   C CG1   1 
ATOM   3763 C  CG2   . ILE   C 2 139 ? 58.17600  -49.58300 19.80600  1.000 10.26332 ? 138 ILE   C CG2   1 
ATOM   3764 C  CD1   . ILE   C 2 139 ? 60.13700  -50.45100 22.07600  1.000 12.72220 ? 138 ILE   C CD1   1 
ATOM   3765 N  N     . VAL   C 2 140 ? 57.44900  -45.93500 20.78800  1.000 13.34532 ? 139 VAL   C N     1 
ATOM   3766 C  CA    . VAL   C 2 140 ? 56.94900  -44.82900 19.98300  1.000 9.13998  ? 139 VAL   C CA    1 
ATOM   3767 C  C     . VAL   C 2 140 ? 58.04500  -43.78200 19.77900  1.000 11.29812 ? 139 VAL   C C     1 
ATOM   3768 O  O     . VAL   C 2 140 ? 58.22500  -43.25400 18.67600  1.000 14.40603 ? 139 VAL   C O     1 
ATOM   3769 C  CB    . VAL   C 2 140 ? 55.69600  -44.22700 20.65000  1.000 8.59236  ? 139 VAL   C CB    1 
ATOM   3770 C  CG1   . VAL   C 2 140 ? 55.28500  -42.90000 19.98500  1.000 9.38077  ? 139 VAL   C CG1   1 
ATOM   3771 C  CG2   . VAL   C 2 140 ? 54.54800  -45.23900 20.64300  1.000 8.98457  ? 139 VAL   C CG2   1 
ATOM   3772 N  N     . GLU   C 2 141 ? 58.78800  -43.46400 20.84200  1.000 12.13995 ? 140 GLU   C N     1 
ATOM   3773 C  CA    . GLU   C 2 141 ? 59.91200  -42.53600 20.72300  1.000 10.79548 ? 140 GLU   C CA    1 
ATOM   3774 C  C     . GLU   C 2 141 ? 60.98100  -43.06700 19.77500  1.000 11.96045 ? 140 GLU   C C     1 
ATOM   3775 O  O     . GLU   C 2 141 ? 61.58700  -42.28900 19.02700  1.000 14.74899 ? 140 GLU   C O     1 
ATOM   3776 C  CB    . GLU   C 2 141 ? 60.51500  -42.26100 22.09800  1.000 13.98008 ? 140 GLU   C CB    1 
ATOM   3777 C  CG    . GLU   C 2 141 ? 59.57300  -41.54900 23.04600  1.000 14.43039 ? 140 GLU   C CG    1 
ATOM   3778 C  CD    . GLU   C 2 141 ? 60.04700  -41.57100 24.48100  1.000 17.56063 ? 140 GLU   C CD    1 
ATOM   3779 O  OE1   . GLU   C 2 141 ? 61.05900  -42.24600 24.78000  1.000 20.68393 ? 140 GLU   C OE1   1 
ATOM   3780 O  OE2   . GLU   C 2 141 ? 59.40800  -40.90600 25.32800  1.000 25.70456 ? 140 GLU   C OE2   1 
ATOM   3781 N  N     . ALA   C 2 142 ? 61.22100  -44.37700 19.77700  1.000 11.47093 ? 141 ALA   C N     1 
ATOM   3782 C  CA    . ALA   C 2 142 ? 62.13600  -44.95100 18.79500  1.000 12.34707 ? 141 ALA   C CA    1 
ATOM   3783 C  C     . ALA   C 2 142 ? 61.60400  -44.76900 17.37300  1.000 10.53894 ? 141 ALA   C C     1 
ATOM   3784 O  O     . ALA   C 2 142 ? 62.35100  -44.39500 16.46400  1.000 15.43972 ? 141 ALA   C O     1 
ATOM   3785 C  CB    . ALA   C 2 142 ? 62.37600  -46.42400 19.10700  1.000 14.34390 ? 141 ALA   C CB    1 
ATOM   3786 N  N     . MET   C 2 143 ? 60.31000  -45.01000 17.16400  1.000 12.32237 ? 142 MET   C N     1 
ATOM   3787 C  CA    . MET   C 2 143 ? 59.73800  -44.81700 15.83100  1.000 11.50838 ? 142 MET   C CA    1 
ATOM   3788 C  C     . MET   C 2 143 ? 59.91900  -43.38200 15.36700  1.000 11.88622 ? 142 MET   C C     1 
ATOM   3789 O  O     . MET   C 2 143 ? 60.28200  -43.12700 14.21100  1.000 10.01325 ? 142 MET   C O     1 
ATOM   3790 C  CB    . MET   C 2 143 ? 58.25900  -45.18300 15.83900  1.000 11.90548 ? 142 MET   C CB    1 
ATOM   3791 C  CG    . MET   C 2 143 ? 57.99200  -46.63000 16.24700  1.000 11.53610 ? 142 MET   C CG    1 
ATOM   3792 S  SD    . MET   C 2 143 ? 56.25300  -46.83400 16.68000  1.000 17.08800 ? 142 MET   C SD    1 
ATOM   3793 C  CE    . MET   C 2 143 ? 55.49400  -46.29600 15.15900  1.000 12.57275 ? 142 MET   C CE    1 
ATOM   3794 N  N     . GLU   C 2 144 ? 59.68600  -42.43500 16.27200  1.000 9.02477  ? 143 GLU   C N     1 
ATOM   3795 C  CA    . GLU   C 2 144 ? 59.78100  -41.03100 15.92700  1.000 12.16663 ? 143 GLU   C CA    1 
ATOM   3796 C  C     . GLU   C 2 144 ? 61.16600  -40.69100 15.39400  1.000 15.98340 ? 143 GLU   C C     1 
ATOM   3797 O  O     . GLU   C 2 144 ? 61.30000  -39.83800 14.51400  1.000 11.99786 ? 143 GLU   C O     1 
ATOM   3798 C  CB    . GLU   C 2 144 ? 59.43400  -40.19100 17.15800  1.000 12.99833 ? 143 GLU   C CB    1 
ATOM   3799 C  CG    . GLU   C 2 144 ? 59.41000  -38.68800 16.93900  1.000 15.39605 ? 143 GLU   C CG    1 
ATOM   3800 C  CD    . GLU   C 2 144 ? 59.15700  -37.95200 18.23000  1.000 17.93325 ? 143 GLU   C CD    1 
ATOM   3801 O  OE1   . GLU   C 2 144 ? 59.62000  -38.45800 19.27300  1.000 16.56974 ? 143 GLU   C OE1   1 
ATOM   3802 O  OE2   . GLU   C 2 144 ? 58.48300  -36.89500 18.20800  1.000 16.00352 ? 143 GLU   C OE2   1 
ATOM   3803 N  N     . ARG   C 2 145 ? 62.20200  -41.39800 15.85900  1.000 16.11140 ? 144 ARG   C N     1 
ATOM   3804 C  CA    . ARG   C 2 145 ? 63.55000  -41.10500 15.38400  1.000 14.09345 ? 144 ARG   C CA    1 
ATOM   3805 C  C     . ARG   C 2 145 ? 63.77100  -41.51400 13.92900  1.000 17.45256 ? 144 ARG   C C     1 
ATOM   3806 O  O     . ARG   C 2 145 ? 64.72700  -41.03300 13.31000  1.000 18.97277 ? 144 ARG   C O     1 
ATOM   3807 C  CB    . ARG   C 2 145 ? 64.59200  -41.77800 16.28400  1.000 15.54245 ? 144 ARG   C CB    1 
ATOM   3808 C  CG    . ARG   C 2 145 ? 64.52100  -41.32800 17.71500  1.000 19.23704 ? 144 ARG   C CG    1 
ATOM   3809 C  CD    . ARG   C 2 145 ? 65.67700  -41.86900 18.55200  1.000 16.50943 ? 144 ARG   C CD    1 
ATOM   3810 N  NE    . ARG   C 2 145 ? 65.56500  -41.35300 19.90900  1.000 24.71514 ? 144 ARG   C NE    1 
ATOM   3811 C  CZ    . ARG   C 2 145 ? 65.02700  -42.01300 20.93000  1.000 22.75021 ? 144 ARG   C CZ    1 
ATOM   3812 N  NH1   . ARG   C 2 145 ? 64.67100  -43.29000 20.82600  1.000 14.22445 ? 144 ARG   C NH1   1 
ATOM   3813 N  NH2   . ARG   C 2 145 ? 64.83400  -41.37400 22.08000  1.000 19.60892 ? 144 ARG   C NH2   1 
ATOM   3814 N  N     . PHE   C 2 146 ? 62.92400  -42.38400 13.37200  1.000 14.18492 ? 145 PHE   C N     1 
ATOM   3815 C  CA    . PHE   C 2 146 ? 63.03100  -42.75600 11.96700  1.000 13.19435 ? 145 PHE   C CA    1 
ATOM   3816 C  C     . PHE   C 2 146 ? 62.33700  -41.77000 11.03300  1.000 13.55159 ? 145 PHE   C C     1 
ATOM   3817 O  O     . PHE   C 2 146 ? 62.41600  -41.94300 9.81300   1.000 16.26779 ? 145 PHE   C O     1 
ATOM   3818 C  CB    . PHE   C 2 146 ? 62.45400  -44.15500 11.72800  1.000 13.56531 ? 145 PHE   C CB    1 
ATOM   3819 C  CG    . PHE   C 2 146 ? 63.25800  -45.25600 12.34500  1.000 13.33463 ? 145 PHE   C CG    1 
ATOM   3820 C  CD1   . PHE   C 2 146 ? 64.33100  -45.81300 11.66300  1.000 16.11787 ? 145 PHE   C CD1   1 
ATOM   3821 C  CD2   . PHE   C 2 146 ? 62.93200  -45.74800 13.60200  1.000 16.46730 ? 145 PHE   C CD2   1 
ATOM   3822 C  CE1   . PHE   C 2 146 ? 65.08300  -46.84000 12.22900  1.000 18.61828 ? 145 PHE   C CE1   1 
ATOM   3823 C  CE2   . PHE   C 2 146 ? 63.67600  -46.77800 14.17500  1.000 16.87222 ? 145 PHE   C CE2   1 
ATOM   3824 C  CZ    . PHE   C 2 146 ? 64.75900  -47.31600 13.48600  1.000 20.37206 ? 145 PHE   C CZ    1 
ATOM   3825 N  N     . GLY   C 2 147 ? 61.67800  -40.74400 11.56400  1.000 13.32468 ? 146 GLY   C N     1 
ATOM   3826 C  CA    . GLY   C 2 147 ? 60.98300  -39.76800 10.74800  1.000 13.77436 ? 146 GLY   C CA    1 
ATOM   3827 C  C     . GLY   C 2 147 ? 61.88600  -38.65000 10.25900  1.000 12.82673 ? 146 GLY   C C     1 
ATOM   3828 O  O     . GLY   C 2 147 ? 63.10900  -38.68300 10.40600  1.000 13.52144 ? 146 GLY   C O     1 
ATOM   3829 N  N     . SER   C 2 148 ? 61.25600  -37.63200 9.67000   1.000 12.56820 ? 147 SER   C N     1 
ATOM   3830 C  CA    . SER   C 2 148 ? 61.99500  -36.48600 9.14300   1.000 12.28424 ? 147 SER   C CA    1 
ATOM   3831 C  C     . SER   C 2 148 ? 61.05200  -35.29900 9.00200   1.000 13.32315 ? 147 SER   C C     1 
ATOM   3832 O  O     . SER   C 2 148 ? 59.84300  -35.41600 9.23100   1.000 11.89414 ? 147 SER   C O     1 
ATOM   3833 C  CB    . SER   C 2 148 ? 62.64900  -36.81400 7.80200   1.000 12.70504 ? 147 SER   C CB    1 
ATOM   3834 O  OG    . SER   C 2 148 ? 61.68200  -37.21900 6.85100   1.000 18.43128 ? 147 SER   C OG    1 
ATOM   3835 N  N     . ARG   C 2 149 ? 61.62800  -34.15300 8.59100   1.000 12.54489 ? 148 ARG   C N     1 
ATOM   3836 C  CA    . ARG   C 2 149 ? 60.87100  -32.90600 8.47700   1.000 18.44939 ? 148 ARG   C CA    1 
ATOM   3837 C  C     . ARG   C 2 149 ? 59.59700  -33.08600 7.68200   1.000 14.78459 ? 148 ARG   C C     1 
ATOM   3838 O  O     . ARG   C 2 149 ? 58.55600  -32.53600 8.05000   1.000 20.40686 ? 148 ARG   C O     1 
ATOM   3839 C  CB    . ARG   C 2 149 ? 61.68300  -31.80700 7.78900   1.000 19.69612 ? 148 ARG   C CB    1 
ATOM   3840 C  CG    . ARG   C 2 149 ? 62.83000  -31.23900 8.53700   1.000 25.99504 ? 148 ARG   C CG    1 
ATOM   3841 C  CD    . ARG   C 2 149 ? 63.33600  -29.99900 7.79400   1.000 22.89749 ? 148 ARG   C CD    1 
ATOM   3842 N  NE    . ARG   C 2 149 ? 62.50600  -28.83300 8.06400   1.000 24.28080 ? 148 ARG   C NE    1 
ATOM   3843 C  CZ    . ARG   C 2 149 ? 61.80300  -28.16900 7.15500   1.000 26.72579 ? 148 ARG   C CZ    1 
ATOM   3844 N  NH1   . ARG   C 2 149 ? 61.85700  -28.48100 5.86900   1.000 21.29170 ? 148 ARG   C NH1   1 
ATOM   3845 N  NH2   . ARG   C 2 149 ? 61.02500  -27.16400 7.54800   1.000 22.42843 ? 148 ARG   C NH2   1 
ATOM   3846 N  N     . ASN   C 2 150 ? 59.66300  -33.80800 6.55900   1.000 11.89032 ? 149 ASN   C N     1 
ATOM   3847 C  CA    . ASN   C 2 150 ? 58.49600  -33.96400 5.70000   1.000 13.95867 ? 149 ASN   C CA    1 
ATOM   3848 C  C     . ASN   C 2 150 ? 57.79900  -35.31000 5.90200   1.000 16.40562 ? 149 ASN   C C     1 
ATOM   3849 O  O     . ASN   C 2 150 ? 56.98800  -35.72300 5.06200   1.000 16.29232 ? 149 ASN   C O     1 
ATOM   3850 C  CB    . ASN   C 2 150 ? 58.87300  -33.73000 4.23200   1.000 17.72067 ? 149 ASN   C CB    1 
ATOM   3851 C  CG    . ASN   C 2 150 ? 59.84100  -34.75400 3.68200   1.000 16.28954 ? 149 ASN   C CG    1 
ATOM   3852 O  OD1   . ASN   C 2 150 ? 60.14200  -35.76500 4.31200   1.000 16.89153 ? 149 ASN   C OD1   1 
ATOM   3853 N  ND2   . ASN   C 2 150 ? 60.31700  -34.50200 2.46600   1.000 21.75210 ? 149 ASN   C ND2   1 
ATOM   3854 N  N     . GLY   C 2 151 ? 58.08600  -35.99300 7.01100   1.000 11.48202 ? 150 GLY   C N     1 
ATOM   3855 C  CA    . GLY   C 2 151 ? 57.40700  -37.22400 7.34100   1.000 13.33300 ? 150 GLY   C CA    1 
ATOM   3856 C  C     . GLY   C 2 151 ? 57.97500  -38.48000 6.72400   1.000 13.96776 ? 150 GLY   C C     1 
ATOM   3857 O  O     . GLY   C 2 151 ? 57.55600  -39.58100 7.11300   1.000 12.53363 ? 150 GLY   C O     1 
ATOM   3858 N  N     . LYS   C 2 152 ? 58.90200  -38.36900 5.78000   1.000 14.37766 ? 151 LYS   C N     1 
ATOM   3859 C  CA    . LYS   C 2 152 ? 59.45800  -39.56000 5.15400   1.000 17.49787 ? 151 LYS   C CA    1 
ATOM   3860 C  C     . LYS   C 2 152 ? 60.31600  -40.31700 6.15600   1.000 15.09743 ? 151 LYS   C C     1 
ATOM   3861 O  O     . LYS   C 2 152 ? 61.07800  -39.71500 6.92300   1.000 13.30446 ? 151 LYS   C O     1 
ATOM   3862 C  CB    . LYS   C 2 152 ? 60.28800  -39.17800 3.93500   1.000 21.05832 ? 151 LYS   C CB    1 
ATOM   3863 C  CG    . LYS   C 2 152 ? 59.48300  -38.60500 2.78500   1.000 20.92433 ? 151 LYS   C CG    1 
ATOM   3864 C  CD    . LYS   C 2 152 ? 58.61700  -39.68900 2.14900   1.000 23.34204 ? 151 LYS   C CD    1 
ATOM   3865 C  CE    . LYS   C 2 152 ? 57.77700  -39.12500 1.00900   1.000 25.35916 ? 151 LYS   C CE    1 
ATOM   3866 N  NZ    . LYS   C 2 152 ? 57.03600  -40.19500 0.29700   1.000 29.40768 ? 151 LYS   C NZ    1 
ATOM   3867 N  N     . THR   C 2 153 ? 60.20600  -41.64100 6.14800   1.000 14.42977 ? 152 THR   C N     1 
ATOM   3868 C  CA    . THR   C 2 153 ? 60.93900  -42.43000 7.12600   1.000 17.73315 ? 152 THR   C CA    1 
ATOM   3869 C  C     . THR   C 2 153 ? 62.20200  -43.02700 6.51600   1.000 17.08350 ? 152 THR   C C     1 
ATOM   3870 O  O     . THR   C 2 153 ? 62.25400  -43.34400 5.32200   1.000 16.04515 ? 152 THR   C O     1 
ATOM   3871 C  CB    . THR   C 2 153 ? 60.05400  -43.52400 7.71900   1.000 17.36635 ? 152 THR   C CB    1 
ATOM   3872 O  OG1   . THR   C 2 153 ? 59.58300  -44.38900 6.68100   1.000 17.18199 ? 152 THR   C OG1   1 
ATOM   3873 C  CG2   . THR   C 2 153 ? 58.87500  -42.88400 8.42900   1.000 13.58739 ? 152 THR   C CG2   1 
ATOM   3874 N  N     . SER   C 2 154 ? 63.24100  -43.15200 7.35700   1.000 14.42987 ? 153 SER   C N     1 
ATOM   3875 C  CA    . SER   C 2 154 ? 64.55500  -43.58600 6.90200   1.000 15.64501 ? 153 SER   C CA    1 
ATOM   3876 C  C     . SER   C 2 154 ? 64.65500  -45.09800 6.73700   1.000 20.15602 ? 153 SER   C C     1 
ATOM   3877 O  O     . SER   C 2 154 ? 65.56100  -45.57600 6.05000   1.000 20.31928 ? 153 SER   C O     1 
ATOM   3878 C  CB    . SER   C 2 154 ? 65.63200  -43.08400 7.86500   1.000 18.42377 ? 153 SER   C CB    1 
ATOM   3879 O  OG    . SER   C 2 154 ? 65.26500  -43.31900 9.21300   1.000 17.04168 ? 153 SER   C OG    1 
ATOM   3880 N  N     . LYS   C 2 155 ? 63.75500  -45.84900 7.35800   1.000 19.38884 ? 154 LYS   C N     1 
ATOM   3881 C  CA    . LYS   C 2 155 ? 63.58100  -47.26600 7.09200   1.000 17.38471 ? 154 LYS   C CA    1 
ATOM   3882 C  C     . LYS   C 2 155 ? 62.08600  -47.53400 7.11200   1.000 15.42984 ? 154 LYS   C C     1 
ATOM   3883 O  O     . LYS   C 2 155 ? 61.29800  -46.68100 7.51300   1.000 16.42718 ? 154 LYS   C O     1 
ATOM   3884 C  CB    . LYS   C 2 155 ? 64.32500  -48.13300 8.11300   1.000 13.53044 ? 154 LYS   C CB    1 
ATOM   3885 C  CG    . LYS   C 2 155 ? 65.84600  -48.07100 8.02400   1.000 19.03910 ? 154 LYS   C CG    1 
ATOM   3886 C  CD    . LYS   C 2 155 ? 66.46900  -49.12500 8.93400   1.000 24.82959 ? 154 LYS   C CD    1 
ATOM   3887 C  CE    . LYS   C 2 155 ? 67.92200  -49.39800 8.59700   1.000 24.15879 ? 154 LYS   C CE    1 
ATOM   3888 N  NZ    . LYS   C 2 155 ? 68.81800  -48.54800 9.38500   1.000 29.68474 ? 154 LYS   C NZ    1 
ATOM   3889 N  N     . LYS   C 2 156 ? 61.69000  -48.71300 6.65900   1.000 12.88028 ? 155 LYS   C N     1 
ATOM   3890 C  CA    . LYS   C 2 156 ? 60.27700  -49.05300 6.60700   1.000 16.15905 ? 155 LYS   C CA    1 
ATOM   3891 C  C     . LYS   C 2 156 ? 59.77800  -49.47800 7.99300   1.000 16.97637 ? 155 LYS   C C     1 
ATOM   3892 O  O     . LYS   C 2 156 ? 60.24000  -50.48100 8.54600   1.000 12.20064 ? 155 LYS   C O     1 
ATOM   3893 C  CB    . LYS   C 2 156 ? 60.03900  -50.15800 5.57800   1.000 12.92821 ? 155 LYS   C CB    1 
ATOM   3894 C  CG    . LYS   C 2 156 ? 58.57600  -50.58300 5.54500   1.000 24.96956 ? 155 LYS   C CG    1 
ATOM   3895 C  CD    . LYS   C 2 156 ? 58.06000  -50.86200 4.14000   1.000 21.95725 ? 155 LYS   C CD    1 
ATOM   3896 C  CE    . LYS   C 2 156 ? 56.54300  -50.76400 4.13100   1.000 14.66136 ? 155 LYS   C CE    1 
ATOM   3897 N  NZ    . LYS   C 2 156 ? 55.99400  -51.46900 2.94800   1.000 27.66753 ? 155 LYS   C NZ    1 
ATOM   3898 N  N     . ILE   C 2 157 ? 58.81800  -48.73400 8.53800   1.000 12.52396 ? 156 ILE   C N     1 
ATOM   3899 C  CA    . ILE   C 2 157 ? 58.25400  -48.99600 9.86200   1.000 9.83739  ? 156 ILE   C CA    1 
ATOM   3900 C  C     . ILE   C 2 157 ? 56.90700  -49.67100 9.66700   1.000 14.29443 ? 156 ILE   C C     1 
ATOM   3901 O  O     . ILE   C 2 157 ? 55.99200  -49.07200 9.08800   1.000 15.90504 ? 156 ILE   C O     1 
ATOM   3902 C  CB    . ILE   C 2 157 ? 58.08600  -47.70200 10.67100  1.000 8.08913  ? 156 ILE   C CB    1 
ATOM   3903 C  CG1   . ILE   C 2 157 ? 59.37400  -46.86600 10.65100  1.000 9.96671  ? 156 ILE   C CG1   1 
ATOM   3904 C  CG2   . ILE   C 2 157 ? 57.69100  -48.01400 12.10500  1.000 10.52647 ? 156 ILE   C CG2   1 
ATOM   3905 C  CD1   . ILE   C 2 157 ? 60.59300  -47.63200 11.10500  1.000 11.86772 ? 156 ILE   C CD1   1 
ATOM   3906 N  N     . THR   C 2 158 ? 56.76200  -50.90300 10.15000  1.000 10.38048 ? 157 THR   C N     1 
ATOM   3907 C  CA    . THR   C 2 158 ? 55.50600  -51.61400 9.94300   1.000 9.89365  ? 157 THR   C CA    1 
ATOM   3908 C  C     . THR   C 2 158 ? 54.94000  -52.18100 11.23500  1.000 9.87234  ? 157 THR   C C     1 
ATOM   3909 O  O     . THR   C 2 158 ? 55.63300  -52.35400 12.23400  1.000 11.56613 ? 157 THR   C O     1 
ATOM   3910 C  CB    . THR   C 2 158 ? 55.64200  -52.75600 8.93800   1.000 10.02240 ? 157 THR   C CB    1 
ATOM   3911 O  OG1   . THR   C 2 158 ? 56.62000  -53.70100 9.40600   1.000 12.76585 ? 157 THR   C OG1   1 
ATOM   3912 C  CG2   . THR   C 2 158 ? 56.03900  -52.19600 7.55900   1.000 10.92314 ? 157 THR   C CG2   1 
ATOM   3913 N  N     . ILE   C 2 159 ? 53.64600  -52.48300 11.15800  1.000 9.38681  ? 158 ILE   C N     1 
ATOM   3914 C  CA    . ILE   C 2 159 ? 52.91800  -53.22200 12.18800  1.000 8.77042  ? 158 ILE   C CA    1 
ATOM   3915 C  C     . ILE   C 2 159 ? 53.05700  -54.69500 11.80900  1.000 11.78128 ? 158 ILE   C C     1 
ATOM   3916 O  O     . ILE   C 2 159 ? 52.25800  -55.24400 11.05000  1.000 11.23844 ? 158 ILE   C O     1 
ATOM   3917 C  CB    . ILE   C 2 159 ? 51.45700  -52.77100 12.25400  1.000 10.23507 ? 158 ILE   C CB    1 
ATOM   3918 C  CG1   . ILE   C 2 159 ? 51.39200  -51.25600 12.50900  1.000 7.89433  ? 158 ILE   C CG1   1 
ATOM   3919 C  CG2   . ILE   C 2 159 ? 50.68700  -53.51100 13.32400  1.000 9.34290  ? 158 ILE   C CG2   1 
ATOM   3920 C  CD1   . ILE   C 2 159 ? 49.95400  -50.68900 12.40600  1.000 9.20138  ? 158 ILE   C CD1   1 
ATOM   3921 N  N     . ALA   C 2 160 ? 54.10100  -55.35300 12.32700  1.000 11.61863 ? 159 ALA   C N     1 
ATOM   3922 C  CA    . ALA   C 2 160 ? 54.32800  -56.74200 11.93400  1.000 13.36281 ? 159 ALA   C CA    1 
ATOM   3923 C  C     . ALA   C 2 160 ? 53.26500  -57.68400 12.49700  1.000 15.68125 ? 159 ALA   C C     1 
ATOM   3924 O  O     . ALA   C 2 160 ? 52.95300  -58.71000 11.87600  1.000 11.92517 ? 159 ALA   C O     1 
ATOM   3925 C  CB    . ALA   C 2 160 ? 55.72300  -57.19500 12.37500  1.000 11.87013 ? 159 ALA   C CB    1 
ATOM   3926 N  N     . ASP   C 2 161 ? 52.72500  -57.37500 13.67300  1.000 13.34160 ? 160 ASP   C N     1 
ATOM   3927 C  CA    . ASP   C 2 161 ? 51.64000  -58.15200 14.26000  1.000 14.56305 ? 160 ASP   C CA    1 
ATOM   3928 C  C     . ASP   C 2 161 ? 50.78300  -57.19000 15.06900  1.000 14.22224 ? 160 ASP   C C     1 
ATOM   3929 O  O     . ASP   C 2 161 ? 51.22600  -56.09900 15.43600  1.000 11.41859 ? 160 ASP   C O     1 
ATOM   3930 C  CB    . ASP   C 2 161 ? 52.17300  -59.29800 15.13900  1.000 12.33138 ? 160 ASP   C CB    1 
ATOM   3931 C  CG    . ASP   C 2 161 ? 51.12200  -60.37800 15.42100  1.000 18.56033 ? 160 ASP   C CG    1 
ATOM   3932 O  OD1   . ASP   C 2 161 ? 50.08500  -60.41100 14.72800  1.000 16.65248 ? 160 ASP   C OD1   1 
ATOM   3933 O  OD2   . ASP   C 2 161 ? 51.34300  -61.20900 16.32900  1.000 22.02481 ? 160 ASP   C OD2   1 
ATOM   3934 N  N     . CYS   C 2 162 ? 49.54000  -57.58500 15.32000  1.000 10.72198 ? 161 CYS   C N     1 
ATOM   3935 C  CA    . CYS   C 2 162 ? 48.62600  -56.75400 16.08700  1.000 13.08060 ? 161 CYS   C CA    1 
ATOM   3936 C  C     . CYS   C 2 162 ? 47.40700  -57.59100 16.44600  1.000 14.50182 ? 161 CYS   C C     1 
ATOM   3937 O  O     . CYS   C 2 162 ? 47.12200  -58.61200 15.80900  1.000 13.50920 ? 161 CYS   C O     1 
ATOM   3938 C  CB    . CYS   C 2 162 ? 48.20600  -55.48100 15.32900  1.000 10.97879 ? 161 CYS   C CB    1 
ATOM   3939 S  SG    . CYS   C 2 162 ? 47.52900  -55.71600 13.62000  1.000 14.43845 ? 161 CYS   C SG    1 
ATOM   3940 N  N     . GLY   C 2 163 ? 46.70700  -57.15800 17.48800  1.000 13.27755 ? 162 GLY   C N     1 
ATOM   3941 C  CA    . GLY   C 2 163 ? 45.56500  -57.90100 17.98000  1.000 15.08129 ? 162 GLY   C CA    1 
ATOM   3942 C  C     . GLY   C 2 163 ? 45.06700  -57.28900 19.27400  1.000 16.49337 ? 162 GLY   C C     1 
ATOM   3943 O  O     . GLY   C 2 163 ? 45.49900  -56.20500 19.67500  1.000 11.88267 ? 162 GLY   C O     1 
ATOM   3944 N  N     . GLN   C 2 164 ? 44.16100  -58.01100 19.92300  1.000 13.32869 ? 163 GLN   C N     1 
ATOM   3945 C  CA    . GLN   C 2 164 ? 43.54400  -57.53600 21.15100  1.000 17.83499 ? 163 GLN   C CA    1 
ATOM   3946 C  C     . GLN   C 2 164 ? 44.14700  -58.25600 22.34500  1.000 20.06492 ? 163 GLN   C C     1 
ATOM   3947 O  O     . GLN   C 2 164 ? 44.25000  -59.48800 22.34700  1.000 26.33376 ? 163 GLN   C O     1 
ATOM   3948 C  CB    . GLN   C 2 164 ? 42.03200  -57.74000 21.12600  1.000 14.93760 ? 163 GLN   C CB    1 
ATOM   3949 C  CG    . GLN   C 2 164 ? 41.31200  -57.09700 22.31100  1.000 20.96143 ? 163 GLN   C CG    1 
ATOM   3950 C  CD    . GLN   C 2 164 ? 39.80600  -57.01600 22.11600  1.000 15.79397 ? 163 GLN   C CD    1 
ATOM   3951 O  OE1   . GLN   C 2 164 ? 39.29300  -57.28900 21.02900  1.000 17.83804 ? 163 GLN   C OE1   1 
ATOM   3952 N  NE2   . GLN   C 2 164 ? 39.09300  -56.64400 23.17300  1.000 16.30751 ? 163 GLN   C NE2   1 
ATOM   3953 N  N     . LEU   C 2 165 ? 44.52900  -57.49100 23.36200  1.000 18.14751 ? 164 LEU   C N     1 
ATOM   3954 C  CA    . LEU   C 2 165 ? 45.12400  -58.05500 24.56900  1.000 23.95880 ? 164 LEU   C CA    1 
ATOM   3955 C  C     . LEU   C 2 165 ? 44.02900  -58.39900 25.57200  1.000 31.98827 ? 164 LEU   C C     1 
ATOM   3956 O  O     . LEU   C 2 165 ? 43.23900  -57.52700 25.95300  1.000 29.83089 ? 164 LEU   C O     1 
ATOM   3957 C  CB    . LEU   C 2 165 ? 46.13400  -57.08200 25.18500  1.000 27.66882 ? 164 LEU   C CB    1 
ATOM   3958 C  CG    . LEU   C 2 165 ? 47.52000  -56.97500 24.53100  1.000 23.65788 ? 164 LEU   C CG    1 
ATOM   3959 C  CD1   . LEU   C 2 165 ? 48.45100  -56.09900 25.35900  1.000 27.20761 ? 164 LEU   C CD1   1 
ATOM   3960 C  CD2   . LEU   C 2 165 ? 48.14800  -58.35100 24.31900  1.000 26.10672 ? 164 LEU   C CD2   1 
ATOM   3961 N  N     . GLU   C 2 166 ? 43.99200  -59.67200 25.97800  1.000 34.97758 ? 165 GLU   C N     1 
ATOM   3962 C  CA    . GLU   C 2 166 ? 43.16000  -60.23700 27.05500  1.000 42.55082 ? 165 GLU   C CA    1 
ATOM   3963 C  C     . GLU   C 2 166 ? 43.02000  -61.74900 26.83800  1.000 42.71845 ? 165 GLU   C C     1 
ATOM   3964 O  O     . GLU   C 2 166 ? 43.34400  -62.27700 25.76800  1.000 43.23318 ? 165 GLU   C O     1 
ATOM   3965 C  CB    . GLU   C 2 166 ? 41.77000  -59.60000 27.12600  1.000 48.44655 ? 165 GLU   C CB    1 
ATOM   3966 C  CG    . GLU   C 2 166 ? 41.08300  -59.74400 28.47700  1.000 47.61959 ? 165 GLU   C CG    1 
ATOM   3967 C  CD    . GLU   C 2 166 ? 40.21900  -58.53800 28.80900  1.000 55.11329 ? 165 GLU   C CD    1 
ATOM   3968 O  OE1   . GLU   C 2 166 ? 40.61700  -57.40200 28.45600  1.000 55.45050 ? 165 GLU   C OE1   1 
ATOM   3969 O  OE2   . GLU   C 2 166 ? 39.14200  -58.72400 29.41600  1.000 61.50959 ? 165 GLU   C OE2   1 
ATOM   3970 O  OXT   . GLU   C 2 166 ? 42.57200  -62.49500 27.71400  1.000 43.61011 ? 165 GLU   C OXT   1 
ATOM   3971 N  N     . SER   D 2 1   ? 71.95800  1.46600   19.42600  1.000 22.62686 ? 0   SER   D N     1 
ATOM   3972 C  CA    . SER   D 2 1   ? 70.71600  0.76700   19.08500  1.000 27.57906 ? 0   SER   D CA    1 
ATOM   3973 C  C     . SER   D 2 1   ? 69.56500  1.74400   18.84500  1.000 27.51648 ? 0   SER   D C     1 
ATOM   3974 O  O     . SER   D 2 1   ? 69.49100  2.79700   19.47900  1.000 24.71331 ? 0   SER   D O     1 
ATOM   3975 C  CB    . SER   D 2 1   ? 70.33200  -0.21600  20.19600  1.000 20.91126 ? 0   SER   D CB    1 
ATOM   3976 O  OG    . SER   D 2 1   ? 69.06200  -0.81500  19.94900  1.000 25.87999 ? 0   SER   D OG    1 
ATOM   3977 N  N     . MET   D 2 2   ? 68.65100  1.37600   17.94400  1.000 27.43226 ? 1   MET   D N     1 
ATOM   3978 C  CA    . MET   D 2 2   ? 67.45200  2.17800   17.72300  1.000 21.65228 ? 1   MET   D CA    1 
ATOM   3979 C  C     . MET   D 2 2   ? 66.41000  1.99100   18.81600  1.000 19.31448 ? 1   MET   D C     1 
ATOM   3980 O  O     . MET   D 2 2   ? 65.50600  2.82800   18.93500  1.000 24.66965 ? 1   MET   D O     1 
ATOM   3981 C  CB    . MET   D 2 2   ? 66.82000  1.83900   16.36900  1.000 21.14934 ? 1   MET   D CB    1 
ATOM   3982 C  CG    . MET   D 2 2   ? 67.67200  2.21300   15.17600  1.000 26.96634 ? 1   MET   D CG    1 
ATOM   3983 S  SD    . MET   D 2 2   ? 67.85000  4.00200   15.02400  1.000 28.95366 ? 1   MET   D SD    1 
ATOM   3984 C  CE    . MET   D 2 2   ? 66.53900  4.38800   13.85800  1.000 21.31026 ? 1   MET   D CE    1 
ATOM   3985 N  N     . VAL   D 2 3   ? 66.49300  0.90200   19.58900  1.000 19.43262 ? 2   VAL   D N     1 
ATOM   3986 C  CA    . VAL   D 2 3   ? 65.52300  0.59200   20.62900  1.000 16.62823 ? 2   VAL   D CA    1 
ATOM   3987 C  C     . VAL   D 2 3   ? 66.18500  0.42400   21.98800  1.000 19.70590 ? 2   VAL   D C     1 
ATOM   3988 O  O     . VAL   D 2 3   ? 65.62900  0.83800   23.01200  1.000 18.31664 ? 2   VAL   D O     1 
ATOM   3989 C  CB    . VAL   D 2 3   ? 64.70400  -0.67000  20.26800  1.000 19.76292 ? 2   VAL   D CB    1 
ATOM   3990 C  CG1   . VAL   D 2 3   ? 65.62300  -1.83300  19.90200  1.000 15.89757 ? 2   VAL   D CG1   1 
ATOM   3991 C  CG2   . VAL   D 2 3   ? 63.79500  -1.06700  21.41000  1.000 16.32990 ? 2   VAL   D CG2   1 
ATOM   3992 N  N     . ASN   D 2 4   ? 67.38100  -0.15500  22.02000  1.000 16.30099 ? 3   ASN   D N     1 
ATOM   3993 C  CA    . ASN   D 2 4   ? 67.93800  -0.49400  23.31600  1.000 14.13100 ? 3   ASN   D CA    1 
ATOM   3994 C  C     . ASN   D 2 4   ? 68.87500  0.59300   23.81500  1.000 15.01037 ? 3   ASN   D C     1 
ATOM   3995 O  O     . ASN   D 2 4   ? 69.67300  1.14100   23.03900  1.000 11.40391 ? 3   ASN   D O     1 
ATOM   3996 C  CB    . ASN   D 2 4   ? 68.68400  -1.82000  23.23200  1.000 11.98215 ? 3   ASN   D CB    1 
ATOM   3997 C  CG    . ASN   D 2 4   ? 67.73800  -2.99400  23.08400  1.000 12.93446 ? 3   ASN   D CG    1 
ATOM   3998 O  OD1   . ASN   D 2 4   ? 66.58100  -2.92100  23.49500  1.000 11.49193 ? 3   ASN   D OD1   1 
ATOM   3999 N  ND2   . ASN   D 2 4   ? 68.22200  -4.07100  22.48200  1.000 11.23317 ? 3   ASN   D ND2   1 
ATOM   4000 N  N     . PRO   D 2 5   ? 68.76300  0.92500   25.09400  1.000 13.76638 ? 4   PRO   D N     1 
ATOM   4001 C  CA    . PRO   D 2 5   ? 69.62600  1.96200   25.65800  1.000 11.48659 ? 4   PRO   D CA    1 
ATOM   4002 C  C     . PRO   D 2 5   ? 71.06400  1.47800   25.80800  1.000 15.97163 ? 4   PRO   D C     1 
ATOM   4003 O  O     . PRO   D 2 5   ? 71.33600  0.28600   25.97300  1.000 11.25034 ? 4   PRO   D O     1 
ATOM   4004 C  CB    . PRO   D 2 5   ? 68.98000  2.26400   27.01900  1.000 14.26800 ? 4   PRO   D CB    1 
ATOM   4005 C  CG    . PRO   D 2 5   ? 68.12400  1.06600   27.34300  1.000 18.58623 ? 4   PRO   D CG    1 
ATOM   4006 C  CD    . PRO   D 2 5   ? 67.72300  0.46100   26.03300  1.000 12.66928 ? 4   PRO   D CD    1 
ATOM   4007 N  N     . THR   D 2 6   ? 71.99000  2.42700   25.71300  1.000 11.41843 ? 5   THR   D N     1 
ATOM   4008 C  CA    . THR   D 2 6   ? 73.41400  2.17300   25.88600  1.000 10.45172 ? 5   THR   D CA    1 
ATOM   4009 C  C     . THR   D 2 6   ? 73.87400  2.93000   27.12300  1.000 11.71733 ? 5   THR   D C     1 
ATOM   4010 O  O     . THR   D 2 6   ? 73.63600  4.13600   27.23200  1.000 11.10614 ? 5   THR   D O     1 
ATOM   4011 C  CB    . THR   D 2 6   ? 74.21000  2.63300   24.66000  1.000 13.73038 ? 5   THR   D CB    1 
ATOM   4012 O  OG1   . THR   D 2 6   ? 73.73600  1.94800   23.49800  1.000 15.98886 ? 5   THR   D OG1   1 
ATOM   4013 C  CG2   . THR   D 2 6   ? 75.69400  2.33400   24.83000  1.000 16.12417 ? 5   THR   D CG2   1 
ATOM   4014 N  N     . VAL   D 2 7   ? 74.52500  2.23100   28.05400  1.000 11.21431 ? 6   VAL   D N     1 
ATOM   4015 C  CA    . VAL   D 2 7   ? 75.08800  2.87500   29.23000  1.000 8.69015  ? 6   VAL   D CA    1 
ATOM   4016 C  C     . VAL   D 2 7   ? 76.59700  2.65300   29.22900  1.000 11.82161 ? 6   VAL   D C     1 
ATOM   4017 O  O     . VAL   D 2 7   ? 77.11200  1.75100   28.56800  1.000 8.63488  ? 6   VAL   D O     1 
ATOM   4018 C  CB    . VAL   D 2 7   ? 74.43100  2.36800   30.53400  1.000 12.28062 ? 6   VAL   D CB    1 
ATOM   4019 C  CG1   . VAL   D 2 7   ? 72.96500  2.78800   30.56500  1.000 11.05422 ? 6   VAL   D CG1   1 
ATOM   4020 C  CG2   . VAL   D 2 7   ? 74.52800  0.86700   30.64700  1.000 9.99821  ? 6   VAL   D CG2   1 
ATOM   4021 N  N     . PHE   D 2 8   ? 77.31200  3.51900   29.95000  1.000 11.76160 ? 7   PHE   D N     1 
ATOM   4022 C  CA    . PHE   D 2 8   ? 78.76400  3.43200   30.04600  1.000 12.33702 ? 7   PHE   D CA    1 
ATOM   4023 C  C     . PHE   D 2 8   ? 79.21400  3.41700   31.50100  1.000 11.53369 ? 7   PHE   D C     1 
ATOM   4024 O  O     . PHE   D 2 8   ? 78.60100  4.05000   32.36200  1.000 12.80693 ? 7   PHE   D O     1 
ATOM   4025 C  CB    . PHE   D 2 8   ? 79.46200  4.60100   29.30500  1.000 12.50370 ? 7   PHE   D CB    1 
ATOM   4026 C  CG    . PHE   D 2 8   ? 79.35600  5.93400   30.00300  1.000 14.00191 ? 7   PHE   D CG    1 
ATOM   4027 C  CD1   . PHE   D 2 8   ? 78.30300  6.79100   29.73600  1.000 15.03501 ? 7   PHE   D CD1   1 
ATOM   4028 C  CD2   . PHE   D 2 8   ? 80.32400  6.33600   30.91500  1.000 16.52506 ? 7   PHE   D CD2   1 
ATOM   4029 C  CE1   . PHE   D 2 8   ? 78.20000  8.02300   30.36700  1.000 16.62426 ? 7   PHE   D CE1   1 
ATOM   4030 C  CE2   . PHE   D 2 8   ? 80.22000  7.55600   31.56900  1.000 13.65006 ? 7   PHE   D CE2   1 
ATOM   4031 C  CZ    . PHE   D 2 8   ? 79.15800  8.40300   31.28900  1.000 15.13334 ? 7   PHE   D CZ    1 
ATOM   4032 N  N     . PHE   D 2 9   ? 80.30500  2.69300   31.76000  1.000 9.23754  ? 8   PHE   D N     1 
ATOM   4033 C  CA    . PHE   D 2 9   ? 81.06400  2.78400   33.00700  1.000 14.07005 ? 8   PHE   D CA    1 
ATOM   4034 C  C     . PHE   D 2 9   ? 82.44900  3.30700   32.65700  1.000 10.23515 ? 8   PHE   D C     1 
ATOM   4035 O  O     . PHE   D 2 9   ? 83.10400  2.75000   31.77400  1.000 12.50092 ? 8   PHE   D O     1 
ATOM   4036 C  CB    . PHE   D 2 9   ? 81.28200  1.42800   33.70500  1.000 10.62213 ? 8   PHE   D CB    1 
ATOM   4037 C  CG    . PHE   D 2 9   ? 80.04700  0.75900   34.28200  1.000 8.76269  ? 8   PHE   D CG    1 
ATOM   4038 C  CD1   . PHE   D 2 9   ? 78.82600  1.39700   34.36500  1.000 9.12173  ? 8   PHE   D CD1   1 
ATOM   4039 C  CD2   . PHE   D 2 9   ? 80.15800  -0.53500  34.78100  1.000 7.91374  ? 8   PHE   D CD2   1 
ATOM   4040 C  CE1   . PHE   D 2 9   ? 77.71800  0.73600   34.90900  1.000 7.64843  ? 8   PHE   D CE1   1 
ATOM   4041 C  CE2   . PHE   D 2 9   ? 79.06400  -1.20900  35.31800  1.000 8.75245  ? 8   PHE   D CE2   1 
ATOM   4042 C  CZ    . PHE   D 2 9   ? 77.83800  -0.56100  35.39000  1.000 8.07073  ? 8   PHE   D CZ    1 
ATOM   4043 N  N     . ASP   D 2 10  ? 82.91900  4.31800   33.37400  1.000 9.68875  ? 9   ASP   D N     1 
ATOM   4044 C  CA    . ASP   D 2 10  ? 84.32700  4.70400   33.33800  1.000 10.42552 ? 9   ASP   D CA    1 
ATOM   4045 C  C     . ASP   D 2 10  ? 84.99000  4.02800   34.53400  1.000 10.87135 ? 9   ASP   D C     1 
ATOM   4046 O  O     . ASP   D 2 10  ? 84.70300  4.37000   35.69000  1.000 10.09454 ? 9   ASP   D O     1 
ATOM   4047 C  CB    . ASP   D 2 10  ? 84.48600  6.22500   33.35500  1.000 11.32630 ? 9   ASP   D CB    1 
ATOM   4048 C  CG    . ASP   D 2 10  ? 84.09800  6.86900   32.02100  1.000 11.86516 ? 9   ASP   D CG    1 
ATOM   4049 O  OD1   . ASP   D 2 10  ? 84.38600  6.28800   30.94900  1.000 15.50640 ? 9   ASP   D OD1   1 
ATOM   4050 O  OD2   . ASP   D 2 10  ? 83.50100  7.96500   32.02800  1.000 16.16214 ? 9   ASP   D OD2   1 
ATOM   4051 N  N     . ILE   D 2 11  ? 85.83000  3.02000   34.24600  1.000 10.16928 ? 10  ILE   D N     1 
ATOM   4052 C  CA    . ILE   D 2 11  ? 86.44500  2.15000   35.24300  1.000 10.11759 ? 10  ILE   D CA    1 
ATOM   4053 C  C     . ILE   D 2 11  ? 87.73800  2.77600   35.73900  1.000 11.69944 ? 10  ILE   D C     1 
ATOM   4054 O  O     . ILE   D 2 11  ? 88.55200  3.25000   34.93600  1.000 14.93337 ? 10  ILE   D O     1 
ATOM   4055 C  CB    . ILE   D 2 11  ? 86.72300  0.75800   34.63900  1.000 11.07790 ? 10  ILE   D CB    1 
ATOM   4056 C  CG1   . ILE   D 2 11  ? 85.44700  0.16900   34.03600  1.000 10.97507 ? 10  ILE   D CG1   1 
ATOM   4057 C  CG2   . ILE   D 2 11  ? 87.31000  -0.17200  35.69700  1.000 14.37664 ? 10  ILE   D CG2   1 
ATOM   4058 C  CD1   . ILE   D 2 11  ? 84.45300  -0.28400  35.07100  1.000 8.27746  ? 10  ILE   D CD1   1 
ATOM   4059 N  N     . ALA   D 2 12  ? 87.95600  2.73100   37.06100  1.000 11.37662 ? 11  ALA   D N     1 
ATOM   4060 C  CA    . ALA   D 2 12  ? 89.16200  3.26100   37.68500  1.000 14.12790 ? 11  ALA   D CA    1 
ATOM   4061 C  C     . ALA   D 2 12  ? 89.88800  2.18100   38.48100  1.000 11.80135 ? 11  ALA   D C     1 
ATOM   4062 O  O     . ALA   D 2 12  ? 89.27100  1.25200   39.01700  1.000 11.91640 ? 11  ALA   D O     1 
ATOM   4063 C  CB    . ALA   D 2 12  ? 88.83900  4.45000   38.61400  1.000 13.81815 ? 11  ALA   D CB    1 
ATOM   4064 N  N     . VAL   D 2 13  ? 91.21100  2.31000   38.54500  1.000 12.75600 ? 12  VAL   D N     1 
ATOM   4065 C  CA    . VAL   D 2 13  ? 92.07300  1.42600   39.32400  1.000 13.11233 ? 12  VAL   D CA    1 
ATOM   4066 C  C     . VAL   D 2 13  ? 92.76800  2.29800   40.35400  1.000 13.99391 ? 12  VAL   D C     1 
ATOM   4067 O  O     . VAL   D 2 13  ? 93.59200  3.14600   39.99600  1.000 16.25738 ? 12  VAL   D O     1 
ATOM   4068 C  CB    . VAL   D 2 13  ? 93.09200  0.68500   38.44800  1.000 13.69510 ? 12  VAL   D CB    1 
ATOM   4069 C  CG1   . VAL   D 2 13  ? 94.07000  -0.12900  39.31700  1.000 14.32199 ? 12  VAL   D CG1   1 
ATOM   4070 C  CG2   . VAL   D 2 13  ? 92.37200  -0.21600  37.46900  1.000 12.94659 ? 12  VAL   D CG2   1 
ATOM   4071 N  N     . ASP   D 2 14  ? 92.44100  2.09700   41.62700  1.000 16.93145 ? 13  ASP   D N     1 
ATOM   4072 C  CA    . ASP   D 2 14  ? 92.90100  2.97600   42.69900  1.000 17.38056 ? 13  ASP   D CA    1 
ATOM   4073 C  C     . ASP   D 2 14  ? 92.74500  4.44200   42.28300  1.000 18.54653 ? 13  ASP   D C     1 
ATOM   4074 O  O     . ASP   D 2 14  ? 93.64100  5.27000   42.44300  1.000 16.22927 ? 13  ASP   D O     1 
ATOM   4075 C  CB    . ASP   D 2 14  ? 94.35200  2.65500   43.10000  1.000 21.26576 ? 13  ASP   D CB    1 
ATOM   4076 C  CG    . ASP   D 2 14  ? 94.50100  1.30500   43.83500  1.000 19.82987 ? 13  ASP   D CG    1 
ATOM   4077 O  OD1   . ASP   D 2 14  ? 93.51500  0.77400   44.38100  1.000 21.64762 ? 13  ASP   D OD1   1 
ATOM   4078 O  OD2   . ASP   D 2 14  ? 95.63400  0.77100   43.88700  1.000 23.16684 ? 13  ASP   D OD2   1 
ATOM   4079 N  N     . GLY   D 2 15  ? 91.59300  4.75400   41.69300  1.000 16.05294 ? 14  GLY   D N     1 
ATOM   4080 C  CA    . GLY   D 2 15  ? 91.28600  6.11200   41.29600  1.000 16.28945 ? 14  GLY   D CA    1 
ATOM   4081 C  C     . GLY   D 2 15  ? 91.79100  6.54700   39.93300  1.000 21.05542 ? 14  GLY   D C     1 
ATOM   4082 O  O     . GLY   D 2 15  ? 91.33400  7.59000   39.42700  1.000 18.28106 ? 14  GLY   D O     1 
ATOM   4083 N  N     . GLU   D 2 16  ? 92.72000  5.80600   39.32100  1.000 15.44338 ? 15  GLU   D N     1 
ATOM   4084 C  CA    . GLU   D 2 16  ? 93.24500  6.17400   38.00500  1.000 17.09070 ? 15  GLU   D CA    1 
ATOM   4085 C  C     . GLU   D 2 16  ? 92.39100  5.58300   36.88700  1.000 15.66422 ? 15  GLU   D C     1 
ATOM   4086 O  O     . GLU   D 2 16  ? 91.99400  4.42100   36.95900  1.000 14.24831 ? 15  GLU   D O     1 
ATOM   4087 C  CB    . GLU   D 2 16  ? 94.68000  5.69700   37.84200  1.000 16.98451 ? 15  GLU   D CB    1 
ATOM   4088 C  CG    . GLU   D 2 16  ? 95.65200  6.43000   38.74600  1.000 18.20606 ? 15  GLU   D CG    1 
ATOM   4089 C  CD    . GLU   D 2 16  ? 95.80400  7.90000   38.37500  1.000 19.20453 ? 15  GLU   D CD    1 
ATOM   4090 O  OE1   . GLU   D 2 16  ? 95.56800  8.26300   37.19900  1.000 19.49797 ? 15  GLU   D OE1   1 
ATOM   4091 O  OE2   . GLU   D 2 16  ? 96.17600  8.69400   39.25900  1.000 20.04885 ? 15  GLU   D OE2   1 
ATOM   4092 N  N     . PRO   D 2 17  ? 92.12900  6.36300   35.83900  1.000 19.25512 ? 16  PRO   D N     1 
ATOM   4093 C  CA    . PRO   D 2 17  ? 91.27700  5.87800   34.75100  1.000 16.44615 ? 16  PRO   D CA    1 
ATOM   4094 C  C     . PRO   D 2 17  ? 91.89500  4.67300   34.05900  1.000 16.41158 ? 16  PRO   D C     1 
ATOM   4095 O  O     . PRO   D 2 17  ? 93.05700  4.70000   33.65000  1.000 19.83658 ? 16  PRO   D O     1 
ATOM   4096 C  CB    . PRO   D 2 17  ? 91.20100  7.07900   33.80100  1.000 15.89854 ? 16  PRO   D CB    1 
ATOM   4097 C  CG    . PRO   D 2 17  ? 91.65600  8.24100   34.59700  1.000 20.77247 ? 16  PRO   D CG    1 
ATOM   4098 C  CD    . PRO   D 2 17  ? 92.64000  7.71400   35.57000  1.000 20.60700 ? 16  PRO   D CD    1 
ATOM   4099 N  N     . LEU   D 2 18  ? 91.09500  3.62000   33.90400  1.000 13.67690 ? 17  LEU   D N     1 
ATOM   4100 C  CA    . LEU   D 2 18  ? 91.50200  2.49700   33.07000  1.000 15.43685 ? 17  LEU   D CA    1 
ATOM   4101 C  C     . LEU   D 2 18  ? 90.94400  2.63700   31.65700  1.000 17.67520 ? 17  LEU   D C     1 
ATOM   4102 O  O     . LEU   D 2 18  ? 91.69600  2.58800   30.67800  1.000 16.59046 ? 17  LEU   D O     1 
ATOM   4103 C  CB    . LEU   D 2 18  ? 91.04100  1.18500   33.71100  1.000 12.82045 ? 17  LEU   D CB    1 
ATOM   4104 C  CG    . LEU   D 2 18  ? 91.37900  -0.11400  32.97700  1.000 19.06304 ? 17  LEU   D CG    1 
ATOM   4105 C  CD1   . LEU   D 2 18  ? 92.88500  -0.31500  32.89200  1.000 16.57712 ? 17  LEU   D CD1   1 
ATOM   4106 C  CD2   . LEU   D 2 18  ? 90.73000  -1.28600  33.67200  1.000 15.73542 ? 17  LEU   D CD2   1 
ATOM   4107 N  N     . GLY   D 2 19  ? 89.63400  2.83100   31.54400  1.000 13.62795 ? 18  GLY   D N     1 
ATOM   4108 C  CA    . GLY   D 2 19  ? 88.98900  3.01300   30.26100  1.000 13.06122 ? 18  GLY   D CA    1 
ATOM   4109 C  C     . GLY   D 2 19  ? 87.48900  2.88800   30.42900  1.000 12.01114 ? 18  GLY   D C     1 
ATOM   4110 O  O     . GLY   D 2 19  ? 86.97400  2.67900   31.53200  1.000 11.26071 ? 18  GLY   D O     1 
ATOM   4111 N  N     . ARG   D 2 20  ? 86.79000  3.01400   29.31100  1.000 12.09534 ? 19  ARG   D N     1 
ATOM   4112 C  CA    . ARG   D 2 20  ? 85.33300  3.02600   29.32900  1.000 11.32206 ? 19  ARG   D CA    1 
ATOM   4113 C  C     . ARG   D 2 20  ? 84.79100  1.71200   28.78800  1.000 13.39003 ? 19  ARG   D C     1 
ATOM   4114 O  O     . ARG   D 2 20  ? 85.24000  1.23200   27.74100  1.000 15.62201 ? 19  ARG   D O     1 
ATOM   4115 C  CB    . ARG   D 2 20  ? 84.79000  4.20400   28.52100  1.000 11.92306 ? 19  ARG   D CB    1 
ATOM   4116 C  CG    . ARG   D 2 20  ? 83.27000  4.22500   28.43900  1.000 13.06035 ? 19  ARG   D CG    1 
ATOM   4117 C  CD    . ARG   D 2 20  ? 82.79200  5.51000   27.78500  1.000 12.68005 ? 19  ARG   D CD    1 
ATOM   4118 N  NE    . ARG   D 2 20  ? 82.85800  6.63000   28.71300  1.000 16.32367 ? 19  ARG   D NE    1 
ATOM   4119 C  CZ    . ARG   D 2 20  ? 82.26100  7.79800   28.52000  1.000 16.24500 ? 19  ARG   D CZ    1 
ATOM   4120 N  NH1   . ARG   D 2 20  ? 81.60800  8.06200   27.39900  1.000 18.28511 ? 19  ARG   D NH1   1 
ATOM   4121 N  NH2   . ARG   D 2 20  ? 82.30900  8.71800   29.48000  1.000 17.22826 ? 19  ARG   D NH2   1 
ATOM   4122 N  N     . VAL   D 2 21  ? 83.82300  1.14400   29.49400  1.000 9.86553  ? 20  VAL   D N     1 
ATOM   4123 C  CA    . VAL   D 2 21  ? 83.05900  -0.00000  29.01200  1.000 12.41111 ? 20  VAL   D CA    1 
ATOM   4124 C  C     . VAL   D 2 21  ? 81.63800  0.47700   28.77000  1.000 10.80218 ? 20  VAL   D C     1 
ATOM   4125 O  O     . VAL   D 2 21  ? 81.03300  1.09400   29.65500  1.000 11.61287 ? 20  VAL   D O     1 
ATOM   4126 C  CB    . VAL   D 2 21  ? 83.09800  -1.16600  30.01300  1.000 9.92123  ? 20  VAL   D CB    1 
ATOM   4127 C  CG1   . VAL   D 2 21  ? 82.30100  -2.35800  29.47800  1.000 9.63150  ? 20  VAL   D CG1   1 
ATOM   4128 C  CG2   . VAL   D 2 21  ? 84.57100  -1.55600  30.31000  1.000 12.30490 ? 20  VAL   D CG2   1 
ATOM   4129 N  N     . SER   D 2 22  ? 81.12500  0.23700   27.56500  1.000 9.39829  ? 21  SER   D N     1 
ATOM   4130 C  CA    . SER   D 2 22  ? 79.73200  0.53400   27.25500  1.000 12.24826 ? 21  SER   D CA    1 
ATOM   4131 C  C     . SER   D 2 22  ? 78.95200  -0.76900  27.07700  1.000 12.44897 ? 21  SER   D C     1 
ATOM   4132 O  O     . SER   D 2 22  ? 79.50600  -1.80200  26.68400  1.000 10.42401 ? 21  SER   D O     1 
ATOM   4133 C  CB    . SER   D 2 22  ? 79.60500  1.41700   26.00500  1.000 11.87410 ? 21  SER   D CB    1 
ATOM   4134 O  OG    . SER   D 2 22  ? 79.94200  0.71500   24.82300  1.000 15.37572 ? 21  SER   D OG    1 
ATOM   4135 N  N     . PHE   D 2 23  ? 77.65900  -0.70800  27.38500  1.000 8.37027  ? 22  PHE   D N     1 
ATOM   4136 C  CA    . PHE   D 2 23  ? 76.78900  -1.87500  27.37100  1.000 7.97544  ? 22  PHE   D CA    1 
ATOM   4137 C  C     . PHE   D 2 23  ? 75.53400  -1.56900  26.57200  1.000 9.12798  ? 22  PHE   D C     1 
ATOM   4138 O  O     . PHE   D 2 23  ? 74.91800  -0.52000  26.77600  1.000 11.82522 ? 22  PHE   D O     1 
ATOM   4139 C  CB    . PHE   D 2 23  ? 76.33200  -2.26500  28.78200  1.000 7.97825  ? 22  PHE   D CB    1 
ATOM   4140 C  CG    . PHE   D 2 23  ? 77.43400  -2.43800  29.77200  1.000 8.77219  ? 22  PHE   D CG    1 
ATOM   4141 C  CD1   . PHE   D 2 23  ? 77.86800  -1.37100  30.54500  1.000 10.50388 ? 22  PHE   D CD1   1 
ATOM   4142 C  CD2   . PHE   D 2 23  ? 78.01100  -3.68500  29.97100  1.000 9.91659  ? 22  PHE   D CD2   1 
ATOM   4143 C  CE1   . PHE   D 2 23  ? 78.87800  -1.53800  31.48700  1.000 9.55693  ? 22  PHE   D CE1   1 
ATOM   4144 C  CE2   . PHE   D 2 23  ? 79.02800  -3.85200  30.89100  1.000 13.29458 ? 22  PHE   D CE2   1 
ATOM   4145 C  CZ    . PHE   D 2 23  ? 79.45800  -2.77000  31.65800  1.000 10.78047 ? 22  PHE   D CZ    1 
ATOM   4146 N  N     . GLU   D 2 24  ? 75.12000  -2.49200  25.70600  1.000 8.85247  ? 23  GLU   D N     1 
ATOM   4147 C  CA    . GLU   D 2 24  ? 73.74700  -2.46800  25.20800  1.000 8.81929  ? 23  GLU   D CA    1 
ATOM   4148 C  C     . GLU   D 2 24  ? 72.87100  -3.20500  26.20600  1.000 10.25518 ? 23  GLU   D C     1 
ATOM   4149 O  O     . GLU   D 2 24  ? 73.18800  -4.32900  26.60800  1.000 8.50137  ? 23  GLU   D O     1 
ATOM   4150 C  CB    . GLU   D 2 24  ? 73.60700  -3.10300  23.82500  1.000 13.03320 ? 23  GLU   D CB    1 
ATOM   4151 C  CG    . GLU   D 2 24  ? 72.16100  -3.10200  23.31400  1.000 10.64295 ? 23  GLU   D CG    1 
ATOM   4152 C  CD    . GLU   D 2 24  ? 72.04100  -3.53700  21.86900  1.000 17.39202 ? 23  GLU   D CD    1 
ATOM   4153 O  OE1   . GLU   D 2 24  ? 73.02400  -3.37700  21.12200  1.000 22.65761 ? 23  GLU   D OE1   1 
ATOM   4154 O  OE2   . GLU   D 2 24  ? 70.96000  -4.03600  21.48200  1.000 19.43857 ? 23  GLU   D OE2   1 
ATOM   4155 N  N     . LEU   D 2 25  ? 71.77300  -2.56700  26.60500  1.000 8.65918  ? 24  LEU   D N     1 
ATOM   4156 C  CA    . LEU   D 2 25  ? 70.81400  -3.16400  27.51900  1.000 8.49613  ? 24  LEU   D CA    1 
ATOM   4157 C  C     . LEU   D 2 25  ? 69.60100  -3.61200  26.72000  1.000 8.15740  ? 24  LEU   D C     1 
ATOM   4158 O  O     . LEU   D 2 25  ? 69.00200  -2.81400  25.99500  1.000 8.75519  ? 24  LEU   D O     1 
ATOM   4159 C  CB    . LEU   D 2 25  ? 70.40000  -2.18500  28.61700  1.000 8.29711  ? 24  LEU   D CB    1 
ATOM   4160 C  CG    . LEU   D 2 25  ? 71.53600  -1.48300  29.35800  1.000 7.27287  ? 24  LEU   D CG    1 
ATOM   4161 C  CD1   . LEU   D 2 25  ? 70.99700  -0.57600  30.47000  1.000 7.28254  ? 24  LEU   D CD1   1 
ATOM   4162 C  CD2   . LEU   D 2 25  ? 72.55400  -2.47500  29.91200  1.000 8.39421  ? 24  LEU   D CD2   1 
ATOM   4163 N  N     . PHE   D 2 26  ? 69.25600  -4.89000  26.85000  1.000 8.00942  ? 25  PHE   D N     1 
ATOM   4164 C  CA    . PHE   D 2 26  ? 68.28100  -5.53700  25.97200  1.000 11.38253 ? 25  PHE   D CA    1 
ATOM   4165 C  C     . PHE   D 2 26  ? 66.87000  -5.25700  26.48800  1.000 11.58015 ? 25  PHE   D C     1 
ATOM   4166 O  O     . PHE   D 2 26  ? 66.14800  -6.14400  26.95400  1.000 12.09977 ? 25  PHE   D O     1 
ATOM   4167 C  CB    . PHE   D 2 26  ? 68.55700  -7.03500  25.88800  1.000 12.30140 ? 25  PHE   D CB    1 
ATOM   4168 C  CG    . PHE   D 2 26  ? 69.89500  -7.37500  25.28200  1.000 10.99576 ? 25  PHE   D CG    1 
ATOM   4169 C  CD1   . PHE   D 2 26  ? 70.32700  -6.75400  24.13000  1.000 14.97401 ? 25  PHE   D CD1   1 
ATOM   4170 C  CD2   . PHE   D 2 26  ? 70.71200  -8.32800  25.86800  1.000 10.61286 ? 25  PHE   D CD2   1 
ATOM   4171 C  CE1   . PHE   D 2 26  ? 71.56100  -7.06500  23.57000  1.000 18.65237 ? 25  PHE   D CE1   1 
ATOM   4172 C  CE2   . PHE   D 2 26  ? 71.94300  -8.64400  25.32800  1.000 13.35460 ? 25  PHE   D CE2   1 
ATOM   4173 C  CZ    . PHE   D 2 26  ? 72.37000  -8.01200  24.16900  1.000 15.06767 ? 25  PHE   D CZ    1 
ATOM   4174 N  N     . ALA   D 2 27  ? 66.48200  -3.98000  26.39100  1.000 10.51508 ? 26  ALA   D N     1 
ATOM   4175 C  CA    . ALA   D 2 27  ? 65.14400  -3.58000  26.82400  1.000 12.02047 ? 26  ALA   D CA    1 
ATOM   4176 C  C     . ALA   D 2 27  ? 64.06200  -4.16000  25.93000  1.000 12.81743 ? 26  ALA   D C     1 
ATOM   4177 O  O     . ALA   D 2 27  ? 62.92900  -4.35200  26.38300  1.000 13.19206 ? 26  ALA   D O     1 
ATOM   4178 C  CB    . ALA   D 2 27  ? 65.03200  -2.06200  26.87000  1.000 10.43023 ? 26  ALA   D CB    1 
ATOM   4179 N  N     . ASP   D 2 28  ? 64.38800  -4.44000  24.66500  1.000 10.85320 ? 27  ASP   D N     1 
ATOM   4180 C  CA    . ASP   D 2 28  ? 63.41600  -5.04500  23.76100  1.000 14.17651 ? 27  ASP   D CA    1 
ATOM   4181 C  C     . ASP   D 2 28  ? 62.93900  -6.40400  24.27000  1.000 15.07211 ? 27  ASP   D C     1 
ATOM   4182 O  O     . ASP   D 2 28  ? 61.77800  -6.76300  24.05900  1.000 13.53180 ? 27  ASP   D O     1 
ATOM   4183 C  CB    . ASP   D 2 28  ? 63.99900  -5.17000  22.34800  1.000 12.83939 ? 27  ASP   D CB    1 
ATOM   4184 C  CG    . ASP   D 2 28  ? 65.39000  -5.82500  22.32000  1.000 15.90398 ? 27  ASP   D CG    1 
ATOM   4185 O  OD1   . ASP   D 2 28  ? 65.94600  -6.15600  23.38200  1.000 12.75476 ? 27  ASP   D OD1   1 
ATOM   4186 O  OD2   . ASP   D 2 28  ? 65.92800  -5.99900  21.21700  1.000 18.71589 ? 27  ASP   D OD2   1 
ATOM   4187 N  N     . LYS   D 2 29  ? 63.79800  -7.14900  24.96800  1.000 11.07454 ? 28  LYS   D N     1 
ATOM   4188 C  CA    . LYS   D 2 29  ? 63.45500  -8.47500  25.46200  1.000 13.72138 ? 28  LYS   D CA    1 
ATOM   4189 C  C     . LYS   D 2 29  ? 63.37900  -8.57500  26.98100  1.000 13.05902 ? 28  LYS   D C     1 
ATOM   4190 O  O     . LYS   D 2 29  ? 62.70500  -9.48000  27.48900  1.000 14.74766 ? 28  LYS   D O     1 
ATOM   4191 C  CB    . LYS   D 2 29  ? 64.47100  -9.50500  24.94900  1.000 12.60795 ? 28  LYS   D CB    1 
ATOM   4192 C  CG    . LYS   D 2 29  ? 64.49000  -9.63300  23.43400  1.000 16.84679 ? 28  LYS   D CG    1 
ATOM   4193 C  CD    . LYS   D 2 29  ? 65.57200  -10.59700 22.97100  1.000 23.19356 ? 28  LYS   D CD    1 
ATOM   4194 C  CE    . LYS   D 2 29  ? 65.61800  -10.66500 21.44700  1.000 27.60188 ? 28  LYS   D CE    1 
ATOM   4195 N  NZ    . LYS   D 2 29  ? 64.23900  -10.83300 20.89600  1.000 34.77824 ? 28  LYS   D NZ    1 
ATOM   4196 N  N     . VAL   D 2 30  ? 64.05700  -7.69500  27.71800  1.000 11.49173 ? 29  VAL   D N     1 
ATOM   4197 C  CA    . VAL   D 2 30  ? 64.05300  -7.76700  29.18000  1.000 9.63822  ? 29  VAL   D CA    1 
ATOM   4198 C  C     . VAL   D 2 30  ? 63.82500  -6.36300  29.73900  1.000 8.95845  ? 29  VAL   D C     1 
ATOM   4199 O  O     . VAL   D 2 30  ? 64.70000  -5.81600  30.43000  1.000 8.14946  ? 29  VAL   D O     1 
ATOM   4200 C  CB    . VAL   D 2 30  ? 65.35300  -8.40800  29.71400  1.000 11.55046 ? 29  VAL   D CB    1 
ATOM   4201 C  CG1   . VAL   D 2 30  ? 65.06800  -9.26600  30.93600  1.000 9.15966  ? 29  VAL   D CG1   1 
ATOM   4202 C  CG2   . VAL   D 2 30  ? 66.01900  -9.27700  28.63500  1.000 10.99399 ? 29  VAL   D CG2   1 
ATOM   4203 N  N     . PRO   D 2 31  ? 62.64700  -5.76800  29.50200  1.000 9.36850  ? 30  PRO   D N     1 
ATOM   4204 C  CA    . PRO   D 2 31  ? 62.47100  -4.33600  29.79400  1.000 11.63471 ? 30  PRO   D CA    1 
ATOM   4205 C  C     . PRO   D 2 31  ? 62.60400  -3.95800  31.26400  1.000 9.80438  ? 30  PRO   D C     1 
ATOM   4206 O  O     . PRO   D 2 31  ? 63.21500  -2.92600  31.55200  1.000 14.11712 ? 30  PRO   D O     1 
ATOM   4207 C  CB    . PRO   D 2 31  ? 61.05700  -4.04800  29.25300  1.000 12.24357 ? 30  PRO   D CB    1 
ATOM   4208 C  CG    . PRO   D 2 31  ? 60.36000  -5.39300  29.23900  1.000 13.70350 ? 30  PRO   D CG    1 
ATOM   4209 C  CD    . PRO   D 2 31  ? 61.44000  -6.37000  28.89900  1.000 10.15157 ? 30  PRO   D CD    1 
ATOM   4210 N  N     . LYS   D 2 32  ? 62.04600  -4.72400  32.20700  1.000 9.27908  ? 31  LYS   D N     1 
ATOM   4211 C  CA    . LYS   D 2 32  ? 62.11000  -4.29300  33.60400  1.000 11.02193 ? 31  LYS   D CA    1 
ATOM   4212 C  C     . LYS   D 2 32  ? 63.54000  -4.34500  34.12200  1.000 11.18180 ? 31  LYS   D C     1 
ATOM   4213 O  O     . LYS   D 2 32  ? 63.98100  -3.44800  34.84700  1.000 11.50765 ? 31  LYS   D O     1 
ATOM   4214 C  CB    . LYS   D 2 32  ? 61.20800  -5.15100  34.49700  1.000 14.10188 ? 31  LYS   D CB    1 
ATOM   4215 C  CG    . LYS   D 2 32  ? 59.70700  -4.88000  34.39000  1.000 21.70174 ? 31  LYS   D CG    1 
ATOM   4216 C  CD    . LYS   D 2 32  ? 58.97000  -5.48400  35.60500  1.000 31.45854 ? 31  LYS   D CD    1 
ATOM   4217 C  CE    . LYS   D 2 32  ? 59.48600  -4.86700  36.93100  1.000 36.47620 ? 31  LYS   D CE    1 
ATOM   4218 N  NZ    . LYS   D 2 32  ? 59.28300  -5.70600  38.16700  1.000 31.16883 ? 31  LYS   D NZ    1 
ATOM   4219 N  N     . THR   D 2 33  ? 64.27300  -5.38900  33.74500  1.000 8.62501  ? 32  THR   D N     1 
ATOM   4220 C  CA    . THR   D 2 33  ? 65.63700  -5.57600  34.22100  1.000 8.23446  ? 32  THR   D CA    1 
ATOM   4221 C  C     . THR   D 2 33  ? 66.60200  -4.60000  33.55400  1.000 11.01102 ? 32  THR   D C     1 
ATOM   4222 O  O     . THR   D 2 33  ? 67.47900  -4.03300  34.21800  1.000 9.83591  ? 32  THR   D O     1 
ATOM   4223 C  CB    . THR   D 2 33  ? 66.06000  -7.02200  33.96500  1.000 6.97946  ? 32  THR   D CB    1 
ATOM   4224 O  OG1   . THR   D 2 33  ? 65.07900  -7.92700  34.51300  1.000 7.81336  ? 32  THR   D OG1   1 
ATOM   4225 C  CG2   . THR   D 2 33  ? 67.40800  -7.29300  34.60700  1.000 7.68399  ? 32  THR   D CG2   1 
ATOM   4226 N  N     . ALA   D 2 34  ? 66.46700  -4.39700  32.24300  1.000 9.20855  ? 33  ALA   D N     1 
ATOM   4227 C  CA    . ALA   D 2 34  ? 67.26600  -3.37000  31.58100  1.000 7.25149  ? 33  ALA   D CA    1 
ATOM   4228 C  C     . ALA   D 2 34  ? 67.02700  -1.98500  32.18900  1.000 9.58179  ? 33  ALA   D C     1 
ATOM   4229 O  O     . ALA   D 2 34  ? 67.98300  -1.24300  32.44800  1.000 8.73952  ? 33  ALA   D O     1 
ATOM   4230 C  CB    . ALA   D 2 34  ? 66.96600  -3.36200  30.08400  1.000 7.69734  ? 33  ALA   D CB    1 
ATOM   4231 N  N     . GLU   D 2 35  ? 65.76100  -1.61700  32.42700  1.000 9.62056  ? 34  GLU   D N     1 
ATOM   4232 C  CA    . GLU   D 2 35  ? 65.46300  -0.29700  32.99300  1.000 8.59612  ? 34  GLU   D CA    1 
ATOM   4233 C  C     . GLU   D 2 35  ? 66.08700  -0.11000  34.37800  1.000 13.75228 ? 34  GLU   D C     1 
ATOM   4234 O  O     . GLU   D 2 35  ? 66.61000  0.96800   34.69200  1.000 10.55426 ? 34  GLU   D O     1 
ATOM   4235 C  CB    . GLU   D 2 35  ? 63.94800  -0.08200  33.04300  1.000 12.15953 ? 34  GLU   D CB    1 
ATOM   4236 C  CG    . GLU   D 2 35  ? 63.51000  1.14800   33.84500  1.000 11.63955 ? 34  GLU   D CG    1 
ATOM   4237 C  CD    . GLU   D 2 35  ? 63.96800  2.45800   33.23000  1.000 14.39516 ? 34  GLU   D CD    1 
ATOM   4238 O  OE1   . GLU   D 2 35  ? 64.36800  2.44900   32.04200  1.000 13.02084 ? 34  GLU   D OE1   1 
ATOM   4239 O  OE2   . GLU   D 2 35  ? 63.92300  3.50600   33.93100  1.000 13.52169 ? 34  GLU   D OE2   1 
ATOM   4240 N  N     . ASN   D 2 36  ? 66.04700  -1.14500  35.22200  1.000 11.92323 ? 35  ASN   D N     1 
ATOM   4241 C  CA    . ASN   D 2 36  ? 66.74100  -1.08600  36.50900  1.000 10.78553 ? 35  ASN   D CA    1 
ATOM   4242 C  C     . ASN   D 2 36  ? 68.20800  -0.69600  36.32900  1.000 12.88428 ? 35  ASN   D C     1 
ATOM   4243 O  O     . ASN   D 2 36  ? 68.67300  0.31800   36.87200  1.000 10.48944 ? 35  ASN   D O     1 
ATOM   4244 C  CB    . ASN   D 2 36  ? 66.61800  -2.43700  37.22400  1.000 11.09187 ? 35  ASN   D CB    1 
ATOM   4245 C  CG    . ASN   D 2 36  ? 67.28500  -2.44400  38.58700  1.000 11.15986 ? 35  ASN   D CG    1 
ATOM   4246 O  OD1   . ASN   D 2 36  ? 66.93200  -1.65800  39.46400  1.000 9.89610  ? 35  ASN   D OD1   1 
ATOM   4247 N  ND2   . ASN   D 2 36  ? 68.25200  -3.34200  38.77300  1.000 10.62370 ? 35  ASN   D ND2   1 
ATOM   4248 N  N     . PHE   D 2 37  ? 68.93800  -1.47100  35.52400  1.000 6.78768  ? 36  PHE   D N     1 
ATOM   4249 C  CA    . PHE   D 2 37  ? 70.35700  -1.20400  35.30500  1.000 8.26038  ? 36  PHE   D CA    1 
ATOM   4250 C  C     . PHE   D 2 37  ? 70.56600  0.18500   34.71500  1.000 9.90414  ? 36  PHE   D C     1 
ATOM   4251 O  O     . PHE   D 2 37  ? 71.46900  0.92000   35.14100  1.000 9.73520  ? 36  PHE   D O     1 
ATOM   4252 C  CB    . PHE   D 2 37  ? 70.94000  -2.28300  34.39300  1.000 10.20062 ? 36  PHE   D CB    1 
ATOM   4253 C  CG    . PHE   D 2 37  ? 72.44600  -2.31200  34.35400  1.000 7.86981  ? 36  PHE   D CG    1 
ATOM   4254 C  CD1   . PHE   D 2 37  ? 73.13700  -1.54200  33.44200  1.000 6.84430  ? 36  PHE   D CD1   1 
ATOM   4255 C  CD2   . PHE   D 2 37  ? 73.15100  -3.11000  35.23500  1.000 8.92319  ? 36  PHE   D CD2   1 
ATOM   4256 C  CE1   . PHE   D 2 37  ? 74.51700  -1.56600  33.38400  1.000 10.37957 ? 36  PHE   D CE1   1 
ATOM   4257 C  CE2   . PHE   D 2 37  ? 74.53600  -3.15400  35.19200  1.000 8.21985  ? 36  PHE   D CE2   1 
ATOM   4258 C  CZ    . PHE   D 2 37  ? 75.21400  -2.37000  34.26600  1.000 7.67388  ? 36  PHE   D CZ    1 
ATOM   4259 N  N     . ARG   D 2 38  ? 69.70900  0.57500   33.76300  1.000 7.36109  ? 37  ARG   D N     1 
ATOM   4260 C  CA    . ARG   D 2 38  ? 69.80000  1.91300   33.17300  1.000 10.34310 ? 37  ARG   D CA    1 
ATOM   4261 C  C     . ARG   D 2 38  ? 69.66600  2.99000   34.23800  1.000 12.84457 ? 37  ARG   D C     1 
ATOM   4262 O  O     . ARG   D 2 38  ? 70.47000  3.93000   34.30000  1.000 11.97464 ? 37  ARG   D O     1 
ATOM   4263 C  CB    . ARG   D 2 38  ? 68.71200  2.12000   32.11600  1.000 8.51497  ? 37  ARG   D CB    1 
ATOM   4264 C  CG    . ARG   D 2 38  ? 68.88800  3.42000   31.30100  1.000 9.26608  ? 37  ARG   D CG    1 
ATOM   4265 C  CD    . ARG   D 2 38  ? 67.61000  3.83700   30.56500  1.000 12.21749 ? 37  ARG   D CD    1 
ATOM   4266 N  NE    . ARG   D 2 38  ? 66.53400  4.12100   31.49900  1.000 10.63302 ? 37  ARG   D NE    1 
ATOM   4267 C  CZ    . ARG   D 2 38  ? 66.47200  5.19600   32.27100  1.000 12.66973 ? 37  ARG   D CZ    1 
ATOM   4268 N  NH1   . ARG   D 2 38  ? 67.38000  6.15300   32.19200  1.000 11.29603 ? 37  ARG   D NH1   1 
ATOM   4269 N  NH2   . ARG   D 2 38  ? 65.47600  5.30500   33.15000  1.000 14.78841 ? 37  ARG   D NH2   1 
ATOM   4270 N  N     . ALA   D 2 39  ? 68.61800  2.89900   35.05800  1.000 10.49718 ? 38  ALA   D N     1 
ATOM   4271 C  CA    . ALA   D 2 39  ? 68.36800  3.96200   36.02900  1.000 9.47115  ? 38  ALA   D CA    1 
ATOM   4272 C  C     . ALA   D 2 39  ? 69.46300  4.01000   37.10300  1.000 12.62664 ? 38  ALA   D C     1 
ATOM   4273 O  O     . ALA   D 2 39  ? 69.84200  5.09300   37.57500  1.000 10.78985 ? 38  ALA   D O     1 
ATOM   4274 C  CB    . ALA   D 2 39  ? 66.97800  3.76900   36.63400  1.000 13.76787 ? 38  ALA   D CB    1 
ATOM   4275 N  N     . LEU   D 2 40  ? 69.99500  2.85000   37.49100  1.000 9.17603  ? 39  LEU   D N     1 
ATOM   4276 C  CA    . LEU   D 2 40  ? 71.11000  2.82600   38.43300  1.000 9.00073  ? 39  LEU   D CA    1 
ATOM   4277 C  C     . LEU   D 2 40  ? 72.38700  3.38900   37.81200  1.000 8.06541  ? 39  LEU   D C     1 
ATOM   4278 O  O     . LEU   D 2 40  ? 73.24700  3.90500   38.53300  1.000 10.52856 ? 39  LEU   D O     1 
ATOM   4279 C  CB    . LEU   D 2 40  ? 71.33300  1.39800   38.93800  1.000 8.71566  ? 39  LEU   D CB    1 
ATOM   4280 C  CG    . LEU   D 2 40  ? 70.20100  0.75600   39.76100  1.000 8.27505  ? 39  LEU   D CG    1 
ATOM   4281 C  CD1   . LEU   D 2 40  ? 70.49100  -0.71900  40.03300  1.000 7.03635  ? 39  LEU   D CD1   1 
ATOM   4282 C  CD2   . LEU   D 2 40  ? 69.97200  1.52700   41.07700  1.000 12.10614 ? 39  LEU   D CD2   1 
ATOM   4283 N  N     . SER   D 2 41  ? 72.53900  3.29600   36.48400  1.000 9.91099  ? 40  SER   D N     1 
ATOM   4284 C  CA    . SER   D 2 41  ? 73.72600  3.84800   35.83900  1.000 8.95457  ? 40  SER   D CA    1 
ATOM   4285 C  C     . SER   D 2 41  ? 73.65600  5.36700   35.71400  1.000 10.07857 ? 40  SER   D C     1 
ATOM   4286 O  O     . SER   D 2 41  ? 74.69000  6.03700   35.81300  1.000 11.18851 ? 40  SER   D O     1 
ATOM   4287 C  CB    . SER   D 2 41  ? 73.92200  3.22300   34.45400  1.000 9.54324  ? 40  SER   D CB    1 
ATOM   4288 O  OG    . SER   D 2 41  ? 74.13700  1.82800   34.55600  1.000 8.78583  ? 40  SER   D OG    1 
ATOM   4289 N  N     . THR   D 2 42  ? 72.46500  5.93200   35.48600  1.000 12.23661 ? 41  THR   D N     1 
ATOM   4290 C  CA    . THR   D 2 42  ? 72.34200  7.38800   35.46500  1.000 12.74015 ? 41  THR   D CA    1 
ATOM   4291 C  C     . THR   D 2 42  ? 72.24100  7.98700   36.86400  1.000 12.70411 ? 41  THR   D C     1 
ATOM   4292 O  O     . THR   D 2 42  ? 72.49000  9.18500   37.02400  1.000 15.98759 ? 41  THR   D O     1 
ATOM   4293 C  CB    . THR   D 2 42  ? 71.10600  7.84900   34.69200  1.000 12.82216 ? 41  THR   D CB    1 
ATOM   4294 O  OG1   . THR   D 2 42  ? 69.95400  7.56500   35.48500  1.000 13.79251 ? 41  THR   D OG1   1 
ATOM   4295 C  CG2   . THR   D 2 42  ? 70.99300  7.14900   33.34400  1.000 17.34082 ? 41  THR   D CG2   1 
ATOM   4296 N  N     . GLY   D 2 43  ? 71.85900  7.19800   37.86400  1.000 12.08011 ? 42  GLY   D N     1 
ATOM   4297 C  CA    . GLY   D 2 43  ? 71.64700  7.73200   39.19700  1.000 13.46172 ? 42  GLY   D CA    1 
ATOM   4298 C  C     . GLY   D 2 43  ? 70.41400  8.60100   39.36100  1.000 15.77587 ? 42  GLY   D C     1 
ATOM   4299 O  O     . GLY   D 2 43  ? 70.27800  9.28100   40.38200  1.000 15.17464 ? 42  GLY   D O     1 
ATOM   4300 N  N     . GLU   D 2 44  ? 69.48400  8.57000   38.40000  1.000 16.01520 ? 43  GLU   D N     1 
ATOM   4301 C  CA    . GLU   D 2 44  ? 68.35000  9.49600   38.41600  1.000 13.55765 ? 43  GLU   D CA    1 
ATOM   4302 C  C     . GLU   D 2 44  ? 67.38100  9.25300   39.57200  1.000 20.25045 ? 43  GLU   D C     1 
ATOM   4303 O  O     . GLU   D 2 44  ? 66.54100  10.11700  39.84400  1.000 18.05864 ? 43  GLU   D O     1 
ATOM   4304 C  CB    . GLU   D 2 44  ? 67.59700  9.41200   37.09400  1.000 18.42552 ? 43  GLU   D CB    1 
ATOM   4305 C  CG    . GLU   D 2 44  ? 67.09800  8.02100   36.75500  1.000 16.77527 ? 43  GLU   D CG    1 
ATOM   4306 C  CD    . GLU   D 2 44  ? 66.60500  7.94100   35.32600  1.000 20.72803 ? 43  GLU   D CD    1 
ATOM   4307 O  OE1   . GLU   D 2 44  ? 67.44500  7.93000   34.40200  1.000 14.63765 ? 43  GLU   D OE1   1 
ATOM   4308 O  OE2   . GLU   D 2 44  ? 65.37400  7.91300   35.12700  1.000 17.79830 ? 43  GLU   D OE2   1 
ATOM   4309 N  N     . LYS   D 2 45  ? 67.46300  8.10600   40.25000  1.000 16.71785 ? 44  LYS   D N     1 
ATOM   4310 C  CA    . LYS   D 2 45  ? 66.62900  7.85400   41.42000  1.000 14.16871 ? 44  LYS   D CA    1 
ATOM   4311 C  C     . LYS   D 2 45  ? 67.25100  8.36000   42.70900  1.000 15.61887 ? 44  LYS   D C     1 
ATOM   4312 O  O     . LYS   D 2 45  ? 66.61000  8.26800   43.75900  1.000 19.33826 ? 44  LYS   D O     1 
ATOM   4313 C  CB    . LYS   D 2 45  ? 66.34100  6.35600   41.57800  1.000 13.51117 ? 44  LYS   D CB    1 
ATOM   4314 C  CG    . LYS   D 2 45  ? 65.73300  5.69700   40.37300  1.000 17.59712 ? 44  LYS   D CG    1 
ATOM   4315 C  CD    . LYS   D 2 45  ? 64.44200  6.37100   39.94600  1.000 17.74910 ? 44  LYS   D CD    1 
ATOM   4316 C  CE    . LYS   D 2 45  ? 63.72400  5.50900   38.91100  1.000 25.67667 ? 44  LYS   D CE    1 
ATOM   4317 N  NZ    . LYS   D 2 45  ? 62.53800  6.18900   38.31600  1.000 23.11397 ? 44  LYS   D NZ    1 
ATOM   4318 N  N     . GLY   D 2 46  ? 68.47100  8.88900   42.65800  1.000 18.05622 ? 45  GLY   D N     1 
ATOM   4319 C  CA    . GLY   D 2 46  ? 69.15600  9.36100   43.84400  1.000 14.68341 ? 45  GLY   D CA    1 
ATOM   4320 C  C     . GLY   D 2 46  ? 70.14600  8.37500   44.41200  1.000 17.19104 ? 45  GLY   D C     1 
ATOM   4321 O  O     . GLY   D 2 46  ? 70.70900  8.63400   45.48100  1.000 16.88539 ? 45  GLY   D O     1 
ATOM   4322 N  N     . PHE   D 2 47  ? 70.36800  7.25700   43.72900  1.000 14.40501 ? 46  PHE   D N     1 
ATOM   4323 C  CA    . PHE   D 2 47  ? 71.30200  6.22300   44.14700  1.000 14.48781 ? 46  PHE   D CA    1 
ATOM   4324 C  C     . PHE   D 2 47  ? 71.67600  5.42900   42.90500  1.000 11.93063 ? 46  PHE   D C     1 
ATOM   4325 O  O     . PHE   D 2 47  ? 70.99500  5.48900   41.88000  1.000 13.46393 ? 46  PHE   D O     1 
ATOM   4326 C  CB    . PHE   D 2 47  ? 70.70800  5.32300   45.24700  1.000 11.68497 ? 46  PHE   D CB    1 
ATOM   4327 C  CG    . PHE   D 2 47  ? 69.37900  4.71200   44.89200  1.000 12.34896 ? 46  PHE   D CG    1 
ATOM   4328 C  CD1   . PHE   D 2 47  ? 69.30600  3.51900   44.18000  1.000 13.24948 ? 46  PHE   D CD1   1 
ATOM   4329 C  CD2   . PHE   D 2 47  ? 68.19900  5.31300   45.28600  1.000 13.39236 ? 46  PHE   D CD2   1 
ATOM   4330 C  CE1   . PHE   D 2 47  ? 68.07900  2.96700   43.85200  1.000 13.46829 ? 46  PHE   D CE1   1 
ATOM   4331 C  CE2   . PHE   D 2 47  ? 66.97500  4.74200   44.96900  1.000 16.19270 ? 46  PHE   D CE2   1 
ATOM   4332 C  CZ    . PHE   D 2 47  ? 66.92000  3.57200   44.24900  1.000 12.56418 ? 46  PHE   D CZ    1 
ATOM   4333 N  N     . GLY   D 2 48  ? 72.78400  4.70700   42.98700  1.000 10.27464 ? 47  GLY   D N     1 
ATOM   4334 C  CA    . GLY   D 2 48  ? 73.20600  3.96700   41.81600  1.000 9.78291  ? 47  GLY   D CA    1 
ATOM   4335 C  C     . GLY   D 2 48  ? 74.66400  3.57400   41.91500  1.000 11.15332 ? 47  GLY   D C     1 
ATOM   4336 O  O     . GLY   D 2 48  ? 75.26400  3.62700   42.98700  1.000 11.68375 ? 47  GLY   D O     1 
ATOM   4337 N  N     . TYR   D 2 49  ? 75.20400  3.19500   40.75400  1.000 10.23575 ? 48  TYR   D N     1 
ATOM   4338 C  CA    . TYR   D 2 49  ? 76.50000  2.53100   40.64100  1.000 10.66807 ? 48  TYR   D CA    1 
ATOM   4339 C  C     . TYR   D 2 49  ? 77.69400  3.46300   40.77900  1.000 11.15856 ? 48  TYR   D C     1 
ATOM   4340 O  O     . TYR   D 2 49  ? 78.79000  2.97300   41.06000  1.000 10.10545 ? 48  TYR   D O     1 
ATOM   4341 C  CB    . TYR   D 2 49  ? 76.61600  1.83300   39.29400  1.000 7.18860  ? 48  TYR   D CB    1 
ATOM   4342 C  CG    . TYR   D 2 49  ? 75.66400  0.65900   39.10600  1.000 8.86740  ? 48  TYR   D CG    1 
ATOM   4343 C  CD1   . TYR   D 2 49  ? 75.50000  -0.29400  40.09700  1.000 9.49611  ? 48  TYR   D CD1   1 
ATOM   4344 C  CD2   . TYR   D 2 49  ? 74.96700  0.50100   37.92300  1.000 9.08044  ? 48  TYR   D CD2   1 
ATOM   4345 C  CE1   . TYR   D 2 49  ? 74.64100  -1.37300  39.92300  1.000 8.48669  ? 48  TYR   D CE1   1 
ATOM   4346 C  CE2   . TYR   D 2 49  ? 74.09800  -0.56100  37.73400  1.000 7.15537  ? 48  TYR   D CE2   1 
ATOM   4347 C  CZ    . TYR   D 2 49  ? 73.94700  -1.50200  38.73200  1.000 9.65180  ? 48  TYR   D CZ    1 
ATOM   4348 O  OH    . TYR   D 2 49  ? 73.09400  -2.57200  38.52900  1.000 8.13690  ? 48  TYR   D OH    1 
ATOM   4349 N  N     . LYS   D 2 50  ? 77.53100  4.76900   40.54000  1.000 11.95683 ? 49  LYS   D N     1 
ATOM   4350 C  CA    . LYS   D 2 50  ? 78.68900  5.66500   40.52900  1.000 11.67065 ? 49  LYS   D CA    1 
ATOM   4351 C  C     . LYS   D 2 50  ? 79.42000  5.60100   41.86300  1.000 10.43124 ? 49  LYS   D C     1 
ATOM   4352 O  O     . LYS   D 2 50  ? 78.82700  5.83800   42.91800  1.000 11.47936 ? 49  LYS   D O     1 
ATOM   4353 C  CB    . LYS   D 2 50  ? 78.25500  7.09800   40.21600  1.000 10.90511 ? 49  LYS   D CB    1 
ATOM   4354 C  CG    . LYS   D 2 50  ? 79.43400  8.09100   40.06400  1.000 14.43593 ? 49  LYS   D CG    1 
ATOM   4355 C  CD    . LYS   D 2 50  ? 78.92800  9.41100   39.53200  1.000 16.31139 ? 49  LYS   D CD    1 
ATOM   4356 C  CE    . LYS   D 2 50  ? 80.06400  10.31200  39.07900  1.000 19.11937 ? 49  LYS   D CE    1 
ATOM   4357 N  NZ    . LYS   D 2 50  ? 79.47700  11.55700  38.49300  1.000 19.88269 ? 49  LYS   D NZ    1 
ATOM   4358 N  N     . GLY   D 2 51  ? 80.70400  5.23400   41.82000  1.000 13.65923 ? 50  GLY   D N     1 
ATOM   4359 C  CA    . GLY   D 2 51  ? 81.52700  5.11300   43.00500  1.000 12.15052 ? 50  GLY   D CA    1 
ATOM   4360 C  C     . GLY   D 2 51  ? 81.67400  3.69900   43.54100  1.000 9.66770  ? 50  GLY   D C     1 
ATOM   4361 O  O     . GLY   D 2 51  ? 82.61700  3.43400   44.29900  1.000 12.01749 ? 50  GLY   D O     1 
ATOM   4362 N  N     . SER   D 2 52  ? 80.75800  2.80200   43.19100  1.000 8.95953  ? 51  SER   D N     1 
ATOM   4363 C  CA    . SER   D 2 52  ? 80.79400  1.43000   43.67800  1.000 10.50429 ? 51  SER   D CA    1 
ATOM   4364 C  C     . SER   D 2 52  ? 81.90900  0.65400   42.97600  1.000 10.01783 ? 51  SER   D C     1 
ATOM   4365 O  O     . SER   D 2 52  ? 82.55500  1.13800   42.03800  1.000 11.84724 ? 51  SER   D O     1 
ATOM   4366 C  CB    . SER   D 2 52  ? 79.44000  0.75000   43.47200  1.000 7.93969  ? 51  SER   D CB    1 
ATOM   4367 O  OG    . SER   D 2 52  ? 79.18200  0.54400   42.09000  1.000 7.73370  ? 51  SER   D OG    1 
ATOM   4368 N  N     . SER   D 2 53  ? 82.15700  -0.55700  43.45800  1.000 10.69274 ? 52  SER   D N     1 
ATOM   4369 C  CA    . SER   D 2 53  ? 83.33500  -1.30600  43.04800  1.000 12.56236 ? 52  SER   D CA    1 
ATOM   4370 C  C     . SER   D 2 53  ? 82.96000  -2.65200  42.44200  1.000 8.72719  ? 52  SER   D C     1 
ATOM   4371 O  O     . SER   D 2 53  ? 81.84100  -3.15000  42.60200  1.000 8.54918  ? 52  SER   D O     1 
ATOM   4372 C  CB    . SER   D 2 53  ? 84.28400  -1.53200  44.22700  1.000 12.54167 ? 52  SER   D CB    1 
ATOM   4373 O  OG    . SER   D 2 53  ? 83.70400  -2.41800  45.17400  1.000 17.34161 ? 52  SER   D OG    1 
ATOM   4374 N  N     . PHE   D 2 54  ? 83.91600  -3.21200  41.70700  1.000 12.41752 ? 53  PHE   D N     1 
ATOM   4375 C  CA    . PHE   D 2 54  ? 83.87900  -4.61900  41.30100  1.000 10.26481 ? 53  PHE   D CA    1 
ATOM   4376 C  C     . PHE   D 2 54  ? 84.59800  -5.39900  42.39300  1.000 10.66427 ? 53  PHE   D C     1 
ATOM   4377 O  O     . PHE   D 2 54  ? 85.83200  -5.42100  42.45600  1.000 12.36487 ? 53  PHE   D O     1 
ATOM   4378 C  CB    . PHE   D 2 54  ? 84.52200  -4.81400  39.93200  1.000 10.62743 ? 53  PHE   D CB    1 
ATOM   4379 C  CG    . PHE   D 2 54  ? 83.64300  -4.39700  38.78900  1.000 9.83481  ? 53  PHE   D CG    1 
ATOM   4380 C  CD1   . PHE   D 2 54  ? 83.55900  -3.06600  38.40900  1.000 7.22409  ? 53  PHE   D CD1   1 
ATOM   4381 C  CD2   . PHE   D 2 54  ? 82.89700  -5.33600  38.09000  1.000 10.22162 ? 53  PHE   D CD2   1 
ATOM   4382 C  CE1   . PHE   D 2 54  ? 82.74000  -2.67600  37.35300  1.000 9.17857  ? 53  PHE   D CE1   1 
ATOM   4383 C  CE2   . PHE   D 2 54  ? 82.08800  -4.96300  37.03500  1.000 9.20440  ? 53  PHE   D CE2   1 
ATOM   4384 C  CZ    . PHE   D 2 54  ? 81.99700  -3.61800  36.67000  1.000 9.79193  ? 53  PHE   D CZ    1 
ATOM   4385 N  N     . HIS   D 2 55  ? 83.82100  -5.99900  43.28800  1.000 11.10880 ? 54  HIS   D N     1 
ATOM   4386 C  CA    . HIS   D 2 55  ? 84.34400  -6.61900  44.49200  1.000 10.59741 ? 54  HIS   D CA    1 
ATOM   4387 C  C     . HIS   D 2 55  ? 84.76900  -8.06200  44.28000  1.000 11.53747 ? 54  HIS   D C     1 
ATOM   4388 O  O     . HIS   D 2 55  ? 85.59100  -8.56800  45.05900  1.000 11.02311 ? 54  HIS   D O     1 
ATOM   4389 C  CB    . HIS   D 2 55  ? 83.29600  -6.55900  45.60600  1.000 12.09314 ? 54  HIS   D CB    1 
ATOM   4390 C  CG    . HIS   D 2 55  ? 82.05400  -7.33400  45.29500  1.000 11.97078 ? 54  HIS   D CG    1 
ATOM   4391 N  ND1   . HIS   D 2 55  ? 81.07000  -6.84900  44.46400  1.000 10.92934 ? 54  HIS   D ND1   1 
ATOM   4392 C  CD2   . HIS   D 2 55  ? 81.64100  -8.56200  45.69200  1.000 12.85642 ? 54  HIS   D CD2   1 
ATOM   4393 C  CE1   . HIS   D 2 55  ? 80.09300  -7.73700  44.37100  1.000 11.26175 ? 54  HIS   D CE1   1 
ATOM   4394 N  NE2   . HIS   D 2 55  ? 80.41200  -8.78300  45.11400  1.000 8.68237  ? 54  HIS   D NE2   1 
ATOM   4395 N  N     . ARG   D 2 56  ? 84.25300  -8.72700  43.24100  1.000 8.67777  ? 55  ARG   D N     1 
ATOM   4396 C  CA    . ARG   D 2 56  ? 84.55100  -10.13600 42.99600  1.000 8.67061  ? 55  ARG   D CA    1 
ATOM   4397 C  C     . ARG   D 2 56  ? 84.91000  -10.32300 41.52500  1.000 12.12178 ? 55  ARG   D C     1 
ATOM   4398 O  O     . ARG   D 2 56  ? 84.04000  -10.26200 40.65200  1.000 9.68045  ? 55  ARG   D O     1 
ATOM   4399 C  CB    . ARG   D 2 56  ? 83.37500  -11.03500 43.39000  1.000 9.90990  ? 55  ARG   D CB    1 
ATOM   4400 C  CG    . ARG   D 2 56  ? 83.68200  -12.53100 43.20900  1.000 12.30409 ? 55  ARG   D CG    1 
ATOM   4401 C  CD    . ARG   D 2 56  ? 82.43400  -13.38800 43.43300  1.000 10.77587 ? 55  ARG   D CD    1 
ATOM   4402 N  NE    . ARG   D 2 56  ? 82.03000  -13.42500 44.83200  1.000 9.27331  ? 55  ARG   D NE    1 
ATOM   4403 C  CZ    . ARG   D 2 56  ? 80.99800  -14.12700 45.27800  1.000 14.39755 ? 55  ARG   D CZ    1 
ATOM   4404 N  NH1   . ARG   D 2 56  ? 80.24300  -14.84700 44.45100  1.000 9.17301  ? 55  ARG   D NH1   1 
ATOM   4405 N  NH2   . ARG   D 2 56  ? 80.72600  -14.12200 46.58200  1.000 12.30196 ? 55  ARG   D NH2   1 
ATOM   4406 N  N     . ILE   D 2 57  ? 86.19000  -10.55700 41.25100  1.000 10.27218 ? 56  ILE   D N     1 
ATOM   4407 C  CA    . ILE   D 2 57  ? 86.68900  -10.72700 39.89300  1.000 9.44444  ? 56  ILE   D CA    1 
ATOM   4408 C  C     . ILE   D 2 57  ? 87.41400  -12.06600 39.87700  1.000 14.06742 ? 56  ILE   D C     1 
ATOM   4409 O  O     . ILE   D 2 57  ? 88.39300  -12.24800 40.60500  1.000 12.85905 ? 56  ILE   D O     1 
ATOM   4410 C  CB    . ILE   D 2 57  ? 87.62200  -9.58700  39.46600  1.000 11.85294 ? 56  ILE   D CB    1 
ATOM   4411 C  CG1   . ILE   D 2 57  ? 86.87500  -8.25200  39.50400  1.000 8.96614  ? 56  ILE   D CG1   1 
ATOM   4412 C  CG2   . ILE   D 2 57  ? 88.15700  -9.81900  38.06900  1.000 10.92302 ? 56  ILE   D CG2   1 
ATOM   4413 C  CD1   . ILE   D 2 57  ? 87.75700  -7.08400  39.16400  1.000 12.99036 ? 56  ILE   D CD1   1 
ATOM   4414 N  N     . ILE   D 2 58  ? 86.91500  -13.01400 39.08800  1.000 12.92858 ? 57  ILE   D N     1 
ATOM   4415 C  CA    . ILE   D 2 58  ? 87.55900  -14.32100 39.00200  1.000 13.23943 ? 57  ILE   D CA    1 
ATOM   4416 C  C     . ILE   D 2 58  ? 87.99500  -14.55900 37.56500  1.000 12.41862 ? 57  ILE   D C     1 
ATOM   4417 O  O     . ILE   D 2 58  ? 87.14100  -14.72600 36.67800  1.000 11.35428 ? 57  ILE   D O     1 
ATOM   4418 C  CB    . ILE   D 2 58  ? 86.63500  -15.44200 39.50100  1.000 11.33498 ? 57  ILE   D CB    1 
ATOM   4419 C  CG1   . ILE   D 2 58  ? 86.17300  -15.12700 40.92000  1.000 11.45114 ? 57  ILE   D CG1   1 
ATOM   4420 C  CG2   . ILE   D 2 58  ? 87.37400  -16.79300 39.47300  1.000 12.56849 ? 57  ILE   D CG2   1 
ATOM   4421 C  CD1   . ILE   D 2 58  ? 85.37500  -16.25600 41.59700  1.000 13.30575 ? 57  ILE   D CD1   1 
ATOM   4422 N  N     . PRO   D 2 59  ? 89.30300  -14.56700 37.30100  1.000 12.70639 ? 58  PRO   D N     1 
ATOM   4423 C  CA    . PRO   D 2 59  ? 89.78900  -14.73300 35.92500  1.000 17.92759 ? 58  PRO   D CA    1 
ATOM   4424 C  C     . PRO   D 2 59  ? 89.27000  -16.02000 35.30800  1.000 17.33764 ? 58  PRO   D C     1 
ATOM   4425 O  O     . PRO   D 2 59  ? 89.18700  -17.05700 35.96600  1.000 14.20839 ? 58  PRO   D O     1 
ATOM   4426 C  CB    . PRO   D 2 59  ? 91.31900  -14.76000 36.08500  1.000 22.36974 ? 58  PRO   D CB    1 
ATOM   4427 C  CG    . PRO   D 2 59  ? 91.57800  -13.99700 37.36500  1.000 16.31891 ? 58  PRO   D CG    1 
ATOM   4428 C  CD    . PRO   D 2 59  ? 90.40400  -14.37300 38.26000  1.000 16.73513 ? 58  PRO   D CD    1 
ATOM   4429 N  N     . GLY   D 2 60  ? 88.88400  -15.92900 34.04000  1.000 15.45794 ? 59  GLY   D N     1 
ATOM   4430 C  CA    . GLY   D 2 60  ? 88.27700  -17.04000 33.34700  1.000 15.87753 ? 59  GLY   D CA    1 
ATOM   4431 C  C     . GLY   D 2 60  ? 86.77700  -17.16700 33.51300  1.000 15.09173 ? 59  GLY   D C     1 
ATOM   4432 O  O     . GLY   D 2 60  ? 86.18200  -18.05900 32.89000  1.000 15.75220 ? 59  GLY   D O     1 
ATOM   4433 N  N     . PHE   D 2 61  ? 86.14200  -16.30200 34.31100  1.000 12.49577 ? 60  PHE   D N     1 
ATOM   4434 C  CA    . PHE   D 2 61  ? 84.71500  -16.43600 34.57400  1.000 12.71203 ? 60  PHE   D CA    1 
ATOM   4435 C  C     . PHE   D 2 61  ? 83.94900  -15.11900 34.46100  1.000 10.80914 ? 60  PHE   D C     1 
ATOM   4436 O  O     . PHE   D 2 61  ? 83.17500  -14.95900 33.51300  1.000 13.36736 ? 60  PHE   D O     1 
ATOM   4437 C  CB    . PHE   D 2 61  ? 84.50200  -17.06500 35.94700  1.000 12.17547 ? 60  PHE   D CB    1 
ATOM   4438 C  CG    . PHE   D 2 61  ? 84.94800  -18.50300 36.02500  1.000 12.36966 ? 60  PHE   D CG    1 
ATOM   4439 C  CD1   . PHE   D 2 61  ? 84.10600  -19.52500 35.61400  1.000 12.69372 ? 60  PHE   D CD1   1 
ATOM   4440 C  CD2   . PHE   D 2 61  ? 86.19500  -18.82300 36.52500  1.000 13.27567 ? 60  PHE   D CD2   1 
ATOM   4441 C  CE1   . PHE   D 2 61  ? 84.50500  -20.84900 35.69100  1.000 14.15414 ? 60  PHE   D CE1   1 
ATOM   4442 C  CE2   . PHE   D 2 61  ? 86.60900  -20.13700 36.62500  1.000 15.23064 ? 60  PHE   D CE2   1 
ATOM   4443 C  CZ    . PHE   D 2 61  ? 85.76300  -21.16300 36.19800  1.000 14.85827 ? 60  PHE   D CZ    1 
ATOM   4444 N  N     . MET   D 2 62  ? 84.14000  -14.17700 35.39300  1.000 9.81799  ? 61  MET   D N     1 
ATOM   4445 C  CA    . MET   D 2 62  ? 83.32800  -12.95700 35.40600  1.000 10.97570 ? 61  MET   D CA    1 
ATOM   4446 C  C     . MET   D 2 62  ? 83.97500  -11.86700 36.24600  1.000 12.46040 ? 61  MET   D C     1 
ATOM   4447 O  O     . MET   D 2 62  ? 84.87800  -12.12500 37.04400  1.000 12.23449 ? 61  MET   D O     1 
ATOM   4448 C  CB    . MET   D 2 62  ? 81.91000  -13.22300 35.93500  1.000 8.05374  ? 61  MET   D CB    1 
ATOM   4449 C  CG    . MET   D 2 62  ? 81.76300  -13.16300 37.47100  1.000 7.88364  ? 61  MET   D CG    1 
ATOM   4450 S  SD    . MET   D 2 62  ? 82.60800  -14.53300 38.30100  1.000 13.84330 ? 61  MET   D SD    1 
ATOM   4451 C  CE    . MET   D 2 62  ? 82.84900  -13.76100 39.90900  1.000 9.24792  ? 61  MET   D CE    1 
ATOM   4452 N  N     . CYS   D 2 63  ? 83.50500  -10.63200 36.02100  1.000 9.23752  ? 62  CYS   D N     1 
ATOM   4453 C  CA    . CYS   D 2 63  ? 83.73500  -9.48300  36.89000  1.000 8.25804  ? 62  CYS   D CA    1 
ATOM   4454 C  C     . CYS   D 2 63  ? 82.39800  -9.07500  37.50400  1.000 9.63291  ? 62  CYS   D C     1 
ATOM   4455 O  O     . CYS   D 2 63  ? 81.46200  -8.74000  36.77600  1.000 8.30294  ? 62  CYS   D O     1 
ATOM   4456 C  CB    . CYS   D 2 63  ? 84.31100  -8.30900  36.10900  1.000 11.25565 ? 62  CYS   D CB    1 
ATOM   4457 S  SG    . CYS   D 2 63  ? 85.83400  -8.64000  35.24600  1.000 11.20540 ? 62  CYS   D SG    1 
ATOM   4458 N  N     . GLN   D 2 64  ? 82.31200  -9.06800  38.83200  1.000 10.27083 ? 63  GLN   D N     1 
ATOM   4459 C  CA    . GLN   D 2 64  ? 81.04800  -8.82700  39.52100  1.000 6.52636  ? 63  GLN   D CA    1 
ATOM   4460 C  C     . GLN   D 2 64  ? 81.11700  -7.56000  40.36000  1.000 8.01401  ? 63  GLN   D C     1 
ATOM   4461 O  O     . GLN   D 2 64  ? 82.12500  -7.29100  41.01500  1.000 8.91670  ? 63  GLN   D O     1 
ATOM   4462 C  CB    . GLN   D 2 64  ? 80.66200  -10.01700 40.40200  1.000 8.44799  ? 63  GLN   D CB    1 
ATOM   4463 C  CG    . GLN   D 2 64  ? 79.31900  -9.87200  41.11200  1.000 7.20252  ? 63  GLN   D CG    1 
ATOM   4464 C  CD    . GLN   D 2 64  ? 78.99000  -11.11300 41.90500  1.000 8.07813  ? 63  GLN   D CD    1 
ATOM   4465 O  OE1   . GLN   D 2 64  ? 79.43700  -12.21100 41.56200  1.000 7.59175  ? 63  GLN   D OE1   1 
ATOM   4466 N  NE2   . GLN   D 2 64  ? 78.24300  -10.94600 42.99000  1.000 12.23102 ? 63  GLN   D NE2   1 
ATOM   4467 N  N     . GLY   D 2 65  ? 80.03300  -6.77800  40.32500  1.000 6.39199  ? 64  GLY   D N     1 
ATOM   4468 C  CA    . GLY   D 2 65  ? 79.98200  -5.56100  41.10600  1.000 8.18326  ? 64  GLY   D CA    1 
ATOM   4469 C  C     . GLY   D 2 65  ? 78.54800  -5.17000  41.37900  1.000 7.04227  ? 64  GLY   D C     1 
ATOM   4470 O  O     . GLY   D 2 65  ? 77.64000  -5.99100  41.20200  1.000 9.27554  ? 64  GLY   D O     1 
ATOM   4471 N  N     . GLY   D 2 66  ? 78.34200  -3.93600  41.84400  1.000 8.73182  ? 65  GLY   D N     1 
ATOM   4472 C  CA    . GLY   D 2 66  ? 77.01900  -3.36900  42.00000  1.000 8.55366  ? 65  GLY   D CA    1 
ATOM   4473 C  C     . GLY   D 2 66  ? 76.56000  -3.15300  43.42500  1.000 10.13108 ? 65  GLY   D C     1 
ATOM   4474 O  O     . GLY   D 2 66  ? 75.42900  -2.68800  43.62300  1.000 12.43542 ? 65  GLY   D O     1 
ATOM   4475 N  N     . ASP   D 2 67  ? 77.36300  -3.48200  44.42900  1.000 6.97501  ? 66  ASP   D N     1 
ATOM   4476 C  CA    . ASP   D 2 67  ? 76.94100  -3.27000  45.81600  1.000 8.83703  ? 66  ASP   D CA    1 
ATOM   4477 C  C     . ASP   D 2 67  ? 77.25300  -1.83200  46.21800  1.000 8.03372  ? 66  ASP   D C     1 
ATOM   4478 O  O     . ASP   D 2 67  ? 78.37900  -1.52500  46.60500  1.000 9.56053  ? 66  ASP   D O     1 
ATOM   4479 C  CB    . ASP   D 2 67  ? 77.62700  -4.26500  46.74400  1.000 9.20158  ? 66  ASP   D CB    1 
ATOM   4480 C  CG    . ASP   D 2 67  ? 77.21500  -4.09600  48.19300  1.000 8.60531  ? 66  ASP   D CG    1 
ATOM   4481 O  OD1   . ASP   D 2 67  ? 76.36500  -3.23400  48.51100  1.000 9.38441  ? 66  ASP   D OD1   1 
ATOM   4482 O  OD2   . ASP   D 2 67  ? 77.72600  -4.85000  49.03300  1.000 9.32792  ? 66  ASP   D OD2   1 
ATOM   4483 N  N     . PHE   D 2 68  ? 76.24300  -0.95000  46.16900  1.000 9.32499  ? 67  PHE   D N     1 
ATOM   4484 C  CA    . PHE   D 2 68  ? 76.40700  0.44000   46.58900  1.000 12.25671 ? 67  PHE   D CA    1 
ATOM   4485 C  C     . PHE   D 2 68  ? 75.72400  0.74400   47.92300  1.000 15.36466 ? 67  PHE   D C     1 
ATOM   4486 O  O     . PHE   D 2 68  ? 75.72500  1.90200   48.36300  1.000 10.47088 ? 67  PHE   D O     1 
ATOM   4487 C  CB    . PHE   D 2 68  ? 75.91600  1.40100   45.48900  1.000 12.56218 ? 67  PHE   D CB    1 
ATOM   4488 C  CG    . PHE   D 2 68  ? 74.48300  1.19400   45.07700  1.000 12.84200 ? 67  PHE   D CG    1 
ATOM   4489 C  CD1   . PHE   D 2 68  ? 73.44600  1.75700   45.80700  1.000 12.41917 ? 67  PHE   D CD1   1 
ATOM   4490 C  CD2   . PHE   D 2 68  ? 74.17200  0.45500   43.94800  1.000 8.93248  ? 67  PHE   D CD2   1 
ATOM   4491 C  CE1   . PHE   D 2 68  ? 72.12000  1.56300   45.42900  1.000 12.84088 ? 67  PHE   D CE1   1 
ATOM   4492 C  CE2   . PHE   D 2 68  ? 72.84400  0.25900   43.56600  1.000 11.64502 ? 67  PHE   D CE2   1 
ATOM   4493 C  CZ    . PHE   D 2 68  ? 71.82500  0.80900   44.30600  1.000 9.79504  ? 67  PHE   D CZ    1 
ATOM   4494 N  N     . THR   D 2 69  ? 75.17200  -0.26500  48.60300  1.000 12.84094 ? 68  THR   D N     1 
ATOM   4495 C  CA    . THR   D 2 69  ? 74.50900  -0.02800  49.88300  1.000 13.50760 ? 68  THR   D CA    1 
ATOM   4496 C  C     . THR   D 2 69  ? 75.30400  -0.52900  51.07500  1.000 14.09232 ? 68  THR   D C     1 
ATOM   4497 O  O     . THR   D 2 69  ? 75.32700  0.13900   52.11200  1.000 17.25828 ? 68  THR   D O     1 
ATOM   4498 C  CB    . THR   D 2 69  ? 73.11200  -0.67000  49.91000  1.000 13.81158 ? 68  THR   D CB    1 
ATOM   4499 O  OG1   . THR   D 2 69  ? 73.23800  -2.08700  49.85200  1.000 12.04738 ? 68  THR   D OG1   1 
ATOM   4500 C  CG2   . THR   D 2 69  ? 72.28200  -0.20800  48.74100  1.000 17.23474 ? 68  THR   D CG2   1 
ATOM   4501 N  N     . ARG   D 2 70  ? 75.94500  -1.69500  50.95600  1.000 10.81984 ? 69  ARG   D N     1 
ATOM   4502 C  CA    . ARG   D 2 70  ? 76.80800  -2.22900  52.00400  1.000 13.12471 ? 69  ARG   D CA    1 
ATOM   4503 C  C     . ARG   D 2 70  ? 78.29000  -2.11600  51.67700  1.000 11.21667 ? 69  ARG   D C     1 
ATOM   4504 O  O     . ARG   D 2 70  ? 79.11400  -2.14200  52.59600  1.000 11.94302 ? 69  ARG   D O     1 
ATOM   4505 C  CB    . ARG   D 2 70  ? 76.49300  -3.70700  52.27600  1.000 11.32056 ? 69  ARG   D CB    1 
ATOM   4506 C  CG    . ARG   D 2 70  ? 75.05400  -4.01400  52.71100  1.000 16.74008 ? 69  ARG   D CG    1 
ATOM   4507 C  CD    . ARG   D 2 70  ? 74.69400  -3.32900  54.02600  1.000 22.40572 ? 69  ARG   D CD    1 
ATOM   4508 N  NE    . ARG   D 2 70  ? 75.82100  -3.26800  54.95000  1.000 35.30565 ? 69  ARG   D NE    1 
ATOM   4509 C  CZ    . ARG   D 2 70  ? 76.22300  -4.26700  55.72800  1.000 36.59380 ? 69  ARG   D CZ    1 
ATOM   4510 N  NH1   . ARG   D 2 70  ? 75.61700  -5.44500  55.71000  1.000 29.32970 ? 69  ARG   D NH1   1 
ATOM   4511 N  NH2   . ARG   D 2 70  ? 77.26300  -4.07900  56.53900  1.000 33.03681 ? 69  ARG   D NH2   1 
ATOM   4512 N  N     . HIS   D 2 71  ? 78.64500  -2.05100  50.39800  1.000 10.37903 ? 70  HIS   D N     1 
ATOM   4513 C  CA    . HIS   D 2 71  ? 80.02500  -1.83000  49.98200  1.000 10.31533 ? 70  HIS   D CA    1 
ATOM   4514 C  C     . HIS   D 2 71  ? 80.92000  -3.00100  50.37200  1.000 14.78164 ? 70  HIS   D C     1 
ATOM   4515 O  O     . HIS   D 2 71  ? 82.10800  -2.82100  50.64300  1.000 12.58544 ? 70  HIS   D O     1 
ATOM   4516 C  CB    . HIS   D 2 71  ? 80.56900  -0.51900  50.55800  1.000 11.11395 ? 70  HIS   D CB    1 
ATOM   4517 C  CG    . HIS   D 2 71  ? 79.65100  0.65400   50.36300  1.000 12.91686 ? 70  HIS   D CG    1 
ATOM   4518 N  ND1   . HIS   D 2 71  ? 79.60200  1.37300   49.19000  1.000 11.20831 ? 70  HIS   D ND1   1 
ATOM   4519 C  CD2   . HIS   D 2 71  ? 78.75800  1.23700   51.19700  1.000 13.25394 ? 70  HIS   D CD2   1 
ATOM   4520 C  CE1   . HIS   D 2 71  ? 78.71600  2.34700   49.30600  1.000 12.45519 ? 70  HIS   D CE1   1 
ATOM   4521 N  NE2   . HIS   D 2 71  ? 78.19100  2.28700   50.51700  1.000 12.77489 ? 70  HIS   D NE2   1 
ATOM   4522 N  N     . ASN   D 2 72  ? 80.35200  -4.21600  50.41000  1.000 10.22593 ? 71  ASN   D N     1 
ATOM   4523 C  CA    . ASN   D 2 72  ? 81.14900  -5.37100  50.80900  1.000 11.40639 ? 71  ASN   D CA    1 
ATOM   4524 C  C     . ASN   D 2 72  ? 80.74000  -6.66000  50.09900  1.000 14.32590 ? 71  ASN   D C     1 
ATOM   4525 O  O     . ASN   D 2 72  ? 81.09900  -7.74400  50.57600  1.000 13.20476 ? 71  ASN   D O     1 
ATOM   4526 C  CB    . ASN   D 2 72  ? 81.07000  -5.56800  52.34000  1.000 13.22695 ? 71  ASN   D CB    1 
ATOM   4527 C  CG    . ASN   D 2 72  ? 79.68300  -5.96000  52.81300  1.000 13.64807 ? 71  ASN   D CG    1 
ATOM   4528 O  OD1   . ASN   D 2 72  ? 78.76900  -6.16800  52.01400  1.000 12.69096 ? 71  ASN   D OD1   1 
ATOM   4529 N  ND2   . ASN   D 2 72  ? 79.51800  -6.05900  54.11700  1.000 16.69933 ? 71  ASN   D ND2   1 
ATOM   4530 N  N     . GLY   D 2 73  ? 79.98400  -6.58600  49.00200  1.000 13.24249 ? 72  GLY   D N     1 
ATOM   4531 C  CA    . GLY   D 2 73  ? 79.59900  -7.77600  48.26800  1.000 11.74249 ? 72  GLY   D CA    1 
ATOM   4532 C  C     . GLY   D 2 73  ? 78.29800  -8.41200  48.69800  1.000 8.89813  ? 72  GLY   D C     1 
ATOM   4533 O  O     . GLY   D 2 73  ? 77.85300  -9.36900  48.05100  1.000 12.72700 ? 72  GLY   D O     1 
ATOM   4534 N  N     . THR   D 2 74  ? 77.66000  -7.91200  49.75700  1.000 9.42063  ? 73  THR   D N     1 
ATOM   4535 C  CA    . THR   D 2 74  ? 76.43200  -8.51500  50.25300  1.000 9.73186  ? 73  THR   D CA    1 
ATOM   4536 C  C     . THR   D 2 74  ? 75.18800  -7.67000  50.01700  1.000 14.12877 ? 73  THR   D C     1 
ATOM   4537 O  O     . THR   D 2 74  ? 74.07800  -8.18400  50.20600  1.000 10.07963 ? 73  THR   D O     1 
ATOM   4538 C  CB    . THR   D 2 74  ? 76.53500  -8.81300  51.75900  1.000 12.25371 ? 73  THR   D CB    1 
ATOM   4539 O  OG1   . THR   D 2 74  ? 76.40900  -7.59600  52.51600  1.000 11.52300 ? 73  THR   D OG1   1 
ATOM   4540 C  CG2   . THR   D 2 74  ? 77.85800  -9.49000  52.09700  1.000 15.61911 ? 73  THR   D CG2   1 
ATOM   4541 N  N     . GLY   D 2 75  ? 75.33200  -6.40300  49.61100  1.000 9.27448  ? 74  GLY   D N     1 
ATOM   4542 C  CA    . GLY   D 2 75  ? 74.22600  -5.47700  49.55800  1.000 10.52099 ? 74  GLY   D CA    1 
ATOM   4543 C  C     . GLY   D 2 75  ? 73.75700  -5.17300  48.15300  1.000 11.96639 ? 74  GLY   D C     1 
ATOM   4544 O  O     . GLY   D 2 75  ? 74.03400  -5.90500  47.19100  1.000 11.38817 ? 74  GLY   D O     1 
ATOM   4545 N  N     . GLY   D 2 76  ? 73.04500  -4.05300  48.02300  1.000 16.27802 ? 75  GLY   D N     1 
ATOM   4546 C  CA    . GLY   D 2 76  ? 72.45300  -3.67700  46.75900  1.000 11.21821 ? 75  GLY   D CA    1 
ATOM   4547 C  C     . GLY   D 2 76  ? 70.94400  -3.52600  46.85100  1.000 13.30680 ? 75  GLY   D C     1 
ATOM   4548 O  O     . GLY   D 2 76  ? 70.31100  -4.03700  47.77900  1.000 11.99384 ? 75  GLY   D O     1 
ATOM   4549 N  N     . LYS   D 2 77  ? 70.36400  -2.80600  45.89700  1.000 8.50896  ? 76  LYS   D N     1 
ATOM   4550 C  CA    . LYS   D 2 77  ? 68.91700  -2.65500  45.83900  1.000 10.85953 ? 76  LYS   D CA    1 
ATOM   4551 C  C     . LYS   D 2 77  ? 68.55300  -2.20000  44.44100  1.000 11.18785 ? 76  LYS   D C     1 
ATOM   4552 O  O     . LYS   D 2 77  ? 69.37900  -1.63300  43.72000  1.000 11.73060 ? 76  LYS   D O     1 
ATOM   4553 C  CB    . LYS   D 2 77  ? 68.38600  -1.67100  46.88800  1.000 14.72310 ? 76  LYS   D CB    1 
ATOM   4554 C  CG    . LYS   D 2 77  ? 68.79200  -0.22300  46.66800  1.000 15.79051 ? 76  LYS   D CG    1 
ATOM   4555 C  CD    . LYS   D 2 77  ? 68.18800  0.69200   47.73800  1.000 18.98915 ? 76  LYS   D CD    1 
ATOM   4556 C  CE    . LYS   D 2 77  ? 68.59900  2.13800   47.53200  1.000 18.25076 ? 76  LYS   D CE    1 
ATOM   4557 N  NZ    . LYS   D 2 77  ? 67.83300  3.09600   48.38200  1.000 24.87984 ? 76  LYS   D NZ    1 
ATOM   4558 N  N     . SER   D 2 78  ? 67.30700  -2.46800  44.05900  1.000 11.08521 ? 77  SER   D N     1 
ATOM   4559 C  CA    . SER   D 2 78  ? 66.83200  -2.10500  42.73900  1.000 9.59029  ? 77  SER   D CA    1 
ATOM   4560 C  C     . SER   D 2 78  ? 66.00900  -0.82700  42.81100  1.000 11.11337 ? 77  SER   D C     1 
ATOM   4561 O  O     . SER   D 2 78  ? 65.67100  -0.33200  43.88900  1.000 10.19635 ? 77  SER   D O     1 
ATOM   4562 C  CB    . SER   D 2 78  ? 65.99900  -3.23200  42.14200  1.000 12.99180 ? 77  SER   D CB    1 
ATOM   4563 O  OG    . SER   D 2 78  ? 64.67100  -3.13400  42.61600  1.000 9.33210  ? 77  SER   D OG    1 
ATOM   4564 N  N     . ILE   D 2 79  ? 65.66300  -0.30800  41.63100  1.000 11.06451 ? 78  ILE   D N     1 
ATOM   4565 C  CA    . ILE   D 2 79  ? 64.75200  0.82600   41.57300  1.000 10.30239 ? 78  ILE   D CA    1 
ATOM   4566 C  C     . ILE   D 2 79  ? 63.32700  0.44700   41.93000  1.000 11.90821 ? 78  ILE   D C     1 
ATOM   4567 O  O     . ILE   D 2 79  ? 62.48800  1.33800   42.09400  1.000 14.53003 ? 78  ILE   D O     1 
ATOM   4568 C  CB    . ILE   D 2 79  ? 64.77400  1.49800   40.18700  1.000 11.43464 ? 78  ILE   D CB    1 
ATOM   4569 C  CG1   . ILE   D 2 79  ? 64.17600  0.56300   39.13000  1.000 10.25320 ? 78  ILE   D CG1   1 
ATOM   4570 C  CG2   . ILE   D 2 79  ? 66.20000  1.91200   39.82300  1.000 10.42055 ? 78  ILE   D CG2   1 
ATOM   4571 C  CD1   . ILE   D 2 79  ? 63.78800  1.27100   37.86100  1.000 13.98741 ? 78  ILE   D CD1   1 
ATOM   4572 N  N     . TYR   D 2 80  ? 63.03600  -0.83900  42.10100  1.000 10.78732 ? 79  TYR   D N     1 
ATOM   4573 C  CA    . TYR   D 2 80  ? 61.69700  -1.30000  42.45400  1.000 17.65194 ? 79  TYR   D CA    1 
ATOM   4574 C  C     . TYR   D 2 80  ? 61.53200  -1.63200  43.93100  1.000 13.05243 ? 79  TYR   D C     1 
ATOM   4575 O  O     . TYR   D 2 80  ? 60.42800  -1.97700  44.35100  1.000 16.64114 ? 79  TYR   D O     1 
ATOM   4576 C  CB    . TYR   D 2 80  ? 61.33700  -2.53400  41.63000  1.000 14.77650 ? 79  TYR   D CB    1 
ATOM   4577 C  CG    . TYR   D 2 80  ? 61.61100  -2.34800  40.16800  1.000 17.12304 ? 79  TYR   D CG    1 
ATOM   4578 C  CD1   . TYR   D 2 80  ? 60.86200  -1.45000  39.42000  1.000 17.92476 ? 79  TYR   D CD1   1 
ATOM   4579 C  CD2   . TYR   D 2 80  ? 62.61600  -3.06600  39.53600  1.000 11.26955 ? 79  TYR   D CD2   1 
ATOM   4580 C  CE1   . TYR   D 2 80  ? 61.10200  -1.27200  38.08100  1.000 18.89389 ? 79  TYR   D CE1   1 
ATOM   4581 C  CE2   . TYR   D 2 80  ? 62.87100  -2.89100  38.18700  1.000 14.13685 ? 79  TYR   D CE2   1 
ATOM   4582 C  CZ    . TYR   D 2 80  ? 62.10900  -1.98200  37.47100  1.000 17.96190 ? 79  TYR   D CZ    1 
ATOM   4583 O  OH    . TYR   D 2 80  ? 62.34300  -1.78300  36.13500  1.000 18.05033 ? 79  TYR   D OH    1 
ATOM   4584 N  N     . GLY   D 2 81  ? 62.58800  -1.54400  44.72100  1.000 12.03456 ? 80  GLY   D N     1 
ATOM   4585 C  CA    . GLY   D 2 81  ? 62.60600  -2.08900  46.05900  1.000 13.78088 ? 80  GLY   D CA    1 
ATOM   4586 C  C     . GLY   D 2 81  ? 63.85100  -2.92900  46.23300  1.000 13.90465 ? 80  GLY   D C     1 
ATOM   4587 O  O     . GLY   D 2 81  ? 64.70500  -2.99500  45.34600  1.000 13.78661 ? 80  GLY   D O     1 
ATOM   4588 N  N     . GLU   D 2 82  ? 63.96300  -3.59500  47.39200  1.000 13.73670 ? 81  GLU   D N     1 
ATOM   4589 C  CA    . GLU   D 2 82  ? 65.17800  -4.34700  47.69200  1.000 14.51274 ? 81  GLU   D CA    1 
ATOM   4590 C  C     . GLU   D 2 82  ? 65.40700  -5.47600  46.68900  1.000 16.13913 ? 81  GLU   D C     1 
ATOM   4591 O  O     . GLU   D 2 82  ? 66.54100  -5.70300  46.25900  1.000 13.90710 ? 81  GLU   D O     1 
ATOM   4592 C  CB    . GLU   D 2 82  ? 65.13300  -4.88100  49.13100  1.000 18.75280 ? 81  GLU   D CB    1 
ATOM   4593 C  CG    . GLU   D 2 82  ? 65.19600  -3.76700  50.17700  1.000 15.93568 ? 81  GLU   D CG    1 
ATOM   4594 C  CD    . GLU   D 2 82  ? 65.20000  -4.26800  51.61500  1.000 23.53859 ? 81  GLU   D CD    1 
ATOM   4595 O  OE1   . GLU   D 2 82  ? 65.23900  -5.50200  51.83000  1.000 17.05385 ? 81  GLU   D OE1   1 
ATOM   4596 O  OE2   . GLU   D 2 82  ? 65.17200  -3.41400  52.53500  1.000 19.67981 ? 81  GLU   D OE2   1 
ATOM   4597 N  N     . LYS   D 2 83  ? 64.35300  -6.19200  46.30300  1.000 15.24656 ? 82  LYS   D N     1 
ATOM   4598 C  CA    . LYS   D 2 83  ? 64.46500  -7.32500  45.39000  1.000 15.50738 ? 82  LYS   D CA    1 
ATOM   4599 C  C     . LYS   D 2 83  ? 63.40800  -7.20800  44.29600  1.000 15.05859 ? 82  LYS   D C     1 
ATOM   4600 O  O     . LYS   D 2 83  ? 62.39200  -6.53100  44.46100  1.000 12.76452 ? 82  LYS   D O     1 
ATOM   4601 C  CB    . LYS   D 2 83  ? 64.27300  -8.66900  46.11600  1.000 17.97403 ? 82  LYS   D CB    1 
ATOM   4602 C  CG    . LYS   D 2 83  ? 64.72000  -8.69800  47.57600  1.000 31.47493 ? 82  LYS   D CG    1 
ATOM   4603 C  CD    . LYS   D 2 83  ? 66.11600  -9.29300  47.69100  1.000 32.53551 ? 82  LYS   D CD    1 
ATOM   4604 C  CE    . LYS   D 2 83  ? 66.92100  -8.67900  48.83300  1.000 30.18130 ? 82  LYS   D CE    1 
ATOM   4605 N  NZ    . LYS   D 2 83  ? 68.27800  -9.27300  48.87500  1.000 25.57544 ? 82  LYS   D NZ    1 
ATOM   4606 N  N     . PHE   D 2 84  ? 63.65100  -7.86600  43.16200  1.000 14.51860 ? 83  PHE   D N     1 
ATOM   4607 C  CA    . PHE   D 2 84  ? 62.59200  -8.04100  42.17900  1.000 19.12544 ? 83  PHE   D CA    1 
ATOM   4608 C  C     . PHE   D 2 84  ? 62.75300  -9.38200  41.47500  1.000 15.27117 ? 83  PHE   D C     1 
ATOM   4609 O  O     . PHE   D 2 84  ? 63.83600  -9.97600  41.43300  1.000 9.97263  ? 83  PHE   D O     1 
ATOM   4610 C  CB    . PHE   D 2 84  ? 62.51000  -6.88000  41.16000  1.000 19.09810 ? 83  PHE   D CB    1 
ATOM   4611 C  CG    . PHE   D 2 84  ? 63.72100  -6.71700  40.27500  1.000 14.57432 ? 83  PHE   D CG    1 
ATOM   4612 C  CD1   . PHE   D 2 84  ? 64.88200  -6.11800  40.75600  1.000 9.61220  ? 83  PHE   D CD1   1 
ATOM   4613 C  CD2   . PHE   D 2 84  ? 63.66400  -7.07200  38.93700  1.000 8.66041  ? 83  PHE   D CD2   1 
ATOM   4614 C  CE1   . PHE   D 2 84  ? 65.96700  -5.93000  39.93200  1.000 13.83136 ? 83  PHE   D CE1   1 
ATOM   4615 C  CE2   . PHE   D 2 84  ? 64.74100  -6.88900  38.12200  1.000 13.54272 ? 83  PHE   D CE2   1 
ATOM   4616 C  CZ    . PHE   D 2 84  ? 65.90900  -6.32200  38.61900  1.000 9.70306  ? 83  PHE   D CZ    1 
ATOM   4617 N  N     . GLU   D 2 85  ? 61.64000  -9.86000  40.92800  1.000 14.38571 ? 84  GLU   D N     1 
ATOM   4618 C  CA    . GLU   D 2 85  ? 61.58100  -11.23200 40.47000  1.000 10.09725 ? 84  GLU   D CA    1 
ATOM   4619 C  C     . GLU   D 2 85  ? 62.35400  -11.41900 39.16900  1.000 12.35456 ? 84  GLU   D C     1 
ATOM   4620 O  O     . GLU   D 2 85  ? 62.62700  -10.47200 38.42100  1.000 14.38909 ? 84  GLU   D O     1 
ATOM   4621 C  CB    . GLU   D 2 85  ? 60.12200  -11.67000 40.30800  1.000 13.01477 ? 84  GLU   D CB    1 
ATOM   4622 C  CG    . GLU   D 2 85  ? 59.38600  -10.90600 39.27200  1.000 17.46004 ? 84  GLU   D CG    1 
ATOM   4623 C  CD    . GLU   D 2 85  ? 57.90400  -11.29400 39.22100  1.000 27.14766 ? 84  GLU   D CD    1 
ATOM   4624 O  OE1   . GLU   D 2 85  ? 57.39100  -11.86100 40.21500  1.000 26.60726 ? 84  GLU   D OE1   1 
ATOM   4625 O  OE2   . GLU   D 2 85  ? 57.26600  -11.03100 38.18200  1.000 31.94574 ? 84  GLU   D OE2   1 
ATOM   4626 N  N     . ASP   D 2 86  ? 62.73200  -12.66800 38.91900  1.000 12.44277 ? 85  ASP   D N     1 
ATOM   4627 C  CA    . ASP   D 2 86  ? 63.36300  -13.02200 37.65700  1.000 10.02742 ? 85  ASP   D CA    1 
ATOM   4628 C  C     . ASP   D 2 86  ? 62.38600  -12.77000 36.50800  1.000 11.89389 ? 85  ASP   D C     1 
ATOM   4629 O  O     . ASP   D 2 86  ? 61.34100  -13.42200 36.41100  1.000 10.49111 ? 85  ASP   D O     1 
ATOM   4630 C  CB    . ASP   D 2 86  ? 63.80900  -14.48500 37.71500  1.000 9.23767  ? 85  ASP   D CB    1 
ATOM   4631 C  CG    . ASP   D 2 86  ? 64.86100  -14.72000 38.80400  1.000 12.29676 ? 85  ASP   D CG    1 
ATOM   4632 O  OD1   . ASP   D 2 86  ? 65.81100  -13.90800 38.87900  1.000 10.38544 ? 85  ASP   D OD1   1 
ATOM   4633 O  OD2   . ASP   D 2 86  ? 64.73800  -15.68700 39.59700  1.000 13.36829 ? 85  ASP   D OD2   1 
ATOM   4634 N  N     . GLU   D 2 87  ? 62.72900  -11.81500 35.64200  1.000 9.44800  ? 86  GLU   D N     1 
ATOM   4635 C  CA    . GLU   D 2 87  ? 61.79000  -11.35100 34.61900  1.000 10.06176 ? 86  GLU   D CA    1 
ATOM   4636 C  C     . GLU   D 2 87  ? 61.52500  -12.42900 33.57100  1.000 11.11671 ? 86  GLU   D C     1 
ATOM   4637 O  O     . GLU   D 2 87  ? 60.37000  -12.75400 33.27700  1.000 13.03154 ? 86  GLU   D O     1 
ATOM   4638 C  CB    . GLU   D 2 87  ? 62.33400  -10.07800 33.96600  1.000 12.21483 ? 86  GLU   D CB    1 
ATOM   4639 C  CG    . GLU   D 2 87  ? 61.43800  -9.49100  32.87900  1.000 11.47220 ? 86  GLU   D CG    1 
ATOM   4640 C  CD    . GLU   D 2 87  ? 61.83000  -8.06000  32.52100  1.000 10.02976 ? 86  GLU   D CD    1 
ATOM   4641 O  OE1   . GLU   D 2 87  ? 62.98300  -7.67800  32.82300  1.000 8.69938  ? 86  GLU   D OE1   1 
ATOM   4642 O  OE2   . GLU   D 2 87  ? 60.98600  -7.32400  31.95700  1.000 9.70526  ? 86  GLU   D OE2   1 
ATOM   4643 N  N     . ASN   D 2 88  ? 62.58100  -12.98100 32.98700  1.000 13.20094 ? 87  ASN   D N     1 
ATOM   4644 C  CA    . ASN   D 2 88  ? 62.47900  -14.10500 32.06000  1.000 12.17297 ? 87  ASN   D CA    1 
ATOM   4645 C  C     . ASN   D 2 88  ? 63.86700  -14.70800 31.91800  1.000 11.08684 ? 87  ASN   D C     1 
ATOM   4646 O  O     . ASN   D 2 88  ? 64.84800  -14.15300 32.40600  1.000 11.66248 ? 87  ASN   D O     1 
ATOM   4647 C  CB    . ASN   D 2 88  ? 61.93100  -13.70200 30.69100  1.000 10.33056 ? 87  ASN   D CB    1 
ATOM   4648 C  CG    . ASN   D 2 88  ? 62.84300  -12.76300 29.92900  1.000 14.60515 ? 87  ASN   D CG    1 
ATOM   4649 O  OD1   . ASN   D 2 88  ? 63.98400  -13.09700 29.58100  1.000 12.70171 ? 87  ASN   D OD1   1 
ATOM   4650 N  ND2   . ASN   D 2 88  ? 62.32600  -11.58000 29.63300  1.000 11.92318 ? 87  ASN   D ND2   1 
ATOM   4651 N  N     . PHE   D 2 89  ? 63.94200  -15.83300 31.21800  1.000 12.83107 ? 88  PHE   D N     1 
ATOM   4652 C  CA    . PHE   D 2 89  ? 65.21600  -16.47300 30.89900  1.000 13.32362 ? 88  PHE   D CA    1 
ATOM   4653 C  C     . PHE   D 2 89  ? 65.37900  -16.65500 29.39200  1.000 11.26432 ? 88  PHE   D C     1 
ATOM   4654 O  O     . PHE   D 2 89  ? 65.92300  -17.65600 28.92100  1.000 15.73289 ? 88  PHE   D O     1 
ATOM   4655 C  CB    . PHE   D 2 89  ? 65.34400  -17.80600 31.63000  1.000 14.80058 ? 88  PHE   D CB    1 
ATOM   4656 C  CG    . PHE   D 2 89  ? 65.29700  -17.66700 33.12700  1.000 12.46217 ? 88  PHE   D CG    1 
ATOM   4657 C  CD1   . PHE   D 2 89  ? 66.30100  -16.97900 33.80100  1.000 9.34898  ? 88  PHE   D CD1   1 
ATOM   4658 C  CD2   . PHE   D 2 89  ? 64.24700  -18.20300 33.85900  1.000 13.28556 ? 88  PHE   D CD2   1 
ATOM   4659 C  CE1   . PHE   D 2 89  ? 66.25500  -16.83800 35.18200  1.000 12.09229 ? 88  PHE   D CE1   1 
ATOM   4660 C  CE2   . PHE   D 2 89  ? 64.20400  -18.07500 35.23900  1.000 12.43954 ? 88  PHE   D CE2   1 
ATOM   4661 C  CZ    . PHE   D 2 89  ? 65.20000  -17.39200 35.90200  1.000 10.15061 ? 88  PHE   D CZ    1 
ATOM   4662 N  N     . ILE   D 2 90  ? 64.93500  -15.66500 28.61400  1.000 10.36950 ? 89  ILE   D N     1 
ATOM   4663 C  CA    . ILE   D 2 90  ? 65.02500  -15.76800 27.15500  1.000 12.71390 ? 89  ILE   D CA    1 
ATOM   4664 C  C     . ILE   D 2 90  ? 66.47700  -15.79700 26.69000  1.000 12.64724 ? 89  ILE   D C     1 
ATOM   4665 O  O     . ILE   D 2 90  ? 66.83100  -16.55000 25.77400  1.000 12.13074 ? 89  ILE   D O     1 
ATOM   4666 C  CB    . ILE   D 2 90  ? 64.26600  -14.60800 26.48200  1.000 13.91577 ? 89  ILE   D CB    1 
ATOM   4667 C  CG1   . ILE   D 2 90  ? 62.76600  -14.68900 26.76100  1.000 11.54877 ? 89  ILE   D CG1   1 
ATOM   4668 C  CG2   . ILE   D 2 90  ? 64.51300  -14.62000 24.98000  1.000 13.81778 ? 89  ILE   D CG2   1 
ATOM   4669 C  CD1   . ILE   D 2 90  ? 62.01800  -13.41900 26.32500  1.000 15.81690 ? 89  ILE   D CD1   1 
ATOM   4670 N  N     . LEU   D 2 91  ? 67.32000  -14.93900 27.26500  1.000 9.89109  ? 90  LEU   D N     1 
ATOM   4671 C  CA    . LEU   D 2 91  ? 68.72100  -14.81600 26.87000  1.000 9.73667  ? 90  LEU   D CA    1 
ATOM   4672 C  C     . LEU   D 2 91  ? 69.61600  -15.72500 27.70900  1.000 13.59811 ? 90  LEU   D C     1 
ATOM   4673 O  O     . LEU   D 2 91  ? 69.34600  -15.99000 28.88200  1.000 12.63417 ? 90  LEU   D O     1 
ATOM   4674 C  CB    . LEU   D 2 91  ? 69.18400  -13.36600 27.00700  1.000 9.06783  ? 90  LEU   D CB    1 
ATOM   4675 C  CG    . LEU   D 2 91  ? 68.48300  -12.38300 26.07000  1.000 9.28536  ? 90  LEU   D CG    1 
ATOM   4676 C  CD1   . LEU   D 2 91  ? 68.91500  -10.97800 26.43100  1.000 10.84708 ? 90  LEU   D CD1   1 
ATOM   4677 C  CD2   . LEU   D 2 91  ? 68.81000  -12.70000 24.60100  1.000 13.93557 ? 90  LEU   D CD2   1 
ATOM   4678 N  N     . LYS   D 2 92  ? 70.69800  -16.20400 27.10100  1.000 12.65835 ? 91  LYS   D N     1 
ATOM   4679 C  CA    . LYS   D 2 92  ? 71.56000  -17.16300 27.77700  1.000 12.90868 ? 91  LYS   D CA    1 
ATOM   4680 C  C     . LYS   D 2 92  ? 72.97200  -16.60500 27.90200  1.000 12.04167 ? 91  LYS   D C     1 
ATOM   4681 O  O     . LYS   D 2 92  ? 73.32400  -15.59300 27.29500  1.000 9.64007  ? 91  LYS   D O     1 
ATOM   4682 C  CB    . LYS   D 2 92  ? 71.55600  -18.50700 27.04100  1.000 13.78159 ? 91  LYS   D CB    1 
ATOM   4683 C  CG    . LYS   D 2 92  ? 70.15200  -19.07500 26.85000  1.000 20.01389 ? 91  LYS   D CG    1 
ATOM   4684 C  CD    . LYS   D 2 92  ? 70.15900  -20.48600 26.28100  1.000 25.27039 ? 91  LYS   D CD    1 
ATOM   4685 C  CE    . LYS   D 2 92  ? 68.74000  -21.04400 26.15600  1.000 32.65229 ? 91  LYS   D CE    1 
ATOM   4686 N  NZ    . LYS   D 2 92  ? 67.87800  -20.69400 27.33400  1.000 35.54168 ? 91  LYS   D NZ    1 
ATOM   4687 N  N     . HIS   D 2 93  ? 73.76900  -17.27900 28.73700  1.000 12.11027 ? 92  HIS   D N     1 
ATOM   4688 C  CA    . HIS   D 2 93  ? 75.16600  -16.91100 28.98000  1.000 12.62282 ? 92  HIS   D CA    1 
ATOM   4689 C  C     . HIS   D 2 93  ? 76.00200  -17.57100 27.89200  1.000 13.84717 ? 92  HIS   D C     1 
ATOM   4690 O  O     . HIS   D 2 93  ? 76.52900  -18.67400 28.04900  1.000 17.72365 ? 92  HIS   D O     1 
ATOM   4691 C  CB    . HIS   D 2 93  ? 75.59500  -17.34400 30.37600  1.000 10.68806 ? 92  HIS   D CB    1 
ATOM   4692 C  CG    . HIS   D 2 93  ? 74.70400  -16.82200 31.46200  1.000 10.54738 ? 92  HIS   D CG    1 
ATOM   4693 N  ND1   . HIS   D 2 93  ? 73.46600  -17.36700 31.73500  1.000 10.08822 ? 92  HIS   D ND1   1 
ATOM   4694 C  CD2   . HIS   D 2 93  ? 74.84700  -15.76900 32.30400  1.000 8.98589  ? 92  HIS   D CD2   1 
ATOM   4695 C  CE1   . HIS   D 2 93  ? 72.90100  -16.69500 32.72500  1.000 10.39747 ? 92  HIS   D CE1   1 
ATOM   4696 N  NE2   . HIS   D 2 93  ? 73.71600  -15.71800 33.08300  1.000 11.26018 ? 92  HIS   D NE2   1 
ATOM   4697 N  N     . THR   D 2 94  ? 76.09500  -16.88500 26.75000  1.000 11.20509 ? 93  THR   D N     1 
ATOM   4698 C  CA    . THR   D 2 94  ? 76.66500  -17.47400 25.54700  1.000 12.96113 ? 93  THR   D CA    1 
ATOM   4699 C  C     . THR   D 2 94  ? 78.14200  -17.16600 25.35300  1.000 14.15790 ? 93  THR   D C     1 
ATOM   4700 O  O     . THR   D 2 94  ? 78.75900  -17.77000 24.47200  1.000 18.01445 ? 93  THR   D O     1 
ATOM   4701 C  CB    . THR   D 2 94  ? 75.91300  -16.99500 24.29500  1.000 21.31601 ? 93  THR   D CB    1 
ATOM   4702 O  OG1   . THR   D 2 94  ? 75.84400  -15.56000 24.28900  1.000 16.93962 ? 93  THR   D OG1   1 
ATOM   4703 C  CG2   . THR   D 2 94  ? 74.49600  -17.58200 24.23800  1.000 15.17896 ? 93  THR   D CG2   1 
ATOM   4704 N  N     . GLY   D 2 95  ? 78.71100  -16.22900 26.10300  1.000 13.62884 ? 94  GLY   D N     1 
ATOM   4705 C  CA    . GLY   D 2 95  ? 80.12300  -15.95100 25.99000  1.000 12.00051 ? 94  GLY   D CA    1 
ATOM   4706 C  C     . GLY   D 2 95  ? 80.55000  -14.64200 26.62400  1.000 11.83940 ? 94  GLY   D C     1 
ATOM   4707 O  O     . GLY   D 2 95  ? 79.80600  -13.99800 27.37900  1.000 14.00989 ? 94  GLY   D O     1 
ATOM   4708 N  N     . PRO   D 2 96  ? 81.77400  -14.21900 26.31500  1.000 16.13415 ? 95  PRO   D N     1 
ATOM   4709 C  CA    . PRO   D 2 96  ? 82.31200  -13.00400 26.93100  1.000 13.61841 ? 95  PRO   D CA    1 
ATOM   4710 C  C     . PRO   D 2 96  ? 81.51900  -11.77900 26.51600  1.000 12.87238 ? 95  PRO   D C     1 
ATOM   4711 O  O     . PRO   D 2 96  ? 81.01400  -11.68100 25.39800  1.000 15.19773 ? 95  PRO   D O     1 
ATOM   4712 C  CB    . PRO   D 2 96  ? 83.75000  -12.93600 26.40800  1.000 14.40253 ? 95  PRO   D CB    1 
ATOM   4713 C  CG    . PRO   D 2 96  ? 84.04400  -14.30500 25.86700  1.000 17.90027 ? 95  PRO   D CG    1 
ATOM   4714 C  CD    . PRO   D 2 96  ? 82.73800  -14.85900 25.40400  1.000 14.88844 ? 95  PRO   D CD    1 
ATOM   4715 N  N     . GLY   D 2 97  ? 81.41300  -10.84200 27.44300  1.000 12.32115 ? 96  GLY   D N     1 
ATOM   4716 C  CA    . GLY   D 2 97  ? 80.64800  -9.64200  27.24200  1.000 9.22062  ? 96  GLY   D CA    1 
ATOM   4717 C  C     . GLY   D 2 97  ? 79.23500  -9.69800  27.77700  1.000 9.71960  ? 96  GLY   D C     1 
ATOM   4718 O  O     . GLY   D 2 97  ? 78.62200  -8.64100  27.95100  1.000 9.81665  ? 96  GLY   D O     1 
ATOM   4719 N  N     . ILE   D 2 98  ? 78.70900  -10.89200 28.06500  1.000 8.78220  ? 97  ILE   D N     1 
ATOM   4720 C  CA    . ILE   D 2 98  ? 77.33900  -11.00100 28.55500  1.000 8.31049  ? 97  ILE   D CA    1 
ATOM   4721 C  C     . ILE   D 2 98  ? 77.20600  -10.31400 29.90600  1.000 9.63113  ? 97  ILE   D C     1 
ATOM   4722 O  O     . ILE   D 2 98  ? 78.02800  -10.50600 30.81800  1.000 8.31347  ? 97  ILE   D O     1 
ATOM   4723 C  CB    . ILE   D 2 98  ? 76.90300  -12.47300 28.63600  1.000 8.39539  ? 97  ILE   D CB    1 
ATOM   4724 C  CG1   . ILE   D 2 98  ? 76.71300  -13.04200 27.22400  1.000 10.59452 ? 97  ILE   D CG1   1 
ATOM   4725 C  CG2   . ILE   D 2 98  ? 75.64200  -12.63400 29.53500  1.000 7.81526  ? 97  ILE   D CG2   1 
ATOM   4726 C  CD1   . ILE   D 2 98  ? 75.58800  -12.40600 26.43700  1.000 11.45619 ? 97  ILE   D CD1   1 
ATOM   4727 N  N     . LEU   D 2 99  ? 76.15400  -9.51700  30.03700  1.000 6.75534  ? 98  LEU   D N     1 
ATOM   4728 C  CA    . LEU   D 2 99  ? 75.83400  -8.79200  31.25600  1.000 8.35170  ? 98  LEU   D CA    1 
ATOM   4729 C  C     . LEU   D 2 99  ? 74.61100  -9.44500  31.88800  1.000 8.16994  ? 98  LEU   D C     1 
ATOM   4730 O  O     . LEU   D 2 99  ? 73.54900  -9.51100  31.26500  1.000 9.46565  ? 98  LEU   D O     1 
ATOM   4731 C  CB    . LEU   D 2 99  ? 75.56400  -7.31600  30.95000  1.000 7.42149  ? 98  LEU   D CB    1 
ATOM   4732 C  CG    . LEU   D 2 99  ? 75.16000  -6.45000  32.14500  1.000 9.36332  ? 98  LEU   D CG    1 
ATOM   4733 C  CD1   . LEU   D 2 99  ? 76.34600  -6.34600  33.12000  1.000 9.65964  ? 98  LEU   D CD1   1 
ATOM   4734 C  CD2   . LEU   D 2 99  ? 74.74200  -5.07200  31.68000  1.000 10.72896 ? 98  LEU   D CD2   1 
ATOM   4735 N  N     . SER   D 2 100 ? 74.74800  -9.89900  33.12900  1.000 7.77252  ? 99  SER   D N     1 
ATOM   4736 C  CA    . SER   D 2 100 ? 73.71100  -10.71600 33.74300  1.000 10.37621 ? 99  SER   D CA    1 
ATOM   4737 C  C     . SER   D 2 100 ? 73.54600  -10.31700 35.20800  1.000 7.85019  ? 99  SER   D C     1 
ATOM   4738 O  O     . SER   D 2 100 ? 74.45400  -9.74900  35.81200  1.000 8.49886  ? 99  SER   D O     1 
ATOM   4739 C  CB    . SER   D 2 100 ? 74.07300  -12.19700 33.59800  1.000 9.34565  ? 99  SER   D CB    1 
ATOM   4740 O  OG    . SER   D 2 100 ? 73.12800  -13.03300 34.20800  1.000 9.15944  ? 99  SER   D OG    1 
ATOM   4741 N  N     . MET   D 2 101 ? 72.38000  -10.61800 35.78200  1.000 8.46106  ? 100 MET   D N     1 
ATOM   4742 C  CA    . MET   D 2 101 ? 72.09900  -10.23100 37.16600  1.000 8.39019  ? 100 MET   D CA    1 
ATOM   4743 C  C     . MET   D 2 101 ? 72.66700  -11.24400 38.14400  1.000 9.17425  ? 100 MET   D C     1 
ATOM   4744 O  O     . MET   D 2 101 ? 72.49800  -12.45800 37.97500  1.000 8.26888  ? 100 MET   D O     1 
ATOM   4745 C  CB    . MET   D 2 101 ? 70.59200  -10.11200 37.42900  1.000 9.16721  ? 100 MET   D CB    1 
ATOM   4746 C  CG    . MET   D 2 101 ? 69.91700  -8.90500  36.80200  1.000 5.97144  ? 100 MET   D CG    1 
ATOM   4747 S  SD    . MET   D 2 101 ? 70.67300  -7.33700  37.25200  1.000 8.58115  ? 100 MET   D SD    1 
ATOM   4748 C  CE    . MET   D 2 101 ? 70.19600  -7.15900  38.97600  1.000 7.06338  ? 100 MET   D CE    1 
ATOM   4749 N  N     . ALA   D 2 102 ? 73.28900  -10.73900 39.20400  1.000 7.55887  ? 101 ALA   D N     1 
ATOM   4750 C  CA    . ALA   D 2 102 ? 73.69500  -11.59900 40.30300  1.000 9.65974  ? 101 ALA   D CA    1 
ATOM   4751 C  C     . ALA   D 2 102 ? 72.51600  -11.78800 41.25500  1.000 10.92900 ? 101 ALA   D C     1 
ATOM   4752 O  O     . ALA   D 2 102 ? 71.58300  -10.98300 41.28200  1.000 11.75312 ? 101 ALA   D O     1 
ATOM   4753 C  CB    . ALA   D 2 102 ? 74.89900  -11.00200 41.04100  1.000 8.70869  ? 101 ALA   D CB    1 
ATOM   4754 N  N     . ASN   D 2 103 ? 72.53900  -12.87100 42.03500  1.000 7.16389  ? 102 ASN   D N     1 
ATOM   4755 C  CA    . ASN   D 2 103 ? 71.40000  -13.08400 42.93000  1.000 9.11431  ? 102 ASN   D CA    1 
ATOM   4756 C  C     . ASN   D 2 103 ? 71.76100  -14.06800 44.03000  1.000 8.15539  ? 102 ASN   D C     1 
ATOM   4757 O  O     . ASN   D 2 103 ? 72.84500  -14.65000 44.04500  1.000 11.71503 ? 102 ASN   D O     1 
ATOM   4758 C  CB    . ASN   D 2 103 ? 70.15600  -13.54500 42.16000  1.000 8.48287  ? 102 ASN   D CB    1 
ATOM   4759 C  CG    . ASN   D 2 103 ? 70.32400  -14.90700 41.50900  1.000 10.15472 ? 102 ASN   D CG    1 
ATOM   4760 O  OD1   . ASN   D 2 103 ? 70.79400  -15.86400 42.13400  1.000 10.54138 ? 102 ASN   D OD1   1 
ATOM   4761 N  ND2   . ASN   D 2 103 ? 69.94600  -14.99700 40.24600  1.000 8.63451  ? 102 ASN   D ND2   1 
ATOM   4762 N  N     . ALA   D 2 104 ? 70.83000  -14.24300 44.95300  1.000 8.72403  ? 103 ALA   D N     1 
ATOM   4763 C  CA    . ALA   D 2 104 ? 70.95100  -15.19300 46.05000  1.000 11.80730 ? 103 ALA   D CA    1 
ATOM   4764 C  C     . ALA   D 2 104 ? 69.87400  -16.26900 45.96800  1.000 12.33477 ? 103 ALA   D C     1 
ATOM   4765 O  O     . ALA   D 2 104 ? 69.30700  -16.68300 46.97800  1.000 11.47617 ? 103 ALA   D O     1 
ATOM   4766 C  CB    . ALA   D 2 104 ? 70.89400  -14.47400 47.39400  1.000 12.99545 ? 103 ALA   D CB    1 
ATOM   4767 N  N     . GLY   D 2 105 ? 69.59500  -16.74200 44.75700  1.000 9.96505  ? 104 GLY   D N     1 
ATOM   4768 C  CA    . GLY   D 2 105 ? 68.54000  -17.69900 44.52500  1.000 12.49839 ? 104 GLY   D CA    1 
ATOM   4769 C  C     . GLY   D 2 105 ? 67.40600  -17.07700 43.73800  1.000 10.33483 ? 104 GLY   D C     1 
ATOM   4770 O  O     . GLY   D 2 105 ? 67.49800  -15.93500 43.29800  1.000 9.61564  ? 104 GLY   D O     1 
ATOM   4771 N  N     . PRO   D 2 106 ? 66.31800  -17.81800 43.53500  1.000 11.01294 ? 105 PRO   D N     1 
ATOM   4772 C  CA    . PRO   D 2 106 ? 65.21600  -17.30100 42.71100  1.000 12.85696 ? 105 PRO   D CA    1 
ATOM   4773 C  C     . PRO   D 2 106 ? 64.66500  -15.96700 43.20400  1.000 12.18369 ? 105 PRO   D C     1 
ATOM   4774 O  O     . PRO   D 2 106 ? 64.47600  -15.75500 44.40600  1.000 16.46657 ? 105 PRO   D O     1 
ATOM   4775 C  CB    . PRO   D 2 106 ? 64.15600  -18.40500 42.81300  1.000 13.96213 ? 105 PRO   D CB    1 
ATOM   4776 C  CG    . PRO   D 2 106 ? 64.94300  -19.67200 43.07300  1.000 16.26106 ? 105 PRO   D CG    1 
ATOM   4777 C  CD    . PRO   D 2 106 ? 66.16300  -19.24600 43.86600  1.000 16.31773 ? 105 PRO   D CD    1 
ATOM   4778 N  N     . ASN   D 2 107 ? 64.41500  -15.06300 42.25900  1.000 10.12400 ? 106 ASN   D N     1 
ATOM   4779 C  CA    . ASN   D 2 107 ? 63.64100  -13.84100 42.50700  1.000 10.27640 ? 106 ASN   D CA    1 
ATOM   4780 C  C     . ASN   D 2 107 ? 64.25900  -12.96400 43.58900  1.000 9.99998  ? 106 ASN   D C     1 
ATOM   4781 O  O     . ASN   D 2 107 ? 63.56100  -12.43900 44.46100  1.000 10.58963 ? 106 ASN   D O     1 
ATOM   4782 C  CB    . ASN   D 2 107 ? 62.19300  -14.20100 42.85000  1.000 11.31082 ? 106 ASN   D CB    1 
ATOM   4783 C  CG    . ASN   D 2 107 ? 61.56300  -15.03400 41.77000  1.000 12.47336 ? 106 ASN   D CG    1 
ATOM   4784 O  OD1   . ASN   D 2 107 ? 61.60600  -14.66200 40.60100  1.000 13.48252 ? 106 ASN   D OD1   1 
ATOM   4785 N  ND2   . ASN   D 2 107 ? 61.04600  -16.19800 42.13400  1.000 12.34963 ? 106 ASN   D ND2   1 
ATOM   4786 N  N     . THR   D 2 108 ? 65.58000  -12.79600 43.53700  1.000 9.32581  ? 107 THR   D N     1 
ATOM   4787 C  CA    . THR   D 2 108 ? 66.30800  -11.93300 44.47400  1.000 9.50243  ? 107 THR   D CA    1 
ATOM   4788 C  C     . THR   D 2 108 ? 67.18000  -10.93100 43.73500  1.000 13.06062 ? 107 THR   D C     1 
ATOM   4789 O  O     . THR   D 2 108 ? 68.27000  -10.56400 44.20100  1.000 13.01012 ? 107 THR   D O     1 
ATOM   4790 C  CB    . THR   D 2 108 ? 67.15500  -12.75100 45.45400  1.000 10.45012 ? 107 THR   D CB    1 
ATOM   4791 O  OG1   . THR   D 2 108 ? 68.09900  -13.55800 44.73600  1.000 10.27584 ? 107 THR   D OG1   1 
ATOM   4792 C  CG2   . THR   D 2 108 ? 66.26000  -13.64300 46.30100  1.000 10.50309 ? 107 THR   D CG2   1 
ATOM   4793 N  N     . ASN   D 2 109 ? 66.72700  -10.45900 42.57100  1.000 9.58355  ? 108 ASN   D N     1 
ATOM   4794 C  CA    . ASN   D 2 109 ? 67.50000  -9.44600  41.86000  1.000 9.11326  ? 108 ASN   D CA    1 
ATOM   4795 C  C     . ASN   D 2 109 ? 67.48600  -8.12700  42.61600  1.000 12.38978 ? 108 ASN   D C     1 
ATOM   4796 O  O     . ASN   D 2 109 ? 66.45900  -7.70700  43.15100  1.000 15.13561 ? 108 ASN   D O     1 
ATOM   4797 C  CB    . ASN   D 2 109 ? 66.97100  -9.25000  40.44300  1.000 7.44878  ? 108 ASN   D CB    1 
ATOM   4798 C  CG    . ASN   D 2 109 ? 66.98700  -10.51600 39.66300  1.000 10.10953 ? 108 ASN   D CG    1 
ATOM   4799 O  OD1   . ASN   D 2 109 ? 68.03900  -10.95300 39.19700  1.000 10.34324 ? 108 ASN   D OD1   1 
ATOM   4800 N  ND2   . ASN   D 2 109 ? 65.82100  -11.12900 39.50600  1.000 9.77064  ? 108 ASN   D ND2   1 
ATOM   4801 N  N     . GLY   D 2 110 ? 68.64600  -7.48200  42.66900  1.000 9.06973  ? 109 GLY   D N     1 
ATOM   4802 C  CA    . GLY   D 2 110 ? 68.76900  -6.19500  43.31000  1.000 10.58197 ? 109 GLY   D CA    1 
ATOM   4803 C  C     . GLY   D 2 110 ? 69.50300  -5.22500  42.42100  1.000 9.77905  ? 109 GLY   D C     1 
ATOM   4804 O  O     . GLY   D 2 110 ? 68.92400  -4.67000  41.49100  1.000 9.16545  ? 109 GLY   D O     1 
ATOM   4805 N  N     . SER   D 2 111 ? 70.79200  -5.02100  42.69600  1.000 10.13877 ? 110 SER   D N     1 
ATOM   4806 C  CA    . SER   D 2 111 ? 71.65600  -4.22600  41.83700  1.000 8.81171  ? 110 SER   D CA    1 
ATOM   4807 C  C     . SER   D 2 111 ? 72.94800  -4.92300  41.43900  1.000 6.35016  ? 110 SER   D C     1 
ATOM   4808 O  O     . SER   D 2 111 ? 73.58000  -4.49100  40.46900  1.000 6.62243  ? 110 SER   D O     1 
ATOM   4809 C  CB    . SER   D 2 111 ? 72.02400  -2.90100  42.51200  1.000 8.59843  ? 110 SER   D CB    1 
ATOM   4810 O  OG    . SER   D 2 111 ? 72.62800  -3.12800  43.77200  1.000 8.16305  ? 110 SER   D OG    1 
ATOM   4811 N  N     . GLN   D 2 112 ? 73.36900  -5.97000  42.13200  1.000 6.40165  ? 111 GLN   D N     1 
ATOM   4812 C  CA    . GLN   D 2 112 ? 74.61600  -6.61300  41.73800  1.000 6.88525  ? 111 GLN   D CA    1 
ATOM   4813 C  C     . GLN   D 2 112 ? 74.45600  -7.32800  40.39700  1.000 8.10910  ? 111 GLN   D C     1 
ATOM   4814 O  O     . GLN   D 2 112 ? 73.39400  -7.86600  40.06400  1.000 9.14565  ? 111 GLN   D O     1 
ATOM   4815 C  CB    . GLN   D 2 112 ? 75.08900  -7.58900  42.81400  1.000 8.26826  ? 111 GLN   D CB    1 
ATOM   4816 C  CG    . GLN   D 2 112 ? 75.51300  -6.95100  44.14100  1.000 8.80193  ? 111 GLN   D CG    1 
ATOM   4817 C  CD    . GLN   D 2 112 ? 76.31900  -7.92900  44.99100  1.000 7.76624  ? 111 GLN   D CD    1 
ATOM   4818 O  OE1   . GLN   D 2 112 ? 77.11700  -8.70500  44.46000  1.000 8.66840  ? 111 GLN   D OE1   1 
ATOM   4819 N  NE2   . GLN   D 2 112 ? 76.10300  -7.91500  46.30700  1.000 10.27275 ? 111 GLN   D NE2   1 
ATOM   4820 N  N     . PHE   D 2 113 ? 75.53400  -7.33400  39.62900  1.000 6.28278  ? 112 PHE   D N     1 
ATOM   4821 C  CA    . PHE   D 2 113 ? 75.54300  -7.83700  38.26900  1.000 7.27500  ? 112 PHE   D CA    1 
ATOM   4822 C  C     . PHE   D 2 113 ? 76.89600  -8.47600  38.05000  1.000 8.73126  ? 112 PHE   D C     1 
ATOM   4823 O  O     . PHE   D 2 113 ? 77.81500  -8.31000  38.85900  1.000 10.22643 ? 112 PHE   D O     1 
ATOM   4824 C  CB    . PHE   D 2 113 ? 75.33600  -6.71700  37.24500  1.000 6.39970  ? 112 PHE   D CB    1 
ATOM   4825 C  CG    . PHE   D 2 113 ? 76.40700  -5.66600  37.31900  1.000 6.36602  ? 112 PHE   D CG    1 
ATOM   4826 C  CD1   . PHE   D 2 113 ? 76.28900  -4.61300  38.21100  1.000 6.58294  ? 112 PHE   D CD1   1 
ATOM   4827 C  CD2   . PHE   D 2 113 ? 77.56100  -5.78400  36.56900  1.000 8.15205  ? 112 PHE   D CD2   1 
ATOM   4828 C  CE1   . PHE   D 2 113 ? 77.28200  -3.66000  38.32600  1.000 8.64184  ? 112 PHE   D CE1   1 
ATOM   4829 C  CE2   . PHE   D 2 113 ? 78.56300  -4.83300  36.66800  1.000 9.37526  ? 112 PHE   D CE2   1 
ATOM   4830 C  CZ    . PHE   D 2 113 ? 78.42400  -3.76900  37.55900  1.000 10.11084 ? 112 PHE   D CZ    1 
ATOM   4831 N  N     . PHE   D 2 114 ? 77.03900  -9.16300  36.92500  1.000 7.38206  ? 113 PHE   D N     1 
ATOM   4832 C  CA    . PHE   D 2 114 ? 78.35000  -9.63900  36.52200  1.000 7.64860  ? 113 PHE   D CA    1 
ATOM   4833 C  C     . PHE   D 2 114 ? 78.48300  -9.57400  35.01100  1.000 7.86682  ? 113 PHE   D C     1 
ATOM   4834 O  O     . PHE   D 2 114 ? 77.50600  -9.69800  34.27400  1.000 8.02027  ? 113 PHE   D O     1 
ATOM   4835 C  CB    . PHE   D 2 114 ? 78.63200  -11.06300 37.03000  1.000 8.30624  ? 113 PHE   D CB    1 
ATOM   4836 C  CG    . PHE   D 2 114 ? 77.65700  -12.11200 36.53400  1.000 8.62564  ? 113 PHE   D CG    1 
ATOM   4837 C  CD1   . PHE   D 2 114 ? 76.35900  -12.16800 37.01800  1.000 7.46158  ? 113 PHE   D CD1   1 
ATOM   4838 C  CD2   . PHE   D 2 114 ? 78.06300  -13.07000 35.61500  1.000 6.87354  ? 113 PHE   D CD2   1 
ATOM   4839 C  CE1   . PHE   D 2 114 ? 75.47500  -13.16700 36.58300  1.000 6.47842  ? 113 PHE   D CE1   1 
ATOM   4840 C  CE2   . PHE   D 2 114 ? 77.19400  -14.06300 35.17900  1.000 8.62026  ? 113 PHE   D CE2   1 
ATOM   4841 C  CZ    . PHE   D 2 114 ? 75.89200  -14.10000 35.66600  1.000 8.12296  ? 113 PHE   D CZ    1 
ATOM   4842 N  N     . ILE   D 2 115 ? 79.71100  -9.32800  34.56900  1.000 7.90236  ? 114 ILE   D N     1 
ATOM   4843 C  CA    . ILE   D 2 115 ? 80.08700  -9.33100  33.16300  1.000 8.99834  ? 114 ILE   D CA    1 
ATOM   4844 C  C     . ILE   D 2 115 ? 80.88200  -10.60800 32.90800  1.000 9.70133  ? 114 ILE   D C     1 
ATOM   4845 O  O     . ILE   D 2 115 ? 81.97000  -10.78800 33.47100  1.000 10.70940 ? 114 ILE   D O     1 
ATOM   4846 C  CB    . ILE   D 2 115 ? 80.92800  -8.09100  32.81000  1.000 9.00468  ? 114 ILE   D CB    1 
ATOM   4847 C  CG1   . ILE   D 2 115 ? 80.20700  -6.80300  33.20500  1.000 7.74054  ? 114 ILE   D CG1   1 
ATOM   4848 C  CG2   . ILE   D 2 115 ? 81.27900  -8.08900  31.34500  1.000 9.80761  ? 114 ILE   D CG2   1 
ATOM   4849 C  CD1   . ILE   D 2 115 ? 81.10200  -5.55500  33.23200  1.000 8.53194  ? 114 ILE   D CD1   1 
ATOM   4850 N  N     . CYS   D 2 116 ? 80.36800  -11.47500 32.04000  1.000 8.04430  ? 115 CYS   D N     1 
ATOM   4851 C  CA    . CYS   D 2 116 ? 81.06200  -12.71700 31.72000  1.000 10.28765 ? 115 CYS   D CA    1 
ATOM   4852 C  C     . CYS   D 2 116 ? 82.32000  -12.45400 30.91000  1.000 13.89514 ? 115 CYS   D C     1 
ATOM   4853 O  O     . CYS   D 2 116 ? 82.32200  -11.64100 29.98500  1.000 14.23394 ? 115 CYS   D O     1 
ATOM   4854 C  CB    . CYS   D 2 116 ? 80.16400  -13.64300 30.91200  1.000 11.21802 ? 115 CYS   D CB    1 
ATOM   4855 S  SG    . CYS   D 2 116 ? 78.68600  -14.12100 31.78600  1.000 11.71960 ? 115 CYS   D SG    1 
ATOM   4856 N  N     . THR   D 2 117 ? 83.39100  -13.16900 31.24400  1.000 14.83446 ? 116 THR   D N     1 
ATOM   4857 C  CA    . THR   D 2 117 ? 84.59200  -13.19000 30.42100  1.000 14.56105 ? 116 THR   D CA    1 
ATOM   4858 C  C     . THR   D 2 117 ? 84.74300  -14.52600 29.71300  1.000 20.03141 ? 116 THR   D C     1 
ATOM   4859 O  O     . THR   D 2 117 ? 85.79100  -14.80100 29.12500  1.000 16.02905 ? 116 THR   D O     1 
ATOM   4860 C  CB    . THR   D 2 117 ? 85.83400  -12.90300 31.26700  1.000 17.33906 ? 116 THR   D CB    1 
ATOM   4861 O  OG1   . THR   D 2 117 ? 85.95100  -13.89100 32.29200  1.000 15.20065 ? 116 THR   D OG1   1 
ATOM   4862 C  CG2   . THR   D 2 117 ? 85.74600  -11.52200 31.90800  1.000 14.05904 ? 116 THR   D CG2   1 
ATOM   4863 N  N     . ALA   D 2 118 ? 83.70200  -15.34700 29.74400  1.000 16.62302 ? 117 ALA   D N     1 
ATOM   4864 C  CA    . ALA   D 2 118 ? 83.69000  -16.68300 29.17800  1.000 15.56902 ? 117 ALA   D CA    1 
ATOM   4865 C  C     . ALA   D 2 118 ? 82.23800  -17.12900 29.16100  1.000 13.74372 ? 117 ALA   D C     1 
ATOM   4866 O  O     . ALA   D 2 118 ? 81.39500  -16.55000 29.84900  1.000 15.83442 ? 117 ALA   D O     1 
ATOM   4867 C  CB    . ALA   D 2 118 ? 84.54500  -17.65800 29.99700  1.000 16.52072 ? 117 ALA   D CB    1 
ATOM   4868 N  N     . LYS   D 2 119 ? 81.95500  -18.15200 28.36700  1.000 15.64852 ? 118 LYS   D N     1 
ATOM   4869 C  CA    . LYS   D 2 119 ? 80.64800  -18.79300 28.43200  1.000 16.72364 ? 118 LYS   D CA    1 
ATOM   4870 C  C     . LYS   D 2 119 ? 80.43000  -19.37800 29.82700  1.000 16.91546 ? 118 LYS   D C     1 
ATOM   4871 O  O     . LYS   D 2 119 ? 81.31100  -20.04100 30.37900  1.000 18.99703 ? 118 LYS   D O     1 
ATOM   4872 C  CB    . LYS   D 2 119 ? 80.56300  -19.87900 27.36200  1.000 17.43218 ? 118 LYS   D CB    1 
ATOM   4873 C  CG    . LYS   D 2 119 ? 79.16700  -20.40300 27.06600  1.000 18.08886 ? 118 LYS   D CG    1 
ATOM   4874 C  CD    . LYS   D 2 119 ? 79.28900  -21.66000 26.21200  1.000 21.66924 ? 118 LYS   D CD    1 
ATOM   4875 C  CE    . LYS   D 2 119 ? 77.94200  -22.26200 25.83700  1.000 28.03018 ? 118 LYS   D CE    1 
ATOM   4876 N  NZ    . LYS   D 2 119 ? 78.16200  -23.44600 24.95300  1.000 29.67392 ? 118 LYS   D NZ    1 
ATOM   4877 N  N     . THR   D 2 120 ? 79.26700  -19.10200 30.41900  1.000 14.79695 ? 119 THR   D N     1 
ATOM   4878 C  CA    . THR   D 2 120 ? 78.91500  -19.62100 31.74700  1.000 15.03561 ? 119 THR   D CA    1 
ATOM   4879 C  C     . THR   D 2 120 ? 77.51300  -20.23100 31.68700  1.000 14.15181 ? 119 THR   D C     1 
ATOM   4880 O  O     . THR   D 2 120 ? 76.59600  -19.80500 32.38700  1.000 13.42542 ? 119 THR   D O     1 
ATOM   4881 C  CB    . THR   D 2 120 ? 78.94400  -18.55500 32.84800  1.000 13.13186 ? 119 THR   D CB    1 
ATOM   4882 O  OG1   . THR   D 2 120 ? 77.95300  -17.55200 32.58900  1.000 11.56757 ? 119 THR   D OG1   1 
ATOM   4883 C  CG2   . THR   D 2 120 ? 80.33400  -17.90500 32.97800  1.000 11.88722 ? 119 THR   D CG2   1 
ATOM   4884 N  N     . GLU   D 2 121 ? 77.35600  -21.24600 30.84500  1.000 12.84230 ? 120 GLU   D N     1 
ATOM   4885 C  CA    . GLU   D 2 121 ? 76.02500  -21.75600 30.52600  1.000 15.67720 ? 120 GLU   D CA    1 
ATOM   4886 C  C     . GLU   D 2 121 ? 75.36100  -22.48700 31.69100  1.000 15.04668 ? 120 GLU   D C     1 
ATOM   4887 O  O     . GLU   D 2 121 ? 74.14200  -22.67300 31.67200  1.000 16.10302 ? 120 GLU   D O     1 
ATOM   4888 C  CB    . GLU   D 2 121 ? 76.10700  -22.67800 29.31300  1.000 15.49873 ? 120 GLU   D CB    1 
ATOM   4889 C  CG    . GLU   D 2 121 ? 76.68100  -24.05600 29.60700  1.000 21.83556 ? 120 GLU   D CG    1 
ATOM   4890 C  CD    . GLU   D 2 121 ? 78.20400  -24.09300 29.77000  1.000 29.13857 ? 120 GLU   D CD    1 
ATOM   4891 O  OE1   . GLU   D 2 121 ? 78.89000  -23.06600 29.55400  1.000 23.78103 ? 120 GLU   D OE1   1 
ATOM   4892 O  OE2   . GLU   D 2 121 ? 78.71800  -25.17800 30.11800  1.000 31.36112 ? 120 GLU   D OE2   1 
ATOM   4893 N  N     . TRP   D 2 122 ? 76.12100  -22.92000 32.69800  1.000 19.53696 ? 121 TRP   D N     1 
ATOM   4894 C  CA    . TRP   D 2 122 ? 75.48700  -23.49000 33.88300  1.000 16.31395 ? 121 TRP   D CA    1 
ATOM   4895 C  C     . TRP   D 2 122 ? 74.64600  -22.46300 34.63200  1.000 13.99160 ? 121 TRP   D C     1 
ATOM   4896 O  O     . TRP   D 2 122 ? 73.86300  -22.84400 35.50600  1.000 13.86944 ? 121 TRP   D O     1 
ATOM   4897 C  CB    . TRP   D 2 122 ? 76.54200  -24.10000 34.81400  1.000 15.53512 ? 121 TRP   D CB    1 
ATOM   4898 C  CG    . TRP   D 2 122 ? 77.50000  -23.08500 35.32800  1.000 18.41096 ? 121 TRP   D CG    1 
ATOM   4899 C  CD1   . TRP   D 2 122 ? 77.38500  -22.35300 36.47500  1.000 13.91939 ? 121 TRP   D CD1   1 
ATOM   4900 C  CD2   . TRP   D 2 122 ? 78.71700  -22.67000 34.70400  1.000 15.85244 ? 121 TRP   D CD2   1 
ATOM   4901 N  NE1   . TRP   D 2 122 ? 78.45600  -21.51200 36.60500  1.000 13.70951 ? 121 TRP   D NE1   1 
ATOM   4902 C  CE2   . TRP   D 2 122 ? 79.29600  -21.69200 35.53600  1.000 16.54415 ? 121 TRP   D CE2   1 
ATOM   4903 C  CE3   . TRP   D 2 122 ? 79.38400  -23.04400 33.53100  1.000 17.02136 ? 121 TRP   D CE3   1 
ATOM   4904 C  CZ2   . TRP   D 2 122 ? 80.50300  -21.05900 35.22100  1.000 17.16027 ? 121 TRP   D CZ2   1 
ATOM   4905 C  CZ3   . TRP   D 2 122 ? 80.58000  -22.42100 33.22000  1.000 18.00269 ? 121 TRP   D CZ3   1 
ATOM   4906 C  CH2   . TRP   D 2 122 ? 81.12800  -21.44000 34.06200  1.000 19.70630 ? 121 TRP   D CH2   1 
ATOM   4907 N  N     . LEU   D 2 123 ? 74.77000  -21.17700 34.30400  1.000 11.12491 ? 122 LEU   D N     1 
ATOM   4908 C  CA    . LEU   D 2 123 ? 73.92700  -20.15400 34.90500  1.000 10.73930 ? 122 LEU   D CA    1 
ATOM   4909 C  C     . LEU   D 2 123 ? 72.64400  -19.90900 34.12300  1.000 12.27019 ? 122 LEU   D C     1 
ATOM   4910 O  O     . LEU   D 2 123 ? 71.78200  -19.15700 34.59700  1.000 11.65525 ? 122 LEU   D O     1 
ATOM   4911 C  CB    . LEU   D 2 123 ? 74.70900  -18.84600 35.03500  1.000 10.57277 ? 122 LEU   D CB    1 
ATOM   4912 C  CG    . LEU   D 2 123 ? 76.02200  -18.98500 35.80300  1.000 9.54457  ? 122 LEU   D CG    1 
ATOM   4913 C  CD1   . LEU   D 2 123 ? 76.69500  -17.64500 35.86100  1.000 8.80272  ? 122 LEU   D CD1   1 
ATOM   4914 C  CD2   . LEU   D 2 123 ? 75.75600  -19.50100 37.19700  1.000 10.84833 ? 122 LEU   D CD2   1 
ATOM   4915 N  N     . ASP   D 2 124 ? 72.50200  -20.50700 32.94000  1.000 12.65423 ? 123 ASP   D N     1 
ATOM   4916 C  CA    . ASP   D 2 124 ? 71.26700  -20.36500 32.17900  1.000 13.95915 ? 123 ASP   D CA    1 
ATOM   4917 C  C     . ASP   D 2 124 ? 70.07300  -20.80500 33.01900  1.000 15.25605 ? 123 ASP   D C     1 
ATOM   4918 O  O     . ASP   D 2 124 ? 70.11900  -21.82600 33.71000  1.000 12.66523 ? 123 ASP   D O     1 
ATOM   4919 C  CB    . ASP   D 2 124 ? 71.32900  -21.19700 30.89200  1.000 13.56596 ? 123 ASP   D CB    1 
ATOM   4920 C  CG    . ASP   D 2 124 ? 72.32800  -20.64400 29.88500  1.000 16.60329 ? 123 ASP   D CG    1 
ATOM   4921 O  OD1   . ASP   D 2 124 ? 72.88200  -19.55000 30.13800  1.000 11.59363 ? 123 ASP   D OD1   1 
ATOM   4922 O  OD2   . ASP   D 2 124 ? 72.55500  -21.30900 28.84600  1.000 17.74504 ? 123 ASP   D OD2   1 
ATOM   4923 N  N     . GLY   D 2 125 ? 68.99100  -20.03400 32.95100  1.000 14.54658 ? 124 GLY   D N     1 
ATOM   4924 C  CA    . GLY   D 2 125 ? 67.79400  -20.37000 33.68900  1.000 11.72490 ? 124 GLY   D CA    1 
ATOM   4925 C  C     . GLY   D 2 125 ? 67.82800  -20.01200 35.15800  1.000 13.19402 ? 124 GLY   D C     1 
ATOM   4926 O  O     . GLY   D 2 125 ? 66.81800  -20.20500 35.84600  1.000 12.40595 ? 124 GLY   D O     1 
ATOM   4927 N  N     . LYS   D 2 126 ? 68.95200  -19.50900 35.67000  1.000 11.17942 ? 125 LYS   D N     1 
ATOM   4928 C  CA    . LYS   D 2 126 ? 69.07600  -19.12300 37.07000  1.000 9.73872  ? 125 LYS   D CA    1 
ATOM   4929 C  C     . LYS   D 2 126 ? 69.42200  -17.65300 37.26500  1.000 10.86625 ? 125 LYS   D C     1 
ATOM   4930 O  O     . LYS   D 2 126 ? 69.13400  -17.09300 38.33200  1.000 10.19973 ? 125 LYS   D O     1 
ATOM   4931 C  CB    . LYS   D 2 126 ? 70.15200  -19.97400 37.76800  1.000 14.68050 ? 125 LYS   D CB    1 
ATOM   4932 C  CG    . LYS   D 2 126 ? 69.89100  -21.46400 37.73500  1.000 18.31912 ? 125 LYS   D CG    1 
ATOM   4933 C  CD    . LYS   D 2 126 ? 68.64800  -21.81800 38.56000  1.000 29.35917 ? 125 LYS   D CD    1 
ATOM   4934 C  CE    . LYS   D 2 126 ? 68.60700  -23.29800 38.88400  1.000 22.44096 ? 125 LYS   D CE    1 
ATOM   4935 N  NZ    . LYS   D 2 126 ? 69.93100  -23.75400 39.39000  1.000 27.91637 ? 125 LYS   D NZ    1 
ATOM   4936 N  N     . HIS   D 2 127 ? 70.04600  -17.02900 36.27400  1.000 8.36584  ? 126 HIS   D N     1 
ATOM   4937 C  CA    . HIS   D 2 127 ? 70.44900  -15.62800 36.33100  1.000 9.40836  ? 126 HIS   D CA    1 
ATOM   4938 C  C     . HIS   D 2 127 ? 69.88400  -14.94200 35.10100  1.000 8.60075  ? 126 HIS   D C     1 
ATOM   4939 O  O     . HIS   D 2 127 ? 70.00000  -15.48100 33.99300  1.000 12.76363 ? 126 HIS   D O     1 
ATOM   4940 C  CB    . HIS   D 2 127 ? 71.97800  -15.50200 36.38600  1.000 8.33272  ? 126 HIS   D CB    1 
ATOM   4941 C  CG    . HIS   D 2 127 ? 72.56400  -15.95000 37.68600  1.000 9.76663  ? 126 HIS   D CG    1 
ATOM   4942 N  ND1   . HIS   D 2 127 ? 72.88800  -15.07200 38.69600  1.000 9.01110  ? 126 HIS   D ND1   1 
ATOM   4943 C  CD2   . HIS   D 2 127 ? 72.86000  -17.18700 38.15200  1.000 9.25983  ? 126 HIS   D CD2   1 
ATOM   4944 C  CE1   . HIS   D 2 127 ? 73.35100  -15.74500 39.73300  1.000 9.88295  ? 126 HIS   D CE1   1 
ATOM   4945 N  NE2   . HIS   D 2 127 ? 73.34400  -17.03200 39.43200  1.000 8.26940  ? 126 HIS   D NE2   1 
ATOM   4946 N  N     . VAL   D 2 128 ? 69.25800  -13.77700 35.28200  1.000 8.14940  ? 127 VAL   D N     1 
ATOM   4947 C  CA    . VAL   D 2 128 ? 68.63400  -13.09300 34.15100  1.000 8.90583  ? 127 VAL   D CA    1 
ATOM   4948 C  C     . VAL   D 2 128 ? 69.69200  -12.31700 33.36700  1.000 10.42067 ? 127 VAL   D C     1 
ATOM   4949 O  O     . VAL   D 2 128 ? 70.28700  -11.35500 33.86400  1.000 8.36047  ? 127 VAL   D O     1 
ATOM   4950 C  CB    . VAL   D 2 128 ? 67.48500  -12.17900 34.59300  1.000 11.10992 ? 127 VAL   D CB    1 
ATOM   4951 C  CG1   . VAL   D 2 128 ? 67.01300  -11.31200 33.41300  1.000 9.26723  ? 127 VAL   D CG1   1 
ATOM   4952 C  CG2   . VAL   D 2 128 ? 66.33800  -13.01800 35.10700  1.000 8.59896  ? 127 VAL   D CG2   1 
ATOM   4953 N  N     . VAL   D 2 129 ? 69.90700  -12.73200 32.12200  1.000 9.13887  ? 128 VAL   D N     1 
ATOM   4954 C  CA    . VAL   D 2 129 ? 70.75800  -12.02000 31.17800  1.000 8.15650  ? 128 VAL   D CA    1 
ATOM   4955 C  C     . VAL   D 2 129 ? 69.96600  -10.85200 30.60900  1.000 8.57352  ? 128 VAL   D C     1 
ATOM   4956 O  O     . VAL   D 2 129 ? 68.80000  -11.00900 30.24000  1.000 8.69541  ? 128 VAL   D O     1 
ATOM   4957 C  CB    . VAL   D 2 129 ? 71.22400  -12.97000 30.05900  1.000 8.72850  ? 128 VAL   D CB    1 
ATOM   4958 C  CG1   . VAL   D 2 129 ? 71.96400  -12.20700 28.95500  1.000 7.59803  ? 128 VAL   D CG1   1 
ATOM   4959 C  CG2   . VAL   D 2 129 ? 72.09300  -14.09400 30.64000  1.000 9.29956  ? 128 VAL   D CG2   1 
ATOM   4960 N  N     . PHE   D 2 130 ? 70.59600  -9.68500  30.52000  1.000 6.62613  ? 129 PHE   D N     1 
ATOM   4961 C  CA    . PHE   D 2 130 ? 69.87100  -8.50600  30.05400  1.000 10.77965 ? 129 PHE   D CA    1 
ATOM   4962 C  C     . PHE   D 2 130 ? 70.73700  -7.52800  29.26900  1.000 11.65245 ? 129 PHE   D C     1 
ATOM   4963 O  O     . PHE   D 2 130 ? 70.25100  -6.44100  28.94000  1.000 10.47677 ? 129 PHE   D O     1 
ATOM   4964 C  CB    . PHE   D 2 130 ? 69.23700  -7.78400  31.25400  1.000 9.46824  ? 129 PHE   D CB    1 
ATOM   4965 C  CG    . PHE   D 2 130 ? 70.24900  -7.19400  32.19900  1.000 8.43419  ? 129 PHE   D CG    1 
ATOM   4966 C  CD1   . PHE   D 2 130 ? 70.78400  -7.96100  33.21600  1.000 8.40019  ? 129 PHE   D CD1   1 
ATOM   4967 C  CD2   . PHE   D 2 130 ? 70.66800  -5.88300  32.07000  1.000 10.14303 ? 129 PHE   D CD2   1 
ATOM   4968 C  CE1   . PHE   D 2 130 ? 71.72600  -7.43400  34.09300  1.000 8.66199  ? 129 PHE   D CE1   1 
ATOM   4969 C  CE2   . PHE   D 2 130 ? 71.61900  -5.34800  32.93900  1.000 11.93029 ? 129 PHE   D CE2   1 
ATOM   4970 C  CZ    . PHE   D 2 130 ? 72.14700  -6.12800  33.95800  1.000 8.09838  ? 129 PHE   D CZ    1 
ATOM   4971 N  N     . GLY   D 2 131 ? 71.98900  -7.85200  28.96400  1.000 9.52719  ? 130 GLY   D N     1 
ATOM   4972 C  CA    . GLY   D 2 131 ? 72.81500  -6.90400  28.23800  1.000 8.99898  ? 130 GLY   D CA    1 
ATOM   4973 C  C     . GLY   D 2 131 ? 74.08800  -7.56300  27.75700  1.000 12.60854 ? 130 GLY   D C     1 
ATOM   4974 O  O     . GLY   D 2 131 ? 74.31500  -8.76000  27.96400  1.000 10.23015 ? 130 GLY   D O     1 
ATOM   4975 N  N     . LYS   D 2 132 ? 74.91500  -6.75900  27.08400  1.000 10.92998 ? 131 LYS   D N     1 
ATOM   4976 C  CA    . LYS   D 2 132 ? 76.19500  -7.22900  26.58100  1.000 9.25170  ? 131 LYS   D CA    1 
ATOM   4977 C  C     . LYS   D 2 132 ? 77.11700  -6.02900  26.41900  1.000 10.66610 ? 131 LYS   D C     1 
ATOM   4978 O  O     . LYS   D 2 132 ? 76.67100  -4.91800  26.09900  1.000 8.77750  ? 131 LYS   D O     1 
ATOM   4979 C  CB    . LYS   D 2 132 ? 76.05500  -7.97400  25.24000  1.000 9.34383  ? 131 LYS   D CB    1 
ATOM   4980 C  CG    . LYS   D 2 132 ? 75.90600  -7.02800  24.03600  1.000 19.91428 ? 131 LYS   D CG    1 
ATOM   4981 C  CD    . LYS   D 2 132 ? 75.50200  -7.70700  22.72300  1.000 23.44772 ? 131 LYS   D CD    1 
ATOM   4982 C  CE    . LYS   D 2 132 ? 75.13800  -6.64300  21.66700  1.000 20.21306 ? 131 LYS   D CE    1 
ATOM   4983 N  NZ    . LYS   D 2 132 ? 74.64700  -7.21800  20.38300  1.000 29.35506 ? 131 LYS   D NZ    1 
ATOM   4984 N  N     . VAL   D 2 133 ? 78.40600  -6.26900  26.65200  1.000 8.26001  ? 132 VAL   D N     1 
ATOM   4985 C  CA    . VAL   D 2 133 ? 79.40700  -5.25000  26.40900  1.000 8.63612  ? 132 VAL   D CA    1 
ATOM   4986 C  C     . VAL   D 2 133 ? 79.38500  -4.88500  24.93300  1.000 13.26902 ? 132 VAL   D C     1 
ATOM   4987 O  O     . VAL   D 2 133 ? 79.34500  -5.75800  24.05000  1.000 12.24698 ? 132 VAL   D O     1 
ATOM   4988 C  CB    . VAL   D 2 133 ? 80.79800  -5.74100  26.84200  1.000 8.85397  ? 132 VAL   D CB    1 
ATOM   4989 C  CG1   . VAL   D 2 133 ? 81.85400  -4.79100  26.35300  1.000 12.37113 ? 132 VAL   D CG1   1 
ATOM   4990 C  CG2   . VAL   D 2 133 ? 80.88600  -5.84800  28.35600  1.000 9.68926  ? 132 VAL   D CG2   1 
ATOM   4991 N  N     . LYS   D 2 134 ? 79.40300  -3.58600  24.66500  1.000 11.48831 ? 133 LYS   D N     1 
ATOM   4992 C  CA    . LYS   D 2 134 ? 79.42400  -3.04200  23.31600  1.000 12.80034 ? 133 LYS   D CA    1 
ATOM   4993 C  C     . LYS   D 2 134 ? 80.85000  -2.60300  23.00400  1.000 13.34485 ? 133 LYS   D C     1 
ATOM   4994 O  O     . LYS   D 2 134 ? 81.55600  -3.25200  22.23000  1.000 18.94828 ? 133 LYS   D O     1 
ATOM   4995 C  CB    . LYS   D 2 134 ? 78.43800  -1.87200  23.19700  1.000 13.34699 ? 133 LYS   D CB    1 
ATOM   4996 C  CG    . LYS   D 2 134 ? 78.41100  -1.21900  21.84000  1.000 19.67893 ? 133 LYS   D CG    1 
ATOM   4997 C  CD    . LYS   D 2 134 ? 77.38100  -0.08000  21.76300  1.000 20.58445 ? 133 LYS   D CD    1 
ATOM   4998 C  CE    . LYS   D 2 134 ? 77.45500  0.61900   20.40700  1.000 23.32871 ? 133 LYS   D CE    1 
ATOM   4999 N  NZ    . LYS   D 2 134 ? 76.58400  1.82600   20.31500  1.000 20.92702 ? 133 LYS   D NZ    1 
ATOM   5000 N  N     . GLU   D 2 135 ? 81.29600  -1.51600  23.61200  1.000 14.29227 ? 134 GLU   D N     1 
ATOM   5001 C  CA    . GLU   D 2 135 ? 82.69500  -1.13000  23.50800  1.000 15.54392 ? 134 GLU   D CA    1 
ATOM   5002 C  C     . GLU   D 2 135 ? 83.40400  -1.37600  24.83500  1.000 11.51996 ? 134 GLU   D C     1 
ATOM   5003 O  O     . GLU   D 2 135 ? 82.78200  -1.37400  25.90200  1.000 10.49459 ? 134 GLU   D O     1 
ATOM   5004 C  CB    . GLU   D 2 135 ? 82.84600  0.33700   23.09500  1.000 18.91012 ? 134 GLU   D CB    1 
ATOM   5005 C  CG    . GLU   D 2 135 ? 82.45200  0.60900   21.66000  1.000 26.92597 ? 134 GLU   D CG    1 
ATOM   5006 C  CD    . GLU   D 2 135 ? 82.42800  2.09100   21.33600  1.000 43.50805 ? 134 GLU   D CD    1 
ATOM   5007 O  OE1   . GLU   D 2 135 ? 82.64300  2.90600   22.26200  1.000 50.09683 ? 134 GLU   D OE1   1 
ATOM   5008 O  OE2   . GLU   D 2 135 ? 82.19300  2.44500   20.15800  1.000 50.28880 ? 134 GLU   D OE2   1 
ATOM   5009 N  N     . GLY   D 2 136 ? 84.71400  -1.60800  24.74600  1.000 15.18913 ? 135 GLY   D N     1 
ATOM   5010 C  CA    . GLY   D 2 136 ? 85.55500  -1.70900  25.92200  1.000 12.29061 ? 135 GLY   D CA    1 
ATOM   5011 C  C     . GLY   D 2 136 ? 85.77500  -3.10400  26.45200  1.000 16.05470 ? 135 GLY   D C     1 
ATOM   5012 O  O     . GLY   D 2 136 ? 86.11900  -3.25200  27.63000  1.000 14.46183 ? 135 GLY   D O     1 
ATOM   5013 N  N     . MET   D 2 137 ? 85.58500  -4.13900  25.63300  1.000 13.41170 ? 136 MET   D N     1 
ATOM   5014 C  CA    . MET   D 2 137 ? 85.88100  -5.48100  26.11300  1.000 14.04714 ? 136 MET   D CA    1 
ATOM   5015 C  C     . MET   D 2 137 ? 87.33800  -5.60200  26.54200  1.000 13.68881 ? 136 MET   D C     1 
ATOM   5016 O  O     . MET   D 2 137 ? 87.64400  -6.29900  27.51600  1.000 13.11222 ? 136 MET   D O     1 
ATOM   5017 C  CB    . MET   D 2 137 ? 85.54000  -6.51700  25.04200  1.000 17.92699 ? 136 MET   D CB    1 
ATOM   5018 C  CG    . MET   D 2 137 ? 85.44600  -7.94500  25.58000  1.000 21.61657 ? 136 MET   D CG    1 
ATOM   5019 S  SD    . MET   D 2 137 ? 84.14500  -8.18200  26.79700  1.000 16.24666 ? 136 MET   D SD    1 
ATOM   5020 C  CE    . MET   D 2 137 ? 84.83700  -9.55200  27.73000  1.000 20.32231 ? 136 MET   D CE    1 
ATOM   5021 N  N     . ASN   D 2 138 ? 88.25000  -4.91700  25.85100  1.000 13.39105 ? 137 ASN   D N     1 
ATOM   5022 C  CA    . ASN   D 2 138 ? 89.64000  -4.95500  26.28700  1.000 15.96473 ? 137 ASN   D CA    1 
ATOM   5023 C  C     . ASN   D 2 138 ? 89.79100  -4.39100  27.69900  1.000 14.98378 ? 137 ASN   D C     1 
ATOM   5024 O  O     . ASN   D 2 138 ? 90.69900  -4.79700  28.43900  1.000 13.71053 ? 137 ASN   D O     1 
ATOM   5025 C  CB    . ASN   D 2 138 ? 90.52000  -4.19300  25.30000  1.000 17.26602 ? 137 ASN   D CB    1 
ATOM   5026 C  CG    . ASN   D 2 138 ? 90.22300  -2.70200  25.28700  1.000 19.86227 ? 137 ASN   D CG    1 
ATOM   5027 O  OD1   . ASN   D 2 138 ? 89.06200  -2.27800  25.25200  1.000 19.07468 ? 137 ASN   D OD1   1 
ATOM   5028 N  ND2   . ASN   D 2 138 ? 91.27900  -1.89900  25.31800  1.000 23.55943 ? 137 ASN   D ND2   1 
ATOM   5029 N  N     . ILE   D 2 139 ? 88.89700  -3.48000  28.09900  1.000 12.53267 ? 138 ILE   D N     1 
ATOM   5030 C  CA    . ILE   D 2 139 ? 88.95900  -2.93600  29.45100  1.000 12.34935 ? 138 ILE   D CA    1 
ATOM   5031 C  C     . ILE   D 2 139 ? 88.47400  -3.97800  30.45800  1.000 12.69798 ? 138 ILE   D C     1 
ATOM   5032 O  O     . ILE   D 2 139 ? 89.01900  -4.09600  31.55700  1.000 12.01352 ? 138 ILE   D O     1 
ATOM   5033 C  CB    . ILE   D 2 139 ? 88.15200  -1.62400  29.54100  1.000 14.80246 ? 138 ILE   D CB    1 
ATOM   5034 C  CG1   . ILE   D 2 139 ? 88.66000  -0.59300  28.52900  1.000 12.51830 ? 138 ILE   D CG1   1 
ATOM   5035 C  CG2   . ILE   D 2 139 ? 88.20000  -1.05900  30.95600  1.000 13.16751 ? 138 ILE   D CG2   1 
ATOM   5036 C  CD1   . ILE   D 2 139 ? 90.15300  -0.23500  28.64800  1.000 15.28977 ? 138 ILE   D CD1   1 
ATOM   5037 N  N     . VAL   D 2 140 ? 87.45100  -4.75700  30.09300  1.000 10.63339 ? 139 VAL   D N     1 
ATOM   5038 C  CA    . VAL   D 2 140 ? 86.99900  -5.85400  30.94400  1.000 11.69592 ? 139 VAL   D CA    1 
ATOM   5039 C  C     . VAL   D 2 140 ? 88.12200  -6.86600  31.13600  1.000 15.01946 ? 139 VAL   D C     1 
ATOM   5040 O  O     . VAL   D 2 140 ? 88.40300  -7.31800  32.25500  1.000 12.03674 ? 139 VAL   D O     1 
ATOM   5041 C  CB    . VAL   D 2 140 ? 85.73600  -6.50200  30.34200  1.000 10.47091 ? 139 VAL   D CB    1 
ATOM   5042 C  CG1   . VAL   D 2 140 ? 85.35700  -7.77200  31.09800  1.000 11.63398 ? 139 VAL   D CG1   1 
ATOM   5043 C  CG2   . VAL   D 2 140 ? 84.58900  -5.51300  30.39000  1.000 9.10536  ? 139 VAL   D CG2   1 
ATOM   5044 N  N     . GLU   D 2 141 ? 88.81400  -7.19500  30.04600  1.000 14.90832 ? 140 GLU   D N     1 
ATOM   5045 C  CA    . GLU   D 2 141 ? 89.93300  -8.12300  30.13500  1.000 14.71737 ? 140 GLU   D CA    1 
ATOM   5046 C  C     . GLU   D 2 141 ? 91.04200  -7.57000  31.02600  1.000 18.35335 ? 140 GLU   D C     1 
ATOM   5047 O  O     . GLU   D 2 141 ? 91.65100  -8.31700  31.80400  1.000 17.39979 ? 140 GLU   D O     1 
ATOM   5048 C  CB    . GLU   D 2 141 ? 90.44300  -8.44600  28.73100  1.000 15.55838 ? 140 GLU   D CB    1 
ATOM   5049 C  CG    . GLU   D 2 141 ? 89.37000  -9.13800  27.86900  1.000 13.56734 ? 140 GLU   D CG    1 
ATOM   5050 C  CD    . GLU   D 2 141 ? 89.69500  -9.13100  26.38500  1.000 23.69076 ? 140 GLU   D CD    1 
ATOM   5051 O  OE1   . GLU   D 2 141 ? 90.65600  -8.44100  25.97400  1.000 22.87044 ? 140 GLU   D OE1   1 
ATOM   5052 O  OE2   . GLU   D 2 141 ? 88.99300  -9.82800  25.62300  1.000 24.23438 ? 140 GLU   D OE2   1 
ATOM   5053 N  N     . ALA   D 2 142 ? 91.30600  -6.26100  30.94600  1.000 13.19196 ? 141 ALA   D N     1 
ATOM   5054 C  CA    . ALA   D 2 142 ? 92.30500  -5.66000  31.83000  1.000 13.65349 ? 141 ALA   D CA    1 
ATOM   5055 C  C     . ALA   D 2 142 ? 91.84700  -5.70000  33.29000  1.000 14.55178 ? 141 ALA   D C     1 
ATOM   5056 O  O     . ALA   D 2 142 ? 92.65400  -5.93600  34.19200  1.000 13.85852 ? 141 ALA   D O     1 
ATOM   5057 C  CB    . ALA   D 2 142 ? 92.60200  -4.22500  31.38600  1.000 14.00902 ? 141 ALA   D CB    1 
ATOM   5058 N  N     . MET   D 2 143 ? 90.55400  -5.47000  33.53800  1.000 13.31801 ? 142 MET   D N     1 
ATOM   5059 C  CA    . MET   D 2 143 ? 90.01500  -5.59000  34.89100  1.000 16.30900 ? 142 MET   D CA    1 
ATOM   5060 C  C     . MET   D 2 143 ? 90.22000  -6.99600  35.43000  1.000 17.82606 ? 142 MET   D C     1 
ATOM   5061 O  O     . MET   D 2 143 ? 90.63900  -7.18300  36.58000  1.000 15.98270 ? 142 MET   D O     1 
ATOM   5062 C  CB    . MET   D 2 143 ? 88.52100  -5.26300  34.89600  1.000 18.08168 ? 142 MET   D CB    1 
ATOM   5063 C  CG    . MET   D 2 143 ? 88.16500  -3.87600  34.44100  1.000 11.54969 ? 142 MET   D CG    1 
ATOM   5064 S  SD    . MET   D 2 143 ? 86.36900  -3.67700  34.25400  1.000 16.17047 ? 142 MET   D SD    1 
ATOM   5065 C  CE    . MET   D 2 143 ? 85.81800  -4.25800  35.86300  1.000 10.36817 ? 142 MET   D CE    1 
ATOM   5066 N  N     . GLU   D 2 144 ? 89.93100  -7.99300  34.59400  1.000 17.96089 ? 143 GLU   D N     1 
ATOM   5067 C  CA    . GLU   D 2 144 ? 89.98900  -9.39000  34.99600  1.000 21.32905 ? 143 GLU   D CA    1 
ATOM   5068 C  C     . GLU   D 2 144 ? 91.34900  -9.75700  35.57500  1.000 15.37938 ? 143 GLU   D C     1 
ATOM   5069 O  O     . GLU   D 2 144 ? 91.43300  -10.62400 36.44800  1.000 20.15941 ? 143 GLU   D O     1 
ATOM   5070 C  CB    . GLU   D 2 144 ? 89.63800  -10.25800 33.78400  1.000 18.15138 ? 143 GLU   D CB    1 
ATOM   5071 C  CG    . GLU   D 2 144 ? 89.48200  -11.74100 34.03200  1.000 16.66082 ? 143 GLU   D CG    1 
ATOM   5072 C  CD    . GLU   D 2 144 ? 89.25200  -12.48300 32.72300  1.000 21.24812 ? 143 GLU   D CD    1 
ATOM   5073 O  OE1   . GLU   D 2 144 ? 89.59500  -11.90500 31.67000  1.000 20.20175 ? 143 GLU   D OE1   1 
ATOM   5074 O  OE2   . GLU   D 2 144 ? 88.72400  -13.61800 32.73900  1.000 22.33664 ? 143 GLU   D OE2   1 
ATOM   5075 N  N     . ARG   D 2 145 ? 92.41800  -9.08500  35.13600  1.000 19.98267 ? 144 ARG   D N     1 
ATOM   5076 C  CA    . ARG   D 2 145 ? 93.74900  -9.38700  35.64200  1.000 17.85458 ? 144 ARG   D CA    1 
ATOM   5077 C  C     . ARG   D 2 145 ? 93.97200  -8.90700  37.07000  1.000 23.16163 ? 144 ARG   D C     1 
ATOM   5078 O  O     . ARG   D 2 145 ? 94.99800  -9.25000  37.66500  1.000 18.95885 ? 144 ARG   D O     1 
ATOM   5079 C  CB    . ARG   D 2 145 ? 94.82000  -8.78300  34.73000  1.000 24.38953 ? 144 ARG   D CB    1 
ATOM   5080 C  CG    . ARG   D 2 145 ? 95.00900  -9.54700  33.43000  1.000 26.03978 ? 144 ARG   D CG    1 
ATOM   5081 C  CD    . ARG   D 2 145 ? 95.29500  -8.59500  32.28400  1.000 32.92692 ? 144 ARG   D CD    1 
ATOM   5082 N  NE    . ARG   D 2 145 ? 95.11900  -9.24900  30.99200  1.000 39.61400 ? 144 ARG   D NE    1 
ATOM   5083 C  CZ    . ARG   D 2 145 ? 94.81100  -8.61700  29.86700  1.000 35.30822 ? 144 ARG   D CZ    1 
ATOM   5084 N  NH1   . ARG   D 2 145 ? 94.62800  -7.30400  29.83900  1.000 30.34355 ? 144 ARG   D NH1   1 
ATOM   5085 N  NH2   . ARG   D 2 145 ? 94.67100  -9.32100  28.74500  1.000 30.40442 ? 144 ARG   D NH2   1 
ATOM   5086 N  N     . PHE   D 2 146 ? 93.05600  -8.13100  37.63500  1.000 17.73672 ? 145 PHE   D N     1 
ATOM   5087 C  CA    . PHE   D 2 146 ? 93.19100  -7.68600  39.00900  1.000 16.36686 ? 145 PHE   D CA    1 
ATOM   5088 C  C     . PHE   D 2 146 ? 92.50100  -8.61100  40.00200  1.000 15.36277 ? 145 PHE   D C     1 
ATOM   5089 O  O     . PHE   D 2 146 ? 92.61800  -8.39300  41.20800  1.000 16.38364 ? 145 PHE   D O     1 
ATOM   5090 C  CB    . PHE   D 2 146 ? 92.64600  -6.26400  39.16300  1.000 12.84961 ? 145 PHE   D CB    1 
ATOM   5091 C  CG    . PHE   D 2 146 ? 93.49800  -5.21900  38.50100  1.000 16.15033 ? 145 PHE   D CG    1 
ATOM   5092 C  CD1   . PHE   D 2 146 ? 94.72000  -4.86300  39.04500  1.000 17.36553 ? 145 PHE   D CD1   1 
ATOM   5093 C  CD2   . PHE   D 2 146 ? 93.08200  -4.59900  37.33500  1.000 18.12533 ? 145 PHE   D CD2   1 
ATOM   5094 C  CE1   . PHE   D 2 146 ? 95.51200  -3.90100  38.44200  1.000 21.44765 ? 145 PHE   D CE1   1 
ATOM   5095 C  CE2   . PHE   D 2 146 ? 93.87100  -3.64700  36.72300  1.000 16.17589 ? 145 PHE   D CE2   1 
ATOM   5096 C  CZ    . PHE   D 2 146 ? 95.08000  -3.29300  37.27900  1.000 19.78097 ? 145 PHE   D CZ    1 
ATOM   5097 N  N     . GLY   D 2 147 ? 91.79300  -9.63400  39.53000  1.000 17.27115 ? 146 GLY   D N     1 
ATOM   5098 C  CA    . GLY   D 2 147 ? 91.12700  -10.57600 40.40300  1.000 13.64887 ? 146 GLY   D CA    1 
ATOM   5099 C  C     . GLY   D 2 147 ? 92.02400  -11.74100 40.76300  1.000 14.47142 ? 146 GLY   D C     1 
ATOM   5100 O  O     . GLY   D 2 147 ? 93.23500  -11.73000 40.54000  1.000 17.10848 ? 146 GLY   D O     1 
ATOM   5101 N  N     . SER   D 2 148 ? 91.40100  -12.77600 41.32300  1.000 19.88127 ? 147 SER   D N     1 
ATOM   5102 C  CA    . SER   D 2 148 ? 92.11700  -13.96700 41.76400  1.000 14.80248 ? 147 SER   D CA    1 
ATOM   5103 C  C     . SER   D 2 148 ? 91.12600  -15.11900 41.87700  1.000 19.06246 ? 147 SER   D C     1 
ATOM   5104 O  O     . SER   D 2 148 ? 89.92100  -14.95400 41.65600  1.000 13.59983 ? 147 SER   D O     1 
ATOM   5105 C  CB    . SER   D 2 148 ? 92.81400  -13.73100 43.09900  1.000 17.35363 ? 147 SER   D CB    1 
ATOM   5106 O  OG    . SER   D 2 148 ? 91.84900  -13.47400 44.10700  1.000 16.46137 ? 147 SER   D OG    1 
ATOM   5107 N  N     . ARG   D 2 149 ? 91.65300  -16.28600 42.27300  1.000 15.80735 ? 148 ARG   D N     1 
ATOM   5108 C  CA    . ARG   D 2 149 ? 90.85100  -17.50700 42.34000  1.000 22.37303 ? 148 ARG   D CA    1 
ATOM   5109 C  C     . ARG   D 2 149 ? 89.64700  -17.37000 43.25400  1.000 15.48044 ? 148 ARG   D C     1 
ATOM   5110 O  O     . ARG   D 2 149 ? 88.61400  -18.00300 43.00900  1.000 19.86310 ? 148 ARG   D O     1 
ATOM   5111 C  CB    . ARG   D 2 149 ? 91.70200  -18.67400 42.82700  1.000 19.03043 ? 148 ARG   D CB    1 
ATOM   5112 C  CG    . ARG   D 2 149 ? 92.18400  -19.55900 41.72000  1.000 30.65146 ? 148 ARG   D CG    1 
ATOM   5113 C  CD    . ARG   D 2 149 ? 93.11400  -20.59100 42.29700  1.000 29.32290 ? 148 ARG   D CD    1 
ATOM   5114 N  NE    . ARG   D 2 149 ? 92.62300  -21.07300 43.58100  1.000 25.47346 ? 148 ARG   D NE    1 
ATOM   5115 C  CZ    . ARG   D 2 149 ? 91.89200  -22.16800 43.73300  1.000 25.20017 ? 148 ARG   D CZ    1 
ATOM   5116 N  NH1   . ARG   D 2 149 ? 91.55000  -22.92200 42.69900  1.000 24.63533 ? 148 ARG   D NH1   1 
ATOM   5117 N  NH2   . ARG   D 2 149 ? 91.51800  -22.52800 44.95400  1.000 20.84372 ? 148 ARG   D NH2   1 
ATOM   5118 N  N     . ASN   D 2 150 ? 89.77300  -16.62000 44.35100  1.000 14.81272 ? 149 ASN   D N     1 
ATOM   5119 C  CA    . ASN   D 2 150 ? 88.67100  -16.49300 45.29600  1.000 15.25799 ? 149 ASN   D CA    1 
ATOM   5120 C  C     . ASN   D 2 150 ? 87.92800  -15.16100 45.15200  1.000 16.02967 ? 149 ASN   D C     1 
ATOM   5121 O  O     . ASN   D 2 150 ? 87.17900  -14.77500 46.05400  1.000 12.65914 ? 149 ASN   D O     1 
ATOM   5122 C  CB    . ASN   D 2 150 ? 89.16300  -16.70200 46.73200  1.000 15.18327 ? 149 ASN   D CB    1 
ATOM   5123 C  CG    . ASN   D 2 150 ? 90.06400  -15.59100 47.22500  1.000 19.92826 ? 149 ASN   D CG    1 
ATOM   5124 O  OD1   . ASN   D 2 150 ? 90.33400  -14.62700 46.50900  1.000 19.79881 ? 149 ASN   D OD1   1 
ATOM   5125 N  ND2   . ASN   D 2 150 ? 90.52400  -15.71300 48.47100  1.000 21.66332 ? 149 ASN   D ND2   1 
ATOM   5126 N  N     . GLY   D 2 151 ? 88.13200  -14.45300 44.04200  1.000 12.43543 ? 150 GLY   D N     1 
ATOM   5127 C  CA    . GLY   D 2 151 ? 87.43600  -13.21400 43.77600  1.000 16.55176 ? 150 GLY   D CA    1 
ATOM   5128 C  C     . GLY   D 2 151 ? 88.09100  -11.95500 44.32200  1.000 15.14283 ? 150 GLY   D C     1 
ATOM   5129 O  O     . GLY   D 2 151 ? 87.76900  -10.85800 43.84800  1.000 13.72513 ? 150 GLY   D O     1 
ATOM   5130 N  N     . LYS   D 2 152 ? 88.99200  -12.06700 45.29700  1.000 12.83000 ? 151 LYS   D N     1 
ATOM   5131 C  CA    . LYS   D 2 152 ? 89.58800  -10.86900 45.88100  1.000 17.79535 ? 151 LYS   D CA    1 
ATOM   5132 C  C     . LYS   D 2 152 ? 90.41400  -10.11500 44.84500  1.000 16.83636 ? 151 LYS   D C     1 
ATOM   5133 O  O     . LYS   D 2 152 ? 91.14000  -10.71800 44.04900  1.000 16.62344 ? 151 LYS   D O     1 
ATOM   5134 C  CB    . LYS   D 2 152 ? 90.47200  -11.22700 47.07800  1.000 18.92157 ? 151 LYS   D CB    1 
ATOM   5135 C  CG    . LYS   D 2 152 ? 89.70600  -11.74600 48.29800  1.000 21.42010 ? 151 LYS   D CG    1 
ATOM   5136 C  CD    . LYS   D 2 152 ? 88.72400  -10.69400 48.80200  1.000 27.65665 ? 151 LYS   D CD    1 
ATOM   5137 C  CE    . LYS   D 2 152 ? 87.98700  -11.15100 50.05500  1.000 31.06696 ? 151 LYS   D CE    1 
ATOM   5138 N  NZ    . LYS   D 2 152 ? 87.00400  -10.12500 50.51200  1.000 25.42640 ? 151 LYS   D NZ    1 
ATOM   5139 N  N     . THR   D 2 153 ? 90.31100  -8.78500  44.86900  1.000 14.09908 ? 152 THR   D N     1 
ATOM   5140 C  CA    . THR   D 2 153 ? 90.99300  -7.93800  43.90700  1.000 14.87864 ? 152 THR   D CA    1 
ATOM   5141 C  C     . THR   D 2 153 ? 92.22300  -7.31400  44.55100  1.000 16.16913 ? 152 THR   D C     1 
ATOM   5142 O  O     . THR   D 2 153 ? 92.22500  -6.99100  45.74600  1.000 13.98661 ? 152 THR   D O     1 
ATOM   5143 C  CB    . THR   D 2 153 ? 90.05900  -6.85100  43.35500  1.000 12.22298 ? 152 THR   D CB    1 
ATOM   5144 O  OG1   . THR   D 2 153 ? 89.62200  -5.99300  44.41800  1.000 15.57817 ? 152 THR   D OG1   1 
ATOM   5145 C  CG2   . THR   D 2 153 ? 88.83000  -7.49800  42.70300  1.000 11.17166 ? 152 THR   D CG2   1 
ATOM   5146 N  N     . SER   D 2 154 ? 93.27500  -7.16900  43.74500  1.000 17.86047 ? 153 SER   D N     1 
ATOM   5147 C  CA    . SER   D 2 154 ? 94.57600  -6.73000  44.22700  1.000 17.01862 ? 153 SER   D CA    1 
ATOM   5148 C  C     . SER   D 2 154 ? 94.72700  -5.21800  44.20900  1.000 15.77035 ? 153 SER   D C     1 
ATOM   5149 O  O     . SER   D 2 154 ? 95.65100  -4.69300  44.84100  1.000 19.19543 ? 153 SER   D O     1 
ATOM   5150 C  CB    . SER   D 2 154 ? 95.67700  -7.38400  43.39000  1.000 17.51654 ? 153 SER   D CB    1 
ATOM   5151 O  OG    . SER   D 2 154 ? 95.42000  -7.19500  42.00900  1.000 19.33616 ? 153 SER   D OG    1 
ATOM   5152 N  N     . LYS   D 2 155 ? 93.83600  -4.52500  43.50100  1.000 16.77944 ? 154 LYS   D N     1 
ATOM   5153 C  CA    . LYS   D 2 155 ? 93.66800  -3.08700  43.56000  1.000 14.06211 ? 154 LYS   D CA    1 
ATOM   5154 C  C     . LYS   D 2 155 ? 92.17300  -2.80300  43.56900  1.000 12.89663 ? 154 LYS   D C     1 
ATOM   5155 O  O     . LYS   D 2 155 ? 91.35700  -3.67400  43.28700  1.000 12.18776 ? 154 LYS   D O     1 
ATOM   5156 C  CB    . LYS   D 2 155 ? 94.37700  -2.39200  42.39200  1.000 14.50369 ? 154 LYS   D CB    1 
ATOM   5157 C  CG    . LYS   D 2 155 ? 95.89700  -2.55600  42.48600  1.000 17.57679 ? 154 LYS   D CG    1 
ATOM   5158 C  CD    . LYS   D 2 155 ? 96.66100  -1.73100  41.45700  1.000 26.69501 ? 154 LYS   D CD    1 
ATOM   5159 C  CE    . LYS   D 2 155 ? 98.17500  -1.91400  41.66200  1.000 31.63087 ? 154 LYS   D CE    1 
ATOM   5160 N  NZ    . LYS   D 2 155 ? 98.98000  -1.55600  40.46100  1.000 36.69467 ? 154 LYS   D NZ    1 
ATOM   5161 N  N     . LYS   D 2 156 ? 91.81900  -1.59100  43.95500  1.000 16.16001 ? 155 LYS   D N     1 
ATOM   5162 C  CA    . LYS   D 2 156 ? 90.42200  -1.18400  44.03600  1.000 12.82055 ? 155 LYS   D CA    1 
ATOM   5163 C  C     . LYS   D 2 156 ? 89.91500  -0.85100  42.63800  1.000 14.67359 ? 155 LYS   D C     1 
ATOM   5164 O  O     . LYS   D 2 156 ? 90.43300  0.06700   41.99200  1.000 11.83410 ? 155 LYS   D O     1 
ATOM   5165 C  CB    . LYS   D 2 156 ? 90.29600  0.02300   44.96200  1.000 17.26619 ? 155 LYS   D CB    1 
ATOM   5166 C  CG    . LYS   D 2 156 ? 88.90200  0.32000   45.46900  1.000 27.97463 ? 155 LYS   D CG    1 
ATOM   5167 C  CD    . LYS   D 2 156 ? 88.48300  -0.67300  46.53600  1.000 33.53525 ? 155 LYS   D CD    1 
ATOM   5168 C  CE    . LYS   D 2 156 ? 87.36900  -0.11400  47.41900  1.000 31.05287 ? 155 LYS   D CE    1 
ATOM   5169 N  NZ    . LYS   D 2 156 ? 86.30800  0.51800   46.62700  1.000 19.25390 ? 155 LYS   D NZ    1 
ATOM   5170 N  N     . ILE   D 2 157 ? 88.90600  -1.58400  42.16800  1.000 11.10931 ? 156 ILE   D N     1 
ATOM   5171 C  CA    . ILE   D 2 157 ? 88.38400  -1.41300  40.81500  1.000 10.04011 ? 156 ILE   D CA    1 
ATOM   5172 C  C     . ILE   D 2 157 ? 87.02000  -0.74600  40.94800  1.000 12.18606 ? 156 ILE   D C     1 
ATOM   5173 O  O     . ILE   D 2 157 ? 86.09200  -1.35000  41.48200  1.000 12.29447 ? 156 ILE   D O     1 
ATOM   5174 C  CB    . ILE   D 2 157 ? 88.26800  -2.75600  40.07900  1.000 12.13221 ? 156 ILE   D CB    1 
ATOM   5175 C  CG1   . ILE   D 2 157 ? 89.56100  -3.57200  40.21300  1.000 10.44501 ? 156 ILE   D CG1   1 
ATOM   5176 C  CG2   . ILE   D 2 157 ? 87.90500  -2.54600  38.61300  1.000 10.85509 ? 156 ILE   D CG2   1 
ATOM   5177 C  CD1   . ILE   D 2 157 ? 90.76800  -2.90500  39.62200  1.000 15.26054 ? 156 ILE   D CD1   1 
ATOM   5178 N  N     . THR   D 2 158 ? 86.87300  0.49300   40.49200  1.000 10.70914 ? 157 THR   D N     1 
ATOM   5179 C  CA    . THR   D 2 158 ? 85.62700  1.20600   40.75800  1.000 9.88747  ? 157 THR   D CA    1 
ATOM   5180 C  C     . THR   D 2 158 ? 85.01000  1.75300   39.48300  1.000 9.91292  ? 157 THR   D C     1 
ATOM   5181 O  O     . THR   D 2 158 ? 85.65700  1.88500   38.44200  1.000 10.07684 ? 157 THR   D O     1 
ATOM   5182 C  CB    . THR   D 2 158 ? 85.81300  2.34900   41.76100  1.000 10.76403 ? 157 THR   D CB    1 
ATOM   5183 O  OG1   . THR   D 2 158 ? 86.77600  3.27500   41.25800  1.000 13.33499 ? 157 THR   D OG1   1 
ATOM   5184 C  CG2   . THR   D 2 158 ? 86.30300  1.80800   43.10200  1.000 17.83899 ? 157 THR   D CG2   1 
ATOM   5185 N  N     . ILE   D 2 159 ? 83.70800  2.01800   39.58100  1.000 11.85937 ? 158 ILE   D N     1 
ATOM   5186 C  CA    . ILE   D 2 159 ? 82.96700  2.72000   38.54300  1.000 8.61777  ? 158 ILE   D CA    1 
ATOM   5187 C  C     . ILE   D 2 159 ? 83.11800  4.20000   38.87800  1.000 13.18483 ? 158 ILE   D C     1 
ATOM   5188 O  O     . ILE   D 2 159 ? 82.36500  4.76800   39.68000  1.000 13.43786 ? 158 ILE   D O     1 
ATOM   5189 C  CB    . ILE   D 2 159 ? 81.51000  2.27300   38.49400  1.000 9.78539  ? 158 ILE   D CB    1 
ATOM   5190 C  CG1   . ILE   D 2 159 ? 81.43600  0.74500   38.34700  1.000 8.98206  ? 158 ILE   D CG1   1 
ATOM   5191 C  CG2   . ILE   D 2 159 ? 80.73700  3.02700   37.39400  1.000 8.19241  ? 158 ILE   D CG2   1 
ATOM   5192 C  CD1   . ILE   D 2 159 ? 80.01200  0.21900   38.62600  1.000 6.91155  ? 158 ILE   D CD1   1 
ATOM   5193 N  N     . ALA   D 2 160 ? 84.13100  4.82600   38.27800  1.000 10.55597 ? 159 ALA   D N     1 
ATOM   5194 C  CA    . ALA   D 2 160 ? 84.43100  6.21300   38.59300  1.000 11.93194 ? 159 ALA   D CA    1 
ATOM   5195 C  C     . ALA   D 2 160 ? 83.35800  7.15000   38.06100  1.000 17.15915 ? 159 ALA   D C     1 
ATOM   5196 O  O     . ALA   D 2 160 ? 83.10400  8.21000   38.65200  1.000 11.80258 ? 159 ALA   D O     1 
ATOM   5197 C  CB    . ALA   D 2 160 ? 85.78700  6.58000   38.01700  1.000 12.06578 ? 159 ALA   D CB    1 
ATOM   5198 N  N     . ASP   D 2 161 ? 82.74000  6.78000   36.94400  1.000 11.39444 ? 160 ASP   D N     1 
ATOM   5199 C  CA    . ASP   D 2 161 ? 81.64300  7.53400   36.36100  1.000 11.39111 ? 160 ASP   D CA    1 
ATOM   5200 C  C     . ASP   D 2 161 ? 80.77800  6.55100   35.59100  1.000 12.48581 ? 160 ASP   D C     1 
ATOM   5201 O  O     . ASP   D 2 161 ? 81.23500  5.48800   35.16700  1.000 11.65672 ? 160 ASP   D O     1 
ATOM   5202 C  CB    . ASP   D 2 161 ? 82.14200  8.65100   35.44500  1.000 11.85115 ? 160 ASP   D CB    1 
ATOM   5203 C  CG    . ASP   D 2 161 ? 81.07400  9.69800   35.16100  1.000 17.42922 ? 160 ASP   D CG    1 
ATOM   5204 O  OD1   . ASP   D 2 161 ? 80.03000  9.70300   35.85300  1.000 15.57018 ? 160 ASP   D OD1   1 
ATOM   5205 O  OD2   . ASP   D 2 161 ? 81.28600  10.52900  34.25300  1.000 16.11748 ? 160 ASP   D OD2   1 
ATOM   5206 N  N     . CYS   D 2 162 ? 79.51100  6.90000   35.43100  1.000 12.50427 ? 161 CYS   D N     1 
ATOM   5207 C  CA    . CYS   D 2 162 ? 78.61900  6.06100   34.65000  1.000 9.69694  ? 161 CYS   D CA    1 
ATOM   5208 C  C     . CYS   D 2 162 ? 77.42700  6.91700   34.25800  1.000 12.16281 ? 161 CYS   D C     1 
ATOM   5209 O  O     . CYS   D 2 162 ? 77.16400  7.95800   34.86800  1.000 10.60079 ? 161 CYS   D O     1 
ATOM   5210 C  CB    . CYS   D 2 162 ? 78.17800  4.80500   35.42100  1.000 8.61189  ? 161 CYS   D CB    1 
ATOM   5211 S  SG    . CYS   D 2 162 ? 77.58400  5.10200   37.09900  1.000 12.81046 ? 161 CYS   D SG    1 
ATOM   5212 N  N     . GLY   D 2 163 ? 76.73500  6.48000   33.21800  1.000 11.02403 ? 162 GLY   D N     1 
ATOM   5213 C  CA    . GLY   D 2 163 ? 75.59200  7.22100   32.72500  1.000 15.76381 ? 162 GLY   D CA    1 
ATOM   5214 C  C     . GLY   D 2 163 ? 75.05900  6.58900   31.46300  1.000 11.31092 ? 162 GLY   D C     1 
ATOM   5215 O  O     . GLY   D 2 163 ? 75.40100  5.45600   31.12600  1.000 10.23892 ? 162 GLY   D O     1 
ATOM   5216 N  N     . GLN   D 2 164 ? 74.21500  7.33700   30.76000  1.000 11.75264 ? 163 GLN   D N     1 
ATOM   5217 C  CA    . GLN   D 2 164 ? 73.57800  6.86300   29.54000  1.000 12.07389 ? 163 GLN   D CA    1 
ATOM   5218 C  C     . GLN   D 2 164 ? 74.15100  7.60100   28.33500  1.000 15.72069 ? 163 GLN   D C     1 
ATOM   5219 O  O     . GLN   D 2 164 ? 74.37600  8.81700   28.38900  1.000 16.93149 ? 163 GLN   D O     1 
ATOM   5220 C  CB    . GLN   D 2 164 ? 72.05500  7.06300   29.60300  1.000 12.80441 ? 163 GLN   D CB    1 
ATOM   5221 C  CG    . GLN   D 2 164 ? 71.31100  6.27900   28.54000  1.000 11.98594 ? 163 GLN   D CG    1 
ATOM   5222 C  CD    . GLN   D 2 164 ? 69.79300  6.36800   28.68900  1.000 15.57245 ? 163 GLN   D CD    1 
ATOM   5223 O  OE1   . GLN   D 2 164 ? 69.28200  6.74600   29.73600  1.000 15.14062 ? 163 GLN   D OE1   1 
ATOM   5224 N  NE2   . GLN   D 2 164 ? 69.07600  6.00700   27.63400  1.000 17.80679 ? 163 GLN   D NE2   1 
ATOM   5225 N  N     . LEU   D 2 165 ? 74.36400  6.86500   27.24700  1.000 11.73170 ? 164 LEU   D N     1 
ATOM   5226 C  CA    . LEU   D 2 165 ? 74.89700  7.42500   26.00300  1.000 14.96520 ? 164 LEU   D CA    1 
ATOM   5227 C  C     . LEU   D 2 165 ? 73.80200  7.72800   24.98800  1.000 21.72816 ? 164 LEU   D C     1 
ATOM   5228 O  O     . LEU   D 2 165 ? 72.96600  6.86700   24.71000  1.000 27.31053 ? 164 LEU   D O     1 
ATOM   5229 C  CB    . LEU   D 2 165 ? 75.92800  6.46700   25.38900  1.000 17.35121 ? 164 LEU   D CB    1 
ATOM   5230 C  CG    . LEU   D 2 165 ? 77.24000  6.26100   26.16300  1.000 17.75394 ? 164 LEU   D CG    1 
ATOM   5231 C  CD1   . LEU   D 2 165 ? 78.16300  5.33600   25.39100  1.000 17.48365 ? 164 LEU   D CD1   1 
ATOM   5232 C  CD2   . LEU   D 2 165 ? 77.91900  7.59400   26.43600  1.000 23.12429 ? 164 LEU   D CD2   1 
HETATM 5233 P  PG    . GNP   E 3 .   ? 49.36100  -31.49000 -2.30600  1.000 8.76739  ? 201 GNP   B PG    1 
HETATM 5234 O  O1G   . GNP   E 3 .   ? 50.84800  -31.46100 -2.12600  1.000 8.98854  ? 201 GNP   B O1G   1 
HETATM 5235 O  O2G   . GNP   E 3 .   ? 48.79900  -30.06400 -2.06200  1.000 9.81632  ? 201 GNP   B O2G   1 
HETATM 5236 O  O3G   . GNP   E 3 .   ? 48.70000  -32.50700 -1.35500  1.000 9.58870  ? 201 GNP   B O3G   1 
HETATM 5237 N  N3B   . GNP   E 3 .   ? 48.95200  -31.98500 -3.88600  1.000 8.76940  ? 201 GNP   B N3B   1 
HETATM 5238 P  PB    . GNP   E 3 .   ? 49.63100  -31.41800 -5.25300  1.000 8.25106  ? 201 GNP   B PB    1 
HETATM 5239 O  O1B   . GNP   E 3 .   ? 49.06800  -30.04000 -5.56900  1.000 8.95949  ? 201 GNP   B O1B   1 
HETATM 5240 O  O2B   . GNP   E 3 .   ? 51.12800  -31.38000 -5.09000  1.000 7.97875  ? 201 GNP   B O2B   1 
HETATM 5241 O  O3A   . GNP   E 3 .   ? 49.22500  -32.47700 -6.42700  1.000 10.40895 ? 201 GNP   B O3A   1 
HETATM 5242 P  PA    . GNP   E 3 .   ? 50.14800  -33.65200 -6.96500  1.000 9.37452  ? 201 GNP   B PA    1 
HETATM 5243 O  O1A   . GNP   E 3 .   ? 51.23300  -33.04800 -7.84700  1.000 9.72210  ? 201 GNP   B O1A   1 
HETATM 5244 O  O2A   . GNP   E 3 .   ? 50.63500  -34.59400 -5.87500  1.000 12.48927 ? 201 GNP   B O2A   1 
HETATM 5245 O  "O5'" . GNP   E 3 .   ? 49.13900  -34.39200 -7.92000  1.000 9.79140  ? 201 GNP   B "O5'" 1 
HETATM 5246 C  "C5'" . GNP   E 3 .   ? 47.89900  -34.94800 -7.43200  1.000 10.35091 ? 201 GNP   B "C5'" 1 
HETATM 5247 C  "C4'" . GNP   E 3 .   ? 47.44200  -36.00900 -8.40100  1.000 14.15119 ? 201 GNP   B "C4'" 1 
HETATM 5248 O  "O4'" . GNP   E 3 .   ? 47.11500  -35.41100 -9.67800  1.000 14.09377 ? 201 GNP   B "O4'" 1 
HETATM 5249 C  "C3'" . GNP   E 3 .   ? 48.45500  -37.11400 -8.69800  1.000 13.70249 ? 201 GNP   B "C3'" 1 
HETATM 5250 O  "O3'" . GNP   E 3 .   ? 47.78800  -38.36400 -8.84000  1.000 19.67133 ? 201 GNP   B "O3'" 1 
HETATM 5251 C  "C2'" . GNP   E 3 .   ? 49.09500  -36.64500 -10.00900 1.000 13.84403 ? 201 GNP   B "C2'" 1 
HETATM 5252 O  "O2'" . GNP   E 3 .   ? 49.55100  -37.71400 -10.83300 1.000 20.54475 ? 201 GNP   B "O2'" 1 
HETATM 5253 C  "C1'" . GNP   E 3 .   ? 47.91300  -35.97300 -10.70300 1.000 13.54880 ? 201 GNP   B "C1'" 1 
HETATM 5254 N  N9    . GNP   E 3 .   ? 48.32000  -34.90400 -11.63700 1.000 12.49969 ? 201 GNP   B N9    1 
HETATM 5255 C  C8    . GNP   E 3 .   ? 49.10100  -33.80500 -11.36200 1.000 11.58223 ? 201 GNP   B C8    1 
HETATM 5256 N  N7    . GNP   E 3 .   ? 49.29200  -33.02000 -12.40100 1.000 10.12499 ? 201 GNP   B N7    1 
HETATM 5257 C  C5    . GNP   E 3 .   ? 48.61200  -33.65200 -13.43400 1.000 12.61144 ? 201 GNP   B C5    1 
HETATM 5258 C  C6    . GNP   E 3 .   ? 48.43200  -33.29900 -14.82700 1.000 15.59814 ? 201 GNP   B C6    1 
HETATM 5259 O  O6    . GNP   E 3 .   ? 48.87500  -32.33000 -15.42100 1.000 11.27925 ? 201 GNP   B O6    1 
HETATM 5260 N  N1    . GNP   E 3 .   ? 47.65400  -34.22500 -15.49800 1.000 14.85541 ? 201 GNP   B N1    1 
HETATM 5261 C  C2    . GNP   E 3 .   ? 47.10900  -35.34900 -14.94400 1.000 13.96039 ? 201 GNP   B C2    1 
HETATM 5262 N  N2    . GNP   E 3 .   ? 46.39400  -36.13300 -15.75300 1.000 14.18380 ? 201 GNP   B N2    1 
HETATM 5263 N  N3    . GNP   E 3 .   ? 47.24900  -35.68300 -13.66000 1.000 13.29864 ? 201 GNP   B N3    1 
HETATM 5264 C  C4    . GNP   E 3 .   ? 48.00700  -34.81600 -12.97200 1.000 11.57943 ? 201 GNP   B C4    1 
HETATM 5265 MG MG    . MG    F 4 .   ? 52.32800  -31.76400 -3.50000  1.000 10.04099 ? 202 MG    B MG    1 
HETATM 5266 C  C1    . A1AOK G 5 .   ? 45.90800  -37.28400 5.81700   1.000 9.62380  ? 203 A1AOK B C1    1 
HETATM 5267 C  C10   . A1AOK G 5 .   ? 52.34100  -31.35800 11.23600  1.000 12.31950 ? 203 A1AOK B C10   1 
HETATM 5268 C  C11   . A1AOK G 5 .   ? 53.85300  -31.15500 11.36200  1.000 9.52113  ? 203 A1AOK B C11   1 
HETATM 5269 C  C12   . A1AOK G 5 .   ? 51.74200  -31.55200 12.63100  1.000 10.34587 ? 203 A1AOK B C12   1 
HETATM 5270 C  C13   . A1AOK G 5 .   ? 51.65500  -30.12700 10.62400  1.000 10.52747 ? 203 A1AOK B C13   1 
HETATM 5271 C  C14   . A1AOK G 5 .   ? 52.07000  -29.63900 9.26800   1.000 9.91196  ? 203 A1AOK B C14   1 
HETATM 5272 C  C15   . A1AOK G 5 .   ? 53.02500  -28.67500 8.98400   1.000 10.28148 ? 203 A1AOK B C15   1 
HETATM 5273 C  C16   . A1AOK G 5 .   ? 53.89500  -27.93200 9.91600   1.000 11.63092 ? 203 A1AOK B C16   1 
HETATM 5274 C  C17   . A1AOK G 5 .   ? 55.27100  -28.22200 10.00300  1.000 15.26550 ? 203 A1AOK B C17   1 
HETATM 5275 C  C18   . A1AOK G 5 .   ? 55.93300  -29.29900 9.17500   1.000 15.26001 ? 203 A1AOK B C18   1 
HETATM 5276 C  C19   . A1AOK G 5 .   ? 57.40100  -29.10800 8.81600   1.000 26.59545 ? 203 A1AOK B C19   1 
HETATM 5277 C  C2    . A1AOK G 5 .   ? 46.38000  -35.68600 7.58900   1.000 6.94331  ? 203 A1AOK B C2    1 
HETATM 5278 C  C20   . A1AOK G 5 .   ? 58.46200  -30.33700 10.62600  1.000 20.96487 ? 203 A1AOK B C20   1 
HETATM 5279 C  C21   . A1AOK G 5 .   ? 56.03300  -27.48800 10.91800  1.000 19.77602 ? 203 A1AOK B C21   1 
HETATM 5280 C  C22   . A1AOK G 5 .   ? 55.47700  -26.50200 11.70600  1.000 18.38774 ? 203 A1AOK B C22   1 
HETATM 5281 C  C23   . A1AOK G 5 .   ? 54.13600  -26.21700 11.60800  1.000 15.66944 ? 203 A1AOK B C23   1 
HETATM 5282 C  C24   . A1AOK G 5 .   ? 53.35000  -26.92600 10.72400  1.000 13.41427 ? 203 A1AOK B C24   1 
HETATM 5283 C  C25   . A1AOK G 5 .   ? 53.94500  -27.55500 6.86500   1.000 9.90827  ? 203 A1AOK B C25   1 
HETATM 5284 C  C26   . A1AOK G 5 .   ? 53.22000  -26.25700 6.60900   1.000 13.95131 ? 203 A1AOK B C26   1 
HETATM 5285 C  C27   . A1AOK G 5 .   ? 46.35600  -34.14800 7.46000   1.000 8.79193  ? 203 A1AOK B C27   1 
HETATM 5286 C  C28   . A1AOK G 5 .   ? 47.34900  -33.63400 6.44800   1.000 7.33692  ? 203 A1AOK B C28   1 
HETATM 5287 C  C29   . A1AOK G 5 .   ? 48.26700  -32.64900 6.80100   1.000 6.93627  ? 203 A1AOK B C29   1 
HETATM 5288 C  C3    . A1AOK G 5 .   ? 46.03900  -36.04100 9.03400   1.000 7.81235  ? 203 A1AOK B C3    1 
HETATM 5289 C  C30   . A1AOK G 5 .   ? 49.18300  -32.14200 5.88000   1.000 6.88181  ? 203 A1AOK B C30   1 
HETATM 5290 C  C31   . A1AOK G 5 .   ? 50.18500  -31.12600 6.30000   1.000 9.65383  ? 203 A1AOK B C31   1 
HETATM 5291 C  C32   . A1AOK G 5 .   ? 50.51000  -30.96000 7.64400   1.000 10.44349 ? 203 A1AOK B C32   1 
HETATM 5292 C  C33   . A1AOK G 5 .   ? 51.50900  -30.04600 8.01200   1.000 9.57985  ? 203 A1AOK B C33   1 
HETATM 5293 C  C34   . A1AOK G 5 .   ? 52.15700  -29.30600 7.00000   1.000 10.70532 ? 203 A1AOK B C34   1 
HETATM 5294 C  C35   . A1AOK G 5 .   ? 51.85200  -29.46000 5.65200   1.000 6.99348  ? 203 A1AOK B C35   1 
HETATM 5295 C  C36   . A1AOK G 5 .   ? 50.87400  -30.37000 5.32500   1.000 11.94675 ? 203 A1AOK B C36   1 
HETATM 5296 C  C37   . A1AOK G 5 .   ? 49.21800  -32.70200 4.59600   1.000 5.75159  ? 203 A1AOK B C37   1 
HETATM 5297 C  C38   . A1AOK G 5 .   ? 48.31200  -33.69200 4.23600   1.000 8.80397  ? 203 A1AOK B C38   1 
HETATM 5298 C  C39   . A1AOK G 5 .   ? 47.37900  -34.15200 5.16000   1.000 8.44073  ? 203 A1AOK B C39   1 
HETATM 5299 C  C4    . A1AOK G 5 .   ? 46.88800  -36.26100 11.39100  1.000 7.73194  ? 203 A1AOK B C4    1 
HETATM 5300 C  C40   . A1AOK G 5 .   ? 44.92100  -37.75200 4.71600   1.000 7.17198  ? 203 A1AOK B C40   1 
HETATM 5301 C  C41   . A1AOK G 5 .   ? 44.65100  -39.27000 4.78500   1.000 10.91975 ? 203 A1AOK B C41   1 
HETATM 5302 C  C42   . A1AOK G 5 .   ? 44.10300  -39.57400 6.17000   1.000 8.91988  ? 203 A1AOK B C42   1 
HETATM 5303 C  C43   . A1AOK G 5 .   ? 43.66700  -39.74200 3.71800   1.000 9.24141  ? 203 A1AOK B C43   1 
HETATM 5304 C  C44   . A1AOK G 5 .   ? 46.44300  -38.07200 2.75000   1.000 8.76782  ? 203 A1AOK B C44   1 
HETATM 5305 C  C45   . A1AOK G 5 .   ? 45.03400  -36.04500 3.02400   1.000 11.42896 ? 203 A1AOK B C45   1 
HETATM 5306 C  C46   . A1AOK G 5 .   ? 45.51700  -35.56600 1.67600   1.000 10.38405 ? 203 A1AOK B C46   1 
HETATM 5307 C  C47   . A1AOK G 5 .   ? 44.75100  -36.17200 0.48300   1.000 9.19116  ? 203 A1AOK B C47   1 
HETATM 5308 C  C48   . A1AOK G 5 .   ? 43.44500  -35.38800 0.55900   1.000 11.42329 ? 203 A1AOK B C48   1 
HETATM 5309 C  C49   . A1AOK G 5 .   ? 43.07600  -32.98600 1.03000   1.000 9.53114  ? 203 A1AOK B C49   1 
HETATM 5310 C  C5    . A1AOK G 5 .   ? 47.29400  -35.05800 12.21900  1.000 8.61043  ? 203 A1AOK B C5    1 
HETATM 5311 C  C50   . A1AOK G 5 .   ? 43.64300  -31.65600 1.46200   1.000 11.61558 ? 203 A1AOK B C50   1 
HETATM 5312 C  C51   . A1AOK G 5 .   ? 43.12600  -30.51600 0.60900   1.000 6.93535  ? 203 A1AOK B C51   1 
HETATM 5313 C  C52   . A1AOK G 5 .   ? 45.28500  -34.07500 1.43700   1.000 10.05083 ? 203 A1AOK B C52   1 
HETATM 5314 C  C6    . A1AOK G 5 .   ? 48.69400  -34.62700 11.83200  1.000 6.56355  ? 203 A1AOK B C6    1 
HETATM 5315 C  C7    . A1AOK G 5 .   ? 48.76300  -34.30400 10.34000  1.000 8.84995  ? 203 A1AOK B C7    1 
HETATM 5316 C  C8    . A1AOK G 5 .   ? 50.20300  -34.01300 9.96500   1.000 7.11982  ? 203 A1AOK B C8    1 
HETATM 5317 C  C9    . A1AOK G 5 .   ? 52.05500  -32.60500 10.39500  1.000 10.25653 ? 203 A1AOK B C9    1 
HETATM 5318 N  N1    . A1AOK G 5 .   ? 45.48100  -36.31700 6.63900   1.000 7.19983  ? 203 A1AOK B N1    1 
HETATM 5319 N  N2    . A1AOK G 5 .   ? 47.04800  -35.92300 9.95700   1.000 5.14905  ? 203 A1AOK B N2    1 
HETATM 5320 N  N3    . A1AOK G 5 .   ? 53.08700  -28.48100 7.60400   1.000 13.22366 ? 203 A1AOK B N3    1 
HETATM 5321 N  N4    . A1AOK G 5 .   ? 48.30000  -35.45100 9.57300   1.000 5.66034  ? 203 A1AOK B N4    1 
HETATM 5322 N  N5    . A1AOK G 5 .   ? 45.45400  -37.25300 3.43700   1.000 8.24187  ? 203 A1AOK B N5    1 
HETATM 5323 N  N6    . A1AOK G 5 .   ? 43.87500  -34.05400 1.00800   1.000 11.26813 ? 203 A1AOK B N6    1 
HETATM 5324 O  O1    . A1AOK G 5 .   ? 47.03100  -37.79700 5.90100   1.000 8.58234  ? 203 A1AOK B O1    1 
HETATM 5325 O  O2    . A1AOK G 5 .   ? 50.65300  -32.94200 10.60900  1.000 11.10337 ? 203 A1AOK B O2    1 
HETATM 5326 O  O3    . A1AOK G 5 .   ? 58.30600  -29.11900 9.91700   1.000 34.38281 ? 203 A1AOK B O3    1 
HETATM 5327 O  O4    . A1AOK G 5 .   ? 50.84200  -34.68300 9.20500   1.000 7.35894  ? 203 A1AOK B O4    1 
HETATM 5328 O  O5    . A1AOK G 5 .   ? 44.92600  -36.41600 9.36000   1.000 10.14822 ? 203 A1AOK B O5    1 
HETATM 5329 O  O6    . A1AOK G 5 .   ? 48.32100  -34.23700 2.96000   1.000 8.95287  ? 203 A1AOK B O6    1 
HETATM 5330 O  O7    . A1AOK G 5 .   ? 41.88900  -33.11400 0.72500   1.000 14.77791 ? 203 A1AOK B O7    1 
HETATM 5331 O  O8    . A1AOK G 5 .   ? 44.28500  -35.37200 3.73400   1.000 10.97006 ? 203 A1AOK B O8    1 
HETATM 5332 P  PG    . GNP   H 3 .   ? 79.43500  -18.95500 53.26400  1.000 8.06813  ? 201 GNP   A PG    1 
HETATM 5333 O  O1G   . GNP   H 3 .   ? 80.91900  -18.99900 53.13200  1.000 8.56676  ? 201 GNP   A O1G   1 
HETATM 5334 O  O2G   . GNP   H 3 .   ? 78.87700  -20.36700 52.99600  1.000 8.15151  ? 201 GNP   A O2G   1 
HETATM 5335 O  O3G   . GNP   H 3 .   ? 78.85200  -17.88300 52.31300  1.000 8.75360  ? 201 GNP   A O3G   1 
HETATM 5336 N  N3B   . GNP   H 3 .   ? 79.05200  -18.46100 54.86000  1.000 8.04742  ? 201 GNP   A N3B   1 
HETATM 5337 P  PB    . GNP   H 3 .   ? 79.80400  -19.06100 56.19100  1.000 8.97236  ? 201 GNP   A PB    1 
HETATM 5338 O  O1B   . GNP   H 3 .   ? 79.21600  -20.39300 56.57000  1.000 9.14727  ? 201 GNP   A O1B   1 
HETATM 5339 O  O2B   . GNP   H 3 .   ? 81.28800  -19.10900 56.00200  1.000 11.21613 ? 201 GNP   A O2B   1 
HETATM 5340 O  O3A   . GNP   H 3 .   ? 79.43500  -18.01500 57.39900  1.000 8.88327  ? 201 GNP   A O3A   1 
HETATM 5341 P  PA    . GNP   H 3 .   ? 80.37200  -16.84900 57.95500  1.000 9.62102  ? 201 GNP   A PA    1 
HETATM 5342 O  O1A   . GNP   H 3 .   ? 81.45700  -17.49300 58.81200  1.000 9.82804  ? 201 GNP   A O1A   1 
HETATM 5343 O  O2A   . GNP   H 3 .   ? 80.74400  -15.90700 56.85900  1.000 9.86168  ? 201 GNP   A O2A   1 
HETATM 5344 O  "O5'" . GNP   H 3 .   ? 79.36400  -16.10200 58.86700  1.000 11.83980 ? 201 GNP   A "O5'" 1 
HETATM 5345 C  "C5'" . GNP   H 3 .   ? 78.15700  -15.53200 58.32000  1.000 9.57700  ? 201 GNP   A "C5'" 1 
HETATM 5346 C  "C4'" . GNP   H 3 .   ? 77.62000  -14.52100 59.29800  1.000 10.18776 ? 201 GNP   A "C4'" 1 
HETATM 5347 O  "O4'" . GNP   H 3 .   ? 77.32900  -15.19300 60.54300  1.000 11.47055 ? 201 GNP   A "O4'" 1 
HETATM 5348 C  "C3'" . GNP   H 3 .   ? 78.56700  -13.36900 59.64600  1.000 10.85135 ? 201 GNP   A "C3'" 1 
HETATM 5349 O  "O3'" . GNP   H 3 .   ? 77.82500  -12.16400 59.79500  1.000 11.77858 ? 201 GNP   A "O3'" 1 
HETATM 5350 C  "C2'" . GNP   H 3 .   ? 79.21600  -13.84500 60.94900  1.000 10.86894 ? 201 GNP   A "C2'" 1 
HETATM 5351 O  "O2'" . GNP   H 3 .   ? 79.69600  -12.78700 61.78200  1.000 16.31085 ? 201 GNP   A "O2'" 1 
HETATM 5352 C  "C1'" . GNP   H 3 .   ? 78.04400  -14.57800 61.60200  1.000 13.11497 ? 201 GNP   A "C1'" 1 
HETATM 5353 N  N9    . GNP   H 3 .   ? 78.45700  -15.63100 62.54100  1.000 10.12631 ? 201 GNP   A N9    1 
HETATM 5354 C  C8    . GNP   H 3 .   ? 79.20900  -16.73800 62.28200  1.000 9.39746  ? 201 GNP   A C8    1 
HETATM 5355 N  N7    . GNP   H 3 .   ? 79.38500  -17.50100 63.33700  1.000 9.33152  ? 201 GNP   A N7    1 
HETATM 5356 C  C5    . GNP   H 3 .   ? 78.70000  -16.84300 64.34900  1.000 11.19217 ? 201 GNP   A C5    1 
HETATM 5357 C  C6    . GNP   H 3 .   ? 78.50700  -17.17200 65.74400  1.000 10.92084 ? 201 GNP   A C6    1 
HETATM 5358 O  O6    . GNP   H 3 .   ? 78.94200  -18.13700 66.35500  1.000 10.30105 ? 201 GNP   A O6    1 
HETATM 5359 N  N1    . GNP   H 3 .   ? 77.74000  -16.23000 66.39500  1.000 11.83808 ? 201 GNP   A N1    1 
HETATM 5360 C  C2    . GNP   H 3 .   ? 77.21200  -15.11000 65.81700  1.000 13.15600 ? 201 GNP   A C2    1 
HETATM 5361 N  N2    . GNP   H 3 .   ? 76.49500  -14.30500 66.60100  1.000 13.58645 ? 201 GNP   A N2    1 
HETATM 5362 N  N3    . GNP   H 3 .   ? 77.37500  -14.79900 64.53500  1.000 11.42712 ? 201 GNP   A N3    1 
HETATM 5363 C  C4    . GNP   H 3 .   ? 78.12400  -15.69700 63.87000  1.000 11.50176 ? 201 GNP   A C4    1 
HETATM 5364 MG MG    . MG    I 4 .   ? 82.54300  -18.64300 54.38100  1.000 10.05688 ? 202 MG    A MG    1 
HETATM 5365 C  C1    A A1AOK J 5 .   ? 76.06100  -13.21100 45.22300  1.000 8.59221  ? 203 A1AOK A C1    1 
HETATM 5366 C  C10   A A1AOK J 5 .   ? 82.52400  -19.16000 39.78500  1.000 11.29531 ? 203 A1AOK A C10   1 
HETATM 5367 C  C11   A A1AOK J 5 .   ? 84.03900  -19.37100 39.71500  1.000 10.19649 ? 203 A1AOK A C11   1 
HETATM 5368 C  C12   A A1AOK J 5 .   ? 81.99800  -19.00300 38.35700  1.000 15.01676 ? 203 A1AOK A C12   1 
HETATM 5369 C  C13   A A1AOK J 5 .   ? 81.80700  -20.36800 40.40600  1.000 9.21889  ? 203 A1AOK A C13   1 
HETATM 5370 C  C14   A A1AOK J 5 .   ? 82.21400  -20.86800 41.76100  1.000 9.54822  ? 203 A1AOK A C14   1 
HETATM 5371 C  C15   A A1AOK J 5 .   ? 83.14100  -21.85100 42.03100  1.000 11.57402 ? 203 A1AOK A C15   1 
HETATM 5372 C  C16   A A1AOK J 5 .   ? 83.97100  -22.60800 41.07300  1.000 13.65114 ? 203 A1AOK A C16   1 
HETATM 5373 C  C17   A A1AOK J 5 .   ? 85.34300  -22.32800 40.95200  1.000 15.52593 ? 203 A1AOK A C17   1 
HETATM 5374 C  C18   A A1AOK J 5 .   ? 85.99300  -21.24400 41.77900  0.500 13.95321 ? 203 A1AOK A C18   1 
HETATM 5375 C  C18   B A1AOK J 5 .   ? 86.12500  -21.20400 41.73500  0.500 13.98714 ? 203 A1AOK A C18   1 
HETATM 5376 C  C19   A A1AOK J 5 .   ? 87.47500  -21.40700 42.00400  0.500 17.24347 ? 203 A1AOK A C19   1 
HETATM 5377 C  C19   B A1AOK J 5 .   ? 87.62700  -21.13300 42.03800  0.500 17.25220 ? 203 A1AOK A C19   1 
HETATM 5378 C  C2    A A1AOK J 5 .   ? 76.47900  -14.85700 43.45200  1.000 8.68767  ? 203 A1AOK A C2    1 
HETATM 5379 C  C20   A A1AOK J 5 .   ? 88.44300  -22.08100 43.98800  0.500 18.27220 ? 203 A1AOK A C20   1 
HETATM 5380 C  C20   B A1AOK J 5 .   ? 88.73700  -20.05400 40.23600  0.500 14.57749 ? 203 A1AOK A C20   1 
HETATM 5381 C  C21   A A1AOK J 5 .   ? 86.08400  -23.07100 40.02900  1.000 16.88469 ? 203 A1AOK A C21   1 
HETATM 5382 C  C22   A A1AOK J 5 .   ? 85.50900  -24.06900 39.26600  1.000 21.89218 ? 203 A1AOK A C22   1 
HETATM 5383 C  C23   A A1AOK J 5 .   ? 84.16600  -24.33800 39.39000  1.000 19.03230 ? 203 A1AOK A C23   1 
HETATM 5384 C  C24   A A1AOK J 5 .   ? 83.40100  -23.61200 40.28100  1.000 13.94956 ? 203 A1AOK A C24   1 
HETATM 5385 C  C25   A A1AOK J 5 .   ? 84.04400  -23.02700 44.12300  1.000 11.38589 ? 203 A1AOK A C25   1 
HETATM 5386 C  C26   A A1AOK J 5 .   ? 83.32300  -24.33700 44.32600  1.000 10.59560 ? 203 A1AOK A C26   1 
HETATM 5387 C  C27   A A1AOK J 5 .   ? 76.45700  -16.39500 43.60900  1.000 6.78853  ? 203 A1AOK A C27   1 
HETATM 5388 C  C28   A A1AOK J 5 .   ? 77.49400  -16.88600 44.58900  1.000 8.81340  ? 203 A1AOK A C28   1 
HETATM 5389 C  C29   A A1AOK J 5 .   ? 78.42000  -17.86700 44.23700  1.000 9.05915  ? 203 A1AOK A C29   1 
HETATM 5390 C  C3    A A1AOK J 5 .   ? 76.16800  -14.48300 42.00900  1.000 7.37113  ? 203 A1AOK A C3    1 
HETATM 5391 C  C30   A A1AOK J 5 .   ? 79.37300  -18.34000 45.14300  1.000 8.08733  ? 203 A1AOK A C30   1 
HETATM 5392 C  C31   A A1AOK J 5 .   ? 80.36700  -19.36500 44.73500  1.000 7.66501  ? 203 A1AOK A C31   1 
HETATM 5393 C  C32   A A1AOK J 5 .   ? 80.70000  -19.52300 43.39800  1.000 10.55773 ? 203 A1AOK A C32   1 
HETATM 5394 C  C33   A A1AOK J 5 .   ? 81.66900  -20.46200 43.02300  1.000 8.71720  ? 203 A1AOK A C33   1 
HETATM 5395 C  C34   A A1AOK J 5 .   ? 82.30300  -21.22200 44.02500  1.000 9.06698  ? 203 A1AOK A C34   1 
HETATM 5396 C  C35   A A1AOK J 5 .   ? 81.99800  -21.06400 45.37500  1.000 9.89688  ? 203 A1AOK A C35   1 
HETATM 5397 C  C36   A A1AOK J 5 .   ? 81.03900  -20.13700 45.70900  1.000 8.51490  ? 203 A1AOK A C36   1 
HETATM 5398 C  C37   A A1AOK J 5 .   ? 79.42700  -17.76100 46.41800  1.000 9.00883  ? 203 A1AOK A C37   1 
HETATM 5399 C  C38   A A1AOK J 5 .   ? 78.52000  -16.77100 46.77100  1.000 11.23999 ? 203 A1AOK A C38   1 
HETATM 5400 C  C39   A A1AOK J 5 .   ? 77.55700  -16.34200 45.86300  1.000 7.88793  ? 203 A1AOK A C39   1 
HETATM 5401 C  C4    A A1AOK J 5 .   ? 77.03800  -14.19900 39.68700  1.000 6.38315  ? 203 A1AOK A C4    1 
HETATM 5402 C  C40   A A1AOK J 5 .   ? 75.07300  -12.68700 46.29700  1.000 8.71950  ? 203 A1AOK A C40   1 
HETATM 5403 C  C41   A A1AOK J 5 .   ? 74.82800  -11.15500 46.20000  1.000 9.49084  ? 203 A1AOK A C41   1 
HETATM 5404 C  C42   A A1AOK J 5 .   ? 73.91400  -10.68400 47.33000  1.000 10.81660 ? 203 A1AOK A C42   1 
HETATM 5405 C  C43   A A1AOK J 5 .   ? 74.24100  -10.76400 44.83800  1.000 10.32188 ? 203 A1AOK A C43   1 
HETATM 5406 C  C44   A A1AOK J 5 .   ? 76.60600  -12.43200 48.27100  1.000 9.72916  ? 203 A1AOK A C44   1 
HETATM 5407 C  C45   A A1AOK J 5 .   ? 75.14100  -14.39800 48.03500  1.000 11.21412 ? 203 A1AOK A C45   1 
HETATM 5408 C  C46   A A1AOK J 5 .   ? 75.67800  -14.89300 49.35600  1.000 8.87472  ? 203 A1AOK A C46   1 
HETATM 5409 C  C47   A A1AOK J 5 .   ? 74.93500  -14.33600 50.58500  1.000 9.80585  ? 203 A1AOK A C47   1 
HETATM 5410 C  C48   A A1AOK J 5 .   ? 73.62300  -15.08300 50.43500  1.000 14.36439 ? 203 A1AOK A C48   1 
HETATM 5411 C  C49   A A1AOK J 5 .   ? 73.23400  -17.48600 49.99600  1.000 14.82323 ? 203 A1AOK A C49   1 
HETATM 5412 C  C5    A A1AOK J 5 .   ? 77.46900  -15.37000 38.83600  1.000 7.91644  ? 203 A1AOK A C5    1 
HETATM 5413 C  C50   A A1AOK J 5 .   ? 73.76700  -18.79800 49.48800  1.000 10.60403 ? 203 A1AOK A C50   1 
HETATM 5414 C  C51   A A1AOK J 5 .   ? 73.38600  -19.96900 50.37100  1.000 13.84852 ? 203 A1AOK A C51   1 
HETATM 5415 C  C52   A A1AOK J 5 .   ? 75.44500  -16.39400 49.55200  1.000 10.52942 ? 203 A1AOK A C52   1 
HETATM 5416 C  C6    A A1AOK J 5 .   ? 78.87600  -15.78900 39.22200  1.000 6.78707  ? 203 A1AOK A C6    1 
HETATM 5417 C  C7    A A1AOK J 5 .   ? 78.94900  -16.14600 40.70400  1.000 8.23122  ? 203 A1AOK A C7    1 
HETATM 5418 C  C8    A A1AOK J 5 .   ? 80.38900  -16.47000 41.07200  1.000 10.98238 ? 203 A1AOK A C8    1 
HETATM 5419 C  C9    A A1AOK J 5 .   ? 82.22000  -17.90600 40.60700  1.000 8.83034  ? 203 A1AOK A C9    1 
HETATM 5420 N  N1    A A1AOK J 5 .   ? 75.61500  -14.18800 44.41400  1.000 6.66359  ? 203 A1AOK A N1    1 
HETATM 5421 N  N2    A A1AOK J 5 .   ? 77.20500  -14.56500 41.11100  1.000 8.51929  ? 203 A1AOK A N2    1 
HETATM 5422 N  N3    A A1AOK J 5 .   ? 83.20700  -22.06300 43.40900  1.000 10.09047 ? 203 A1AOK A N3    1 
HETATM 5423 N  N4    A A1AOK J 5 .   ? 78.47100  -15.02300 41.50200  1.000 9.21132  ? 203 A1AOK A N4    1 
HETATM 5424 N  N5    A A1AOK J 5 .   ? 75.57400  -13.20300 47.58300  1.000 9.92675  ? 203 A1AOK A N5    1 
HETATM 5425 N  N6    A A1AOK J 5 .   ? 74.04100  -16.42300 49.99500  1.000 12.09135 ? 203 A1AOK A N6    1 
HETATM 5426 O  O1    A A1AOK J 5 .   ? 77.22000  -12.77500 45.20400  1.000 8.27554  ? 203 A1AOK A O1    1 
HETATM 5427 O  O2    A A1AOK J 5 .   ? 80.81400  -17.55400 40.42800  1.000 9.64266  ? 203 A1AOK A O2    1 
HETATM 5428 O  O3    A A1AOK J 5 .   ? 87.68000  -22.49100 42.87400  0.500 16.74421 ? 203 A1AOK A O3    1 
HETATM 5429 O  O3    B A1AOK J 5 .   ? 88.50700  -21.25900 40.94000  0.500 17.82031 ? 203 A1AOK A O3    1 
HETATM 5430 O  O4    A A1AOK J 5 .   ? 81.04700  -15.82700 41.84400  1.000 8.06623  ? 203 A1AOK A O4    1 
HETATM 5431 O  O5    A A1AOK J 5 .   ? 75.05300  -14.12500 41.65700  1.000 9.10637  ? 203 A1AOK A O5    1 
HETATM 5432 O  O6    A A1AOK J 5 .   ? 78.55500  -16.20800 48.01800  1.000 7.72283  ? 203 A1AOK A O6    1 
HETATM 5433 O  O7    A A1AOK J 5 .   ? 72.08200  -17.37300 50.38300  1.000 12.14759 ? 203 A1AOK A O7    1 
HETATM 5434 O  O8    A A1AOK J 5 .   ? 74.35200  -15.06300 47.37000  1.000 9.93625  ? 203 A1AOK A O8    1 
HETATM 5435 O  O     . HOH   K 6 .   ? 34.45300  -17.46000 -12.85500 1.000 37.20955 ? 301 HOH   B O     1 
HETATM 5436 O  O     . HOH   K 6 .   ? 64.30100  -3.04500  -19.13700 1.000 28.07742 ? 302 HOH   B O     1 
HETATM 5437 O  O     . HOH   K 6 .   ? 65.565    -0.354    -11.757   1.000 27.91710 ? 303 HOH   B O     1 
HETATM 5438 O  O     . HOH   K 6 .   ? 50.83900  -12.47500 8.30900   1.000 19.59181 ? 304 HOH   B O     1 
HETATM 5439 O  O     . HOH   K 6 .   ? 47.46500  -39.11300 -12.43000 1.000 20.45405 ? 305 HOH   B O     1 
HETATM 5440 O  O     . HOH   K 6 .   ? 52.87700  -22.47900 -22.84500 1.000 31.30418 ? 306 HOH   B O     1 
HETATM 5441 O  O     . HOH   K 6 .   ? 53.971    -0.431    2.421     1.000 16.12381 ? 307 HOH   B O     1 
HETATM 5442 O  O     . HOH   K 6 .   ? 54.35100  -37.08400 1.55500   1.000 20.37703 ? 308 HOH   B O     1 
HETATM 5443 O  O     . HOH   K 6 .   ? 52.94000  -29.71400 -3.18900  1.000 8.70883  ? 309 HOH   B O     1 
HETATM 5444 O  O     . HOH   K 6 .   ? 38.79100  -31.47300 -20.74800 1.000 21.12867 ? 310 HOH   B O     1 
HETATM 5445 O  O     . HOH   K 6 .   ? 69.50400  -10.35700 -7.65600  1.000 25.45274 ? 311 HOH   B O     1 
HETATM 5446 O  O     . HOH   K 6 .   ? 45.29500  -1.99100  -6.76400  1.000 33.74624 ? 312 HOH   B O     1 
HETATM 5447 O  O     . HOH   K 6 .   ? 62.36800  -18.71300 -23.07900 1.000 23.15105 ? 313 HOH   B O     1 
HETATM 5448 O  O     . HOH   K 6 .   ? 74.32600  -15.33700 -16.70900 1.000 30.39990 ? 314 HOH   B O     1 
HETATM 5449 O  O     . HOH   K 6 .   ? 56.16800  -6.60000  -3.90300  1.000 31.32497 ? 315 HOH   B O     1 
HETATM 5450 O  O     . HOH   K 6 .   ? 66.71200  -12.65300 -6.64900  1.000 15.72869 ? 316 HOH   B O     1 
HETATM 5451 O  O     . HOH   K 6 .   ? 45.31500  -19.07100 -22.50000 1.000 23.07475 ? 317 HOH   B O     1 
HETATM 5452 O  O     . HOH   K 6 .   ? 54.07700  -42.12600 -15.40800 1.000 34.02988 ? 318 HOH   B O     1 
HETATM 5453 O  O     . HOH   K 6 .   ? 51.98900  -37.85000 -8.90900  1.000 22.77176 ? 319 HOH   B O     1 
HETATM 5454 O  O     . HOH   K 6 .   ? 44.31900  -8.58200  -6.61300  1.000 28.05446 ? 320 HOH   B O     1 
HETATM 5455 O  O     . HOH   K 6 .   ? 40.03400  -34.54600 -0.24400  1.000 26.59732 ? 321 HOH   B O     1 
HETATM 5456 O  O     . HOH   K 6 .   ? 74.32800  -25.66700 -10.58100 1.000 25.57817 ? 322 HOH   B O     1 
HETATM 5457 O  O     . HOH   K 6 .   ? 54.59000  -7.29100  5.64100   1.000 10.81025 ? 323 HOH   B O     1 
HETATM 5458 O  O     . HOH   K 6 .   ? 57.59900  -32.47900 -4.09000  1.000 17.48684 ? 324 HOH   B O     1 
HETATM 5459 O  O     . HOH   K 6 .   ? 62.47000  -32.54500 -0.45600  1.000 20.31581 ? 325 HOH   B O     1 
HETATM 5460 O  O     . HOH   K 6 .   ? 71.67200  -14.58400 -14.47600 1.000 22.18763 ? 326 HOH   B O     1 
HETATM 5461 O  O     . HOH   K 6 .   ? 56.61400  -33.46000 1.60500   1.000 11.18963 ? 327 HOH   B O     1 
HETATM 5462 O  O     . HOH   K 6 .   ? 75.19900  -21.35500 -18.03100 1.000 32.66704 ? 328 HOH   B O     1 
HETATM 5463 O  O     . HOH   K 6 .   ? 45.69800  -37.54500 -20.02600 1.000 22.69592 ? 329 HOH   B O     1 
HETATM 5464 O  O     . HOH   K 6 .   ? 59.18100  -3.42900  -14.79600 1.000 29.71910 ? 330 HOH   B O     1 
HETATM 5465 O  O     . HOH   K 6 .   ? 35.64000  -31.58600 -10.61200 1.000 8.71152  ? 331 HOH   B O     1 
HETATM 5466 O  O     . HOH   K 6 .   ? 55.04700  -16.38700 10.38600  1.000 18.83754 ? 332 HOH   B O     1 
HETATM 5467 O  O     . HOH   K 6 .   ? 37.23300  -20.97100 -2.57000  1.000 26.97978 ? 333 HOH   B O     1 
HETATM 5468 O  O     . HOH   K 6 .   ? 39.61900  -36.63500 -15.66800 1.000 31.14666 ? 334 HOH   B O     1 
HETATM 5469 O  O     . HOH   K 6 .   ? 43.16700  -24.20300 -0.79200  1.000 17.40237 ? 335 HOH   B O     1 
HETATM 5470 O  O     . HOH   K 6 .   ? 55.99300  -33.72800 -1.99900  1.000 18.18233 ? 336 HOH   B O     1 
HETATM 5471 O  O     . HOH   K 6 .   ? 51.84500  -41.93100 -2.43000  1.000 19.56996 ? 337 HOH   B O     1 
HETATM 5472 O  O     . HOH   K 6 .   ? 50.877    -0.920    4.813     1.000 11.03540 ? 338 HOH   B O     1 
HETATM 5473 O  O     . HOH   K 6 .   ? 73.84500  -11.88900 -9.49500  1.000 17.54536 ? 339 HOH   B O     1 
HETATM 5474 O  O     . HOH   K 6 .   ? 37.48400  -14.75900 -14.37100 1.000 19.45558 ? 340 HOH   B O     1 
HETATM 5475 O  O     . HOH   K 6 .   ? 50.96400  -23.78600 -22.46800 1.000 29.17000 ? 341 HOH   B O     1 
HETATM 5476 O  O     . HOH   K 6 .   ? 62.73600  -16.13700 -24.35200 1.000 14.73568 ? 342 HOH   B O     1 
HETATM 5477 O  O     . HOH   K 6 .   ? 51.93200  -33.77900 -3.71900  1.000 10.13036 ? 343 HOH   B O     1 
HETATM 5478 O  O     . HOH   K 6 .   ? 52.27100  -36.66000 -6.10500  1.000 11.16772 ? 344 HOH   B O     1 
HETATM 5479 O  O     . HOH   K 6 .   ? 48.13200  -22.28900 4.23000   1.000 27.72693 ? 345 HOH   B O     1 
HETATM 5480 O  O     . HOH   K 6 .   ? 51.47200  -25.41200 2.96000   1.000 14.64203 ? 346 HOH   B O     1 
HETATM 5481 O  O     . HOH   K 6 .   ? 62.51900  -12.71100 -0.73300  1.000 25.84796 ? 347 HOH   B O     1 
HETATM 5482 O  O     . HOH   K 6 .   ? 67.20000  -15.33700 -3.88300  1.000 18.91942 ? 348 HOH   B O     1 
HETATM 5483 O  O     . HOH   K 6 .   ? 39.71900  -12.00100 -7.76600  1.000 24.87805 ? 349 HOH   B O     1 
HETATM 5484 O  O     . HOH   K 6 .   ? 49.25700  -32.36200 1.30300   1.000 8.01008  ? 350 HOH   B O     1 
HETATM 5485 O  O     . HOH   K 6 .   ? 53.54900  -11.16300 -12.05200 1.000 10.95635 ? 351 HOH   B O     1 
HETATM 5486 O  O     . HOH   K 6 .   ? 48.59700  -31.70900 -22.31500 1.000 28.23620 ? 352 HOH   B O     1 
HETATM 5487 O  O     . HOH   K 6 .   ? 38.57500  -13.58300 0.28100   1.000 27.36872 ? 353 HOH   B O     1 
HETATM 5488 O  O     . HOH   K 6 .   ? 52.26600  -40.38000 1.03000   1.000 15.30532 ? 354 HOH   B O     1 
HETATM 5489 O  O     . HOH   K 6 .   ? 54.01700  -26.74200 3.15100   1.000 8.30377  ? 355 HOH   B O     1 
HETATM 5490 O  O     . HOH   K 6 .   ? 34.18700  -30.10500 -20.15300 1.000 19.39193 ? 356 HOH   B O     1 
HETATM 5491 O  O     . HOH   K 6 .   ? 66.85800  -22.51400 -21.71600 1.000 32.88994 ? 357 HOH   B O     1 
HETATM 5492 O  O     . HOH   K 6 .   ? 44.38800  -12.24900 3.50400   1.000 28.81152 ? 358 HOH   B O     1 
HETATM 5493 O  O     . HOH   K 6 .   ? 40.89100  -10.61500 -4.75600  1.000 24.71651 ? 359 HOH   B O     1 
HETATM 5494 O  O     . HOH   K 6 .   ? 59.79000  -10.38400 -5.29500  1.000 18.98727 ? 360 HOH   B O     1 
HETATM 5495 O  O     . HOH   K 6 .   ? 65.61300  -7.09500  -13.73400 1.000 18.78715 ? 361 HOH   B O     1 
HETATM 5496 O  O     . HOH   K 6 .   ? 65.91800  -31.49800 -3.22900  1.000 23.90694 ? 362 HOH   B O     1 
HETATM 5497 O  O     . HOH   K 6 .   ? 52.63900  -9.30100  -15.84300 1.000 28.50802 ? 363 HOH   B O     1 
HETATM 5498 O  O     . HOH   K 6 .   ? 53.74400  -13.13900 10.45400  1.000 27.52845 ? 364 HOH   B O     1 
HETATM 5499 O  O     . HOH   K 6 .   ? 61.61500  -28.22900 2.15800   1.000 20.27472 ? 365 HOH   B O     1 
HETATM 5500 O  O     . HOH   K 6 .   ? 61.24600  -30.84800 3.58500   1.000 25.40651 ? 366 HOH   B O     1 
HETATM 5501 O  O     . HOH   K 6 .   ? 45.37000  -38.32300 -14.48000 1.000 23.02640 ? 367 HOH   B O     1 
HETATM 5502 O  O     . HOH   K 6 .   ? 74.34400  -17.39300 -19.18100 1.000 26.60898 ? 368 HOH   B O     1 
HETATM 5503 O  O     . HOH   K 6 .   ? 44.92800  -25.46100 12.34100  1.000 34.63353 ? 369 HOH   B O     1 
HETATM 5504 O  O     . HOH   K 6 .   ? 44.06600  -33.66200 -2.47400  1.000 14.20207 ? 370 HOH   B O     1 
HETATM 5505 O  O     . HOH   K 6 .   ? 56.38300  -8.58700  -12.78900 1.000 16.42425 ? 371 HOH   B O     1 
HETATM 5506 O  O     . HOH   K 6 .   ? 61.63200  -3.05800  -7.69400  1.000 30.42826 ? 372 HOH   B O     1 
HETATM 5507 O  O     . HOH   K 6 .   ? 60.76500  -35.48700 -3.76800  1.000 22.70291 ? 373 HOH   B O     1 
HETATM 5508 O  O     . HOH   K 6 .   ? 68.16000  -18.22200 -23.67600 1.000 19.82757 ? 374 HOH   B O     1 
HETATM 5509 O  O     . HOH   K 6 .   ? 55.10500  -16.95300 -21.26200 1.000 18.71077 ? 375 HOH   B O     1 
HETATM 5510 O  O     . HOH   K 6 .   ? 47.54400  -24.10900 0.57300   1.000 13.19533 ? 376 HOH   B O     1 
HETATM 5511 O  O     . HOH   K 6 .   ? 45.83700  -26.21700 -23.38700 1.000 32.11102 ? 377 HOH   B O     1 
HETATM 5512 O  O     . HOH   K 6 .   ? 64.19500  -26.11600 -16.85200 1.000 27.02435 ? 378 HOH   B O     1 
HETATM 5513 O  O     . HOH   K 6 .   ? 49.91000  -23.83900 -0.97800  1.000 10.96488 ? 379 HOH   B O     1 
HETATM 5514 O  O     . HOH   K 6 .   ? 64.67500  -12.29900 -18.71600 1.000 18.95252 ? 380 HOH   B O     1 
HETATM 5515 O  O     . HOH   K 6 .   ? 47.12100  -11.57100 -18.42900 1.000 26.38588 ? 381 HOH   B O     1 
HETATM 5516 O  O     . HOH   K 6 .   ? 47.01300  -40.24500 -16.26200 1.000 35.28840 ? 382 HOH   B O     1 
HETATM 5517 O  O     . HOH   K 6 .   ? 50.64800  -8.53800  -6.83200  1.000 25.93703 ? 383 HOH   B O     1 
HETATM 5518 O  O     . HOH   K 6 .   ? 57.53500  -39.34400 -3.82700  1.000 24.70878 ? 384 HOH   B O     1 
HETATM 5519 O  O     . HOH   K 6 .   ? 42.03700  -36.31000 -22.51200 1.000 23.75939 ? 385 HOH   B O     1 
HETATM 5520 O  O     . HOH   K 6 .   ? 34.55700  -32.81400 -21.60800 1.000 17.56577 ? 386 HOH   B O     1 
HETATM 5521 O  O     . HOH   K 6 .   ? 67.94000  -30.42300 -9.77500  1.000 23.98541 ? 387 HOH   B O     1 
HETATM 5522 O  O     . HOH   K 6 .   ? 55.51300  -7.93900  -10.17000 1.000 25.22435 ? 388 HOH   B O     1 
HETATM 5523 O  O     . HOH   K 6 .   ? 47.05700  -21.42400 11.62700  1.000 30.57828 ? 389 HOH   B O     1 
HETATM 5524 O  O     . HOH   K 6 .   ? 41.87900  -32.36700 -10.23600 1.000 12.20597 ? 390 HOH   B O     1 
HETATM 5525 O  O     . HOH   K 6 .   ? 41.98800  -35.42900 -12.16100 1.000 17.42824 ? 391 HOH   B O     1 
HETATM 5526 O  O     . HOH   K 6 .   ? 63.01400  -30.75800 0.82500   1.000 31.32703 ? 392 HOH   B O     1 
HETATM 5527 O  O     . HOH   K 6 .   ? 45.07000  -13.37900 -19.70300 1.000 22.12960 ? 393 HOH   B O     1 
HETATM 5528 O  O     . HOH   K 6 .   ? 55.75500  -35.13700 -12.19700 1.000 14.66752 ? 394 HOH   B O     1 
HETATM 5529 O  O     . HOH   K 6 .   ? 31.99900  -26.36200 -12.44700 1.000 20.23709 ? 395 HOH   B O     1 
HETATM 5530 O  O     . HOH   K 6 .   ? 39.52700  -9.31900  -17.21600 1.000 26.04294 ? 396 HOH   B O     1 
HETATM 5531 O  O     . HOH   K 6 .   ? 44.24900  -23.63200 -6.21200  1.000 13.62601 ? 397 HOH   B O     1 
HETATM 5532 O  O     . HOH   K 6 .   ? 70.16100  -28.19900 -15.08100 1.000 29.77693 ? 398 HOH   B O     1 
HETATM 5533 O  O     . HOH   K 6 .   ? 43.71500  -32.96100 5.05000   1.000 11.35674 ? 399 HOH   B O     1 
HETATM 5534 O  O     . HOH   K 6 .   ? 39.49200  -29.10300 -22.25700 1.000 26.48654 ? 400 HOH   B O     1 
HETATM 5535 O  O     . HOH   K 6 .   ? 41.38400  -29.33400 -3.72800  1.000 13.13127 ? 401 HOH   B O     1 
HETATM 5536 O  O     . HOH   K 6 .   ? 54.579    -10.416   7.517     1.000 24.40951 ? 402 HOH   B O     1 
HETATM 5537 O  O     . HOH   K 6 .   ? 46.88900  -31.07000 9.88400   1.000 6.08679  ? 403 HOH   B O     1 
HETATM 5538 O  O     . HOH   K 6 .   ? 58.77100  -19.24000 -21.09900 1.000 18.52770 ? 404 HOH   B O     1 
HETATM 5539 O  O     . HOH   K 6 .   ? 62.06800  -24.69200 -22.19300 1.000 29.23308 ? 405 HOH   B O     1 
HETATM 5540 O  O     . HOH   K 6 .   ? 57.74000  -27.60400 -20.60100 1.000 18.07265 ? 406 HOH   B O     1 
HETATM 5541 O  O     . HOH   K 6 .   ? 56.47400  -36.60200 -19.41000 1.000 25.21806 ? 407 HOH   B O     1 
HETATM 5542 O  O     . HOH   K 6 .   ? 49.384    -5.843    4.520     1.000 15.27289 ? 408 HOH   B O     1 
HETATM 5543 O  O     . HOH   K 6 .   ? 35.90300  -33.06600 -13.67100 1.000 18.48330 ? 409 HOH   B O     1 
HETATM 5544 O  O     . HOH   K 6 .   ? 56.59800  -12.54400 -18.57400 1.000 22.68124 ? 410 HOH   B O     1 
HETATM 5545 O  O     . HOH   K 6 .   ? 73.48100  -20.62500 -3.78700  1.000 17.59519 ? 411 HOH   B O     1 
HETATM 5546 O  O     . HOH   K 6 .   ? 63.30800  -10.09300 -6.01500  1.000 26.52088 ? 412 HOH   B O     1 
HETATM 5547 O  O     . HOH   K 6 .   ? 47.23200  -30.99100 2.40600   1.000 15.12023 ? 413 HOH   B O     1 
HETATM 5548 O  O     . HOH   K 6 .   ? 45.145    -14.913   7.202     1.000 33.71541 ? 414 HOH   B O     1 
HETATM 5549 O  O     . HOH   K 6 .   ? 58.15600  -10.02400 1.99000   1.000 24.84921 ? 415 HOH   B O     1 
HETATM 5550 O  O     . HOH   K 6 .   ? 68.08300  -16.65200 -2.17800  1.000 28.58177 ? 416 HOH   B O     1 
HETATM 5551 O  O     . HOH   K 6 .   ? 43.99600  -22.48200 -25.28500 1.000 37.92599 ? 417 HOH   B O     1 
HETATM 5552 O  O     . HOH   K 6 .   ? 39.61500  -17.06300 -7.50800  1.000 13.16658 ? 418 HOH   B O     1 
HETATM 5553 O  O     . HOH   K 6 .   ? 45.27000  -8.44800  0.68800   1.000 14.41914 ? 419 HOH   B O     1 
HETATM 5554 O  O     . HOH   K 6 .   ? 59.73000  -18.98500 0.84300   1.000 18.28796 ? 420 HOH   B O     1 
HETATM 5555 O  O     . HOH   K 6 .   ? 59.60100  -36.09300 -19.19000 1.000 34.35933 ? 421 HOH   B O     1 
HETATM 5556 O  O     . HOH   K 6 .   ? 42.39600  -28.78100 -22.38100 1.000 31.89069 ? 422 HOH   B O     1 
HETATM 5557 O  O     . HOH   K 6 .   ? 40.96600  -27.94700 -1.28800  1.000 19.40473 ? 423 HOH   B O     1 
HETATM 5558 O  O     . HOH   K 6 .   ? 62.59900  -11.33000 -21.63600 1.000 14.42028 ? 424 HOH   B O     1 
HETATM 5559 O  O     . HOH   K 6 .   ? 42.43700  -30.83000 -8.21300  1.000 17.26071 ? 425 HOH   B O     1 
HETATM 5560 O  O     . HOH   K 6 .   ? 53.60000  -6.89400  -17.32900 1.000 32.63601 ? 426 HOH   B O     1 
HETATM 5561 O  O     . HOH   K 6 .   ? 65.15800  -24.70500 -2.64200  1.000 15.43020 ? 427 HOH   B O     1 
HETATM 5562 O  O     . HOH   K 6 .   ? 65.10600  -18.81300 -22.51100 1.000 18.54105 ? 428 HOH   B O     1 
HETATM 5563 O  O     . HOH   K 6 .   ? 55.38700  -26.98000 -23.61200 1.000 27.24551 ? 429 HOH   B O     1 
HETATM 5564 O  O     . HOH   K 6 .   ? 42.63700  -17.00100 2.52100   1.000 32.96143 ? 430 HOH   B O     1 
HETATM 5565 O  O     . HOH   K 6 .   ? 34.93400  -29.12900 -9.91100  1.000 17.01262 ? 431 HOH   B O     1 
HETATM 5566 O  O     . HOH   K 6 .   ? 52.42000  -1.65700  -3.37000  1.000 26.10316 ? 432 HOH   B O     1 
HETATM 5567 O  O     . HOH   K 6 .   ? 42.42000  -24.37900 -23.81700 1.000 32.67045 ? 433 HOH   B O     1 
HETATM 5568 O  O     . HOH   K 6 .   ? 45.25600  -39.50100 -7.91000  1.000 28.59908 ? 434 HOH   B O     1 
HETATM 5569 O  O     . HOH   K 6 .   ? 37.68800  -23.34200 -22.13400 1.000 28.38255 ? 435 HOH   B O     1 
HETATM 5570 O  O     . HOH   K 6 .   ? 51.00100  -8.88300  -9.00700  1.000 30.02287 ? 436 HOH   B O     1 
HETATM 5571 O  O     . HOH   K 6 .   ? 50.22600  -21.27400 12.41600  1.000 33.65681 ? 437 HOH   B O     1 
HETATM 5572 O  O     . HOH   K 6 .   ? 36.15500  -18.20500 -2.38000  1.000 26.86368 ? 438 HOH   B O     1 
HETATM 5573 O  O     . HOH   K 6 .   ? 53.55400  -0.96400  -11.50000 1.000 42.17666 ? 439 HOH   B O     1 
HETATM 5574 O  O     . HOH   K 6 .   ? 50.70300  -16.10700 -21.18400 1.000 31.95297 ? 440 HOH   B O     1 
HETATM 5575 O  O     . HOH   K 6 .   ? 46.43000  -6.95100  -17.55900 1.000 25.69330 ? 441 HOH   B O     1 
HETATM 5576 O  O     . HOH   K 6 .   ? 65.14400  -38.36000 -13.16800 1.000 31.58163 ? 442 HOH   B O     1 
HETATM 5577 O  O     . HOH   K 6 .   ? 35.27500  -28.28700 -7.16100  1.000 17.33689 ? 443 HOH   B O     1 
HETATM 5578 O  O     . HOH   K 6 .   ? 44.30100  -17.42900 9.10800   1.000 39.13319 ? 444 HOH   B O     1 
HETATM 5579 O  O     . HOH   K 6 .   ? 47.57400  -42.45100 -5.72300  1.000 25.56680 ? 445 HOH   B O     1 
HETATM 5580 O  O     . HOH   K 6 .   ? 70.43500  -13.26700 -7.36700  1.000 20.86805 ? 446 HOH   B O     1 
HETATM 5581 O  O     . HOH   K 6 .   ? 60.27100  -37.78800 -7.03300  1.000 28.80498 ? 447 HOH   B O     1 
HETATM 5582 O  O     . HOH   K 6 .   ? 34.91700  -21.69100 -3.14300  1.000 28.95798 ? 448 HOH   B O     1 
HETATM 5583 O  O     . HOH   K 6 .   ? 56.78400  -25.02300 -21.59500 1.000 17.94286 ? 449 HOH   B O     1 
HETATM 5584 O  O     . HOH   K 6 .   ? 67.25900  -30.34100 -5.61900  1.000 19.31654 ? 450 HOH   B O     1 
HETATM 5585 O  O     . HOH   K 6 .   ? 57.11500  -14.98300 -20.32500 1.000 14.72062 ? 451 HOH   B O     1 
HETATM 5586 O  O     . HOH   K 6 .   ? 32.29700  -24.83600 -5.42200  1.000 31.27934 ? 452 HOH   B O     1 
HETATM 5587 O  O     . HOH   K 6 .   ? 55.04000  -37.02000 -10.53300 1.000 20.77169 ? 453 HOH   B O     1 
HETATM 5588 O  O     . HOH   K 6 .   ? 71.07600  -28.12300 -11.09600 1.000 15.29300 ? 454 HOH   B O     1 
HETATM 5589 O  O     . HOH   K 6 .   ? 37.31300  -20.74100 -22.82600 1.000 29.65639 ? 455 HOH   B O     1 
HETATM 5590 O  O     . HOH   K 6 .   ? 43.28700  -34.88600 -7.85800  1.000 25.56831 ? 456 HOH   B O     1 
HETATM 5591 O  O     . HOH   K 6 .   ? 49.06700  -14.69300 -20.34100 1.000 25.39093 ? 457 HOH   B O     1 
HETATM 5592 O  O     . HOH   K 6 .   ? 44.85700  -36.28100 -11.80600 1.000 20.66741 ? 458 HOH   B O     1 
HETATM 5593 O  O     . HOH   K 6 .   ? 40.96400  -28.09400 9.64500   1.000 30.85498 ? 459 HOH   B O     1 
HETATM 5594 O  O     . HOH   K 6 .   ? 66.46500  -10.66200 -18.57300 1.000 24.82686 ? 460 HOH   B O     1 
HETATM 5595 O  O     . HOH   K 6 .   ? 46.41900  -21.16100 6.50100   1.000 30.76298 ? 461 HOH   B O     1 
HETATM 5596 O  O     . HOH   K 6 .   ? 52.82400  -15.19900 10.85500  1.000 24.92604 ? 462 HOH   B O     1 
HETATM 5597 O  O     . HOH   K 6 .   ? 52.45600  -44.21600 -10.18100 1.000 33.70711 ? 463 HOH   B O     1 
HETATM 5598 O  O     . HOH   K 6 .   ? 58.46600  -35.96600 -0.23200  1.000 29.20544 ? 464 HOH   B O     1 
HETATM 5599 O  O     . HOH   K 6 .   ? 76.26800  -10.51700 -9.60100  1.000 29.06614 ? 465 HOH   B O     1 
HETATM 5600 O  O     . HOH   K 6 .   ? 46.34900  -30.06100 7.21000   1.000 18.02973 ? 466 HOH   B O     1 
HETATM 5601 O  O     . HOH   K 6 .   ? 53.94600  -1.59400  -1.46600  1.000 29.90146 ? 467 HOH   B O     1 
HETATM 5602 O  O     . HOH   K 6 .   ? 43.33600  -27.04500 -0.30800  1.000 10.78763 ? 468 HOH   B O     1 
HETATM 5603 O  O     . HOH   K 6 .   ? 39.32700  -10.37100 -10.06900 1.000 34.90241 ? 469 HOH   B O     1 
HETATM 5604 O  O     . HOH   K 6 .   ? 67.89400  -24.38800 -19.05100 1.000 28.85942 ? 470 HOH   B O     1 
HETATM 5605 O  O     . HOH   K 6 .   ? 45.72700  -18.98900 12.05500  1.000 30.40908 ? 471 HOH   B O     1 
HETATM 5606 O  O     . HOH   K 6 .   ? 42.25300  -14.14500 2.04400   1.000 31.16178 ? 472 HOH   B O     1 
HETATM 5607 O  O     . HOH   K 6 .   ? 52.63400  -43.53700 -13.68600 1.000 37.22435 ? 473 HOH   B O     1 
HETATM 5608 O  O     . HOH   K 6 .   ? 62.54600  -10.39200 -17.45000 1.000 18.87084 ? 474 HOH   B O     1 
HETATM 5609 O  O     . HOH   K 6 .   ? 43.70900  -29.18100 4.18900   1.000 13.33384 ? 475 HOH   B O     1 
HETATM 5610 O  O     . HOH   K 6 .   ? 64.61400  -38.44800 -10.42800 1.000 35.03817 ? 476 HOH   B O     1 
HETATM 5611 O  O     . HOH   K 6 .   ? 49.57100  -21.02200 -22.27400 1.000 17.80876 ? 477 HOH   B O     1 
HETATM 5612 O  O     . HOH   K 6 .   ? 54.21700  -46.03900 -2.50800  1.000 29.51553 ? 478 HOH   B O     1 
HETATM 5613 O  O     . HOH   K 6 .   ? 65.483    -33.905   -6.148    1.000 32.91579 ? 479 HOH   B O     1 
HETATM 5614 O  O     . HOH   K 6 .   ? 44.84000  -38.17600 -10.20200 1.000 23.59415 ? 480 HOH   B O     1 
HETATM 5615 O  O     . HOH   K 6 .   ? 63.35800  -23.65800 -1.06500  1.000 26.56213 ? 481 HOH   B O     1 
HETATM 5616 O  O     . HOH   K 6 .   ? 47.71800  -21.55700 2.18700   1.000 26.18229 ? 482 HOH   B O     1 
HETATM 5617 O  O     . HOH   K 6 .   ? 51.72400  -22.79100 11.32800  1.000 23.11257 ? 483 HOH   B O     1 
HETATM 5618 O  O     . HOH   K 6 .   ? 34.99000  -14.54400 -16.79500 1.000 27.95992 ? 484 HOH   B O     1 
HETATM 5619 O  O     . HOH   K 6 .   ? 37.844    -9.143    -19.610   1.000 38.35415 ? 485 HOH   B O     1 
HETATM 5620 O  O     . HOH   K 6 .   ? 50.15600  -44.95200 -16.72900 1.000 36.51767 ? 486 HOH   B O     1 
HETATM 5621 O  O     . HOH   K 6 .   ? 43.51200  -8.33200  -2.32000  1.000 34.23452 ? 487 HOH   B O     1 
HETATM 5622 O  O     . HOH   K 6 .   ? 37.97600  -11.86600 -14.08900 1.000 26.73249 ? 488 HOH   B O     1 
HETATM 5623 O  O     . HOH   K 6 .   ? 57.26300  -8.65800  3.79000   1.000 30.82784 ? 489 HOH   B O     1 
HETATM 5624 O  O     . HOH   K 6 .   ? 51.07900  -7.37300  -10.67000 1.000 33.23324 ? 490 HOH   B O     1 
HETATM 5625 O  O     . HOH   K 6 .   ? 63.25100  -36.33500 -4.52500  1.000 26.59527 ? 491 HOH   B O     1 
HETATM 5626 O  O     . HOH   K 6 .   ? 50.89300  -22.56200 3.03900   1.000 22.63019 ? 492 HOH   B O     1 
HETATM 5627 O  O     . HOH   K 6 .   ? 63.63100  -3.54500  -6.71100  1.000 35.93098 ? 493 HOH   B O     1 
HETATM 5628 O  O     . HOH   K 6 .   ? 62.738    0.859     -15.116   1.000 34.82153 ? 494 HOH   B O     1 
HETATM 5629 O  O     . HOH   K 6 .   ? 58.29100  -1.32900  -15.04100 1.000 37.71090 ? 495 HOH   B O     1 
HETATM 5630 O  O     . HOH   K 6 .   ? 39.15100  -32.75700 -9.05200  1.000 24.83110 ? 496 HOH   B O     1 
HETATM 5631 O  O     . HOH   K 6 .   ? 40.63100  -26.77200 3.15400   1.000 32.09536 ? 497 HOH   B O     1 
HETATM 5632 O  O     . HOH   K 6 .   ? 43.43900  -38.15700 -21.21000 1.000 29.76517 ? 498 HOH   B O     1 
HETATM 5633 O  O     . HOH   K 6 .   ? 52.83000  -8.98500  -11.10400 1.000 28.70100 ? 499 HOH   B O     1 
HETATM 5634 O  O     . HOH   K 6 .   ? 73.43400  -13.48800 -23.10400 1.000 33.15376 ? 500 HOH   B O     1 
HETATM 5635 O  O     . HOH   K 6 .   ? 74.273    -12.991   -17.096   1.000 33.82244 ? 501 HOH   B O     1 
HETATM 5636 O  O     . HOH   K 6 .   ? 66.23200  -7.14500  -16.09400 1.000 29.76456 ? 502 HOH   B O     1 
HETATM 5637 O  O     . HOH   K 6 .   ? 61.038    -12.315   7.111     1.000 23.72189 ? 503 HOH   B O     1 
HETATM 5638 O  O     . HOH   K 6 .   ? 43.08500  -27.27600 2.37500   1.000 17.86635 ? 504 HOH   B O     1 
HETATM 5639 O  O     . HOH   K 6 .   ? 40.72000  -6.88600  -16.65300 1.000 28.98177 ? 505 HOH   B O     1 
HETATM 5640 O  O     . HOH   K 6 .   ? 55.65900  -43.81700 -14.45200 1.000 43.20539 ? 506 HOH   B O     1 
HETATM 5641 O  O     . HOH   K 6 .   ? 47.42200  -37.53300 -21.77500 1.000 30.23908 ? 507 HOH   B O     1 
HETATM 5642 O  O     . HOH   K 6 .   ? 41.949    -14.673   6.756     1.000 26.53803 ? 508 HOH   B O     1 
HETATM 5643 O  O     . HOH   K 6 .   ? 62.86100  -11.41200 1.80500   1.000 32.75002 ? 509 HOH   B O     1 
HETATM 5644 O  O     . HOH   K 6 .   ? 68.62700  -11.12700 -5.07500  1.000 28.18342 ? 510 HOH   B O     1 
HETATM 5645 O  O     . HOH   K 6 .   ? 32.30000  -28.69700 -11.13400 1.000 20.62809 ? 511 HOH   B O     1 
HETATM 5646 O  O     . HOH   K 6 .   ? 57.68500  -8.77300  -3.80300  1.000 25.29542 ? 512 HOH   B O     1 
HETATM 5647 O  O     . HOH   K 6 .   ? 75.30100  -13.42600 -21.01300 1.000 33.68963 ? 513 HOH   B O     1 
HETATM 5648 O  O     . HOH   K 6 .   ? 44.95800  -19.92300 0.89800   1.000 27.19085 ? 514 HOH   B O     1 
HETATM 5649 O  O     . HOH   K 6 .   ? 68.78400  -28.33000 -17.20600 1.000 39.90364 ? 515 HOH   B O     1 
HETATM 5650 O  O     . HOH   K 6 .   ? 45.362    -12.409   8.846     1.000 27.68051 ? 516 HOH   B O     1 
HETATM 5651 O  O     . HOH   K 6 .   ? 41.91000  -32.79300 -6.33900  1.000 29.20413 ? 517 HOH   B O     1 
HETATM 5652 O  O     . HOH   K 6 .   ? 40.40000  -27.03400 5.53800   1.000 26.65028 ? 518 HOH   B O     1 
HETATM 5653 O  O     . HOH   K 6 .   ? 43.97300  -28.26600 -24.29600 1.000 33.56934 ? 519 HOH   B O     1 
HETATM 5654 O  O     . HOH   K 6 .   ? 56.48700  -34.91500 -4.34300  1.000 20.60878 ? 520 HOH   B O     1 
HETATM 5655 O  O     . HOH   K 6 .   ? 51.58700  -9.76900  -17.93100 1.000 29.78635 ? 521 HOH   B O     1 
HETATM 5656 O  O     . HOH   K 6 .   ? 43.48900  -10.11100 -4.48300  1.000 23.67965 ? 522 HOH   B O     1 
HETATM 5657 O  O     . HOH   K 6 .   ? 39.89900  -31.84100 -3.99700  1.000 28.33021 ? 523 HOH   B O     1 
HETATM 5658 O  O     . HOH   K 6 .   ? 58.84300  -34.51300 -20.69100 1.000 39.21429 ? 524 HOH   B O     1 
HETATM 5659 O  O     . HOH   K 6 .   ? 66.89400  -29.70700 0.00000   0.50  23.22164 ? 525 HOH   B O     1 
HETATM 5660 O  O     . HOH   K 6 .   ? 50.95600  -18.23400 -22.96900 1.000 32.82016 ? 526 HOH   B O     1 
HETATM 5661 O  O     . HOH   K 6 .   ? 31.611    -28.906   -19.701   1.000 22.09733 ? 527 HOH   B O     1 
HETATM 5662 O  O     . HOH   K 6 .   ? 48.80900  -16.88900 -23.30800 1.000 24.38887 ? 528 HOH   B O     1 
HETATM 5663 O  O     . HOH   K 6 .   ? 37.982    -14.058   2.736     1.000 26.77862 ? 529 HOH   B O     1 
HETATM 5664 O  O     . HOH   K 6 .   ? 67.578    -28.136   -1.876    1.000 24.88918 ? 530 HOH   B O     1 
HETATM 5665 O  O     . HOH   K 6 .   ? 67.430    -36.387   -7.525    1.000 24.39685 ? 531 HOH   B O     1 
HETATM 5666 O  O     . HOH   K 6 .   ? 40.34800  -36.57200 -1.03600  1.000 28.41323 ? 532 HOH   B O     1 
HETATM 5667 O  O     . HOH   K 6 .   ? 59.60400  -21.26900 -22.36500 1.000 28.04073 ? 533 HOH   B O     1 
HETATM 5668 O  O     . HOH   K 6 .   ? 45.76100  -30.88300 4.67300   1.000 10.47240 ? 534 HOH   B O     1 
HETATM 5669 O  O     . HOH   K 6 .   ? 66.811    -1.823    -14.012   1.000 30.42352 ? 535 HOH   B O     1 
HETATM 5670 O  O     . HOH   K 6 .   ? 38.72400  -24.39600 -23.95100 1.000 35.56604 ? 536 HOH   B O     1 
HETATM 5671 O  O     . HOH   K 6 .   ? 54.68400  -36.24500 -6.05200  1.000 17.40572 ? 537 HOH   B O     1 
HETATM 5672 O  O     . HOH   K 6 .   ? 53.95200  -12.09800 -20.22300 1.000 25.31490 ? 538 HOH   B O     1 
HETATM 5673 O  O     . HOH   K 6 .   ? 44.75800  -36.05600 -6.17700  1.000 28.57868 ? 539 HOH   B O     1 
HETATM 5674 O  O     . HOH   K 6 .   ? 34.49300  -26.08200 -20.18200 1.000 26.86909 ? 540 HOH   B O     1 
HETATM 5675 O  O     . HOH   K 6 .   ? 38.76900  -30.55200 -0.74600  1.000 34.84591 ? 541 HOH   B O     1 
HETATM 5676 O  O     . HOH   K 6 .   ? 32.54600  -26.94200 -7.04000  1.000 24.63731 ? 542 HOH   B O     1 
HETATM 5677 O  O     . HOH   K 6 .   ? 66.83400  -25.67200 1.22900   1.000 29.05525 ? 543 HOH   B O     1 
HETATM 5678 O  O     . HOH   K 6 .   ? 49.62200  -18.92500 14.23300  1.000 31.82588 ? 544 HOH   B O     1 
HETATM 5679 O  O     . HOH   K 6 .   ? 39.50200  -28.90600 1.64100   1.000 30.01032 ? 545 HOH   B O     1 
HETATM 5680 O  O     . HOH   K 6 .   ? 40.86200  -34.86000 -24.41300 1.000 25.90185 ? 546 HOH   B O     1 
HETATM 5681 O  O     . HOH   K 6 .   ? 50.13000  -21.37400 0.78800   1.000 15.87542 ? 547 HOH   B O     1 
HETATM 5682 O  O     . HOH   K 6 .   ? 73.995    -11.978   -19.059   1.000 33.54340 ? 548 HOH   B O     1 
HETATM 5683 O  O     . HOH   K 6 .   ? 49.31100  -38.27200 -22.65500 1.000 31.82981 ? 549 HOH   B O     1 
HETATM 5684 O  O     . HOH   K 6 .   ? 44.23700  -38.40900 -6.22900  1.000 29.09689 ? 550 HOH   B O     1 
HETATM 5685 O  O     . HOH   K 6 .   ? 52.93200  -15.27800 -20.66100 1.000 26.75229 ? 551 HOH   B O     1 
HETATM 5686 O  O     . HOH   K 6 .   ? 39.33100  -6.42900  -14.57400 1.000 40.08009 ? 552 HOH   B O     1 
HETATM 5687 O  O     . HOH   K 6 .   ? 47.41400  -8.67900  -19.03900 1.000 30.98339 ? 553 HOH   B O     1 
HETATM 5688 O  O     . HOH   K 6 .   ? 58.29000  -39.43100 -7.84800  1.000 23.04679 ? 554 HOH   B O     1 
HETATM 5689 O  O     . HOH   K 6 .   ? 42.59200  -35.07500 -4.50300  1.000 30.11869 ? 555 HOH   B O     1 
HETATM 5690 O  O     . HOH   K 6 .   ? 44.30800  -40.78100 -11.49600 1.000 36.00664 ? 556 HOH   B O     1 
HETATM 5691 O  O     . HOH   K 6 .   ? 67.88500  -32.67800 -1.59400  1.000 39.68753 ? 557 HOH   B O     1 
HETATM 5692 O  O     . HOH   K 6 .   ? 63.10200  -23.45600 -23.78000 1.000 38.01010 ? 558 HOH   B O     1 
HETATM 5693 O  O     . HOH   K 6 .   ? 41.61500  -39.86800 -21.10800 1.000 30.02052 ? 559 HOH   B O     1 
HETATM 5694 O  O     . HOH   K 6 .   ? 75.41000  -23.21900 -20.65900 1.000 29.21116 ? 560 HOH   B O     1 
HETATM 5695 O  O     . HOH   K 6 .   ? 36.69100  -31.16000 -3.18900  1.000 35.21342 ? 561 HOH   B O     1 
HETATM 5696 O  O     . HOH   K 6 .   ? 36.82400  -33.54700 -1.48900  1.000 41.89722 ? 562 HOH   B O     1 
HETATM 5697 O  O     . HOH   L 6 .   ? 65.21300  -28.00100 54.42400  1.000 25.68536 ? 301 HOH   A O     1 
HETATM 5698 O  O     . HOH   L 6 .   ? 86.29200  -17.05100 53.02700  1.000 23.97143 ? 302 HOH   A O     1 
HETATM 5699 O  O     . HOH   L 6 .   ? 75.41800  -30.45800 73.47500  1.000 24.12038 ? 303 HOH   A O     1 
HETATM 5700 O  O     . HOH   L 6 .   ? 97.29500  -19.65000 63.22300  1.000 25.01415 ? 304 HOH   A O     1 
HETATM 5701 O  O     . HOH   L 6 .   ? 104.52300 -32.89800 72.02500  1.000 40.57062 ? 305 HOH   A O     1 
HETATM 5702 O  O     . HOH   L 6 .   ? 74.15900  -25.19500 70.97000  1.000 24.84646 ? 306 HOH   A O     1 
HETATM 5703 O  O     . HOH   L 6 .   ? 64.12900  -24.79200 70.53600  1.000 30.75960 ? 307 HOH   A O     1 
HETATM 5704 O  O     . HOH   L 6 .   ? 81.31600  -2.67400  55.76300  1.000 35.58639 ? 308 HOH   A O     1 
HETATM 5705 O  O     . HOH   L 6 .   ? 76.39400  -10.38500 67.75200  1.000 30.42579 ? 309 HOH   A O     1 
HETATM 5706 O  O     . HOH   L 6 .   ? 81.06400  -32.88800 71.94900  1.000 27.41019 ? 310 HOH   A O     1 
HETATM 5707 O  O     . HOH   L 6 .   ? 75.90200  -12.85200 70.81600  1.000 18.85366 ? 311 HOH   A O     1 
HETATM 5708 O  O     . HOH   L 6 .   ? 95.36100  -25.61800 71.79800  1.000 23.26308 ? 312 HOH   A O     1 
HETATM 5709 O  O     . HOH   L 6 .   ? 87.79800  -18.13700 55.42000  1.000 19.41930 ? 313 HOH   A O     1 
HETATM 5710 O  O     . HOH   L 6 .   ? 84.51300  -40.87400 68.95000  1.000 30.18834 ? 314 HOH   A O     1 
HETATM 5711 O  O     . HOH   L 6 .   ? 96.80400  -37.73800 57.94500  1.000 19.04109 ? 315 HOH   A O     1 
HETATM 5712 O  O     . HOH   L 6 .   ? 90.98000  -15.16500 54.58300  1.000 22.89602 ? 316 HOH   A O     1 
HETATM 5713 O  O     . HOH   L 6 .   ? 83.63100  -26.51000 74.42500  1.000 30.06900 ? 317 HOH   A O     1 
HETATM 5714 O  O     . HOH   L 6 .   ? 70.33100  -32.85200 75.67300  1.000 23.21221 ? 318 HOH   A O     1 
HETATM 5715 O  O     . HOH   L 6 .   ? 83.00300  -20.78100 54.32400  1.000 10.97545 ? 319 HOH   A O     1 
HETATM 5716 O  O     . HOH   L 6 .   ? 67.30100  -29.38000 53.32300  1.000 25.09913 ? 320 HOH   A O     1 
HETATM 5717 O  O     . HOH   L 6 .   ? 81.96500  -16.67200 54.82200  1.000 10.42208 ? 321 HOH   A O     1 
HETATM 5718 O  O     . HOH   L 6 .   ? 104.42000 -35.33200 67.92400  1.000 28.24088 ? 322 HOH   A O     1 
HETATM 5719 O  O     . HOH   L 6 .   ? 71.99200  -18.07600 61.20200  1.000 14.27129 ? 323 HOH   A O     1 
HETATM 5720 O  O     . HOH   L 6 .   ? 93.49300  -21.87800 71.54600  1.000 21.73949 ? 324 HOH   A O     1 
HETATM 5721 O  O     . HOH   L 6 .   ? 78.66000  -35.40900 41.59800  1.000 26.44285 ? 325 HOH   A O     1 
HETATM 5722 O  O     . HOH   L 6 .   ? 100.13900 -22.37900 66.01500  1.000 28.60144 ? 326 HOH   A O     1 
HETATM 5723 O  O     . HOH   L 6 .   ? 79.33500  -18.85000 73.95100  1.000 25.81448 ? 327 HOH   A O     1 
HETATM 5724 O  O     . HOH   L 6 .   ? 78.892    -50.416   55.510    1.000 23.77979 ? 328 HOH   A O     1 
HETATM 5725 O  O     . HOH   L 6 .   ? 79.36800  -18.09900 49.83100  1.000 7.68642  ? 329 HOH   A O     1 
HETATM 5726 O  O     . HOH   L 6 .   ? 63.42700  -29.55000 60.66900  1.000 28.06626 ? 330 HOH   A O     1 
HETATM 5727 O  O     . HOH   L 6 .   ? 63.42900  -27.48500 66.02500  1.000 37.84926 ? 331 HOH   A O     1 
HETATM 5728 O  O     . HOH   L 6 .   ? 97.52800  -35.14300 54.75100  1.000 21.32948 ? 332 HOH   A O     1 
HETATM 5729 O  O     . HOH   L 6 .   ? 85.13500  -34.06500 40.93000  1.000 21.01301 ? 333 HOH   A O     1 
HETATM 5730 O  O     . HOH   L 6 .   ? 84.14700  -48.71200 51.77100  1.000 23.26632 ? 334 HOH   A O     1 
HETATM 5731 O  O     . HOH   L 6 .   ? 64.703    -17.901   72.073    1.000 14.48902 ? 335 HOH   A O     1 
HETATM 5732 O  O     . HOH   L 6 .   ? 71.59400  -20.22700 43.68100  1.000 32.64314 ? 336 HOH   A O     1 
HETATM 5733 O  O     . HOH   L 6 .   ? 68.73500  -19.09800 71.53400  1.000 23.54012 ? 337 HOH   A O     1 
HETATM 5734 O  O     . HOH   L 6 .   ? 90.280    -28.128   73.735    1.000 25.15166 ? 338 HOH   A O     1 
HETATM 5735 O  O     . HOH   L 6 .   ? 84.38900  -11.86800 69.79700  1.000 39.31615 ? 339 HOH   A O     1 
HETATM 5736 O  O     . HOH   L 6 .   ? 82.10200  -12.95100 60.04200  1.000 23.54572 ? 340 HOH   A O     1 
HETATM 5737 O  O     . HOH   L 6 .   ? 85.02400  -13.05100 61.77300  1.000 25.94962 ? 341 HOH   A O     1 
HETATM 5738 O  O     . HOH   L 6 .   ? 87.61200  -22.67300 71.87000  1.000 16.80484 ? 342 HOH   A O     1 
HETATM 5739 O  O     . HOH   L 6 .   ? 83.72700  -39.52700 62.89300  1.000 13.54242 ? 343 HOH   A O     1 
HETATM 5740 O  O     . HOH   L 6 .   ? 78.44100  -28.06400 46.75900  1.000 23.64316 ? 344 HOH   A O     1 
HETATM 5741 O  O     . HOH   L 6 .   ? 72.64700  -26.06200 74.53100  1.000 31.16582 ? 345 HOH   A O     1 
HETATM 5742 O  O     . HOH   L 6 .   ? 72.26200  -21.40500 72.75900  1.000 27.81899 ? 346 HOH   A O     1 
HETATM 5743 O  O     . HOH   L 6 .   ? 89.98600  -39.98800 56.27100  1.000 19.63794 ? 347 HOH   A O     1 
HETATM 5744 O  O     . HOH   L 6 .   ? 70.05500  -38.85400 58.46500  1.000 25.30625 ? 348 HOH   A O     1 
HETATM 5745 O  O     . HOH   L 6 .   ? 89.99000  -25.24600 44.03100  1.000 33.63479 ? 349 HOH   A O     1 
HETATM 5746 O  O     . HOH   L 6 .   ? 86.71900  -17.06900 49.35700  1.000 8.37695  ? 350 HOH   A O     1 
HETATM 5747 O  O     . HOH   L 6 .   ? 75.18900  -25.58600 38.39800  1.000 25.71512 ? 351 HOH   A O     1 
HETATM 5748 O  O     . HOH   L 6 .   ? 70.79700  -39.99100 55.58300  1.000 28.49201 ? 352 HOH   A O     1 
HETATM 5749 O  O     . HOH   L 6 .   ? 81.029    -49.418   46.035    1.000 10.89394 ? 353 HOH   A O     1 
HETATM 5750 O  O     . HOH   L 6 .   ? 86.80400  -37.65700 68.83900  1.000 28.70545 ? 354 HOH   A O     1 
HETATM 5751 O  O     . HOH   L 6 .   ? 98.40000  -31.33100 73.88100  1.000 25.51770 ? 355 HOH   A O     1 
HETATM 5752 O  O     . HOH   L 6 .   ? 69.65400  -41.09400 68.06500  1.000 19.63323 ? 356 HOH   A O     1 
HETATM 5753 O  O     . HOH   L 6 .   ? 95.90000  -18.95500 54.40200  1.000 22.20279 ? 357 HOH   A O     1 
HETATM 5754 O  O     . HOH   L 6 .   ? 85.03400  -18.62600 75.16500  1.000 29.25272 ? 358 HOH   A O     1 
HETATM 5755 O  O     . HOH   L 6 .   ? 91.64900  -41.45100 57.78700  1.000 31.21229 ? 359 HOH   A O     1 
HETATM 5756 O  O     . HOH   L 6 .   ? 75.44300  -41.92100 50.18500  1.000 18.69304 ? 360 HOH   A O     1 
HETATM 5757 O  O     . HOH   L 6 .   ? 64.15900  -20.35500 70.78800  1.000 15.94931 ? 361 HOH   A O     1 
HETATM 5758 O  O     . HOH   L 6 .   ? 73.34500  -26.25100 51.75300  1.000 16.00031 ? 362 HOH   A O     1 
HETATM 5759 O  O     . HOH   L 6 .   ? 82.42400  -13.83900 57.16400  1.000 10.82408 ? 363 HOH   A O     1 
HETATM 5760 O  O     . HOH   L 6 .   ? 80.98400  -41.89100 58.94400  1.000 25.34776 ? 364 HOH   A O     1 
HETATM 5761 O  O     . HOH   L 6 .   ? 81.98500  -8.61300  53.10300  1.000 18.81322 ? 365 HOH   A O     1 
HETATM 5762 O  O     . HOH   L 6 .   ? 65.70700  -18.88800 61.27800  1.000 11.18781 ? 366 HOH   A O     1 
HETATM 5763 O  O     . HOH   L 6 .   ? 71.90500  -45.36600 63.58400  1.000 30.40574 ? 367 HOH   A O     1 
HETATM 5764 O  O     . HOH   L 6 .   ? 94.77800  -37.74800 70.14400  1.000 18.54610 ? 368 HOH   A O     1 
HETATM 5765 O  O     . HOH   L 6 .   ? 97.07000  -27.07100 72.25900  1.000 29.93479 ? 369 HOH   A O     1 
HETATM 5766 O  O     . HOH   L 6 .   ? 84.03800  -33.26200 71.60500  1.000 21.96780 ? 370 HOH   A O     1 
HETATM 5767 O  O     . HOH   L 6 .   ? 76.07400  -24.04600 74.08100  1.000 26.66863 ? 371 HOH   A O     1 
HETATM 5768 O  O     . HOH   L 6 .   ? 79.10200  -28.92300 72.88800  1.000 24.26145 ? 372 HOH   A O     1 
HETATM 5769 O  O     . HOH   L 6 .   ? 70.00600  -40.73500 61.14900  1.000 28.95127 ? 373 HOH   A O     1 
HETATM 5770 O  O     . HOH   L 6 .   ? 89.81600  -31.51900 49.97400  1.000 19.63686 ? 374 HOH   A O     1 
HETATM 5771 O  O     . HOH   L 6 .   ? 84.07100  -23.73600 47.91700  1.000 9.78334  ? 375 HOH   A O     1 
HETATM 5772 O  O     . HOH   L 6 .   ? 69.548    -13.652   66.334    1.000 25.85580 ? 376 HOH   A O     1 
HETATM 5773 O  O     . HOH   L 6 .   ? 84.69200  -13.25500 49.09400  1.000 21.18144 ? 377 HOH   A O     1 
HETATM 5774 O  O     . HOH   L 6 .   ? 75.65100  -11.81200 65.82100  1.000 25.68325 ? 378 HOH   A O     1 
HETATM 5775 O  O     . HOH   L 6 .   ? 93.20500  -11.45700 68.18900  1.000 35.67590 ? 379 HOH   A O     1 
HETATM 5776 O  O     . HOH   L 6 .   ? 101.61900 -35.96200 65.99100  1.000 25.54560 ? 380 HOH   A O     1 
HETATM 5777 O  O     . HOH   L 6 .   ? 92.65700  -18.27200 51.48500  1.000 23.85465 ? 381 HOH   A O     1 
HETATM 5778 O  O     . HOH   L 6 .   ? 85.81200  -15.39400 63.33100  1.000 13.00977 ? 382 HOH   A O     1 
HETATM 5779 O  O     . HOH   L 6 .   ? 91.86900  -22.29000 48.92400  1.000 17.21873 ? 383 HOH   A O     1 
HETATM 5780 O  O     . HOH   L 6 .   ? 81.50100  -38.35000 42.76500  1.000 24.63907 ? 384 HOH   A O     1 
HETATM 5781 O  O     . HOH   L 6 .   ? 94.50700  -23.88400 68.24500  1.000 25.95295 ? 385 HOH   A O     1 
HETATM 5782 O  O     . HOH   L 6 .   ? 81.67000  -25.00500 47.81800  1.000 16.71343 ? 386 HOH   A O     1 
HETATM 5783 O  O     . HOH   L 6 .   ? 85.10200  -23.52000 74.79700  1.000 16.04156 ? 387 HOH   A O     1 
HETATM 5784 O  O     . HOH   L 6 .   ? 79.63700  -44.63600 46.43600  1.000 14.46753 ? 388 HOH   A O     1 
HETATM 5785 O  O     . HOH   L 6 .   ? 93.32300  -40.15800 56.90600  1.000 30.52868 ? 389 HOH   A O     1 
HETATM 5786 O  O     . HOH   L 6 .   ? 87.714    -43.822   48.796    1.000 33.88888 ? 390 HOH   A O     1 
HETATM 5787 O  O     . HOH   L 6 .   ? 74.37600  -26.94900 57.14500  1.000 10.65564 ? 391 HOH   A O     1 
HETATM 5788 O  O     . HOH   L 6 .   ? 78.11600  -38.06900 69.79000  1.000 26.53721 ? 392 HOH   A O     1 
HETATM 5789 O  O     . HOH   L 6 .   ? 71.18600  -22.64100 52.14800  1.000 14.13476 ? 393 HOH   A O     1 
HETATM 5790 O  O     . HOH   L 6 .   ? 80.66500  -26.25700 73.74000  1.000 24.04342 ? 394 HOH   A O     1 
HETATM 5791 O  O     . HOH   L 6 .   ? 62.07800  -24.44600 63.39200  1.000 28.33464 ? 395 HOH   A O     1 
HETATM 5792 O  O     . HOH   L 6 .   ? 94.52900  -32.82300 75.82400  1.000 23.69122 ? 396 HOH   A O     1 
HETATM 5793 O  O     . HOH   L 6 .   ? 71.82300  -14.95200 62.84300  1.000 19.77795 ? 397 HOH   A O     1 
HETATM 5794 O  O     . HOH   L 6 .   ? 91.53200  -19.46100 47.51800  1.000 28.79963 ? 398 HOH   A O     1 
HETATM 5795 O  O     . HOH   L 6 .   ? 95.688    -43.714   65.824    1.000 32.89444 ? 399 HOH   A O     1 
HETATM 5796 O  O     . HOH   L 6 .   ? 67.42600  -35.93000 65.37100  1.000 21.02337 ? 400 HOH   A O     1 
HETATM 5797 O  O     . HOH   L 6 .   ? 77.42900  -19.46300 48.54400  1.000 18.56702 ? 401 HOH   A O     1 
HETATM 5798 O  O     . HOH   L 6 .   ? 79.30100  -36.03600 70.89400  1.000 25.42371 ? 402 HOH   A O     1 
HETATM 5799 O  O     . HOH   L 6 .   ? 93.36100  -14.23800 55.97000  1.000 29.02418 ? 403 HOH   A O     1 
HETATM 5800 O  O     . HOH   L 6 .   ? 64.92000  -21.59200 60.73500  1.000 17.94229 ? 404 HOH   A O     1 
HETATM 5801 O  O     . HOH   L 6 .   ? 77.70300  -26.36900 50.37700  1.000 16.36864 ? 405 HOH   A O     1 
HETATM 5802 O  O     . HOH   L 6 .   ? 92.30600  -25.46000 73.51000  1.000 31.38884 ? 406 HOH   A O     1 
HETATM 5803 O  O     . HOH   L 6 .   ? 72.90800  -26.98800 70.20200  1.000 18.45048 ? 407 HOH   A O     1 
HETATM 5804 O  O     . HOH   L 6 .   ? 103.88400 -38.73100 60.60300  1.000 21.72483 ? 408 HOH   A O     1 
HETATM 5805 O  O     . HOH   L 6 .   ? 80.00200  -26.69900 51.90300  1.000 7.08355  ? 409 HOH   A O     1 
HETATM 5806 O  O     . HOH   L 6 .   ? 86.64600  -42.24800 63.33600  1.000 28.51296 ? 410 HOH   A O     1 
HETATM 5807 O  O     . HOH   L 6 .   ? 72.61900  -36.60800 48.88800  1.000 27.76102 ? 411 HOH   A O     1 
HETATM 5808 O  O     . HOH   L 6 .   ? 70.29200  -18.87800 48.74300  1.000 25.53322 ? 412 HOH   A O     1 
HETATM 5809 O  O     . HOH   L 6 .   ? 87.60300  -10.86400 68.07400  1.000 25.54220 ? 413 HOH   A O     1 
HETATM 5810 O  O     . HOH   L 6 .   ? 70.46600  -36.60500 73.46500  1.000 15.39461 ? 414 HOH   A O     1 
HETATM 5811 O  O     . HOH   L 6 .   ? 92.03800  -47.98500 59.75500  1.000 35.72949 ? 415 HOH   A O     1 
HETATM 5812 O  O     . HOH   L 6 .   ? 88.35500  -31.28100 73.24000  1.000 28.08116 ? 416 HOH   A O     1 
HETATM 5813 O  O     . HOH   L 6 .   ? 88.96700  -20.46900 73.19900  1.000 24.60385 ? 417 HOH   A O     1 
HETATM 5814 O  O     . HOH   L 6 .   ? 74.20200  -16.70000 53.76000  1.000 12.08364 ? 418 HOH   A O     1 
HETATM 5815 O  O     . HOH   L 6 .   ? 86.98600  -25.18900 72.43600  1.000 14.52787 ? 419 HOH   A O     1 
HETATM 5816 O  O     . HOH   L 6 .   ? 69.48600  -25.23500 48.82700  1.000 37.99817 ? 420 HOH   A O     1 
HETATM 5817 O  O     . HOH   L 6 .   ? 72.720    -32.218   76.908    1.000 22.17746 ? 421 HOH   A O     1 
HETATM 5818 O  O     . HOH   L 6 .   ? 103.37700 -29.91700 54.53500  1.000 13.97564 ? 422 HOH   A O     1 
HETATM 5819 O  O     . HOH   L 6 .   ? 66.34300  -32.33200 53.36300  1.000 27.39421 ? 423 HOH   A O     1 
HETATM 5820 O  O     . HOH   L 6 .   ? 100.90600 -36.97600 58.36900  1.000 20.98882 ? 424 HOH   A O     1 
HETATM 5821 O  O     . HOH   L 6 .   ? 69.43100  -21.35100 73.11500  1.000 24.43740 ? 425 HOH   A O     1 
HETATM 5822 O  O     . HOH   L 6 .   ? 73.99600  -17.58600 45.94100  1.000 8.69454  ? 426 HOH   A O     1 
HETATM 5823 O  O     . HOH   L 6 .   ? 74.75200  -44.70700 70.77000  1.000 30.85451 ? 427 HOH   A O     1 
HETATM 5824 O  O     . HOH   L 6 .   ? 76.38700  -20.66100 43.79200  1.000 14.92973 ? 428 HOH   A O     1 
HETATM 5825 O  O     . HOH   L 6 .   ? 89.90200  -14.86600 70.12200  1.000 30.59172 ? 429 HOH   A O     1 
HETATM 5826 O  O     . HOH   L 6 .   ? 95.41300  -31.03100 73.66400  1.000 21.93591 ? 430 HOH   A O     1 
HETATM 5827 O  O     . HOH   L 6 .   ? 85.72200  -4.07100  56.16000  1.000 39.64507 ? 431 HOH   A O     1 
HETATM 5828 O  O     . HOH   L 6 .   ? 82.606    -48.710   54.608    1.000 22.77033 ? 432 HOH   A O     1 
HETATM 5829 O  O     . HOH   L 6 .   ? 91.573    -30.484   73.932    1.000 31.42299 ? 433 HOH   A O     1 
HETATM 5830 O  O     . HOH   L 6 .   ? 77.01100  -19.41600 41.20400  1.000 6.37639  ? 434 HOH   A O     1 
HETATM 5831 O  O     . HOH   L 6 .   ? 74.89800  -14.47700 62.75000  1.000 16.46427 ? 435 HOH   A O     1 
HETATM 5832 O  O     . HOH   L 6 .   ? 89.30100  -47.00700 66.99400  1.000 26.92411 ? 436 HOH   A O     1 
HETATM 5833 O  O     . HOH   L 6 .   ? 82.08100  -6.69200  64.15100  1.000 38.42420 ? 437 HOH   A O     1 
HETATM 5834 O  O     . HOH   L 6 .   ? 73.76200  -28.35400 76.33000  1.000 27.09308 ? 438 HOH   A O     1 
HETATM 5835 O  O     . HOH   L 6 .   ? 80.15400  -29.29600 38.72800  1.000 24.59907 ? 439 HOH   A O     1 
HETATM 5836 O  O     . HOH   L 6 .   ? 97.60400  -20.29800 56.26100  1.000 15.76698 ? 440 HOH   A O     1 
HETATM 5837 O  O     . HOH   L 6 .   ? 73.05100  -19.97900 59.11500  1.000 17.08961 ? 441 HOH   A O     1 
HETATM 5838 O  O     . HOH   L 6 .   ? 76.34800  -44.10300 68.31800  1.000 25.19235 ? 442 HOH   A O     1 
HETATM 5839 O  O     . HOH   L 6 .   ? 101.161   -22.362   62.294    1.000 14.69678 ? 443 HOH   A O     1 
HETATM 5840 O  O     . HOH   L 6 .   ? 65.75800  -17.50800 64.31300  1.000 11.88182 ? 444 HOH   A O     1 
HETATM 5841 O  O     . HOH   L 6 .   ? 93.40000  -26.90300 51.49500  1.000 27.24128 ? 445 HOH   A O     1 
HETATM 5842 O  O     . HOH   L 6 .   ? 86.42900  -13.95100 70.67600  1.000 30.67367 ? 446 HOH   A O     1 
HETATM 5843 O  O     . HOH   L 6 .   ? 104.13200 -24.83500 61.24600  1.000 30.26449 ? 447 HOH   A O     1 
HETATM 5844 O  O     . HOH   L 6 .   ? 69.71200  -33.52100 58.35400  1.000 13.86400 ? 448 HOH   A O     1 
HETATM 5845 O  O     . HOH   L 6 .   ? 87.21900  -35.04000 71.76600  1.000 29.41463 ? 449 HOH   A O     1 
HETATM 5846 O  O     . HOH   L 6 .   ? 71.38600  -21.35700 54.88700  1.000 14.59120 ? 450 HOH   A O     1 
HETATM 5847 O  O     . HOH   L 6 .   ? 98.08500  -20.00900 61.13800  1.000 21.58486 ? 451 HOH   A O     1 
HETATM 5848 O  O     . HOH   L 6 .   ? 65.27100  -22.22100 58.12500  1.000 20.43776 ? 452 HOH   A O     1 
HETATM 5849 O  O     . HOH   L 6 .   ? 77.65700  -8.08000  56.44200  1.000 19.65183 ? 453 HOH   A O     1 
HETATM 5850 O  O     . HOH   L 6 .   ? 70.48900  -14.93400 51.24000  1.000 24.14018 ? 454 HOH   A O     1 
HETATM 5851 O  O     . HOH   L 6 .   ? 95.32300  -25.81500 53.41900  1.000 22.94279 ? 455 HOH   A O     1 
HETATM 5852 O  O     . HOH   L 6 .   ? 73.57000  -23.61600 51.36300  1.000 9.30757  ? 456 HOH   A O     1 
HETATM 5853 O  O     . HOH   L 6 .   ? 67.54000  -29.69100 73.80900  1.000 22.83278 ? 457 HOH   A O     1 
HETATM 5854 O  O     . HOH   L 6 .   ? 68.67300  -36.93000 75.37500  1.000 21.37432 ? 458 HOH   A O     1 
HETATM 5855 O  O     . HOH   L 6 .   ? 71.05800  -24.06000 44.90400  1.000 34.74014 ? 459 HOH   A O     1 
HETATM 5856 O  O     . HOH   L 6 .   ? 105.94200 -39.80100 61.46300  1.000 25.91336 ? 460 HOH   A O     1 
HETATM 5857 O  O     . HOH   L 6 .   ? 83.26500  -35.63600 40.50700  1.000 27.83495 ? 461 HOH   A O     1 
HETATM 5858 O  O     . HOH   L 6 .   ? 68.41900  -37.30200 50.74700  1.000 33.13388 ? 462 HOH   A O     1 
HETATM 5859 O  O     . HOH   L 6 .   ? 90.34400  -40.24100 52.95900  1.000 28.79805 ? 463 HOH   A O     1 
HETATM 5860 O  O     . HOH   L 6 .   ? 75.41100  -37.27700 70.71300  1.000 24.64142 ? 464 HOH   A O     1 
HETATM 5861 O  O     . HOH   L 6 .   ? 87.17300  -43.60500 52.09900  1.000 31.14123 ? 465 HOH   A O     1 
HETATM 5862 O  O     . HOH   L 6 .   ? 72.79900  -38.06800 73.35900  1.000 25.90627 ? 466 HOH   A O     1 
HETATM 5863 O  O     . HOH   L 6 .   ? 95.48200  -16.69100 58.21500  1.000 26.45646 ? 467 HOH   A O     1 
HETATM 5864 O  O     . HOH   L 6 .   ? 68.26200  -38.31700 65.12700  1.000 24.81539 ? 468 HOH   A O     1 
HETATM 5865 O  O     . HOH   L 6 .   ? 75.17000  -29.91700 45.93700  1.000 29.99175 ? 469 HOH   A O     1 
HETATM 5866 O  O     . HOH   L 6 .   ? 67.94200  -26.71300 73.10700  1.000 20.71699 ? 470 HOH   A O     1 
HETATM 5867 O  O     . HOH   L 6 .   ? 76.67100  -28.70500 44.21900  1.000 31.82551 ? 471 HOH   A O     1 
HETATM 5868 O  O     . HOH   L 6 .   ? 88.48700  -14.55600 51.16700  1.000 27.75544 ? 472 HOH   A O     1 
HETATM 5869 O  O     . HOH   L 6 .   ? 69.90100  -25.72300 74.50500  1.000 35.47611 ? 473 HOH   A O     1 
HETATM 5870 O  O     . HOH   L 6 .   ? 81.98600  -27.90700 39.66600  1.000 15.05639 ? 474 HOH   A O     1 
HETATM 5871 O  O     . HOH   L 6 .   ? 74.95800  -12.31500 61.28700  1.000 25.13173 ? 475 HOH   A O     1 
HETATM 5872 O  O     . HOH   L 6 .   ? 74.04500  -12.59800 72.22600  1.000 33.30119 ? 476 HOH   A O     1 
HETATM 5873 O  O     . HOH   L 6 .   ? 84.49000  -9.64300  57.08200  1.000 25.60807 ? 477 HOH   A O     1 
HETATM 5874 O  O     . HOH   L 6 .   ? 76.37200  -9.40800  62.23800  1.000 35.43980 ? 478 HOH   A O     1 
HETATM 5875 O  O     . HOH   L 6 .   ? 103.88300 -37.43200 66.08200  1.000 27.82934 ? 479 HOH   A O     1 
HETATM 5876 O  O     . HOH   L 6 .   ? 90.31800  -12.36300 57.80500  1.000 34.27135 ? 480 HOH   A O     1 
HETATM 5877 O  O     . HOH   L 6 .   ? 88.42700  -40.80300 48.97900  1.000 22.11397 ? 481 HOH   A O     1 
HETATM 5878 O  O     . HOH   L 6 .   ? 77.83700  -28.95600 48.89500  1.000 22.66299 ? 482 HOH   A O     1 
HETATM 5879 O  O     . HOH   L 6 .   ? 92.58400  -29.47200 53.23100  1.000 23.18185 ? 483 HOH   A O     1 
HETATM 5880 O  O     . HOH   L 6 .   ? 70.69000  -40.60500 74.39900  1.000 34.81363 ? 484 HOH   A O     1 
HETATM 5881 O  O     . HOH   L 6 .   ? 62.40200  -22.04800 61.72000  1.000 18.67992 ? 485 HOH   A O     1 
HETATM 5882 O  O     . HOH   L 6 .   ? 76.96000  -34.35800 72.22900  1.000 21.45332 ? 486 HOH   A O     1 
HETATM 5883 O  O     . HOH   L 6 .   ? 67.657    -19.258   57.782    1.000 33.79135 ? 487 HOH   A O     1 
HETATM 5884 O  O     . HOH   L 6 .   ? 98.416    -26.745   52.170    1.000 29.10789 ? 488 HOH   A O     1 
HETATM 5885 O  O     . HOH   L 6 .   ? 72.12300  -17.93600 56.92200  1.000 23.54051 ? 489 HOH   A O     1 
HETATM 5886 O  O     . HOH   L 6 .   ? 73.13800  -33.47400 47.83500  1.000 30.34496 ? 490 HOH   A O     1 
HETATM 5887 O  O     . HOH   L 6 .   ? 67.404    -18.325   74.014    1.000 28.77998 ? 491 HOH   A O     1 
HETATM 5888 O  O     . HOH   L 6 .   ? 81.22700  -40.44000 68.52100  1.000 20.43242 ? 492 HOH   A O     1 
HETATM 5889 O  O     . HOH   L 6 .   ? 68.15700  -36.69700 48.54700  1.000 34.61522 ? 493 HOH   A O     1 
HETATM 5890 O  O     . HOH   L 6 .   ? 97.006    -45.699   63.931    1.000 25.74254 ? 494 HOH   A O     1 
HETATM 5891 O  O     . HOH   L 6 .   ? 86.97200  -20.39200 74.68600  1.000 29.02696 ? 495 HOH   A O     1 
HETATM 5892 O  O     . HOH   L 6 .   ? 87.79200  -41.65500 46.79900  1.000 27.75438 ? 496 HOH   A O     1 
HETATM 5893 O  O     . HOH   L 6 .   ? 73.72400  -21.30800 46.90500  1.000 14.41247 ? 497 HOH   A O     1 
HETATM 5894 O  O     . HOH   L 6 .   ? 84.31900  -3.83700  53.40700  1.000 26.19914 ? 498 HOH   A O     1 
HETATM 5895 O  O     . HOH   L 6 .   ? 102.46500 -25.69700 68.31800  1.000 29.75147 ? 499 HOH   A O     1 
HETATM 5896 O  O     . HOH   L 6 .   ? 75.10200  -15.03900 57.36500  1.000 24.22065 ? 500 HOH   A O     1 
HETATM 5897 O  O     . HOH   L 6 .   ? 82.855    -29.999   74.976    1.000 31.98039 ? 501 HOH   A O     1 
HETATM 5898 O  O     . HOH   L 6 .   ? 73.23100  -23.06700 48.54200  1.000 19.42113 ? 502 HOH   A O     1 
HETATM 5899 O  O     . HOH   L 6 .   ? 81.31000  -27.89100 48.24700  1.000 21.11477 ? 503 HOH   A O     1 
HETATM 5900 O  O     . HOH   L 6 .   ? 67.64800  -20.93700 54.93100  1.000 31.37750 ? 504 HOH   A O     1 
HETATM 5901 O  O     . HOH   L 6 .   ? 67.81900  -40.10300 62.49100  1.000 33.83648 ? 505 HOH   A O     1 
HETATM 5902 O  O     . HOH   L 6 .   ? 96.076    -22.938   49.208    1.000 27.48261 ? 506 HOH   A O     1 
HETATM 5903 O  O     . HOH   L 6 .   ? 73.77900  -40.05000 55.77700  1.000 25.39438 ? 507 HOH   A O     1 
HETATM 5904 O  O     . HOH   L 6 .   ? 74.92000  -30.29900 49.63400  1.000 25.50044 ? 508 HOH   A O     1 
HETATM 5905 O  O     . HOH   L 6 .   ? 78.33900  -41.87200 68.76300  1.000 29.74134 ? 509 HOH   A O     1 
HETATM 5906 O  O     . HOH   L 6 .   ? 85.209    -32.129   73.488    1.000 22.21426 ? 510 HOH   A O     1 
HETATM 5907 O  O     . HOH   L 6 .   ? 76.942    -9.621    73.592    1.000 32.71018 ? 511 HOH   A O     1 
HETATM 5908 O  O     . HOH   L 6 .   ? 63.700    -39.764   74.460    1.000 37.97869 ? 512 HOH   A O     1 
HETATM 5909 O  O     . HOH   L 6 .   ? 78.28100  -26.51500 36.70500  1.000 30.37193 ? 513 HOH   A O     1 
HETATM 5910 O  O     . HOH   L 6 .   ? 90.57800  -13.79800 52.39600  1.000 38.25322 ? 514 HOH   A O     1 
HETATM 5911 O  O     . HOH   L 6 .   ? 61.641    -21.621   70.199    1.000 22.95132 ? 515 HOH   A O     1 
HETATM 5912 O  O     . HOH   L 6 .   ? 70.95300  -43.84500 68.04200  1.000 22.86074 ? 516 HOH   A O     1 
HETATM 5913 O  O     . HOH   L 6 .   ? 97.45400  -18.45500 58.82500  1.000 28.12982 ? 517 HOH   A O     1 
HETATM 5914 O  O     . HOH   L 6 .   ? 95.33200  -41.38000 68.45600  1.000 26.57700 ? 518 HOH   A O     1 
HETATM 5915 O  O     . HOH   L 6 .   ? 72.73500  -30.76800 46.08600  1.000 33.38371 ? 519 HOH   A O     1 
HETATM 5916 O  O     . HOH   L 6 .   ? 69.10200  -30.44700 75.60500  1.000 23.26953 ? 520 HOH   A O     1 
HETATM 5917 O  O     . HOH   L 6 .   ? 84.74600  -7.59700  53.02100  1.000 32.27912 ? 521 HOH   A O     1 
HETATM 5918 O  O     . HOH   L 6 .   ? 86.80400  -15.44500 55.12400  1.000 23.19371 ? 522 HOH   A O     1 
HETATM 5919 O  O     . HOH   L 6 .   ? 96.780    -39.038   74.612    1.000 30.96352 ? 523 HOH   A O     1 
HETATM 5920 O  O     . HOH   L 6 .   ? 87.84000  -41.89700 54.92500  1.000 28.23566 ? 524 HOH   A O     1 
HETATM 5921 O  O     . HOH   L 6 .   ? 88.11200  -11.43200 59.57600  1.000 30.18359 ? 525 HOH   A O     1 
HETATM 5922 O  O     . HOH   L 6 .   ? 99.542    -30.306   50.925    1.000 29.63661 ? 526 HOH   A O     1 
HETATM 5923 O  O     . HOH   L 6 .   ? 84.42700  -37.83100 70.92900  1.000 34.17981 ? 527 HOH   A O     1 
HETATM 5924 O  O     . HOH   L 6 .   ? 91.550    -38.893   43.286    1.000 28.28260 ? 528 HOH   A O     1 
HETATM 5925 O  O     . HOH   L 6 .   ? 65.46900  -20.69600 56.37800  1.000 33.54519 ? 529 HOH   A O     1 
HETATM 5926 O  O     . HOH   L 6 .   ? 70.68000  -44.63700 72.63500  1.000 25.56671 ? 530 HOH   A O     1 
HETATM 5927 O  O     . HOH   L 6 .   ? 75.83300  -19.61400 46.22300  1.000 12.80242 ? 531 HOH   A O     1 
HETATM 5928 O  O     . HOH   L 6 .   ? 64.57000  -22.79800 72.28600  1.000 23.24095 ? 532 HOH   A O     1 
HETATM 5929 O  O     . HOH   L 6 .   ? 95.745    -47.158   71.860    1.000 26.12585 ? 533 HOH   A O     1 
HETATM 5930 O  O     . HOH   L 6 .   ? 68.22700  -34.50100 59.64300  1.000 25.93841 ? 534 HOH   A O     1 
HETATM 5931 O  O     . HOH   L 6 .   ? 93.52400  -42.94800 56.24800  1.000 32.91682 ? 535 HOH   A O     1 
HETATM 5932 O  O     . HOH   L 6 .   ? 66.88100  -26.32000 48.71900  1.000 38.74953 ? 536 HOH   A O     1 
HETATM 5933 O  O     . HOH   L 6 .   ? 91.94000  -30.89400 51.62200  1.000 28.68909 ? 537 HOH   A O     1 
HETATM 5934 O  O     . HOH   L 6 .   ? 92.13400  -10.64300 56.89000  1.000 44.04878 ? 538 HOH   A O     1 
HETATM 5935 O  O     . HOH   L 6 .   ? 106.195   -40.454   66.492    1.000 18.30385 ? 539 HOH   A O     1 
HETATM 5936 O  O     . HOH   L 6 .   ? 62.86200  -23.01200 57.52500  1.000 31.11124 ? 540 HOH   A O     1 
HETATM 5937 O  O     . HOH   L 6 .   ? 61.12400  -23.59800 59.53000  1.000 29.68070 ? 541 HOH   A O     1 
HETATM 5938 O  O     . HOH   L 6 .   ? 88.41900  -13.31400 56.00400  1.000 34.13734 ? 542 HOH   A O     1 
HETATM 5939 O  O     . HOH   L 6 .   ? 85.50300  -12.82100 59.25800  1.000 31.35611 ? 543 HOH   A O     1 
HETATM 5940 O  O     . HOH   L 6 .   ? 80.28900  -29.27400 50.30300  1.000 23.03490 ? 544 HOH   A O     1 
HETATM 5941 O  O     . HOH   L 6 .   ? 66.96600  -35.13800 62.94100  1.000 25.95954 ? 545 HOH   A O     1 
HETATM 5942 O  O     . HOH   L 6 .   ? 64.83800  -33.94300 63.50700  1.000 26.17172 ? 546 HOH   A O     1 
HETATM 5943 O  O     . HOH   L 6 .   ? 68.02600  -34.95500 76.68500  1.000 28.75801 ? 547 HOH   A O     1 
HETATM 5944 O  O     . HOH   L 6 .   ? 93.55400  -41.03600 53.78400  1.000 31.92507 ? 548 HOH   A O     1 
HETATM 5945 O  O     . HOH   L 6 .   ? 102.91300 -30.52000 74.40300  1.000 32.63283 ? 549 HOH   A O     1 
HETATM 5946 O  O     . HOH   L 6 .   ? 73.09700  -15.25900 55.38700  1.000 27.02814 ? 550 HOH   A O     1 
HETATM 5947 O  O     . HOH   L 6 .   ? 77.42500  -17.02400 74.94700  1.000 27.22203 ? 551 HOH   A O     1 
HETATM 5948 O  O     . HOH   L 6 .   ? 70.18300  -16.91600 56.02900  1.000 35.11686 ? 552 HOH   A O     1 
HETATM 5949 O  O     . HOH   L 6 .   ? 95.76700  -16.61500 55.17800  1.000 34.07153 ? 553 HOH   A O     1 
HETATM 5950 O  O     . HOH   L 6 .   ? 71.84600  -11.10800 71.48100  1.000 35.18513 ? 554 HOH   A O     1 
HETATM 5951 O  O     . HOH   L 6 .   ? 69.012    -14.018   75.390    1.000 25.01683 ? 555 HOH   A O     1 
HETATM 5952 O  O     . HOH   L 6 .   ? 77.71500  -46.19300 67.65400  1.000 34.91996 ? 556 HOH   A O     1 
HETATM 5953 O  O     . HOH   L 6 .   ? 85.173    -39.597   72.276    1.000 33.02593 ? 557 HOH   A O     1 
HETATM 5954 O  O     . HOH   L 6 .   ? 101.12400 -29.53100 75.41900  1.000 42.32200 ? 558 HOH   A O     1 
HETATM 5955 O  O     . HOH   L 6 .   ? 70.61300  -45.27000 69.73000  1.000 24.65668 ? 559 HOH   A O     1 
HETATM 5956 O  O     . HOH   L 6 .   ? 72.55900  -13.30500 54.32500  1.000 31.31804 ? 560 HOH   A O     1 
HETATM 5957 O  O     . HOH   L 6 .   ? 88.35400  -4.31800  54.28200  1.000 33.44688 ? 561 HOH   A O     1 
HETATM 5958 O  O     . HOH   L 6 .   ? 67.20400  -19.77400 52.33600  1.000 38.52354 ? 562 HOH   A O     1 
HETATM 5959 O  O     . HOH   M 6 .   ? 53.04700  -29.23600 21.25000  1.000 22.76673 ? 201 HOH   C O     1 
HETATM 5960 O  O     . HOH   M 6 .   ? 28.90900  -42.60200 19.94100  1.000 23.02718 ? 202 HOH   C O     1 
HETATM 5961 O  O     . HOH   M 6 .   ? 25.66100  -37.69900 13.40300  1.000 26.25578 ? 203 HOH   C O     1 
HETATM 5962 O  O     . HOH   M 6 .   ? 47.85100  -36.15300 28.06400  1.000 24.08252 ? 204 HOH   C O     1 
HETATM 5963 O  O     . HOH   M 6 .   ? 66.26800  -49.92100 4.72500   1.000 25.34130 ? 205 HOH   C O     1 
HETATM 5964 O  O     . HOH   M 6 .   ? 27.62500  -37.36900 8.68200   1.000 33.12953 ? 206 HOH   C O     1 
HETATM 5965 O  O     . HOH   M 6 .   ? 41.67000  -53.46600 28.64000  1.000 27.51363 ? 207 HOH   C O     1 
HETATM 5966 O  O     . HOH   M 6 .   ? 64.96400  -56.40100 17.68900  1.000 19.69601 ? 208 HOH   C O     1 
HETATM 5967 O  O     . HOH   M 6 .   ? 35.29700  -49.44800 -1.37100  1.000 27.71612 ? 209 HOH   C O     1 
HETATM 5968 O  O     . HOH   M 6 .   ? 41.39000  -26.63100 25.13000  1.000 31.83447 ? 210 HOH   C O     1 
HETATM 5969 O  O     . HOH   M 6 .   ? 65.18900  -39.73700 9.61600   1.000 19.12679 ? 211 HOH   C O     1 
HETATM 5970 O  O     . HOH   M 6 .   ? 50.35300  -64.13500 11.36000  1.000 33.88820 ? 212 HOH   C O     1 
HETATM 5971 O  O     . HOH   M 6 .   ? 59.79200  -25.01900 7.65100   1.000 28.23776 ? 213 HOH   C O     1 
HETATM 5972 O  O     . HOH   M 6 .   ? 41.45900  -27.30800 22.85800  1.000 26.53635 ? 214 HOH   C O     1 
HETATM 5973 O  O     . HOH   M 6 .   ? 36.77400  -58.74400 4.57300   1.000 24.54640 ? 215 HOH   C O     1 
HETATM 5974 O  O     . HOH   M 6 .   ? 66.00800  -41.47800 10.76100  1.000 23.72914 ? 216 HOH   C O     1 
HETATM 5975 O  O     . HOH   M 6 .   ? 38.59600  -37.39900 12.94800  1.000 13.96122 ? 217 HOH   C O     1 
HETATM 5976 O  O     . HOH   M 6 .   ? 42.84600  -61.52200 22.89800  1.000 27.87769 ? 218 HOH   C O     1 
HETATM 5977 O  O     . HOH   M 6 .   ? 59.47000  -37.86400 21.73200  1.000 15.50061 ? 219 HOH   C O     1 
HETATM 5978 O  O     . HOH   M 6 .   ? 65.470    -56.544   6.697     1.000 30.60025 ? 220 HOH   C O     1 
HETATM 5979 O  O     . HOH   M 6 .   ? 55.86600  -39.86700 4.26900   1.000 14.37893 ? 221 HOH   C O     1 
HETATM 5980 O  O     . HOH   M 6 .   ? 33.29600  -49.57100 21.46900  1.000 20.57306 ? 222 HOH   C O     1 
HETATM 5981 O  O     . HOH   M 6 .   ? 33.23100  -58.81000 14.19400  1.000 23.87520 ? 223 HOH   C O     1 
HETATM 5982 O  O     . HOH   M 6 .   ? 53.60600  -61.16700 17.61900  1.000 20.62064 ? 224 HOH   C O     1 
HETATM 5983 O  O     . HOH   M 6 .   ? 37.98000  -42.55900 4.67000   1.000 18.10957 ? 225 HOH   C O     1 
HETATM 5984 O  O     . HOH   M 6 .   ? 44.03300  -52.83900 -1.61500  1.000 24.63296 ? 226 HOH   C O     1 
HETATM 5985 O  O     . HOH   M 6 .   ? 28.13000  -38.95000 17.13400  1.000 27.90405 ? 227 HOH   C O     1 
HETATM 5986 O  O     . HOH   M 6 .   ? 56.71200  -30.60800 19.70800  1.000 22.58383 ? 228 HOH   C O     1 
HETATM 5987 O  O     . HOH   M 6 .   ? 37.95000  -49.19100 31.22600  1.000 30.43602 ? 229 HOH   C O     1 
HETATM 5988 O  O     . HOH   M 6 .   ? 35.35400  -44.37700 -3.35400  1.000 18.03250 ? 230 HOH   C O     1 
HETATM 5989 O  O     . HOH   M 6 .   ? 63.47600  -43.03100 24.05400  1.000 22.60361 ? 231 HOH   C O     1 
HETATM 5990 O  O     . HOH   M 6 .   ? 46.55300  -61.14200 16.33100  1.000 28.28713 ? 232 HOH   C O     1 
HETATM 5991 O  O     . HOH   M 6 .   ? 38.22600  -34.70100 1.88900   1.000 22.71359 ? 233 HOH   C O     1 
HETATM 5992 O  O     . HOH   M 6 .   ? 49.31900  -44.58900 29.54700  1.000 18.60534 ? 234 HOH   C O     1 
HETATM 5993 O  O     . HOH   M 6 .   ? 57.63900  -46.41400 7.30700   1.000 9.08746  ? 235 HOH   C O     1 
HETATM 5994 O  O     . HOH   M 6 .   ? 50.04400  -46.18100 6.25900   1.000 11.27866 ? 236 HOH   C O     1 
HETATM 5995 O  O     . HOH   M 6 .   ? 39.16400  -55.61200 2.34000   1.000 27.73141 ? 237 HOH   C O     1 
HETATM 5996 O  O     . HOH   M 6 .   ? 49.72700  -48.76600 9.95000   1.000 15.55381 ? 238 HOH   C O     1 
HETATM 5997 O  O     . HOH   M 6 .   ? 44.08400  -31.85400 9.74900   1.000 15.15993 ? 239 HOH   C O     1 
HETATM 5998 O  O     . HOH   M 6 .   ? 41.29000  -42.12900 9.03500   1.000 9.37186  ? 240 HOH   C O     1 
HETATM 5999 O  O     . HOH   M 6 .   ? 59.41000  -35.25900 20.12200  1.000 22.57585 ? 241 HOH   C O     1 
HETATM 6000 O  O     . HOH   M 6 .   ? 56.60300  -52.50300 25.10600  1.000 19.18926 ? 242 HOH   C O     1 
HETATM 6001 O  O     . HOH   M 6 .   ? 66.43000  -57.63000 15.51300  1.000 20.57572 ? 243 HOH   C O     1 
HETATM 6002 O  O     . HOH   M 6 .   ? 47.76100  -62.11500 14.27100  1.000 29.34207 ? 244 HOH   C O     1 
HETATM 6003 O  O     . HOH   M 6 .   ? 32.16900  -54.56400 14.94300  1.000 21.68819 ? 245 HOH   C O     1 
HETATM 6004 O  O     . HOH   M 6 .   ? 30.25100  -49.70300 16.19800  1.000 17.59354 ? 246 HOH   C O     1 
HETATM 6005 O  O     . HOH   M 6 .   ? 35.65400  -31.71800 25.57100  1.000 23.44377 ? 247 HOH   C O     1 
HETATM 6006 O  O     . HOH   M 6 .   ? 56.17700  -48.78600 28.55100  1.000 17.49831 ? 248 HOH   C O     1 
HETATM 6007 O  O     . HOH   M 6 .   ? 34.36700  -33.33700 4.49800   1.000 16.01859 ? 249 HOH   C O     1 
HETATM 6008 O  O     . HOH   M 6 .   ? 34.49400  -59.66800 17.90100  1.000 31.51537 ? 250 HOH   C O     1 
HETATM 6009 O  O     . HOH   M 6 .   ? 45.85400  -54.89300 3.37700   1.000 20.71765 ? 251 HOH   C O     1 
HETATM 6010 O  O     . HOH   M 6 .   ? 63.78300  -39.86400 6.70900   1.000 19.78524 ? 252 HOH   C O     1 
HETATM 6011 O  O     . HOH   M 6 .   ? 63.36900  -45.17500 22.70300  1.000 16.03195 ? 253 HOH   C O     1 
HETATM 6012 O  O     . HOH   M 6 .   ? 38.84800  -45.70100 14.33200  1.000 8.84951  ? 254 HOH   C O     1 
HETATM 6013 O  O     . HOH   M 6 .   ? 29.32000  -42.19000 9.89300   1.000 19.28096 ? 255 HOH   C O     1 
HETATM 6014 O  O     . HOH   M 6 .   ? 52.15200  -54.72200 26.81000  1.000 28.03823 ? 256 HOH   C O     1 
HETATM 6015 O  O     . HOH   M 6 .   ? 41.63200  -26.60500 17.63200  1.000 23.20577 ? 257 HOH   C O     1 
HETATM 6016 O  O     . HOH   M 6 .   ? 30.45400  -40.51800 25.06200  1.000 20.82063 ? 258 HOH   C O     1 
HETATM 6017 O  O     . HOH   M 6 .   ? 62.09600  -39.54200 19.68600  1.000 17.12833 ? 259 HOH   C O     1 
HETATM 6018 O  O     . HOH   M 6 .   ? 48.91600  -39.48400 4.65400   1.000 9.44821  ? 260 HOH   C O     1 
HETATM 6019 O  O     . HOH   M 6 .   ? 34.77100  -28.92600 16.58800  1.000 16.95204 ? 261 HOH   C O     1 
HETATM 6020 O  O     . HOH   M 6 .   ? 67.25900  -52.42700 7.98300   1.000 26.47523 ? 262 HOH   C O     1 
HETATM 6021 O  O     . HOH   M 6 .   ? 57.43300  -39.00600 25.34400  1.000 20.06720 ? 263 HOH   C O     1 
HETATM 6022 O  O     . HOH   M 6 .   ? 55.13200  -41.08300 2.05900   1.000 24.65743 ? 264 HOH   C O     1 
HETATM 6023 O  O     . HOH   M 6 .   ? 38.96600  -59.88700 20.21300  1.000 28.10831 ? 265 HOH   C O     1 
HETATM 6024 O  O     . HOH   M 6 .   ? 52.65600  -58.94500 9.15600   1.000 20.17089 ? 266 HOH   C O     1 
HETATM 6025 O  O     . HOH   M 6 .   ? 59.19500  -53.18800 8.59900   1.000 15.77617 ? 267 HOH   C O     1 
HETATM 6026 O  O     . HOH   M 6 .   ? 29.89500  -45.06000 7.16800   1.000 21.36876 ? 268 HOH   C O     1 
HETATM 6027 O  O     . HOH   M 6 .   ? 37.01400  -36.63600 9.79800   1.000 10.20111 ? 269 HOH   C O     1 
HETATM 6028 O  O     . HOH   M 6 .   ? 38.03100  -36.01700 20.21800  1.000 10.46418 ? 270 HOH   C O     1 
HETATM 6029 O  O     . HOH   M 6 .   ? 38.88200  -56.19800 10.77200  1.000 15.28132 ? 271 HOH   C O     1 
HETATM 6030 O  O     . HOH   M 6 .   ? 49.857    -37.718   27.335    1.000 24.22453 ? 272 HOH   C O     1 
HETATM 6031 O  O     . HOH   M 6 .   ? 43.99900  -60.86300 15.80400  1.000 24.17768 ? 273 HOH   C O     1 
HETATM 6032 O  O     . HOH   M 6 .   ? 33.04100  -55.17100 19.98500  1.000 20.08642 ? 274 HOH   C O     1 
HETATM 6033 O  O     . HOH   M 6 .   ? 35.20600  -51.75600 21.17400  1.000 17.68054 ? 275 HOH   C O     1 
HETATM 6034 O  O     . HOH   M 6 .   ? 36.74600  -33.03900 11.49200  1.000 15.92924 ? 276 HOH   C O     1 
HETATM 6035 O  O     . HOH   M 6 .   ? 34.70000  -42.39300 0.21800   1.000 31.92812 ? 277 HOH   C O     1 
HETATM 6036 O  O     . HOH   M 6 .   ? 56.67400  -36.21600 2.33400   1.000 19.74774 ? 278 HOH   C O     1 
HETATM 6037 O  O     . HOH   M 6 .   ? 66.17400  -53.55700 10.04200  1.000 20.23085 ? 279 HOH   C O     1 
HETATM 6038 O  O     . HOH   M 6 .   ? 58.46300  -50.95600 26.76700  1.000 16.22524 ? 280 HOH   C O     1 
HETATM 6039 O  O     . HOH   M 6 .   ? 42.89700  -41.73000 30.24400  1.000 31.28171 ? 281 HOH   C O     1 
HETATM 6040 O  O     . HOH   M 6 .   ? 43.07500  -55.77800 28.12800  1.000 34.59561 ? 282 HOH   C O     1 
HETATM 6041 O  O     . HOH   M 6 .   ? 39.81600  -44.44300 30.62900  1.000 34.90236 ? 283 HOH   C O     1 
HETATM 6042 O  O     . HOH   M 6 .   ? 34.95000  -40.61300 14.67300  1.000 10.74955 ? 284 HOH   C O     1 
HETATM 6043 O  O     . HOH   M 6 .   ? 36.34300  -56.11500 23.30000  1.000 22.07539 ? 285 HOH   C O     1 
HETATM 6044 O  O     . HOH   M 6 .   ? 32.35500  -36.86000 4.38200   1.000 23.07007 ? 286 HOH   C O     1 
HETATM 6045 O  O     . HOH   M 6 .   ? 43.67500  -39.46600 0.06000   1.000 12.43116 ? 287 HOH   C O     1 
HETATM 6046 O  O     . HOH   M 6 .   ? 45.91800  -54.31900 -0.62700  1.000 15.75649 ? 288 HOH   C O     1 
HETATM 6047 O  O     . HOH   M 6 .   ? 29.81000  -56.62000 13.82400  1.000 38.03103 ? 289 HOH   C O     1 
HETATM 6048 O  O     . HOH   M 6 .   ? 57.71100  -42.94900 4.70900   1.000 15.83735 ? 290 HOH   C O     1 
HETATM 6049 O  O     . HOH   M 6 .   ? 50.53500  -61.17100 23.33500  1.000 34.78807 ? 291 HOH   C O     1 
HETATM 6050 O  O     . HOH   M 6 .   ? 40.76000  -61.94800 13.17500  1.000 28.56875 ? 292 HOH   C O     1 
HETATM 6051 O  O     . HOH   M 6 .   ? 36.82800  -37.69800 21.64600  1.000 15.55187 ? 293 HOH   C O     1 
HETATM 6052 O  O     . HOH   M 6 .   ? 40.32800  -39.54500 5.21400   1.000 14.17236 ? 294 HOH   C O     1 
HETATM 6053 O  O     . HOH   M 6 .   ? 33.330    -32.557   12.482    1.000 12.79345 ? 295 HOH   C O     1 
HETATM 6054 O  O     . HOH   M 6 .   ? 34.24300  -49.21900 28.34300  1.000 23.98127 ? 296 HOH   C O     1 
HETATM 6055 O  O     . HOH   M 6 .   ? 58.08200  -56.28300 17.26200  1.000 15.53464 ? 297 HOH   C O     1 
HETATM 6056 O  O     . HOH   M 6 .   ? 41.86400  -43.90700 6.26000   1.000 17.21342 ? 298 HOH   C O     1 
HETATM 6057 O  O     . HOH   M 6 .   ? 41.35300  -46.93100 -0.61100  1.000 25.67934 ? 299 HOH   C O     1 
HETATM 6058 O  O     . HOH   M 6 .   ? 44.85100  -56.52400 11.19100  1.000 11.84316 ? 300 HOH   C O     1 
HETATM 6059 O  O     . HOH   M 6 .   ? 39.55100  -33.29200 19.39900  1.000 12.96809 ? 301 HOH   C O     1 
HETATM 6060 O  O     . HOH   M 6 .   ? 33.63300  -58.62900 6.66400   1.000 21.52555 ? 302 HOH   C O     1 
HETATM 6061 O  O     . HOH   M 6 .   ? 51.83800  -57.35800 25.93100  1.000 24.12279 ? 303 HOH   C O     1 
HETATM 6062 O  O     . HOH   M 6 .   ? 57.10200  -38.26700 22.85600  1.000 24.57278 ? 304 HOH   C O     1 
HETATM 6063 O  O     . HOH   M 6 .   ? 43.44500  -60.53100 18.68800  1.000 20.10479 ? 305 HOH   C O     1 
HETATM 6064 O  O     . HOH   M 6 .   ? 35.551    -30.798   12.822    1.000 14.41334 ? 306 HOH   C O     1 
HETATM 6065 O  O     . HOH   M 6 .   ? 47.65800  -54.29000 6.12800   1.000 17.41735 ? 307 HOH   C O     1 
HETATM 6066 O  O     . HOH   M 6 .   ? 40.85500  -55.91900 25.54000  1.000 16.21961 ? 308 HOH   C O     1 
HETATM 6067 O  O     . HOH   M 6 .   ? 58.79200  -54.02500 23.46600  1.000 18.90697 ? 309 HOH   C O     1 
HETATM 6068 O  O     . HOH   M 6 .   ? 55.83900  -56.25200 8.24300   1.000 21.99891 ? 310 HOH   C O     1 
HETATM 6069 O  O     . HOH   M 6 .   ? 34.96900  -54.44700 2.92700   1.000 32.57983 ? 311 HOH   C O     1 
HETATM 6070 O  O     . HOH   M 6 .   ? 40.73900  -31.92600 9.62800   1.000 20.84203 ? 312 HOH   C O     1 
HETATM 6071 O  O     . HOH   M 6 .   ? 61.34000  -42.57100 2.66600   1.000 33.73164 ? 313 HOH   C O     1 
HETATM 6072 O  O     . HOH   M 6 .   ? 63.00900  -36.47600 4.35500   1.000 14.87339 ? 314 HOH   C O     1 
HETATM 6073 O  O     . HOH   M 6 .   ? 40.63400  -61.81200 4.19800   1.000 22.12154 ? 315 HOH   C O     1 
HETATM 6074 O  O     . HOH   M 6 .   ? 60.45800  -46.10600 4.47500   1.000 24.54958 ? 316 HOH   C O     1 
HETATM 6075 O  O     . HOH   M 6 .   ? 67.26700  -45.34800 9.89600   1.000 27.80836 ? 317 HOH   C O     1 
HETATM 6076 O  O     . HOH   M 6 .   ? 41.28400  -42.20800 2.00900   1.000 14.20866 ? 318 HOH   C O     1 
HETATM 6077 O  O     . HOH   M 6 .   ? 41.72300  -50.69300 29.88000  1.000 29.71663 ? 319 HOH   C O     1 
HETATM 6078 O  O     . HOH   M 6 .   ? 64.95400  -38.13100 12.93200  1.000 31.38617 ? 320 HOH   C O     1 
HETATM 6079 O  O     . HOH   M 6 .   ? 66.81300  -38.70500 20.18200  1.000 29.60693 ? 321 HOH   C O     1 
HETATM 6080 O  O     . HOH   M 6 .   ? 29.70700  -34.33500 12.20600  1.000 28.00746 ? 322 HOH   C O     1 
HETATM 6081 O  O     . HOH   M 6 .   ? 49.99800  -42.17000 26.82600  1.000 12.81790 ? 323 HOH   C O     1 
HETATM 6082 O  O     . HOH   M 6 .   ? 64.53800  -33.91000 8.16100   1.000 16.18090 ? 324 HOH   C O     1 
HETATM 6083 O  O     . HOH   M 6 .   ? 30.60900  -33.75800 6.14800   1.000 20.89830 ? 325 HOH   C O     1 
HETATM 6084 O  O     . HOH   M 6 .   ? 42.65900  -36.70700 26.29400  1.000 21.20119 ? 326 HOH   C O     1 
HETATM 6085 O  O     . HOH   M 6 .   ? 45.52200  -58.78200 13.06700  1.000 13.15050 ? 327 HOH   C O     1 
HETATM 6086 O  O     . HOH   M 6 .   ? 30.77800  -42.05100 13.99600  1.000 22.09760 ? 328 HOH   C O     1 
HETATM 6087 O  O     . HOH   M 6 .   ? 46.63600  -61.20500 22.82400  1.000 29.88618 ? 329 HOH   C O     1 
HETATM 6088 O  O     . HOH   M 6 .   ? 44.81300  -30.11800 24.18400  1.000 20.93065 ? 330 HOH   C O     1 
HETATM 6089 O  O     . HOH   M 6 .   ? 43.96600  -55.92300 5.18000   1.000 11.83660 ? 331 HOH   C O     1 
HETATM 6090 O  O     . HOH   M 6 .   ? 59.29300  -58.64900 13.07700  1.000 18.17950 ? 332 HOH   C O     1 
HETATM 6091 O  O     . HOH   M 6 .   ? 55.05400  -46.72700 3.48500   1.000 27.63379 ? 333 HOH   C O     1 
HETATM 6092 O  O     . HOH   M 6 .   ? 48.45600  -34.70900 21.77700  1.000 19.67623 ? 334 HOH   C O     1 
HETATM 6093 O  O     . HOH   M 6 .   ? 51.19200  -38.76600 2.77800   1.000 28.96903 ? 335 HOH   C O     1 
HETATM 6094 O  O     . HOH   M 6 .   ? 34.48800  -51.30900 4.56900   1.000 23.98216 ? 336 HOH   C O     1 
HETATM 6095 O  O     . HOH   M 6 .   ? 51.04700  -61.90400 21.22400  1.000 25.83187 ? 337 HOH   C O     1 
HETATM 6096 O  O     . HOH   M 6 .   ? 38.92000  -25.91400 9.13100   1.000 34.80784 ? 338 HOH   C O     1 
HETATM 6097 O  O     . HOH   M 6 .   ? 60.40900  -32.10000 12.63700  1.000 24.45810 ? 339 HOH   C O     1 
HETATM 6098 O  O     . HOH   M 6 .   ? 54.55200  -37.39100 4.33800   1.000 16.97598 ? 340 HOH   C O     1 
HETATM 6099 O  O     . HOH   M 6 .   ? 54.32400  -46.28100 27.99400  1.000 14.71077 ? 341 HOH   C O     1 
HETATM 6100 O  O     . HOH   M 6 .   ? 31.10500  -40.00500 6.42200   1.000 24.21834 ? 342 HOH   C O     1 
HETATM 6101 O  O     . HOH   M 6 .   ? 41.63300  -25.68000 15.40700  1.000 33.38041 ? 343 HOH   C O     1 
HETATM 6102 O  O     . HOH   M 6 .   ? 36.39400  -27.58000 25.20700  1.000 29.19388 ? 344 HOH   C O     1 
HETATM 6103 O  O     . HOH   M 6 .   ? 29.36300  -39.86300 21.16000  1.000 19.81278 ? 345 HOH   C O     1 
HETATM 6104 O  O     . HOH   M 6 .   ? 40.82800  -34.46200 27.16500  1.000 20.98864 ? 346 HOH   C O     1 
HETATM 6105 O  O     . HOH   M 6 .   ? 28.70600  -49.29600 4.13500   1.000 37.37602 ? 347 HOH   C O     1 
HETATM 6106 O  O     . HOH   M 6 .   ? 42.99700  -32.91700 7.73800   1.000 13.41911 ? 348 HOH   C O     1 
HETATM 6107 O  O     . HOH   M 6 .   ? 57.68000  -56.64500 19.96800  1.000 22.88588 ? 349 HOH   C O     1 
HETATM 6108 O  O     . HOH   M 6 .   ? 44.33700  -27.73100 12.61200  1.000 23.31792 ? 350 HOH   C O     1 
HETATM 6109 O  O     . HOH   M 6 .   ? 43.157    -58.396   3.764     1.000 24.30419 ? 351 HOH   C O     1 
HETATM 6110 O  O     . HOH   M 6 .   ? 50.97900  -46.51900 3.54700   1.000 18.20190 ? 352 HOH   C O     1 
HETATM 6111 O  O     . HOH   M 6 .   ? 59.78300  -43.43100 27.41000  1.000 26.48668 ? 353 HOH   C O     1 
HETATM 6112 O  O     . HOH   M 6 .   ? 56.83200  -54.12000 4.44600   1.000 15.06287 ? 354 HOH   C O     1 
HETATM 6113 O  O     . HOH   M 6 .   ? 29.53700  -43.15900 25.23900  1.000 26.83159 ? 355 HOH   C O     1 
HETATM 6114 O  O     . HOH   M 6 .   ? 39.50800  -58.06800 2.39000   1.000 36.71873 ? 356 HOH   C O     1 
HETATM 6115 O  O     . HOH   M 6 .   ? 55.60000  -60.03900 21.02500  1.000 31.88879 ? 357 HOH   C O     1 
HETATM 6116 O  O     . HOH   M 6 .   ? 41.84700  -45.13600 -2.30200  1.000 27.14427 ? 358 HOH   C O     1 
HETATM 6117 O  O     . HOH   M 6 .   ? 57.93000  -46.52600 27.99200  1.000 20.58150 ? 359 HOH   C O     1 
HETATM 6118 O  O     . HOH   M 6 .   ? 62.54900  -39.13500 22.51400  1.000 29.21800 ? 360 HOH   C O     1 
HETATM 6119 O  O     . HOH   M 6 .   ? 37.895    -47.270   -3.196    1.000 34.13429 ? 361 HOH   C O     1 
HETATM 6120 O  O     . HOH   M 6 .   ? 35.57600  -30.31300 23.75500  1.000 26.18141 ? 362 HOH   C O     1 
HETATM 6121 O  O     . HOH   M 6 .   ? 65.78700  -53.39700 16.43300  1.000 29.44346 ? 363 HOH   C O     1 
HETATM 6122 O  O     . HOH   M 6 .   ? 53.19400  -39.10600 3.93700   1.000 28.03135 ? 364 HOH   C O     1 
HETATM 6123 O  O     . HOH   M 6 .   ? 41.79600  -48.28300 -6.38000  1.000 34.61181 ? 365 HOH   C O     1 
HETATM 6124 O  O     . HOH   M 6 .   ? 28.70000  -40.78500 15.33200  1.000 20.39841 ? 366 HOH   C O     1 
HETATM 6125 O  O     . HOH   M 6 .   ? 43.19000  -43.23900 -2.64600  1.000 25.99208 ? 367 HOH   C O     1 
HETATM 6126 O  O     . HOH   M 6 .   ? 61.26300  -53.43500 4.61000   1.000 28.00954 ? 368 HOH   C O     1 
HETATM 6127 O  O     . HOH   M 6 .   ? 64.60300  -53.11800 14.56900  1.000 21.09643 ? 369 HOH   C O     1 
HETATM 6128 O  O     . HOH   M 6 .   ? 38.07600  -31.39600 10.06400  1.000 20.03907 ? 370 HOH   C O     1 
HETATM 6129 O  O     . HOH   M 6 .   ? 37.44700  -37.36900 1.27300   1.000 25.59889 ? 371 HOH   C O     1 
HETATM 6130 O  O     . HOH   M 6 .   ? 53.21200  -45.36500 2.46600   1.000 22.49197 ? 372 HOH   C O     1 
HETATM 6131 O  O     . HOH   M 6 .   ? 64.27600  -38.30800 18.84700  1.000 20.69359 ? 373 HOH   C O     1 
HETATM 6132 O  O     . HOH   M 6 .   ? 44.35600  -26.28200 24.80300  1.000 32.84578 ? 374 HOH   C O     1 
HETATM 6133 O  O     . HOH   M 6 .   ? 44.47900  -57.95700 9.18800   1.000 20.53521 ? 375 HOH   C O     1 
HETATM 6134 O  O     . HOH   M 6 .   ? 45.15900  -60.82100 11.59000  1.000 26.63262 ? 376 HOH   C O     1 
HETATM 6135 O  O     . HOH   M 6 .   ? 62.57400  -37.79500 17.41800  1.000 22.66390 ? 377 HOH   C O     1 
HETATM 6136 O  O     . HOH   M 6 .   ? 44.57800  -24.46300 19.48300  1.000 29.01920 ? 378 HOH   C O     1 
HETATM 6137 O  O     . HOH   M 6 .   ? 48.55600  -40.17000 27.57000  1.000 25.67953 ? 379 HOH   C O     1 
HETATM 6138 O  O     . HOH   M 6 .   ? 53.05400  -62.73400 20.54800  1.000 35.30860 ? 380 HOH   C O     1 
HETATM 6139 O  O     . HOH   M 6 .   ? 27.89600  -47.30200 19.63600  1.000 30.12065 ? 381 HOH   C O     1 
HETATM 6140 O  O     . HOH   M 6 .   ? 30.10000  -49.26800 18.84600  1.000 28.57239 ? 382 HOH   C O     1 
HETATM 6141 O  O     . HOH   M 6 .   ? 68.64400  -45.70400 11.60900  1.000 29.64595 ? 383 HOH   C O     1 
HETATM 6142 O  O     . HOH   M 6 .   ? 48.919    -42.062   30.703    1.000 28.70558 ? 384 HOH   C O     1 
HETATM 6143 O  O     . HOH   M 6 .   ? 39.87000  -52.23300 -0.24000  1.000 29.90675 ? 385 HOH   C O     1 
HETATM 6144 O  O     . HOH   M 6 .   ? 29.34400  -45.53200 4.70600   1.000 35.62119 ? 386 HOH   C O     1 
HETATM 6145 O  O     . HOH   M 6 .   ? 57.60000  -52.32600 -0.23600  1.000 38.57481 ? 387 HOH   C O     1 
HETATM 6146 O  O     . HOH   M 6 .   ? 54.58000  -52.09900 33.67100  1.000 46.37317 ? 388 HOH   C O     1 
HETATM 6147 O  O     . HOH   M 6 .   ? 41.64100  -31.10300 4.88700   1.000 13.02770 ? 389 HOH   C O     1 
HETATM 6148 O  O     . HOH   M 6 .   ? 30.002    -42.654   3.827     1.000 32.16557 ? 390 HOH   C O     1 
HETATM 6149 O  O     . HOH   M 6 .   ? 34.72200  -50.01400 1.90000   1.000 27.50237 ? 391 HOH   C O     1 
HETATM 6150 O  O     . HOH   M 6 .   ? 63.15300  -39.18500 25.17100  1.000 33.36174 ? 392 HOH   C O     1 
HETATM 6151 O  O     . HOH   M 6 .   ? 34.70700  -57.29200 21.52100  1.000 29.42593 ? 393 HOH   C O     1 
HETATM 6152 O  O     . HOH   M 6 .   ? 62.66400  -33.17200 12.07700  1.000 33.15096 ? 394 HOH   C O     1 
HETATM 6153 O  O     . HOH   M 6 .   ? 37.28000  -40.95900 2.73300   1.000 31.09381 ? 395 HOH   C O     1 
HETATM 6154 O  O     . HOH   M 6 .   ? 26.99300  -43.58200 13.49600  1.000 40.84414 ? 396 HOH   C O     1 
HETATM 6155 O  O     . HOH   M 6 .   ? 59.01500  -54.19100 5.90300   1.000 13.12953 ? 397 HOH   C O     1 
HETATM 6156 O  O     . HOH   M 6 .   ? 56.67300  -58.01500 23.06400  1.000 32.69445 ? 398 HOH   C O     1 
HETATM 6157 O  O     . HOH   M 6 .   ? 58.10200  -29.49300 17.48800  1.000 29.65405 ? 399 HOH   C O     1 
HETATM 6158 O  O     . HOH   M 6 .   ? 29.15400  -38.86000 7.43900   1.000 33.80141 ? 400 HOH   C O     1 
HETATM 6159 O  O     . HOH   M 6 .   ? 25.578    -35.672   8.892     1.000 32.13803 ? 401 HOH   C O     1 
HETATM 6160 O  O     . HOH   M 6 .   ? 62.08300  -35.55300 18.73200  1.000 25.98001 ? 402 HOH   C O     1 
HETATM 6161 O  O     . HOH   M 6 .   ? 54.25400  -30.04700 24.52000  1.000 33.02778 ? 403 HOH   C O     1 
HETATM 6162 O  O     . HOH   M 6 .   ? 38.22000  -28.31800 21.19300  1.000 30.36462 ? 404 HOH   C O     1 
HETATM 6163 O  O     . HOH   M 6 .   ? 59.65000  -39.70500 -2.54400  1.000 35.24528 ? 405 HOH   C O     1 
HETATM 6164 O  O     . HOH   M 6 .   ? 58.54200  -56.83700 6.60200   1.000 16.34156 ? 406 HOH   C O     1 
HETATM 6165 O  O     . HOH   M 6 .   ? 44.96900  -40.76100 -4.51500  1.000 20.79294 ? 407 HOH   C O     1 
HETATM 6166 O  O     . HOH   M 6 .   ? 39.11000  -48.51900 0.12800   1.000 25.37005 ? 408 HOH   C O     1 
HETATM 6167 O  O     . HOH   M 6 .   ? 40.83500  -42.25100 4.56300   1.000 12.36771 ? 409 HOH   C O     1 
HETATM 6168 O  O     . HOH   M 6 .   ? 56.098    -54.062   28.506    1.000 34.26913 ? 410 HOH   C O     1 
HETATM 6169 O  O     . HOH   M 6 .   ? 49.405    -47.804   32.131    1.000 31.41220 ? 411 HOH   C O     1 
HETATM 6170 O  O     . HOH   M 6 .   ? 66.555    -53.011   12.778    1.000 17.09362 ? 412 HOH   C O     1 
HETATM 6171 O  O     . HOH   M 6 .   ? 33.66200  -61.53200 6.21400   1.000 42.64354 ? 413 HOH   C O     1 
HETATM 6172 O  O     . HOH   M 6 .   ? 59.03700  -53.76000 1.61700   1.000 33.53679 ? 414 HOH   C O     1 
HETATM 6173 O  O     . HOH   M 6 .   ? 38.720    -39.234   31.138    1.000 31.05731 ? 415 HOH   C O     1 
HETATM 6174 O  O     . HOH   M 6 .   ? 41.62000  -54.24200 2.49200   1.000 18.75136 ? 416 HOH   C O     1 
HETATM 6175 O  O     . HOH   M 6 .   ? 64.72900  -37.70500 15.65300  1.000 26.32282 ? 417 HOH   C O     1 
HETATM 6176 O  O     . HOH   M 6 .   ? 31.632    -35.660   1.645     1.000 37.41216 ? 418 HOH   C O     1 
HETATM 6177 O  O     . HOH   M 6 .   ? 61.54900  -37.49500 24.70200  1.000 37.72570 ? 419 HOH   C O     1 
HETATM 6178 O  O     . HOH   M 6 .   ? 43.763    -36.088   30.143    1.000 24.04336 ? 420 HOH   C O     1 
HETATM 6179 O  O     . HOH   M 6 .   ? 33.45300  -53.62800 5.16700   1.000 29.29467 ? 421 HOH   C O     1 
HETATM 6180 O  O     . HOH   M 6 .   ? 28.54100  -36.84500 6.38500   1.000 37.35932 ? 422 HOH   C O     1 
HETATM 6181 O  O     . HOH   M 6 .   ? 60.82000  -58.21500 5.76400   1.000 17.88984 ? 423 HOH   C O     1 
HETATM 6182 O  O     . HOH   M 6 .   ? 41.66400  -61.69800 19.90500  1.000 26.09963 ? 424 HOH   C O     1 
HETATM 6183 O  O     . HOH   M 6 .   ? 57.51400  -58.05000 15.38800  1.000 19.95797 ? 425 HOH   C O     1 
HETATM 6184 O  O     . HOH   M 6 .   ? 34.85000  -53.42000 23.04500  1.000 20.57382 ? 426 HOH   C O     1 
HETATM 6185 O  O     . HOH   M 6 .   ? 54.94200  -43.86500 -0.95300  1.000 30.34347 ? 427 HOH   C O     1 
HETATM 6186 O  O     . HOH   M 6 .   ? 51.727    -36.699   29.040    1.000 23.06591 ? 428 HOH   C O     1 
HETATM 6187 O  O     . HOH   M 6 .   ? 55.18600  -48.33900 30.72100  1.000 28.18253 ? 429 HOH   C O     1 
HETATM 6188 O  O     . HOH   M 6 .   ? 46.22900  -39.27900 28.50400  1.000 24.44874 ? 430 HOH   C O     1 
HETATM 6189 O  O     . HOH   M 6 .   ? 33.31400  -31.13000 4.77400   1.000 31.05584 ? 431 HOH   C O     1 
HETATM 6190 O  O     . HOH   M 6 .   ? 60.16100  -46.48700 29.21600  1.000 33.29793 ? 432 HOH   C O     1 
HETATM 6191 O  O     . HOH   M 6 .   ? 55.00500  -54.28100 26.17100  1.000 26.99554 ? 433 HOH   C O     1 
HETATM 6192 O  O     . HOH   M 6 .   ? 30.44500  -55.53800 19.47700  1.000 35.18498 ? 434 HOH   C O     1 
HETATM 6193 O  O     . HOH   M 6 .   ? 45.09600  -23.69000 14.85200  1.000 35.50748 ? 435 HOH   C O     1 
HETATM 6194 O  O     . HOH   M 6 .   ? 56.18400  -60.34600 23.44100  1.000 38.36549 ? 436 HOH   C O     1 
HETATM 6195 O  O     . HOH   M 6 .   ? 42.04800  -53.38000 0.08300   1.000 25.66192 ? 437 HOH   C O     1 
HETATM 6196 O  O     . HOH   M 6 .   ? 65.31400  -40.14100 4.66400   1.000 33.98589 ? 438 HOH   C O     1 
HETATM 6197 O  O     . HOH   M 6 .   ? 58.11100  -31.53300 21.93200  1.000 27.50511 ? 439 HOH   C O     1 
HETATM 6198 O  O     . HOH   M 6 .   ? 43.63100  -39.15000 -2.70100  1.000 18.57810 ? 440 HOH   C O     1 
HETATM 6199 O  O     . HOH   M 6 .   ? 41.37300  -38.39100 0.75900   1.000 19.63806 ? 441 HOH   C O     1 
HETATM 6200 O  O     . HOH   M 6 .   ? 39.50100  -39.05000 2.57600   1.000 18.99074 ? 442 HOH   C O     1 
HETATM 6201 O  O     . HOH   M 6 .   ? 57.73900  -51.15900 29.07700  1.000 27.10547 ? 443 HOH   C O     1 
HETATM 6202 O  O     . HOH   M 6 .   ? 43.21400  -39.22200 27.18000  1.000 28.89469 ? 444 HOH   C O     1 
HETATM 6203 O  O     . HOH   M 6 .   ? 58.89200  -30.73400 23.86500  1.000 35.81271 ? 445 HOH   C O     1 
HETATM 6204 O  O     . HOH   N 6 .   ? 74.20800  -1.96800  19.89500  1.000 31.68219 ? 201 HOH   D O     1 
HETATM 6205 O  O     . HOH   N 6 .   ? 67.41100  -19.43700 29.51500  1.000 29.30525 ? 202 HOH   D O     1 
HETATM 6206 O  O     . HOH   N 6 .   ? 74.10500  -20.75300 27.09900  1.000 23.09806 ? 203 HOH   D O     1 
HETATM 6207 O  O     . HOH   N 6 .   ? 71.23500  -22.66600 41.10800  1.000 29.10079 ? 204 HOH   D O     1 
HETATM 6208 O  O     . HOH   N 6 .   ? 58.87600  -8.23700  31.21000  1.000 17.97425 ? 205 HOH   D O     1 
HETATM 6209 O  O     . HOH   N 6 .   ? 77.60800  -14.51100 22.94800  1.000 23.91109 ? 206 HOH   D O     1 
HETATM 6210 O  O     . HOH   N 6 .   ? 74.34800  2.37500   52.43200  1.000 21.36823 ? 207 HOH   D O     1 
HETATM 6211 O  O     . HOH   N 6 .   ? 87.21600  -11.47100 26.08300  1.000 22.30341 ? 208 HOH   D O     1 
HETATM 6212 O  O     . HOH   N 6 .   ? 83.26100  -21.58100 30.24400  1.000 22.70340 ? 209 HOH   D O     1 
HETATM 6213 O  O     . HOH   N 6 .   ? 87.14800  -14.42800 48.53900  1.000 16.08051 ? 210 HOH   D O     1 
HETATM 6214 O  O     . HOH   N 6 .   ? 96.07900  2.96800   40.29300  1.000 23.83708 ? 211 HOH   D O     1 
HETATM 6215 O  O     . HOH   N 6 .   ? 72.36500  2.83100   17.34800  1.000 28.18434 ? 212 HOH   D O     1 
HETATM 6216 O  O     . HOH   N 6 .   ? 93.32700  -11.42700 29.15800  1.000 35.52989 ? 213 HOH   D O     1 
HETATM 6217 O  O     . HOH   N 6 .   ? 95.15200  5.93400   32.92900  1.000 23.13451 ? 214 HOH   D O     1 
HETATM 6218 O  O     . HOH   N 6 .   ? 71.31700  -8.52200  41.85700  1.000 5.49273  ? 215 HOH   D O     1 
HETATM 6219 O  O     . HOH   N 6 .   ? 95.24000  -10.17900 40.77800  1.000 24.62403 ? 216 HOH   D O     1 
HETATM 6220 O  O     . HOH   N 6 .   ? 80.628    -18.764   23.033    1.000 27.75346 ? 217 HOH   D O     1 
HETATM 6221 O  O     . HOH   N 6 .   ? 80.00200  -1.72400  41.18100  1.000 12.36289 ? 218 HOH   D O     1 
HETATM 6222 O  O     . HOH   N 6 .   ? 64.67500  -7.84000  50.86700  1.000 25.93026 ? 219 HOH   D O     1 
HETATM 6223 O  O     . HOH   N 6 .   ? 66.98500  -17.44900 39.73700  1.000 19.54361 ? 220 HOH   D O     1 
HETATM 6224 O  O     . HOH   N 6 .   ? 60.36300  -0.81400  34.76200  1.000 17.55109 ? 221 HOH   D O     1 
HETATM 6225 O  O     . HOH   N 6 .   ? 89.54300  -12.31200 29.10500  1.000 27.09598 ? 222 HOH   D O     1 
HETATM 6226 O  O     . HOH   N 6 .   ? 76.21800  10.64400  28.52200  1.000 22.97071 ? 223 HOH   D O     1 
HETATM 6227 O  O     . HOH   N 6 .   ? 71.70700  -8.03200  49.14600  1.000 20.37301 ? 224 HOH   D O     1 
HETATM 6228 O  O     . HOH   N 6 .   ? 70.87700  -23.18900 28.19400  1.000 33.25119 ? 225 HOH   D O     1 
HETATM 6229 O  O     . HOH   N 6 .   ? 71.64800  -23.91800 33.46000  1.000 22.77478 ? 226 HOH   D O     1 
HETATM 6230 O  O     . HOH   N 6 .   ? 69.67100  -11.43400 48.45800  1.000 17.83895 ? 227 HOH   D O     1 
HETATM 6231 O  O     . HOH   N 6 .   ? 95.07500  -11.85400 37.49300  1.000 33.23300 ? 228 HOH   D O     1 
HETATM 6232 O  O     . HOH   N 6 .   ? 65.152    -6.166    54.359    1.000 15.24539 ? 229 HOH   D O     1 
HETATM 6233 O  O     . HOH   N 6 .   ? 75.97600  4.46100   47.82400  1.000 22.71984 ? 230 HOH   D O     1 
HETATM 6234 O  O     . HOH   N 6 .   ? 64.386    -5.224    19.222    1.000 25.41715 ? 231 HOH   D O     1 
HETATM 6235 O  O     . HOH   N 6 .   ? 79.29700  -10.95200 46.12700  1.000 8.78948  ? 232 HOH   D O     1 
HETATM 6236 O  O     . HOH   N 6 .   ? 69.01000  5.65700   40.14400  1.000 11.06326 ? 233 HOH   D O     1 
HETATM 6237 O  O     . HOH   N 6 .   ? 58.18500  -11.50700 34.11300  1.000 17.73041 ? 234 HOH   D O     1 
HETATM 6238 O  O     . HOH   N 6 .   ? 87.76900  -3.95100  43.51300  1.000 9.40830  ? 235 HOH   D O     1 
HETATM 6239 O  O     . HOH   N 6 .   ? 55.527    -12.855   37.345    1.000 22.78516 ? 236 HOH   D O     1 
HETATM 6240 O  O     . HOH   N 6 .   ? 60.361    -4.181    25.717    1.000 23.48913 ? 237 HOH   D O     1 
HETATM 6241 O  O     . HOH   N 6 .   ? 77.90200  11.55800  36.34800  1.000 31.34824 ? 238 HOH   D O     1 
HETATM 6242 O  O     . HOH   N 6 .   ? 92.08800  -11.02300 31.35300  1.000 17.62168 ? 239 HOH   D O     1 
HETATM 6243 O  O     . HOH   N 6 .   ? 73.07200  -14.51900 24.86800  1.000 16.16812 ? 240 HOH   D O     1 
HETATM 6244 O  O     . HOH   N 6 .   ? 71.38000  -3.38100  51.26200  1.000 23.16624 ? 241 HOH   D O     1 
HETATM 6245 O  O     . HOH   N 6 .   ? 97.667    1.686     42.413    1.000 29.02129 ? 242 HOH   D O     1 
HETATM 6246 O  O     . HOH   N 6 .   ? 62.02100  4.01900   35.74000  1.000 19.32343 ? 243 HOH   D O     1 
HETATM 6247 O  O     . HOH   N 6 .   ? 69.06000  9.35300   30.35900  1.000 24.86837 ? 244 HOH   D O     1 
HETATM 6248 O  O     . HOH   N 6 .   ? 93.80100  -10.33000 44.12900  1.000 24.07163 ? 245 HOH   D O     1 
HETATM 6249 O  O     . HOH   N 6 .   ? 63.44100  8.58300   36.87500  1.000 31.97974 ? 246 HOH   D O     1 
HETATM 6250 O  O     . HOH   N 6 .   ? 78.22200  -6.13700  21.63000  1.000 25.03995 ? 247 HOH   D O     1 
HETATM 6251 O  O     . HOH   N 6 .   ? 93.79600  -2.86300  25.14300  1.000 35.84527 ? 248 HOH   D O     1 
HETATM 6252 O  O     . HOH   N 6 .   ? 62.52100  -13.51500 46.71200  1.000 27.18927 ? 249 HOH   D O     1 
HETATM 6253 O  O     . HOH   N 6 .   ? 59.34700  -14.52100 37.87300  1.000 29.33600 ? 250 HOH   D O     1 
HETATM 6254 O  O     . HOH   N 6 .   ? 80.29800  -8.29000  23.89900  1.000 22.44220 ? 251 HOH   D O     1 
HETATM 6255 O  O     . HOH   N 6 .   ? 84.73000  4.94400   45.07400  1.000 15.33084 ? 252 HOH   D O     1 
HETATM 6256 O  O     . HOH   N 6 .   ? 70.43600  -10.99000 45.77700  1.000 13.38476 ? 253 HOH   D O     1 
HETATM 6257 O  O     . HOH   N 6 .   ? 60.42100  -10.07700 26.15300  1.000 14.22775 ? 254 HOH   D O     1 
HETATM 6258 O  O     . HOH   N 6 .   ? 85.05400  -9.02900  48.97000  1.000 24.22959 ? 255 HOH   D O     1 
HETATM 6259 O  O     . HOH   N 6 .   ? 89.37600  2.90000   41.97500  1.000 16.05458 ? 256 HOH   D O     1 
HETATM 6260 O  O     . HOH   N 6 .   ? 74.34200  -18.85000 41.20000  1.000 15.00043 ? 257 HOH   D O     1 
HETATM 6261 O  O     . HOH   N 6 .   ? 76.06500  3.72300   51.44200  1.000 19.43022 ? 258 HOH   D O     1 
HETATM 6262 O  O     . HOH   N 6 .   ? 80.25500  -4.10200  44.60800  1.000 10.41265 ? 259 HOH   D O     1 
HETATM 6263 O  O     . HOH   N 6 .   ? 83.91600  10.53300  32.85800  1.000 20.38605 ? 260 HOH   D O     1 
HETATM 6264 O  O     . HOH   N 6 .   ? 68.70000  -13.34600 38.05700  1.000 11.68569 ? 261 HOH   D O     1 
HETATM 6265 O  O     . HOH   N 6 .   ? 88.30400  0.15800   24.26800  1.000 23.66985 ? 262 HOH   D O     1 
HETATM 6266 O  O     . HOH   N 6 .   ? 64.72000  -17.14300 46.75400  1.000 16.72185 ? 263 HOH   D O     1 
HETATM 6267 O  O     . HOH   N 6 .   ? 63.16500  -1.05600  29.55100  1.000 13.81846 ? 264 HOH   D O     1 
HETATM 6268 O  O     . HOH   N 6 .   ? 67.68300  -4.76200  19.51600  1.000 30.70139 ? 265 HOH   D O     1 
HETATM 6269 O  O     . HOH   N 6 .   ? 87.86300  -7.52300  46.19900  1.000 14.24677 ? 266 HOH   D O     1 
HETATM 6270 O  O     . HOH   N 6 .   ? 63.84300  0.60400   25.09000  1.000 16.76387 ? 267 HOH   D O     1 
HETATM 6271 O  O     . HOH   N 6 .   ? 89.32300  8.18100   37.64600  1.000 20.05896 ? 268 HOH   D O     1 
HETATM 6272 O  O     . HOH   N 6 .   ? 85.84700  -10.69000 46.79600  1.000 19.61382 ? 269 HOH   D O     1 
HETATM 6273 O  O     . HOH   N 6 .   ? 93.20400  -5.66300  27.67500  1.000 15.89615 ? 270 HOH   D O     1 
HETATM 6274 O  O     . HOH   N 6 .   ? 71.61500  3.05000   22.11700  1.000 24.44916 ? 271 HOH   D O     1 
HETATM 6275 O  O     . HOH   N 6 .   ? 88.27500  3.52900   27.04000  1.000 21.43755 ? 272 HOH   D O     1 
HETATM 6276 O  O     . HOH   N 6 .   ? 91.23500  -7.48900  48.27800  1.000 26.27584 ? 273 HOH   D O     1 
HETATM 6277 O  O     . HOH   N 6 .   ? 77.667    3.924     44.548    1.000 15.77672 ? 274 HOH   D O     1 
HETATM 6278 O  O     . HOH   N 6 .   ? 82.33300  -10.08200 49.75300  1.000 17.95513 ? 275 HOH   D O     1 
HETATM 6279 O  O     . HOH   N 6 .   ? 87.06600  -12.56600 28.09900  1.000 22.42091 ? 276 HOH   D O     1 
HETATM 6280 O  O     . HOH   N 6 .   ? 93.32500  -7.72000  26.18800  1.000 29.74645 ? 277 HOH   D O     1 
HETATM 6281 O  O     . HOH   N 6 .   ? 66.74700  -12.81300 29.55400  1.000 11.99157 ? 278 HOH   D O     1 
HETATM 6282 O  O     . HOH   N 6 .   ? 68.94000  -4.92900  36.59900  1.000 8.49411  ? 279 HOH   D O     1 
HETATM 6283 O  O     . HOH   N 6 .   ? 63.03300  4.51200   30.74500  1.000 16.78785 ? 280 HOH   D O     1 
HETATM 6284 O  O     . HOH   N 6 .   ? 86.76900  1.89600   25.50900  1.000 18.31338 ? 281 HOH   D O     1 
HETATM 6285 O  O     . HOH   N 6 .   ? 68.34300  -7.82100  46.07500  1.000 18.30390 ? 282 HOH   D O     1 
HETATM 6286 O  O     . HOH   N 6 .   ? 64.96500  -9.96200  36.41500  1.000 7.67533  ? 283 HOH   D O     1 
HETATM 6287 O  O     . HOH   N 6 .   ? 63.27100  3.88500   42.91900  1.000 24.96962 ? 284 HOH   D O     1 
HETATM 6288 O  O     . HOH   N 6 .   ? 73.74200  -10.87600 50.85900  1.000 16.46103 ? 285 HOH   D O     1 
HETATM 6289 O  O     . HOH   N 6 .   ? 84.50500  3.54700   24.24400  1.000 26.25231 ? 286 HOH   D O     1 
HETATM 6290 O  O     . HOH   N 6 .   ? 95.37100  -5.38900  33.81300  1.000 21.20753 ? 287 HOH   D O     1 
HETATM 6291 O  O     . HOH   N 6 .   ? 70.94700  -18.57700 41.46500  1.000 19.14644 ? 288 HOH   D O     1 
HETATM 6292 O  O     . HOH   N 6 .   ? 81.72000  -11.80100 47.78900  1.000 19.24088 ? 289 HOH   D O     1 
HETATM 6293 O  O     . HOH   N 6 .   ? 67.04700  -13.91200 41.41700  1.000 8.88947  ? 290 HOH   D O     1 
HETATM 6294 O  O     . HOH   N 6 .   ? 67.88200  -6.43500  51.50400  1.000 31.62178 ? 291 HOH   D O     1 
HETATM 6295 O  O     . HOH   N 6 .   ? 60.89100  -8.70700  37.05400  1.000 18.31990 ? 292 HOH   D O     1 
HETATM 6296 O  O     . HOH   N 6 .   ? 73.46300  9.84000   31.86700  1.000 13.06217 ? 293 HOH   D O     1 
HETATM 6297 O  O     . HOH   N 6 .   ? 93.12200  -14.09100 46.58900  1.000 14.88731 ? 294 HOH   D O     1 
HETATM 6298 O  O     . HOH   N 6 .   ? 59.27700  -8.28700  41.07500  1.000 20.94144 ? 295 HOH   D O     1 
HETATM 6299 O  O     . HOH   N 6 .   ? 63.27800  -18.01200 38.85700  1.000 12.13681 ? 296 HOH   D O     1 
HETATM 6300 O  O     . HOH   N 6 .   ? 80.81000  -5.22500  20.32300  1.000 29.83698 ? 297 HOH   D O     1 
HETATM 6301 O  O     . HOH   N 6 .   ? 70.84600  5.03200   25.18700  1.000 11.28920 ? 298 HOH   D O     1 
HETATM 6302 O  O     . HOH   N 6 .   ? 81.65400  -23.53200 29.06400  1.000 29.41790 ? 299 HOH   D O     1 
HETATM 6303 O  O     . HOH   N 6 .   ? 79.81000  2.71000   22.78900  1.000 24.51132 ? 300 HOH   D O     1 
HETATM 6304 O  O     . HOH   N 6 .   ? 73.16100  -25.07100 30.46900  1.000 28.81814 ? 301 HOH   D O     1 
HETATM 6305 O  O     . HOH   N 6 .   ? 73.83800  0.16100   21.13700  1.000 22.18787 ? 302 HOH   D O     1 
HETATM 6306 O  O     . HOH   N 6 .   ? 74.13800  10.51400  35.10400  1.000 29.07550 ? 303 HOH   D O     1 
HETATM 6307 O  O     . HOH   N 6 .   ? 68.04300  -14.65400 31.05600  1.000 9.64491  ? 304 HOH   D O     1 
HETATM 6308 O  O     . HOH   N 6 .   ? 86.05600  -1.57900  22.21000  1.000 25.42946 ? 305 HOH   D O     1 
HETATM 6309 O  O     . HOH   N 6 .   ? 64.46100  0.70000   46.28100  1.000 25.70131 ? 306 HOH   D O     1 
HETATM 6310 O  O     . HOH   N 6 .   ? 84.94200  -4.13500  47.12300  1.000 23.68839 ? 307 HOH   D O     1 
HETATM 6311 O  O     . HOH   N 6 .   ? 90.64800  -4.13900  46.36800  1.000 20.98987 ? 308 HOH   D O     1 
HETATM 6312 O  O     . HOH   N 6 .   ? 64.83900  -21.85900 34.52200  1.000 18.19345 ? 309 HOH   D O     1 
HETATM 6313 O  O     . HOH   N 6 .   ? 69.48100  5.44100   48.85600  1.000 28.96233 ? 310 HOH   D O     1 
HETATM 6314 O  O     . HOH   N 6 .   ? 75.44100  8.10200   37.71600  1.000 21.02364 ? 311 HOH   D O     1 
HETATM 6315 O  O     . HOH   N 6 .   ? 84.90000  -12.99500 46.37500  1.000 18.08718 ? 312 HOH   D O     1 
HETATM 6316 O  O     . HOH   N 6 .   ? 69.61700  -17.40300 31.82600  1.000 12.14805 ? 313 HOH   D O     1 
HETATM 6317 O  O     . HOH   N 6 .   ? 70.782    11.335    46.611    1.000 31.57547 ? 314 HOH   D O     1 
HETATM 6318 O  O     . HOH   N 6 .   ? 75.01800  6.03700   39.48500  1.000 11.29130 ? 315 HOH   D O     1 
HETATM 6319 O  O     . HOH   N 6 .   ? 67.75100  -8.13000  22.09400  1.000 23.85831 ? 316 HOH   D O     1 
HETATM 6320 O  O     . HOH   N 6 .   ? 59.75900  -5.58800  43.56000  1.000 27.29459 ? 317 HOH   D O     1 
HETATM 6321 O  O     . HOH   N 6 .   ? 73.13100  -17.52400 43.46800  1.000 15.64397 ? 318 HOH   D O     1 
HETATM 6322 O  O     . HOH   N 6 .   ? 97.74800  -5.38900  41.89200  1.000 30.65323 ? 319 HOH   D O     1 
HETATM 6323 O  O     . HOH   N 6 .   ? 72.34200  -6.62800  44.82100  1.000 16.09875 ? 320 HOH   D O     1 
HETATM 6324 O  O     . HOH   N 6 .   ? 64.54700  -0.53600  52.31200  1.000 23.86668 ? 321 HOH   D O     1 
HETATM 6325 O  O     . HOH   N 6 .   ? 84.29600  -4.44700  22.98200  1.000 17.81356 ? 322 HOH   D O     1 
HETATM 6326 O  O     . HOH   N 6 .   ? 81.61300  6.75900   24.72700  1.000 17.32609 ? 323 HOH   D O     1 
HETATM 6327 O  O     . HOH   N 6 .   ? 79.83500  -13.47800 23.33800  1.000 21.81346 ? 324 HOH   D O     1 
HETATM 6328 O  O     . HOH   N 6 .   ? 68.36800  -15.62600 49.60100  1.000 25.31586 ? 325 HOH   D O     1 
HETATM 6329 O  O     . HOH   N 6 .   ? 74.17600  5.36900   45.55300  1.000 13.56734 ? 326 HOH   D O     1 
HETATM 6330 O  O     . HOH   N 6 .   ? 63.638    -8.074    19.882    1.000 27.80111 ? 327 HOH   D O     1 
HETATM 6331 O  O     . HOH   N 6 .   ? 78.47300  -16.13200 29.28400  1.000 16.12059 ? 328 HOH   D O     1 
HETATM 6332 O  O     . HOH   N 6 .   ? 69.57300  -0.78200  16.06600  1.000 30.91094 ? 329 HOH   D O     1 
HETATM 6333 O  O     . HOH   N 6 .   ? 58.69500  -9.79000  35.84400  1.000 17.32140 ? 330 HOH   D O     1 
HETATM 6334 O  O     . HOH   N 6 .   ? 88.17400  5.84300   33.45800  1.000 10.98063 ? 331 HOH   D O     1 
HETATM 6335 O  O     . HOH   N 6 .   ? 62.329    -12.798   22.139    1.000 28.09465 ? 332 HOH   D O     1 
HETATM 6336 O  O     . HOH   N 6 .   ? 84.14800  -19.07000 26.50600  1.000 29.20876 ? 333 HOH   D O     1 
HETATM 6337 O  O     . HOH   N 6 .   ? 74.36500  -22.96100 38.48200  1.000 24.14697 ? 334 HOH   D O     1 
HETATM 6338 O  O     . HOH   N 6 .   ? 81.01000  11.41400  29.94800  1.000 27.56501 ? 335 HOH   D O     1 
HETATM 6339 O  O     . HOH   N 6 .   ? 92.52000  -13.63400 49.40300  1.000 22.60995 ? 336 HOH   D O     1 
HETATM 6340 O  O     . HOH   N 6 .   ? 54.547    -10.860   40.523    1.000 34.81515 ? 337 HOH   D O     1 
HETATM 6341 O  O     . HOH   N 6 .   ? 64.83500  0.76900   29.56200  1.000 13.21948 ? 338 HOH   D O     1 
HETATM 6342 O  O     . HOH   N 6 .   ? 72.24200  10.87300  27.72700  1.000 22.61754 ? 339 HOH   D O     1 
HETATM 6343 O  O     . HOH   N 6 .   ? 66.34800  12.94900  38.75500  1.000 33.90548 ? 340 HOH   D O     1 
HETATM 6344 O  O     . HOH   N 6 .   ? 66.10400  6.23000   28.26500  1.000 28.17908 ? 341 HOH   D O     1 
HETATM 6345 O  O     . HOH   N 6 .   ? 60.92200  -17.25000 44.99500  1.000 22.51183 ? 342 HOH   D O     1 
HETATM 6346 O  O     . HOH   N 6 .   ? 64.86600  -20.21400 27.40900  1.000 29.33419 ? 343 HOH   D O     1 
HETATM 6347 O  O     . HOH   N 6 .   ? 73.44900  8.10200   46.75300  1.000 25.01657 ? 344 HOH   D O     1 
HETATM 6348 O  O     . HOH   N 6 .   ? 87.90100  -3.97700  22.94900  1.000 15.56516 ? 345 HOH   D O     1 
HETATM 6349 O  O     . HOH   N 6 .   ? 69.72000  -6.18900  49.88900  1.000 28.78480 ? 346 HOH   D O     1 
HETATM 6350 O  O     . HOH   N 6 .   ? 82.93400  8.45800   41.72200  1.000 21.91211 ? 347 HOH   D O     1 
HETATM 6351 O  O     . HOH   N 6 .   ? 76.46600  -26.21900 31.96700  1.000 36.41815 ? 348 HOH   D O     1 
HETATM 6352 O  O     . HOH   N 6 .   ? 59.36900  -10.80900 30.15600  1.000 13.80718 ? 349 HOH   D O     1 
HETATM 6353 O  O     . HOH   N 6 .   ? 81.28700  -4.02400  47.46000  1.000 16.15514 ? 350 HOH   D O     1 
HETATM 6354 O  O     . HOH   N 6 .   ? 61.30600  -10.25200 44.50600  1.000 20.32639 ? 351 HOH   D O     1 
HETATM 6355 O  O     . HOH   N 6 .   ? 97.24500  -7.37400  36.49900  1.000 31.02443 ? 352 HOH   D O     1 
HETATM 6356 O  O     . HOH   N 6 .   ? 69.68200  7.77200   48.35800  1.000 35.53408 ? 353 HOH   D O     1 
HETATM 6357 O  O     . HOH   N 6 .   ? 68.01800  -19.24400 41.23800  1.000 25.31839 ? 354 HOH   D O     1 
HETATM 6358 O  O     . HOH   N 6 .   ? 67.11300  -4.31800  54.91100  1.000 32.91055 ? 355 HOH   D O     1 
HETATM 6359 O  O     . HOH   N 6 .   ? 86.99200  3.60000   46.08100  1.000 15.80688 ? 356 HOH   D O     1 
HETATM 6360 O  O     . HOH   N 6 .   ? 87.38400  6.40900   41.55000  1.000 21.38326 ? 357 HOH   D O     1 
HETATM 6361 O  O     . HOH   N 6 .   ? 65.42900  -19.76800 38.70700  1.000 13.41051 ? 358 HOH   D O     1 
HETATM 6362 O  O     . HOH   N 6 .   ? 82.26000  5.63700   20.53400  1.000 26.94851 ? 359 HOH   D O     1 
HETATM 6363 O  O     . HOH   N 6 .   ? 67.78700  -21.71000 30.46400  1.000 25.36296 ? 360 HOH   D O     1 
HETATM 6364 O  O     . HOH   N 6 .   ? 85.21600  5.92300   42.28900  1.000 26.48057 ? 361 HOH   D O     1 
HETATM 6365 O  O     . HOH   N 6 .   ? 60.51400  2.56300   39.79600  1.000 30.47891 ? 362 HOH   D O     1 
HETATM 6366 O  O     . HOH   N 6 .   ? 72.94400  8.87700   42.49200  1.000 28.05020 ? 363 HOH   D O     1 
HETATM 6367 O  O     . HOH   N 6 .   ? 83.74700  -5.10500  48.84000  1.000 26.63828 ? 364 HOH   D O     1 
HETATM 6368 O  O     . HOH   N 6 .   ? 73.23700  -7.33200  53.57100  1.000 26.56618 ? 365 HOH   D O     1 
HETATM 6369 O  O     . HOH   N 6 .   ? 67.04200  -19.02300 47.83200  1.000 28.64094 ? 366 HOH   D O     1 
HETATM 6370 O  O     . HOH   N 6 .   ? 61.471    -8.922    20.712    1.000 30.19149 ? 367 HOH   D O     1 
HETATM 6371 O  O     . HOH   N 6 .   ? 85.04800  -7.34600  50.57900  1.000 27.66973 ? 368 HOH   D O     1 
HETATM 6372 O  O     . HOH   N 6 .   ? 93.81000  -20.98200 46.95100  1.000 28.80821 ? 369 HOH   D O     1 
HETATM 6373 O  O     . HOH   N 6 .   ? 60.11900  -1.55500  32.03200  1.000 28.30893 ? 370 HOH   D O     1 
HETATM 6374 O  O     . HOH   N 6 .   ? 93.48700  -15.93500 39.39400  1.000 33.09724 ? 371 HOH   D O     1 
HETATM 6375 O  O     . HOH   N 6 .   ? 69.34000  1.96000   51.25300  1.000 36.76057 ? 372 HOH   D O     1 
HETATM 6376 O  O     . HOH   N 6 .   ? 72.764    -9.995    19.558    1.000 19.23498 ? 373 HOH   D O     1 
HETATM 6377 O  O     . HOH   N 6 .   ? 75.89400  2.98300   17.10900  1.000 46.65480 ? 374 HOH   D O     1 
HETATM 6378 O  O     . HOH   N 6 .   ? 74.59600  7.39500   41.69000  1.000 22.62328 ? 375 HOH   D O     1 
HETATM 6379 O  O     . HOH   N 6 .   ? 68.19000  4.28400   22.65200  1.000 24.00194 ? 376 HOH   D O     1 
HETATM 6380 O  O     . HOH   N 6 .   ? 72.65100  -26.12900 35.40500  1.000 36.00113 ? 377 HOH   D O     1 
HETATM 6381 O  O     . HOH   N 6 .   ? 68.85400  -2.24700  50.47500  1.000 30.66988 ? 378 HOH   D O     1 
HETATM 6382 O  O     . HOH   N 6 .   ? 68.13700  -21.96700 41.88300  1.000 28.99989 ? 379 HOH   D O     1 
HETATM 6383 O  O     . HOH   N 6 .   ? 91.30600  -17.91600 39.13300  1.000 27.21114 ? 380 HOH   D O     1 
HETATM 6384 O  O     . HOH   N 6 .   ? 78.24300  -10.35400 23.59700  1.000 22.99330 ? 381 HOH   D O     1 
HETATM 6385 O  O     . HOH   N 6 .   ? 64.67400  -0.37700  48.79700  1.000 29.92823 ? 382 HOH   D O     1 
HETATM 6386 O  O     . HOH   N 6 .   ? 71.76300  -19.19700 46.26800  1.000 14.98108 ? 383 HOH   D O     1 
HETATM 6387 O  O     . HOH   N 6 .   ? 87.02700  -3.39100  46.16300  1.000 31.55023 ? 384 HOH   D O     1 
HETATM 6388 O  O     . HOH   N 6 .   ? 88.54900  6.25300   31.06000  1.000 15.44441 ? 385 HOH   D O     1 
HETATM 6389 O  O     . HOH   N 6 .   ? 79.55500  11.04100  27.82200  1.000 32.40976 ? 386 HOH   D O     1 
HETATM 6390 O  O     . HOH   N 6 .   ? 69.85900  9.20900   26.06800  1.000 31.44835 ? 387 HOH   D O     1 
HETATM 6391 O  O     . HOH   N 6 .   ? 92.84100  -12.93600 33.11800  1.000 29.46589 ? 388 HOH   D O     1 
HETATM 6392 O  O     . HOH   N 6 .   ? 57.78100  -2.59200  41.81800  1.000 35.80334 ? 389 HOH   D O     1 
HETATM 6393 O  O     . HOH   N 6 .   ? 72.95300  -3.47600  57.40800  1.000 35.80180 ? 390 HOH   D O     1 
HETATM 6394 O  O     . HOH   N 6 .   ? 75.520    -12.420   22.295    1.000 26.60276 ? 391 HOH   D O     1 
HETATM 6395 O  O     . HOH   N 6 .   ? 67.95300  7.26300   24.29900  1.000 27.22456 ? 392 HOH   D O     1 
HETATM 6396 O  O     . HOH   N 6 .   ? 89.38600  3.65500   44.50200  1.000 12.23774 ? 393 HOH   D O     1 
HETATM 6397 O  O     . HOH   N 6 .   ? 91.81600  4.07900   45.48000  1.000 28.05470 ? 394 HOH   D O     1 
HETATM 6398 O  O     . HOH   N 6 .   ? 75.63500  11.07000  31.09400  1.000 33.83718 ? 395 HOH   D O     1 
HETATM 6399 O  O     . HOH   N 6 .   ? 93.94100  -6.55300  49.04900  1.000 30.51460 ? 396 HOH   D O     1 
HETATM 6400 O  O     . HOH   N 6 .   ? 62.56700  -18.72200 27.47900  1.000 28.95835 ? 397 HOH   D O     1 
HETATM 6401 O  O     . HOH   N 6 .   ? 58.95000  -7.57400  26.47600  1.000 22.92097 ? 398 HOH   D O     1 
HETATM 6402 O  O     . HOH   N 6 .   ? 57.302    -15.572   41.832    1.000 38.79246 ? 399 HOH   D O     1 
HETATM 6403 O  O     . HOH   N 6 .   ? 75.594    -10.913   20.146    1.000 20.36845 ? 400 HOH   D O     1 
HETATM 6404 O  O     . HOH   N 6 .   ? 63.00900  8.89800   42.63000  1.000 23.19667 ? 401 HOH   D O     1 
HETATM 6405 O  O     . HOH   N 6 .   ? 70.96400  -8.16800  46.38400  1.000 19.94514 ? 402 HOH   D O     1 
HETATM 6406 O  O     . HOH   N 6 .   ? 95.32900  -13.00800 45.67300  1.000 33.03237 ? 403 HOH   D O     1 
HETATM 6407 O  O     . HOH   N 6 .   ? 67.022    11.338    46.042    1.000 34.75083 ? 404 HOH   D O     1 
HETATM 6408 O  O     . HOH   N 6 .   ? 53.739    -11.354   36.593    1.000 26.23313 ? 405 HOH   D O     1 
HETATM 6409 O  O     . HOH   N 6 .   ? 75.08900  -9.70300  55.57800  1.000 19.36070 ? 406 HOH   D O     1 
HETATM 6410 O  O     . HOH   N 6 .   ? 75.99000  10.99500  25.51500  1.000 30.57813 ? 407 HOH   D O     1 
HETATM 6411 O  O     . HOH   N 6 .   ? 82.60600  -9.05000  22.90200  1.000 31.90235 ? 408 HOH   D O     1 
HETATM 6412 O  O     . HOH   N 6 .   ? 66.45600  -0.27600  50.39200  1.000 31.27444 ? 409 HOH   D O     1 
HETATM 6413 O  O     . HOH   N 6 .   ? 73.42200  -24.95800 27.38600  1.000 33.85994 ? 410 HOH   D O     1 
HETATM 6414 O  O     . HOH   N 6 .   ? 71.52800  -9.19600  53.15500  1.000 33.67564 ? 411 HOH   D O     1 
HETATM 6415 O  O     . HOH   N 6 .   ? 90.12400  -10.82300 52.97200  1.000 31.13944 ? 412 HOH   D O     1 
HETATM 6416 O  O     . HOH   N 6 .   ? 60.54100  -0.46200  29.72800  1.000 25.13168 ? 413 HOH   D O     1 
HETATM 6417 O  O     . HOH   N 6 .   ? 71.87500  3.74500   48.36100  1.000 19.41976 ? 414 HOH   D O     1 
HETATM 6418 O  O     . HOH   N 6 .   ? 67.39700  -13.20700 49.70900  1.000 27.93047 ? 415 HOH   D O     1 
HETATM 6419 O  O     . HOH   N 6 .   ? 94.68300  -12.97600 35.47900  1.000 29.05510 ? 416 HOH   D O     1 
HETATM 6420 O  O     . HOH   N 6 .   ? 92.42500  -15.16000 31.73600  1.000 33.55532 ? 417 HOH   D O     1 
HETATM 6421 O  O     . HOH   N 6 .   ? 83.98200  7.53800   24.03800  1.000 24.36764 ? 418 HOH   D O     1 
HETATM 6422 O  O     . HOH   N 6 .   ? 59.58600  1.26400   35.34700  1.000 29.72953 ? 419 HOH   D O     1 
HETATM 6423 O  O     . HOH   N 6 .   ? 87.72800  -6.51100  48.48500  1.000 30.25539 ? 420 HOH   D O     1 
HETATM 6424 O  O     . HOH   N 6 .   ? 73.55200  12.93800  35.43000  1.000 44.42859 ? 421 HOH   D O     1 
HETATM 6425 O  O     . HOH   N 6 .   ? 65.42600  4.59800   26.06600  1.000 22.48801 ? 422 HOH   D O     1 
HETATM 6426 O  O     . HOH   N 6 .   ? 66.498    -25.919   40.648    1.000 31.04838 ? 423 HOH   D O     1 
HETATM 6427 O  O     . HOH   N 6 .   ? 94.32900  -15.28500 50.32300  1.000 35.85631 ? 424 HOH   D O     1 
HETATM 6428 O  O     . HOH   N 6 .   ? 72.16900  -5.32800  52.71600  1.000 26.87028 ? 425 HOH   D O     1 
HETATM 6429 O  O     . HOH   N 6 .   ? 72.44200  3.13500   50.78000  1.000 30.69754 ? 426 HOH   D O     1 
HETATM 6430 O  O     . HOH   N 6 .   ? 78.13400  -4.90900  19.40600  1.000 33.14713 ? 427 HOH   D O     1 
HETATM 6431 O  O     . HOH   N 6 .   ? 71.15600  10.88900  30.39600  1.000 28.63510 ? 428 HOH   D O     1 
HETATM 6432 O  O     . HOH   N 6 .   ? 91.112    7.658     45.024    1.000 21.66231 ? 429 HOH   D O     1 
HETATM 6433 O  O     . HOH   N 6 .   ? 88.604    6.604     44.279    1.000 20.56757 ? 430 HOH   D O     1 
HETATM 6434 O  O     . HOH   N 6 .   ? 60.67600  -11.05400 23.43400  1.000 32.97343 ? 431 HOH   D O     1 
HETATM 6435 O  O     . HOH   N 6 .   ? 87.69900  -0.13900  21.66700  1.000 33.06182 ? 432 HOH   D O     1 
HETATM 6436 O  O     . HOH   N 6 .   ? 62.08400  3.43100   28.40200  1.000 23.35738 ? 433 HOH   D O     1 
HETATM 6437 O  O     . HOH   N 6 .   ? 58.06400  -2.90000  31.67400  1.000 27.57912 ? 434 HOH   D O     1 
HETATM 6438 O  O     . HOH   N 6 .   ? 82.54800  -5.99500  18.91500  1.000 37.55381 ? 435 HOH   D O     1 
HETATM 6439 O  O     . HOH   N 6 .   ? 85.527    -17.414   25.575    1.000 31.62209 ? 436 HOH   D O     1 
HETATM 6440 O  O     . HOH   N 6 .   ? 76.86700  -3.07000  18.94500  1.000 31.64751 ? 437 HOH   D O     1 
HETATM 6441 O  O     . HOH   N 6 .   ? 63.59200  -19.45600 46.67100  1.000 30.28582 ? 438 HOH   D O     1 
HETATM 6442 O  O     . HOH   N 6 .   ? 94.22800  -0.88300  29.45500  1.000 29.27335 ? 439 HOH   D O     1 
HETATM 6443 O  O     . HOH   N 6 .   ? 73.24600  -11.95300 23.82000  1.000 23.15944 ? 440 HOH   D O     1 
HETATM 6444 O  O     . HOH   N 6 .   ? 57.74500  -7.47500  28.87900  1.000 23.76673 ? 441 HOH   D O     1 
HETATM 6445 O  O     . HOH   N 6 .   ? 70.60900  -24.37500 26.20400  1.000 36.56509 ? 442 HOH   D O     1 
HETATM 6446 O  O     . HOH   N 6 .   ? 62.32800  -11.48600 48.67800  1.000 39.46925 ? 443 HOH   D O     1 
HETATM 6447 O  O     . HOH   N 6 .   ? 64.40900  2.59600   27.54800  1.000 15.96482 ? 444 HOH   D O     1 
HETATM 6448 O  O     . HOH   N 6 .   ? 58.32800  -11.55300 27.52600  1.000 23.95603 ? 445 HOH   D O     1 
HETATM 6449 O  O     . HOH   N 6 .   ? 73.84500  -11.23600 53.54200  1.000 19.26033 ? 446 HOH   D O     1 
HETATM 6450 O  O     . HOH   N 6 .   ? 79.02300  10.99300  25.10600  1.000 39.42171 ? 447 HOH   D O     1 
HETATM 6451 O  O     . HOH   N 6 .   ? 67.60400  13.47800  36.93800  1.000 33.05485 ? 448 HOH   D O     1 
HETATM 6452 O  O     . HOH   N 6 .   ? 72.54900  -20.98500 24.27200  1.000 23.54491 ? 449 HOH   D O     1 
HETATM 6453 O  O     . HOH   N 6 .   ? 71.66100  -12.22100 50.04700  1.000 14.93853 ? 450 HOH   D O     1 
HETATM 6454 O  O     . HOH   N 6 .   ? 86.41100  -8.41500  21.97400  1.000 28.73546 ? 451 HOH   D O     1 
HETATM 6455 O  O     . HOH   N 6 .   ? 80.88700  -25.51100 36.19900  1.000 33.57923 ? 452 HOH   D O     1 
HETATM 6456 O  O     . HOH   N 6 .   ? 99.08700  -8.55600  35.41900  1.000 32.55915 ? 453 HOH   D O     1 
HETATM 6457 O  O     . HOH   N 6 .   ? 56.00700  -10.95800 32.53100  1.000 29.49166 ? 454 HOH   D O     1 
HETATM 6458 O  O     . HOH   N 6 .   ? 62.04400  6.42700   43.07200  1.000 27.51714 ? 455 HOH   D O     1 
HETATM 6459 O  O     . HOH   N 6 .   ? 79.88500  8.18100   22.88400  1.000 30.70614 ? 456 HOH   D O     1 
HETATM 6460 O  O     . HOH   N 6 .   ? 56.15000  -4.82100  41.79600  1.000 39.60840 ? 457 HOH   D O     1 
HETATM 6461 O  O     . HOH   N 6 .   ? 85.79200  5.97000   24.54900  1.000 29.36163 ? 458 HOH   D O     1 
HETATM 6462 O  O     . HOH   N 6 .   ? 54.87900  -6.44000  40.65300  1.000 34.69922 ? 459 HOH   D O     1 
HETATM 6463 O  O     . HOH   N 6 .   ? 58.69800  1.86700   38.62500  1.000 33.63092 ? 460 HOH   D O     1 
HETATM 6464 O  O     . HOH   N 6 .   ? 82.97800  -24.82200 35.70300  1.000 34.65096 ? 461 HOH   D O     1 
HETATM 6465 O  O     . HOH   N 6 .   ? 57.44400  -0.16100  38.74900  1.000 24.79999 ? 462 HOH   D O     1 
HETATM 6466 O  O     . HOH   N 6 .   ? 95.27700  -15.01700 30.50300  1.000 42.07312 ? 463 HOH   D 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   ? 0.31894 0.51384 0.51776 -0.09129 0.06234  0.01081  0   SER B N     
2    C CA    . SER A 1   ? 0.19078 0.37726 0.38979 -0.08691 0.04857  0.00989  0   SER B CA    
3    C C     . SER A 1   ? 0.30487 0.47753 0.48208 -0.07998 0.04864  0.00596  0   SER B C     
4    O O     . SER A 1   ? 0.38738 0.55535 0.54829 -0.07954 0.05806  0.00416  0   SER B O     
5    C CB    . SER A 1   ? 0.21745 0.38975 0.41263 -0.09554 0.03952  0.01265  0   SER B CB    
6    O OG    . SER A 1   ? 0.13896 0.30275 0.33331 -0.09183 0.02672  0.00999  0   SER B OG    
7    N N     . MET A 2   ? 0.18604 0.35231 0.36250 -0.07510 0.03775  0.00459  1   MET B N     
8    C CA    . MET A 2   ? 0.18093 0.33486 0.33898 -0.06903 0.03719  0.00135  1   MET B CA    
9    C C     . MET A 2   ? 0.12700 0.26684 0.27604 -0.07034 0.02516  0.00225  1   MET B C     
10   O O     . MET A 2   ? 0.16324 0.30223 0.32028 -0.07507 0.01713  0.00367  1   MET B O     
11   C CB    . MET A 2   ? 0.17061 0.33419 0.33856 -0.05808 0.03957  -0.00357 1   MET B CB    
12   C CG    . MET A 2   ? 0.15233 0.32724 0.34048 -0.05292 0.02980  -0.00347 1   MET B CG    
13   S SD    . MET A 2   ? 0.37614 0.55544 0.57264 -0.03861 0.03257  -0.00941 1   MET B SD    
14   C CE    . MET A 2   ? 0.25680 0.45634 0.47434 -0.03715 0.04391  -0.01123 1   MET B CE    
15   N N     . THR A 3   ? 0.09752 0.22561 0.22886 -0.06652 0.02434  0.00065  2   THR B N     
16   C CA    . THR A 3   ? 0.09651 0.21121 0.21657 -0.06688 0.01430  0.00115  2   THR B CA    
17   C C     . THR A 3   ? 0.10320 0.21754 0.22175 -0.05704 0.01174  -0.00236 2   THR B C     
18   O O     . THR A 3   ? 0.15308 0.27697 0.28011 -0.05109 0.01812  -0.00568 2   THR B O     
19   C CB    . THR A 3   ? 0.12078 0.21818 0.21880 -0.07231 0.01515  0.00509  2   THR B CB    
20   O OG1   . THR A 3   ? 0.19555 0.29234 0.28248 -0.07022 0.02369  0.00491  2   THR B OG1   
21   C CG2   . THR A 3   ? 0.11420 0.20775 0.21284 -0.08142 0.01582  0.00920  2   THR B CG2   
22   N N     . GLU A 4   ? 0.09800 0.19731 0.20416 -0.05375 0.00255  -0.00155 3   GLU B N     
23   C CA    . GLU A 4   ? 0.14659 0.24047 0.24779 -0.04368 -0.00108 -0.00333 3   GLU B CA    
24   C C     . GLU A 4   ? 0.14878 0.22309 0.22877 -0.04243 -0.00494 -0.00202 3   GLU B C     
25   O O     . GLU A 4   ? 0.15664 0.22170 0.23013 -0.04771 -0.00915 -0.00070 3   GLU B O     
26   C CB    . GLU A 4   ? 0.15499 0.25740 0.27068 -0.04035 -0.00977 -0.00396 3   GLU B CB    
27   C CG    . GLU A 4   ? 0.13106 0.22836 0.24253 -0.03069 -0.01394 -0.00436 3   GLU B CG    
28   C CD    . GLU A 4   ? 0.18128 0.28956 0.30952 -0.02779 -0.02302 -0.00335 3   GLU B CD    
29   O OE1   . GLU A 4   ? 0.16831 0.29182 0.31591 -0.03234 -0.02475 -0.00311 3   GLU B OE1   
30   O OE2   . GLU A 4   ? 0.21872 0.32109 0.34150 -0.02145 -0.02892 -0.00204 3   GLU B OE2   
31   N N     . TYR A 5   ? 0.07494 0.14296 0.14574 -0.03554 -0.00305 -0.00272 4   TYR B N     
32   C CA    . TYR A 5   ? 0.12014 0.17252 0.17413 -0.03359 -0.00489 -0.00155 4   TYR B CA    
33   C C     . TYR A 5   ? 0.09366 0.14188 0.14303 -0.02586 -0.00727 -0.00272 4   TYR B C     
34   O O     . TYR A 5   ? 0.11500 0.16920 0.17004 -0.02150 -0.00457 -0.00377 4   TYR B O     
35   C CB    . TYR A 5   ? 0.08430 0.13304 0.12994 -0.03554 0.00101  0.00046  4   TYR B CB    
36   C CG    . TYR A 5   ? 0.13498 0.18702 0.18238 -0.04409 0.00428  0.00304  4   TYR B CG    
37   C CD1   . TYR A 5   ? 0.17498 0.21737 0.21834 -0.04942 0.00045  0.00611  4   TYR B CD1   
38   C CD2   . TYR A 5   ? 0.08464 0.14833 0.13713 -0.04736 0.01188  0.00227  4   TYR B CD2   
39   C CE1   . TYR A 5   ? 0.17042 0.21462 0.21488 -0.05845 0.00334  0.00980  4   TYR B CE1   
40   C CE2   . TYR A 5   ? 0.09293 0.16007 0.14551 -0.05651 0.01590  0.00534  4   TYR B CE2   
41   C CZ    . TYR A 5   ? 0.11572 0.17292 0.16412 -0.06232 0.01122  0.00987  4   TYR B CZ    
42   O OH    . TYR A 5   ? 0.13615 0.19549 0.18410 -0.07237 0.01502  0.01415  4   TYR B OH    
43   N N     . LYS A 6   ? 0.09459 0.13155 0.13328 -0.02442 -0.01152 -0.00272 5   LYS B N     
44   C CA    . LYS A 6   ? 0.13845 0.17045 0.17017 -0.01839 -0.01270 -0.00305 5   LYS B CA    
45   C C     . LYS A 6   ? 0.11189 0.13708 0.13559 -0.01646 -0.00826 -0.00214 5   LYS B C     
46   O O     . LYS A 6   ? 0.09675 0.11363 0.11419 -0.01752 -0.00840 -0.00183 5   LYS B O     
47   C CB    . LYS A 6   ? 0.14616 0.17119 0.16983 -0.01852 -0.01888 -0.00422 5   LYS B CB    
48   C CG    . LYS A 6   ? 0.23236 0.26498 0.26424 -0.02152 -0.02569 -0.00448 5   LYS B CG    
49   C CD    . LYS A 6   ? 0.39327 0.41709 0.41262 -0.02360 -0.03252 -0.00638 5   LYS B CD    
50   C CE    . LYS A 6   ? 0.29358 0.30815 0.30743 -0.02934 -0.03287 -0.00938 5   LYS B CE    
51   N NZ    . LYS A 6   ? 0.40672 0.42982 0.43379 -0.03616 -0.03643 -0.00905 5   LYS B NZ    
52   N N     . LEU A 7   ? 0.12896 0.15765 0.15441 -0.01374 -0.00467 -0.00184 6   LEU B N     
53   C CA    . LEU A 7   ? 0.12724 0.15171 0.14691 -0.01246 -0.00171 -0.00071 6   LEU B CA    
54   C C     . LEU A 7   ? 0.10895 0.12961 0.12454 -0.00813 -0.00195 -0.00064 6   LEU B C     
55   O O     . LEU A 7   ? 0.10200 0.12436 0.11993 -0.00595 -0.00324 -0.00087 6   LEU B O     
56   C CB    . LEU A 7   ? 0.14126 0.17127 0.16347 -0.01434 0.00238  -0.00099 6   LEU B CB    
57   C CG    . LEU A 7   ? 0.09319 0.12929 0.11938 -0.01947 0.00445  -0.00119 6   LEU B CG    
58   C CD1   . LEU A 7   ? 0.12590 0.16652 0.15074 -0.02178 0.00973  -0.00269 6   LEU B CD1   
59   C CD2   . LEU A 7   ? 0.10494 0.13581 0.12676 -0.02345 0.00239  0.00205  6   LEU B CD2   
60   N N     . VAL A 8   ? 0.08838 0.10420 0.09907 -0.00693 -0.00064 0.00033  7   VAL B N     
61   C CA    . VAL A 8   ? 0.07324 0.08612 0.07987 -0.00400 0.00058  0.00076  7   VAL B CA    
62   C C     . VAL A 8   ? 0.06762 0.08222 0.07638 -0.00395 0.00338  0.00225  7   VAL B C     
63   O O     . VAL A 8   ? 0.10835 0.12336 0.11895 -0.00475 0.00348  0.00340  7   VAL B O     
64   C CB    . VAL A 8   ? 0.07976 0.08637 0.07933 -0.00279 0.00046  -0.00049 7   VAL B CB    
65   C CG1   . VAL A 8   ? 0.08833 0.09294 0.08230 -0.00084 0.00307  0.00030  7   VAL B CG1   
66   C CG2   . VAL A 8   ? 0.10374 0.10864 0.10045 -0.00456 -0.00398 -0.00228 7   VAL B CG2   
67   N N     . VAL A 9   ? 0.10233 0.11760 0.11157 -0.00346 0.00469  0.00277  8   VAL B N     
68   C CA    . VAL A 9   ? 0.09172 0.10914 0.10353 -0.00477 0.00645  0.00391  8   VAL B CA    
69   C C     . VAL A 9   ? 0.08705 0.10324 0.09787 -0.00336 0.00895  0.00551  8   VAL B C     
70   O O     . VAL A 9   ? 0.09437 0.10725 0.10130 -0.00271 0.00989  0.00625  8   VAL B O     
71   C CB    . VAL A 9   ? 0.10541 0.12312 0.11885 -0.00639 0.00690  0.00252  8   VAL B CB    
72   C CG1   . VAL A 9   ? 0.09888 0.11880 0.11381 -0.00964 0.00738  0.00296  8   VAL B CG1   
73   C CG2   . VAL A 9   ? 0.06412 0.08402 0.07904 -0.00726 0.00654  -0.00007 8   VAL B CG2   
74   N N     . VAL A 10  ? 0.10806 0.12745 0.12332 -0.00304 0.01018  0.00667  9   VAL B N     
75   C CA    . VAL A 10  ? 0.12427 0.14495 0.14137 -0.00157 0.01439  0.00764  9   VAL B CA    
76   C C     . VAL A 10  ? 0.07682 0.10491 0.10399 -0.00355 0.01448  0.00999  9   VAL B C     
77   O O     . VAL A 10  ? 0.07758 0.10871 0.10808 -0.00590 0.01038  0.01083  9   VAL B O     
78   C CB    . VAL A 10  ? 0.08155 0.09970 0.09752 0.00202  0.01670  0.00581  9   VAL B CB    
79   C CG1   . VAL A 10  ? 0.08008 0.09106 0.08537 0.00232  0.01487  0.00322  9   VAL B CG1   
80   C CG2   . VAL A 10  ? 0.08147 0.10198 0.10615 0.00331  0.01426  0.00681  9   VAL B CG2   
81   N N     . GLY A 11  ? 0.12957 0.16117 0.16096 -0.00351 0.01913  0.01121  10  GLY B N     
82   C CA    . GLY A 11  ? 0.09152 0.13217 0.13506 -0.00612 0.01901  0.01376  10  GLY B CA    
83   C C     . GLY A 11  ? 0.10758 0.14960 0.15191 -0.00945 0.02369  0.01528  10  GLY B C     
84   O O     . GLY A 11  ? 0.11584 0.15003 0.14932 -0.01004 0.02582  0.01509  10  GLY B O     
85   N N     . ALA A 12  ? 0.10500 0.15713 0.16280 -0.01224 0.02456  0.01764  11  ALA B N     
86   C CA    . ALA A 12  ? 0.13495 0.18964 0.19554 -0.01639 0.03009  0.01977  11  ALA B CA    
87   C C     . ALA A 12  ? 0.09436 0.13896 0.14511 -0.02152 0.02779  0.02023  11  ALA B C     
88   O O     . ALA A 12  ? 0.07921 0.11873 0.12616 -0.02292 0.02182  0.01832  11  ALA B O     
89   C CB    . ALA A 12  ? 0.09949 0.16904 0.17984 -0.01956 0.02998  0.02239  11  ALA B CB    
90   N N     . CYS A 13  ? 0.09991 0.14112 0.14676 -0.02448 0.03327  0.02286  12  CYS B N     
91   C CA    . CYS A 13  ? 0.09694 0.12690 0.13666 -0.02911 0.03117  0.02431  12  CYS B CA    
92   C C     . CYS A 13  ? 0.10701 0.13913 0.15569 -0.03528 0.02627  0.02332  12  CYS B C     
93   O O     . CYS A 13  ? 0.09385 0.13814 0.15599 -0.03927 0.02648  0.02457  12  CYS B O     
94   C CB    . CYS A 13  ? 0.11444 0.14102 0.14939 -0.03274 0.03792  0.02917  12  CYS B CB    
95   S SG    . CYS A 13  ? 0.14695 0.19002 0.19916 -0.03864 0.04531  0.03218  12  CYS B SG    
96   N N     . GLY A 14  ? 0.09892 0.11939 0.14063 -0.03625 0.02186  0.02067  13  GLY B N     
97   C CA    . GLY A 14  ? 0.10285 0.12130 0.14861 -0.04300 0.01765  0.01814  13  GLY B CA    
98   C C     . GLY A 14  ? 0.10134 0.12572 0.14821 -0.04311 0.01201  0.01377  13  GLY B C     
99   O O     . GLY A 14  ? 0.10287 0.12484 0.14986 -0.04956 0.00808  0.01058  13  GLY B O     
100  N N     . VAL A 15  ? 0.10317 0.13392 0.14924 -0.03703 0.01128  0.01357  14  VAL B N     
101  C CA    . VAL A 15  ? 0.08469 0.12157 0.13131 -0.03842 0.00550  0.01146  14  VAL B CA    
102  C C     . VAL A 15  ? 0.13926 0.16641 0.17418 -0.03865 0.00368  0.00589  14  VAL B C     
103  O O     . VAL A 15  ? 0.10433 0.13408 0.13581 -0.04284 -0.00089 0.00345  14  VAL B O     
104  C CB    . VAL A 15  ? 0.08750 0.13347 0.13861 -0.03251 0.00493  0.01401  14  VAL B CB    
105  C CG1   . VAL A 15  ? 0.07400 0.13158 0.13972 -0.03180 0.00757  0.01833  14  VAL B CG1   
106  C CG2   . VAL A 15  ? 0.07291 0.11171 0.11536 -0.02536 0.00819  0.01270  14  VAL B CG2   
107  N N     . GLY A 16  ? 0.15820 0.17508 0.18711 -0.03432 0.00712  0.00398  15  GLY B N     
108  C CA    . GLY A 16  ? 0.09470 0.10356 0.11608 -0.03405 0.00702  -0.00204 15  GLY B CA    
109  C C     . GLY A 16  ? 0.08846 0.09746 0.10667 -0.02734 0.00836  -0.00268 15  GLY B C     
110  O O     . GLY A 16  ? 0.09161 0.09899 0.10528 -0.02740 0.00877  -0.00745 15  GLY B O     
111  N N     . LYS A 17  ? 0.08236 0.09349 0.10258 -0.02239 0.00949  0.00162  16  LYS B N     
112  C CA    . LYS A 17  ? 0.09290 0.10408 0.11073 -0.01701 0.00981  0.00118  16  LYS B CA    
113  C C     . LYS A 17  ? 0.11869 0.12263 0.13601 -0.01452 0.01087  -0.00220 16  LYS B C     
114  O O     . LYS A 17  ? 0.08192 0.08783 0.09902 -0.01288 0.01127  -0.00541 16  LYS B O     
115  C CB    . LYS A 17  ? 0.07509 0.08733 0.09288 -0.01329 0.01077  0.00538  16  LYS B CB    
116  C CG    . LYS A 17  ? 0.07804 0.09795 0.09964 -0.01387 0.01122  0.00801  16  LYS B CG    
117  C CD    . LYS A 17  ? 0.10205 0.12126 0.12115 -0.01001 0.01395  0.00998  16  LYS B CD    
118  C CE    . LYS A 17  ? 0.07970 0.09477 0.09612 -0.01121 0.01717  0.01275  16  LYS B CE    
119  N NZ    . LYS A 17  ? 0.08128 0.10085 0.10515 -0.01586 0.01916  0.01470  16  LYS B NZ    
120  N N     . SER A 18  ? 0.11881 0.11454 0.13749 -0.01407 0.01153  -0.00093 17  SER B N     
121  C CA    . SER A 18  ? 0.15923 0.14729 0.18078 -0.01029 0.01200  -0.00335 17  SER B CA    
122  C C     . SER A 18  ? 0.13917 0.12442 0.16148 -0.01258 0.01434  -0.01111 17  SER B C     
123  O O     . SER A 18  ? 0.13416 0.11989 0.16001 -0.00896 0.01623  -0.01542 17  SER B O     
124  C CB    . SER A 18  ? 0.12126 0.09909 0.14365 -0.00950 0.01133  0.00144  17  SER B CB    
125  O OG    . SER A 18  ? 0.11732 0.09705 0.13592 -0.00746 0.00979  0.00800  17  SER B OG    
126  N N     . ALA A 19  ? 0.12555 0.10836 0.14468 -0.01907 0.01452  -0.01345 18  ALA B N     
127  C CA    . ALA A 19  ? 0.16391 0.14280 0.17983 -0.02274 0.01688  -0.02207 18  ALA B CA    
128  C C     . ALA A 19  ? 0.13417 0.12226 0.14570 -0.02304 0.01836  -0.02563 18  ALA B C     
129  O O     . ALA A 19  ? 0.18061 0.16644 0.19168 -0.02197 0.02282  -0.03286 18  ALA B O     
130  C CB    . ALA A 19  ? 0.12406 0.10067 0.13574 -0.03147 0.01487  -0.02324 18  ALA B CB    
131  N N     . LEU A 20  ? 0.10226 0.10035 0.11132 -0.02428 0.01537  -0.02048 19  LEU B N     
132  C CA    . LEU A 20  ? 0.09958 0.10523 0.10419 -0.02510 0.01634  -0.02190 19  LEU B CA    
133  C C     . LEU A 20  ? 0.15067 0.15780 0.16168 -0.01886 0.01964  -0.02330 19  LEU B C     
134  O O     . LEU A 20  ? 0.14068 0.15025 0.15030 -0.01964 0.02410  -0.02873 19  LEU B O     
135  C CB    . LEU A 20  ? 0.10998 0.12362 0.11306 -0.02652 0.01182  -0.01501 19  LEU B CB    
136  C CG    . LEU A 20  ? 0.10451 0.12079 0.10332 -0.03326 0.00746  -0.01324 19  LEU B CG    
137  C CD1   . LEU A 20  ? 0.10079 0.12431 0.10404 -0.03189 0.00321  -0.00563 19  LEU B CD1   
138  C CD2   . LEU A 20  ? 0.17251 0.18933 0.15939 -0.04029 0.00749  -0.01802 19  LEU B CD2   
139  N N     . THR A 21  ? 0.12647 0.13274 0.14463 -0.01318 0.01762  -0.01854 20  THR B N     
140  C CA    . THR A 21  ? 0.15039 0.15970 0.17657 -0.00769 0.01882  -0.01904 20  THR B CA    
141  C C     . THR A 21  ? 0.13397 0.13857 0.16745 -0.00460 0.02338  -0.02556 20  THR B C     
142  O O     . THR A 21  ? 0.12577 0.13625 0.16553 -0.00268 0.02741  -0.02969 20  THR B O     
143  C CB    . THR A 21  ? 0.10395 0.11227 0.13355 -0.00333 0.01429  -0.01242 20  THR B CB    
144  O OG1   . THR A 21  ? 0.19452 0.20667 0.21808 -0.00558 0.01172  -0.00819 20  THR B OG1   
145  C CG2   . THR A 21  ? 0.11542 0.12833 0.15449 0.00163  0.01335  -0.01224 20  THR B CG2   
146  N N     . ILE A 22  ? 0.14045 0.13420 0.17443 -0.00424 0.02345  -0.02684 21  ILE B N     
147  C CA    . ILE A 22  ? 0.17184 0.15828 0.21472 0.00004  0.02775  -0.03316 21  ILE B CA    
148  C C     . ILE A 22  ? 0.17269 0.16028 0.21056 -0.00393 0.03515  -0.04360 21  ILE B C     
149  O O     . ILE A 22  ? 0.19781 0.18564 0.24520 0.00055  0.04132  -0.05039 21  ILE B O     
150  C CB    . ILE A 22  ? 0.19949 0.17138 0.24329 0.00059  0.02541  -0.03096 21  ILE B CB    
151  C CG1   . ILE A 22  ? 0.18254 0.15352 0.23098 0.00524  0.01923  -0.02066 21  ILE B CG1   
152  C CG2   . ILE A 22  ? 0.18187 0.14251 0.23367 0.00414  0.03034  -0.03894 21  ILE B CG2   
153  C CD1   . ILE A 22  ? 0.26559 0.22520 0.30966 0.00249  0.01640  -0.01524 21  ILE B CD1   
154  N N     . GLN A 23  ? 0.14958 0.13897 0.17274 -0.01237 0.03477  -0.04491 22  GLN B N     
155  C CA    . GLN A 23  ? 0.20609 0.19780 0.21978 -0.01774 0.04133  -0.05390 22  GLN B CA    
156  C C     . GLN A 23  ? 0.23712 0.24156 0.25468 -0.01613 0.04548  -0.05398 22  GLN B C     
157  O O     . GLN A 23  ? 0.22564 0.23216 0.24573 -0.01541 0.05425  -0.06249 22  GLN B O     
158  C CB    . GLN A 23  ? 0.17689 0.16899 0.17332 -0.02776 0.03745  -0.05295 22  GLN B CB    
159  C CG    . GLN A 23  ? 0.22308 0.20310 0.21230 -0.03302 0.03736  -0.05923 22  GLN B CG    
160  C CD    . GLN A 23  ? 0.24036 0.21381 0.22246 -0.03552 0.04631  -0.07270 22  GLN B CD    
161  O OE1   . GLN A 23  ? 0.21672 0.19526 0.20282 -0.03171 0.05423  -0.07769 22  GLN B OE1   
162  N NE2   . GLN A 23  ? 0.19396 0.15626 0.16576 -0.04247 0.04565  -0.07932 22  GLN B NE2   
163  N N     . LEU A 24  ? 0.16624 0.17915 0.18497 -0.01587 0.04002  -0.04506 23  LEU B N     
164  C CA    . LEU A 24  ? 0.17091 0.19535 0.19405 -0.01565 0.04345  -0.04456 23  LEU B CA    
165  C C     . LEU A 24  ? 0.21208 0.24021 0.25481 -0.00753 0.04776  -0.04781 23  LEU B C     
166  O O     . LEU A 24  ? 0.23275 0.26897 0.28081 -0.00788 0.05584  -0.05339 23  LEU B O     
167  C CB    . LEU A 24  ? 0.20568 0.23560 0.22729 -0.01671 0.03622  -0.03488 23  LEU B CB    
168  C CG    . LEU A 24  ? 0.15251 0.19324 0.17839 -0.01816 0.03889  -0.03354 23  LEU B CG    
169  C CD1   . LEU A 24  ? 0.16764 0.21138 0.17825 -0.02707 0.04225  -0.03421 23  LEU B CD1   
170  C CD2   . LEU A 24  ? 0.15631 0.19923 0.18706 -0.01592 0.03152  -0.02562 23  LEU B CD2   
171  N N     . ILE A 25  ? 0.14016 0.16304 0.19435 -0.00042 0.04252  -0.04399 24  ILE B N     
172  C CA    . ILE A 25  ? 0.21491 0.24252 0.29020 0.00800  0.04345  -0.04439 24  ILE B CA    
173  C C     . ILE A 25  ? 0.23059 0.25165 0.31542 0.01270  0.05139  -0.05389 24  ILE B C     
174  O O     . ILE A 25  ? 0.21743 0.24701 0.31870 0.01730  0.05809  -0.05904 24  ILE B O     
175  C CB    . ILE A 25  ? 0.18324 0.20719 0.26457 0.01308  0.03323  -0.03503 24  ILE B CB    
176  C CG1   . ILE A 25  ? 0.17165 0.20141 0.24447 0.00912  0.02667  -0.02750 24  ILE B CG1   
177  C CG2   . ILE A 25  ? 0.19152 0.21940 0.29581 0.02218  0.03202  -0.03438 24  ILE B CG2   
178  C CD1   . ILE A 25  ? 0.22064 0.26457 0.30104 0.00769  0.02790  -0.02737 24  ILE B CD1   
179  N N     . GLN A 26  ? 0.21487 0.22061 0.29167 0.01186  0.05100  -0.05658 25  GLN B N     
180  C CA    . GLN A 26  ? 0.21346 0.20841 0.30110 0.01771  0.05691  -0.06485 25  GLN B CA    
181  C C     . GLN A 26  ? 0.23043 0.21698 0.30330 0.01126  0.06581  -0.07705 25  GLN B C     
182  O O     . GLN A 26  ? 0.26651 0.24340 0.34551 0.01507  0.07037  -0.08375 25  GLN B O     
183  C CB    . GLN A 26  ? 0.18995 0.17046 0.28263 0.02243  0.04873  -0.05795 25  GLN B CB    
184  C CG    . GLN A 26  ? 0.20735 0.19473 0.31278 0.02867  0.03959  -0.04633 25  GLN B CG    
185  C CD    . GLN A 26  ? 0.29476 0.26764 0.40058 0.03154  0.03128  -0.03777 25  GLN B CD    
186  O OE1   . GLN A 26  ? 0.36669 0.32405 0.46505 0.02880  0.03239  -0.04014 25  GLN B OE1   
187  N NE2   . GLN A 26  ? 0.31566 0.29327 0.42884 0.03594  0.02256  -0.02741 25  GLN B NE2   
188  N N     . ASN A 27  ? 0.18945 0.17955 0.24084 0.00083  0.06570  -0.07743 26  ASN B N     
189  C CA    . ASN A 27  ? 0.27386 0.25727 0.30677 -0.00748 0.07275  -0.08856 26  ASN B CA    
190  C C     . ASN A 27  ? 0.22993 0.19422 0.25963 -0.00794 0.07120  -0.09311 26  ASN B C     
191  O O     . ASN A 27  ? 0.29159 0.24913 0.31708 -0.00907 0.07660  -0.10113 26  ASN B O     
192  C CB    . ASN A 27  ? 0.23502 0.22644 0.26997 -0.00711 0.08173  -0.09447 26  ASN B CB    
193  C CG    . ASN A 27  ? 0.43710 0.44630 0.47261 -0.00940 0.08327  -0.08969 26  ASN B CG    
194  O OD1   . ASN A 27  ? 0.50750 0.52109 0.52359 -0.01902 0.08342  -0.08873 26  ASN B OD1   
195  N ND2   . ASN A 27  ? 0.43074 0.45001 0.48872 -0.00109 0.08326  -0.08562 26  ASN B ND2   
196  N N     . HIS A 28  ? 0.25646 0.21316 0.28757 -0.00770 0.06202  -0.08490 27  HIS B N     
197  C CA    . HIS A 28  ? 0.27551 0.21388 0.30044 -0.01163 0.06005  -0.08879 27  HIS B CA    
198  C C     . HIS A 28  ? 0.22701 0.16563 0.24627 -0.01663 0.04917  -0.07683 27  HIS B C     
199  O O     . HIS A 28  ? 0.24784 0.19867 0.26970 -0.01494 0.04382  -0.06621 27  HIS B O     
200  C CB    . HIS A 28  ? 0.31015 0.23491 0.35242 -0.00205 0.06216  -0.09101 27  HIS B CB    
201  C CG    . HIS A 28  ? 0.31366 0.23906 0.37464 0.00747  0.05645  -0.08011 27  HIS B CG    
202  N ND1   . HIS A 28  ? 0.40497 0.32188 0.46521 0.00620  0.04756  -0.06949 27  HIS B ND1   
203  C CD2   . HIS A 28  ? 0.40490 0.34025 0.48451 0.01758  0.05690  -0.07624 27  HIS B CD2   
204  C CE1   . HIS A 28  ? 0.42669 0.34729 0.50124 0.01480  0.04266  -0.05951 27  HIS B CE1   
205  N NE2   . HIS A 28  ? 0.41969 0.35165 0.50687 0.02187  0.04733  -0.06329 27  HIS B NE2   
206  N N     . PHE A 29  ? 0.23918 0.16413 0.25113 -0.02327 0.04658  -0.07939 28  PHE B N     
207  C CA    . PHE A 29  ? 0.23485 0.16059 0.24280 -0.02934 0.03777  -0.06946 28  PHE B CA    
208  C C     . PHE A 29  ? 0.29419 0.20053 0.30655 -0.03071 0.03640  -0.07039 28  PHE B C     
209  O O     . PHE A 29  ? 0.33113 0.22252 0.34096 -0.03253 0.04125  -0.08193 28  PHE B O     
210  C CB    . PHE A 29  ? 0.25931 0.19325 0.25049 -0.04090 0.03451  -0.07096 28  PHE B CB    
211  C CG    . PHE A 29  ? 0.23599 0.16981 0.22563 -0.04842 0.02647  -0.06357 28  PHE B CG    
212  C CD1   . PHE A 29  ? 0.21601 0.16287 0.21058 -0.04706 0.02110  -0.05142 28  PHE B CD1   
213  C CD2   . PHE A 29  ? 0.30058 0.22173 0.28465 -0.05730 0.02486  -0.06951 28  PHE B CD2   
214  C CE1   . PHE A 29  ? 0.21679 0.16601 0.21283 -0.05364 0.01524  -0.04507 28  PHE B CE1   
215  C CE2   . PHE A 29  ? 0.26090 0.18453 0.24646 -0.06488 0.01779  -0.06248 28  PHE B CE2   
216  C CZ    . PHE A 29  ? 0.21959 0.15832 0.21212 -0.06271 0.01343  -0.05010 28  PHE B CZ    
217  N N     . VAL A 30  ? 0.33225 0.23782 0.35043 -0.03037 0.03046  -0.05859 29  VAL B N     
218  C CA    . VAL A 30  ? 0.34051 0.22803 0.36191 -0.03379 0.02848  -0.05707 29  VAL B CA    
219  C C     . VAL A 30  ? 0.29350 0.18810 0.31105 -0.04290 0.02247  -0.04814 29  VAL B C     
220  O O     . VAL A 30  ? 0.28592 0.19721 0.30362 -0.04183 0.01973  -0.03960 29  VAL B O     
221  C CB    . VAL A 30  ? 0.40870 0.28464 0.44370 -0.02371 0.02823  -0.05026 29  VAL B CB    
222  C CG1   . VAL A 30  ? 0.39641 0.26177 0.44027 -0.01465 0.03446  -0.06037 29  VAL B CG1   
223  C CG2   . VAL A 30  ? 0.36550 0.25648 0.40433 -0.01795 0.02433  -0.03732 29  VAL B CG2   
224  N N     . ASP A 31  ? 0.32999 0.21125 0.34576 -0.05185 0.02089  -0.05053 30  ASP B N     
225  C CA    . ASP A 31  ? 0.33084 0.21912 0.34651 -0.06145 0.01587  -0.04254 30  ASP B CA    
226  C C     . ASP A 31  ? 0.32062 0.20916 0.34434 -0.05768 0.01484  -0.02887 30  ASP B C     
227  O O     . ASP A 31  ? 0.27206 0.17376 0.29734 -0.06262 0.01250  -0.02073 30  ASP B O     
228  C CB    . ASP A 31  ? 0.41269 0.28595 0.42508 -0.07307 0.01430  -0.04937 30  ASP B CB    
229  C CG    . ASP A 31  ? 0.47774 0.35915 0.47847 -0.07968 0.01191  -0.05879 30  ASP B CG    
230  O OD1   . ASP A 31  ? 0.44019 0.34042 0.43761 -0.08319 0.00901  -0.05603 30  ASP B OD1   
231  O OD2   . ASP A 31  ? 0.48211 0.35091 0.47654 -0.08113 0.01262  -0.06831 30  ASP B OD2   
232  N N     . GLU A 32  ? 0.31056 0.18443 0.33949 -0.04948 0.01655  -0.02610 31  GLU B N     
233  C CA    . GLU A 32  ? 0.30859 0.17957 0.34152 -0.04753 0.01506  -0.01264 31  GLU B CA    
234  C C     . GLU A 32  ? 0.25438 0.14611 0.28576 -0.04273 0.01439  -0.00498 31  GLU B C     
235  O O     . GLU A 32  ? 0.28730 0.18868 0.31814 -0.03543 0.01495  -0.00844 31  GLU B O     
236  C CB    . GLU A 32  ? 0.41478 0.26557 0.45355 -0.03892 0.01532  -0.01065 31  GLU B CB    
237  C CG    . GLU A 32  ? 0.39768 0.24121 0.43755 -0.03822 0.01282  0.00431  31  GLU B CG    
238  C CD    . GLU A 32  ? 0.48373 0.30253 0.53033 -0.03190 0.01140  0.00676  31  GLU B CD    
239  O OE1   . GLU A 32  ? 0.60137 0.41660 0.65383 -0.02224 0.01224  -0.00104 31  GLU B OE1   
240  O OE2   . GLU A 32  ? 0.48221 0.28962 0.52490 -0.03592 0.00890  0.01646  31  GLU B OE2   
241  N N     . TYR A 33  ? 0.25871 0.15706 0.28947 -0.04750 0.01393  0.00481  32  TYR B N     
242  C CA    . TYR A 33  ? 0.19969 0.11578 0.22814 -0.04377 0.01425  0.01118  32  TYR B CA    
243  C C     . TYR A 33  ? 0.20950 0.11813 0.23561 -0.03680 0.01346  0.01992  32  TYR B C     
244  O O     . TYR A 33  ? 0.20313 0.09935 0.22814 -0.04012 0.01332  0.02775  32  TYR B O     
245  C CB    . TYR A 33  ? 0.19314 0.12157 0.22309 -0.05252 0.01554  0.01600  32  TYR B CB    
246  C CG    . TYR A 33  ? 0.20732 0.15288 0.23568 -0.04947 0.01753  0.02176  32  TYR B CG    
247  C CD1   . TYR A 33  ? 0.14934 0.10112 0.17365 -0.04045 0.01696  0.02097  32  TYR B CD1   
248  C CD2   . TYR A 33  ? 0.20020 0.15572 0.23220 -0.05617 0.02062  0.02736  32  TYR B CD2   
249  C CE1   . TYR A 33  ? 0.15109 0.11616 0.17313 -0.03829 0.01925  0.02497  32  TYR B CE1   
250  C CE2   . TYR A 33  ? 0.15047 0.12054 0.18167 -0.05327 0.02399  0.03110  32  TYR B CE2   
251  C CZ    . TYR A 33  ? 0.16465 0.13821 0.18989 -0.04433 0.02324  0.02961  32  TYR B CZ    
252  O OH    . TYR A 33  ? 0.13407 0.11999 0.15798 -0.04207 0.02722  0.03220  32  TYR B OH    
253  N N     . ASP A 34  ? 0.17365 0.08947 0.19858 -0.02803 0.01224  0.01917  33  ASP B N     
254  C CA    . ASP A 34  ? 0.18061 0.09222 0.20220 -0.02198 0.00966  0.02779  33  ASP B CA    
255  C C     . ASP A 34  ? 0.16458 0.09254 0.17933 -0.02115 0.01045  0.03085  33  ASP B C     
256  O O     . ASP A 34  ? 0.15166 0.08960 0.16723 -0.01590 0.00945  0.02631  33  ASP B O     
257  C CB    . ASP A 34  ? 0.18086 0.08662 0.20911 -0.01247 0.00669  0.02429  33  ASP B CB    
258  C CG    . ASP A 34  ? 0.22306 0.12292 0.24942 -0.00671 0.00154  0.03445  33  ASP B CG    
259  O OD1   . ASP A 34  ? 0.19713 0.09443 0.21375 -0.01083 0.00066  0.04431  33  ASP B OD1   
260  O OD2   . ASP A 34  ? 0.27218 0.17097 0.30688 0.00166  -0.00173 0.03273  33  ASP B OD2   
261  N N     . PRO A 35  ? 0.16891 0.09947 0.17690 -0.02640 0.01296  0.03808  34  PRO B N     
262  C CA    . PRO A 35  ? 0.15791 0.10356 0.15994 -0.02591 0.01554  0.03877  34  PRO B CA    
263  C C     . PRO A 35  ? 0.16469 0.11124 0.15979 -0.01893 0.01170  0.04053  34  PRO B C     
264  O O     . PRO A 35  ? 0.17818 0.11434 0.16806 -0.01687 0.00762  0.04716  34  PRO B O     
265  C CB    . PRO A 35  ? 0.16895 0.11427 0.16526 -0.03313 0.02040  0.04636  34  PRO B CB    
266  C CG    . PRO A 35  ? 0.18041 0.11443 0.18321 -0.03962 0.02053  0.04777  34  PRO B CG    
267  C CD    . PRO A 35  ? 0.18591 0.10555 0.19205 -0.03376 0.01475  0.04528  34  PRO B CD    
268  N N     . THR A 36  ? 0.14215 0.10097 0.13746 -0.01591 0.01220  0.03515  35  THR B N     
269  C CA    . THR A 36  ? 0.13923 0.10033 0.13067 -0.01004 0.00776  0.03464  35  THR B CA    
270  C C     . THR A 36  ? 0.17212 0.13331 0.14873 -0.01115 0.00801  0.04026  35  THR B C     
271  O O     . THR A 36  ? 0.15149 0.11739 0.12243 -0.01509 0.01418  0.04078  35  THR B O     
272  C CB    . THR A 36  ? 0.12580 0.09836 0.12292 -0.00781 0.00849  0.02671  35  THR B CB    
273  O OG1   . THR A 36  ? 0.11714 0.08895 0.12445 -0.00750 0.00839  0.02126  35  THR B OG1   
274  C CG2   . THR A 36  ? 0.11925 0.09544 0.11324 -0.00326 0.00417  0.02579  35  THR B CG2   
275  N N     . ILE A 37  ? 0.16616 0.12266 0.13660 -0.00783 0.00129  0.04422  36  ILE B N     
276  C CA    . ILE A 37  ? 0.16654 0.12451 0.12034 -0.00900 0.00041  0.04690  36  ILE B CA    
277  C C     . ILE A 37  ? 0.15862 0.12548 0.11571 -0.00538 -0.00200 0.03967  36  ILE B C     
278  O O     . ILE A 37  ? 0.15565 0.12876 0.10843 -0.00652 0.00293  0.03475  36  ILE B O     
279  C CB    . ILE A 37  ? 0.18747 0.13512 0.12993 -0.00917 -0.00721 0.05671  36  ILE B CB    
280  C CG1   . ILE A 37  ? 0.21515 0.15220 0.15241 -0.01410 -0.00425 0.06518  36  ILE B CG1   
281  C CG2   . ILE A 37  ? 0.19872 0.14816 0.12148 -0.01092 -0.00968 0.05781  36  ILE B CG2   
282  C CD1   . ILE A 37  ? 0.21325 0.15235 0.13476 -0.02115 0.00503  0.06705  36  ILE B CD1   
283  N N     . GLU A 38  ? 0.14927 0.11668 0.11625 -0.00095 -0.00912 0.03892  37  GLU B N     
284  C CA    . GLU A 38  ? 0.14543 0.12154 0.11871 0.00158  -0.01132 0.03248  37  GLU B CA    
285  C C     . GLU A 38  ? 0.14627 0.12385 0.13597 0.00629  -0.01662 0.03195  37  GLU B C     
286  O O     . GLU A 38  ? 0.17128 0.14305 0.16305 0.00864  -0.02278 0.03819  37  GLU B O     
287  C CB    . GLU A 38  ? 0.15870 0.13568 0.11753 0.00016  -0.01558 0.03310  37  GLU B CB    
288  C CG    . GLU A 38  ? 0.15817 0.14312 0.12319 0.00123  -0.01711 0.02627  37  GLU B CG    
289  C CD    . GLU A 38  ? 0.22993 0.21450 0.18310 -0.00045 -0.02437 0.02697  37  GLU B CD    
290  O OE1   . GLU A 38  ? 0.21676 0.19760 0.15230 -0.00382 -0.02138 0.02551  37  GLU B OE1   
291  O OE2   . GLU A 38  ? 0.21849 0.20673 0.18040 0.00138  -0.03303 0.02878  37  GLU B OE2   
292  N N     . ASP A 39  ? 0.15844 0.14365 0.16020 0.00776  -0.01408 0.02501  38  ASP B N     
293  C CA    . ASP A 39  ? 0.18401 0.17265 0.20247 0.01226  -0.01699 0.02317  38  ASP B CA    
294  C C     . ASP A 39  ? 0.13110 0.13087 0.15628 0.01210  -0.01636 0.01720  38  ASP B C     
295  O O     . ASP A 39  ? 0.13891 0.14177 0.15803 0.00878  -0.01227 0.01358  38  ASP B O     
296  C CB    . ASP A 39  ? 0.17215 0.15570 0.20016 0.01358  -0.01204 0.02052  38  ASP B CB    
297  C CG    . ASP A 39  ? 0.16691 0.13770 0.19253 0.01429  -0.01422 0.02739  38  ASP B CG    
298  O OD1   . ASP A 39  ? 0.16878 0.13578 0.20051 0.01867  -0.02089 0.03275  38  ASP B OD1   
299  O OD2   . ASP A 39  ? 0.22537 0.18994 0.24372 0.01010  -0.00982 0.02831  38  ASP B OD2   
300  N N     . SER A 40  ? 0.14775 0.15376 0.18708 0.01569  -0.02067 0.01692  39  SER B N     
301  C CA    . SER A 40  ? 0.18946 0.20690 0.23729 0.01472  -0.02009 0.01213  39  SER B CA    
302  C C     . SER A 40  ? 0.17226 0.19600 0.23988 0.01862  -0.01654 0.00810  39  SER B C     
303  O O     . SER A 40  ? 0.24021 0.26044 0.31853 0.02385  -0.01813 0.01004  39  SER B O     
304  C CB    . SER A 40  ? 0.19302 0.21550 0.23966 0.01371  -0.02902 0.01521  39  SER B CB    
305  O OG    . SER A 40  ? 0.26897 0.28516 0.29543 0.00962  -0.03054 0.01675  39  SER B OG    
306  N N     . TYR A 41  ? 0.16090 0.19332 0.23315 0.01595  -0.01118 0.00246  40  TYR B N     
307  C CA    . TYR A 41  ? 0.14175 0.18139 0.23043 0.01835  -0.00496 -0.00303 40  TYR B CA    
308  C C     . TYR A 41  ? 0.12591 0.17860 0.22092 0.01455  -0.00336 -0.00566 40  TYR B C     
309  O O     . TYR A 41  ? 0.11275 0.16526 0.19587 0.00909  -0.00453 -0.00484 40  TYR B O     
310  C CB    . TYR A 41  ? 0.12916 0.16230 0.21143 0.01674  0.00372  -0.00831 40  TYR B CB    
311  C CG    . TYR A 41  ? 0.19695 0.21636 0.27200 0.01842  0.00253  -0.00570 40  TYR B CG    
312  C CD1   . TYR A 41  ? 0.18390 0.19699 0.27035 0.02416  0.00284  -0.00613 40  TYR B CD1   
313  C CD2   . TYR A 41  ? 0.15058 0.16333 0.20910 0.01421  0.00141  -0.00260 40  TYR B CD2   
314  C CE1   . TYR A 41  ? 0.25040 0.24941 0.33011 0.02454  0.00157  -0.00293 40  TYR B CE1   
315  C CE2   . TYR A 41  ? 0.14414 0.14558 0.19709 0.01444  0.00092  0.00028  40  TYR B CE2   
316  C CZ    . TYR A 41  ? 0.22095 0.21485 0.28359 0.01904  0.00075  0.00041  40  TYR B CZ    
317  O OH    . TYR A 41  ? 0.21196 0.19307 0.26867 0.01808  0.00016  0.00403  40  TYR B OH    
318  N N     . ARG A 42  ? 0.11698 0.18073 0.23215 0.01749  -0.00021 -0.00880 41  ARG B N     
319  C CA    . ARG A 42  ? 0.10067 0.17833 0.22474 0.01312  0.00367  -0.01172 41  ARG B CA    
320  C C     . ARG A 42  ? 0.14205 0.22429 0.27352 0.01354  0.01600  -0.01917 41  ARG B C     
321  O O     . ARG A 42  ? 0.15787 0.23775 0.30019 0.02009  0.01956  -0.02239 41  ARG B O     
322  C CB    . ARG A 42  ? 0.15699 0.24793 0.30167 0.01528  -0.00382 -0.00857 41  ARG B CB    
323  C CG    . ARG A 42  ? 0.18212 0.26942 0.31592 0.01217  -0.01583 -0.00254 41  ARG B CG    
324  C CD    . ARG A 42  ? 0.14996 0.24861 0.30315 0.01489  -0.02617 0.00162  41  ARG B CD    
325  N NE    . ARG A 42  ? 0.17986 0.29754 0.35651 0.01284  -0.02316 -0.00100 41  ARG B NE    
326  C CZ    . ARG A 42  ? 0.19501 0.32047 0.37166 0.00466  -0.02575 -0.00093 41  ARG B CZ    
327  N NH1   . ARG A 42  ? 0.19897 0.31326 0.35232 -0.00190 -0.03001 0.00026  41  ARG B NH1   
328  N NH2   . ARG A 42  ? 0.22511 0.36666 0.42064 0.00281  -0.02274 -0.00225 41  ARG B NH2   
329  N N     . LYS A 43  ? 0.10223 0.18944 0.22638 0.00624  0.02268  -0.02196 42  LYS B N     
330  C CA    . LYS A 43  ? 0.13575 0.22816 0.26304 0.00463  0.03531  -0.02939 42  LYS B CA    
331  C C     . LYS A 43  ? 0.12804 0.23240 0.25599 -0.00357 0.04007  -0.02951 42  LYS B C     
332  O O     . LYS A 43  ? 0.16874 0.26911 0.28209 -0.01012 0.03567  -0.02491 42  LYS B O     
333  C CB    . LYS A 43  ? 0.17858 0.25760 0.28480 0.00213  0.03985  -0.03275 42  LYS B CB    
334  C CG    . LYS A 43  ? 0.22355 0.30647 0.32894 -0.00051 0.05309  -0.04158 42  LYS B CG    
335  C CD    . LYS A 43  ? 0.28777 0.35728 0.37188 -0.00383 0.05590  -0.04529 42  LYS B CD    
336  C CE    . LYS A 43  ? 0.26251 0.33342 0.34629 -0.00489 0.06903  -0.05606 42  LYS B CE    
337  N NZ    . LYS A 43  ? 0.34645 0.41423 0.44876 0.00501  0.07086  -0.06040 42  LYS B NZ    
338  N N     . GLN A 44  ? 0.08058 0.19649 0.22253 -0.00317 0.04863  -0.03376 43  GLN B N     
339  C CA    . GLN A 44  ? 0.11524 0.23949 0.25378 -0.01154 0.05341  -0.03243 43  GLN B CA    
340  C C     . GLN A 44  ? 0.16025 0.27813 0.27799 -0.01726 0.06334  -0.03665 43  GLN B C     
341  O O     . GLN A 44  ? 0.12239 0.23669 0.23882 -0.01351 0.07056  -0.04334 43  GLN B O     
342  C CB    . GLN A 44  ? 0.10519 0.24391 0.26615 -0.00854 0.05569  -0.03258 43  GLN B CB    
343  C CG    . GLN A 44  ? 0.10512 0.25294 0.26392 -0.01728 0.06245  -0.03134 43  GLN B CG    
344  C CD    . GLN A 44  ? 0.23036 0.39525 0.41416 -0.01471 0.06414  -0.03081 43  GLN B CD    
345  O OE1   . GLN A 44  ? 0.32776 0.49950 0.52943 -0.01006 0.05486  -0.02754 43  GLN B OE1   
346  N NE2   . GLN A 44  ? 0.21577 0.38818 0.40048 -0.01809 0.07563  -0.03378 43  GLN B NE2   
347  N N     . VAL A 45  ? 0.09733 0.21241 0.19794 -0.02662 0.06263  -0.03244 44  VAL B N     
348  C CA    . VAL A 45  ? 0.12951 0.23772 0.20700 -0.03349 0.06897  -0.03412 44  VAL B CA    
349  C C     . VAL A 45  ? 0.12130 0.23472 0.19411 -0.04221 0.07150  -0.02934 44  VAL B C     
350  O O     . VAL A 45  ? 0.13830 0.25897 0.22432 -0.04370 0.06762  -0.02458 44  VAL B O     
351  C CB    . VAL A 45  ? 0.17689 0.27310 0.23463 -0.03635 0.06347  -0.03165 44  VAL B CB    
352  C CG1   . VAL A 45  ? 0.22708 0.31744 0.28894 -0.02846 0.06204  -0.03649 44  VAL B CG1   
353  C CG2   . VAL A 45  ? 0.14861 0.24374 0.20618 -0.03959 0.05426  -0.02349 44  VAL B CG2   
354  N N     . VAL A 46  ? 0.15166 0.26080 0.20514 -0.04853 0.07767  -0.03063 45  VAL B N     
355  C CA    . VAL A 46  ? 0.14521 0.25578 0.18897 -0.05794 0.07946  -0.02484 45  VAL B CA    
356  C C     . VAL A 46  ? 0.18605 0.28378 0.20364 -0.06421 0.07436  -0.02015 45  VAL B C     
357  O O     . VAL A 46  ? 0.17177 0.26322 0.17377 -0.06478 0.07643  -0.02445 45  VAL B O     
358  C CB    . VAL A 46  ? 0.16339 0.28190 0.20808 -0.06046 0.09127  -0.02953 45  VAL B CB    
359  C CG1   . VAL A 46  ? 0.17806 0.29574 0.20855 -0.07119 0.09290  -0.02277 45  VAL B CG1   
360  C CG2   . VAL A 46  ? 0.15832 0.29155 0.23241 -0.05392 0.09535  -0.03260 45  VAL B CG2   
361  N N     . ILE A 47  ? 0.14693 0.24017 0.16082 -0.06864 0.06669  -0.01128 46  ILE B N     
362  C CA    . ILE A 47  ? 0.15700 0.23828 0.14938 -0.07373 0.05993  -0.00475 46  ILE B CA    
363  C C     . ILE A 47  ? 0.19087 0.26991 0.17536 -0.08224 0.05942  0.00320  46  ILE B C     
364  O O     . ILE A 47  ? 0.18269 0.26351 0.17934 -0.08350 0.05694  0.00751  46  ILE B O     
365  C CB    . ILE A 47  ? 0.15226 0.22723 0.14816 -0.06991 0.05011  -0.00081 46  ILE B CB    
366  C CG1   . ILE A 47  ? 0.12362 0.20116 0.12867 -0.06170 0.05090  -0.00820 46  ILE B CG1   
367  C CG2   . ILE A 47  ? 0.15158 0.21500 0.12801 -0.07416 0.04269  0.00679  46  ILE B CG2   
368  C CD1   . ILE A 47  ? 0.11665 0.18766 0.12620 -0.05656 0.04116  -0.00472 46  ILE B CD1   
369  N N     . ASP A 48  ? 0.18627 0.26073 0.15022 -0.08859 0.06113  0.00517  47  ASP B N     
370  C CA    . ASP A 48  ? 0.21516 0.28653 0.16941 -0.09723 0.06085  0.01327  47  ASP B CA    
371  C C     . ASP A 48  ? 0.20723 0.28949 0.17724 -0.09926 0.06923  0.01181  47  ASP B C     
372  O O     . ASP A 48  ? 0.21109 0.29165 0.18566 -0.10387 0.06679  0.01891  47  ASP B O     
373  C CB    . ASP A 48  ? 0.20139 0.26129 0.15228 -0.09877 0.04931  0.02386  47  ASP B CB    
374  C CG    . ASP A 48  ? 0.20066 0.25135 0.13772 -0.09708 0.04069  0.02683  47  ASP B CG    
375  O OD1   . ASP A 48  ? 0.28394 0.33602 0.20893 -0.09785 0.04331  0.02194  47  ASP B OD1   
376  O OD2   . ASP A 48  ? 0.22088 0.26295 0.16006 -0.09508 0.03133  0.03374  47  ASP B OD2   
377  N N     . GLY A 49  ? 0.20706 0.30044 0.18675 -0.09568 0.07913  0.00248  48  GLY B N     
378  C CA    . GLY A 49  ? 0.21083 0.31720 0.20833 -0.09692 0.08764  0.00087  48  GLY B CA    
379  C C     . GLY A 49  ? 0.19170 0.30500 0.21557 -0.09231 0.08360  0.00179  48  GLY B C     
380  O O     . GLY A 49  ? 0.19618 0.32216 0.23822 -0.09330 0.08957  0.00101  48  GLY B O     
381  N N     . GLU A 50  ? 0.17442 0.28049 0.20125 -0.08789 0.07338  0.00359  49  GLU B N     
382  C CA    . GLU A 50  ? 0.20577 0.31708 0.25523 -0.08437 0.06775  0.00424  49  GLU B CA    
383  C C     . GLU A 50  ? 0.14204 0.25855 0.20412 -0.07414 0.06669  -0.00295 49  GLU B C     
384  O O     . GLU A 50  ? 0.13710 0.24531 0.18792 -0.07028 0.06347  -0.00491 49  GLU B O     
385  C CB    . GLU A 50  ? 0.15889 0.25696 0.20207 -0.08762 0.05682  0.01151  49  GLU B CB    
386  C CG    . GLU A 50  ? 0.24342 0.33400 0.27462 -0.09729 0.05696  0.01948  49  GLU B CG    
387  C CD    . GLU A 50  ? 0.31471 0.38893 0.33829 -0.09962 0.04621  0.02664  49  GLU B CD    
388  O OE1   . GLU A 50  ? 0.21937 0.28794 0.24497 -0.09401 0.03903  0.02523  49  GLU B OE1   
389  O OE2   . GLU A 50  ? 0.31306 0.37960 0.32882 -0.10703 0.04531  0.03374  49  GLU B OE2   
390  N N     . THR A 51  ? 0.13941 0.26988 0.22571 -0.06992 0.06889  -0.00613 50  THR B N     
391  C CA    . THR A 51  ? 0.12331 0.25907 0.22413 -0.05973 0.06715  -0.01194 50  THR B CA    
392  C C     . THR A 51  ? 0.14165 0.27225 0.24729 -0.05721 0.05500  -0.00932 50  THR B C     
393  O O     . THR A 51  ? 0.10702 0.23817 0.21927 -0.06191 0.04863  -0.00469 50  THR B O     
394  C CB    . THR A 51  ? 0.16156 0.31484 0.28773 -0.05602 0.07236  -0.01473 50  THR B CB    
395  O OG1   . THR A 51  ? 0.21742 0.37540 0.33829 -0.05829 0.08491  -0.01832 50  THR B OG1   
396  C CG2   . THR A 51  ? 0.12596 0.28349 0.26812 -0.04478 0.06895  -0.01949 50  THR B CG2   
397  N N     . SER A 52  ? 0.09903 0.22403 0.20113 -0.05025 0.05182  -0.01274 51  SER B N     
398  C CA    . SER A 52  ? 0.12956 0.24955 0.23410 -0.04808 0.04086  -0.01082 51  SER B CA    
399  C C     . SER A 52  ? 0.11937 0.24156 0.23435 -0.03788 0.03859  -0.01542 51  SER B C     
400  O O     . SER A 52  ? 0.11772 0.23882 0.23039 -0.03297 0.04525  -0.02010 51  SER B O     
401  C CB    . SER A 52  ? 0.16340 0.26865 0.24589 -0.05261 0.03695  -0.00707 51  SER B CB    
402  O OG    . SER A 52  ? 0.16419 0.26481 0.23882 -0.06137 0.03660  -0.00137 51  SER B OG    
403  N N     . LEU A 53  ? 0.07215 0.19335 0.19519 -0.03425 0.02779  -0.01325 52  LEU B N     
404  C CA    . LEU A 53  ? 0.09089 0.20711 0.21684 -0.02426 0.02202  -0.01429 52  LEU B CA    
405  C C     . LEU A 53  ? 0.10082 0.19872 0.20415 -0.02327 0.01596  -0.01157 52  LEU B C     
406  O O     . LEU A 53  ? 0.13268 0.22378 0.22760 -0.02718 0.00939  -0.00819 52  LEU B O     
407  C CB    . LEU A 53  ? 0.14530 0.27061 0.29057 -0.02108 0.01268  -0.01237 52  LEU B CB    
408  C CG    . LEU A 53  ? 0.28585 0.42661 0.45748 -0.01450 0.01508  -0.01459 52  LEU B CG    
409  C CD1   . LEU A 53  ? 0.26884 0.40302 0.44108 -0.00480 0.01824  -0.01776 52  LEU B CD1   
410  C CD2   . LEU A 53  ? 0.32613 0.47812 0.50460 -0.01868 0.02536  -0.01595 52  LEU B CD2   
411  N N     . LEU A 54  ? 0.08346 0.17341 0.17808 -0.01834 0.01866  -0.01355 53  LEU B N     
412  C CA    . LEU A 54  ? 0.06462 0.13985 0.14171 -0.01677 0.01370  -0.01110 53  LEU B CA    
413  C C     . LEU A 54  ? 0.09657 0.16822 0.17779 -0.00978 0.00676  -0.00989 53  LEU B C     
414  O O     . LEU A 54  ? 0.11030 0.18455 0.20160 -0.00413 0.00853  -0.01187 53  LEU B O     
415  C CB    . LEU A 54  ? 0.09024 0.15912 0.15483 -0.01726 0.01966  -0.01317 53  LEU B CB    
416  C CG    . LEU A 54  ? 0.13142 0.20481 0.19063 -0.02454 0.02719  -0.01437 53  LEU B CG    
417  C CD1   . LEU A 54  ? 0.16910 0.23564 0.21327 -0.02608 0.03093  -0.01622 53  LEU B CD1   
418  C CD2   . LEU A 54  ? 0.11588 0.18796 0.17004 -0.03119 0.02373  -0.00923 53  LEU B CD2   
419  N N     . ASP A 55  ? 0.06357 0.12862 0.13680 -0.01044 -0.00099 -0.00664 54  ASP B N     
420  C CA    . ASP A 55  ? 0.06556 0.12471 0.13592 -0.00545 -0.00768 -0.00442 54  ASP B CA    
421  C C     . ASP A 55  ? 0.08329 0.13034 0.13719 -0.00464 -0.00607 -0.00367 54  ASP B C     
422  O O     . ASP A 55  ? 0.12136 0.16235 0.16429 -0.00759 -0.00707 -0.00292 54  ASP B O     
423  C CB    . ASP A 55  ? 0.12274 0.18190 0.19161 -0.00774 -0.01652 -0.00229 54  ASP B CB    
424  C CG    . ASP A 55  ? 0.13485 0.20787 0.22192 -0.01004 -0.01929 -0.00253 54  ASP B CG    
425  O OD1   . ASP A 55  ? 0.19938 0.28250 0.30382 -0.00603 -0.01689 -0.00322 54  ASP B OD1   
426  O OD2   . ASP A 55  ? 0.18299 0.25679 0.26834 -0.01593 -0.02368 -0.00234 54  ASP B OD2   
427  N N     . ILE A 56  ? 0.08980 0.13337 0.14368 -0.00074 -0.00340 -0.00405 55  ILE B N     
428  C CA    . ILE A 56  ? 0.08924 0.12400 0.13073 -0.00101 -0.00103 -0.00349 55  ILE B CA    
429  C C     . ILE A 56  ? 0.12210 0.14958 0.15741 0.00199  -0.00514 -0.00014 55  ILE B C     
430  O O     . ILE A 56  ? 0.09612 0.12269 0.13738 0.00568  -0.00736 0.00141  55  ILE B O     
431  C CB    . ILE A 56  ? 0.11235 0.14707 0.15559 -0.00107 0.00519  -0.00665 55  ILE B CB    
432  C CG1   . ILE A 56  ? 0.10807 0.14969 0.15302 -0.00555 0.00977  -0.00942 55  ILE B CG1   
433  C CG2   . ILE A 56  ? 0.12354 0.15081 0.15607 -0.00225 0.00618  -0.00549 55  ILE B CG2   
434  C CD1   . ILE A 56  ? 0.19723 0.24142 0.24665 -0.00541 0.01647  -0.01449 55  ILE B CD1   
435  N N     . LEU A 57  ? 0.09507 0.11704 0.11866 0.00042  -0.00572 0.00122  56  LEU B N     
436  C CA    . LEU A 57  ? 0.10121 0.11630 0.11563 0.00183  -0.00757 0.00427  56  LEU B CA    
437  C C     . LEU A 57  ? 0.12029 0.13174 0.13131 0.00145  -0.00254 0.00462  56  LEU B C     
438  O O     . LEU A 57  ? 0.10279 0.11481 0.11120 -0.00030 0.00033  0.00350  56  LEU B O     
439  C CB    . LEU A 57  ? 0.08450 0.09648 0.08842 0.00008  -0.01011 0.00414  56  LEU B CB    
440  C CG    . LEU A 57  ? 0.12978 0.13484 0.12051 0.00034  -0.01061 0.00665  56  LEU B CG    
441  C CD1   . LEU A 57  ? 0.14804 0.15209 0.13948 0.00198  -0.01641 0.01109  56  LEU B CD1   
442  C CD2   . LEU A 57  ? 0.16393 0.16515 0.14319 -0.00181 -0.01169 0.00407  56  LEU B CD2   
443  N N     . ASP A 58  ? 0.09765 0.10533 0.11030 0.00292  -0.00216 0.00661  57  ASP B N     
444  C CA    . ASP A 58  ? 0.12753 0.13179 0.13823 0.00137  0.00186  0.00724  57  ASP B CA    
445  C C     . ASP A 58  ? 0.11480 0.11428 0.11582 0.00072  0.00223  0.01134  57  ASP B C     
446  O O     . ASP A 58  ? 0.12166 0.11582 0.11897 0.00173  -0.00057 0.01537  57  ASP B O     
447  C CB    . ASP A 58  ? 0.11017 0.11102 0.12808 0.00246  0.00255  0.00639  57  ASP B CB    
448  C CG    . ASP A 58  ? 0.14572 0.14221 0.16221 -0.00054 0.00580  0.00664  57  ASP B CG    
449  O OD1   . ASP A 58  ? 0.16636 0.16599 0.17945 -0.00351 0.00781  0.00697  57  ASP B OD1   
450  O OD2   . ASP A 58  ? 0.13274 0.12245 0.15316 0.00011  0.00605  0.00650  57  ASP B OD2   
451  N N     . THR A 59  ? 0.11305 0.11456 0.11018 -0.00092 0.00587  0.01069  58  THR B N     
452  C CA    . THR A 59  ? 0.09627 0.09468 0.08380 -0.00182 0.00849  0.01336  58  THR B CA    
453  C C     . THR A 59  ? 0.09846 0.09616 0.08832 -0.00437 0.01275  0.01607  58  THR B C     
454  O O     . THR A 59  ? 0.09912 0.09933 0.09772 -0.00576 0.01342  0.01486  58  THR B O     
455  C CB    . THR A 59  ? 0.11388 0.11479 0.09770 -0.00144 0.01154  0.01036  58  THR B CB    
456  O OG1   . THR A 59  ? 0.08816 0.09466 0.08132 -0.00173 0.01508  0.00911  58  THR B OG1   
457  C CG2   . THR A 59  ? 0.13237 0.13303 0.11459 -0.00032 0.00711  0.00723  58  THR B CG2   
458  N N     . ALA A 60  ? 0.10965 0.10389 0.09044 -0.00602 0.01567  0.01970  59  ALA B N     
459  C CA    . ALA A 60  ? 0.11359 0.10817 0.09676 -0.00971 0.02074  0.02282  59  ALA B CA    
460  C C     . ALA A 60  ? 0.10819 0.11201 0.09758 -0.01018 0.02685  0.02019  59  ALA B C     
461  O O     . ALA A 60  ? 0.11542 0.12140 0.10070 -0.00776 0.02921  0.01726  59  ALA B O     
462  C CB    . ALA A 60  ? 0.13062 0.11803 0.10055 -0.01222 0.02229  0.02876  59  ALA B CB    
463  N N     . GLY A 61  ? 0.10423 0.11319 0.10459 -0.01335 0.02911  0.02118  60  GLY B N     
464  C CA    . GLY A 61  ? 0.12170 0.14113 0.13125 -0.01379 0.03491  0.02032  60  GLY B CA    
465  C C     . GLY A 61  ? 0.12215 0.14213 0.12543 -0.01620 0.04319  0.02312  60  GLY B C     
466  O O     . GLY A 61  ? 0.11960 0.14053 0.12612 -0.02150 0.04625  0.02725  60  GLY B O     
467  N N     . GLN A 62  ? 0.13598 0.15437 0.12865 -0.01327 0.04725  0.02068  61  GLN B N     
468  C CA    . GLN A 62  ? 0.13717 0.15574 0.12004 -0.01601 0.05661  0.02238  61  GLN B CA    
469  C C     . GLN A 62  ? 0.22659 0.24915 0.20855 -0.01147 0.06331  0.01599  61  GLN B C     
470  O O     . GLN A 62  ? 0.25647 0.27642 0.23860 -0.00674 0.05858  0.01135  61  GLN B O     
471  C CB    . GLN A 62  ? 0.19164 0.19767 0.15263 -0.01895 0.05387  0.02687  61  GLN B CB    
472  C CG    . GLN A 62  ? 0.20962 0.20772 0.15892 -0.01520 0.04560  0.02423  61  GLN B CG    
473  C CD    . GLN A 62  ? 0.21245 0.20942 0.14854 -0.01333 0.05028  0.01845  61  GLN B CD    
474  O OE1   . GLN A 62  ? 0.31588 0.31483 0.24430 -0.01548 0.06050  0.01749  61  GLN B OE1   
475  N NE2   . GLN A 62  ? 0.22145 0.21494 0.15479 -0.00987 0.04350  0.01401  61  GLN B NE2   
476  N N     . GLU A 63  ? 0.28769 0.31584 0.26868 -0.01322 0.07508  0.01548  62  GLU B N     
477  C CA    . GLU A 63  ? 0.32807 0.35944 0.30970 -0.00837 0.08369  0.00809  62  GLU B CA    
478  C C     . GLU A 63  ? 0.34035 0.36667 0.29926 -0.01161 0.09345  0.00648  62  GLU B C     
479  O O     . GLU A 63  ? 0.39107 0.42415 0.35483 -0.00904 0.10159  0.00117  62  GLU B O     
480  C CB    . GLU A 63  ? 0.33036 0.37751 0.34017 -0.00529 0.08991  0.00677  62  GLU B CB    
481  C CG    . GLU A 63  ? 0.35249 0.40262 0.38019 -0.00005 0.08014  0.00569  62  GLU B CG    
482  C CD    . GLU A 63  ? 0.44214 0.50891 0.49884 0.00083  0.08162  0.00810  62  GLU B CD    
483  O OE1   . GLU A 63  ? 0.48910 0.56565 0.55311 -0.00188 0.08901  0.00903  62  GLU B OE1   
484  O OE2   . GLU A 63  ? 0.47477 0.54448 0.54485 0.00340  0.07230  0.00919  62  GLU B OE2   
485  N N     . GLU A 64  ? 0.28211 0.29703 0.21714 -0.01677 0.08887  0.01126  63  GLU B N     
486  C CA    . GLU A 64  ? 0.33080 0.34112 0.24296 -0.02020 0.09271  0.01094  63  GLU B CA    
487  C C     . GLU A 64  ? 0.29809 0.29532 0.18524 -0.01969 0.08694  0.00677  63  GLU B C     
488  O O     . GLU A 64  ? 0.36573 0.35974 0.23437 -0.02180 0.09046  0.00433  63  GLU B O     
489  C CB    . GLU A 64  ? 0.29417 0.30226 0.19788 -0.02740 0.09092  0.02150  63  GLU B CB    
490  C CG    . GLU A 64  ? 0.40628 0.42762 0.32793 -0.03019 0.09898  0.02476  63  GLU B CG    
491  C CD    . GLU A 64  ? 0.45155 0.47576 0.39223 -0.03260 0.09387  0.03085  63  GLU B CD    
492  O OE1   . GLU A 64  ? 0.44992 0.47773 0.40785 -0.02841 0.09049  0.02742  63  GLU B OE1   
493  O OE2   . GLU A 64  ? 0.47456 0.49641 0.41245 -0.03889 0.09297  0.03926  63  GLU B OE2   
494  N N     . TYR A 65  ? 0.31247 0.30318 0.19980 -0.01726 0.07675  0.00605  64  TYR B N     
495  C CA    . TYR A 65  ? 0.32379 0.30325 0.18954 -0.01807 0.06749  0.00379  64  TYR B CA    
496  C C     . TYR A 65  ? 0.32906 0.30783 0.20476 -0.01228 0.06450  -0.00534 64  TYR B C     
497  O O     . TYR A 65  ? 0.29453 0.27360 0.18258 -0.00972 0.05378  -0.00399 64  TYR B O     
498  C CB    . TYR A 65  ? 0.30054 0.27511 0.16312 -0.02025 0.05330  0.01320  64  TYR B CB    
499  C CG    . TYR A 65  ? 0.28155 0.25397 0.13389 -0.02618 0.05601  0.02304  64  TYR B CG    
500  C CD1   . TYR A 65  ? 0.26960 0.23717 0.09888 -0.03052 0.05659  0.02528  64  TYR B CD1   
501  C CD2   . TYR A 65  ? 0.26521 0.24219 0.13621 -0.02670 0.05630  0.02961  64  TYR B CD2   
502  C CE1   . TYR A 65  ? 0.32094 0.28776 0.14559 -0.03493 0.05767  0.03477  64  TYR B CE1   
503  C CE2   . TYR A 65  ? 0.24435 0.21784 0.10679 -0.03285 0.05886  0.03905  64  TYR B CE2   
504  C CZ    . TYR A 65  ? 0.26961 0.23904 0.11124 -0.03601 0.05876  0.04174  64  TYR B CZ    
505  O OH    . TYR A 65  ? 0.28463 0.25175 0.12182 -0.04073 0.05986  0.05122  64  TYR B OH    
506  N N     . SER A 66  ? 0.33078 0.30766 0.20031 -0.01058 0.07479  -0.01484 65  SER B N     
507  C CA    . SER A 66  ? 0.32930 0.30402 0.21045 -0.00487 0.07378  -0.02345 65  SER B CA    
508  C C     . SER A 66  ? 0.32042 0.28404 0.18567 -0.00689 0.06232  -0.02680 65  SER B C     
509  O O     . SER A 66  ? 0.32960 0.29177 0.20809 -0.00350 0.05614  -0.02972 65  SER B O     
510  C CB    . SER A 66  ? 0.35047 0.32660 0.23454 -0.00137 0.08762  -0.03259 65  SER B CB    
511  O OG    . SER A 66  ? 0.43263 0.42268 0.33777 0.00074  0.09606  -0.02887 65  SER B OG    
512  N N     . ALA A 67  ? 0.29950 0.25559 0.13666 -0.01315 0.05875  -0.02577 66  ALA B N     
513  C CA    . ALA A 67  ? 0.30684 0.25395 0.12982 -0.01611 0.04661  -0.02879 66  ALA B CA    
514  C C     . ALA A 67  ? 0.31087 0.26253 0.14881 -0.01555 0.03179  -0.02064 66  ALA B C     
515  O O     . ALA A 67  ? 0.30161 0.25058 0.14372 -0.01554 0.02293  -0.02379 66  ALA B O     
516  C CB    . ALA A 67  ? 0.36900 0.31084 0.16453 -0.02240 0.04363  -0.02805 66  ALA B CB    
517  N N     . MET A 68  ? 0.28958 0.24774 0.13603 -0.01545 0.02958  -0.01061 67  MET B N     
518  C CA    . MET A 68  ? 0.28374 0.24684 0.14815 -0.01357 0.01830  -0.00450 67  MET B CA    
519  C C     . MET A 68  ? 0.20289 0.17191 0.09245 -0.00853 0.02069  -0.00770 67  MET B C     
520  O O     . MET A 68  ? 0.23707 0.20743 0.13700 -0.00761 0.01276  -0.00827 67  MET B O     
521  C CB    . MET A 68  ? 0.23114 0.19704 0.09810 -0.01452 0.01622  0.00601  67  MET B CB    
522  C CG    . MET A 68  ? 0.29337 0.25285 0.13755 -0.01945 0.00899  0.01227  67  MET B CG    
523  S SD    . MET A 68  ? 0.45184 0.41080 0.29738 -0.01983 -0.00878 0.01388  67  MET B SD    
524  C CE    . MET A 68  ? 0.36970 0.33749 0.24894 -0.01380 -0.01198 0.01723  67  MET B CE    
525  N N     . ARG A 69  ? 0.22950 0.20292 0.12938 -0.00575 0.03132  -0.00913 68  ARG B N     
526  C CA    . ARG A 69  ? 0.18423 0.16293 0.10643 -0.00132 0.03264  -0.01118 68  ARG B CA    
527  C C     . ARG A 69  ? 0.19579 0.16818 0.11749 -0.00022 0.02959  -0.01809 68  ARG B C     
528  O O     . ARG A 69  ? 0.16337 0.13764 0.09779 0.00073  0.02331  -0.01705 68  ARG B O     
529  C CB    . ARG A 69  ? 0.17190 0.15660 0.10459 0.00141  0.04419  -0.01222 68  ARG B CB    
530  C CG    . ARG A 69  ? 0.23555 0.22493 0.19017 0.00624  0.04476  -0.01403 68  ARG B CG    
531  C CD    . ARG A 69  ? 0.27329 0.26797 0.23837 0.00994  0.05625  -0.01697 68  ARG B CD    
532  N NE    . ARG A 69  ? 0.31780 0.30384 0.27102 0.01167  0.06354  -0.02582 68  ARG B NE    
533  C CZ    . ARG A 69  ? 0.38026 0.36917 0.33627 0.01441  0.07641  -0.03048 68  ARG B CZ    
534  N NH1   . ARG A 69  ? 0.34737 0.34937 0.31983 0.01551  0.08302  -0.02632 68  ARG B NH1   
535  N NH2   . ARG A 69  ? 0.36161 0.34030 0.30402 0.01566  0.08327  -0.04015 68  ARG B NH2   
536  N N     . ASP A 70  ? 0.20861 0.17246 0.11444 -0.00111 0.03449  -0.02550 69  ASP B N     
537  C CA    . ASP A 70  ? 0.24645 0.20158 0.15150 -0.00061 0.03217  -0.03295 69  ASP B CA    
538  C C     . ASP A 70  ? 0.20640 0.15992 0.10923 -0.00474 0.01912  -0.03090 69  ASP B C     
539  O O     . ASP A 70  ? 0.21773 0.16933 0.13160 -0.00430 0.01499  -0.03243 69  ASP B O     
540  C CB    . ASP A 70  ? 0.22661 0.17101 0.11142 -0.00181 0.04002  -0.04262 69  ASP B CB    
541  C CG    . ASP A 70  ? 0.30891 0.25575 0.20196 0.00366  0.05484  -0.04670 69  ASP B CG    
542  O OD1   . ASP A 70  ? 0.27622 0.23364 0.19164 0.00802  0.05735  -0.04130 69  ASP B OD1   
543  O OD2   . ASP A 70  ? 0.31600 0.25469 0.19335 0.00333  0.06411  -0.05576 69  ASP B OD2   
544  N N     . GLN A 71  ? 0.19826 0.15306 0.08827 -0.00897 0.01229  -0.02668 70  GLN B N     
545  C CA    . GLN A 71  ? 0.25312 0.20912 0.14506 -0.01250 -0.00022 -0.02455 70  GLN B CA    
546  C C     . GLN A 71  ? 0.20941 0.17526 0.12493 -0.00990 -0.00357 -0.01883 70  GLN B C     
547  O O     . GLN A 71  ? 0.21288 0.18013 0.13735 -0.01166 -0.00970 -0.01948 70  GLN B O     
548  C CB    . GLN A 71  ? 0.30483 0.26094 0.18030 -0.01680 -0.00804 -0.02004 70  GLN B CB    
549  C CG    . GLN A 71  ? 0.28897 0.24864 0.16946 -0.02028 -0.02169 -0.01776 70  GLN B CG    
550  C CD    . GLN A 71  ? 0.34318 0.29642 0.22189 -0.02400 -0.02477 -0.02588 70  GLN B CD    
551  O OE1   . GLN A 71  ? 0.36755 0.30944 0.22840 -0.02650 -0.02076 -0.03397 70  GLN B OE1   
552  N NE2   . GLN A 71  ? 0.35831 0.31817 0.25564 -0.02480 -0.03109 -0.02419 70  GLN B NE2   
553  N N     . TYR A 72  ? 0.18376 0.15625 0.10872 -0.00661 0.00091  -0.01366 71  TYR B N     
554  C CA    . TYR A 72  ? 0.15883 0.13937 0.10334 -0.00460 -0.00064 -0.00979 71  TYR B CA    
555  C C     . TYR A 72  ? 0.14112 0.12019 0.09558 -0.00365 0.00117  -0.01313 71  TYR B C     
556  O O     . TYR A 72  ? 0.14607 0.12919 0.11124 -0.00479 -0.00292 -0.01152 71  TYR B O     
557  C CB    . TYR A 72  ? 0.20163 0.18717 0.15253 -0.00210 0.00496  -0.00552 71  TYR B CB    
558  C CG    . TYR A 72  ? 0.14740 0.13356 0.09186 -0.00301 0.00330  -0.00020 71  TYR B CG    
559  C CD1   . TYR A 72  ? 0.21296 0.19795 0.15122 -0.00479 -0.00514 0.00257  71  TYR B CD1   
560  C CD2   . TYR A 72  ? 0.15084 0.13888 0.09730 -0.00231 0.00946  0.00294  71  TYR B CD2   
561  C CE1   . TYR A 72  ? 0.17247 0.15630 0.10565 -0.00517 -0.00748 0.00893  71  TYR B CE1   
562  C CE2   . TYR A 72  ? 0.18528 0.17172 0.12593 -0.00368 0.00800  0.00868  71  TYR B CE2   
563  C CZ    . TYR A 72  ? 0.19865 0.18217 0.13248 -0.00473 -0.00055 0.01201  71  TYR B CZ    
564  O OH    . TYR A 72  ? 0.17658 0.15684 0.10547 -0.00570 -0.00264 0.01912  71  TYR B OH    
565  N N     . MET A 73  ? 0.17269 0.14615 0.12479 -0.00135 0.00798  -0.01725 72  MET B N     
566  C CA    . MET A 73  ? 0.13604 0.10633 0.09855 0.00035  0.00918  -0.01910 72  MET B CA    
567  C C     . MET A 73  ? 0.18502 0.14634 0.14225 -0.00331 0.00421  -0.02360 72  MET B C     
568  O O     . MET A 73  ? 0.16764 0.12791 0.13464 -0.00436 0.00144  -0.02221 72  MET B O     
569  C CB    . MET A 73  ? 0.14013 0.10807 0.10584 0.00526  0.01809  -0.02177 72  MET B CB    
570  C CG    . MET A 73  ? 0.15277 0.13158 0.12796 0.00758  0.02188  -0.01644 72  MET B CG    
571  S SD    . MET A 73  ? 0.19645 0.17755 0.17939 0.01310  0.03304  -0.01885 72  MET B SD    
572  C CE    . MET A 73  ? 0.18756 0.18302 0.18430 0.01278  0.03275  -0.01089 72  MET B CE    
573  N N     . ARG A 74  ? 0.16244 0.11694 0.10337 -0.00640 0.00248  -0.02859 73  ARG B N     
574  C CA    . ARG A 74  ? 0.23007 0.17617 0.16596 -0.01151 -0.00361 -0.03316 73  ARG B CA    
575  C C     . ARG A 74  ? 0.24964 0.20470 0.19617 -0.01565 -0.01211 -0.02797 73  ARG B C     
576  O O     . ARG A 74  ? 0.24590 0.19783 0.19992 -0.01879 -0.01495 -0.02849 73  ARG B O     
577  C CB    . ARG A 74  ? 0.21943 0.15758 0.13334 -0.01542 -0.00536 -0.03932 73  ARG B CB    
578  C CG    . ARG A 74  ? 0.28982 0.21278 0.19289 -0.01424 0.00192  -0.04916 73  ARG B CG    
579  C CD    . ARG A 74  ? 0.35090 0.26455 0.22855 -0.02028 -0.00095 -0.05639 73  ARG B CD    
580  N NE    . ARG A 74  ? 0.38162 0.30257 0.24608 -0.02118 -0.00136 -0.05202 73  ARG B NE    
581  C CZ    . ARG A 74  ? 0.42084 0.34020 0.27361 -0.01846 0.00883  -0.05409 73  ARG B CZ    
582  N NH1   . ARG A 74  ? 0.32340 0.23574 0.17803 -0.01361 0.02103  -0.06137 73  ARG B NH1   
583  N NH2   . ARG A 74  ? 0.31568 0.24083 0.15593 -0.02062 0.00703  -0.04829 73  ARG B NH2   
584  N N     . THR A 75  ? 0.16952 0.13561 0.11800 -0.01567 -0.01559 -0.02280 74  THR B N     
585  C CA    . THR A 75  ? 0.19053 0.16690 0.15098 -0.01879 -0.02248 -0.01872 74  THR B CA    
586  C C     . THR A 75  ? 0.21142 0.19507 0.18816 -0.01709 -0.01912 -0.01466 74  THR B C     
587  O O     . THR A 75  ? 0.17508 0.16452 0.16206 -0.02083 -0.02233 -0.01318 74  THR B O     
588  C CB    . THR A 75  ? 0.20173 0.18609 0.16024 -0.01804 -0.02709 -0.01462 74  THR B CB    
589  O OG1   . THR A 75  ? 0.36901 0.34610 0.30863 -0.02052 -0.03070 -0.01739 74  THR B OG1   
590  C CG2   . THR A 75  ? 0.27523 0.27123 0.24865 -0.02046 -0.03410 -0.01134 74  THR B CG2   
591  N N     . GLY A 76  ? 0.15395 0.13831 0.13295 -0.01241 -0.01281 -0.01271 75  GLY B N     
592  C CA    . GLY A 76  ? 0.11602 0.10736 0.10710 -0.01189 -0.01066 -0.00879 75  GLY B CA    
593  C C     . GLY A 76  ? 0.15140 0.13780 0.14681 -0.01486 -0.01083 -0.00871 75  GLY B C     
594  O O     . GLY A 76  ? 0.16121 0.13656 0.15223 -0.01429 -0.00988 -0.01150 75  GLY B O     
595  N N     . GLU A 77  ? 0.09944 0.09330 0.10340 -0.01820 -0.01148 -0.00545 76  GLU B N     
596  C CA    . GLU A 77  ? 0.13041 0.11952 0.13762 -0.02196 -0.01148 -0.00323 76  GLU B CA    
597  C C     . GLU A 77  ? 0.14537 0.13487 0.15452 -0.01968 -0.00849 0.00120  76  GLU B C     
598  O O     . GLU A 77  ? 0.20173 0.18369 0.21178 -0.02122 -0.00916 0.00412  76  GLU B O     
599  C CB    . GLU A 77  ? 0.15737 0.15481 0.17164 -0.02856 -0.01316 -0.00169 76  GLU B CB    
600  C CG    . GLU A 77  ? 0.16009 0.16004 0.17583 -0.03182 -0.01797 -0.00507 76  GLU B CG    
601  C CD    . GLU A 77  ? 0.21329 0.22573 0.24080 -0.03791 -0.01856 -0.00328 76  GLU B CD    
602  O OE1   . GLU A 77  ? 0.22067 0.23005 0.25078 -0.04442 -0.01844 -0.00144 76  GLU B OE1   
603  O OE2   . GLU A 77  ? 0.16072 0.18591 0.19597 -0.03612 -0.01871 -0.00348 76  GLU B OE2   
604  N N     . GLY A 78  ? 0.13049 0.12799 0.14045 -0.01670 -0.00617 0.00224  77  GLY B N     
605  C CA    . GLY A 78  ? 0.10195 0.10086 0.11315 -0.01532 -0.00476 0.00626  77  GLY B CA    
606  C C     . GLY A 78  ? 0.11663 0.12069 0.12765 -0.01122 -0.00257 0.00519  77  GLY B C     
607  O O     . GLY A 78  ? 0.09582 0.10349 0.10586 -0.01038 -0.00194 0.00261  77  GLY B O     
608  N N     . PHE A 79  ? 0.08014 0.08461 0.09329 -0.00900 -0.00207 0.00796  78  PHE B N     
609  C CA    . PHE A 79  ? 0.10943 0.11795 0.12377 -0.00579 0.00015  0.00727  78  PHE B CA    
610  C C     . PHE A 79  ? 0.08891 0.10334 0.10569 -0.00778 -0.00094 0.01085  78  PHE B C     
611  O O     . PHE A 79  ? 0.09982 0.11349 0.11871 -0.00893 -0.00381 0.01510  78  PHE B O     
612  C CB    . PHE A 79  ? 0.10775 0.11179 0.12422 -0.00083 0.00235  0.00599  78  PHE B CB    
613  C CG    . PHE A 79  ? 0.16408 0.16080 0.17447 0.00010  0.00329  0.00142  78  PHE B CG    
614  C CD1   . PHE A 79  ? 0.12879 0.11714 0.13843 -0.00086 0.00138  0.00030  78  PHE B CD1   
615  C CD2   . PHE A 79  ? 0.12468 0.12187 0.12858 0.00080  0.00521  -0.00142 78  PHE B CD2   
616  C CE1   . PHE A 79  ? 0.13384 0.11482 0.13617 -0.00144 0.00132  -0.00482 78  PHE B CE1   
617  C CE2   . PHE A 79  ? 0.14509 0.13555 0.14057 0.00039  0.00472  -0.00552 78  PHE B CE2   
618  C CZ    . PHE A 79  ? 0.11106 0.09362 0.10561 -0.00097 0.00268  -0.00785 78  PHE B CZ    
619  N N     . LEU A 80  ? 0.07460 0.09379 0.09038 -0.00875 0.00055  0.00938  79  LEU B N     
620  C CA    . LEU A 80  ? 0.11493 0.13907 0.13219 -0.01109 -0.00071 0.01155  79  LEU B CA    
621  C C     . LEU A 80  ? 0.08108 0.10735 0.10495 -0.00774 0.00045  0.01245  79  LEU B C     
622  O O     . LEU A 80  ? 0.08954 0.11469 0.11283 -0.00568 0.00389  0.01007  79  LEU B O     
623  C CB    . LEU A 80  ? 0.08446 0.11080 0.09766 -0.01435 0.00090  0.00839  79  LEU B CB    
624  C CG    . LEU A 80  ? 0.11619 0.14330 0.12426 -0.01832 0.00175  0.00661  79  LEU B CG    
625  C CD1   . LEU A 80  ? 0.09946 0.12785 0.10503 -0.02055 0.00444  0.00223  79  LEU B CD1   
626  C CD2   . LEU A 80  ? 0.13596 0.16375 0.14000 -0.02262 -0.00135 0.01101  79  LEU B CD2   
627  N N     . LEU A 81  ? 0.08305 0.11299 0.11388 -0.00742 -0.00251 0.01658  80  LEU B N     
628  C CA    . LEU A 81  ? 0.07386 0.10924 0.11508 -0.00470 -0.00112 0.01791  80  LEU B CA    
629  C C     . LEU A 81  ? 0.07161 0.11378 0.11410 -0.00999 -0.00398 0.01926  80  LEU B C     
630  O O     . LEU A 81  ? 0.08096 0.12718 0.12517 -0.01321 -0.01000 0.02317  80  LEU B O     
631  C CB    . LEU A 81  ? 0.07927 0.11557 0.13141 -0.00036 -0.00331 0.02176  80  LEU B CB    
632  C CG    . LEU A 81  ? 0.15290 0.18151 0.20669 0.00567  0.00074  0.01912  80  LEU B CG    
633  C CD1   . LEU A 81  ? 0.10357 0.12313 0.14434 0.00408  0.00179  0.01528  80  LEU B CD1   
634  C CD2   . LEU A 81  ? 0.11558 0.14264 0.18047 0.00948  -0.00323 0.02376  80  LEU B CD2   
635  N N     . VAL A 82  ? 0.08861 0.13084 0.12908 -0.01164 -0.00041 0.01631  81  VAL B N     
636  C CA    . VAL A 82  ? 0.09179 0.13723 0.13130 -0.01777 -0.00280 0.01593  81  VAL B CA    
637  C C     . VAL A 82  ? 0.07342 0.12713 0.12571 -0.01851 -0.00241 0.01844  81  VAL B C     
638  O O     . VAL A 82  ? 0.06478 0.11896 0.12186 -0.01531 0.00343  0.01812  81  VAL B O     
639  C CB    . VAL A 82  ? 0.06687 0.10518 0.09723 -0.01961 0.00050  0.01117  81  VAL B CB    
640  C CG1   . VAL A 82  ? 0.07248 0.11111 0.10014 -0.02651 -0.00189 0.00917  81  VAL B CG1   
641  C CG2   . VAL A 82  ? 0.07675 0.10979 0.09889 -0.01807 0.00117  0.00874  81  VAL B CG2   
642  N N     . PHE A 83  ? 0.07572 0.13688 0.13349 -0.02341 -0.00870 0.02124  82  PHE B N     
643  C CA    . PHE A 83  ? 0.07208 0.14272 0.14299 -0.02668 -0.00932 0.02327  82  PHE B CA    
644  C C     . PHE A 83  ? 0.08405 0.15362 0.14765 -0.03594 -0.01447 0.02125  82  PHE B C     
645  O O     . PHE A 83  ? 0.10024 0.16273 0.14912 -0.03884 -0.01687 0.01828  82  PHE B O     
646  C CB    . PHE A 83  ? 0.09139 0.17486 0.18107 -0.02374 -0.01345 0.02914  82  PHE B CB    
647  C CG    . PHE A 83  ? 0.07365 0.16110 0.16227 -0.02765 -0.02453 0.03339  82  PHE B CG    
648  C CD1   . PHE A 83  ? 0.09205 0.17328 0.17223 -0.02474 -0.02772 0.03539  82  PHE B CD1   
649  C CD2   . PHE A 83  ? 0.08230 0.17932 0.17722 -0.03530 -0.03232 0.03595  82  PHE B CD2   
650  C CE1   . PHE A 83  ? 0.08441 0.16838 0.16070 -0.02938 -0.03828 0.04063  82  PHE B CE1   
651  C CE2   . PHE A 83  ? 0.10852 0.20898 0.19951 -0.03997 -0.04386 0.04063  82  PHE B CE2   
652  C CZ    . PHE A 83  ? 0.09062 0.18437 0.17156 -0.03694 -0.04671 0.04339  82  PHE B CZ    
653  N N     . ALA A 84  ? 0.07817 0.15450 0.15186 -0.04118 -0.01533 0.02217  83  ALA B N     
654  C CA    . ALA A 84  ? 0.12043 0.19472 0.18772 -0.05119 -0.02039 0.01931  83  ALA B CA    
655  C C     . ALA A 84  ? 0.13433 0.22308 0.21395 -0.05676 -0.03025 0.02428  83  ALA B C     
656  O O     . ALA A 84  ? 0.08656 0.18842 0.18658 -0.05370 -0.03023 0.02945  83  ALA B O     
657  C CB    . ALA A 84  ? 0.10190 0.17011 0.17011 -0.05478 -0.01459 0.01638  83  ALA B CB    
658  N N     . ILE A 85  ? 0.10288 0.18962 0.17003 -0.06489 -0.03865 0.02255  84  ILE B N     
659  C CA    . ILE A 85  ? 0.11192 0.20778 0.18479 -0.06710 -0.04839 0.02725  84  ILE B CA    
660  C C     . ILE A 85  ? 0.11972 0.22219 0.20603 -0.07133 -0.04933 0.02710  84  ILE B C     
661  O O     . ILE A 85  ? 0.12382 0.23656 0.22043 -0.07214 -0.05673 0.03168  84  ILE B O     
662  C CB    . ILE A 85  ? 0.14970 0.23861 0.20003 -0.07387 -0.05572 0.02514  84  ILE B CB    
663  C CG1   . ILE A 85  ? 0.15710 0.23508 0.19229 -0.08269 -0.05383 0.01599  84  ILE B CG1   
664  C CG2   . ILE A 85  ? 0.13813 0.22142 0.17565 -0.07034 -0.05401 0.02566  84  ILE B CG2   
665  C CD1   . ILE A 85  ? 0.26074 0.33706 0.28164 -0.09103 -0.06237 0.01469  84  ILE B CD1   
666  N N     . ASN A 86  ? 0.13610 0.23287 0.22352 -0.07405 -0.04195 0.02261  85  ASN B N     
667  C CA    . ASN A 86  ? 0.12043 0.22311 0.22183 -0.07837 -0.04109 0.02273  85  ASN B CA    
668  C C     . ASN A 86  ? 0.10918 0.21761 0.22701 -0.07258 -0.03080 0.02535  85  ASN B C     
669  O O     . ASN A 86  ? 0.12343 0.23272 0.24895 -0.07700 -0.02666 0.02451  85  ASN B O     
670  C CB    . ASN A 86  ? 0.13371 0.22292 0.22195 -0.08786 -0.04106 0.01568  85  ASN B CB    
671  C CG    . ASN A 86  ? 0.15071 0.22455 0.22875 -0.08671 -0.03195 0.01136  85  ASN B CG    
672  O OD1   . ASN A 86  ? 0.13573 0.20767 0.21014 -0.08013 -0.02756 0.01250  85  ASN B OD1   
673  N ND2   . ASN A 86  ? 0.16910 0.23131 0.24314 -0.09318 -0.02957 0.00671  85  ASN B ND2   
674  N N     . ASN A 87  ? 0.10898 0.22035 0.23079 -0.06323 -0.02603 0.02824  86  ASN B N     
675  C CA    . ASN A 87  ? 0.12131 0.23779 0.25575 -0.05706 -0.01525 0.03009  86  ASN B CA    
676  C C     . ASN A 87  ? 0.12768 0.25549 0.27602 -0.04758 -0.01589 0.03409  86  ASN B C     
677  O O     . ASN A 87  ? 0.09649 0.22012 0.23972 -0.04082 -0.01457 0.03470  86  ASN B O     
678  C CB    . ASN A 87  ? 0.11448 0.21818 0.23613 -0.05495 -0.00675 0.02809  86  ASN B CB    
679  C CG    . ASN A 87  ? 0.14117 0.24838 0.27083 -0.04928 0.00491  0.02976  86  ASN B CG    
680  O OD1   . ASN A 87  ? 0.10753 0.22719 0.25264 -0.04488 0.00758  0.03153  86  ASN B OD1   
681  N ND2   . ASN A 87  ? 0.15869 0.25340 0.27556 -0.04903 0.01199  0.02863  86  ASN B ND2   
682  N N     . THR A 88  ? 0.09337 0.23512 0.26051 -0.04704 -0.01771 0.03665  87  THR B N     
683  C CA    . THR A 88  ? 0.11656 0.26807 0.29907 -0.03766 -0.01887 0.04035  87  THR B CA    
684  C C     . THR A 88  ? 0.11964 0.26931 0.30530 -0.02834 -0.00645 0.03886  87  THR B C     
685  O O     . THR A 88  ? 0.12102 0.26877 0.30864 -0.01988 -0.00689 0.04015  87  THR B O     
686  C CB    . THR A 88  ? 0.10200 0.26970 0.30584 -0.03934 -0.02254 0.04299  87  THR B CB    
687  O OG1   . THR A 88  ? 0.10261 0.27133 0.30210 -0.04585 -0.03650 0.04537  87  THR B OG1   
688  C CG2   . THR A 88  ? 0.09359 0.27175 0.31780 -0.02829 -0.01926 0.04569  87  THR B CG2   
689  N N     . LYS A 89  ? 0.08161 0.23007 0.26569 -0.03025 0.00470  0.03608  88  LYS B N     
690  C CA    . LYS A 89  ? 0.12867 0.27386 0.31113 -0.02238 0.01692  0.03389  88  LYS B CA    
691  C C     . LYS A 89  ? 0.15144 0.28292 0.31719 -0.01844 0.01682  0.03275  88  LYS B C     
692  O O     . LYS A 89  ? 0.14796 0.27682 0.31461 -0.00974 0.02206  0.03136  88  LYS B O     
693  C CB    . LYS A 89  ? 0.13911 0.28335 0.31725 -0.02708 0.02806  0.03201  88  LYS B CB    
694  C CG    . LYS A 89  ? 0.22394 0.36393 0.39601 -0.01994 0.04075  0.02923  88  LYS B CG    
695  C CD    . LYS A 89  ? 0.40375 0.53787 0.56285 -0.02578 0.05043  0.02856  88  LYS B CD    
696  C CE    . LYS A 89  ? 0.27243 0.39967 0.41918 -0.01940 0.06165  0.02543  88  LYS B CE    
697  N NZ    . LYS A 89  ? 0.32143 0.43208 0.44769 -0.01739 0.06032  0.02469  88  LYS B NZ    
698  N N     . SER A 90  ? 0.09400 0.21622 0.24453 -0.02487 0.01129  0.03264  89  SER B N     
699  C CA    . SER A 90  ? 0.09167 0.19916 0.22305 -0.02091 0.01124  0.03012  89  SER B CA    
700  C C     . SER A 90  ? 0.12813 0.23652 0.26318 -0.01497 0.00437  0.03191  89  SER B C     
701  O O     . SER A 90  ? 0.08895 0.18691 0.21343 -0.00886 0.00699  0.02954  89  SER B O     
702  C CB    . SER A 90  ? 0.07870 0.17339 0.19036 -0.02790 0.00696  0.02758  89  SER B CB    
703  O OG    . SER A 90  ? 0.09847 0.19575 0.20958 -0.03328 -0.00384 0.02866  89  SER B OG    
704  N N     . PHE A 91  ? 0.06395 0.18454 0.21440 -0.01716 -0.00504 0.03679  90  PHE B N     
705  C CA    . PHE A 91  ? 0.08780 0.20919 0.24365 -0.01149 -0.01237 0.04060  90  PHE B CA    
706  C C     . PHE A 91  ? 0.08300 0.20782 0.25510 -0.00088 -0.00535 0.04031  90  PHE B C     
707  O O     . PHE A 91  ? 0.08821 0.20645 0.26031 0.00625  -0.00549 0.04088  90  PHE B O     
708  C CB    . PHE A 91  ? 0.07278 0.19974 0.23064 -0.01725 -0.02528 0.04488  90  PHE B CB    
709  C CG    . PHE A 91  ? 0.12775 0.25409 0.28999 -0.01216 -0.03377 0.05050  90  PHE B CG    
710  C CD1   . PHE A 91  ? 0.08065 0.19699 0.22720 -0.01278 -0.03892 0.05229  90  PHE B CD1   
711  C CD2   . PHE A 91  ? 0.13905 0.27449 0.32104 -0.00734 -0.03678 0.05446  90  PHE B CD2   
712  C CE1   . PHE A 91  ? 0.11610 0.22949 0.26509 -0.00886 -0.04680 0.05858  90  PHE B CE1   
713  C CE2   . PHE A 91  ? 0.13375 0.26655 0.31965 -0.00279 -0.04497 0.06055  90  PHE B CE2   
714  C CZ    . PHE A 91  ? 0.18138 0.30218 0.34992 -0.00379 -0.04996 0.06289  90  PHE B CZ    
715  N N     . GLU A 92  ? 0.10782 0.24199 0.29324 -0.00010 0.00137  0.03878  91  GLU B N     
716  C CA    . GLU A 92  ? 0.08533 0.22223 0.28416 0.00948  0.01046  0.03641  91  GLU B CA    
717  C C     . GLU A 92  ? 0.15898 0.28445 0.34516 0.01417  0.02217  0.03068  91  GLU B C     
718  O O     . GLU A 92  ? 0.12702 0.24950 0.31900 0.02267  0.02865  0.02746  91  GLU B O     
719  C CB    . GLU A 92  ? 0.13666 0.28749 0.35076 0.00757  0.01594  0.03562  91  GLU B CB    
720  C CG    . GLU A 92  ? 0.11953 0.28238 0.34789 0.00342  0.00409  0.04102  91  GLU B CG    
721  C CD    . GLU A 92  ? 0.31167 0.48991 0.55623 -0.00002 0.00905  0.04036  91  GLU B CD    
722  O OE1   . GLU A 92  ? 0.27260 0.45082 0.51196 -0.00280 0.02052  0.03636  91  GLU B OE1   
723  O OE2   . GLU A 92  ? 0.24118 0.43169 0.50345 -0.00035 0.00116  0.04438  91  GLU B OE2   
724  N N     . ASP A 93  ? 0.10379 0.22183 0.27198 0.00866  0.02486  0.02897  92  ASP B N     
725  C CA    . ASP A 93  ? 0.15694 0.26071 0.30618 0.01191  0.03371  0.02320  92  ASP B CA    
726  C C     . ASP A 93  ? 0.15035 0.23981 0.28711 0.01605  0.02821  0.02181  92  ASP B C     
727  O O     . ASP A 93  ? 0.16553 0.24363 0.28996 0.01993  0.03468  0.01650  92  ASP B O     
728  C CB    . ASP A 93  ? 0.15685 0.25248 0.28468 0.00430  0.03567  0.02164  92  ASP B CB    
729  C CG    . ASP A 93  ? 0.24141 0.34436 0.37358 0.00114  0.04628  0.02132  92  ASP B CG    
730  O OD1   . ASP A 93  ? 0.20799 0.32070 0.35519 0.00493  0.05249  0.02022  92  ASP B OD1   
731  O OD2   . ASP A 93  ? 0.23047 0.32664 0.34749 -0.00531 0.04731  0.02159  92  ASP B OD2   
732  N N     . ILE A 94  ? 0.08982 0.17909 0.22754 0.01401  0.01638  0.02648  93  ILE B N     
733  C CA    . ILE A 94  ? 0.16789 0.24290 0.29004 0.01500  0.01123  0.02583  93  ILE B CA    
734  C C     . ILE A 94  ? 0.11585 0.18322 0.24290 0.02376  0.01581  0.02302  93  ILE B C     
735  O O     . ILE A 94  ? 0.10916 0.16265 0.21988 0.02458  0.01807  0.01855  93  ILE B O     
736  C CB    . ILE A 94  ? 0.12449 0.20201 0.24745 0.01073  -0.00147 0.03228  93  ILE B CB    
737  C CG1   . ILE A 94  ? 0.11001 0.18942 0.22093 0.00129  -0.00495 0.03208  93  ILE B CG1   
738  C CG2   . ILE A 94  ? 0.13153 0.19571 0.24336 0.01256  -0.00587 0.03311  93  ILE B CG2   
739  C CD1   . ILE A 94  ? 0.10315 0.16939 0.19079 -0.00172 -0.00213 0.02698  93  ILE B CD1   
740  N N     . HIS A 95  ? 0.08407 0.16027 0.23509 0.03045  0.01705  0.02527  94  HIS B N     
741  C CA    . HIS A 95  ? 0.11516 0.18182 0.27246 0.03942  0.02101  0.02216  94  HIS B CA    
742  C C     . HIS A 95  ? 0.11766 0.17493 0.26110 0.04143  0.03380  0.01234  94  HIS B C     
743  O O     . HIS A 95  ? 0.10646 0.14862 0.24130 0.04510  0.03570  0.00762  94  HIS B O     
744  C CB    . HIS A 95  ? 0.12334 0.20086 0.30916 0.04656  0.02032  0.02565  94  HIS B CB    
745  C CG    . HIS A 95  ? 0.12590 0.21527 0.32061 0.04724  0.03044  0.02131  94  HIS B CG    
746  N ND1   . HIS A 95  ? 0.15380 0.23923 0.35101 0.05375  0.04218  0.01348  94  HIS B ND1   
747  C CD2   . HIS A 95  ? 0.16033 0.26512 0.36162 0.04151  0.03036  0.02375  94  HIS B CD2   
748  C CE1   . HIS A 95  ? 0.18986 0.28901 0.39500 0.05212  0.04931  0.01182  94  HIS B CE1   
749  N NE2   . HIS A 95  ? 0.19393 0.30473 0.40236 0.04469  0.04220  0.01815  94  HIS B NE2   
750  N N     . HIS A 96  ? 0.14500 0.20985 0.28404 0.03787  0.04197  0.00951  95  HIS B N     
751  C CA    . HIS A 96  ? 0.15400 0.20963 0.27510 0.03801  0.05307  0.00117  95  HIS B CA    
752  C C     . HIS A 96  ? 0.12965 0.16936 0.22425 0.03355  0.04788  -0.00101 95  HIS B C     
753  O O     . HIS A 96  ? 0.11876 0.14569 0.19998 0.03550  0.05244  -0.00780 95  HIS B O     
754  C CB    . HIS A 96  ? 0.11821 0.18438 0.23723 0.03318  0.06127  0.00094  95  HIS B CB    
755  C CG    . HIS A 96  ? 0.18914 0.27031 0.33034 0.03632  0.06791  0.00115  95  HIS B CG    
756  N ND1   . HIS A 96  ? 0.19073 0.26967 0.33862 0.04348  0.07460  -0.00463 95  HIS B ND1   
757  C CD2   . HIS A 96  ? 0.22321 0.31977 0.37687 0.03177  0.06672  0.00576  95  HIS B CD2   
758  C CE1   . HIS A 96  ? 0.23163 0.32571 0.39689 0.04391  0.07779  -0.00317 95  HIS B CE1   
759  N NE2   . HIS A 96  ? 0.19048 0.29547 0.35952 0.03659  0.07285  0.00316  95  HIS B NE2   
760  N N     . TYR A 97  ? 0.09586 0.13661 0.18318 0.02722  0.03858  0.00410  96  TYR B N     
761  C CA    . TYR A 97  ? 0.13804 0.16655 0.20441 0.02330  0.03395  0.00232  96  TYR B CA    
762  C C     . TYR A 97  ? 0.14846 0.16577 0.21432 0.02637  0.02973  0.00112  96  TYR B C     
763  O O     . TYR A 97  ? 0.16370 0.16926 0.21509 0.02578  0.03100  -0.00409 96  TYR B O     
764  C CB    . TYR A 97  ? 0.14217 0.17458 0.20357 0.01674  0.02634  0.00711  96  TYR B CB    
765  C CG    . TYR A 97  ? 0.17967 0.21730 0.23634 0.01261  0.03019  0.00745  96  TYR B CG    
766  C CD1   . TYR A 97  ? 0.16683 0.19694 0.20602 0.01020  0.03246  0.00480  96  TYR B CD1   
767  C CD2   . TYR A 97  ? 0.14502 0.19475 0.21538 0.01065  0.03076  0.01114  96  TYR B CD2   
768  C CE1   . TYR A 97  ? 0.10053 0.13329 0.13518 0.00633  0.03551  0.00645  96  TYR B CE1   
769  C CE2   . TYR A 97  ? 0.13579 0.18856 0.20218 0.00602  0.03435  0.01197  96  TYR B CE2   
770  C CZ    . TYR A 97  ? 0.15586 0.19927 0.20402 0.00406  0.03692  0.00993  96  TYR B CZ    
771  O OH    . TYR A 97  ? 0.14051 0.18519 0.18485 -0.00072 0.03999  0.01213  96  TYR B OH    
772  N N     . ARG A 98  ? 0.09812 0.11833 0.17942 0.02898  0.02391  0.00647  97  ARG B N     
773  C CA    . ARG A 98  ? 0.11744 0.12508 0.19832 0.03124  0.01957  0.00666  97  ARG B CA    
774  C C     . ARG A 98  ? 0.15328 0.15051 0.23587 0.03779  0.02766  -0.00112 97  ARG B C     
775  O O     . ARG A 98  ? 0.13000 0.11227 0.20229 0.03721  0.02658  -0.00507 97  ARG B O     
776  C CB    . ARG A 98  ? 0.18051 0.19261 0.27721 0.03273  0.01108  0.01552  97  ARG B CB    
777  C CG    . ARG A 98  ? 0.21838 0.21590 0.31597 0.03496  0.00633  0.01747  97  ARG B CG    
778  C CD    . ARG A 98  ? 0.23639 0.23826 0.34654 0.03505  -0.00384 0.02846  97  ARG B CD    
779  N NE    . ARG A 98  ? 0.23516 0.22236 0.35108 0.03897  -0.00780 0.03165  97  ARG B NE    
780  C CZ    . ARG A 98  ? 0.34507 0.32039 0.44834 0.03326  -0.01347 0.03511  97  ARG B CZ    
781  N NH1   . ARG A 98  ? 0.24867 0.22613 0.33363 0.02405  -0.01492 0.03480  97  ARG B NH1   
782  N NH2   . ARG A 98  ? 0.33896 0.29987 0.44952 0.03689  -0.01737 0.03917  97  ARG B NH2   
783  N N     . GLU A 99  ? 0.12407 0.12902 0.21976 0.04351  0.03642  -0.00405 98  GLU B N     
784  C CA    . GLU A 99  ? 0.14659 0.14162 0.24315 0.04998  0.04643  -0.01332 98  GLU B CA    
785  C C     . GLU A 99  ? 0.20080 0.18475 0.27046 0.04517  0.05114  -0.02188 98  GLU B C     
786  O O     . GLU A 99  ? 0.17456 0.14230 0.23532 0.04658  0.05295  -0.02904 98  GLU B O     
787  C CB    . GLU A 99  ? 0.17139 0.18025 0.28780 0.05628  0.05682  -0.01507 98  GLU B CB    
788  C CG    . GLU A 99  ? 0.28609 0.30415 0.43181 0.06268  0.05145  -0.00768 98  GLU B CG    
789  C CD    . GLU A 99  ? 0.28836 0.32606 0.44981 0.06362  0.05616  -0.00615 98  GLU B CD    
790  O OE1   . GLU A 99  ? 0.21446 0.25801 0.36680 0.06058  0.06604  -0.01118 98  GLU B OE1   
791  O OE2   . GLU A 99  ? 0.26656 0.31339 0.44893 0.06678  0.04936  0.00064  98  GLU B OE2   
792  N N     . GLN A 100 ? 0.14205 0.13368 0.19841 0.03906  0.05230  -0.02096 99  GLN B N     
793  C CA    . GLN A 100 ? 0.18570 0.16821 0.21643 0.03405  0.05480  -0.02721 99  GLN B CA    
794  C C     . GLN A 100 ? 0.18425 0.15545 0.20265 0.02940  0.04484  -0.02690 99  GLN B C     
795  O O     . GLN A 100 ? 0.20318 0.16179 0.20523 0.02732  0.04576  -0.03403 99  GLN B O     
796  C CB    . GLN A 100 ? 0.20104 0.19394 0.22286 0.02880  0.05653  -0.02381 99  GLN B CB    
797  C CG    . GLN A 100 ? 0.29587 0.30050 0.32793 0.03135  0.06781  -0.02432 99  GLN B CG    
798  C CD    . GLN A 100 ? 0.44779 0.44581 0.46832 0.03349  0.08090  -0.03415 99  GLN B CD    
799  O OE1   . GLN A 100 ? 0.44288 0.42593 0.44881 0.03388  0.08124  -0.04169 99  GLN B OE1   
800  N NE2   . GLN A 100 ? 0.53788 0.54716 0.56458 0.03407  0.09228  -0.03453 99  GLN B NE2   
801  N N     . ILE A 101 ? 0.15117 0.12722 0.17678 0.02690  0.03554  -0.01901 100 ILE B N     
802  C CA    . ILE A 101 ? 0.17925 0.14725 0.19569 0.02181  0.02717  -0.01814 100 ILE B CA    
803  C C     . ILE A 101 ? 0.15188 0.10466 0.17005 0.02411  0.02661  -0.02235 100 ILE B C     
804  O O     . ILE A 101 ? 0.17209 0.11387 0.17707 0.02000  0.02432  -0.02731 100 ILE B O     
805  C CB    . ILE A 101 ? 0.13308 0.10990 0.15673 0.01854  0.01944  -0.00938 100 ILE B CB    
806  C CG1   . ILE A 101 ? 0.13800 0.12602 0.15751 0.01531  0.01950  -0.00673 100 ILE B CG1   
807  C CG2   . ILE A 101 ? 0.16625 0.13624 0.18329 0.01326  0.01257  -0.00842 100 ILE B CG2   
808  C CD1   . ILE A 101 ? 0.12306 0.11968 0.15025 0.01279  0.01403  0.00019  100 ILE B CD1   
809  N N     . LYS A 102 ? 0.15348 0.10504 0.18902 0.03051  0.02798  -0.02014 101 LYS B N     
810  C CA    . LYS A 102 ? 0.18167 0.11630 0.22115 0.03375  0.02778  -0.02384 101 LYS B CA    
811  C C     . LYS A 102 ? 0.19041 0.11257 0.21786 0.03551  0.03635  -0.03651 101 LYS B C     
812  O O     . LYS A 102 ? 0.20650 0.11139 0.22618 0.03351  0.03466  -0.04219 101 LYS B O     
813  C CB    . LYS A 102 ? 0.18963 0.12635 0.25297 0.04193  0.02767  -0.01829 101 LYS B CB    
814  C CG    . LYS A 102 ? 0.20807 0.15422 0.28053 0.03918  0.01772  -0.00558 101 LYS B CG    
815  C CD    . LYS A 102 ? 0.25325 0.19391 0.34587 0.04585  0.01368  0.00088  101 LYS B CD    
816  C CE    . LYS A 102 ? 0.23886 0.18872 0.35234 0.05578  0.02036  -0.00050 101 LYS B CE    
817  N NZ    . LYS A 102 ? 0.27562 0.21576 0.41018 0.06450  0.01772  0.00329  101 LYS B NZ    
818  N N     . ARG A 103 ? 0.19227 0.12232 0.21708 0.03839  0.04592  -0.04129 102 ARG B N     
819  C CA    . ARG A 103 ? 0.21482 0.13339 0.22465 0.03928  0.05546  -0.05401 102 ARG B CA    
820  C C     . ARG A 103 ? 0.22178 0.13281 0.20492 0.02984  0.05055  -0.05819 102 ARG B C     
821  O O     . ARG A 103 ? 0.24297 0.13684 0.21338 0.02775  0.05114  -0.06742 102 ARG B O     
822  C CB    . ARG A 103 ? 0.21588 0.14674 0.22802 0.04312  0.06756  -0.05682 102 ARG B CB    
823  C CG    . ARG A 103 ? 0.27165 0.19222 0.26488 0.04292  0.07815  -0.06982 102 ARG B CG    
824  C CD    . ARG A 103 ? 0.30105 0.23770 0.29379 0.04373  0.08795  -0.06964 102 ARG B CD    
825  N NE    . ARG A 103 ? 0.36517 0.31163 0.34651 0.03729  0.08665  -0.06364 102 ARG B NE    
826  C CZ    . ARG A 103 ? 0.33985 0.28031 0.29315 0.02921  0.08364  -0.06560 102 ARG B CZ    
827  N NH1   . ARG A 103 ? 0.37244 0.29732 0.30566 0.02574  0.08146  -0.07405 102 ARG B NH1   
828  N NH2   . ARG A 103 ? 0.43359 0.38513 0.38038 0.02391  0.07978  -0.05730 102 ARG B NH2   
829  N N     . VAL A 104 ? 0.20612 0.12959 0.18133 0.02412  0.04546  -0.05175 103 VAL B N     
830  C CA    . VAL A 104 ? 0.22299 0.14219 0.17582 0.01570  0.03949  -0.05415 103 VAL B CA    
831  C C     . VAL A 104 ? 0.21472 0.12372 0.16756 0.01107  0.02978  -0.05405 103 VAL B C     
832  O O     . VAL A 104 ? 0.23196 0.12952 0.16847 0.00547  0.02672  -0.06100 103 VAL B O     
833  C CB    . VAL A 104 ? 0.20730 0.14195 0.15722 0.01208  0.03535  -0.04575 103 VAL B CB    
834  C CG1   . VAL A 104 ? 0.19859 0.13059 0.13141 0.00424  0.02640  -0.04594 103 VAL B CG1   
835  C CG2   . VAL A 104 ? 0.25062 0.19281 0.19629 0.01436  0.04515  -0.04638 103 VAL B CG2   
836  N N     . LYS A 105 ? 0.19960 0.11266 0.17006 0.01233  0.02469  -0.04598 104 LYS B N     
837  C CA    . LYS A 105 ? 0.24305 0.14807 0.21568 0.00716  0.01630  -0.04398 104 LYS B CA    
838  C C     . LYS A 105 ? 0.22178 0.10719 0.19815 0.00975  0.01831  -0.04999 104 LYS B C     
839  O O     . LYS A 105 ? 0.22873 0.10402 0.20434 0.00400  0.01180  -0.04963 104 LYS B O     
840  C CB    . LYS A 105 ? 0.20519 0.12236 0.19239 0.00661  0.01100  -0.03244 104 LYS B CB    
841  C CG    . LYS A 105 ? 0.22295 0.15553 0.20593 0.00234  0.00741  -0.02775 104 LYS B CG    
842  C CD    . LYS A 105 ? 0.37434 0.30766 0.35930 -0.00479 -0.00028 -0.02376 104 LYS B CD    
843  C CE    . LYS A 105 ? 0.23027 0.17872 0.21522 -0.00799 -0.00339 -0.01927 104 LYS B CE    
844  N NZ    . LYS A 105 ? 0.14970 0.09807 0.12429 -0.01295 -0.00753 -0.02339 104 LYS B NZ    
845  N N     . ASP A 106 ? 0.23288 0.11265 0.21466 0.01817  0.02760  -0.05555 105 ASP B N     
846  C CA    . ASP A 106 ? 0.25469 0.11432 0.24300 0.02276  0.03077  -0.06189 105 ASP B CA    
847  C C     . ASP A 106 ? 0.25398 0.10843 0.25768 0.02197  0.02247  -0.05207 105 ASP B C     
848  O O     . ASP A 106 ? 0.26610 0.10256 0.26692 0.01757  0.01819  -0.05467 105 ASP B O     
849  C CB    . ASP A 106 ? 0.28162 0.12244 0.24896 0.01715  0.03198  -0.07530 105 ASP B CB    
850  C CG    . ASP A 106 ? 0.30743 0.12727 0.28091 0.02238  0.03540  -0.08280 105 ASP B CG    
851  O OD1   . ASP A 106 ? 0.31153 0.13460 0.29816 0.03286  0.04258  -0.08339 105 ASP B OD1   
852  O OD2   . ASP A 106 ? 0.32992 0.13431 0.29603 0.01577  0.02875  -0.08630 105 ASP B OD2   
853  N N     . SER A 107 ? 0.22963 0.09948 0.24860 0.02530  0.01991  -0.04034 106 SER B N     
854  C CA    . SER A 107 ? 0.26407 0.13094 0.29460 0.02343  0.01168  -0.02921 106 SER B CA    
855  C C     . SER A 107 ? 0.26020 0.13963 0.30967 0.03085  0.01119  -0.01919 106 SER B C     
856  O O     . SER A 107 ? 0.25091 0.14786 0.30311 0.03372  0.01480  -0.01819 106 SER B O     
857  C CB    . SER A 107 ? 0.25501 0.13014 0.27633 0.01237  0.00396  -0.02311 106 SER B CB    
858  O OG    . SER A 107 ? 0.32429 0.19668 0.35451 0.00966  -0.00271 -0.01204 106 SER B OG    
859  N N     . GLU A 108 ? 0.27334 0.14315 0.33579 0.03312  0.00571  -0.01102 107 GLU B N     
860  C CA    . GLU A 108 ? 0.29042 0.17228 0.36983 0.03799  0.00151  0.00104  107 GLU B CA    
861  C C     . GLU A 108 ? 0.32365 0.21907 0.39617 0.02892  -0.00624 0.01178  107 GLU B C     
862  O O     . GLU A 108 ? 0.32573 0.23484 0.40747 0.03085  -0.00993 0.02076  107 GLU B O     
863  C CB    . GLU A 108 ? 0.34784 0.21292 0.44342 0.04416  -0.00257 0.00693  107 GLU B CB    
864  C CG    . GLU A 108 ? 0.35474 0.21113 0.45525 0.05349  0.00568  -0.00360 107 GLU B CG    
865  C CD    . GLU A 108 ? 0.35773 0.23204 0.47592 0.06337  0.00981  -0.00217 107 GLU B CD    
866  O OE1   . GLU A 108 ? 0.40280 0.29286 0.52066 0.06408  0.01599  -0.00644 107 GLU B OE1   
867  O OE2   . GLU A 108 ? 0.38608 0.25888 0.51883 0.06982  0.00669  0.00352  107 GLU B OE2   
868  N N     . ASP A 109 ? 0.28441 0.17680 0.34149 0.01880  -0.00857 0.01055  108 ASP B N     
869  C CA    . ASP A 109 ? 0.32546 0.22714 0.37640 0.00972  -0.01477 0.02013  108 ASP B CA    
870  C C     . ASP A 109 ? 0.29141 0.20499 0.32929 0.00316  -0.01224 0.01437  108 ASP B C     
871  O O     . ASP A 109 ? 0.29164 0.19871 0.32102 -0.00325 -0.01256 0.00979  108 ASP B O     
872  C CB    . ASP A 109 ? 0.29667 0.18166 0.34642 0.00366  -0.02042 0.02655  108 ASP B CB    
873  C CG    . ASP A 109 ? 0.39901 0.29306 0.44095 -0.00672 -0.02503 0.03593  108 ASP B CG    
874  O OD1   . ASP A 109 ? 0.35397 0.26330 0.39614 -0.00676 -0.02675 0.04214  108 ASP B OD1   
875  O OD2   . ASP A 109 ? 0.44659 0.33230 0.48199 -0.01550 -0.02651 0.03661  108 ASP B OD2   
876  N N     . VAL A 110 ? 0.21539 0.14620 0.25313 0.00471  -0.01034 0.01483  109 VAL B N     
877  C CA    . VAL A 110 ? 0.17491 0.11710 0.20285 0.00001  -0.00838 0.01054  109 VAL B CA    
878  C C     . VAL A 110 ? 0.19034 0.14651 0.21773 -0.00405 -0.01090 0.01766  109 VAL B C     
879  O O     . VAL A 110 ? 0.13838 0.10125 0.17209 -0.00060 -0.01190 0.02237  109 VAL B O     
880  C CB    . VAL A 110 ? 0.23724 0.18448 0.26330 0.00540  -0.00250 0.00285  109 VAL B CB    
881  C CG1   . VAL A 110 ? 0.13374 0.09123 0.15055 0.00063  -0.00218 0.00036  109 VAL B CG1   
882  C CG2   . VAL A 110 ? 0.15181 0.08468 0.17550 0.00921  0.00145  -0.00579 109 VAL B CG2   
883  N N     . PRO A 111 ? 0.15603 0.11784 0.17658 -0.01150 -0.01167 0.01802  110 PRO B N     
884  C CA    . PRO A 111 ? 0.13015 0.10429 0.14839 -0.01559 -0.01247 0.02292  110 PRO B CA    
885  C C     . PRO A 111 ? 0.13280 0.11745 0.15262 -0.01128 -0.01021 0.02084  110 PRO B C     
886  O O     . PRO A 111 ? 0.09774 0.08539 0.11608 -0.00893 -0.00696 0.01480  110 PRO B O     
887  C CB    . PRO A 111 ? 0.15126 0.12990 0.16462 -0.02257 -0.01121 0.02038  110 PRO B CB    
888  C CG    . PRO A 111 ? 0.18837 0.15508 0.20208 -0.02460 -0.01256 0.01808  110 PRO B CG    
889  C CD    . PRO A 111 ? 0.14329 0.10065 0.15908 -0.01690 -0.01177 0.01358  110 PRO B CD    
890  N N     . MET A 112 ? 0.15615 0.14583 0.17868 -0.01096 -0.01276 0.02661  111 MET B N     
891  C CA    . MET A 112 ? 0.15050 0.14997 0.17585 -0.00827 -0.01146 0.02549  111 MET B CA    
892  C C     . MET A 112 ? 0.12616 0.13236 0.14854 -0.01315 -0.01555 0.03145  111 MET B C     
893  O O     . MET A 112 ? 0.11260 0.11516 0.13347 -0.01614 -0.02043 0.03848  111 MET B O     
894  C CB    . MET A 112 ? 0.17276 0.17139 0.20918 -0.00061 -0.01054 0.02524  111 MET B CB    
895  C CG    . MET A 112 ? 0.20531 0.19749 0.24239 0.00432  -0.00523 0.01813  111 MET B CG    
896  S SD    . MET A 112 ? 0.19611 0.18935 0.24899 0.01332  -0.00254 0.01836  111 MET B SD    
897  C CE    . MET A 112 ? 0.19454 0.17192 0.24427 0.01723  0.00210  0.01069  111 MET B CE    
898  N N     . VAL A 113 ? 0.12775 0.14256 0.14840 -0.01436 -0.01409 0.02894  112 VAL B N     
899  C CA    . VAL A 113 ? 0.12296 0.14398 0.13912 -0.01962 -0.01818 0.03300  112 VAL B CA    
900  C C     . VAL A 113 ? 0.09361 0.12190 0.11739 -0.01700 -0.01835 0.03168  112 VAL B C     
901  O O     . VAL A 113 ? 0.09234 0.12165 0.11859 -0.01401 -0.01315 0.02604  112 VAL B O     
902  C CB    . VAL A 113 ? 0.15058 0.17372 0.15395 -0.02671 -0.01528 0.02972  112 VAL B CB    
903  C CG1   . VAL A 113 ? 0.12236 0.15097 0.11817 -0.03269 -0.01866 0.03153  112 VAL B CG1   
904  C CG2   . VAL A 113 ? 0.15197 0.16993 0.14914 -0.03096 -0.01506 0.03260  112 VAL B CG2   
905  N N     . LEU A 114 ? 0.09129 0.12467 0.11975 -0.01838 -0.02494 0.03779  113 LEU B N     
906  C CA    . LEU A 114 ? 0.08704 0.12926 0.12430 -0.01777 -0.02595 0.03723  113 LEU B CA    
907  C C     . LEU A 114 ? 0.10142 0.14685 0.12663 -0.02580 -0.02667 0.03415  113 LEU B C     
908  O O     . LEU A 114 ? 0.12273 0.16764 0.13602 -0.03248 -0.03121 0.03692  113 LEU B O     
909  C CB    . LEU A 114 ? 0.09527 0.14339 0.14670 -0.01545 -0.03382 0.04542  113 LEU B CB    
910  C CG    . LEU A 114 ? 0.08816 0.14811 0.15344 -0.01510 -0.03533 0.04572  113 LEU B CG    
911  C CD1   . LEU A 114 ? 0.08067 0.14167 0.15712 -0.00821 -0.02598 0.04029  113 LEU B CD1   
912  C CD2   . LEU A 114 ? 0.09516 0.16274 0.17532 -0.01371 -0.04530 0.05510  113 LEU B CD2   
913  N N     . VAL A 115 ? 0.08301 0.13051 0.11015 -0.02561 -0.02192 0.02835  114 VAL B N     
914  C CA    . VAL A 115 ? 0.08676 0.13430 0.10322 -0.03241 -0.02111 0.02343  114 VAL B CA    
915  C C     . VAL A 115 ? 0.08745 0.14203 0.11257 -0.03499 -0.02430 0.02405  114 VAL B C     
916  O O     . VAL A 115 ? 0.08248 0.13906 0.11862 -0.03099 -0.02021 0.02288  114 VAL B O     
917  C CB    . VAL A 115 ? 0.08172 0.12319 0.09331 -0.03039 -0.01293 0.01609  114 VAL B CB    
918  C CG1   . VAL A 115 ? 0.09197 0.13152 0.09460 -0.03628 -0.01126 0.01008  114 VAL B CG1   
919  C CG2   . VAL A 115 ? 0.08268 0.11963 0.08865 -0.02870 -0.01038 0.01573  114 VAL B CG2   
920  N N     . GLY A 116 ? 0.09729 0.15560 0.11623 -0.04277 -0.03151 0.02585  115 GLY B N     
921  C CA    . GLY A 116 ? 0.10009 0.16523 0.12602 -0.04772 -0.03568 0.02578  115 GLY B CA    
922  C C     . GLY A 116 ? 0.11202 0.17058 0.12465 -0.05456 -0.03239 0.01725  115 GLY B C     
923  O O     . GLY A 116 ? 0.12029 0.17598 0.11664 -0.06211 -0.03565 0.01470  115 GLY B O     
924  N N     . ASN A 117 ? 0.11443 0.16930 0.13284 -0.05212 -0.02560 0.01272  116 ASN B N     
925  C CA    . ASN A 117 ? 0.14456 0.18954 0.15216 -0.05609 -0.02083 0.00416  116 ASN B CA    
926  C C     . ASN A 117 ? 0.15418 0.20035 0.16464 -0.06432 -0.02467 0.00216  116 ASN B C     
927  O O     . ASN A 117 ? 0.14693 0.20368 0.17065 -0.06641 -0.03029 0.00782  116 ASN B O     
928  C CB    . ASN A 117 ? 0.12164 0.15946 0.13283 -0.04845 -0.01207 0.00146  116 ASN B CB    
929  C CG    . ASN A 117 ? 0.14852 0.17493 0.15113 -0.05047 -0.00708 -0.00688 116 ASN B CG    
930  O OD1   . ASN A 117 ? 0.13843 0.16086 0.12868 -0.05458 -0.00660 -0.01243 116 ASN B OD1   
931  N ND2   . ASN A 117 ? 0.10504 0.12560 0.11410 -0.04766 -0.00301 -0.00768 116 ASN B ND2   
932  N N     . LYS A 118 ? 0.12787 0.16292 0.12705 -0.06910 -0.02135 -0.00645 117 LYS B N     
933  C CA    . LYS A 118 ? 0.14120 0.17319 0.13898 -0.07883 -0.02489 -0.01062 117 LYS B CA    
934  C C     . LYS A 118 ? 0.18725 0.22678 0.17727 -0.08879 -0.03555 -0.00918 117 LYS B C     
935  O O     . LYS A 118 ? 0.19351 0.23655 0.19002 -0.09319 -0.04075 -0.00762 117 LYS B O     
936  C CB    . LYS A 118 ? 0.16951 0.20527 0.18545 -0.07830 -0.02409 -0.00640 117 LYS B CB    
937  C CG    . LYS A 118 ? 0.12320 0.15255 0.14519 -0.06882 -0.01497 -0.00548 117 LYS B CG    
938  C CD    . LYS A 118 ? 0.12888 0.15654 0.16208 -0.07180 -0.01286 -0.00350 117 LYS B CD    
939  C CE    . LYS A 118 ? 0.12158 0.14254 0.15770 -0.06328 -0.00489 -0.00122 117 LYS B CE    
940  N NZ    . LYS A 118 ? 0.12177 0.14071 0.16702 -0.06745 -0.00242 0.00208  117 LYS B NZ    
941  N N     . SER A 119 ? 0.15953 0.19980 0.13508 -0.08923 -0.03754 -0.00872 118 SER B N     
942  C CA    . SER A 119 ? 0.17748 0.22169 0.14264 -0.09452 -0.04603 -0.00528 118 SER B CA    
943  C C     . SER A 119 ? 0.24857 0.28320 0.19850 -0.10284 -0.04614 -0.01407 118 SER B C     
944  O O     . SER A 119 ? 0.22348 0.26115 0.16477 -0.10867 -0.05376 -0.01143 118 SER B O     
945  C CB    . SER A 119 ? 0.22472 0.26953 0.17605 -0.09346 -0.04634 -0.00210 118 SER B CB    
946  O OG    . SER A 119 ? 0.24916 0.30088 0.21409 -0.08571 -0.04604 0.00515  118 SER B OG    
947  N N     . ASP A 120 ? 0.20231 0.22465 0.14924 -0.10338 -0.03808 -0.02424 119 ASP B N     
948  C CA    . ASP A 120 ? 0.22545 0.23696 0.16056 -0.11045 -0.03756 -0.03336 119 ASP B CA    
949  C C     . ASP A 120 ? 0.22896 0.24371 0.17757 -0.11482 -0.04415 -0.03095 119 ASP B C     
950  O O     . ASP A 120 ? 0.26347 0.27044 0.20292 -0.12190 -0.04599 -0.03758 119 ASP B O     
951  C CB    . ASP A 120 ? 0.24143 0.23697 0.17138 -0.10781 -0.02606 -0.04496 119 ASP B CB    
952  C CG    . ASP A 120 ? 0.23407 0.22698 0.18288 -0.10217 -0.02186 -0.04340 119 ASP B CG    
953  O OD1   . ASP A 120 ? 0.19224 0.19088 0.14877 -0.09582 -0.01904 -0.03874 119 ASP B OD1   
954  O OD2   . ASP A 120 ? 0.21843 0.20334 0.17417 -0.10468 -0.02165 -0.04614 119 ASP B OD2   
955  N N     . LEU A 121 ? 0.22384 0.24954 0.19387 -0.11101 -0.04674 -0.02245 120 LEU B N     
956  C CA    . LEU A 121 ? 0.21411 0.24136 0.19844 -0.11513 -0.04972 -0.02178 120 LEU B CA    
957  C C     . LEU A 121 ? 0.23247 0.27314 0.22179 -0.12024 -0.06101 -0.01559 120 LEU B C     
958  O O     . LEU A 121 ? 0.21778 0.26995 0.20865 -0.11743 -0.06653 -0.00775 120 LEU B O     
959  C CB    . LEU A 121 ? 0.20712 0.23968 0.21343 -0.10913 -0.04495 -0.01609 120 LEU B CB    
960  C CG    . LEU A 121 ? 0.24618 0.26253 0.24953 -0.10628 -0.03483 -0.02233 120 LEU B CG    
961  C CD1   . LEU A 121 ? 0.28836 0.30919 0.31074 -0.10141 -0.02986 -0.01557 120 LEU B CD1   
962  C CD2   . LEU A 121 ? 0.22446 0.22375 0.21850 -0.11261 -0.03340 -0.03198 120 LEU B CD2   
963  N N     . PRO A 122 ? 0.23832 0.27713 0.23111 -0.12783 -0.06493 -0.01873 121 PRO B N     
964  C CA    . PRO A 122 ? 0.25314 0.30531 0.25229 -0.13341 -0.07628 -0.01318 121 PRO B CA    
965  C C     . PRO A 122 ? 0.23250 0.30277 0.26082 -0.12959 -0.07881 -0.00356 121 PRO B C     
966  O O     . PRO A 122 ? 0.24224 0.32420 0.28016 -0.13439 -0.08780 0.00051  121 PRO B O     
967  C CB    . PRO A 122 ? 0.27381 0.31496 0.26481 -0.14361 -0.07823 -0.02216 121 PRO B CB    
968  C CG    . PRO A 122 ? 0.26622 0.29472 0.26387 -0.14117 -0.06807 -0.02743 121 PRO B CG    
969  C CD    . PRO A 122 ? 0.26284 0.28616 0.25432 -0.13186 -0.05946 -0.02751 121 PRO B CD    
970  N N     . SER A 123 ? 0.22159 0.29489 0.26429 -0.12128 -0.07079 -0.00012 122 SER B N     
971  C CA    . SER A 123 ? 0.21775 0.30645 0.28817 -0.11789 -0.06959 0.00686  122 SER B CA    
972  C C     . SER A 123 ? 0.17889 0.28080 0.26118 -0.10771 -0.06945 0.01541  122 SER B C     
973  O O     . SER A 123 ? 0.16360 0.27356 0.26461 -0.10144 -0.06286 0.01926  122 SER B O     
974  C CB    . SER A 123 ? 0.18967 0.27034 0.26779 -0.11744 -0.05910 0.00392  122 SER B CB    
975  O OG    . SER A 123 ? 0.17947 0.24844 0.24651 -0.11134 -0.05120 0.00156  122 SER B OG    
976  N N     . ARG A 124 ? 0.21218 0.31564 0.28318 -0.10628 -0.07645 0.01849  123 ARG B N     
977  C CA    . ARG A 124 ? 0.20565 0.31757 0.28547 -0.09640 -0.07640 0.02616  123 ARG B CA    
978  C C     . ARG A 124 ? 0.19581 0.32566 0.30497 -0.09143 -0.07759 0.03326  123 ARG B C     
979  O O     . ARG A 124 ? 0.17361 0.31333 0.29332 -0.09655 -0.08489 0.03540  123 ARG B O     
980  C CB    . ARG A 124 ? 0.18908 0.29903 0.25179 -0.09773 -0.08521 0.02954  123 ARG B CB    
981  C CG    . ARG A 124 ? 0.18231 0.30070 0.25658 -0.08832 -0.08754 0.03885  123 ARG B CG    
982  C CD    . ARG A 124 ? 0.18716 0.30152 0.24272 -0.09102 -0.09613 0.04319  123 ARG B CD    
983  N NE    . ARG A 124 ? 0.21516 0.31489 0.24360 -0.09383 -0.09119 0.03716  123 ARG B NE    
984  C CZ    . ARG A 124 ? 0.26608 0.36099 0.29027 -0.08747 -0.08536 0.03801  123 ARG B CZ    
985  N NH1   . ARG A 124 ? 0.21059 0.31225 0.25479 -0.07760 -0.08323 0.04395  123 ARG B NH1   
986  N NH2   . ARG A 124 ? 0.18529 0.26837 0.18503 -0.09114 -0.08095 0.03216  123 ARG B NH2   
987  N N     . THR A 125 ? 0.17417 0.30841 0.29672 -0.08137 -0.06986 0.03637  124 THR B N     
988  C CA    . THR A 125 ? 0.13853 0.28920 0.28838 -0.07446 -0.06915 0.04247  124 THR B CA    
989  C C     . THR A 125 ? 0.13155 0.28469 0.28641 -0.06398 -0.07013 0.04840  124 THR B C     
990  O O     . THR A 125 ? 0.13062 0.29651 0.30787 -0.05763 -0.07091 0.05348  124 THR B O     
991  C CB    . THR A 125 ? 0.12775 0.28210 0.29244 -0.07188 -0.05652 0.03999  124 THR B CB    
992  O OG1   . THR A 125 ? 0.11451 0.25953 0.27116 -0.06518 -0.04710 0.03824  124 THR B OG1   
993  C CG2   . THR A 125 ? 0.13583 0.28504 0.29580 -0.08225 -0.05475 0.03466  124 THR B CG2   
994  N N     . VAL A 126 ? 0.12792 0.26896 0.26378 -0.06194 -0.06946 0.04756  125 VAL B N     
995  C CA    . VAL A 126 ? 0.18499 0.32561 0.32380 -0.05291 -0.07075 0.05316  125 VAL B CA    
996  C C     . VAL A 126 ? 0.14922 0.28377 0.26893 -0.05803 -0.08189 0.05674  125 VAL B C     
997  O O     . VAL A 126 ? 0.20994 0.33345 0.30524 -0.06480 -0.08196 0.05203  125 VAL B O     
998  C CB    . VAL A 126 ? 0.13494 0.26671 0.26743 -0.04683 -0.06049 0.04987  125 VAL B CB    
999  C CG1   . VAL A 126 ? 0.14761 0.27823 0.28530 -0.03749 -0.06189 0.05551  125 VAL B CG1   
1000 C CG2   . VAL A 126 ? 0.12762 0.26297 0.27310 -0.04375 -0.04840 0.04584  125 VAL B CG2   
1001 N N     . ASP A 127 ? 0.21074 0.35181 0.34055 -0.05517 -0.09072 0.06490  126 ASP B N     
1002 C CA    . ASP A 127 ? 0.23409 0.36806 0.34277 -0.06112 -0.10065 0.06896  126 ASP B CA    
1003 C C     . ASP A 127 ? 0.25217 0.37550 0.34932 -0.05603 -0.09778 0.07115  126 ASP B C     
1004 O O     . ASP A 127 ? 0.22516 0.34902 0.33697 -0.04607 -0.09161 0.07235  126 ASP B O     
1005 C CB    . ASP A 127 ? 0.43068 0.57436 0.55164 -0.06201 -0.11288 0.07770  126 ASP B CB    
1006 C CG    . ASP A 127 ? 0.43937 0.58897 0.58461 -0.05028 -0.11332 0.08519  126 ASP B CG    
1007 O OD1   . ASP A 127 ? 0.42116 0.56189 0.55859 -0.04641 -0.11487 0.08992  126 ASP B OD1   
1008 O OD2   . ASP A 127 ? 0.54352 0.70639 0.71588 -0.04529 -0.11185 0.08606  126 ASP B OD2   
1009 N N     . THR A 128 ? 0.22418 0.33732 0.29395 -0.06353 -0.10136 0.07086  127 THR B N     
1010 C CA    . THR A 128 ? 0.24671 0.34934 0.30308 -0.06063 -0.09724 0.07155  127 THR B CA    
1011 C C     . THR A 128 ? 0.26047 0.36298 0.32869 -0.05334 -0.10236 0.08172  127 THR B C     
1012 O O     . THR A 128 ? 0.20361 0.29965 0.27265 -0.04700 -0.09735 0.08253  127 THR B O     
1013 C CB    . THR A 128 ? 0.30324 0.39565 0.32722 -0.07111 -0.09773 0.06772  127 THR B CB    
1014 O OG1   . THR A 128 ? 0.47228 0.56286 0.48633 -0.07567 -0.10733 0.07598  127 THR B OG1   
1015 C CG2   . THR A 128 ? 0.21630 0.30884 0.23039 -0.07952 -0.09624 0.05873  127 THR B CG2   
1016 N N     . LYS A 129 ? 0.23818 0.34750 0.31736 -0.05380 -0.11240 0.08941  128 LYS B N     
1017 C CA    . LYS A 129 ? 0.30900 0.41758 0.40284 -0.04590 -0.11712 0.09886  128 LYS B CA    
1018 C C     . LYS A 129 ? 0.25210 0.36334 0.37108 -0.03298 -0.10841 0.09691  128 LYS B C     
1019 O O     . LYS A 129 ? 0.21778 0.32124 0.34078 -0.02594 -0.10673 0.10037  128 LYS B O     
1020 C CB    . LYS A 129 ? 0.21701 0.33470 0.32269 -0.04787 -0.12946 0.10709  128 LYS B CB    
1021 C CG    . LYS A 129 ? 0.28426 0.39998 0.40468 -0.04015 -0.13544 0.11732  128 LYS B CG    
1022 C CD    . LYS A 129 ? 0.24790 0.37669 0.39020 -0.03890 -0.14626 0.12467  128 LYS B CD    
1023 C CE    . LYS A 129 ? 0.43676 0.56091 0.58497 -0.03518 -0.15575 0.13633  128 LYS B CE    
1024 N NZ    . LYS A 129 ? 0.61618 0.73046 0.73335 -0.04675 -0.16401 0.14164  128 LYS B NZ    
1025 N N     . GLN A 130 ? 0.21856 0.33990 0.35384 -0.03021 -0.10214 0.09093  129 GLN B N     
1026 C CA    . GLN A 130 ? 0.22043 0.34390 0.37623 -0.01894 -0.09148 0.08726  129 GLN B CA    
1027 C C     . GLN A 130 ? 0.14389 0.25501 0.28584 -0.01645 -0.08353 0.08311  129 GLN B C     
1028 O O     . GLN A 130 ? 0.14187 0.24740 0.29351 -0.00723 -0.07918 0.08402  129 GLN B O     
1029 C CB    . GLN A 130 ? 0.24868 0.38373 0.41759 -0.01941 -0.08446 0.08059  129 GLN B CB    
1030 C CG    . GLN A 130 ? 0.28667 0.43639 0.48322 -0.01521 -0.08670 0.08365  129 GLN B CG    
1031 C CD    . GLN A 130 ? 0.44791 0.60833 0.65391 -0.01815 -0.07934 0.07705  129 GLN B CD    
1032 O OE1   . GLN A 130 ? 0.44209 0.60541 0.63846 -0.02830 -0.08381 0.07528  129 GLN B OE1   
1033 N NE2   . GLN A 130 ? 0.40869 0.57352 0.63169 -0.00993 -0.06726 0.07286  129 GLN B NE2   
1034 N N     . ALA A 131 ? 0.13101 0.23770 0.25096 -0.02460 -0.08120 0.07773  130 ALA B N     
1035 C CA    . ALA A 131 ? 0.17080 0.26780 0.27837 -0.02300 -0.07401 0.07354  130 ALA B CA    
1036 C C     . ALA A 131 ? 0.13175 0.21720 0.22616 -0.02322 -0.07876 0.07958  130 ALA B C     
1037 O O     . ALA A 131 ? 0.15422 0.23172 0.24952 -0.01723 -0.07384 0.07907  130 ALA B O     
1038 C CB    . ALA A 131 ? 0.14698 0.24282 0.23554 -0.03202 -0.07055 0.06594  130 ALA B CB    
1039 N N     . GLN A 132 ? 0.15907 0.24264 0.24022 -0.03082 -0.08799 0.08527  131 GLN B N     
1040 C CA    . GLN A 132 ? 0.16357 0.23613 0.23261 -0.03210 -0.09226 0.09203  131 GLN B CA    
1041 C C     . GLN A 132 ? 0.18972 0.25910 0.28056 -0.02101 -0.09304 0.09757  131 GLN B C     
1042 O O     . GLN A 132 ? 0.19957 0.25751 0.28645 -0.01770 -0.09041 0.09902  131 GLN B O     
1043 C CB    . GLN A 132 ? 0.20347 0.27605 0.25634 -0.04237 -0.10191 0.09747  131 GLN B CB    
1044 C CG    . GLN A 132 ? 0.22929 0.30108 0.25613 -0.05392 -0.09974 0.09060  131 GLN B CG    
1045 C CD    . GLN A 132 ? 0.35848 0.42975 0.36851 -0.06423 -0.10871 0.09534  131 GLN B CD    
1046 O OE1   . GLN A 132 ? 0.34277 0.41780 0.36400 -0.06299 -0.11821 0.10395  131 GLN B OE1   
1047 N NE2   . GLN A 132 ? 0.36074 0.42745 0.34411 -0.07438 -0.10543 0.08932  131 GLN B NE2   
1048 N N     . ASP A 133 ? 0.17094 0.24998 0.28549 -0.01519 -0.09593 0.09991  132 ASP B N     
1049 C CA    . ASP A 133 ? 0.18543 0.26167 0.32222 -0.00409 -0.09588 0.10390  132 ASP B CA    
1050 C C     . ASP A 133 ? 0.15671 0.22799 0.30331 0.00544  -0.08389 0.09652  132 ASP B C     
1051 O O     . ASP A 133 ? 0.17312 0.23370 0.32648 0.01273  -0.08202 0.09801  132 ASP B O     
1052 C CB    . ASP A 133 ? 0.17735 0.26730 0.33826 -0.00022 -0.10051 0.10695  132 ASP B CB    
1053 C CG    . ASP A 133 ? 0.27995 0.37366 0.43343 -0.00857 -0.11393 0.11558  132 ASP B CG    
1054 O OD1   . ASP A 133 ? 0.26675 0.35076 0.39667 -0.01644 -0.11905 0.11975  132 ASP B OD1   
1055 O OD2   . ASP A 133 ? 0.23586 0.34263 0.40680 -0.00771 -0.11906 0.11808  132 ASP B OD2   
1056 N N     . LEU A 134 ? 0.13950 0.21770 0.28703 0.00535  -0.07554 0.08823  133 LEU B N     
1057 C CA    . LEU A 134 ? 0.12764 0.20094 0.28226 0.01362  -0.06386 0.08091  133 LEU B CA    
1058 C C     . LEU A 134 ? 0.15086 0.20869 0.28695 0.01198  -0.06259 0.08070  133 LEU B C     
1059 O O     . LEU A 134 ? 0.17043 0.21667 0.31190 0.01929  -0.05835 0.07945  133 LEU B O     
1060 C CB    . LEU A 134 ? 0.11660 0.20063 0.27419 0.01241  -0.05544 0.07292  133 LEU B CB    
1061 C CG    . LEU A 134 ? 0.17289 0.25235 0.33689 0.02061  -0.04245 0.06498  133 LEU B CG    
1062 C CD1   . LEU A 134 ? 0.22347 0.30491 0.40979 0.03079  -0.03710 0.06335  133 LEU B CD1   
1063 C CD2   . LEU A 134 ? 0.12871 0.21460 0.28632 0.01647  -0.03403 0.05743  133 LEU B CD2   
1064 N N     . ALA A 135 ? 0.16308 0.21984 0.27642 0.00178  -0.06592 0.08136  134 ALA B N     
1065 C CA    . ALA A 135 ? 0.19652 0.23917 0.29002 -0.00152 -0.06344 0.08040  134 ALA B CA    
1066 C C     . ALA A 135 ? 0.22586 0.25596 0.31928 0.00008  -0.06918 0.08855  134 ALA B C     
1067 O O     . ALA A 135 ? 0.18480 0.20121 0.27457 0.00271  -0.06524 0.08748  134 ALA B O     
1068 C CB    . ALA A 135 ? 0.17035 0.21452 0.23838 -0.01365 -0.06433 0.07824  134 ALA B CB    
1069 N N     . ARG A 136 ? 0.20215 0.23553 0.29857 -0.00233 -0.07791 0.09586  135 ARG B N     
1070 C CA    . ARG A 136 ? 0.25004 0.27174 0.34793 -0.00066 -0.08309 0.10330  135 ARG B CA    
1071 C C     . ARG A 136 ? 0.23232 0.24692 0.35185 0.01200  -0.07786 0.10043  135 ARG B C     
1072 O O     . ARG A 136 ? 0.21027 0.20931 0.32688 0.01407  -0.07667 0.10158  135 ARG B O     
1073 C CB    . ARG A 136 ? 0.23402 0.26235 0.33362 -0.00485 -0.09411 0.11199  135 ARG B CB    
1074 C CG    . ARG A 136 ? 0.30031 0.31782 0.40549 -0.00186 -0.10048 0.12075  135 ARG B CG    
1075 C CD    . ARG A 136 ? 0.42799 0.45147 0.53115 -0.00765 -0.11265 0.13055  135 ARG B CD    
1076 N NE    . ARG A 136 ? 0.49470 0.52400 0.57381 -0.02055 -0.11534 0.13026  135 ARG B NE    
1077 C CZ    . ARG A 136 ? 0.40624 0.44889 0.48661 -0.02451 -0.11916 0.12928  135 ARG B CZ    
1078 N NH1   . ARG A 136 ? 0.41660 0.47001 0.52203 -0.01714 -0.12150 0.12971  135 ARG B NH1   
1079 N NH2   . ARG A 136 ? 0.42990 0.47496 0.48585 -0.03641 -0.12006 0.12719  135 ARG B NH2   
1080 N N     . SER A 137 ? 0.21092 0.23637 0.35157 0.01997  -0.07366 0.09574  136 SER B N     
1081 C CA    . SER A 137 ? 0.24702 0.26611 0.40685 0.03195  -0.06637 0.09070  136 SER B CA    
1082 C C     . SER A 137 ? 0.21481 0.22093 0.36629 0.03426  -0.05655 0.08223  136 SER B C     
1083 O O     . SER A 137 ? 0.24699 0.24029 0.40602 0.04172  -0.05163 0.07838  136 SER B O     
1084 C CB    . SER A 137 ? 0.22319 0.25835 0.40486 0.03846  -0.06160 0.08614  136 SER B CB    
1085 O OG    . SER A 137 ? 0.18574 0.22883 0.36287 0.03659  -0.05335 0.07812  136 SER B OG    
1086 N N     . TYR A 138 ? 0.21191 0.22039 0.34760 0.02777  -0.05389 0.07902  137 TYR B N     
1087 C CA    . TYR A 138 ? 0.18318 0.17923 0.30827 0.02803  -0.04585 0.07157  137 TYR B CA    
1088 C C     . TYR A 138 ? 0.19458 0.17568 0.30049 0.02023  -0.04996 0.07613  137 TYR B C     
1089 O O     . TYR A 138 ? 0.18553 0.15454 0.28219 0.01936  -0.04322 0.06872  137 TYR B O     
1090 C CB    . TYR A 138 ? 0.15583 0.16233 0.26822 0.02287  -0.03806 0.06204  137 TYR B CB    
1091 C CG    . TYR A 138 ? 0.16895 0.18809 0.29721 0.02920  -0.03098 0.05594  137 TYR B CG    
1092 C CD1   . TYR A 138 ? 0.19421 0.21399 0.34640 0.04008  -0.02804 0.05553  137 TYR B CD1   
1093 C CD2   . TYR A 138 ? 0.17518 0.20522 0.29521 0.02418  -0.02637 0.05052  137 TYR B CD2   
1094 C CE1   . TYR A 138 ? 0.22730 0.26027 0.39433 0.04505  -0.01977 0.04981  137 TYR B CE1   
1095 C CE2   . TYR A 138 ? 0.19716 0.23860 0.33096 0.02860  -0.01924 0.04578  137 TYR B CE2   
1096 C CZ    . TYR A 138 ? 0.19905 0.24282 0.35598 0.03862  -0.01555 0.04545  137 TYR B CZ    
1097 O OH    . TYR A 138 ? 0.18190 0.23845 0.35284 0.04222  -0.00694 0.04079  137 TYR B OH    
1098 N N     . GLY A 139 ? 0.16672 0.14958 0.26405 0.01296  -0.05959 0.08640  138 GLY B N     
1099 C CA    . GLY A 139 ? 0.23132 0.20327 0.30806 0.00332  -0.06179 0.09054  138 GLY B CA    
1100 C C     . GLY A 139 ? 0.20848 0.18484 0.26583 -0.00523 -0.05553 0.08367  138 GLY B C     
1101 O O     . GLY A 139 ? 0.22671 0.19348 0.27151 -0.01103 -0.05242 0.08225  138 GLY B O     
1102 N N     . ILE A 140 ? 0.19916 0.19041 0.25460 -0.00649 -0.05271 0.07806  139 ILE B N     
1103 C CA    . ILE A 140 ? 0.13996 0.13606 0.17890 -0.01349 -0.04570 0.06969  139 ILE B CA    
1104 C C     . ILE A 140 ? 0.20070 0.20746 0.22799 -0.02169 -0.05042 0.07326  139 ILE B C     
1105 O O     . ILE A 140 ? 0.18325 0.19663 0.21724 -0.02120 -0.05887 0.08040  139 ILE B O     
1106 C CB    . ILE A 140 ? 0.14175 0.14251 0.18699 -0.00773 -0.03656 0.05787  139 ILE B CB    
1107 C CG1   . ILE A 140 ? 0.12895 0.14233 0.18703 -0.00348 -0.03789 0.05777  139 ILE B CG1   
1108 C CG2   . ILE A 140 ? 0.22438 0.21351 0.27686 -0.00101 -0.03168 0.05299  139 ILE B CG2   
1109 C CD1   . ILE A 140 ? 0.12966 0.14734 0.19160 0.00071  -0.02871 0.04761  139 ILE B CD1   
1110 N N     . PRO A 141 ? 0.17216 0.18116 0.18252 -0.02946 -0.04522 0.06790  140 PRO B N     
1111 C CA    . PRO A 141 ? 0.15199 0.16972 0.14921 -0.03750 -0.04786 0.06832  140 PRO B CA    
1112 C C     . PRO A 141 ? 0.13105 0.15886 0.13678 -0.03434 -0.04683 0.06234  140 PRO B C     
1113 O O     . PRO A 141 ? 0.11898 0.14779 0.13625 -0.02732 -0.04066 0.05554  140 PRO B O     
1114 C CB    . PRO A 141 ? 0.18086 0.19735 0.16172 -0.04450 -0.03950 0.06176  140 PRO B CB    
1115 C CG    . PRO A 141 ? 0.16012 0.16687 0.14367 -0.04306 -0.03685 0.06349  140 PRO B CG    
1116 C CD    . PRO A 141 ? 0.14528 0.14846 0.14768 -0.03219 -0.03738 0.06200  140 PRO B CD    
1117 N N     . PHE A 142 ? 0.15139 0.18616 0.14943 -0.04093 -0.05311 0.06510  141 PHE B N     
1118 C CA    . PHE A 142 ? 0.13114 0.17500 0.13370 -0.04141 -0.05269 0.05945  141 PHE B CA    
1119 C C     . PHE A 142 ? 0.15977 0.20430 0.14073 -0.05157 -0.05039 0.05377  141 PHE B C     
1120 O O     . PHE A 142 ? 0.17512 0.21822 0.13916 -0.05993 -0.05555 0.05880  141 PHE B O     
1121 C CB    . PHE A 142 ? 0.14890 0.20136 0.16577 -0.04010 -0.06370 0.06755  141 PHE B CB    
1122 C CG    . PHE A 142 ? 0.13242 0.19446 0.15074 -0.04438 -0.06505 0.06279  141 PHE B CG    
1123 C CD1   . PHE A 142 ? 0.11785 0.18190 0.14479 -0.04039 -0.05600 0.05381  141 PHE B CD1   
1124 C CD2   . PHE A 142 ? 0.19071 0.25685 0.19969 -0.05295 -0.07397 0.06645  141 PHE B CD2   
1125 C CE1   . PHE A 142 ? 0.11714 0.18826 0.14559 -0.04534 -0.05718 0.04972  141 PHE B CE1   
1126 C CE2   . PHE A 142 ? 0.15367 0.22591 0.16348 -0.05740 -0.07438 0.06099  141 PHE B CE2   
1127 C CZ    . PHE A 142 ? 0.15619 0.23283 0.17687 -0.05463 -0.06784 0.05357  141 PHE B CZ    
1128 N N     . ILE A 143 ? 0.12964 0.17514 0.11032 -0.05092 -0.04221 0.04327  142 ILE B N     
1129 C CA    . ILE A 143 ? 0.15351 0.19772 0.11604 -0.05878 -0.03745 0.03532  142 ILE B CA    
1130 C C     . ILE A 143 ? 0.13431 0.18249 0.10112 -0.06027 -0.03812 0.02964  142 ILE B C     
1131 O O     . ILE A 143 ? 0.15097 0.20014 0.13266 -0.05364 -0.03412 0.02649  142 ILE B O     
1132 C CB    . ILE A 143 ? 0.17391 0.21332 0.13335 -0.05621 -0.02584 0.02740  142 ILE B CB    
1133 C CG1   . ILE A 143 ? 0.20229 0.23790 0.15877 -0.05600 -0.02479 0.03279  142 ILE B CG1   
1134 C CG2   . ILE A 143 ? 0.21213 0.25045 0.15639 -0.06284 -0.01969 0.01795  142 ILE B CG2   
1135 C CD1   . ILE A 143 ? 0.22388 0.25848 0.16120 -0.06587 -0.02829 0.03827  142 ILE B CD1   
1136 N N     . GLU A 144 ? 0.18470 0.23408 0.13670 -0.06994 -0.04273 0.02794  143 GLU B N     
1137 C CA    . GLU A 144 ? 0.21276 0.26384 0.16663 -0.07341 -0.04323 0.02138  143 GLU B CA    
1138 C C     . GLU A 144 ? 0.26900 0.31231 0.21277 -0.07459 -0.03199 0.00895  143 GLU B C     
1139 O O     . GLU A 144 ? 0.20194 0.24109 0.12763 -0.07960 -0.02751 0.00463  143 GLU B O     
1140 C CB    . GLU A 144 ? 0.23517 0.28952 0.17839 -0.08314 -0.05366 0.02472  143 GLU B CB    
1141 C CG    . GLU A 144 ? 0.31772 0.37880 0.27497 -0.07983 -0.06407 0.03744  143 GLU B CG    
1142 C CD    . GLU A 144 ? 0.44541 0.50725 0.39361 -0.08732 -0.07215 0.04066  143 GLU B CD    
1143 O OE1   . GLU A 144 ? 0.40816 0.47161 0.35751 -0.09128 -0.07342 0.03543  143 GLU B OE1   
1144 O OE2   . GLU A 144 ? 0.38360 0.44384 0.32332 -0.08984 -0.07743 0.04849  143 GLU B OE2   
1145 N N     . THR A 145 ? 0.15609 0.19742 0.11216 -0.06994 -0.02708 0.00356  144 THR B N     
1146 C CA    . THR A 145 ? 0.19027 0.22337 0.14167 -0.06865 -0.01682 -0.00712 144 THR B CA    
1147 C C     . THR A 145 ? 0.21637 0.24536 0.16937 -0.07264 -0.01719 -0.01340 144 THR B C     
1148 O O     . THR A 145 ? 0.18408 0.21817 0.14741 -0.07428 -0.02380 -0.00889 144 THR B O     
1149 C CB    . THR A 145 ? 0.19327 0.22463 0.15786 -0.05801 -0.00962 -0.00705 144 THR B CB    
1150 O OG1   . THR A 145 ? 0.11379 0.14728 0.09442 -0.05296 -0.01133 -0.00343 144 THR B OG1   
1151 C CG2   . THR A 145 ? 0.13306 0.16741 0.09769 -0.05466 -0.00965 -0.00101 144 THR B CG2   
1152 N N     . SER A 146 ? 0.15887 0.17848 0.10315 -0.07418 -0.00950 -0.02407 145 SER B N     
1153 C CA    . SER A 146 ? 0.18404 0.19543 0.13324 -0.07510 -0.00715 -0.03072 145 SER B CA    
1154 C C     . SER A 146 ? 0.17832 0.18085 0.13068 -0.06774 0.00353  -0.03795 145 SER B C     
1155 O O     . SER A 146 ? 0.19522 0.19356 0.13630 -0.06928 0.00989  -0.04597 145 SER B O     
1156 C CB    . SER A 146 ? 0.18596 0.19233 0.11981 -0.08704 -0.01090 -0.03793 145 SER B CB    
1157 O OG    . SER A 146 ? 0.20258 0.19643 0.13903 -0.08751 -0.00591 -0.04689 145 SER B OG    
1158 N N     . ALA A 147 ? 0.15235 0.15257 0.12019 -0.05997 0.00554  -0.03493 146 ALA B N     
1159 C CA    . ALA A 147 ? 0.15687 0.14800 0.12987 -0.05307 0.01362  -0.04094 146 ALA B CA    
1160 C C     . ALA A 147 ? 0.20733 0.18528 0.17367 -0.05756 0.01762  -0.05225 146 ALA B C     
1161 O O     . ALA A 147 ? 0.20637 0.17707 0.17488 -0.05248 0.02532  -0.05960 146 ALA B O     
1162 C CB    . ALA A 147 ? 0.14844 0.13831 0.13627 -0.04572 0.01312  -0.03434 146 ALA B CB    
1163 N N     . LYS A 148 ? 0.18111 0.15573 0.14052 -0.06706 0.01248  -0.05432 147 LYS B N     
1164 C CA    . LYS A 148 ? 0.21839 0.17767 0.17105 -0.07187 0.01622  -0.06609 147 LYS B CA    
1165 C C     . LYS A 148 ? 0.27409 0.23094 0.20790 -0.07727 0.02124  -0.07714 147 LYS B C     
1166 O O     . LYS A 148 ? 0.30396 0.24976 0.23666 -0.07403 0.02937  -0.08680 147 LYS B O     
1167 C CB    . LYS A 148 ? 0.23153 0.18759 0.18396 -0.08147 0.00853  -0.06476 147 LYS B CB    
1168 C CG    . LYS A 148 ? 0.25981 0.19878 0.20662 -0.08524 0.01156  -0.07539 147 LYS B CG    
1169 C CD    . LYS A 148 ? 0.29178 0.23084 0.24057 -0.09362 0.00294  -0.07157 147 LYS B CD    
1170 C CE    . LYS A 148 ? 0.35366 0.27529 0.29758 -0.09639 0.00520  -0.08113 147 LYS B CE    
1171 N NZ    . LYS A 148 ? 0.39596 0.31990 0.34036 -0.10612 -0.00407 -0.07812 147 LYS B NZ    
1172 N N     . THR A 149 ? 0.26443 0.23276 0.18544 -0.08328 0.01638  -0.07290 148 THR B N     
1173 C CA    . THR A 149 ? 0.24242 0.21109 0.14634 -0.08665 0.02112  -0.07841 148 THR B CA    
1174 C C     . THR A 149 ? 0.26706 0.24346 0.17010 -0.08174 0.02843  -0.07782 148 THR B C     
1175 O O     . THR A 149 ? 0.29350 0.27046 0.18493 -0.08403 0.03463  -0.08232 148 THR B O     
1176 C CB    . THR A 149 ? 0.25347 0.22881 0.14334 -0.09653 0.01100  -0.07249 148 THR B CB    
1177 O OG1   . THR A 149 ? 0.25948 0.24816 0.15185 -0.09635 0.00408  -0.06072 148 THR B OG1   
1178 C CG2   . THR A 149 ? 0.25934 0.23017 0.15383 -0.10141 0.00274  -0.07167 148 THR B CG2   
1179 N N     . ARG A 150 ? 0.21086 0.19397 0.12792 -0.07461 0.02769  -0.07083 149 ARG B N     
1180 C CA    . ARG A 150 ? 0.23258 0.22495 0.15389 -0.06885 0.03269  -0.06682 149 ARG B CA    
1181 C C     . ARG A 150 ? 0.26071 0.26289 0.16847 -0.07580 0.02652  -0.05846 149 ARG B C     
1182 O O     . ARG A 150 ? 0.19368 0.20315 0.10374 -0.07284 0.02954  -0.05383 149 ARG B O     
1183 C CB    . ARG A 150 ? 0.23896 0.22821 0.15895 -0.06592 0.04633  -0.07857 149 ARG B CB    
1184 C CG    . ARG A 150 ? 0.37276 0.36990 0.31172 -0.05539 0.05128  -0.07440 149 ARG B CG    
1185 C CD    . ARG A 150 ? 0.42705 0.42998 0.36319 -0.05558 0.06237  -0.08027 149 ARG B CD    
1186 N NE    . ARG A 150 ? 0.45249 0.46685 0.40205 -0.04998 0.06450  -0.07424 149 ARG B NE    
1187 C CZ    . ARG A 150 ? 0.41323 0.42921 0.38588 -0.03934 0.06577  -0.07308 149 ARG B CZ    
1188 N NH1   . ARG A 150 ? 0.40451 0.41073 0.38835 -0.03290 0.06668  -0.07817 149 ARG B NH1   
1189 N NH2   . ARG A 150 ? 0.43031 0.45716 0.41467 -0.03570 0.06525  -0.06615 149 ARG B NH2   
1190 N N     . GLN A 151 ? 0.21735 0.21984 0.11233 -0.08516 0.01695  -0.05545 150 GLN B N     
1191 C CA    . GLN A 151 ? 0.21278 0.22389 0.09845 -0.09020 0.00908  -0.04453 150 GLN B CA    
1192 C C     . GLN A 151 ? 0.23955 0.25833 0.14157 -0.08232 0.00542  -0.03310 150 GLN B C     
1193 O O     . GLN A 151 ? 0.20709 0.22670 0.12715 -0.07567 0.00190  -0.02892 150 GLN B O     
1194 C CB    . GLN A 151 ? 0.22304 0.23484 0.10370 -0.09715 -0.00262 -0.03929 150 GLN B CB    
1195 C CG    . GLN A 151 ? 0.29912 0.31991 0.17897 -0.09936 -0.01357 -0.02530 150 GLN B CG    
1196 C CD    . GLN A 151 ? 0.39215 0.41713 0.28151 -0.10114 -0.02574 -0.01856 150 GLN B CD    
1197 O OE1   . GLN A 151 ? 0.42008 0.44070 0.31211 -0.10324 -0.02617 -0.02464 150 GLN B OE1   
1198 N NE2   . GLN A 151 ? 0.41735 0.45072 0.31412 -0.09977 -0.03531 -0.00581 150 GLN B NE2   
1199 N N     . GLY A 152 ? 0.23839 0.26185 0.13450 -0.08299 0.00719  -0.02794 151 GLY B N     
1200 C CA    . GLY A 152 ? 0.17167 0.20049 0.08147 -0.07662 0.00282  -0.01667 151 GLY B CA    
1201 C C     . GLY A 152 ? 0.22713 0.25605 0.15598 -0.06593 0.00925  -0.01805 151 GLY B C     
1202 O O     . GLY A 152 ? 0.19497 0.22696 0.13344 -0.06121 0.00639  -0.01014 151 GLY B O     
1203 N N     . VAL A 153 ? 0.18334 0.20826 0.11758 -0.06214 0.01737  -0.02778 152 VAL B N     
1204 C CA    . VAL A 153 ? 0.17382 0.19890 0.12665 -0.05207 0.02099  -0.02785 152 VAL B CA    
1205 C C     . VAL A 153 ? 0.15041 0.18110 0.10689 -0.05005 0.02531  -0.02544 152 VAL B C     
1206 O O     . VAL A 153 ? 0.13713 0.17013 0.10396 -0.04515 0.02188  -0.01889 152 VAL B O     
1207 C CB    . VAL A 153 ? 0.19791 0.21652 0.15657 -0.04840 0.02756  -0.03774 152 VAL B CB    
1208 C CG1   . VAL A 153 ? 0.21733 0.23696 0.19406 -0.03851 0.03014  -0.03658 152 VAL B CG1   
1209 C CG2   . VAL A 153 ? 0.16283 0.17490 0.12055 -0.05066 0.02243  -0.03874 152 VAL B CG2   
1210 N N     . ASP A 154 ? 0.20122 0.23411 0.14969 -0.05421 0.03364  -0.03147 153 ASP B N     
1211 C CA    . ASP A 154 ? 0.20152 0.24119 0.15387 -0.05429 0.03786  -0.02851 153 ASP B CA    
1212 C C     . ASP A 154 ? 0.18657 0.22728 0.13296 -0.05816 0.02977  -0.01714 153 ASP B C     
1213 O O     . ASP A 154 ? 0.18078 0.22404 0.13683 -0.05529 0.02852  -0.01181 153 ASP B O     
1214 C CB    . ASP A 154 ? 0.24849 0.29159 0.19047 -0.06034 0.04901  -0.03625 153 ASP B CB    
1215 C CG    . ASP A 154 ? 0.21411 0.25696 0.16750 -0.05450 0.05888  -0.04795 153 ASP B CG    
1216 O OD1   . ASP A 154 ? 0.26069 0.30168 0.23198 -0.04540 0.05655  -0.04822 153 ASP B OD1   
1217 O OD2   . ASP A 154 ? 0.31375 0.35609 0.26025 -0.05775 0.06645  -0.05510 153 ASP B OD2   
1218 N N     . ASP A 155 ? 0.19469 0.23278 0.12566 -0.06487 0.02353  -0.01329 154 ASP B N     
1219 C CA    . ASP A 155 ? 0.25307 0.29104 0.17892 -0.06828 0.01489  -0.00160 154 ASP B CA    
1220 C C     . ASP A 155 ? 0.22063 0.25745 0.16401 -0.05975 0.00871  0.00452  154 ASP B C     
1221 O O     . ASP A 155 ? 0.15837 0.19453 0.10529 -0.05924 0.00616  0.01158  154 ASP B O     
1222 C CB    . ASP A 155 ? 0.23440 0.27051 0.14429 -0.07557 0.00699  0.00161  154 ASP B CB    
1223 C CG    . ASP A 155 ? 0.31776 0.35352 0.21831 -0.08111 -0.00125 0.01398  154 ASP B CG    
1224 O OD1   . ASP A 155 ? 0.30546 0.34088 0.21113 -0.07976 0.00001  0.01966  154 ASP B OD1   
1225 O OD2   . ASP A 155 ? 0.44309 0.47837 0.33114 -0.08737 -0.00974 0.01838  154 ASP B OD2   
1226 N N     . ALA A 156 ? 0.16795 0.20352 0.12151 -0.05360 0.00683  0.00156  155 ALA B N     
1227 C CA    . ALA A 156 ? 0.12876 0.16322 0.09652 -0.04610 0.00229  0.00632  155 ALA B CA    
1228 C C     . ALA A 156 ? 0.16242 0.19693 0.13932 -0.04151 0.00628  0.00552  155 ALA B C     
1229 O O     . ALA A 156 ? 0.13580 0.16826 0.11737 -0.03943 0.00283  0.01106  155 ALA B O     
1230 C CB    . ALA A 156 ? 0.14125 0.17482 0.11630 -0.04191 0.00146  0.00283  155 ALA B CB    
1231 N N     . PHE A 157 ? 0.14248 0.17905 0.12308 -0.03987 0.01309  -0.00158 156 PHE B N     
1232 C CA    . PHE A 157 ? 0.10060 0.13901 0.09168 -0.03593 0.01536  -0.00223 156 PHE B CA    
1233 C C     . PHE A 157 ? 0.10327 0.14430 0.09121 -0.04152 0.01702  0.00109  156 PHE B C     
1234 O O     . PHE A 157 ? 0.09446 0.13423 0.08859 -0.04021 0.01449  0.00453  156 PHE B O     
1235 C CB    . PHE A 157 ? 0.09231 0.13341 0.09127 -0.03214 0.02111  -0.00969 156 PHE B CB    
1236 C CG    . PHE A 157 ? 0.11644 0.15317 0.12069 -0.02617 0.01876  -0.01111 156 PHE B CG    
1237 C CD1   . PHE A 157 ? 0.07333 0.10850 0.08544 -0.02068 0.01528  -0.00857 156 PHE B CD1   
1238 C CD2   . PHE A 157 ? 0.11366 0.14695 0.11337 -0.02718 0.01998  -0.01490 156 PHE B CD2   
1239 C CE1   . PHE A 157 ? 0.12986 0.16067 0.14476 -0.01633 0.01365  -0.00881 156 PHE B CE1   
1240 C CE2   . PHE A 157 ? 0.14013 0.16869 0.14467 -0.02288 0.01810  -0.01525 156 PHE B CE2   
1241 C CZ    . PHE A 157 ? 0.17193 0.19944 0.18385 -0.01742 0.01515  -0.01165 156 PHE B CZ    
1242 N N     . TYR A 158 ? 0.13797 0.18188 0.11506 -0.04869 0.02157  -0.00011 157 TYR B N     
1243 C CA    . TYR A 158 ? 0.11720 0.16372 0.09012 -0.05553 0.02416  0.00388  157 TYR B CA    
1244 C C     . TYR A 158 ? 0.14831 0.18793 0.11651 -0.05777 0.01588  0.01397  157 TYR B C     
1245 O O     . TYR A 158 ? 0.14687 0.18505 0.11899 -0.05996 0.01521  0.01834  157 TYR B O     
1246 C CB    . TYR A 158 ? 0.13894 0.18927 0.09730 -0.06381 0.03146  0.00073  157 TYR B CB    
1247 C CG    . TYR A 158 ? 0.13855 0.19568 0.10299 -0.06192 0.04208  -0.01016 157 TYR B CG    
1248 C CD1   . TYR A 158 ? 0.14737 0.20652 0.13009 -0.05271 0.04288  -0.01529 157 TYR B CD1   
1249 C CD2   . TYR A 158 ? 0.21049 0.26976 0.16326 -0.06772 0.04977  -0.01511 157 TYR B CD2   
1250 C CE1   . TYR A 158 ? 0.13551 0.20027 0.12681 -0.04977 0.05218  -0.02474 157 TYR B CE1   
1251 C CE2   . TYR A 158 ? 0.26021 0.32361 0.22127 -0.06391 0.05901  -0.02552 157 TYR B CE2   
1252 C CZ    . TYR A 158 ? 0.20638 0.27330 0.18743 -0.05515 0.06088  -0.03028 157 TYR B CZ    
1253 O OH    . TYR A 158 ? 0.34725 0.41718 0.33871 -0.05027 0.06921  -0.03971 157 TYR B OH    
1254 N N     . THR A 159 ? 0.13946 0.17468 0.10057 -0.05750 0.00924  0.01793  158 THR B N     
1255 C CA    . THR A 159 ? 0.12836 0.15684 0.08882 -0.05764 0.00078  0.02778  158 THR B CA    
1256 C C     . THR A 159 ? 0.11682 0.14090 0.09189 -0.05005 -0.00149 0.02794  158 THR B C     
1257 O O     . THR A 159 ? 0.12206 0.13967 0.09908 -0.05106 -0.00473 0.03383  158 THR B O     
1258 C CB    . THR A 159 ? 0.18191 0.20934 0.13718 -0.05738 -0.00645 0.03142  158 THR B CB    
1259 O OG1   . THR A 159 ? 0.21614 0.24596 0.15358 -0.06654 -0.00572 0.03206  158 THR B OG1   
1260 C CG2   . THR A 159 ? 0.18050 0.20169 0.14093 -0.05478 -0.01554 0.04146  158 THR B CG2   
1261 N N     . LEU A 160 ? 0.10755 0.13366 0.09154 -0.04304 0.00024  0.02141  159 LEU B N     
1262 C CA    . LEU A 160 ? 0.09621 0.11796 0.09042 -0.03692 -0.00125 0.02045  159 LEU B CA    
1263 C C     . LEU A 160 ? 0.12751 0.14917 0.12483 -0.04019 0.00106  0.01976  159 LEU B C     
1264 O O     . LEU A 160 ? 0.10031 0.11481 0.10150 -0.03900 -0.00196 0.02171  159 LEU B O     
1265 C CB    . LEU A 160 ? 0.08528 0.10949 0.08542 -0.03044 0.00049  0.01431  159 LEU B CB    
1266 C CG    . LEU A 160 ? 0.08455 0.10358 0.09115 -0.02493 -0.00116 0.01312  159 LEU B CG    
1267 C CD1   . LEU A 160 ? 0.09019 0.10177 0.09812 -0.02254 -0.00512 0.01773  159 LEU B CD1   
1268 C CD2   . LEU A 160 ? 0.09241 0.11329 0.10205 -0.01967 0.00036  0.00862  159 LEU B CD2   
1269 N N     . VAL A 161 ? 0.09911 0.12887 0.09595 -0.04452 0.00678  0.01639  160 VAL B N     
1270 C CA    . VAL A 161 ? 0.12650 0.15900 0.12909 -0.04874 0.00905  0.01619  160 VAL B CA    
1271 C C     . VAL A 161 ? 0.14004 0.16599 0.13622 -0.05609 0.00692  0.02405  160 VAL B C     
1272 O O     . VAL A 161 ? 0.13267 0.15354 0.13391 -0.05820 0.00470  0.02598  160 VAL B O     
1273 C CB    . VAL A 161 ? 0.11867 0.16359 0.12568 -0.05108 0.01692  0.01058  160 VAL B CB    
1274 C CG1   . VAL A 161 ? 0.10508 0.15571 0.11896 -0.05788 0.02001  0.01180  160 VAL B CG1   
1275 C CG2   . VAL A 161 ? 0.08867 0.13769 0.10566 -0.04307 0.01728  0.00413  160 VAL B CG2   
1276 N N     . ARG A 162 ? 0.12481 0.14947 0.10884 -0.06075 0.00670  0.02917  161 ARG B N     
1277 C CA    . ARG A 162 ? 0.14954 0.16612 0.12630 -0.06786 0.00339  0.03874  161 ARG B CA    
1278 C C     . ARG A 162 ? 0.20712 0.21029 0.18924 -0.06259 -0.00459 0.04332  161 ARG B C     
1279 O O     . ARG A 162 ? 0.16072 0.15474 0.14396 -0.06667 -0.00697 0.04864  161 ARG B O     
1280 C CB    . ARG A 162 ? 0.17153 0.18879 0.13204 -0.07379 0.00277  0.04426  161 ARG B CB    
1281 C CG    . ARG A 162 ? 0.17236 0.20070 0.12518 -0.07925 0.01197  0.03836  161 ARG B CG    
1282 C CD    . ARG A 162 ? 0.19563 0.22170 0.13045 -0.08500 0.00997  0.04284  161 ARG B CD    
1283 N NE    . ARG A 162 ? 0.24805 0.28294 0.17570 -0.08801 0.01906  0.03424  161 ARG B NE    
1284 C CZ    . ARG A 162 ? 0.21215 0.25090 0.13545 -0.08605 0.02131  0.02711  161 ARG B CZ    
1285 N NH1   . ARG A 162 ? 0.18647 0.22248 0.11051 -0.08205 0.01476  0.02856  161 ARG B NH1   
1286 N NH2   . ARG A 162 ? 0.25464 0.29955 0.17330 -0.08824 0.03057  0.01824  161 ARG B NH2   
1287 N N     . GLU A 163 ? 0.14037 0.14173 0.12648 -0.05377 -0.00809 0.04107  162 GLU B N     
1288 C CA    . GLU A 163 ? 0.15035 0.13993 0.14360 -0.04745 -0.01352 0.04330  162 GLU B CA    
1289 C C     . GLU A 163 ? 0.21679 0.20155 0.21730 -0.04617 -0.01210 0.03772  162 GLU B C     
1290 O O     . GLU A 163 ? 0.14151 0.11327 0.14497 -0.04577 -0.01542 0.04028  162 GLU B O     
1291 C CB    . GLU A 163 ? 0.14257 0.13449 0.14013 -0.03881 -0.01542 0.04092  162 GLU B CB    
1292 C CG    . GLU A 163 ? 0.19238 0.18842 0.18360 -0.04094 -0.01921 0.04717  162 GLU B CG    
1293 C CD    . GLU A 163 ? 0.21725 0.20373 0.20773 -0.04250 -0.02655 0.05834  162 GLU B CD    
1294 O OE1   . GLU A 163 ? 0.22262 0.20070 0.22393 -0.03538 -0.02987 0.05993  162 GLU B OE1   
1295 O OE2   . GLU A 163 ? 0.23734 0.22401 0.21617 -0.05079 -0.02883 0.06564  162 GLU B OE2   
1296 N N     . ILE A 164 ? 0.16222 0.15647 0.16585 -0.04558 -0.00792 0.03003  163 ILE B N     
1297 C CA    . ILE A 164 ? 0.13691 0.12807 0.14633 -0.04605 -0.00816 0.02521  163 ILE B CA    
1298 C C     . ILE A 164 ? 0.20105 0.18873 0.21065 -0.05565 -0.00827 0.02951  163 ILE B C     
1299 O O     . ILE A 164 ? 0.21124 0.18696 0.22314 -0.05736 -0.01149 0.02968  163 ILE B O     
1300 C CB    . ILE A 164 ? 0.15942 0.16290 0.17335 -0.04375 -0.00519 0.01797  163 ILE B CB    
1301 C CG1   . ILE A 164 ? 0.10003 0.10272 0.11335 -0.03492 -0.00582 0.01430  163 ILE B CG1   
1302 C CG2   . ILE A 164 ? 0.16180 0.16531 0.18181 -0.04712 -0.00680 0.01441  163 ILE B CG2   
1303 C CD1   . ILE A 164 ? 0.08968 0.10286 0.10643 -0.03192 -0.00364 0.00907  163 ILE B CD1   
1304 N N     . ARG A 165 ? 0.16505 0.16233 0.17147 -0.06278 -0.00413 0.03281  164 ARG B N     
1305 C CA    . ARG A 165 ? 0.24390 0.23923 0.25029 -0.07342 -0.00300 0.03785  164 ARG B CA    
1306 C C     . ARG A 165 ? 0.24012 0.21707 0.24117 -0.07572 -0.00850 0.04670  164 ARG B C     
1307 O O     . ARG A 165 ? 0.24329 0.21024 0.24755 -0.08143 -0.01056 0.04891  164 ARG B O     
1308 C CB    . ARG A 165 ? 0.15936 0.16902 0.16140 -0.08067 0.00436  0.03941  164 ARG B CB    
1309 C CG    . ARG A 165 ? 0.17097 0.19828 0.18266 -0.07830 0.01044  0.03052  164 ARG B CG    
1310 C CD    . ARG A 165 ? 0.18302 0.22258 0.18932 -0.08166 0.01915  0.02935  164 ARG B CD    
1311 N NE    . ARG A 165 ? 0.18751 0.24304 0.20688 -0.07893 0.02551  0.02117  164 ARG B NE    
1312 C CZ    . ARG A 165 ? 0.17764 0.24307 0.19512 -0.07858 0.03383  0.01702  164 ARG B CZ    
1313 N NH1   . ARG A 165 ? 0.14540 0.20708 0.14585 -0.08193 0.03657  0.01959  164 ARG B NH1   
1314 N NH2   . ARG A 165 ? 0.12431 0.20304 0.15740 -0.07457 0.03887  0.00998  164 ARG B NH2   
1315 N N     . LYS A 166 ? 0.22045 0.19214 0.21488 -0.07126 -0.01175 0.05204  165 LYS B N     
1316 C CA    . LYS A 166 ? 0.23569 0.18965 0.22779 -0.07194 -0.01807 0.06154  165 LYS B CA    
1317 C C     . LYS A 166 ? 0.23058 0.16954 0.23163 -0.06536 -0.02161 0.05710  165 LYS B C     
1318 O O     . LYS A 166 ? 0.29073 0.21289 0.29306 -0.06861 -0.02522 0.06231  165 LYS B O     
1319 C CB    . LYS A 166 ? 0.23862 0.19229 0.22508 -0.06739 -0.02233 0.06811  165 LYS B CB    
1320 C CG    . LYS A 166 ? 0.30326 0.26872 0.27670 -0.07389 -0.01983 0.07184  165 LYS B CG    
1321 C CD    . LYS A 166 ? 0.31059 0.28116 0.28005 -0.06922 -0.02358 0.07394  165 LYS B CD    
1322 C CE    . LYS A 166 ? 0.29384 0.25401 0.26425 -0.06523 -0.03306 0.08350  165 LYS B CE    
1323 N NZ    . LYS A 166 ? 0.30713 0.27362 0.27888 -0.05963 -0.03772 0.08480  165 LYS B NZ    
1324 N N     . HIS A 167 ? 0.23037 0.17385 0.23644 -0.05647 -0.02028 0.04734  166 HIS B N     
1325 C CA    . HIS A 167 ? 0.23687 0.16661 0.24848 -0.05057 -0.02211 0.04110  166 HIS B CA    
1326 C C     . HIS A 167 ? 0.28694 0.21085 0.29999 -0.05854 -0.02217 0.03728  166 HIS B C     
1327 O O     . HIS A 167 ? 0.26941 0.17481 0.28433 -0.05866 -0.02500 0.03615  166 HIS B O     
1328 C CB    . HIS A 167 ? 0.23201 0.16988 0.24552 -0.04118 -0.01970 0.03202  166 HIS B CB    
1329 C CG    . HIS A 167 ? 0.28196 0.20832 0.29734 -0.03675 -0.01978 0.02328  166 HIS B CG    
1330 N ND1   . HIS A 167 ? 0.40599 0.31616 0.42476 -0.03000 -0.02086 0.02256  166 HIS B ND1   
1331 C CD2   . HIS A 167 ? 0.29276 0.22134 0.30633 -0.03830 -0.01894 0.01454  166 HIS B CD2   
1332 C CE1   . HIS A 167 ? 0.30607 0.20805 0.32292 -0.02809 -0.01951 0.01263  166 HIS B CE1   
1333 N NE2   . HIS A 167 ? 0.32787 0.24078 0.34049 -0.03356 -0.01917 0.00813  166 HIS B NE2   
1334 N N     . LYS A 168 ? 0.24920 0.18877 0.26282 -0.06542 -0.01915 0.03498  167 LYS B N     
1335 C CA    . LYS A 168 ? 0.26133 0.19908 0.27906 -0.07388 -0.02001 0.03145  167 LYS B CA    
1336 C C     . LYS A 168 ? 0.31183 0.23671 0.32898 -0.08301 -0.02154 0.03915  167 LYS B C     
1337 O O     . LYS A 168 ? 0.37756 0.29533 0.39799 -0.08740 -0.02306 0.03519  167 LYS B O     
1338 C CB    . LYS A 168 ? 0.21703 0.17741 0.23972 -0.07838 -0.01622 0.02838  167 LYS B CB    
1339 C CG    . LYS A 168 ? 0.25012 0.22130 0.27520 -0.07037 -0.01612 0.01963  167 LYS B CG    
1340 C CD    . LYS A 168 ? 0.21396 0.20712 0.24702 -0.07400 -0.01235 0.01824  167 LYS B CD    
1341 C CE    . LYS A 168 ? 0.23641 0.23881 0.27460 -0.06873 -0.01464 0.01077  167 LYS B CE    
1342 N NZ    . LYS A 168 ? 0.17950 0.20286 0.23103 -0.07327 -0.01200 0.00993  167 LYS B NZ    
1343 N N     . GLU A 169 ? 0.29547 0.21949 0.30731 -0.08352 -0.02056 0.04861  168 GLU B N     
1344 C CA    . GLU A 169 ? 0.34147 0.25475 0.35120 -0.08901 -0.02126 0.05542  168 GLU B CA    
1345 C C     . GLU A 169 ? 0.40139 0.29012 0.41292 -0.08446 -0.02614 0.05537  168 GLU B C     
1346 O O     . GLU A 169 ? 0.37774 0.25515 0.38983 -0.08979 -0.02687 0.05806  168 GLU B O     
1347 C CB    . GLU A 169 ? 0.38989 0.30783 0.39104 -0.09045 -0.02024 0.06565  168 GLU B CB    
1348 C CG    . GLU A 169 ? 0.42646 0.36630 0.42383 -0.09584 -0.01364 0.06542  168 GLU B CG    
1349 C CD    . GLU A 169 ? 0.45089 0.39239 0.43616 -0.09808 -0.01339 0.07465  168 GLU B CD    
1350 O OE1   . GLU A 169 ? 0.56603 0.49755 0.54718 -0.09259 -0.01933 0.08035  168 GLU B OE1   
1351 O OE2   . GLU A 169 ? 0.58024 0.53316 0.56056 -0.10526 -0.00752 0.07601  168 GLU B OE2   
1352 N N     . LYS A 170 ? 0.38231 0.26242 0.39551 -0.07444 -0.02870 0.05217  169 LYS B N     
1353 C CA    . LYS A 170 ? 0.39794 0.25531 0.41414 -0.06790 -0.03175 0.05162  169 LYS B CA    
1354 C C     . LYS A 170 ? 0.46571 0.31029 0.48385 -0.07161 -0.03160 0.04223  169 LYS B C     
1355 O O     . LYS A 170 ? 0.38017 0.23275 0.39837 -0.07504 -0.03073 0.03331  169 LYS B O     
1356 C CB    . LYS A 170 ? 0.47883 0.33309 0.49873 -0.05534 -0.03280 0.04876  169 LYS B CB    
1357 C CG    . LYS A 170 ? 0.45953 0.32459 0.47860 -0.05133 -0.03440 0.05862  169 LYS B CG    
1358 C CD    . LYS A 170 ? 0.53767 0.40518 0.56302 -0.03939 -0.03434 0.05446  169 LYS B CD    
1359 C CE    . LYS A 170 ? 0.54566 0.42426 0.57120 -0.03607 -0.03726 0.06450  169 LYS B CE    
1360 N NZ    . LYS A 170 ? 0.55624 0.42559 0.58307 -0.03484 -0.04188 0.07417  169 LYS B NZ    
1361 O OXT   . LYS A 170 ? 0.53599 0.36194 0.55536 -0.07171 -0.03278 0.04344  169 LYS B OXT   
1362 N N     . SER B 1   ? 0.31198 0.53120 0.49451 0.09812  -0.06691 0.03783  0   SER A N     
1363 C CA    . SER B 1   ? 0.16121 0.37559 0.34739 0.09291  -0.05592 0.03542  0   SER A CA    
1364 C C     . SER B 1   ? 0.26015 0.46013 0.43371 0.08328  -0.05650 0.03190  0   SER A C     
1365 O O     . SER B 1   ? 0.27535 0.47127 0.43948 0.07980  -0.06573 0.03073  0   SER A O     
1366 C CB    . SER B 1   ? 0.22692 0.42764 0.40438 0.10351  -0.04329 0.03887  0   SER A CB    
1367 O OG    . SER B 1   ? 0.21647 0.41509 0.39801 0.09948  -0.03279 0.03668  0   SER A OG    
1368 N N     . MET B 2   ? 0.14314 0.33588 0.31580 0.07929  -0.04662 0.03036  1   MET A N     
1369 C CA    . MET B 2   ? 0.15357 0.33144 0.31326 0.07197  -0.04599 0.02781  1   MET A CA    
1370 C C     . MET B 2   ? 0.15138 0.31356 0.30189 0.07517  -0.03334 0.02880  1   MET A C     
1371 O O     . MET B 2   ? 0.14533 0.30755 0.29899 0.08240  -0.02532 0.03064  1   MET A O     
1372 C CB    . MET B 2   ? 0.20073 0.38950 0.37248 0.05847  -0.05100 0.02305  1   MET A CB    
1373 C CG    . MET B 2   ? 0.20094 0.39868 0.38611 0.05332  -0.04174 0.02265  1   MET A CG    
1374 S SD    . MET B 2   ? 0.45836 0.66280 0.65241 0.03642  -0.04626 0.01764  1   MET A SD    
1375 C CE    . MET B 2   ? 0.16065 0.39192 0.38005 0.03382  -0.05157 0.01613  1   MET A CE    
1376 N N     . THR B 3   ? 0.12902 0.27710 0.26764 0.06999  -0.03209 0.02715  2   THR A N     
1377 C CA    . THR B 3   ? 0.14036 0.27159 0.26927 0.07178  -0.02185 0.02724  2   THR A CA    
1378 C C     . THR B 3   ? 0.16059 0.29281 0.29192 0.06074  -0.02102 0.02473  2   THR A C     
1379 O O     . THR B 3   ? 0.13982 0.28182 0.27767 0.05188  -0.02864 0.02291  2   THR A O     
1380 C CB    . THR B 3   ? 0.18957 0.29885 0.29978 0.07787  -0.02093 0.02912  2   THR A CB    
1381 O OG1   . THR B 3   ? 0.15140 0.25946 0.25400 0.07342  -0.02941 0.02853  2   THR A OG1   
1382 C CG2   . THR B 3   ? 0.15621 0.26255 0.26390 0.08866  -0.02037 0.03287  2   THR A CG2   
1383 N N     . GLU B 4   ? 0.09361 0.21077 0.21672 0.05942  -0.01201 0.02299  3   GLU A N     
1384 C CA    . GLU B 4   ? 0.08614 0.19725 0.20599 0.04782  -0.01027 0.01960  3   GLU A CA    
1385 C C     . GLU B 4   ? 0.10834 0.19476 0.20997 0.04726  -0.00577 0.01680  3   GLU A C     
1386 O O     . GLU B 4   ? 0.14435 0.22006 0.23983 0.05500  -0.00027 0.01685  3   GLU A O     
1387 C CB    . GLU B 4   ? 0.14976 0.27490 0.28241 0.04582  -0.00348 0.02060  3   GLU A CB    
1388 C CG    . GLU B 4   ? 0.13212 0.25469 0.26391 0.03407  -0.00238 0.01906  3   GLU A CG    
1389 C CD    . GLU B 4   ? 0.21956 0.35924 0.36580 0.03223  0.00454  0.02223  3   GLU A CD    
1390 O OE1   . GLU B 4   ? 0.23156 0.39112 0.39416 0.03773  0.00599  0.02564  3   GLU A OE1   
1391 O OE2   . GLU B 4   ? 0.16563 0.30009 0.30737 0.02577  0.00891  0.02213  3   GLU A OE2   
1392 N N     . TYR B 5   ? 0.08647 0.16384 0.18056 0.03816  -0.00836 0.01419  4   TYR A N     
1393 C CA    . TYR B 5   ? 0.09656 0.15368 0.17615 0.03647  -0.00529 0.01163  4   TYR A CA    
1394 C C     . TYR B 5   ? 0.14036 0.19476 0.21742 0.02756  -0.00404 0.00899  4   TYR A C     
1395 O O     . TYR B 5   ? 0.10280 0.16396 0.18455 0.02098  -0.00833 0.00920  4   TYR A O     
1396 C CB    . TYR B 5   ? 0.12572 0.17317 0.19634 0.03697  -0.00997 0.01246  4   TYR A CB    
1397 C CG    . TYR B 5   ? 0.10565 0.15565 0.17678 0.04652  -0.01181 0.01649  4   TYR A CG    
1398 C CD1   . TYR B 5   ? 0.22026 0.25968 0.28795 0.05450  -0.00608 0.01840  4   TYR A CD1   
1399 C CD2   . TYR B 5   ? 0.18471 0.24700 0.25924 0.04807  -0.01972 0.01824  4   TYR A CD2   
1400 C CE1   . TYR B 5   ? 0.18845 0.22940 0.25617 0.06467  -0.00736 0.02348  4   TYR A CE1   
1401 C CE2   . TYR B 5   ? 0.15127 0.21720 0.22512 0.05830  -0.02204 0.02275  4   TYR A CE2   
1402 C CZ    . TYR B 5   ? 0.12208 0.17711 0.19248 0.06690  -0.01538 0.02608  4   TYR A CZ    
1403 O OH    . TYR B 5   ? 0.15052 0.20798 0.21965 0.07810  -0.01721 0.03176  4   TYR A OH    
1404 N N     . LYS B 6   ? 0.12020 0.16411 0.18957 0.02768  0.00138  0.00635  5   LYS A N     
1405 C CA    . LYS B 6   ? 0.12671 0.16707 0.19118 0.02087  0.00234  0.00430  5   LYS A CA    
1406 C C     . LYS B 6   ? 0.12114 0.14795 0.17648 0.01764  -0.00040 0.00231  5   LYS A C     
1407 O O     . LYS B 6   ? 0.12925 0.14491 0.17849 0.01975  0.00182  0.00001  5   LYS A O     
1408 C CB    . LYS B 6   ? 0.15927 0.19829 0.21958 0.02355  0.00886  0.00205  5   LYS A CB    
1409 C CG    . LYS B 6   ? 0.24205 0.29579 0.31156 0.02799  0.01360  0.00469  5   LYS A CG    
1410 C CD    . LYS B 6   ? 0.30985 0.36031 0.37096 0.03209  0.02061  0.00162  5   LYS A CD    
1411 C CE    . LYS B 6   ? 0.33281 0.37442 0.38961 0.04119  0.02391  -0.00196 5   LYS A CE    
1412 N NZ    . LYS B 6   ? 0.42529 0.48080 0.49407 0.04909  0.02738  0.00187  5   LYS A NZ    
1413 N N     . LEU B 7   ? 0.08537 0.11316 0.14079 0.01257  -0.00499 0.00308  6   LEU A N     
1414 C CA    . LEU B 7   ? 0.11508 0.13294 0.16329 0.01004  -0.00700 0.00193  6   LEU A CA    
1415 C C     . LEU B 7   ? 0.11021 0.12601 0.15516 0.00510  -0.00665 0.00049  6   LEU A C     
1416 O O     . LEU B 7   ? 0.07936 0.10106 0.12762 0.00217  -0.00704 0.00174  6   LEU A O     
1417 C CB    . LEU B 7   ? 0.16452 0.18395 0.21264 0.00968  -0.01214 0.00320  6   LEU A CB    
1418 C CG    . LEU B 7   ? 0.09802 0.12399 0.14995 0.01484  -0.01452 0.00525  6   LEU A CG    
1419 C CD1   . LEU B 7   ? 0.12698 0.15510 0.17651 0.01431  -0.02104 0.00498  6   LEU A CD1   
1420 C CD2   . LEU B 7   ? 0.12301 0.14188 0.17126 0.02105  -0.01097 0.00702  6   LEU A CD2   
1421 N N     . VAL B 8   ? 0.09522 0.10321 0.13472 0.00414  -0.00603 -0.00149 7   VAL A N     
1422 C CA    . VAL B 8   ? 0.13556 0.14260 0.17151 0.00078  -0.00648 -0.00265 7   VAL A CA    
1423 C C     . VAL B 8   ? 0.10634 0.10933 0.14058 -0.00087 -0.00888 -0.00241 7   VAL A C     
1424 O O     . VAL B 8   ? 0.08762 0.08633 0.12180 -0.00001 -0.00819 -0.00276 7   VAL A O     
1425 C CB    . VAL B 8   ? 0.09466 0.09895 0.12648 0.00152  -0.00430 -0.00623 7   VAL A CB    
1426 C CG1   . VAL B 8   ? 0.12474 0.12999 0.15197 -0.00091 -0.00590 -0.00699 7   VAL A CG1   
1427 C CG2   . VAL B 8   ? 0.08865 0.09679 0.12094 0.00501  -0.00067 -0.00659 7   VAL A CG2   
1428 N N     . VAL B 9   ? 0.08928 0.09324 0.12257 -0.00284 -0.01089 -0.00126 8   VAL A N     
1429 C CA    . VAL B 9   ? 0.08916 0.09005 0.12065 -0.00298 -0.01253 -0.00100 8   VAL A CA    
1430 C C     . VAL B 9   ? 0.08290 0.08441 0.11292 -0.00397 -0.01274 -0.00174 8   VAL A C     
1431 O O     . VAL B 9   ? 0.09778 0.10085 0.12571 -0.00464 -0.01319 -0.00083 8   VAL A O     
1432 C CB    . VAL B 9   ? 0.09327 0.09283 0.12413 -0.00346 -0.01507 -0.00003 8   VAL A CB    
1433 C CG1   . VAL B 9   ? 0.07225 0.06787 0.09970 -0.00153 -0.01594 -0.00029 8   VAL A CG1   
1434 C CG2   . VAL B 9   ? 0.12467 0.12653 0.15816 -0.00312 -0.01652 -0.00007 8   VAL A CG2   
1435 N N     . VAL B 10  ? 0.08259 0.08384 0.11434 -0.00404 -0.01246 -0.00277 9   VAL A N     
1436 C CA    . VAL B 10  ? 0.11319 0.11769 0.14561 -0.00510 -0.01405 -0.00405 9   VAL A CA    
1437 C C     . VAL B 10  ? 0.08420 0.09081 0.12051 -0.00431 -0.01417 -0.00256 9   VAL A C     
1438 O O     . VAL B 10  ? 0.08632 0.09090 0.12368 -0.00291 -0.01201 -0.00090 9   VAL A O     
1439 C CB    . VAL B 10  ? 0.08882 0.09329 0.12266 -0.00707 -0.01413 -0.00804 9   VAL A CB    
1440 C CG1   . VAL B 10  ? 0.13616 0.13924 0.16491 -0.00609 -0.01301 -0.00971 9   VAL A CG1   
1441 C CG2   . VAL B 10  ? 0.10486 0.10566 0.14435 -0.00818 -0.01181 -0.00804 9   VAL A CG2   
1442 N N     . GLY B 11  ? 0.08778 0.09975 0.12590 -0.00435 -0.01654 -0.00288 10  GLY A N     
1443 C CA    . GLY B 11  ? 0.07975 0.09668 0.12340 -0.00271 -0.01634 -0.00104 10  GLY A CA    
1444 C C     . GLY B 11  ? 0.11585 0.13690 0.15765 0.00032  -0.01932 0.00046  10  GLY A C     
1445 O O     . GLY B 11  ? 0.07600 0.09396 0.11084 0.00130  -0.02083 0.00122  10  GLY A O     
1446 N N     . ALA B 12  ? 0.07701 0.10577 0.12590 0.00240  -0.01957 0.00188  11  ALA A N     
1447 C CA    . ALA B 12  ? 0.08892 0.12353 0.13761 0.00641  -0.02287 0.00375  11  ALA A CA    
1448 C C     . ALA B 12  ? 0.07778 0.10256 0.11719 0.01095  -0.02204 0.00661  11  ALA A C     
1449 O O     . ALA B 12  ? 0.08959 0.10483 0.12476 0.01102  -0.01931 0.00649  11  ALA A O     
1450 C CB    . ALA B 12  ? 0.08899 0.13508 0.14912 0.00896  -0.02230 0.00544  11  ALA A CB    
1451 N N     . CYS B 13  ? 0.08341 0.11018 0.11971 0.01475  -0.02492 0.00924  12  CYS A N     
1452 C CA    . CYS B 13  ? 0.09062 0.10583 0.11903 0.01845  -0.02391 0.01263  12  CYS A CA    
1453 C C     . CYS B 13  ? 0.10575 0.11494 0.13505 0.02323  -0.02113 0.01304  12  CYS A C     
1454 O O     . CYS B 13  ? 0.10254 0.12037 0.13859 0.02694  -0.02022 0.01318  12  CYS A O     
1455 C CB    . CYS B 13  ? 0.09876 0.11686 0.12310 0.02282  -0.02702 0.01683  12  CYS A CB    
1456 S SG    . CYS B 13  ? 0.14737 0.18083 0.18023 0.02951  -0.03031 0.01846  12  CYS A SG    
1457 N N     . GLY B 14  ? 0.09942 0.09409 0.12216 0.02317  -0.01976 0.01292  13  GLY A N     
1458 C CA    . GLY B 14  ? 0.10734 0.09281 0.12737 0.02839  -0.01777 0.01186  13  GLY A CA    
1459 C C     . GLY B 14  ? 0.10528 0.09146 0.12560 0.02802  -0.01525 0.00804  13  GLY A C     
1460 O O     . GLY B 14  ? 0.14707 0.12565 0.16274 0.03348  -0.01348 0.00630  13  GLY A O     
1461 N N     . VAL B 15  ? 0.12445 0.11845 0.14871 0.02272  -0.01474 0.00680  14  VAL A N     
1462 C CA    . VAL B 15  ? 0.09617 0.09126 0.11993 0.02372  -0.01155 0.00499  14  VAL A CA    
1463 C C     . VAL B 15  ? 0.11997 0.10306 0.13482 0.02300  -0.01247 0.00170  14  VAL A C     
1464 O O     . VAL B 15  ? 0.12126 0.10276 0.13134 0.02639  -0.01025 0.00007  14  VAL A O     
1465 C CB    . VAL B 15  ? 0.08995 0.09505 0.12106 0.01863  -0.01031 0.00546  14  VAL A CB    
1466 C CG1   . VAL B 15  ? 0.08118 0.09956 0.12302 0.01881  -0.01022 0.00753  14  VAL A CG1   
1467 C CG2   . VAL B 15  ? 0.09346 0.09581 0.12334 0.01230  -0.01299 0.00414  14  VAL A CG2   
1468 N N     . GLY B 16  ? 0.15596 0.13157 0.16861 0.01888  -0.01575 0.00088  15  GLY A N     
1469 C CA    . GLY B 16  ? 0.12380 0.09017 0.13094 0.01688  -0.01810 -0.00273 15  GLY A CA    
1470 C C     . GLY B 16  ? 0.16102 0.13172 0.17155 0.01057  -0.01953 -0.00289 15  GLY A C     
1471 O O     . GLY B 16  ? 0.16241 0.13013 0.16982 0.00962  -0.02173 -0.00590 15  GLY A O     
1472 N N     . LYS B 17  ? 0.09896 0.07701 0.11518 0.00713  -0.01865 -0.00014 16  LYS A N     
1473 C CA    . LYS B 17  ? 0.12970 0.11159 0.14912 0.00246  -0.01918 -0.00022 16  LYS A CA    
1474 C C     . LYS B 17  ? 0.10707 0.08356 0.12710 -0.00108 -0.02190 -0.00106 16  LYS A C     
1475 O O     . LYS B 17  ? 0.11222 0.09076 0.13389 -0.00296 -0.02364 -0.00281 16  LYS A O     
1476 C CB    . LYS B 17  ? 0.09038 0.07881 0.11330 0.00039  -0.01784 0.00195  16  LYS A CB    
1477 C CG    . LYS B 17  ? 0.10828 0.10312 0.13360 0.00183  -0.01632 0.00184  16  LYS A CG    
1478 C CD    . LYS B 17  ? 0.07223 0.07243 0.09896 -0.00011 -0.01674 0.00216  16  LYS A CD    
1479 C CE    . LYS B 17  ? 0.08806 0.08715 0.11169 0.00120  -0.01808 0.00484  16  LYS A CE    
1480 N NZ    . LYS B 17  ? 0.09105 0.09200 0.11546 0.00525  -0.01913 0.00618  16  LYS A NZ    
1481 N N     . SER B 18  ? 0.11839 0.08831 0.13830 -0.00209 -0.02238 0.00070  17  SER A N     
1482 C CA    . SER B 18  ? 0.13081 0.09508 0.15420 -0.00712 -0.02448 0.00074  17  SER A CA    
1483 C C     . SER B 18  ? 0.15369 0.10966 0.17419 -0.00703 -0.02880 -0.00481 17  SER A C     
1484 O O     . SER B 18  ? 0.14220 0.09923 0.16766 -0.01186 -0.03216 -0.00694 17  SER A O     
1485 C CB    . SER B 18  ? 0.14031 0.09754 0.16385 -0.00790 -0.02297 0.00540  17  SER A CB    
1486 O OG    . SER B 18  ? 0.14372 0.10937 0.16894 -0.00876 -0.01975 0.01029  17  SER A OG    
1487 N N     . ALA B 19  ? 0.15687 0.10522 0.16945 -0.00124 -0.02906 -0.00759 18  ALA A N     
1488 C CA    . ALA B 19  ? 0.18796 0.12722 0.19459 -0.00004 -0.03351 -0.01423 18  ALA A CA    
1489 C C     . ALA B 19  ? 0.15872 0.10669 0.16356 0.00049  -0.03587 -0.01725 18  ALA A C     
1490 O O     . ALA B 19  ? 0.18678 0.13130 0.18967 -0.00130 -0.04164 -0.02267 18  ALA A O     
1491 C CB    . ALA B 19  ? 0.16971 0.09978 0.16663 0.00807  -0.03193 -0.01649 18  ALA A CB    
1492 N N     . LEU B 20  ? 0.17250 0.13117 0.17788 0.00310  -0.03197 -0.01386 19  LEU A N     
1493 C CA    . LEU B 20  ? 0.15134 0.11764 0.15526 0.00429  -0.03344 -0.01485 19  LEU A CA    
1494 C C     . LEU B 20  ? 0.15086 0.12354 0.16436 -0.00192 -0.03696 -0.01464 19  LEU A C     
1495 O O     . LEU B 20  ? 0.15921 0.13425 0.17178 -0.00213 -0.04235 -0.01813 19  LEU A O     
1496 C CB    . LEU B 20  ? 0.13194 0.10591 0.13620 0.00757  -0.02769 -0.01044 19  LEU A CB    
1497 C CG    . LEU B 20  ? 0.15195 0.12423 0.14860 0.01426  -0.02364 -0.00986 19  LEU A CG    
1498 C CD1   . LEU B 20  ? 0.11665 0.09665 0.11851 0.01466  -0.01800 -0.00494 19  LEU A CD1   
1499 C CD2   . LEU B 20  ? 0.12585 0.09500 0.11070 0.01976  -0.02587 -0.01334 19  LEU A CD2   
1500 N N     . THR B 21  ? 0.16289 0.13963 0.18555 -0.00641 -0.03405 -0.01048 20  THR A N     
1501 C CA    . THR B 21  ? 0.09729 0.08213 0.13080 -0.01179 -0.03569 -0.00920 20  THR A CA    
1502 C C     . THR B 21  ? 0.16731 0.14766 0.20578 -0.01734 -0.04179 -0.01280 20  THR A C     
1503 O O     . THR B 21  ? 0.16039 0.14875 0.20590 -0.02004 -0.04652 -0.01468 20  THR A O     
1504 C CB    . THR B 21  ? 0.12810 0.11694 0.16756 -0.01424 -0.03016 -0.00390 20  THR A CB    
1505 O OG1   . THR B 21  ? 0.15949 0.15131 0.19443 -0.00980 -0.02598 -0.00237 20  THR A OG1   
1506 C CG2   . THR B 21  ? 0.15539 0.15484 0.20660 -0.01853 -0.02988 -0.00164 20  THR A CG2   
1507 N N     . ILE B 22  ? 0.14638 0.11371 0.18201 -0.01902 -0.04228 -0.01402 21  ILE A N     
1508 C CA    . ILE B 22  ? 0.16995 0.13018 0.21177 -0.02575 -0.04809 -0.01777 21  ILE A CA    
1509 C C     . ILE B 22  ? 0.17822 0.13597 0.21316 -0.02377 -0.05635 -0.02640 21  ILE A C     
1510 O O     . ILE B 22  ? 0.19438 0.15399 0.23771 -0.03010 -0.06350 -0.03063 21  ILE A O     
1511 C CB    . ILE B 22  ? 0.16306 0.10689 0.20263 -0.02714 -0.04598 -0.01645 21  ILE A CB    
1512 C CG1   . ILE B 22  ? 0.21069 0.15887 0.25890 -0.03078 -0.03934 -0.00739 21  ILE A CG1   
1513 C CG2   . ILE B 22  ? 0.18688 0.11768 0.22981 -0.03331 -0.05303 -0.02276 21  ILE A CG2   
1514 C CD1   . ILE B 22  ? 0.33954 0.27292 0.38385 -0.02989 -0.03619 -0.00382 21  ILE A CD1   
1515 N N     . GLN B 23  ? 0.14415 0.09853 0.16395 -0.01501 -0.05566 -0.02912 22  GLN A N     
1516 C CA    . GLN B 23  ? 0.16908 0.12291 0.17902 -0.01123 -0.06297 -0.03668 22  GLN A CA    
1517 C C     . GLN B 23  ? 0.19555 0.16628 0.21250 -0.01210 -0.06664 -0.03553 22  GLN A C     
1518 O O     . GLN B 23  ? 0.19227 0.16629 0.21100 -0.01455 -0.07586 -0.04154 22  GLN A O     
1519 C CB    . GLN B 23  ? 0.21136 0.16017 0.20359 -0.00064 -0.05913 -0.03765 22  GLN A CB    
1520 C CG    . GLN B 23  ? 0.22922 0.16046 0.21064 0.00256  -0.05981 -0.04336 22  GLN A CG    
1521 C CD    . GLN B 23  ? 0.24926 0.17204 0.22128 0.00288  -0.06971 -0.05429 22  GLN A CD    
1522 O OE1   . GLN B 23  ? 0.25825 0.18816 0.23724 -0.00285 -0.07777 -0.05768 22  GLN A OE1   
1523 N NE2   . GLN B 23  ? 0.23527 0.14354 0.19132 0.01014  -0.06949 -0.06036 22  GLN A NE2   
1524 N N     . LEU B 24  ? 0.13184 0.11343 0.15312 -0.00978 -0.06006 -0.02823 23  LEU A N     
1525 C CA    . LEU B 24  ? 0.13431 0.13133 0.16288 -0.00930 -0.06281 -0.02639 23  LEU A CA    
1526 C C     . LEU B 24  ? 0.18334 0.18880 0.23037 -0.01846 -0.06767 -0.02700 23  LEU A C     
1527 O O     . LEU B 24  ? 0.20418 0.21984 0.25658 -0.01934 -0.07573 -0.03023 23  LEU A O     
1528 C CB    . LEU B 24  ? 0.17900 0.18295 0.20958 -0.00554 -0.05428 -0.01897 23  LEU A CB    
1529 C CG    . LEU B 24  ? 0.19838 0.21667 0.23528 -0.00291 -0.05656 -0.01676 23  LEU A CG    
1530 C CD1   . LEU B 24  ? 0.16919 0.18668 0.19136 0.00606  -0.05845 -0.01734 23  LEU A CD1   
1531 C CD2   . LEU B 24  ? 0.15366 0.17813 0.19912 -0.00282 -0.04859 -0.01046 23  LEU A CD2   
1532 N N     . ILE B 25  ? 0.17699 0.17934 0.23435 -0.02518 -0.06285 -0.02336 24  ILE A N     
1533 C CA    . ILE B 25  ? 0.19089 0.20308 0.26840 -0.03428 -0.06463 -0.02140 24  ILE A CA    
1534 C C     . ILE B 25  ? 0.21807 0.22221 0.29728 -0.04069 -0.07052 -0.02729 24  ILE A C     
1535 O O     . ILE B 25  ? 0.24373 0.25877 0.33236 -0.04463 -0.07495 -0.02921 24  ILE A O     
1536 C CB    . ILE B 25  ? 0.20838 0.22032 0.29298 -0.03739 -0.05468 -0.01346 24  ILE A CB    
1537 C CG1   . ILE B 25  ? 0.22332 0.24315 0.30348 -0.03019 -0.04718 -0.00842 24  ILE A CG1   
1538 C CG2   . ILE B 25  ? 0.16847 0.19012 0.27306 -0.04651 -0.05405 -0.00999 24  ILE A CG2   
1539 C CD1   . ILE B 25  ? 0.19770 0.23589 0.28954 -0.02899 -0.04741 -0.00614 24  ILE A CD1   
1540 N N     . GLN B 26  ? 0.19245 0.17751 0.26239 -0.04135 -0.06980 -0.03000 25  GLN A N     
1541 C CA    . GLN B 26  ? 0.22152 0.19613 0.29385 -0.04786 -0.07270 -0.03425 25  GLN A CA    
1542 C C     . GLN B 26  ? 0.23024 0.19261 0.28630 -0.04354 -0.07977 -0.04422 25  GLN A C     
1543 O O     . GLN B 26  ? 0.25542 0.20790 0.31251 -0.04874 -0.08291 -0.04911 25  GLN A O     
1544 C CB    . GLN B 26  ? 0.22698 0.18768 0.30187 -0.05167 -0.06577 -0.02908 25  GLN A CB    
1545 C CG    . GLN B 26  ? 0.22087 0.19295 0.31085 -0.05632 -0.05825 -0.01904 25  GLN A CG    
1546 C CD    . GLN B 26  ? 0.31234 0.27049 0.40233 -0.05877 -0.05139 -0.01289 25  GLN A CD    
1547 O OE1   . GLN B 26  ? 0.32975 0.26922 0.41009 -0.05739 -0.05243 -0.01627 25  GLN A OE1   
1548 N NE2   . GLN B 26  ? 0.34596 0.31314 0.44580 -0.06136 -0.04389 -0.00342 25  GLN A NE2   
1549 N N     . ASN B 27  ? 0.19040 0.15269 0.23087 -0.03396 -0.08181 -0.04726 26  ASN A N     
1550 C CA    . ASN B 27  ? 0.24851 0.20164 0.27118 -0.02798 -0.08787 -0.05643 26  ASN A CA    
1551 C C     . ASN B 27  ? 0.26480 0.19615 0.27888 -0.02804 -0.08658 -0.06091 26  ASN A C     
1552 O O     . ASN B 27  ? 0.28903 0.21244 0.29714 -0.02908 -0.09210 -0.06889 26  ASN A O     
1553 C CB    . ASN B 27  ? 0.23845 0.20258 0.26523 -0.03123 -0.09637 -0.06165 26  ASN A CB    
1554 C CG    . ASN B 27  ? 0.34301 0.32640 0.37062 -0.02621 -0.09846 -0.05854 26  ASN A CG    
1555 O OD1   . ASN B 27  ? 0.34913 0.33228 0.35958 -0.01619 -0.09984 -0.06033 26  ASN A OD1   
1556 N ND2   . ASN B 27  ? 0.34702 0.34726 0.39410 -0.03216 -0.09762 -0.05295 26  ASN A ND2   
1557 N N     . HIS B 28  ? 0.26979 0.19130 0.28285 -0.02634 -0.07938 -0.05589 27  HIS A N     
1558 C CA    . HIS B 28  ? 0.25528 0.15609 0.25816 -0.02341 -0.07726 -0.05940 27  HIS A CA    
1559 C C     . HIS B 28  ? 0.29445 0.18934 0.29272 -0.01730 -0.06959 -0.05331 27  HIS A C     
1560 O O     . HIS B 28  ? 0.25621 0.16174 0.26167 -0.01796 -0.06609 -0.04632 27  HIS A O     
1561 C CB    . HIS B 28  ? 0.33680 0.22844 0.35135 -0.03337 -0.07757 -0.05964 27  HIS A CB    
1562 C CG    . HIS B 28  ? 0.37793 0.27397 0.40902 -0.04048 -0.07129 -0.04930 27  HIS A CG    
1563 N ND1   . HIS B 28  ? 0.41751 0.30203 0.44702 -0.03820 -0.06420 -0.04304 27  HIS A ND1   
1564 C CD2   . HIS B 28  ? 0.38255 0.29407 0.43111 -0.04872 -0.07050 -0.04362 27  HIS A CD2   
1565 C CE1   . HIS B 28  ? 0.40343 0.29558 0.44742 -0.04482 -0.05945 -0.03387 27  HIS A CE1   
1566 N NE2   . HIS B 28  ? 0.32787 0.23655 0.38378 -0.05124 -0.06268 -0.03410 27  HIS A NE2   
1567 N N     . PHE B 29  ? 0.26553 0.14366 0.25193 -0.01092 -0.06702 -0.05625 28  PHE A N     
1568 C CA    . PHE B 29  ? 0.27146 0.14358 0.25230 -0.00322 -0.05994 -0.05121 28  PHE A CA    
1569 C C     . PHE B 29  ? 0.24883 0.10359 0.22972 -0.00324 -0.05660 -0.05018 28  PHE A C     
1570 O O     . PHE B 29  ? 0.33609 0.17911 0.31161 -0.00367 -0.05954 -0.05726 28  PHE A O     
1571 C CB    . PHE B 29  ? 0.26142 0.13444 0.22453 0.00938  -0.05836 -0.05523 28  PHE A CB    
1572 C CG    . PHE B 29  ? 0.30714 0.17899 0.26632 0.01828  -0.04923 -0.04909 28  PHE A CG    
1573 C CD1   . PHE B 29  ? 0.23166 0.12058 0.19797 0.01926  -0.04260 -0.03956 28  PHE A CD1   
1574 C CD2   . PHE B 29  ? 0.25213 0.10659 0.20100 0.02603  -0.04766 -0.05336 28  PHE A CD2   
1575 C CE1   . PHE B 29  ? 0.23549 0.12563 0.20045 0.02680  -0.03561 -0.03443 28  PHE A CE1   
1576 C CE2   . PHE B 29  ? 0.27701 0.13271 0.22417 0.03488  -0.03989 -0.04762 28  PHE A CE2   
1577 C CZ    . PHE B 29  ? 0.25241 0.12725 0.20848 0.03486  -0.03418 -0.03801 28  PHE A CZ    
1578 N N     . VAL B 30  ? 0.34381 0.19658 0.33024 -0.00237 -0.05063 -0.04135 29  VAL A N     
1579 C CA    . VAL B 30  ? 0.38950 0.22594 0.37388 0.00068  -0.04645 -0.03899 29  VAL A CA    
1580 C C     . VAL B 30  ? 0.29603 0.13388 0.27486 0.01176  -0.04062 -0.03332 29  VAL A C     
1581 O O     . VAL B 30  ? 0.34389 0.19798 0.32670 0.01267  -0.03811 -0.02737 29  VAL A O     
1582 C CB    . VAL B 30  ? 0.40263 0.23429 0.40045 -0.00935 -0.04449 -0.03189 29  VAL A CB    
1583 C CG1   . VAL B 30  ? 0.39964 0.23150 0.40564 -0.02073 -0.04969 -0.03717 29  VAL A CG1   
1584 C CG2   . VAL B 30  ? 0.38113 0.22588 0.38797 -0.01168 -0.04091 -0.02111 29  VAL A CG2   
1585 N N     . ASP B 31  ? 0.35772 0.18281 0.32906 0.01995  -0.03728 -0.03444 30  ASP A N     
1586 C CA    . ASP B 31  ? 0.41395 0.24293 0.38164 0.03153  -0.03160 -0.02890 30  ASP A CA    
1587 C C     . ASP B 31  ? 0.34130 0.17283 0.31797 0.03006  -0.02849 -0.01745 30  ASP A C     
1588 O O     . ASP B 31  ? 0.31725 0.16070 0.29432 0.03751  -0.02507 -0.01167 30  ASP A O     
1589 C CB    . ASP B 31  ? 0.46109 0.27745 0.41951 0.04126  -0.02867 -0.03326 30  ASP A CB    
1590 C CG    . ASP B 31  ? 0.46728 0.28527 0.41321 0.04722  -0.02999 -0.04292 30  ASP A CG    
1591 O OD1   . ASP B 31  ? 0.46109 0.29358 0.40341 0.05385  -0.02741 -0.04178 30  ASP A OD1   
1592 O OD2   . ASP B 31  ? 0.57491 0.38004 0.51454 0.04521  -0.03341 -0.05139 30  ASP A OD2   
1593 N N     . GLU B 32  ? 0.34938 0.17278 0.33352 0.02074  -0.02895 -0.01349 31  GLU A N     
1594 C CA    . GLU B 32  ? 0.32670 0.15079 0.31629 0.02092  -0.02525 -0.00175 31  GLU A CA    
1595 C C     . GLU B 32  ? 0.31033 0.15674 0.30527 0.01827  -0.02478 0.00414  31  GLU A C     
1596 O O     . GLU B 32  ? 0.30996 0.16802 0.30958 0.01042  -0.02683 0.00124  31  GLU A O     
1597 C CB    . GLU B 32  ? 0.37963 0.19069 0.37562 0.01144  -0.02398 0.00187  31  GLU A CB    
1598 C CG    . GLU B 32  ? 0.38451 0.19250 0.38243 0.01404  -0.01888 0.01473  31  GLU A CG    
1599 C CD    . GLU B 32  ? 0.45633 0.24892 0.45894 0.00566  -0.01569 0.01913  31  GLU A CD    
1600 O OE1   . GLU B 32  ? 0.45081 0.24341 0.46022 -0.00607 -0.01788 0.01504  31  GLU A OE1   
1601 O OE2   . GLU B 32  ? 0.48053 0.26160 0.48020 0.01127  -0.01073 0.02723  31  GLU A OE2   
1602 N N     . TYR B 33  ? 0.24279 0.09896 0.23724 0.02515  -0.02141 0.01198  32  TYR A N     
1603 C CA    . TYR B 33  ? 0.23936 0.11934 0.23788 0.02326  -0.02024 0.01636  32  TYR A CA    
1604 C C     . TYR B 33  ? 0.24185 0.12238 0.24444 0.01683  -0.01852 0.02504  32  TYR A C     
1605 O O     . TYR B 33  ? 0.22087 0.09157 0.22124 0.02056  -0.01648 0.03272  32  TYR A O     
1606 C CB    . TYR B 33  ? 0.21891 0.11104 0.21540 0.03383  -0.01873 0.01900  32  TYR A CB    
1607 C CG    . TYR B 33  ? 0.19617 0.11140 0.19656 0.03260  -0.01853 0.02242  32  TYR A CG    
1608 C CD1   . TYR B 33  ? 0.15451 0.07988 0.15841 0.02378  -0.01903 0.02113  32  TYR A CD1   
1609 C CD2   . TYR B 33  ? 0.23532 0.16228 0.23634 0.04073  -0.01833 0.02628  32  TYR A CD2   
1610 C CE1   . TYR B 33  ? 0.14078 0.08439 0.14698 0.02313  -0.01912 0.02296  32  TYR A CE1   
1611 C CE2   . TYR B 33  ? 0.24089 0.18795 0.24552 0.03903  -0.01944 0.02785  32  TYR A CE2   
1612 C CZ    . TYR B 33  ? 0.15113 0.10497 0.15748 0.03025  -0.01975 0.02578  32  TYR A CZ    
1613 O OH    . TYR B 33  ? 0.14597 0.11701 0.15477 0.02897  -0.02116 0.02604  32  TYR A OH    
1614 N N     . ASP B 34  ? 0.18113 0.07271 0.18918 0.00804  -0.01873 0.02443  33  ASP A N     
1615 C CA    . ASP B 34  ? 0.20084 0.09671 0.21257 0.00244  -0.01574 0.03275  33  ASP A CA    
1616 C C     . ASP B 34  ? 0.17821 0.09583 0.18910 0.00363  -0.01496 0.03359  33  ASP A C     
1617 O O     . ASP B 34  ? 0.18695 0.11513 0.20215 -0.00154 -0.01558 0.02930  33  ASP A O     
1618 C CB    . ASP B 34  ? 0.20302 0.09392 0.22361 -0.00868 -0.01610 0.03132  33  ASP A CB    
1619 C CG    . ASP B 34  ? 0.26740 0.16109 0.29270 -0.01398 -0.01114 0.04162  33  ASP A CG    
1620 O OD1   . ASP B 34  ? 0.19118 0.08840 0.21000 -0.00829 -0.00771 0.04978  33  ASP A OD1   
1621 O OD2   . ASP B 34  ? 0.28426 0.17773 0.31995 -0.02358 -0.01061 0.04185  33  ASP A OD2   
1622 N N     . PRO B 35  ? 0.16298 0.08748 0.16836 0.01067  -0.01420 0.03859  34  PRO A N     
1623 C CA    . PRO B 35  ? 0.14820 0.09198 0.15240 0.01182  -0.01490 0.03705  34  PRO A CA    
1624 C C     . PRO B 35  ? 0.15341 0.10503 0.15918 0.00553  -0.01231 0.03894  34  PRO A C     
1625 O O     . PRO B 35  ? 0.19431 0.14141 0.19903 0.00355  -0.00877 0.04637  34  PRO A O     
1626 C CB    . PRO B 35  ? 0.18020 0.12795 0.17820 0.02036  -0.01565 0.04277  34  PRO A CB    
1627 C CG    . PRO B 35  ? 0.16918 0.10124 0.16616 0.02591  -0.01572 0.04478  34  PRO A CG    
1628 C CD    . PRO B 35  ? 0.17851 0.09339 0.17852 0.01858  -0.01356 0.04519  34  PRO A CD    
1629 N N     . THR B 36  ? 0.13897 0.10232 0.14725 0.00319  -0.01334 0.03284  35  THR A N     
1630 C CA    . THR B 36  ? 0.13593 0.10690 0.14665 -0.00179 -0.01063 0.03309  35  THR A CA    
1631 C C     . THR B 36  ? 0.15890 0.13899 0.16178 0.00150  -0.00871 0.03697  35  THR A C     
1632 O O     . THR B 36  ? 0.12633 0.11228 0.12360 0.00649  -0.01170 0.03529  35  THR A O     
1633 C CB    . THR B 36  ? 0.11037 0.08817 0.12582 -0.00410 -0.01244 0.02516  35  THR A CB    
1634 O OG1   . THR B 36  ? 0.11027 0.08003 0.13005 -0.00591 -0.01472 0.02139  35  THR A OG1   
1635 C CG2   . THR B 36  ? 0.12014 0.10587 0.13932 -0.00808 -0.00941 0.02515  35  THR A CG2   
1636 N N     . ILE B 37  ? 0.15724 0.13952 0.15995 -0.00119 -0.00378 0.04204  36  ILE A N     
1637 C CA    . ILE B 37  ? 0.13484 0.12744 0.12894 0.00189  -0.00140 0.04317  36  ILE A CA    
1638 C C     . ILE B 37  ? 0.12361 0.12406 0.12286 -0.00108 -0.00064 0.03626  36  ILE A C     
1639 O O     . ILE B 37  ? 0.13328 0.13935 0.12888 0.00115  -0.00358 0.02943  36  ILE A O     
1640 C CB    . ILE B 37  ? 0.14975 0.14115 0.13902 0.00246  0.00523  0.05387  36  ILE A CB    
1641 C CG1   . ILE B 37  ? 0.16382 0.14662 0.14568 0.00732  0.00446  0.06172  36  ILE A CG1   
1642 C CG2   . ILE B 37  ? 0.15372 0.15638 0.13262 0.00625  0.00842  0.05358  36  ILE A CG2   
1643 C CD1   . ILE B 37  ? 0.16757 0.15743 0.13641 0.01544  -0.00018 0.06013  36  ILE A CD1   
1644 N N     . GLU B 38  ? 0.13209 0.13273 0.14111 -0.00622 0.00302  0.03808  37  GLU A N     
1645 C CA    . GLU B 38  ? 0.15479 0.16237 0.17070 -0.00828 0.00339  0.03221  37  GLU A CA    
1646 C C     . GLU B 38  ? 0.11019 0.11756 0.13998 -0.01454 0.00517  0.03489  37  GLU A C     
1647 O O     . GLU B 38  ? 0.14882 0.15485 0.18233 -0.01744 0.00948  0.04259  37  GLU A O     
1648 C CB    . GLU B 38  ? 0.15993 0.17665 0.16874 -0.00450 0.00773  0.03153  37  GLU A CB    
1649 C CG    . GLU B 38  ? 0.12093 0.14375 0.13632 -0.00490 0.00857  0.02574  37  GLU A CG    
1650 C CD    . GLU B 38  ? 0.20858 0.23956 0.21833 -0.00080 0.01500  0.02648  37  GLU A CD    
1651 O OE1   . GLU B 38  ? 0.18777 0.21892 0.18447 0.00416  0.01435  0.02216  37  GLU A OE1   
1652 O OE2   . GLU B 38  ? 0.20491 0.24276 0.22360 -0.00239 0.02073  0.03115  37  GLU A OE2   
1653 N N     . ASP B 39  ? 0.10964 0.11864 0.14743 -0.01673 0.00161  0.02890  38  ASP A N     
1654 C CA    . ASP B 39  ? 0.15103 0.16215 0.20290 -0.02274 0.00122  0.02988  38  ASP A CA    
1655 C C     . ASP B 39  ? 0.13795 0.15824 0.19584 -0.02186 -0.00023 0.02468  38  ASP A C     
1656 O O     . ASP B 39  ? 0.11092 0.13039 0.16240 -0.01767 -0.00262 0.01931  38  ASP A O     
1657 C CB    . ASP B 39  ? 0.12704 0.12625 0.18193 -0.02643 -0.00432 0.02802  38  ASP A CB    
1658 C CG    . ASP B 39  ? 0.20639 0.19492 0.25855 -0.02784 -0.00222 0.03459  38  ASP A CG    
1659 O OD1   . ASP B 39  ? 0.18606 0.17576 0.24645 -0.03278 0.00215  0.04141  38  ASP A OD1   
1660 O OD2   . ASP B 39  ? 0.21453 0.19403 0.25697 -0.02359 -0.00440 0.03374  38  ASP A OD2   
1661 N N     . SER B 40  ? 0.15567 0.18503 0.22739 -0.02593 0.00126  0.02697  39  SER A N     
1662 C CA    . SER B 40  ? 0.16345 0.20378 0.24271 -0.02412 0.00034  0.02366  39  SER A CA    
1663 C C     . SER B 40  ? 0.15647 0.20077 0.25062 -0.03017 -0.00514 0.02257  39  SER A C     
1664 O O     . SER B 40  ? 0.13874 0.18244 0.24283 -0.03721 -0.00491 0.02644  39  SER A O     
1665 C CB    . SER B 40  ? 0.16859 0.22178 0.25126 -0.02097 0.00836  0.02761  39  SER A CB    
1666 O OG    . SER B 40  ? 0.20245 0.25228 0.27000 -0.01426 0.01144  0.02542  39  SER A OG    
1667 N N     . TYR B 41  ? 0.09846 0.14653 0.19417 -0.02750 -0.01038 0.01741  40  TYR A N     
1668 C CA    . TYR B 41  ? 0.12967 0.18328 0.23820 -0.03235 -0.01736 0.01514  40  TYR A CA    
1669 C C     . TYR B 41  ? 0.10496 0.17295 0.22022 -0.02747 -0.01860 0.01388  40  TYR A C     
1670 O O     . TYR B 41  ? 0.10420 0.17232 0.21101 -0.01993 -0.01521 0.01329  40  TYR A O     
1671 C CB    . TYR B 41  ? 0.10512 0.14494 0.20508 -0.03342 -0.02534 0.00926  40  TYR A CB    
1672 C CG    . TYR B 41  ? 0.15762 0.18193 0.25026 -0.03636 -0.02399 0.01053  40  TYR A CG    
1673 C CD1   . TYR B 41  ? 0.18900 0.20816 0.29101 -0.04450 -0.02571 0.01210  40  TYR A CD1   
1674 C CD2   . TYR B 41  ? 0.15445 0.16952 0.23210 -0.03089 -0.02104 0.01052  40  TYR A CD2   
1675 C CE1   . TYR B 41  ? 0.21784 0.22101 0.31256 -0.04585 -0.02402 0.01411  40  TYR A CE1   
1676 C CE2   . TYR B 41  ? 0.15802 0.16039 0.22932 -0.03197 -0.02001 0.01231  40  TYR A CE2   
1677 C CZ    . TYR B 41  ? 0.21610 0.21167 0.29506 -0.03880 -0.02121 0.01438  40  TYR A CZ    
1678 O OH    . TYR B 41  ? 0.21179 0.19300 0.28361 -0.03848 -0.01977 0.01693  40  TYR A OH    
1679 N N     . ARG B 42  ? 0.07708 0.15722 0.20874 -0.03192 -0.02377 0.01357  41  ARG A N     
1680 C CA    . ARG B 42  ? 0.09873 0.19432 0.23856 -0.02675 -0.02657 0.01276  41  ARG A CA    
1681 C C     . ARG B 42  ? 0.11228 0.20882 0.25548 -0.02974 -0.03857 0.00725  41  ARG A C     
1682 O O     . ARG B 42  ? 0.16780 0.26102 0.31651 -0.03823 -0.04261 0.00527  41  ARG A O     
1683 C CB    . ARG B 42  ? 0.14214 0.25846 0.30201 -0.02788 -0.02064 0.01862  41  ARG A CB    
1684 C CG    . ARG B 42  ? 0.13762 0.25545 0.29106 -0.02079 -0.00890 0.02276  41  ARG A CG    
1685 C CD    . ARG B 42  ? 0.18141 0.31859 0.35317 -0.02218 -0.00044 0.02973  41  ARG A CD    
1686 N NE    . ARG B 42  ? 0.12633 0.28225 0.31256 -0.01885 -0.00211 0.02973  41  ARG A NE    
1687 C CZ    . ARG B 42  ? 0.10607 0.27105 0.29239 -0.00804 0.00205  0.03034  41  ARG A CZ    
1688 N NH1   . ARG B 42  ? 0.23258 0.38692 0.40294 0.00052  0.00708  0.02927  41  ARG A NH1   
1689 N NH2   . ARG B 42  ? 0.09086 0.27235 0.29013 -0.00540 0.00093  0.03051  41  ARG A NH2   
1690 N N     . LYS B 43  ? 0.07773 0.17559 0.21281 -0.02184 -0.04327 0.00433  42  LYS A N     
1691 C CA    . LYS B 43  ? 0.13891 0.23954 0.27462 -0.02287 -0.05519 -0.00113 42  LYS A CA    
1692 C C     . LYS B 43  ? 0.12160 0.23583 0.25863 -0.01350 -0.05826 -0.00025 42  LYS A C     
1693 O O     . LYS B 43  ? 0.13061 0.24059 0.25742 -0.00449 -0.05252 0.00244  42  LYS A O     
1694 C CB    . LYS B 43  ? 0.16372 0.24436 0.27892 -0.02175 -0.05928 -0.00653 42  LYS A CB    
1695 C CG    . LYS B 43  ? 0.18328 0.26435 0.29442 -0.02267 -0.07059 -0.01324 42  LYS A CG    
1696 C CD    . LYS B 43  ? 0.24657 0.30893 0.33788 -0.02016 -0.07439 -0.01870 42  LYS A CD    
1697 C CE    . LYS B 43  ? 0.24435 0.30519 0.32824 -0.02105 -0.08375 -0.02593 42  LYS A CE    
1698 N NZ    . LYS B 43  ? 0.24763 0.30784 0.34346 -0.03220 -0.08534 -0.02854 42  LYS A NZ    
1699 N N     . GLN B 44  ? 0.15796 0.28503 0.30184 -0.01511 -0.06502 -0.00264 43  GLN A N     
1700 C CA    . GLN B 44  ? 0.13394 0.27377 0.27693 -0.00547 -0.06936 -0.00162 43  GLN A CA    
1701 C C     . GLN B 44  ? 0.19777 0.32745 0.32191 -0.00156 -0.07825 -0.00628 43  GLN A C     
1702 O O     . GLN B 44  ? 0.19225 0.31495 0.31119 -0.00837 -0.08449 -0.01227 43  GLN A O     
1703 C CB    . GLN B 44  ? 0.11772 0.28042 0.27870 -0.00811 -0.07203 -0.00112 43  GLN A CB    
1704 C CG    . GLN B 44  ? 0.10605 0.28355 0.26630 0.00284  -0.07652 0.00116  43  GLN A CG    
1705 C CD    . GLN B 44  ? 0.29576 0.49900 0.47580 0.00121  -0.07913 0.00115  43  GLN A CD    
1706 O OE1   . GLN B 44  ? 0.26354 0.47584 0.46079 -0.00165 -0.07195 0.00235  43  GLN A OE1   
1707 N NE2   . GLN B 44  ? 0.24932 0.46370 0.42735 0.00266  -0.08954 0.00102  43  GLN A NE2   
1708 N N     . VAL B 45  ? 0.15203 0.27902 0.26463 0.01011  -0.07768 -0.00334 44  VAL A N     
1709 C CA    . VAL B 45  ? 0.12175 0.23892 0.21349 0.01640  -0.08364 -0.00596 44  VAL A CA    
1710 C C     . VAL B 45  ? 0.18082 0.30771 0.26990 0.02757  -0.08503 -0.00043 44  VAL A C     
1711 O O     . VAL B 45  ? 0.15954 0.29620 0.26078 0.03214  -0.07996 0.00542  44  VAL A O     
1712 C CB    . VAL B 45  ? 0.15592 0.25263 0.23030 0.01970  -0.07802 -0.00621 44  VAL A CB    
1713 C CG1   . VAL B 45  ? 0.19460 0.27931 0.26944 0.00906  -0.07590 -0.01049 44  VAL A CG1   
1714 C CG2   . VAL B 45  ? 0.14198 0.23502 0.21660 0.02534  -0.06613 0.00088  44  VAL A CG2   
1715 N N     . VAL B 46  ? 0.20707 0.32960 0.27919 0.03249  -0.09145 -0.00213 45  VAL A N     
1716 C CA    . VAL B 46  ? 0.21920 0.34427 0.28264 0.04428  -0.09192 0.00380  45  VAL A CA    
1717 C C     . VAL B 46  ? 0.22529 0.33184 0.26503 0.05199  -0.08679 0.00554  45  VAL A C     
1718 O O     . VAL B 46  ? 0.20275 0.29999 0.22680 0.05061  -0.09015 0.00039  45  VAL A O     
1719 C CB    . VAL B 46  ? 0.21416 0.35087 0.27690 0.04433  -0.10314 0.00152  45  VAL A CB    
1720 C CG1   . VAL B 46  ? 0.26841 0.40690 0.32245 0.05708  -0.10305 0.00837  45  VAL A CG1   
1721 C CG2   . VAL B 46  ? 0.25389 0.40999 0.34177 0.03531  -0.10791 0.00052  45  VAL A CG2   
1722 N N     . ILE B 47  ? 0.18788 0.28827 0.22523 0.05999  -0.07775 0.01298  46  ILE A N     
1723 C CA    . ILE B 47  ? 0.22882 0.31207 0.24626 0.06681  -0.07084 0.01704  46  ILE A CA    
1724 C C     . ILE B 47  ? 0.21157 0.29381 0.22209 0.07731  -0.06812 0.02504  46  ILE A C     
1725 O O     . ILE B 47  ? 0.21286 0.29733 0.23409 0.08093  -0.06329 0.02993  46  ILE A O     
1726 C CB    . ILE B 47  ? 0.16762 0.23971 0.18816 0.06496  -0.06085 0.01888  46  ILE A CB    
1727 C CG1   . ILE B 47  ? 0.13268 0.20174 0.15886 0.05229  -0.06141 0.01126  46  ILE A CG1   
1728 C CG2   . ILE B 47  ? 0.16345 0.21803 0.16636 0.07054  -0.05242 0.02464  46  ILE A CG2   
1729 C CD1   . ILE B 47  ? 0.13544 0.19543 0.16870 0.04675  -0.05083 0.01249  46  ILE A CD1   
1730 N N     . ASP B 48  ? 0.21324 0.29110 0.20505 0.08264  -0.07063 0.02612  47  ASP A N     
1731 C CA    . ASP B 48  ? 0.25670 0.33309 0.23968 0.09287  -0.06846 0.03388  47  ASP A CA    
1732 C C     . ASP B 48  ? 0.22814 0.32083 0.22609 0.09512  -0.07485 0.03478  47  ASP A C     
1733 O O     . ASP B 48  ? 0.27186 0.36306 0.27302 0.10226  -0.06991 0.04174  47  ASP A O     
1734 C CB    . ASP B 48  ? 0.25296 0.31325 0.23189 0.09753  -0.05538 0.04242  47  ASP A CB    
1735 C CG    . ASP B 48  ? 0.26215 0.30749 0.22842 0.09528  -0.04826 0.04295  47  ASP A CG    
1736 O OD1   . ASP B 48  ? 0.25615 0.30238 0.21130 0.09342  -0.05294 0.03775  47  ASP A OD1   
1737 O OD2   . ASP B 48  ? 0.25333 0.28566 0.22135 0.09527  -0.03783 0.04829  47  ASP A OD2   
1738 N N     . GLY B 49  ? 0.20719 0.31514 0.21534 0.08868  -0.08567 0.02774  48  GLY A N     
1739 C CA    . GLY B 49  ? 0.21098 0.33679 0.23548 0.09003  -0.09246 0.02868  48  GLY A CA    
1740 C C     . GLY B 49  ? 0.19811 0.33120 0.24597 0.08740  -0.08776 0.03029  48  GLY A C     
1741 O O     . GLY B 49  ? 0.19980 0.34950 0.26404 0.08822  -0.09303 0.03102  48  GLY A O     
1742 N N     . GLU B 50  ? 0.21651 0.33849 0.26662 0.08471  -0.07796 0.03070  49  GLU A N     
1743 C CA    . GLU B 50  ? 0.16667 0.29409 0.23630 0.08317  -0.07190 0.03160  49  GLU A CA    
1744 C C     . GLU B 50  ? 0.17175 0.30517 0.25388 0.07112  -0.07328 0.02532  49  GLU A C     
1745 O O     . GLU B 50  ? 0.16371 0.28590 0.23614 0.06634  -0.07124 0.02221  49  GLU A O     
1746 C CB    . GLU B 50  ? 0.22283 0.33239 0.28530 0.08924  -0.05932 0.03654  49  GLU A CB    
1747 C CG    . GLU B 50  ? 0.20866 0.30990 0.25974 0.10055  -0.05638 0.04373  49  GLU A CG    
1748 C CD    . GLU B 50  ? 0.38000 0.45874 0.42146 0.10429  -0.04420 0.04831  49  GLU A CD    
1749 O OE1   . GLU B 50  ? 0.31157 0.38284 0.35816 0.09948  -0.03759 0.04583  49  GLU A OE1   
1750 O OE2   . GLU B 50  ? 0.35052 0.41887 0.37944 0.11173  -0.04136 0.05451  49  GLU A OE2   
1751 N N     . THR B 51  ? 0.15116 0.30204 0.25533 0.06637  -0.07613 0.02391  50  THR A N     
1752 C CA    . THR B 51  ? 0.15855 0.31566 0.27632 0.05420  -0.07664 0.01921  50  THR A CA    
1753 C C     . THR B 51  ? 0.17009 0.31991 0.29119 0.05421  -0.06474 0.01994  50  THR A C     
1754 O O     . THR B 51  ? 0.16576 0.31596 0.29118 0.06164  -0.05714 0.02348  50  THR A O     
1755 C CB    . THR B 51  ? 0.22961 0.40797 0.37151 0.04864  -0.08290 0.01856  50  THR A CB    
1756 O OG1   . THR B 51  ? 0.22498 0.41139 0.36329 0.04979  -0.09430 0.01841  50  THR A OG1   
1757 C CG2   . THR B 51  ? 0.17457 0.35808 0.32856 0.03427  -0.08309 0.01533  50  THR A CG2   
1758 N N     . SER B 52  ? 0.10743 0.25040 0.22535 0.04609  -0.06294 0.01631  51  SER A N     
1759 C CA    . SER B 52  ? 0.11940 0.25626 0.23946 0.04518  -0.05186 0.01731  51  SER A CA    
1760 C C     . SER B 52  ? 0.13316 0.27029 0.26118 0.03165  -0.05121 0.01341  51  SER A C     
1761 O O     . SER B 52  ? 0.11217 0.24714 0.23775 0.02404  -0.05894 0.00886  51  SER A O     
1762 C CB    . SER B 52  ? 0.16069 0.27268 0.25947 0.04885  -0.04524 0.01821  51  SER A CB    
1763 O OG    . SER B 52  ? 0.20507 0.31450 0.29665 0.06130  -0.04467 0.02321  51  SER A OG    
1764 N N     . LEU B 53  ? 0.08218 0.22017 0.21792 0.02955  -0.04148 0.01532  52  LEU A N     
1765 C CA    . LEU B 53  ? 0.08580 0.22043 0.22579 0.01822  -0.03822 0.01356  52  LEU A CA    
1766 C C     . LEU B 53  ? 0.07482 0.18654 0.19621 0.01769  -0.03135 0.01230  52  LEU A C     
1767 O O     . LEU B 53  ? 0.07550 0.18021 0.19050 0.02424  -0.02367 0.01388  52  LEU A O     
1768 C CB    . LEU B 53  ? 0.09537 0.24698 0.25442 0.01681  -0.03133 0.01729  52  LEU A CB    
1769 C CG    . LEU B 53  ? 0.22009 0.37251 0.38745 0.00424  -0.03004 0.01703  52  LEU A CG    
1770 C CD1   . LEU B 53  ? 0.27692 0.44641 0.46018 -0.00152 -0.03427 0.01596  52  LEU A CD1   
1771 C CD2   . LEU B 53  ? 0.20948 0.35786 0.37412 0.00515  -0.01745 0.02015  52  LEU A CD2   
1772 N N     . LEU B 54  ? 0.07439 0.17452 0.18758 0.01029  -0.03461 0.00901  53  LEU A N     
1773 C CA    . LEU B 54  ? 0.07961 0.16092 0.17758 0.00918  -0.02925 0.00785  53  LEU A CA    
1774 C C     . LEU B 54  ? 0.10191 0.18283 0.20470 0.00218  -0.02384 0.00866  53  LEU A C     
1775 O O     . LEU B 54  ? 0.12386 0.20922 0.23536 -0.00562 -0.02714 0.00840  53  LEU A O     
1776 C CB    . LEU B 54  ? 0.08473 0.15389 0.16983 0.00746  -0.03505 0.00449  53  LEU A CB    
1777 C CG    . LEU B 54  ? 0.12381 0.19446 0.20232 0.01442  -0.04124 0.00423  53  LEU A CG    
1778 C CD1   . LEU B 54  ? 0.12743 0.18527 0.19077 0.01367  -0.04487 0.00101  53  LEU A CD1   
1779 C CD2   . LEU B 54  ? 0.09085 0.15963 0.16538 0.02401  -0.03591 0.00832  53  LEU A CD2   
1780 N N     . ASP B 55  ? 0.07677 0.15218 0.17379 0.00518  -0.01569 0.00975  54  ASP A N     
1781 C CA    . ASP B 55  ? 0.09049 0.16359 0.18691 0.00043  -0.01012 0.01096  54  ASP A CA    
1782 C C     . ASP B 55  ? 0.08642 0.14272 0.16761 -0.00071 -0.01033 0.00837  54  ASP A C     
1783 O O     . ASP B 55  ? 0.14646 0.19467 0.21845 0.00410  -0.00819 0.00665  54  ASP A O     
1784 C CB    . ASP B 55  ? 0.09487 0.17377 0.19274 0.00556  -0.00152 0.01290  54  ASP A CB    
1785 C CG    . ASP B 55  ? 0.13595 0.23367 0.25021 0.00857  -0.00002 0.01606  54  ASP A CG    
1786 O OD1   . ASP B 55  ? 0.28112 0.39107 0.41010 0.00245  -0.00330 0.01838  54  ASP A OD1   
1787 O OD2   . ASP B 55  ? 0.16994 0.27004 0.28314 0.01713  0.00454  0.01607  54  ASP A OD2   
1788 N N     . ILE B 56  ? 0.08752 0.13853 0.16731 -0.00697 -0.01291 0.00820  55  ILE A N     
1789 C CA    . ILE B 56  ? 0.11206 0.14938 0.17940 -0.00741 -0.01398 0.00600  55  ILE A CA    
1790 C C     . ILE B 56  ? 0.08402 0.11783 0.14735 -0.00970 -0.00961 0.00788  55  ILE A C     
1791 O O     . ILE B 56  ? 0.08762 0.12381 0.15652 -0.01434 -0.00880 0.01096  55  ILE A O     
1792 C CB    . ILE B 56  ? 0.10211 0.13391 0.16788 -0.01034 -0.02063 0.00380  55  ILE A CB    
1793 C CG1   . ILE B 56  ? 0.17412 0.21042 0.24116 -0.00673 -0.02546 0.00210  55  ILE A CG1   
1794 C CG2   . ILE B 56  ? 0.12691 0.14661 0.18089 -0.00919 -0.02043 0.00217  55  ILE A CG2   
1795 C CD1   . ILE B 56  ? 0.24061 0.27502 0.30788 -0.00986 -0.03300 -0.00099 55  ILE A CD1   
1796 N N     . LEU B 57  ? 0.10988 0.13779 0.16363 -0.00656 -0.00718 0.00624  56  LEU A N     
1797 C CA    . LEU B 57  ? 0.10035 0.12497 0.14740 -0.00740 -0.00455 0.00742  56  LEU A CA    
1798 C C     . LEU B 57  ? 0.10696 0.12271 0.14793 -0.00837 -0.00821 0.00600  56  LEU A C     
1799 O O     . LEU B 57  ? 0.06971 0.08162 0.10695 -0.00628 -0.00955 0.00302  56  LEU A O     
1800 C CB    . LEU B 57  ? 0.12039 0.14570 0.16107 -0.00318 -0.00060 0.00531  56  LEU A CB    
1801 C CG    . LEU B 57  ? 0.15849 0.18282 0.19035 -0.00274 0.00168  0.00629  56  LEU A CG    
1802 C CD1   . LEU B 57  ? 0.08541 0.11562 0.12064 -0.00461 0.00561  0.01255  56  LEU A CD1   
1803 C CD2   . LEU B 57  ? 0.16232 0.18626 0.18675 0.00178  0.00424  0.00183  56  LEU A CD2   
1804 N N     . ASP B 58  ? 0.09629 0.10880 0.13740 -0.01131 -0.00917 0.00876  57  ASP A N     
1805 C CA    . ASP B 58  ? 0.10216 0.10669 0.13791 -0.01102 -0.01188 0.00822  57  ASP A CA    
1806 C C     . ASP B 58  ? 0.13898 0.14352 0.16786 -0.00917 -0.00998 0.01009  57  ASP A C     
1807 O O     . ASP B 58  ? 0.12005 0.12477 0.14789 -0.01012 -0.00762 0.01476  57  ASP A O     
1808 C CB    . ASP B 58  ? 0.10297 0.10187 0.14242 -0.01449 -0.01415 0.00987  57  ASP A CB    
1809 C CG    . ASP B 58  ? 0.10726 0.09677 0.14098 -0.01263 -0.01654 0.00899  57  ASP A CG    
1810 O OD1   . ASP B 58  ? 0.10899 0.09865 0.13816 -0.00895 -0.01698 0.00683  57  ASP A OD1   
1811 O OD2   . ASP B 58  ? 0.16052 0.14236 0.19546 -0.01489 -0.01762 0.01069  57  ASP A OD2   
1812 N N     . THR B 59  ? 0.12053 0.12539 0.14507 -0.00665 -0.01113 0.00685  58  THR A N     
1813 C CA    . THR B 59  ? 0.08535 0.09218 0.10314 -0.00459 -0.01117 0.00714  58  THR A CA    
1814 C C     . THR B 59  ? 0.08477 0.08853 0.10053 -0.00311 -0.01393 0.00897  58  THR A C     
1815 O O     . THR B 59  ? 0.08419 0.08395 0.10318 -0.00307 -0.01544 0.00837  58  THR A O     
1816 C CB    . THR B 59  ? 0.10648 0.11588 0.12261 -0.00355 -0.01196 0.00168  58  THR A CB    
1817 O OG1   . THR B 59  ? 0.09384 0.10165 0.11387 -0.00395 -0.01445 -0.00057 58  THR A OG1   
1818 C CG2   . THR B 59  ? 0.11345 0.12390 0.13197 -0.00351 -0.00895 -0.00041 58  THR A CG2   
1819 N N     . ALA B 60  ? 0.09149 0.09761 0.10082 -0.00069 -0.01450 0.01125  59  ALA A N     
1820 C CA    . ALA B 60  ? 0.09496 0.10016 0.10253 0.00236  -0.01742 0.01336  59  ALA A CA    
1821 C C     . ALA B 60  ? 0.11114 0.12260 0.12144 0.00324  -0.02099 0.00845  59  ALA A C     
1822 O O     . ALA B 60  ? 0.14688 0.16297 0.15634 0.00195  -0.02195 0.00392  59  ALA A O     
1823 C CB    . ALA B 60  ? 0.10608 0.11232 0.10509 0.00562  -0.01705 0.01891  59  ALA A CB    
1824 N N     . GLY B 61  ? 0.08939 0.10076 0.10377 0.00540  -0.02267 0.00929  60  GLY A N     
1825 C CA    . GLY B 61  ? 0.10074 0.12075 0.12040 0.00622  -0.02587 0.00634  60  GLY A CA    
1826 C C     . GLY B 61  ? 0.13136 0.15884 0.14634 0.00953  -0.03008 0.00765  60  GLY A C     
1827 O O     . GLY B 61  ? 0.14036 0.16817 0.15387 0.01447  -0.03127 0.01234  60  GLY A O     
1828 N N     . GLN B 62  ? 0.14807 0.18070 0.15920 0.00772  -0.03257 0.00339  61  GLN A N     
1829 C CA    . GLN B 62  ? 0.16332 0.20413 0.16739 0.01125  -0.03785 0.00339  61  GLN A CA    
1830 C C     . GLN B 62  ? 0.21405 0.26103 0.21961 0.00743  -0.04215 -0.00529 61  GLN A C     
1831 O O     . GLN B 62  ? 0.19786 0.23939 0.20565 0.00302  -0.03927 -0.00980 61  GLN A O     
1832 C CB    . GLN B 62  ? 0.18672 0.22309 0.17650 0.01485  -0.03537 0.00870  61  GLN A CB    
1833 C CG    . GLN B 62  ? 0.16318 0.19367 0.14785 0.01180  -0.03001 0.00699  61  GLN A CG    
1834 C CD    . GLN B 62  ? 0.24351 0.27855 0.22092 0.01138  -0.03259 -0.00063 61  GLN A CD    
1835 O OE1   . GLN B 62  ? 0.25414 0.29681 0.22681 0.01356  -0.03921 -0.00422 61  GLN A OE1   
1836 N NE2   . GLN B 62  ? 0.19239 0.22280 0.16883 0.00906  -0.02788 -0.00370 61  GLN A NE2   
1837 N N     . GLU B 63  ? 0.27685 0.33465 0.28101 0.00942  -0.04957 -0.00786 62  GLU A N     
1838 C CA    . GLU B 63  ? 0.30029 0.36341 0.30620 0.00513  -0.05541 -0.01759 62  GLU A CA    
1839 C C     . GLU B 63  ? 0.34386 0.41281 0.33387 0.00961  -0.06173 -0.02037 62  GLU A C     
1840 O O     . GLU B 63  ? 0.35035 0.42876 0.34228 0.00796  -0.07058 -0.02784 62  GLU A O     
1841 C CB    . GLU B 63  ? 0.34483 0.41819 0.36956 0.00098  -0.05996 -0.02038 62  GLU A CB    
1842 C CG    . GLU B 63  ? 0.31433 0.38187 0.35243 -0.00272 -0.05286 -0.01765 62  GLU A CG    
1843 C CD    . GLU B 63  ? 0.47513 0.55461 0.53276 -0.00601 -0.05543 -0.01819 62  GLU A CD    
1844 O OE1   . GLU B 63  ? 0.53450 0.62813 0.59749 -0.00583 -0.06356 -0.02081 62  GLU A OE1   
1845 O OE2   . GLU B 63  ? 0.47684 0.55284 0.54469 -0.00849 -0.04928 -0.01566 62  GLU A OE2   
1846 N N     . GLU B 64  ? 0.23034 0.29414 0.20426 0.01531  -0.05741 -0.01430 63  GLU A N     
1847 C CA    . GLU B 64  ? 0.26604 0.33478 0.22106 0.02126  -0.06191 -0.01539 63  GLU A CA    
1848 C C     . GLU B 64  ? 0.29730 0.35828 0.23709 0.02198  -0.05682 -0.01915 63  GLU A C     
1849 O O     . GLU B 64  ? 0.29230 0.35730 0.21440 0.02699  -0.06078 -0.02262 63  GLU A O     
1850 C CB    . GLU B 64  ? 0.22526 0.29580 0.17144 0.02937  -0.06052 -0.00333 63  GLU A CB    
1851 C CG    . GLU B 64  ? 0.35806 0.43992 0.31325 0.03278  -0.06792 -0.00019 63  GLU A CG    
1852 C CD    . GLU B 64  ? 0.44027 0.51771 0.41241 0.03104  -0.06304 0.00554  63  GLU A CD    
1853 O OE1   . GLU B 64  ? 0.46382 0.53821 0.44994 0.02393  -0.06045 0.00069  63  GLU A OE1   
1854 O OE2   . GLU B 64  ? 0.48747 0.56348 0.45758 0.03760  -0.06156 0.01510  63  GLU A OE2   
1855 N N     . TYR B 65  ? 0.25667 0.30765 0.20208 0.01818  -0.04815 -0.01848 64  TYR A N     
1856 C CA    . TYR B 65  ? 0.25311 0.29818 0.18554 0.02048  -0.04133 -0.01960 64  TYR A CA    
1857 C C     . TYR B 65  ? 0.26038 0.29858 0.20077 0.01513  -0.03976 -0.02899 64  TYR A C     
1858 O O     . TYR B 65  ? 0.20164 0.23373 0.15112 0.01253  -0.03275 -0.02582 64  TYR A O     
1859 C CB    . TYR B 65  ? 0.21339 0.25434 0.14481 0.02258  -0.03151 -0.00728 64  TYR A CB    
1860 C CG    . TYR B 65  ? 0.20192 0.24684 0.12449 0.02835  -0.03259 0.00265  64  TYR A CG    
1861 C CD1   . TYR B 65  ? 0.19798 0.24746 0.10006 0.03561  -0.03352 0.00409  64  TYR A CD1   
1862 C CD2   . TYR B 65  ? 0.20271 0.24584 0.13598 0.02759  -0.03260 0.01057  64  TYR A CD2   
1863 C CE1   . TYR B 65  ? 0.24542 0.29794 0.13829 0.04198  -0.03445 0.01441  64  TYR A CE1   
1864 C CE2   . TYR B 65  ? 0.17952 0.22425 0.10451 0.03385  -0.03336 0.02024  64  TYR A CE2   
1865 C CZ    . TYR B 65  ? 0.19954 0.24911 0.10463 0.04098  -0.03427 0.02268  64  TYR A CZ    
1866 O OH    . TYR B 65  ? 0.21282 0.26349 0.10853 0.04821  -0.03483 0.03344  64  TYR A OH    
1867 N N     . SER B 66  ? 0.21677 0.25548 0.15299 0.01389  -0.04682 -0.04074 65  SER A N     
1868 C CA    . SER B 66  ? 0.22754 0.25776 0.17281 0.00843  -0.04640 -0.04976 65  SER A CA    
1869 C C     . SER B 66  ? 0.18654 0.20820 0.12156 0.01216  -0.03843 -0.05230 65  SER A C     
1870 O O     . SER B 66  ? 0.25183 0.26513 0.19664 0.00909  -0.03419 -0.05441 65  SER A O     
1871 C CB    . SER B 66  ? 0.24386 0.27629 0.19018 0.00469  -0.05732 -0.06196 65  SER A CB    
1872 O OG    . SER B 66  ? 0.37076 0.40606 0.29559 0.01070  -0.06208 -0.06832 65  SER A OG    
1873 N N     . ALA B 67  ? 0.20414 0.22833 0.11956 0.01966  -0.03571 -0.05145 66  ALA A N     
1874 C CA    . ALA B 67  ? 0.23125 0.24949 0.13786 0.02445  -0.02681 -0.05307 66  ALA A CA    
1875 C C     . ALA B 67  ? 0.23243 0.25058 0.15148 0.02357  -0.01689 -0.04196 66  ALA A C     
1876 O O     . ALA B 67  ? 0.23323 0.24592 0.15677 0.02435  -0.01082 -0.04384 66  ALA A O     
1877 C CB    . ALA B 67  ? 0.30675 0.32949 0.18865 0.03355  -0.02510 -0.05354 66  ALA A CB    
1878 N N     . MET B 68  ? 0.25110 0.27502 0.17620 0.02221  -0.01566 -0.03070 67  MET A N     
1879 C CA    . MET B 68  ? 0.18428 0.20798 0.12294 0.01985  -0.00834 -0.02149 67  MET A CA    
1880 C C     . MET B 68  ? 0.15750 0.17594 0.11342 0.01379  -0.01054 -0.02421 67  MET A C     
1881 O O     . MET B 68  ? 0.15947 0.17531 0.12366 0.01326  -0.00537 -0.02299 67  MET A O     
1882 C CB    . MET B 68  ? 0.15851 0.18671 0.09850 0.01960  -0.00726 -0.00992 67  MET A CB    
1883 C CG    . MET B 68  ? 0.22115 0.25401 0.14621 0.02574  -0.00114 -0.00297 67  MET A CG    
1884 S SD    . MET B 68  ? 0.35893 0.39418 0.28908 0.02708  0.01138  0.00264  67  MET A SD    
1885 C CE    . MET B 68  ? 0.31258 0.34620 0.26568 0.01909  0.01230  0.01062  67  MET A CE    
1886 N N     . ARG B 69  ? 0.14254 0.16076 0.10441 0.00977  -0.01793 -0.02699 68  ARG A N     
1887 C CA    . ARG B 69  ? 0.14857 0.16204 0.12528 0.00451  -0.01946 -0.02925 68  ARG A CA    
1888 C C     . ARG B 69  ? 0.13711 0.14250 0.11412 0.00474  -0.01723 -0.03664 68  ARG A C     
1889 O O     . ARG B 69  ? 0.14536 0.14633 0.13188 0.00354  -0.01348 -0.03456 68  ARG A O     
1890 C CB    . ARG B 69  ? 0.15733 0.17394 0.13951 0.00083  -0.02734 -0.03224 68  ARG A CB    
1891 C CG    . ARG B 69  ? 0.22742 0.23965 0.22436 -0.00467 -0.02834 -0.03474 68  ARG A CG    
1892 C CD    . ARG B 69  ? 0.25140 0.26767 0.25375 -0.00878 -0.03622 -0.04089 68  ARG A CD    
1893 N NE    . ARG B 69  ? 0.25749 0.27015 0.25091 -0.00882 -0.04037 -0.05142 68  ARG A NE    
1894 C CZ    . ARG B 69  ? 0.33605 0.35270 0.33227 -0.01260 -0.04886 -0.05903 68  ARG A CZ    
1895 N NH1   . ARG B 69  ? 0.30573 0.33227 0.31516 -0.01642 -0.05357 -0.05638 68  ARG A NH1   
1896 N NH2   . ARG B 69  ? 0.35893 0.37019 0.34474 -0.01226 -0.05299 -0.07005 68  ARG A NH2   
1897 N N     . ASP B 70  ? 0.15408 0.15670 0.11951 0.00707  -0.01985 -0.04562 69  ASP A N     
1898 C CA    . ASP B 70  ? 0.16996 0.16190 0.13427 0.00807  -0.01792 -0.05386 69  ASP A CA    
1899 C C     . ASP B 70  ? 0.16265 0.15361 0.12627 0.01352  -0.00877 -0.04940 69  ASP A C     
1900 O O     . ASP B 70  ? 0.16161 0.14473 0.13248 0.01378  -0.00566 -0.05071 69  ASP A O     
1901 C CB    . ASP B 70  ? 0.18681 0.17530 0.13571 0.01058  -0.02279 -0.06548 69  ASP A CB    
1902 C CG    . ASP B 70  ? 0.24358 0.23084 0.19834 0.00356  -0.03294 -0.07315 69  ASP A CG    
1903 O OD1   . ASP B 70  ? 0.18282 0.17225 0.15409 -0.00276 -0.03473 -0.06857 69  ASP A OD1   
1904 O OD2   . ASP B 70  ? 0.26850 0.25343 0.21142 0.00453  -0.03915 -0.08402 69  ASP A OD2   
1905 N N     . GLN B 71  ? 0.16331 0.16298 0.11946 0.01807  -0.00412 -0.04320 70  GLN A N     
1906 C CA    . GLN B 71  ? 0.17237 0.17437 0.13107 0.02286  0.00466  -0.03857 70  GLN A CA    
1907 C C     . GLN B 71  ? 0.14277 0.14695 0.11881 0.01892  0.00609  -0.03080 70  GLN A C     
1908 O O     . GLN B 71  ? 0.15263 0.15577 0.13542 0.02165  0.01057  -0.02977 70  GLN A O     
1909 C CB    . GLN B 71  ? 0.23001 0.24180 0.17821 0.02810  0.01042  -0.03289 70  GLN A CB    
1910 C CG    . GLN B 71  ? 0.23824 0.25547 0.19165 0.03320  0.02020  -0.02806 70  GLN A CG    
1911 C CD    . GLN B 71  ? 0.26318 0.27233 0.21230 0.03950  0.02320  -0.03697 70  GLN A CD    
1912 O OE1   . GLN B 71  ? 0.26730 0.26951 0.20036 0.04383  0.02177  -0.04652 70  GLN A OE1   
1913 N NE2   . GLN B 71  ? 0.26713 0.27643 0.23011 0.04057  0.02682  -0.03427 70  GLN A NE2   
1914 N N     . TYR B 72  ? 0.13044 0.13757 0.11306 0.01340  0.00192  -0.02576 71  TYR A N     
1915 C CA    . TYR B 72  ? 0.14990 0.15742 0.14645 0.00994  0.00193  -0.02035 71  TYR A CA    
1916 C C     . TYR B 72  ? 0.13999 0.13875 0.14229 0.00958  0.00117  -0.02469 71  TYR A C     
1917 O O     . TYR B 72  ? 0.13614 0.13501 0.14612 0.01106  0.00384  -0.02150 71  TYR A O     
1918 C CB    . TYR B 72  ? 0.15308 0.16224 0.15343 0.00516  -0.00278 -0.01657 71  TYR A CB    
1919 C CG    . TYR B 72  ? 0.11186 0.12705 0.10796 0.00527  -0.00215 -0.01050 71  TYR A CG    
1920 C CD1   . TYR B 72  ? 0.12029 0.14100 0.11491 0.00762  0.00371  -0.00541 71  TYR A CD1   
1921 C CD2   . TYR B 72  ? 0.10774 0.12324 0.10268 0.00326  -0.00679 -0.00881 71  TYR A CD2   
1922 C CE1   . TYR B 72  ? 0.12746 0.15188 0.11882 0.00727  0.00516  0.00166  71  TYR A CE1   
1923 C CE2   . TYR B 72  ? 0.14634 0.16501 0.13708 0.00407  -0.00589 -0.00228 71  TYR A CE2   
1924 C CZ    . TYR B 72  ? 0.18113 0.20326 0.16982 0.00571  0.00018  0.00319  71  TYR A CZ    
1925 O OH    . TYR B 72  ? 0.14240 0.16586 0.12729 0.00614  0.00182  0.01104  71  TYR A OH    
1926 N N     . MET B 73  ? 0.12274 0.11404 0.12206 0.00746  -0.00276 -0.03154 72  MET A N     
1927 C CA    . MET B 73  ? 0.14006 0.12118 0.14592 0.00604  -0.00300 -0.03439 72  MET A CA    
1928 C C     . MET B 73  ? 0.18938 0.16295 0.19199 0.01198  0.00163  -0.03826 72  MET A C     
1929 O O     . MET B 73  ? 0.17886 0.14536 0.18806 0.01323  0.00376  -0.03662 72  MET A O     
1930 C CB    . MET B 73  ? 0.13449 0.11090 0.14119 0.00048  -0.00872 -0.04020 72  MET A CB    
1931 C CG    . MET B 73  ? 0.12165 0.10642 0.13396 -0.00394 -0.01240 -0.03525 72  MET A CG    
1932 S SD    . MET B 73  ? 0.19241 0.17714 0.20929 -0.01046 -0.01955 -0.04144 72  MET A SD    
1933 C CE    . MET B 73  ? 0.16606 0.16204 0.19039 -0.01242 -0.02128 -0.03321 72  MET A CE    
1934 N N     . ARG B 74  ? 0.19258 0.16750 0.18424 0.01697  0.00386  -0.04275 73  ARG A N     
1935 C CA    . ARG B 74  ? 0.20798 0.17559 0.19615 0.02428  0.00910  -0.04668 73  ARG A CA    
1936 C C     . ARG B 74  ? 0.22766 0.20346 0.22462 0.02891  0.01462  -0.03831 73  ARG A C     
1937 O O     . ARG B 74  ? 0.25796 0.22674 0.25893 0.03373  0.01769  -0.03855 73  ARG A O     
1938 C CB    . ARG B 74  ? 0.21847 0.18641 0.19082 0.02994  0.01097  -0.05373 73  ARG A CB    
1939 C CG    . ARG B 74  ? 0.29435 0.24723 0.25749 0.02885  0.00631  -0.06639 73  ARG A CG    
1940 C CD    . ARG B 74  ? 0.34595 0.29746 0.29017 0.03664  0.00849  -0.07481 73  ARG A CD    
1941 N NE    . ARG B 74  ? 0.28564 0.25240 0.22078 0.03780  0.00868  -0.07030 73  ARG A NE    
1942 C CZ    . ARG B 74  ? 0.28486 0.25441 0.21070 0.03433  0.00148  -0.07428 73  ARG A CZ    
1943 N NH1   . ARG B 74  ? 0.30305 0.26321 0.22934 0.02824  -0.00738 -0.08365 73  ARG A NH1   
1944 N NH2   . ARG B 74  ? 0.28148 0.26417 0.19840 0.03701  0.00315  -0.06811 73  ARG A NH2   
1945 N N     . THR B 75  ? 0.13938 0.12982 0.14039 0.02735  0.01540  -0.03074 74  THR A N     
1946 C CA    . THR B 75  ? 0.14641 0.14791 0.15751 0.03066  0.01950  -0.02332 74  THR A CA    
1947 C C     . THR B 75  ? 0.17216 0.17346 0.19447 0.02725  0.01601  -0.01837 74  THR A C     
1948 O O     . THR B 75  ? 0.13625 0.14288 0.16684 0.03138  0.01797  -0.01436 74  THR A O     
1949 C CB    . THR B 75  ? 0.18378 0.19975 0.19529 0.02917  0.02172  -0.01764 74  THR A CB    
1950 O OG1   . THR B 75  ? 0.30418 0.32112 0.30305 0.03416  0.02616  -0.02130 74  THR A OG1   
1951 C CG2   . THR B 75  ? 0.22545 0.25487 0.25067 0.03070  0.02499  -0.01025 74  THR A CG2   
1952 N N     . GLY B 76  ? 0.12438 0.12063 0.14661 0.02071  0.01089  -0.01854 75  GLY A N     
1953 C CA    . GLY B 76  ? 0.10292 0.09972 0.13295 0.01827  0.00806  -0.01370 75  GLY A CA    
1954 C C     . GLY B 76  ? 0.12973 0.11694 0.16206 0.02244  0.00940  -0.01379 75  GLY A C     
1955 O O     . GLY B 76  ? 0.14186 0.11652 0.17013 0.02348  0.01064  -0.01876 75  GLY A O     
1956 N N     . GLU B 77  ? 0.12187 0.11436 0.16055 0.02493  0.00874  -0.00823 76  GLU A N     
1957 C CA    . GLU B 77  ? 0.12465 0.10815 0.16476 0.02962  0.00984  -0.00605 76  GLU A CA    
1958 C C     . GLU B 77  ? 0.15803 0.13528 0.19766 0.02560  0.00737  -0.00315 76  GLU A C     
1959 O O     . GLU B 77  ? 0.13078 0.09619 0.16991 0.02787  0.00939  -0.00151 76  GLU A O     
1960 C CB    . GLU B 77  ? 0.15079 0.14513 0.19725 0.03647  0.01012  -0.00107 76  GLU A CB    
1961 C CG    . GLU B 77  ? 0.19592 0.19854 0.24531 0.04215  0.01417  -0.00247 76  GLU A CG    
1962 C CD    . GLU B 77  ? 0.25013 0.26768 0.30935 0.04814  0.01337  0.00298  76  GLU A CD    
1963 O OE1   . GLU B 77  ? 0.25424 0.26704 0.31449 0.05557  0.01387  0.00584  76  GLU A OE1   
1964 O OE2   . GLU B 77  ? 0.17621 0.21035 0.24285 0.04522  0.01193  0.00479  76  GLU A OE2   
1965 N N     . GLY B 78  ? 0.12387 0.10844 0.16367 0.02047  0.00382  -0.00180 77  GLY A N     
1966 C CA    . GLY B 78  ? 0.10071 0.08119 0.13933 0.01770  0.00241  0.00106  77  GLY A CA    
1967 C C     . GLY B 78  ? 0.11946 0.10445 0.15708 0.01148  -0.00028 -0.00087 77  GLY A C     
1968 O O     . GLY B 78  ? 0.10341 0.09595 0.14124 0.00994  -0.00182 -0.00238 77  GLY A O     
1969 N N     . PHE B 79  ? 0.09691 0.07757 0.13416 0.00838  -0.00022 0.00007  78  PHE A N     
1970 C CA    . PHE B 79  ? 0.12713 0.11182 0.16409 0.00367  -0.00249 -0.00162 78  PHE A CA    
1971 C C     . PHE B 79  ? 0.13831 0.12397 0.17437 0.00379  -0.00276 0.00203  78  PHE A C     
1972 O O     . PHE B 79  ? 0.08596 0.06678 0.12292 0.00471  0.00022  0.00521  78  PHE A O     
1973 C CB    . PHE B 79  ? 0.08952 0.07028 0.12831 -0.00048 -0.00224 -0.00585 78  PHE A CB    
1974 C CG    . PHE B 79  ? 0.17741 0.15628 0.21385 0.00038  -0.00198 -0.01070 78  PHE A CG    
1975 C CD1   . PHE B 79  ? 0.15148 0.12149 0.18817 0.00315  0.00085  -0.01223 78  PHE A CD1   
1976 C CD2   . PHE B 79  ? 0.11876 0.10390 0.15146 -0.00045 -0.00389 -0.01334 78  PHE A CD2   
1977 C CE1   . PHE B 79  ? 0.16090 0.12864 0.19369 0.00544  0.00172  -0.01748 78  PHE A CE1   
1978 C CE2   . PHE B 79  ? 0.12031 0.10421 0.14860 0.00162  -0.00274 -0.01768 78  PHE A CE2   
1979 C CZ    . PHE B 79  ? 0.17078 0.14627 0.19888 0.00482  0.00008  -0.02026 78  PHE A CZ    
1980 N N     . LEU B 80  ? 0.13773 0.12866 0.17160 0.00320  -0.00564 0.00181  79  LEU A N     
1981 C CA    . LEU B 80  ? 0.10949 0.10096 0.14116 0.00387  -0.00562 0.00377  79  LEU A CA    
1982 C C     . LEU B 80  ? 0.10163 0.09497 0.13693 0.00043  -0.00544 0.00239  79  LEU A C     
1983 O O     . LEU B 80  ? 0.11839 0.11444 0.15359 -0.00141 -0.00799 0.00003  79  LEU A O     
1984 C CB    . LEU B 80  ? 0.09577 0.08964 0.12288 0.00543  -0.00928 0.00316  79  LEU A CB    
1985 C CG    . LEU B 80  ? 0.15662 0.15150 0.18026 0.00889  -0.01171 0.00388  79  LEU A CG    
1986 C CD1   . LEU B 80  ? 0.13724 0.13261 0.15700 0.00870  -0.01610 0.00153  79  LEU A CD1   
1987 C CD2   . LEU B 80  ? 0.20525 0.19746 0.22452 0.01372  -0.00899 0.00768  79  LEU A CD2   
1988 N N     . LEU B 81  ? 0.10855 0.10145 0.14784 -0.00027 -0.00228 0.00459  80  LEU A N     
1989 C CA    . LEU B 81  ? 0.10788 0.10566 0.15343 -0.00330 -0.00249 0.00378  80  LEU A CA    
1990 C C     . LEU B 81  ? 0.08185 0.08323 0.12479 0.00036  -0.00155 0.00625  80  LEU A C     
1991 O O     . LEU B 81  ? 0.10351 0.10472 0.14607 0.00300  0.00275  0.01014  80  LEU A O     
1992 C CB    . LEU B 81  ? 0.12773 0.12424 0.18244 -0.00709 0.00069  0.00490  80  LEU A CB    
1993 C CG    . LEU B 81  ? 0.15372 0.14217 0.21016 -0.00955 0.00124  0.00266  80  LEU A CG    
1994 C CD1   . LEU B 81  ? 0.09895 0.08497 0.16696 -0.01513 0.00386  0.00325  80  LEU A CD1   
1995 C CD2   . LEU B 81  ? 0.13905 0.12756 0.19184 -0.01059 -0.00321 -0.00349 80  LEU A CD2   
1996 N N     . VAL B 82  ? 0.07094 0.07451 0.11098 0.00138  -0.00493 0.00436  81  VAL A N     
1997 C CA    . VAL B 82  ? 0.10591 0.10983 0.14136 0.00609  -0.00435 0.00549  81  VAL A CA    
1998 C C     . VAL B 82  ? 0.07390 0.08547 0.11666 0.00658  -0.00345 0.00660  81  VAL A C     
1999 O O     . VAL B 82  ? 0.06963 0.08552 0.11722 0.00380  -0.00665 0.00508  81  VAL A O     
2000 C CB    . VAL B 82  ? 0.07446 0.07352 0.10264 0.00727  -0.00841 0.00312  81  VAL A CB    
2001 C CG1   . VAL B 82  ? 0.08800 0.08335 0.10903 0.01277  -0.00795 0.00285  81  VAL A CG1   
2002 C CG2   . VAL B 82  ? 0.08419 0.07981 0.10959 0.00549  -0.01020 0.00195  81  VAL A CG2   
2003 N N     . PHE B 83  ? 0.07666 0.09124 0.12003 0.01088  0.00098  0.00946  82  PHE A N     
2004 C CA    . PHE B 83  ? 0.10481 0.12777 0.15439 0.01397  0.00210  0.01086  82  PHE A CA    
2005 C C     . PHE B 83  ? 0.08509 0.10343 0.12438 0.02216  0.00435  0.01097  82  PHE A C     
2006 O O     . PHE B 83  ? 0.10637 0.11651 0.13455 0.02466  0.00503  0.00995  82  PHE A O     
2007 C CB    . PHE B 83  ? 0.07646 0.11065 0.14049 0.01153  0.00672  0.01458  82  PHE A CB    
2008 C CG    . PHE B 83  ? 0.11102 0.14458 0.17307 0.01476  0.01455  0.01925  82  PHE A CG    
2009 C CD1   . PHE B 83  ? 0.08532 0.11239 0.14532 0.01157  0.01680  0.02099  82  PHE A CD1   
2010 C CD2   . PHE B 83  ? 0.11090 0.15024 0.17223 0.02211  0.02029  0.02253  82  PHE A CD2   
2011 C CE1   . PHE B 83  ? 0.09300 0.11919 0.14949 0.01538  0.02438  0.02667  82  PHE A CE1   
2012 C CE2   . PHE B 83  ? 0.11053 0.14971 0.16784 0.02607  0.02843  0.02766  82  PHE A CE2   
2013 C CZ    . PHE B 83  ? 0.09932 0.13187 0.15390 0.02254  0.03041  0.03017  82  PHE A CZ    
2014 N N     . ALA B 84  ? 0.11304 0.13665 0.15556 0.02704  0.00499  0.01172  83  ALA A N     
2015 C CA    . ALA B 84  ? 0.11549 0.13377 0.14804 0.03611  0.00766  0.01103  83  ALA A CA    
2016 C C     . ALA B 84  ? 0.12433 0.15387 0.16329 0.04139  0.01565  0.01549  83  ALA A C     
2017 O O     . ALA B 84  ? 0.09626 0.14014 0.15133 0.03920  0.01731  0.01891  83  ALA A O     
2018 C CB    . ALA B 84  ? 0.13179 0.14576 0.16218 0.03993  0.00374  0.00923  83  ALA A CB    
2019 N N     . ILE B 85  ? 0.13941 0.16347 0.16589 0.04854  0.02056  0.01541  84  ILE A N     
2020 C CA    . ILE B 85  ? 0.11886 0.15424 0.15037 0.05415  0.03012  0.02094  84  ILE A CA    
2021 C C     . ILE B 85  ? 0.13232 0.17786 0.17251 0.06114  0.03283  0.02237  84  ILE A C     
2022 O O     . ILE B 85  ? 0.14379 0.20447 0.19568 0.06416  0.04084  0.02817  84  ILE A O     
2023 C CB    . ILE B 85  ? 0.14158 0.16867 0.15400 0.06197  0.03501  0.02053  84  ILE A CB    
2024 C CG1   . ILE B 85  ? 0.14666 0.15966 0.14106 0.07005  0.03106  0.01311  84  ILE A CG1   
2025 C CG2   . ILE B 85  ? 0.16531 0.18602 0.17163 0.05611  0.03304  0.02108  84  ILE A CG2   
2026 C CD1   . ILE B 85  ? 0.20542 0.21717 0.18505 0.08290  0.03882  0.01307  84  ILE A CD1   
2027 N N     . ASN B 86  ? 0.12271 0.16111 0.15904 0.06388  0.02673  0.01815  85  ASN A N     
2028 C CA    . ASN B 86  ? 0.13966 0.18719 0.18426 0.07173  0.02850  0.01992  85  ASN A CA    
2029 C C     . ASN B 86  ? 0.15090 0.20910 0.21180 0.06552  0.02203  0.02145  85  ASN A C     
2030 O O     . ASN B 86  ? 0.14753 0.20908 0.21197 0.07212  0.02022  0.02207  85  ASN A O     
2031 C CB    . ASN B 86  ? 0.18886 0.21898 0.21605 0.08185  0.02713  0.01475  85  ASN A CB    
2032 C CG    . ASN B 86  ? 0.20496 0.21853 0.22479 0.07629  0.01773  0.01018  85  ASN A CG    
2033 O OD1   . ASN B 86  ? 0.19289 0.20621 0.21614 0.06559  0.01277  0.01001  85  ASN A OD1   
2034 N ND2   . ASN B 86  ? 0.19417 0.19284 0.20367 0.08383  0.01597  0.00664  85  ASN A ND2   
2035 N N     . ASN B 87  ? 0.11102 0.17383 0.18047 0.05385  0.01822  0.02181  86  ASN A N     
2036 C CA    . ASN B 87  ? 0.09328 0.16512 0.17481 0.04764  0.01090  0.02182  86  ASN A CA    
2037 C C     . ASN B 87  ? 0.08491 0.17137 0.18384 0.03815  0.01195  0.02400  86  ASN A C     
2038 O O     . ASN B 87  ? 0.09112 0.17048 0.18748 0.02961  0.00998  0.02201  86  ASN A O     
2039 C CB    . ASN B 87  ? 0.11465 0.17089 0.18397 0.04295  0.00348  0.01774  86  ASN A CB    
2040 C CG    . ASN B 87  ? 0.08841 0.15314 0.16596 0.03810  -0.00391 0.01762  86  ASN A CG    
2041 O OD1   . ASN B 87  ? 0.11519 0.19758 0.20876 0.03529  -0.00515 0.01919  86  ASN A OD1   
2042 N ND2   . ASN B 87  ? 0.14640 0.19898 0.21290 0.03687  -0.00898 0.01571  86  ASN A ND2   
2043 N N     . THR B 88  ? 0.08984 0.19674 0.20782 0.03965  0.01503  0.02809  87  THR A N     
2044 C CA    . THR B 88  ? 0.07870 0.19917 0.21607 0.02955  0.01647  0.03029  87  THR A CA    
2045 C C     . THR B 88  ? 0.07417 0.19365 0.21536 0.01910  0.00650  0.02550  87  THR A C     
2046 O O     . THR B 88  ? 0.10500 0.22101 0.25070 0.00952  0.00662  0.02437  87  THR A O     
2047 C CB    . THR B 88  ? 0.12920 0.27465 0.28960 0.03265  0.02080  0.03560  87  THR A CB    
2048 O OG1   . THR B 88  ? 0.10301 0.24785 0.25778 0.04175  0.03218  0.04007  87  THR A OG1   
2049 C CG2   . THR B 88  ? 0.18056 0.33852 0.36207 0.01959  0.01987  0.03627  87  THR A CG2   
2050 N N     . LYS B 89  ? 0.07904 0.20001 0.21664 0.02166  -0.00190 0.02270  88  LYS A N     
2051 C CA    . LYS B 89  ? 0.08414 0.20524 0.22308 0.01320  -0.01125 0.01781  88  LYS A CA    
2052 C C     . LYS B 89  ? 0.13665 0.23744 0.25971 0.00801  -0.01148 0.01412  88  LYS A C     
2053 O O     . LYS B 89  ? 0.13124 0.23081 0.25859 -0.00092 -0.01470 0.01051  88  LYS A O     
2054 C CB    . LYS B 89  ? 0.13808 0.26353 0.27225 0.01900  -0.01929 0.01689  88  LYS A CB    
2055 C CG    . LYS B 89  ? 0.18921 0.32040 0.32621 0.01174  -0.02939 0.01193  88  LYS A CG    
2056 C CD    . LYS B 89  ? 0.24724 0.36163 0.36251 0.01339  -0.03331 0.00946  88  LYS A CD    
2057 C CE    . LYS B 89  ? 0.26307 0.38077 0.37701 0.00667  -0.04219 0.00361  88  LYS A CE    
2058 N NZ    . LYS B 89  ? 0.23693 0.33780 0.32949 0.00802  -0.04335 0.00213  88  LYS A NZ    
2059 N N     . SER B 90  ? 0.07459 0.15948 0.18010 0.01363  -0.00824 0.01458  89  SER A N     
2060 C CA    . SER B 90  ? 0.10763 0.17605 0.20013 0.00944  -0.00849 0.01165  89  SER A CA    
2061 C C     . SER B 90  ? 0.15555 0.22225 0.25406 0.00362  -0.00337 0.01260  89  SER A C     
2062 O O     . SER B 90  ? 0.12542 0.18373 0.22040 -0.00218 -0.00517 0.00965  89  SER A O     
2063 C CB    . SER B 90  ? 0.10464 0.15853 0.18029 0.01595  -0.00648 0.01187  89  SER A CB    
2064 O OG    . SER B 90  ? 0.08677 0.13810 0.15999 0.02015  0.00062  0.01428  89  SER A OG    
2065 N N     . PHE B 91  ? 0.10568 0.17989 0.21304 0.00581  0.00380  0.01739  90  PHE A N     
2066 C CA    . PHE B 91  ? 0.13066 0.20352 0.24532 0.00007  0.00946  0.02008  90  PHE A CA    
2067 C C     . PHE B 91  ? 0.11333 0.19461 0.24595 -0.01007 0.00546  0.01792  90  PHE A C     
2068 O O     . PHE B 91  ? 0.07945 0.15198 0.21350 -0.01685 0.00608  0.01671  90  PHE A O     
2069 C CB    . PHE B 91  ? 0.08831 0.16800 0.20756 0.00544  0.01943  0.02701  90  PHE A CB    
2070 C CG    . PHE B 91  ? 0.14619 0.22357 0.27226 0.00022  0.02667  0.03192  90  PHE A CG    
2071 C CD1   . PHE B 91  ? 0.15838 0.21987 0.26903 0.00147  0.02921  0.03266  90  PHE A CD1   
2072 C CD2   . PHE B 91  ? 0.12409 0.21546 0.27316 -0.00605 0.03083  0.03641  90  PHE A CD2   
2073 C CE1   . PHE B 91  ? 0.14539 0.20328 0.26143 -0.00231 0.03641  0.03859  90  PHE A CE1   
2074 C CE2   . PHE B 91  ? 0.11973 0.20691 0.27576 -0.01132 0.03841  0.04220  90  PHE A CE2   
2075 C CZ    . PHE B 91  ? 0.14000 0.20961 0.27843 -0.00883 0.04147  0.04367  90  PHE A CZ    
2076 N N     . GLU B 92  ? 0.08799 0.18577 0.23423 -0.01086 0.00065  0.01692  91  GLU A N     
2077 C CA    . GLU B 92  ? 0.10921 0.21627 0.27286 -0.02091 -0.00537 0.01313  91  GLU A CA    
2078 C C     . GLU B 92  ? 0.12723 0.22271 0.27932 -0.02508 -0.01388 0.00506  91  GLU A C     
2079 O O     . GLU B 92  ? 0.21250 0.30878 0.37452 -0.03407 -0.01840 0.00019  91  GLU A O     
2080 C CB    . GLU B 92  ? 0.10064 0.23056 0.28092 -0.01934 -0.00990 0.01381  91  GLU A CB    
2081 C CG    . GLU B 92  ? 0.10875 0.25206 0.30256 -0.01608 -0.00057 0.02136  91  GLU A CG    
2082 C CD    . GLU B 92  ? 0.22197 0.38483 0.42446 -0.01113 -0.00436 0.02142  91  GLU A CD    
2083 O OE1   . GLU B 92  ? 0.20892 0.37451 0.40513 -0.00726 -0.01342 0.01759  91  GLU A OE1   
2084 O OE2   . GLU B 92  ? 0.16385 0.33918 0.37905 -0.01052 0.00210  0.02577  91  GLU A OE2   
2085 N N     . ASP B 93  ? 0.11221 0.19672 0.24392 -0.01883 -0.01579 0.00340  92  ASP A N     
2086 C CA    . ASP B 93  ? 0.11220 0.18630 0.23163 -0.02135 -0.02193 -0.00315 92  ASP A CA    
2087 C C     . ASP B 93  ? 0.16256 0.22008 0.27517 -0.02466 -0.01780 -0.00433 92  ASP A C     
2088 O O     . ASP B 93  ? 0.13337 0.18285 0.23829 -0.02718 -0.02191 -0.01016 92  ASP A O     
2089 C CB    . ASP B 93  ? 0.14610 0.21571 0.24828 -0.01374 -0.02448 -0.00301 92  ASP A CB    
2090 C CG    . ASP B 93  ? 0.21123 0.29454 0.31641 -0.00994 -0.03080 -0.00293 92  ASP A CG    
2091 O OD1   . ASP B 93  ? 0.16240 0.26090 0.28363 -0.01336 -0.03450 -0.00397 92  ASP A OD1   
2092 O OD2   . ASP B 93  ? 0.24148 0.32047 0.33369 -0.00349 -0.03210 -0.00133 92  ASP A OD2   
2093 N N     . ILE B 94  ? 0.10556 0.15799 0.21937 -0.02334 -0.00960 0.00134  93  ILE A N     
2094 C CA    . ILE B 94  ? 0.12003 0.15678 0.22496 -0.02388 -0.00580 0.00151  93  ILE A CA    
2095 C C     . ILE B 94  ? 0.14326 0.17342 0.25498 -0.03185 -0.00800 -0.00348 93  ILE A C     
2096 O O     . ILE B 94  ? 0.08775 0.10605 0.18907 -0.03154 -0.00941 -0.00753 93  ILE A O     
2097 C CB    . ILE B 94  ? 0.11351 0.14769 0.21826 -0.02028 0.00311  0.00924  93  ILE A CB    
2098 C CG1   . ILE B 94  ? 0.07440 0.10902 0.16625 -0.01148 0.00409  0.01139  93  ILE A CG1   
2099 C CG2   . ILE B 94  ? 0.10089 0.12046 0.20020 -0.02134 0.00693  0.01053  93  ILE A CG2   
2100 C CD1   . ILE B 94  ? 0.09610 0.12074 0.17235 -0.00882 0.00005  0.00760  93  ILE A CD1   
2101 N N     . HIS B 95  ? 0.10318 0.14075 0.23324 -0.03910 -0.00825 -0.00356 94  HIS A N     
2102 C CA    . HIS B 95  ? 0.15081 0.17876 0.28799 -0.04743 -0.01009 -0.00884 94  HIS A CA    
2103 C C     . HIS B 95  ? 0.16879 0.19309 0.29642 -0.04841 -0.01925 -0.01942 94  HIS A C     
2104 O O     . HIS B 95  ? 0.12257 0.13224 0.24554 -0.05103 -0.01981 -0.02472 94  HIS A O     
2105 C CB    . HIS B 95  ? 0.12847 0.16523 0.28422 -0.05489 -0.00904 -0.00695 94  HIS A CB    
2106 C CG    . HIS B 95  ? 0.16070 0.21519 0.32309 -0.05675 -0.01696 -0.01111 94  HIS A CG    
2107 N ND1   . HIS B 95  ? 0.20748 0.26222 0.37075 -0.06299 -0.02493 -0.01946 94  HIS A ND1   
2108 C CD2   . HIS B 95  ? 0.19701 0.26992 0.36541 -0.05250 -0.01806 -0.00765 94  HIS A CD2   
2109 C CE1   . HIS B 95  ? 0.15824 0.23178 0.32768 -0.06274 -0.03103 -0.02071 94  HIS A CE1   
2110 N NE2   . HIS B 95  ? 0.15558 0.24034 0.32856 -0.05611 -0.02681 -0.01346 94  HIS A NE2   
2111 N N     . HIS B 96  ? 0.11595 0.15234 0.23848 -0.04494 -0.02576 -0.02207 95  HIS A N     
2112 C CA    . HIS B 96  ? 0.12930 0.16287 0.23921 -0.04409 -0.03359 -0.03100 95  HIS A CA    
2113 C C     . HIS B 96  ? 0.14931 0.16889 0.24033 -0.03802 -0.03003 -0.03110 95  HIS A C     
2114 O O     . HIS B 96  ? 0.11959 0.13051 0.20132 -0.03827 -0.03293 -0.03846 95  HIS A O     
2115 C CB    . HIS B 96  ? 0.13376 0.18338 0.24114 -0.04021 -0.04036 -0.03144 95  HIS A CB    
2116 C CG    . HIS B 96  ? 0.14103 0.20611 0.26383 -0.04517 -0.04541 -0.03250 95  HIS A CG    
2117 N ND1   . HIS B 96  ? 0.25875 0.34150 0.38812 -0.04119 -0.04769 -0.02798 95  HIS A ND1   
2118 C CD2   . HIS B 96  ? 0.20461 0.26944 0.33482 -0.05291 -0.04791 -0.03670 95  HIS A CD2   
2119 C CE1   . HIS B 96  ? 0.16400 0.25856 0.30516 -0.04639 -0.05125 -0.02914 95  HIS A CE1   
2120 N NE2   . HIS B 96  ? 0.24706 0.33104 0.38920 -0.05418 -0.05179 -0.03459 95  HIS A NE2   
2121 N N     . TYR B 97  ? 0.10781 0.12594 0.19309 -0.03221 -0.02402 -0.02349 96  TYR A N     
2122 C CA    . TYR B 97  ? 0.09398 0.10149 0.16509 -0.02723 -0.02091 -0.02314 96  TYR A CA    
2123 C C     . TYR B 97  ? 0.15997 0.15348 0.23244 -0.02933 -0.01705 -0.02473 96  TYR A C     
2124 O O     . TYR B 97  ? 0.12634 0.11140 0.18955 -0.02725 -0.01744 -0.02949 96  TYR A O     
2125 C CB    . TYR B 97  ? 0.11209 0.12129 0.17852 -0.02162 -0.01666 -0.01566 96  TYR A CB    
2126 C CG    . TYR B 97  ? 0.10271 0.12092 0.16428 -0.01810 -0.02008 -0.01440 96  TYR A CG    
2127 C CD1   . TYR B 97  ? 0.13294 0.14964 0.18282 -0.01494 -0.02195 -0.01582 96  TYR A CD1   
2128 C CD2   . TYR B 97  ? 0.11940 0.14760 0.18872 -0.01745 -0.02073 -0.01109 96  TYR A CD2   
2129 C CE1   . TYR B 97  ? 0.10392 0.12671 0.14922 -0.01160 -0.02445 -0.01343 96  TYR A CE1   
2130 C CE2   . TYR B 97  ? 0.11266 0.14717 0.17731 -0.01317 -0.02363 -0.00941 96  TYR A CE2   
2131 C CZ    . TYR B 97  ? 0.14338 0.17406 0.19564 -0.01048 -0.02555 -0.01039 96  TYR A CZ    
2132 O OH    . TYR B 97  ? 0.17494 0.20992 0.22249 -0.00614 -0.02786 -0.00756 96  TYR A OH    
2133 N N     . ARG B 98  ? 0.10393 0.09454 0.18773 -0.03265 -0.01252 -0.02010 97  ARG A N     
2134 C CA    . ARG B 98  ? 0.11451 0.08986 0.19984 -0.03413 -0.00835 -0.02030 97  ARG A CA    
2135 C C     . ARG B 98  ? 0.15480 0.12231 0.24208 -0.03951 -0.01317 -0.03042 97  ARG A C     
2136 O O     . ARG B 98  ? 0.14300 0.09637 0.22331 -0.03729 -0.01163 -0.03414 97  ARG A O     
2137 C CB    . ARG B 98  ? 0.16511 0.13887 0.26261 -0.03705 -0.00195 -0.01219 97  ARG A CB    
2138 C CG    . ARG B 98  ? 0.13119 0.08693 0.23060 -0.03833 0.00291  -0.01098 97  ARG A CG    
2139 C CD    . ARG B 98  ? 0.25367 0.20703 0.36130 -0.03887 0.01114  -0.00009 97  ARG A CD    
2140 N NE    . ARG B 98  ? 0.27343 0.20943 0.38393 -0.04113 0.01518  0.00116  97  ARG A NE    
2141 C CZ    . ARG B 98  ? 0.33001 0.25184 0.43105 -0.03460 0.01877  0.00373  97  ARG A CZ    
2142 N NH1   . ARG B 98  ? 0.38989 0.31504 0.47808 -0.02559 0.01861  0.00558  97  ARG A NH1   
2143 N NH2   . ARG B 98  ? 0.31637 0.22364 0.41761 -0.03580 0.02148  0.00443  97  ARG A NH2   
2144 N N     . GLU B 99  ? 0.15465 0.13136 0.25139 -0.04610 -0.01943 -0.03550 98  GLU A N     
2145 C CA    . GLU B 99  ? 0.17046 0.14009 0.26497 -0.05053 -0.02472 -0.04524 98  GLU A CA    
2146 C C     . GLU B 99  ? 0.18429 0.14990 0.26216 -0.04532 -0.02910 -0.05415 98  GLU A C     
2147 O O     . GLU B 99  ? 0.19136 0.14350 0.26143 -0.04516 -0.02976 -0.06120 98  GLU A O     
2148 C CB    . GLU B 99  ? 0.17216 0.15596 0.27628 -0.05691 -0.03092 -0.04727 98  GLU A CB    
2149 C CG    . GLU B 99  ? 0.24618 0.23414 0.36777 -0.06293 -0.02635 -0.03974 98  GLU A CG    
2150 C CD    . GLU B 99  ? 0.29046 0.29946 0.42343 -0.06654 -0.03146 -0.03899 98  GLU A CD    
2151 O OE1   . GLU B 99  ? 0.25255 0.27219 0.37879 -0.06385 -0.03897 -0.04387 98  GLU A OE1   
2152 O OE2   . GLU B 99  ? 0.28714 0.30251 0.43565 -0.07145 -0.02759 -0.03295 98  GLU A OE2   
2153 N N     . GLN B 100 ? 0.14906 0.12634 0.21773 -0.03945 -0.03063 -0.05189 99  GLN A N     
2154 C CA    . GLN B 100 ? 0.17826 0.15385 0.22888 -0.03333 -0.03292 -0.05775 99  GLN A CA    
2155 C C     . GLN B 100 ? 0.17107 0.13473 0.21260 -0.02689 -0.02567 -0.05557 99  GLN A C     
2156 O O     . GLN B 100 ? 0.17904 0.13476 0.20904 -0.02320 -0.02594 -0.06278 99  GLN A O     
2157 C CB    . GLN B 100 ? 0.18300 0.17416 0.22661 -0.02900 -0.03565 -0.05375 99  GLN A CB    
2158 C CG    . GLN B 100 ? 0.26403 0.26810 0.31270 -0.03298 -0.04475 -0.05812 99  GLN A CG    
2159 C CD    . GLN B 100 ? 0.30135 0.30078 0.34355 -0.03559 -0.05238 -0.07122 99  GLN A CD    
2160 O OE1   . GLN B 100 ? 0.36611 0.35475 0.39350 -0.03130 -0.05074 -0.07683 99  GLN A OE1   
2161 N NE2   . GLN B 100 ? 0.47007 0.47769 0.52018 -0.04116 -0.05830 -0.07291 99  GLN A NE2   
2162 N N     . ILE B 101 ? 0.14803 0.11141 0.19413 -0.02462 -0.01938 -0.04591 100 ILE A N     
2163 C CA    . ILE B 101 ? 0.16531 0.11956 0.20553 -0.01837 -0.01326 -0.04320 100 ILE A CA    
2164 C C     . ILE B 101 ? 0.15553 0.09208 0.19756 -0.01951 -0.01145 -0.04871 100 ILE A C     
2165 O O     . ILE B 101 ? 0.18521 0.11326 0.21858 -0.01338 -0.00867 -0.05200 100 ILE A O     
2166 C CB    . ILE B 101 ? 0.12457 0.08245 0.16968 -0.01617 -0.00855 -0.03246 100 ILE A CB    
2167 C CG1   . ILE B 101 ? 0.11022 0.08215 0.15247 -0.01446 -0.01016 -0.02793 100 ILE A CG1   
2168 C CG2   . ILE B 101 ? 0.14626 0.09617 0.18728 -0.00960 -0.00337 -0.02964 100 ILE A CG2   
2169 C CD1   . ILE B 101 ? 0.11369 0.08856 0.16105 -0.01370 -0.00719 -0.01959 100 ILE A CD1   
2170 N N     . LYS B 102 ? 0.16316 0.09346 0.21752 -0.02714 -0.01229 -0.04924 101 LYS A N     
2171 C CA    . LYS B 102 ? 0.18214 0.09243 0.23938 -0.02933 -0.01066 -0.05462 101 LYS A CA    
2172 C C     . LYS B 102 ? 0.20000 0.10483 0.24623 -0.02942 -0.01615 -0.06727 101 LYS A C     
2173 O O     . LYS B 102 ? 0.21785 0.10683 0.25611 -0.02535 -0.01362 -0.07167 101 LYS A O     
2174 C CB    . LYS B 102 ? 0.20737 0.11605 0.27822 -0.03768 -0.00956 -0.04900 101 LYS A CB    
2175 C CG    . LYS B 102 ? 0.21666 0.12640 0.29540 -0.03597 -0.00231 -0.03610 101 LYS A CG    
2176 C CD    . LYS B 102 ? 0.22015 0.13325 0.31232 -0.04385 -0.00070 -0.03005 101 LYS A CD    
2177 C CE    . LYS B 102 ? 0.28786 0.18503 0.38211 -0.04838 0.00005  -0.03253 101 LYS A CE    
2178 N NZ    . LYS B 102 ? 0.27856 0.18273 0.38748 -0.05810 -0.00065 -0.02977 101 LYS A NZ    
2179 N N     . ARG B 103 ? 0.19779 0.11563 0.24187 -0.03302 -0.02361 -0.07265 102 ARG A N     
2180 C CA    . ARG B 103 ? 0.21727 0.13110 0.24805 -0.03235 -0.02917 -0.08419 102 ARG A CA    
2181 C C     . ARG B 103 ? 0.22042 0.13107 0.23447 -0.02161 -0.02636 -0.08883 102 ARG A C     
2182 O O     . ARG B 103 ? 0.24162 0.13920 0.24380 -0.01767 -0.02539 -0.09631 102 ARG A O     
2183 C CB    . ARG B 103 ? 0.22010 0.15094 0.25162 -0.03715 -0.03793 -0.08722 102 ARG A CB    
2184 C CG    . ARG B 103 ? 0.23712 0.16514 0.25335 -0.03634 -0.04449 -0.09890 102 ARG A CG    
2185 C CD    . ARG B 103 ? 0.23387 0.18097 0.24918 -0.03879 -0.05329 -0.10041 102 ARG A CD    
2186 N NE    . ARG B 103 ? 0.30088 0.26260 0.31143 -0.03240 -0.05275 -0.09500 102 ARG A NE    
2187 C CZ    . ARG B 103 ? 0.37424 0.33688 0.36663 -0.02328 -0.05133 -0.09755 102 ARG A CZ    
2188 N NH1   . ARG B 103 ? 0.30514 0.25565 0.28170 -0.01821 -0.04950 -0.10539 102 ARG A NH1   
2189 N NH2   . ARG B 103 ? 0.30716 0.28326 0.29650 -0.01861 -0.05010 -0.09001 102 ARG A NH2   
2190 N N     . VAL B 104 ? 0.20105 0.12549 0.21228 -0.01622 -0.02339 -0.08101 103 VAL A N     
2191 C CA    . VAL B 104 ? 0.20367 0.13118 0.19933 -0.00608 -0.01913 -0.08089 103 VAL A CA    
2192 C C     . VAL B 104 ? 0.20905 0.12350 0.20425 0.00057  -0.01117 -0.07909 103 VAL A C     
2193 O O     . VAL B 104 ? 0.27229 0.18038 0.25509 0.00832  -0.00826 -0.08524 103 VAL A O     
2194 C CB    . VAL B 104 ? 0.19646 0.14256 0.19178 -0.00388 -0.01764 -0.07030 103 VAL A CB    
2195 C CG1   . VAL B 104 ? 0.23229 0.18214 0.21820 0.00548  -0.01066 -0.06635 103 VAL A CG1   
2196 C CG2   . VAL B 104 ? 0.18723 0.14526 0.17752 -0.00666 -0.02506 -0.07314 103 VAL A CG2   
2197 N N     . LYS B 105 ? 0.19936 0.11020 0.20717 -0.00114 -0.00732 -0.07036 104 LYS A N     
2198 C CA    . LYS B 105 ? 0.22266 0.12203 0.23093 0.00602  -0.00034 -0.06730 104 LYS A CA    
2199 C C     . LYS B 105 ? 0.24199 0.11769 0.25209 0.00415  -0.00018 -0.07509 104 LYS A C     
2200 O O     . LYS B 105 ? 0.24570 0.10874 0.25518 0.01130  0.00565  -0.07333 104 LYS A O     
2201 C CB    . LYS B 105 ? 0.28189 0.18833 0.30044 0.00635  0.00324  -0.05403 104 LYS A CB    
2202 C CG    . LYS B 105 ? 0.26061 0.18804 0.27821 0.00683  0.00220  -0.04746 104 LYS A CG    
2203 C CD    . LYS B 105 ? 0.29058 0.22476 0.31448 0.01001  0.00560  -0.03644 104 LYS A CD    
2204 C CE    . LYS B 105 ? 0.23057 0.16490 0.25184 0.01982  0.01060  -0.03445 104 LYS A CE    
2205 N NZ    . LYS B 105 ? 0.20609 0.15510 0.22236 0.02358  0.01154  -0.03444 104 LYS A NZ    
2206 N N     . ASP B 106 ? 0.24044 0.11156 0.25199 -0.00517 -0.00655 -0.08189 105 ASP A N     
2207 C CA    . ASP B 106 ? 0.26619 0.11774 0.27641 -0.00902 -0.00702 -0.08573 105 ASP A CA    
2208 C C     . ASP B 106 ? 0.26790 0.10768 0.28751 -0.00807 -0.00092 -0.07549 105 ASP A C     
2209 O O     . ASP B 106 ? 0.28829 0.11004 0.30220 -0.00253 0.00268  -0.07637 105 ASP A O     
2210 C CB    . ASP B 106 ? 0.29096 0.13047 0.28344 -0.00166 -0.00628 -0.09646 105 ASP A CB    
2211 C CG    . ASP B 106 ? 0.32167 0.13921 0.31100 -0.00655 -0.00790 -0.10257 105 ASP A CG    
2212 O OD1   . ASP B 106 ? 0.32556 0.14313 0.32370 -0.01820 -0.01354 -0.10353 105 ASP A OD1   
2213 O OD2   . ASP B 106 ? 0.34369 0.14414 0.32179 0.00151  -0.00334 -0.10667 105 ASP A OD2   
2214 N N     . SER B 107 ? 0.24797 0.09830 0.28076 -0.01258 0.00028  -0.06518 106 SER A N     
2215 C CA    . SER B 107 ? 0.27412 0.11726 0.31405 -0.01026 0.00648  -0.05351 106 SER A CA    
2216 C C     . SER B 107 ? 0.23503 0.08764 0.28845 -0.01925 0.00626  -0.04513 106 SER A C     
2217 O O     . SER B 107 ? 0.24993 0.11939 0.30763 -0.02313 0.00297  -0.04522 106 SER A O     
2218 C CB    . SER B 107 ? 0.28911 0.13822 0.32638 0.00117  0.01183  -0.04682 106 SER A CB    
2219 O OG    . SER B 107 ? 0.33046 0.17084 0.37094 0.00523  0.01701  -0.03631 106 SER A OG    
2220 N N     . GLU B 108 ? 0.24641 0.08848 0.30611 -0.02166 0.01023  -0.03743 107 GLU A N     
2221 C CA    . GLU B 108 ? 0.30713 0.15900 0.37896 -0.02793 0.01239  -0.02760 107 GLU A CA    
2222 C C     . GLU B 108 ? 0.29013 0.14809 0.36149 -0.02018 0.01831  -0.01552 107 GLU A C     
2223 O O     . GLU B 108 ? 0.28059 0.14781 0.35945 -0.02339 0.02089  -0.00701 107 GLU A O     
2224 C CB    . GLU B 108 ? 0.33150 0.17077 0.41120 -0.03547 0.01409  -0.02490 107 GLU A CB    
2225 C CG    . GLU B 108 ? 0.34467 0.18007 0.42654 -0.04499 0.00710  -0.03657 107 GLU A CG    
2226 C CD    . GLU B 108 ? 0.37370 0.21307 0.47109 -0.05665 0.00702  -0.03268 107 GLU A CD    
2227 O OE1   . GLU B 108 ? 0.34513 0.16913 0.44719 -0.05981 0.01089  -0.02826 107 GLU A OE1   
2228 O OE2   . GLU B 108 ? 0.37443 0.23275 0.47989 -0.06239 0.00319  -0.03378 107 GLU A OE2   
2229 N N     . ASP B 109 ? 0.24281 0.09720 0.30509 -0.00944 0.02033  -0.01474 108 ASP A N     
2230 C CA    . ASP B 109 ? 0.23439 0.09360 0.29428 -0.00071 0.02491  -0.00353 108 ASP A CA    
2231 C C     . ASP B 109 ? 0.20996 0.08074 0.26486 0.00630  0.02304  -0.00640 108 ASP A C     
2232 O O     . ASP B 109 ? 0.29500 0.16232 0.34375 0.01508  0.02402  -0.00847 108 ASP A O     
2233 C CB    . ASP B 109 ? 0.31229 0.15638 0.36783 0.00643  0.02914  0.00200  108 ASP A CB    
2234 C CG    . ASP B 109 ? 0.36815 0.21887 0.41938 0.01660  0.03242  0.01315  108 ASP A CG    
2235 O OD1   . ASP B 109 ? 0.49293 0.35703 0.54543 0.01609  0.03253  0.01883  108 ASP A OD1   
2236 O OD2   . ASP B 109 ? 0.37985 0.22301 0.42591 0.02558  0.03421  0.01589  108 ASP A OD2   
2237 N N     . VAL B 110 ? 0.20204 0.09131 0.25728 0.00263  0.01943  -0.00604 109 VAL A N     
2238 C CA    . VAL B 110 ? 0.16351 0.06956 0.21199 0.00737  0.01614  -0.00756 109 VAL A CA    
2239 C C     . VAL B 110 ? 0.18209 0.10064 0.22989 0.00960  0.01630  0.00147  109 VAL A C     
2240 O O     . VAL B 110 ? 0.14420 0.06583 0.19611 0.00434  0.01673  0.00502  109 VAL A O     
2241 C CB    . VAL B 110 ? 0.15302 0.06841 0.20021 0.00159  0.01092  -0.01640 109 VAL A CB    
2242 C CG1   . VAL B 110 ? 0.13927 0.07026 0.18046 0.00627  0.00891  -0.01613 109 VAL A CG1   
2243 C CG2   . VAL B 110 ? 0.18286 0.08581 0.22803 -0.00014 0.00978  -0.02680 109 VAL A CG2   
2244 N N     . PRO B 111 ? 0.14253 0.06936 0.18563 0.01734  0.01573  0.00494  110 PRO A N     
2245 C CA    . PRO B 111 ? 0.13658 0.07452 0.17731 0.01956  0.01450  0.01176  110 PRO A CA    
2246 C C     . PRO B 111 ? 0.14044 0.08956 0.18164 0.01328  0.01098  0.00911  110 PRO A C     
2247 O O     . PRO B 111 ? 0.12104 0.07737 0.16173 0.01114  0.00771  0.00350  110 PRO A O     
2248 C CB    . PRO B 111 ? 0.16746 0.11401 0.20532 0.02749  0.01251  0.01274  110 PRO A CB    
2249 C CG    . PRO B 111 ? 0.18743 0.12314 0.22624 0.03235  0.01569  0.01073  110 PRO A CG    
2250 C CD    . PRO B 111 ? 0.16153 0.08659 0.20210 0.02534  0.01667  0.00328  110 PRO A CD    
2251 N N     . MET B 112 ? 0.18222 0.13265 0.22389 0.01137  0.01243  0.01402  111 MET A N     
2252 C CA    . MET B 112 ? 0.10867 0.06834 0.15129 0.00668  0.01006  0.01234  111 MET A CA    
2253 C C     . MET B 112 ? 0.10963 0.07260 0.14834 0.00980  0.01211  0.01908  111 MET A C     
2254 O O     . MET B 112 ? 0.15390 0.11048 0.19126 0.01314  0.01673  0.02578  111 MET A O     
2255 C CB    . MET B 112 ? 0.19629 0.15365 0.24707 -0.00106 0.01077  0.00920  111 MET A CB    
2256 C CG    . MET B 112 ? 0.21676 0.17197 0.26944 -0.00476 0.00767  0.00098  111 MET A CG    
2257 S SD    . MET B 112 ? 0.20934 0.16256 0.27372 -0.01403 0.00783  -0.00133 111 MET A SD    
2258 C CE    . MET B 112 ? 0.17358 0.11764 0.23634 -0.01618 0.00449  -0.01185 111 MET A CE    
2259 N N     . VAL B 113 ? 0.13004 0.10192 0.16607 0.00916  0.00917  0.01744  112 VAL A N     
2260 C CA    . VAL B 113 ? 0.12129 0.09655 0.15142 0.01289  0.01090  0.02208  112 VAL A CA    
2261 C C     . VAL B 113 ? 0.14128 0.12273 0.17518 0.00903  0.01044  0.01971  112 VAL A C     
2262 O O     . VAL B 113 ? 0.11176 0.09701 0.14732 0.00611  0.00595  0.01426  112 VAL A O     
2263 C CB    . VAL B 113 ? 0.11873 0.09779 0.13872 0.01891  0.00640  0.02163  112 VAL A CB    
2264 C CG1   . VAL B 113 ? 0.15098 0.13312 0.16237 0.02285  0.00712  0.02370  112 VAL A CG1   
2265 C CG2   . VAL B 113 ? 0.15399 0.12910 0.17079 0.02448  0.00701  0.02558  112 VAL A CG2   
2266 N N     . LEU B 114 ? 0.12360 0.10660 0.15935 0.00962  0.01572  0.02467  113 LEU A N     
2267 C CA    . LEU B 114 ? 0.09707 0.08772 0.13697 0.00791  0.01598  0.02345  113 LEU A CA    
2268 C C     . LEU B 114 ? 0.11309 0.10634 0.14089 0.01460  0.01466  0.02308  113 LEU A C     
2269 O O     . LEU B 114 ? 0.11811 0.10941 0.13632 0.02070  0.01776  0.02733  113 LEU A O     
2270 C CB    . LEU B 114 ? 0.10224 0.09528 0.15285 0.00511  0.02315  0.02925  113 LEU A CB    
2271 C CG    . LEU B 114 ? 0.09844 0.10225 0.15568 0.00461  0.02450  0.02932  113 LEU A CG    
2272 C CD1   . LEU B 114 ? 0.11879 0.12728 0.18507 -0.00146 0.01808  0.02262  113 LEU A CD1   
2273 C CD2   . LEU B 114 ? 0.12083 0.12884 0.18883 0.00312  0.03348  0.03733  113 LEU A CD2   
2274 N N     . VAL B 115 ? 0.09948 0.09604 0.12669 0.01391  0.01002  0.01796  114 VAL A N     
2275 C CA    . VAL B 115 ? 0.10907 0.10503 0.12489 0.01948  0.00752  0.01560  114 VAL A CA    
2276 C C     . VAL B 115 ? 0.13884 0.13987 0.15778 0.02116  0.00991  0.01565  114 VAL A C     
2277 O O     . VAL B 115 ? 0.08889 0.09360 0.11638 0.01728  0.00760  0.01354  114 VAL A O     
2278 C CB    . VAL B 115 ? 0.09180 0.08497 0.10442 0.01762  0.00007  0.00994  114 VAL A CB    
2279 C CG1   . VAL B 115 ? 0.09924 0.08923 0.10048 0.02250  -0.00320 0.00654  114 VAL A CG1   
2280 C CG2   . VAL B 115 ? 0.09723 0.08842 0.11017 0.01618  -0.00194 0.01013  114 VAL A CG2   
2281 N N     . GLY B 116 ? 0.10573 0.10756 0.11689 0.02804  0.01461  0.01825  115 GLY A N     
2282 C CA    . GLY B 116 ? 0.10835 0.11483 0.12041 0.03227  0.01732  0.01802  115 GLY A CA    
2283 C C     . GLY B 116 ? 0.12809 0.12709 0.12583 0.03788  0.01266  0.01207  115 GLY A C     
2284 O O     . GLY B 116 ? 0.15019 0.14475 0.13338 0.04456  0.01365  0.01121  115 GLY A O     
2285 N N     . ASN B 117 ? 0.11752 0.11422 0.11860 0.03535  0.00743  0.00788  116 ASN A N     
2286 C CA    . ASN B 117 ? 0.15196 0.13863 0.14189 0.03838  0.00208  0.00180  116 ASN A CA    
2287 C C     . ASN B 117 ? 0.12849 0.11355 0.11444 0.04612  0.00491  0.00053  116 ASN A C     
2288 O O     . ASN B 117 ? 0.14520 0.13978 0.13947 0.04896  0.01077  0.00482  116 ASN A O     
2289 C CB    . ASN B 117 ? 0.11478 0.09793 0.11037 0.03112  -0.00448 -0.00081 116 ASN A CB    
2290 C CG    . ASN B 117 ? 0.12734 0.09910 0.11374 0.03181  -0.01030 -0.00662 116 ASN A CG    
2291 O OD1   . ASN B 117 ? 0.15301 0.12031 0.12920 0.03435  -0.01251 -0.00987 116 ASN A OD1   
2292 N ND2   . ASN B 117 ? 0.12042 0.08698 0.11007 0.02988  -0.01298 -0.00789 116 ASN A ND2   
2293 N N     . LYS B 118 ? 0.14090 0.11363 0.11466 0.04972  0.00053  -0.00577 117 LYS A N     
2294 C CA    . LYS B 118 ? 0.15501 0.12137 0.12134 0.05859  0.00256  -0.00874 117 LYS A CA    
2295 C C     . LYS B 118 ? 0.17524 0.14504 0.13100 0.06874  0.00994  -0.00766 117 LYS A C     
2296 O O     . LYS B 118 ? 0.22511 0.19725 0.18037 0.07717  0.01565  -0.00668 117 LYS A O     
2297 C CB    . LYS B 118 ? 0.17924 0.15099 0.15835 0.05888  0.00425  -0.00530 117 LYS A CB    
2298 C CG    . LYS B 118 ? 0.15819 0.12721 0.14589 0.05006  -0.00201 -0.00508 117 LYS A CG    
2299 C CD    . LYS B 118 ? 0.19160 0.15944 0.18456 0.05372  -0.00215 -0.00334 117 LYS A CD    
2300 C CE    . LYS B 118 ? 0.13156 0.09803 0.13119 0.04572  -0.00723 -0.00158 117 LYS A CE    
2301 N NZ    . LYS B 118 ? 0.13624 0.10031 0.13911 0.04963  -0.00807 0.00124  117 LYS A NZ    
2302 N N     . SER B 119 ? 0.17195 0.14260 0.11867 0.06907  0.01035  -0.00721 118 SER A N     
2303 C CA    . SER B 119 ? 0.18596 0.16056 0.12076 0.07900  0.01832  -0.00458 118 SER A CA    
2304 C C     . SER B 119 ? 0.20959 0.17283 0.12482 0.09034  0.01823  -0.01230 118 SER A C     
2305 O O     . SER B 119 ? 0.26213 0.22946 0.16692 0.10083  0.02666  -0.00992 118 SER A O     
2306 C CB    . SER B 119 ? 0.18782 0.16396 0.11489 0.07753  0.01753  -0.00213 118 SER A CB    
2307 O OG    . SER B 119 ? 0.27564 0.25867 0.21945 0.06734  0.01677  0.00345  118 SER A OG    
2308 N N     . ASP B 120 ? 0.22151 0.16986 0.13126 0.08871  0.00947  -0.02140 119 ASP A N     
2309 C CA    . ASP B 120 ? 0.24231 0.17634 0.13338 0.09923  0.00863  -0.03037 119 ASP A CA    
2310 C C     . ASP B 120 ? 0.24766 0.18295 0.14361 0.10773  0.01621  -0.02835 119 ASP A C     
2311 O O     . ASP B 120 ? 0.26849 0.19584 0.15120 0.11527  0.01724  -0.03295 119 ASP A O     
2312 C CB    . ASP B 120 ? 0.30594 0.22201 0.19243 0.09309  -0.00343 -0.04061 119 ASP A CB    
2313 C CG    . ASP B 120 ? 0.26278 0.17731 0.16861 0.08353  -0.00652 -0.03782 119 ASP A CG    
2314 O OD1   . ASP B 120 ? 0.23761 0.16234 0.15798 0.07339  -0.00819 -0.03203 119 ASP A OD1   
2315 O OD2   . ASP B 120 ? 0.29402 0.19666 0.19940 0.08724  -0.00673 -0.04106 119 ASP A OD2   
2316 N N     . LEU B 121 ? 0.22704 0.17473 0.14392 0.10311  0.01967  -0.02037 120 LEU A N     
2317 C CA    . LEU B 121 ? 0.24110 0.19040 0.16492 0.11001  0.02429  -0.01864 120 LEU A CA    
2318 C C     . LEU B 121 ? 0.24372 0.20942 0.16953 0.11769  0.03545  -0.01175 120 LEU A C     
2319 O O     . LEU B 121 ? 0.24149 0.22075 0.17065 0.11706  0.04154  -0.00537 120 LEU A O     
2320 C CB    . LEU B 121 ? 0.22216 0.17925 0.16776 0.10197  0.02176  -0.01312 120 LEU A CB    
2321 C CG    . LEU B 121 ? 0.27672 0.21745 0.22213 0.09373  0.01162  -0.01803 120 LEU A CG    
2322 C CD1   . LEU B 121 ? 0.24170 0.19276 0.20651 0.08547  0.00951  -0.01135 120 LEU A CD1   
2323 C CD2   . LEU B 121 ? 0.28422 0.20537 0.21800 0.10115  0.00980  -0.02487 120 LEU A CD2   
2324 N N     . PRO B 122 ? 0.24964 0.21402 0.17427 0.12474  0.03857  -0.01227 121 PRO A N     
2325 C CA    . PRO B 122 ? 0.25696 0.23700 0.18435 0.13233  0.04920  -0.00558 121 PRO A CA    
2326 C C     . PRO B 122 ? 0.23875 0.24054 0.19232 0.12974  0.05424  0.00383  121 PRO A C     
2327 O O     . PRO B 122 ? 0.24598 0.26103 0.20492 0.13562  0.06243  0.00927  121 PRO A O     
2328 C CB    . PRO B 122 ? 0.28322 0.24926 0.19614 0.14166  0.04885  -0.01210 121 PRO A CB    
2329 C CG    . PRO B 122 ? 0.27903 0.23147 0.19742 0.13716  0.04048  -0.01679 121 PRO A CG    
2330 C CD    . PRO B 122 ? 0.26276 0.20942 0.18237 0.12652  0.03271  -0.01908 121 PRO A CD    
2331 N N     . SER B 123 ? 0.21727 0.22348 0.18717 0.12113  0.04896  0.00568  122 SER A N     
2332 C CA    . SER B 123 ? 0.23243 0.25759 0.22693 0.11817  0.05019  0.01254  122 SER A CA    
2333 C C     . SER B 123 ? 0.21935 0.26265 0.23250 0.10881  0.05198  0.01941  122 SER A C     
2334 O O     . SER B 123 ? 0.16445 0.21883 0.19657 0.10234  0.04789  0.02238  122 SER A O     
2335 C CB    . SER B 123 ? 0.19831 0.21381 0.19657 0.11635  0.04160  0.00939  122 SER A CB    
2336 O OG    . SER B 123 ? 0.22900 0.22955 0.21991 0.10980  0.03410  0.00485  122 SER A OG    
2337 N N     . ARG B 124 ? 0.18312 0.22948 0.19077 0.10804  0.05802  0.02228  123 ARG A N     
2338 C CA    . ARG B 124 ? 0.16587 0.22490 0.18933 0.09834  0.05982  0.02840  123 ARG A CA    
2339 C C     . ARG B 124 ? 0.17904 0.26114 0.23013 0.09283  0.06280  0.03571  123 ARG A C     
2340 O O     . ARG B 124 ? 0.16508 0.25739 0.22102 0.09792  0.06887  0.03928  123 ARG A O     
2341 C CB    . ARG B 124 ? 0.17565 0.23260 0.18633 0.10004  0.06710  0.03161  123 ARG A CB    
2342 C CG    . ARG B 124 ? 0.16833 0.23747 0.19660 0.08977  0.07077  0.03950  123 ARG A CG    
2343 C CD    . ARG B 124 ? 0.21743 0.28361 0.23191 0.09247  0.07869  0.04457  123 ARG A CD    
2344 N NE    . ARG B 124 ? 0.22260 0.26984 0.21184 0.09473  0.07252  0.03786  123 ARG A NE    
2345 C CZ    . ARG B 124 ? 0.21405 0.25339 0.20278 0.08477  0.06516  0.03665  123 ARG A CZ    
2346 N NH1   . ARG B 124 ? 0.15675 0.20286 0.16680 0.07259  0.06311  0.04041  123 ARG A NH1   
2347 N NH2   . ARG B 124 ? 0.28671 0.31145 0.25309 0.08756  0.05946  0.03107  123 ARG A NH2   
2348 N N     . THR B 125 ? 0.13651 0.22681 0.20586 0.08212  0.05771  0.03735  124 THR A N     
2349 C CA    . THR B 125 ? 0.12726 0.23871 0.22330 0.07394  0.05853  0.04291  124 THR A CA    
2350 C C     . THR B 125 ? 0.13281 0.24953 0.24130 0.06210  0.06072  0.04738  124 THR A C     
2351 O O     . THR B 125 ? 0.11623 0.24820 0.24528 0.05464  0.06277  0.05194  124 THR A O     
2352 C CB    . THR B 125 ? 0.11693 0.23454 0.22538 0.07083  0.04840  0.03996  124 THR A CB    
2353 O OG1   . THR B 125 ? 0.10720 0.21261 0.21014 0.06249  0.03932  0.03549  124 THR A OG1   
2354 C CG2   . THR B 125 ? 0.12830 0.23878 0.22533 0.08236  0.04639  0.03648  124 THR A CG2   
2355 N N     . VAL B 126 ? 0.12165 0.22116 0.21465 0.05799  0.05794  0.04461  125 VAL A N     
2356 C CA    . VAL B 126 ? 0.15663 0.25510 0.25711 0.04682  0.05917  0.04813  125 VAL A CA    
2357 C C     . VAL B 126 ? 0.17036 0.26257 0.25608 0.05274  0.06933  0.05343  125 VAL A C     
2358 O O     . VAL B 126 ? 0.14344 0.22035 0.20436 0.05987  0.06761  0.04915  125 VAL A O     
2359 C CB    . VAL B 126 ? 0.12053 0.20409 0.21390 0.03808  0.04800  0.04144  125 VAL A CB    
2360 C CG1   . VAL B 126 ? 0.15571 0.23784 0.25874 0.02728  0.04950  0.04489  125 VAL A CG1   
2361 C CG2   . VAL B 126 ? 0.10566 0.19362 0.20756 0.03472  0.03795  0.03614  125 VAL A CG2   
2362 N N     . ASP B 127 ? 0.15456 0.25858 0.25540 0.04961  0.07957  0.06288  126 ASP A N     
2363 C CA    . ASP B 127 ? 0.14676 0.24339 0.23155 0.05480  0.08866  0.06913  126 ASP A CA    
2364 C C     . ASP B 127 ? 0.15460 0.23493 0.22666 0.05055  0.08525  0.06823  126 ASP A C     
2365 O O     . ASP B 127 ? 0.15728 0.23379 0.24092 0.03898  0.07838  0.06604  126 ASP A O     
2366 C CB    . ASP B 127 ? 0.20865 0.31573 0.31040 0.04954  0.09645  0.07838  126 ASP A CB    
2367 C CG    . ASP B 127 ? 0.38527 0.50573 0.49217 0.05649  0.10077  0.07996  126 ASP A CG    
2368 O OD1   . ASP B 127 ? 0.36616 0.48365 0.45704 0.06770  0.09935  0.07467  126 ASP A OD1   
2369 O OD2   . ASP B 127 ? 0.41760 0.55074 0.54460 0.05076  0.10544  0.08613  126 ASP A OD2   
2370 N N     . THR B 128 ? 0.17613 0.24561 0.22228 0.06022  0.08853  0.06902  127 THR A N     
2371 C CA    . THR B 128 ? 0.22636 0.28051 0.25874 0.05740  0.08413  0.06853  127 THR A CA    
2372 C C     . THR B 128 ? 0.20231 0.25782 0.25125 0.04820  0.09051  0.07837  127 THR A C     
2373 O O     . THR B 128 ? 0.20682 0.25232 0.25838 0.04017  0.08384  0.07604  127 THR A O     
2374 C CB    . THR B 128 ? 0.20857 0.25413 0.21077 0.07052  0.08685  0.06856  127 THR A CB    
2375 O OG1   . THR B 128 ? 0.22953 0.26854 0.21625 0.07647  0.07780  0.05694  127 THR A OG1   
2376 C CG2   . THR B 128 ? 0.22490 0.25817 0.21507 0.06883  0.08387  0.07089  127 THR A CG2   
2377 N N     . LYS B 129 ? 0.23314 0.29844 0.29328 0.04863  0.10129  0.08800  128 LYS A N     
2378 C CA    . LYS B 129 ? 0.20457 0.26731 0.28083 0.03872  0.10468  0.09548  128 LYS A CA    
2379 C C     . LYS B 129 ? 0.18347 0.24818 0.28438 0.02402  0.09747  0.09078  128 LYS A C     
2380 O O     . LYS B 129 ? 0.17402 0.22802 0.28028 0.01603  0.09575  0.09211  128 LYS A O     
2381 C CB    . LYS B 129 ? 0.19394 0.26643 0.27940 0.04047  0.11392  0.10383  128 LYS A CB    
2382 C CG    . LYS B 129 ? 0.25233 0.31905 0.34927 0.03280  0.11891  0.11232  128 LYS A CG    
2383 C CD    . LYS B 129 ? 0.27976 0.36019 0.39830 0.02832  0.12606  0.11887  128 LYS A CD    
2384 C CE    . LYS B 129 ? 0.23951 0.31282 0.36213 0.02544  0.13410  0.12935  128 LYS A CE    
2385 N NZ    . LYS B 129 ? 0.29123 0.34731 0.41300 0.01838  0.12938  0.12803  128 LYS A NZ    
2386 N N     . GLN B 130 ? 0.19816 0.27561 0.31313 0.02103  0.09234  0.08460  129 GLN A N     
2387 C CA    . GLN B 130 ? 0.18881 0.26829 0.32430 0.00796  0.08340  0.07848  129 GLN A CA    
2388 C C     . GLN B 130 ? 0.15818 0.22148 0.28262 0.00495  0.07513  0.07206  129 GLN A C     
2389 O O     . GLN B 130 ? 0.12767 0.18377 0.26314 -0.00540 0.07163  0.07058  129 GLN A O     
2390 C CB    . GLN B 130 ? 0.16806 0.26339 0.31501 0.00821  0.07740  0.07224  129 GLN A CB    
2391 C CG    . GLN B 130 ? 0.21745 0.32845 0.37443 0.01147  0.08341  0.07691  129 GLN A CG    
2392 C CD    . GLN B 130 ? 0.35849 0.48435 0.52380 0.01429  0.07739  0.07118  129 GLN A CD    
2393 O OE1   . GLN B 130 ? 0.26670 0.38979 0.41988 0.02157  0.07272  0.06570  129 GLN A OE1   
2394 N NE2   . GLN B 130 ? 0.40997 0.55163 0.59608 0.00902  0.07746  0.07263  129 GLN A NE2   
2395 N N     . ALA B 131 ? 0.16518 0.22025 0.26530 0.01413  0.06986  0.06625  130 ALA A N     
2396 C CA    . ALA B 131 ? 0.19049 0.23042 0.27777 0.01227  0.06018  0.05889  130 ALA A CA    
2397 C C     . ALA B 131 ? 0.13557 0.16241 0.21510 0.01238  0.06455  0.06498  130 ALA A C     
2398 O O     . ALA B 131 ? 0.18801 0.20467 0.26984 0.00630  0.05935  0.06166  130 ALA A O     
2399 C CB    . ALA B 131 ? 0.13511 0.17100 0.20141 0.02118  0.05384  0.05181  130 ALA A CB    
2400 N N     . GLN B 132 ? 0.14765 0.17434 0.21662 0.02048  0.07435  0.07415  131 GLN A N     
2401 C CA    . GLN B 132 ? 0.16093 0.17573 0.22276 0.02175  0.07963  0.08224  131 GLN A CA    
2402 C C     . GLN B 132 ? 0.16313 0.17454 0.24814 0.00979  0.08354  0.08717  131 GLN A C     
2403 O O     . GLN B 132 ? 0.16608 0.16357 0.25027 0.00614  0.08037  0.08632  131 GLN A O     
2404 C CB    . GLN B 132 ? 0.20213 0.21966 0.24912 0.03300  0.09088  0.09272  131 GLN A CB    
2405 C CG    . GLN B 132 ? 0.22123 0.23819 0.24171 0.04536  0.08606  0.08667  131 GLN A CG    
2406 C CD    . GLN B 132 ? 0.27281 0.29307 0.27590 0.05779  0.09715  0.09592  131 GLN A CD    
2407 O OE1   . GLN B 132 ? 0.22441 0.25062 0.23913 0.05683  0.10528  0.10313  131 GLN A OE1   
2408 N NE2   . GLN B 132 ? 0.31286 0.32802 0.28883 0.06879  0.09205  0.09107  131 GLN A NE2   
2409 N N     . ASP B 133 ? 0.16376 0.18711 0.26860 0.00398  0.08745  0.08930  132 ASP A N     
2410 C CA    . ASP B 133 ? 0.17059 0.18991 0.29474 -0.00729 0.08700  0.08962  132 ASP A CA    
2411 C C     . ASP B 133 ? 0.15990 0.17238 0.29298 -0.01710 0.07649  0.07920  132 ASP A C     
2412 O O     . ASP B 133 ? 0.19120 0.19048 0.32836 -0.02306 0.07489  0.07807  132 ASP A O     
2413 C CB    . ASP B 133 ? 0.17403 0.20965 0.31689 -0.01146 0.09101  0.09232  132 ASP A CB    
2414 C CG    . ASP B 133 ? 0.21680 0.25737 0.35180 -0.00217 0.10244  0.10324  132 ASP A CG    
2415 O OD1   . ASP B 133 ? 0.25400 0.28412 0.36915 0.00673  0.10666  0.10858  132 ASP A OD1   
2416 O OD2   . ASP B 133 ? 0.19332 0.24882 0.34104 -0.00299 0.10683  0.10630  132 ASP A OD2   
2417 N N     . LEU B 134 ? 0.14629 0.16718 0.28144 -0.01810 0.06924  0.07117  133 LEU A N     
2418 C CA    . LEU B 134 ? 0.14371 0.15858 0.28454 -0.02602 0.05872  0.06052  133 LEU A CA    
2419 C C     . LEU B 134 ? 0.17967 0.17549 0.30346 -0.02251 0.05581  0.05830  133 LEU A C     
2420 O O     . LEU B 134 ? 0.15613 0.13950 0.28530 -0.02885 0.05330  0.05503  133 LEU A O     
2421 C CB    . LEU B 134 ? 0.12368 0.15053 0.26182 -0.02396 0.04954  0.05122  133 LEU A CB    
2422 C CG    . LEU B 134 ? 0.12935 0.15103 0.26959 -0.03058 0.03817  0.03972  133 LEU A CG    
2423 C CD1   . LEU B 134 ? 0.17898 0.20189 0.33974 -0.04228 0.03643  0.03735  133 LEU A CD1   
2424 C CD2   . LEU B 134 ? 0.15788 0.18975 0.29256 -0.02719 0.02978  0.03225  133 LEU A CD2   
2425 N N     . ALA B 135 ? 0.14134 0.13510 0.24355 -0.01157 0.05528  0.05903  134 ALA A N     
2426 C CA    . ALA B 135 ? 0.14081 0.12012 0.22769 -0.00689 0.05221  0.05755  134 ALA A CA    
2427 C C     . ALA B 135 ? 0.18922 0.15465 0.27959 -0.00820 0.05984  0.06649  134 ALA A C     
2428 O O     . ALA B 135 ? 0.16874 0.12069 0.25878 -0.01025 0.05672  0.06315  134 ALA A O     
2429 C CB    . ALA B 135 ? 0.16752 0.14927 0.23297 0.00469  0.05091  0.05820  134 ALA A CB    
2430 N N     . ARG B 136 ? 0.16925 0.13756 0.26208 -0.00614 0.06999  0.07764  135 ARG A N     
2431 C CA    . ARG B 136 ? 0.18810 0.14531 0.28243 -0.00677 0.07479  0.08329  135 ARG A CA    
2432 C C     . ARG B 136 ? 0.23333 0.18378 0.34468 -0.01865 0.07060  0.07629  135 ARG A C     
2433 O O     . ARG B 136 ? 0.23156 0.16674 0.34014 -0.01916 0.06953  0.07521  135 ARG A O     
2434 C CB    . ARG B 136 ? 0.20982 0.17474 0.30509 -0.00319 0.08484  0.09399  135 ARG A CB    
2435 C CG    . ARG B 136 ? 0.31496 0.26792 0.40759 -0.00112 0.09102  0.10220  135 ARG A CG    
2436 C CD    . ARG B 136 ? 0.27999 0.24092 0.37410 0.00245  0.10147  0.11314  135 ARG A CD    
2437 N NE    . ARG B 136 ? 0.32675 0.29337 0.39939 0.01620  0.10507  0.11849  135 ARG A NE    
2438 C CZ    . ARG B 136 ? 0.40148 0.35985 0.45486 0.02640  0.10633  0.12336  135 ARG A CZ    
2439 N NH1   . ARG B 136 ? 0.28996 0.23385 0.34294 0.02516  0.10482  0.12424  135 ARG A NH1   
2440 N NH2   . ARG B 136 ? 0.35604 0.32113 0.38934 0.03871  0.10849  0.12664  135 ARG A NH2   
2441 N N     . SER B 137 ? 0.18769 0.14972 0.31556 -0.02758 0.06749  0.07085  136 SER A N     
2442 C CA    . SER B 137 ? 0.22756 0.18392 0.36940 -0.03874 0.06215  0.06304  136 SER A CA    
2443 C C     . SER B 137 ? 0.23292 0.17689 0.36726 -0.03923 0.05377  0.05267  136 SER A C     
2444 O O     . SER B 137 ? 0.29919 0.23056 0.43727 -0.04482 0.05108  0.04776  136 SER A O     
2445 C CB    . SER B 137 ? 0.22344 0.19733 0.38210 -0.04677 0.05837  0.05823  136 SER A CB    
2446 O OG    . SER B 137 ? 0.22634 0.20921 0.38189 -0.04552 0.05067  0.05007  136 SER A OG    
2447 N N     . TYR B 138 ? 0.17094 0.11761 0.29411 -0.03301 0.05005  0.04949  137 TYR A N     
2448 C CA    . TYR B 138 ? 0.19639 0.13288 0.31132 -0.03170 0.04297  0.04037  137 TYR A CA    
2449 C C     . TYR B 138 ? 0.25013 0.17176 0.35131 -0.02308 0.04617  0.04518  137 TYR A C     
2450 O O     . TYR B 138 ? 0.17957 0.09114 0.27513 -0.02153 0.04162  0.03824  137 TYR A O     
2451 C CB    . TYR B 138 ? 0.17431 0.12184 0.28329 -0.02858 0.03705  0.03484  137 TYR A CB    
2452 C CG    . TYR B 138 ? 0.19611 0.15806 0.31627 -0.03567 0.03097  0.02743  137 TYR A CG    
2453 C CD1   . TYR B 138 ? 0.19471 0.15792 0.32881 -0.04501 0.02865  0.02321  137 TYR A CD1   
2454 C CD2   . TYR B 138 ? 0.14782 0.12335 0.25989 -0.03109 0.02589  0.02373  137 TYR A CD2   
2455 C CE1   . TYR B 138 ? 0.21407 0.19219 0.35717 -0.05022 0.02197  0.01664  137 TYR A CE1   
2456 C CE2   . TYR B 138 ? 0.16249 0.15130 0.28374 -0.03597 0.02014  0.01793  137 TYR A CE2   
2457 C CZ    . TYR B 138 ? 0.21190 0.20277 0.35174 -0.04628 0.01840  0.01485  137 TYR A CZ    
2458 O OH    . TYR B 138 ? 0.22315 0.22940 0.37138 -0.05007 0.01146  0.00912  137 TYR A OH    
2459 N N     . GLY B 139 ? 0.18532 0.10677 0.28008 -0.01639 0.05370  0.05677  138 GLY A N     
2460 C CA    . GLY B 139 ? 0.21423 0.12516 0.29460 -0.00652 0.05564  0.06188  138 GLY A CA    
2461 C C     . GLY B 139 ? 0.20762 0.12232 0.27432 0.00241  0.05125  0.06038  138 GLY A C     
2462 O O     . GLY B 139 ? 0.18842 0.09564 0.24564 0.00959  0.04936  0.06033  138 GLY A O     
2463 N N     . ILE B 140 ? 0.16748 0.09707 0.23182 0.00257  0.04785  0.05716  139 ILE A N     
2464 C CA    . ILE B 140 ? 0.18391 0.12146 0.23484 0.00946  0.04044  0.05148  139 ILE A CA    
2465 C C     . ILE B 140 ? 0.17200 0.12029 0.21209 0.01600  0.04186  0.05624  139 ILE A C     
2466 O O     . ILE B 140 ? 0.18778 0.14039 0.23181 0.01463  0.04832  0.06224  139 ILE A O     
2467 C CB    . ILE B 140 ? 0.16796 0.11237 0.22368 0.00357  0.03248  0.03943  139 ILE A CB    
2468 C CG1   . ILE B 140 ? 0.16469 0.12081 0.22844 -0.00212 0.03255  0.03793  139 ILE A CG1   
2469 C CG2   . ILE B 140 ? 0.24221 0.17539 0.30560 -0.00173 0.03087  0.03340  139 ILE A CG2   
2470 C CD1   . ILE B 140 ? 0.14213 0.10539 0.20872 -0.00657 0.02471  0.02750  139 ILE A CD1   
2471 N N     . PRO B 141 ? 0.19272 0.14598 0.21954 0.02317  0.03590  0.05319  140 PRO A N     
2472 C CA    . PRO B 141 ? 0.19223 0.15384 0.20646 0.02983  0.03604  0.05562  140 PRO A CA    
2473 C C     . PRO B 141 ? 0.17748 0.14882 0.19576 0.02561  0.03399  0.04965  140 PRO A C     
2474 O O     . PRO B 141 ? 0.13970 0.11345 0.16757 0.01871  0.02959  0.04234  140 PRO A O     
2475 C CB    . PRO B 141 ? 0.24136 0.20487 0.24322 0.03685  0.02820  0.05207  140 PRO A CB    
2476 C CG    . PRO B 141 ? 0.27435 0.22988 0.28160 0.03656  0.02737  0.05237  140 PRO A CG    
2477 C CD    . PRO B 141 ? 0.20461 0.15552 0.22706 0.02658  0.02950  0.04851  140 PRO A CD    
2478 N N     . PHE B 142 ? 0.14542 0.12218 0.15476 0.03118  0.03753  0.05320  141 PHE A N     
2479 C CA    . PHE B 142 ? 0.18267 0.16790 0.19227 0.03048  0.03554  0.04782  141 PHE A CA    
2480 C C     . PHE B 142 ? 0.21126 0.19798 0.20166 0.03954  0.03164  0.04516  141 PHE A C     
2481 O O     . PHE B 142 ? 0.21947 0.20451 0.19649 0.04756  0.03532  0.05115  141 PHE A O     
2482 C CB    . PHE B 142 ? 0.15352 0.14478 0.17311 0.02858  0.04473  0.05387  141 PHE A CB    
2483 C CG    . PHE B 142 ? 0.14221 0.14222 0.15938 0.03140  0.04395  0.04977  141 PHE A CG    
2484 C CD1   . PHE B 142 ? 0.12336 0.12665 0.14727 0.02671  0.03670  0.04131  141 PHE A CD1   
2485 C CD2   . PHE B 142 ? 0.20131 0.20554 0.20837 0.03985  0.05107  0.05483  141 PHE A CD2   
2486 C CE1   . PHE B 142 ? 0.12177 0.13128 0.14325 0.03039  0.03612  0.03799  141 PHE A CE1   
2487 C CE2   . PHE B 142 ? 0.17200 0.18283 0.17624 0.04384  0.05080  0.05063  141 PHE A CE2   
2488 C CZ    . PHE B 142 ? 0.15894 0.17185 0.17095 0.03906  0.04311  0.04222  141 PHE A CZ    
2489 N N     . ILE B 143 ? 0.16317 0.15226 0.15151 0.03841  0.02404  0.03618  142 ILE A N     
2490 C CA    . ILE B 143 ? 0.16373 0.15243 0.13514 0.04542  0.01862  0.03136  142 ILE A CA    
2491 C C     . ILE B 143 ? 0.20408 0.19511 0.17599 0.04511  0.01740  0.02558  142 ILE A C     
2492 O O     . ILE B 143 ? 0.14794 0.14032 0.13198 0.03834  0.01453  0.02179  142 ILE A O     
2493 C CB    . ILE B 143 ? 0.22886 0.21564 0.19759 0.04415  0.00874  0.02570  142 ILE A CB    
2494 C CG1   . ILE B 143 ? 0.25957 0.24427 0.22898 0.04575  0.01025  0.03188  142 ILE A CG1   
2495 C CG2   . ILE B 143 ? 0.26361 0.24988 0.21566 0.05051  0.00200  0.01995  142 ILE A CG2   
2496 C CD1   . ILE B 143 ? 0.29436 0.27989 0.26762 0.04343  0.00226  0.02749  142 ILE A CD1   
2497 N N     . GLU B 144 ? 0.15294 0.14381 0.11033 0.05349  0.01961  0.02493  143 GLU A N     
2498 C CA    . GLU B 144 ? 0.23493 0.22564 0.19017 0.05543  0.01833  0.01891  143 GLU A CA    
2499 C C     . GLU B 144 ? 0.20546 0.18930 0.15069 0.05575  0.00756  0.00914  143 GLU A C     
2500 O O     . GLU B 144 ? 0.23784 0.21882 0.16920 0.06008  0.00298  0.00693  143 GLU A O     
2501 C CB    . GLU B 144 ? 0.25511 0.24818 0.19901 0.06538  0.02683  0.02226  143 GLU A CB    
2502 C CG    . GLU B 144 ? 0.34033 0.34062 0.29181 0.06631  0.03879  0.03372  143 GLU A CG    
2503 C CD    . GLU B 144 ? 0.38707 0.39020 0.32350 0.07817  0.04789  0.03749  143 GLU A CD    
2504 O OE1   . GLU B 144 ? 0.38572 0.38949 0.31792 0.08330  0.04838  0.03224  143 GLU A OE1   
2505 O OE2   . GLU B 144 ? 0.37130 0.37533 0.29889 0.08335  0.05493  0.04595  143 GLU A OE2   
2506 N N     . THR B 145 ? 0.18525 0.16667 0.13801 0.05105  0.00324  0.00364  144 THR A N     
2507 C CA    . THR B 145 ? 0.17296 0.14706 0.12015 0.04915  -0.00658 -0.00493 144 THR A CA    
2508 C C     . THR B 145 ? 0.20076 0.16810 0.14442 0.05184  -0.00738 -0.01045 144 THR A C     
2509 O O     . THR B 145 ? 0.17932 0.14988 0.12908 0.05382  -0.00114 -0.00730 144 THR A O     
2510 C CB    . THR B 145 ? 0.16595 0.14147 0.12707 0.03942  -0.01184 -0.00550 144 THR A CB    
2511 O OG1   . THR B 145 ? 0.12571 0.10360 0.09977 0.03493  -0.00876 -0.00341 144 THR A OG1   
2512 C CG2   . THR B 145 ? 0.13894 0.11980 0.10391 0.03779  -0.01081 -0.00035 144 THR A CG2   
2513 N N     . SER B 146 ? 0.17048 0.12838 0.10561 0.05163  -0.01564 -0.01879 145 SER A N     
2514 C CA    . SER B 146 ? 0.18217 0.12982 0.11684 0.05160  -0.01828 -0.02457 145 SER A CA    
2515 C C     . SER B 146 ? 0.18390 0.12528 0.12334 0.04304  -0.02794 -0.02999 145 SER A C     
2516 O O     . SER B 146 ? 0.19460 0.13272 0.12546 0.04306  -0.03503 -0.03590 145 SER A O     
2517 C CB    . SER B 146 ? 0.21044 0.14929 0.12649 0.06237  -0.01704 -0.03046 145 SER A CB    
2518 O OG    . SER B 146 ? 0.21024 0.13505 0.12468 0.06179  -0.02155 -0.03759 145 SER A OG    
2519 N N     . ALA B 147 ? 0.18821 0.12913 0.14168 0.03580  -0.02832 -0.02763 146 ALA A N     
2520 C CA    . ALA B 147 ? 0.17134 0.10554 0.13057 0.02766  -0.03595 -0.03186 146 ALA A CA    
2521 C C     . ALA B 147 ? 0.21817 0.13575 0.16705 0.03003  -0.04113 -0.04083 146 ALA A C     
2522 O O     . ALA B 147 ? 0.24053 0.15209 0.19158 0.02361  -0.04913 -0.04649 146 ALA A O     
2523 C CB    . ALA B 147 ? 0.16718 0.10346 0.14086 0.02119  -0.03364 -0.02631 146 ALA A CB    
2524 N N     . LYS B 148 ? 0.20845 0.11848 0.14668 0.03924  -0.03679 -0.04270 147 LYS A N     
2525 C CA    . LYS B 148 ? 0.23269 0.12386 0.15961 0.04251  -0.04142 -0.05230 147 LYS A CA    
2526 C C     . LYS B 148 ? 0.30835 0.19624 0.21974 0.04551  -0.04843 -0.06154 147 LYS A C     
2527 O O     . LYS B 148 ? 0.31812 0.19376 0.22679 0.04112  -0.05706 -0.07040 147 LYS A O     
2528 C CB    . LYS B 148 ? 0.23498 0.11944 0.15457 0.05340  -0.03405 -0.05166 147 LYS A CB    
2529 C CG    . LYS B 148 ? 0.29495 0.15790 0.20138 0.05821  -0.03791 -0.06197 147 LYS A CG    
2530 C CD    . LYS B 148 ? 0.27136 0.13102 0.17491 0.06835  -0.02951 -0.05898 147 LYS A CD    
2531 C CE    . LYS B 148 ? 0.39774 0.24058 0.29302 0.07015  -0.03194 -0.06630 147 LYS A CE    
2532 N NZ    . LYS B 148 ? 0.41897 0.26107 0.30795 0.08251  -0.02357 -0.06451 147 LYS A NZ    
2533 N N     . THR B 149 ? 0.24182 0.14118 0.14338 0.05268  -0.04484 -0.05898 148 THR A N     
2534 C CA    . THR B 149 ? 0.30647 0.20402 0.19002 0.05765  -0.05144 -0.06703 148 THR A CA    
2535 C C     . THR B 149 ? 0.31947 0.23039 0.20947 0.05131  -0.05767 -0.06479 148 THR A C     
2536 O O     . THR B 149 ? 0.30380 0.21524 0.18002 0.05486  -0.06506 -0.07127 148 THR A O     
2537 C CB    . THR B 149 ? 0.27205 0.17319 0.13721 0.07171  -0.04302 -0.06495 148 THR A CB    
2538 O OG1   . THR B 149 ? 0.30949 0.22811 0.18271 0.07155  -0.03569 -0.05304 148 THR A OG1   
2539 C CG2   . THR B 149 ? 0.29795 0.19021 0.15995 0.07946  -0.03466 -0.06493 148 THR A CG2   
2540 N N     . ARG B 150 ? 0.23432 0.15653 0.14388 0.04333  -0.05473 -0.05580 149 ARG A N     
2541 C CA    . ARG B 150 ? 0.25012 0.18643 0.16865 0.03849  -0.05809 -0.05144 149 ARG A CA    
2542 C C     . ARG B 150 ? 0.26771 0.21420 0.17623 0.04716  -0.05244 -0.04488 149 ARG A C     
2543 O O     . ARG B 150 ? 0.23487 0.19223 0.14935 0.04513  -0.05452 -0.04048 149 ARG A O     
2544 C CB    . ARG B 150 ? 0.23500 0.17079 0.15442 0.03289  -0.07135 -0.06014 149 ARG A CB    
2545 C CG    . ARG B 150 ? 0.31469 0.26321 0.25524 0.02319  -0.07384 -0.05495 149 ARG A CG    
2546 C CD    . ARG B 150 ? 0.31427 0.26314 0.26376 0.01446  -0.08631 -0.06289 149 ARG A CD    
2547 N NE    . ARG B 150 ? 0.32116 0.28374 0.29279 0.00606  -0.08572 -0.05609 149 ARG A NE    
2548 C CZ    . ARG B 150 ? 0.32299 0.30136 0.29857 0.00863  -0.08561 -0.05060 149 ARG A CZ    
2549 N NH1   . ARG B 150 ? 0.32965 0.31215 0.28909 0.01845  -0.08713 -0.05071 149 ARG A NH1   
2550 N NH2   . ARG B 150 ? 0.32469 0.31446 0.31992 0.00221  -0.08332 -0.04436 149 ARG A NH2   
2551 N N     . GLN B 151 ? 0.25708 0.20067 0.15182 0.05699  -0.04441 -0.04297 150 GLN A N     
2552 C CA    . GLN B 151 ? 0.27992 0.23266 0.16714 0.06459  -0.03678 -0.03440 150 GLN A CA    
2553 C C     . GLN B 151 ? 0.21402 0.17676 0.12010 0.05823  -0.03150 -0.02416 150 GLN A C     
2554 O O     . GLN B 151 ? 0.20229 0.16545 0.12287 0.05290  -0.02648 -0.02078 150 GLN A O     
2555 C CB    . GLN B 151 ? 0.34159 0.29152 0.21769 0.07431  -0.02617 -0.03183 150 GLN A CB    
2556 C CG    . GLN B 151 ? 0.33545 0.29538 0.20945 0.08004  -0.01548 -0.02006 150 GLN A CG    
2557 C CD    . GLN B 151 ? 0.44436 0.40634 0.31993 0.08541  -0.00276 -0.01435 150 GLN A CD    
2558 O OE1   . GLN B 151 ? 0.40471 0.37508 0.28521 0.08720  0.00713  -0.00375 150 GLN A OE1   
2559 N NE2   . GLN B 151 ? 0.50234 0.45674 0.37501 0.08804  -0.00286 -0.02105 150 GLN A NE2   
2560 N N     . GLY B 152 ? 0.21279 0.18301 0.11767 0.05957  -0.03308 -0.01960 151 GLY A N     
2561 C CA    . GLY B 152 ? 0.20927 0.18666 0.12861 0.05573  -0.02728 -0.01010 151 GLY A CA    
2562 C C     . GLY B 152 ? 0.17506 0.15535 0.11385 0.04535  -0.03117 -0.01083 151 GLY A C     
2563 O O     . GLY B 152 ? 0.14878 0.13355 0.09864 0.04256  -0.02646 -0.00417 151 GLY A O     
2564 N N     . VAL B 153 ? 0.20671 0.18394 0.14979 0.03970  -0.03917 -0.01855 152 VAL A N     
2565 C CA    . VAL B 153 ? 0.14567 0.12633 0.10698 0.03025  -0.04123 -0.01815 152 VAL A CA    
2566 C C     . VAL B 153 ? 0.14064 0.13107 0.10885 0.02953  -0.04419 -0.01489 152 VAL A C     
2567 O O     . VAL B 153 ? 0.15293 0.14758 0.13234 0.02676  -0.03938 -0.00949 152 VAL A O     
2568 C CB    . VAL B 153 ? 0.18604 0.16064 0.15077 0.02427  -0.04852 -0.02597 152 VAL A CB    
2569 C CG1   . VAL B 153 ? 0.15265 0.13277 0.13595 0.01503  -0.04990 -0.02413 152 VAL A CG1   
2570 C CG2   . VAL B 153 ? 0.17645 0.14027 0.13589 0.02584  -0.04456 -0.02815 152 VAL A CG2   
2571 N N     . ASP B 154 ? 0.18047 0.17484 0.14214 0.03247  -0.05272 -0.01873 153 ASP A N     
2572 C CA    . ASP B 154 ? 0.19550 0.20080 0.16373 0.03380  -0.05565 -0.01492 153 ASP A CA    
2573 C C     . ASP B 154 ? 0.21218 0.21781 0.17705 0.04008  -0.04660 -0.00562 153 ASP A C     
2574 O O     . ASP B 154 ? 0.17759 0.18782 0.15395 0.03864  -0.04350 -0.00070 153 ASP A O     
2575 C CB    . ASP B 154 ? 0.16555 0.17631 0.12486 0.03786  -0.06702 -0.02034 153 ASP A CB    
2576 C CG    . ASP B 154 ? 0.27618 0.28796 0.24449 0.02929  -0.07730 -0.02960 153 ASP A CG    
2577 O OD1   . ASP B 154 ? 0.22824 0.23727 0.21080 0.02041  -0.07478 -0.03011 153 ASP A OD1   
2578 O OD2   . ASP B 154 ? 0.31039 0.32557 0.27141 0.03134  -0.08818 -0.03629 153 ASP A OD2   
2579 N N     . ASP B 155 ? 0.19222 0.19212 0.14158 0.04717  -0.04153 -0.00295 154 ASP A N     
2580 C CA    . ASP B 155 ? 0.17263 0.17141 0.11958 0.05240  -0.03222 0.00682  154 ASP A CA    
2581 C C     . ASP B 155 ? 0.16806 0.16470 0.13082 0.04563  -0.02464 0.01047  154 ASP A C     
2582 O O     . ASP B 155 ? 0.16442 0.16105 0.13266 0.04682  -0.02005 0.01683  154 ASP A O     
2583 C CB    . ASP B 155 ? 0.21167 0.20526 0.14172 0.05981  -0.02609 0.00968  154 ASP A CB    
2584 C CG    . ASP B 155 ? 0.25121 0.24655 0.16102 0.06919  -0.03263 0.00726  154 ASP A CG    
2585 O OD1   . ASP B 155 ? 0.26813 0.27003 0.17760 0.07115  -0.04133 0.00598  154 ASP A OD1   
2586 O OD2   . ASP B 155 ? 0.36804 0.35917 0.26173 0.07548  -0.02899 0.00674  154 ASP A OD2   
2587 N N     . ALA B 156 ? 0.13567 0.12962 0.10498 0.03906  -0.02367 0.00624  155 ALA A N     
2588 C CA    . ALA B 156 ? 0.14882 0.14149 0.13120 0.03302  -0.01774 0.00861  155 ALA A CA    
2589 C C     . ALA B 156 ? 0.12076 0.11750 0.11457 0.02947  -0.01990 0.00869  155 ALA A C     
2590 O O     . ALA B 156 ? 0.11430 0.10954 0.11349 0.02962  -0.01493 0.01300  155 ALA A O     
2591 C CB    . ALA B 156 ? 0.11486 0.10513 0.10055 0.02811  -0.01772 0.00422  155 ALA A CB    
2592 N N     . PHE B 157 ? 0.12001 0.12171 0.11818 0.02640  -0.02695 0.00393  156 PHE A N     
2593 C CA    . PHE B 157 ? 0.13222 0.14008 0.14213 0.02385  -0.02794 0.00449  156 PHE A CA    
2594 C C     . PHE B 157 ? 0.10784 0.11987 0.11659 0.03067  -0.02857 0.00871  156 PHE A C     
2595 O O     . PHE B 157 ? 0.13794 0.15117 0.15424 0.03140  -0.02509 0.01147  156 PHE A O     
2596 C CB    . PHE B 157 ? 0.09801 0.11171 0.11517 0.01838  -0.03450 -0.00039 156 PHE A CB    
2597 C CG    . PHE B 157 ? 0.09220 0.10114 0.11255 0.01198  -0.03272 -0.00277 156 PHE A CG    
2598 C CD1   . PHE B 157 ? 0.09782 0.09995 0.11054 0.01145  -0.03468 -0.00613 156 PHE A CD1   
2599 C CD2   . PHE B 157 ? 0.10896 0.11980 0.13847 0.00774  -0.02889 -0.00148 156 PHE A CD2   
2600 C CE1   . PHE B 157 ? 0.13137 0.12851 0.14673 0.00685  -0.03306 -0.00741 156 PHE A CE1   
2601 C CE2   . PHE B 157 ? 0.15817 0.16486 0.18904 0.00300  -0.02748 -0.00264 156 PHE A CE2   
2602 C CZ    . PHE B 157 ? 0.16167 0.16144 0.18609 0.00258  -0.02965 -0.00519 156 PHE A CZ    
2603 N N     . TYR B 158 ? 0.11868 0.13274 0.11705 0.03671  -0.03324 0.00908  157 TYR A N     
2604 C CA    . TYR B 158 ? 0.14409 0.16282 0.14053 0.04464  -0.03443 0.01410  157 TYR A CA    
2605 C C     . TYR B 158 ? 0.13896 0.14845 0.13206 0.04899  -0.02502 0.02171  157 TYR A C     
2606 O O     . TYR B 158 ? 0.13292 0.14289 0.13075 0.05325  -0.02287 0.02621  157 TYR A O     
2607 C CB    . TYR B 158 ? 0.14423 0.16760 0.12777 0.05101  -0.04237 0.01272  157 TYR A CB    
2608 C CG    . TYR B 158 ? 0.15163 0.18470 0.14066 0.04647  -0.05350 0.00474  157 TYR A CG    
2609 C CD1   . TYR B 158 ? 0.12780 0.16450 0.13291 0.03694  -0.05446 0.00075  157 TYR A CD1   
2610 C CD2   . TYR B 158 ? 0.15554 0.19384 0.13342 0.05152  -0.06316 0.00124  157 TYR A CD2   
2611 C CE1   . TYR B 158 ? 0.13729 0.18211 0.14972 0.03152  -0.06408 -0.00576 157 TYR A CE1   
2612 C CE2   . TYR B 158 ? 0.20223 0.24880 0.18691 0.04600  -0.07429 -0.00695 157 TYR A CE2   
2613 C CZ    . TYR B 158 ? 0.20974 0.25917 0.21277 0.03547  -0.07438 -0.01011 157 TYR A CZ    
2614 O OH    . TYR B 158 ? 0.31076 0.36780 0.32280 0.02875  -0.08503 -0.01759 157 TYR A OH    
2615 N N     . THR B 159 ? 0.14811 0.14894 0.13444 0.04792  -0.01900 0.02340  158 THR A N     
2616 C CA    . THR B 159 ? 0.13712 0.12872 0.12368 0.04973  -0.00966 0.03068  158 THR A CA    
2617 C C     . THR B 159 ? 0.17079 0.15889 0.17097 0.04420  -0.00615 0.02947  158 THR A C     
2618 O O     . THR B 159 ? 0.20482 0.18615 0.20757 0.04723  -0.00132 0.03447  158 THR A O     
2619 C CB    . THR B 159 ? 0.13972 0.12601 0.12058 0.04816  -0.00379 0.03238  158 THR A CB    
2620 O OG1   . THR B 159 ? 0.18425 0.17225 0.14911 0.05584  -0.00533 0.03456  158 THR A OG1   
2621 C CG2   . THR B 159 ? 0.20679 0.18410 0.19297 0.04687  0.00596  0.03940  158 THR A CG2   
2622 N N     . LEU B 160 ? 0.11512 0.10646 0.12283 0.03670  -0.00834 0.02285  159 LEU A N     
2623 C CA    . LEU B 160 ? 0.10862 0.09732 0.12635 0.03242  -0.00552 0.02071  159 LEU A CA    
2624 C C     . LEU B 160 ? 0.13888 0.13157 0.16107 0.03734  -0.00697 0.02169  159 LEU A C     
2625 O O     . LEU B 160 ? 0.12802 0.11359 0.15383 0.03899  -0.00237 0.02312  159 LEU A O     
2626 C CB    . LEU B 160 ? 0.09720 0.08982 0.11970 0.02499  -0.00777 0.01456  159 LEU A CB    
2627 C CG    . LEU B 160 ? 0.09279 0.08333 0.12253 0.02132  -0.00513 0.01168  159 LEU A CG    
2628 C CD1   . LEU B 160 ? 0.09854 0.07820 0.12923 0.02016  0.00046  0.01317  159 LEU A CD1   
2629 C CD2   . LEU B 160 ? 0.11244 0.10739 0.14472 0.01511  -0.00729 0.00706  159 LEU A CD2   
2630 N N     . VAL B 161 ? 0.14501 0.14917 0.16778 0.03993  -0.01351 0.02060  160 VAL A N     
2631 C CA    . VAL B 161 ? 0.11323 0.12463 0.14211 0.04583  -0.01504 0.02240  160 VAL A CA    
2632 C C     . VAL B 161 ? 0.12953 0.13282 0.15300 0.05484  -0.01123 0.02954  160 VAL A C     
2633 O O     . VAL B 161 ? 0.15653 0.15569 0.18487 0.05909  -0.00726 0.03147  160 VAL A O     
2634 C CB    . VAL B 161 ? 0.11603 0.14314 0.14801 0.04643  -0.02399 0.02025  160 VAL A CB    
2635 C CG1   . VAL B 161 ? 0.11673 0.15428 0.15531 0.05487  -0.02624 0.02378  160 VAL A CG1   
2636 C CG2   . VAL B 161 ? 0.09987 0.13331 0.14031 0.03738  -0.02611 0.01456  160 VAL A CG2   
2637 N N     . ARG B 162 ? 0.15473 0.15427 0.16705 0.05857  -0.01158 0.03395  161 ARG A N     
2638 C CA    . ARG B 162 ? 0.18237 0.17241 0.18842 0.06722  -0.00672 0.04264  161 ARG A CA    
2639 C C     . ARG B 162 ? 0.25121 0.22475 0.26167 0.06399  0.00238  0.04434  161 ARG A C     
2640 O O     . ARG B 162 ? 0.26388 0.22826 0.27515 0.07047  0.00664  0.04971  161 ARG A O     
2641 C CB    . ARG B 162 ? 0.26219 0.25098 0.25372 0.07137  -0.00723 0.04749  161 ARG A CB    
2642 C CG    . ARG B 162 ? 0.18512 0.18865 0.16969 0.07645  -0.01760 0.04535  161 ARG A CG    
2643 C CD    . ARG B 162 ? 0.22119 0.22227 0.18749 0.08289  -0.01740 0.05028  161 ARG A CD    
2644 N NE    . ARG B 162 ? 0.22593 0.24015 0.18516 0.08535  -0.02838 0.04499  161 ARG A NE    
2645 C CZ    . ARG B 162 ? 0.26404 0.28199 0.21638 0.08260  -0.03429 0.03809  161 ARG A CZ    
2646 N NH1   . ARG B 162 ? 0.20034 0.21025 0.15218 0.07572  -0.02856 0.03544  161 ARG A NH1   
2647 N NH2   . ARG B 162 ? 0.27762 0.30657 0.22620 0.08325  -0.04509 0.03175  161 ARG A NH2   
2648 N N     . GLU B 163 ? 0.17464 0.14390 0.18849 0.05422  0.00486  0.03946  162 GLU A N     
2649 C CA    . GLU B 163 ? 0.22827 0.18283 0.24753 0.04999  0.01175  0.03941  162 GLU A CA    
2650 C C     . GLU B 163 ? 0.24219 0.19454 0.26847 0.05111  0.01207  0.03480  162 GLU A C     
2651 O O     . GLU B 163 ? 0.21702 0.15469 0.24544 0.05271  0.01728  0.03627  162 GLU A O     
2652 C CB    . GLU B 163 ? 0.19375 0.14747 0.21592 0.03977  0.01286  0.03486  162 GLU A CB    
2653 C CG    . GLU B 163 ? 0.20534 0.15887 0.22148 0.03963  0.01540  0.04036  162 GLU A CG    
2654 C CD    . GLU B 163 ? 0.25465 0.19458 0.27075 0.04159  0.02349  0.04926  162 GLU A CD    
2655 O OE1   . GLU B 163 ? 0.22426 0.15387 0.24938 0.03514  0.02764  0.04783  162 GLU A OE1   
2656 O OE2   . GLU B 163 ? 0.25232 0.19155 0.25920 0.04948  0.02553  0.05775  162 GLU A OE2   
2657 N N     . ILE B 164 ? 0.21444 0.18038 0.24444 0.05034  0.00718  0.02924  163 ILE A N     
2658 C CA    . ILE B 164 ? 0.18171 0.14791 0.21751 0.05332  0.00854  0.02563  163 ILE A CA    
2659 C C     . ILE B 164 ? 0.27595 0.24030 0.31161 0.06505  0.00986  0.03184  163 ILE A C     
2660 O O     . ILE B 164 ? 0.26825 0.22179 0.30601 0.06973  0.01449  0.03130  163 ILE A O     
2661 C CB    . ILE B 164 ? 0.18297 0.16627 0.22387 0.04992  0.00409  0.02029  163 ILE A CB    
2662 C CG1   . ILE B 164 ? 0.15157 0.13398 0.19178 0.03961  0.00361  0.01479  163 ILE A CG1   
2663 C CG2   . ILE B 164 ? 0.21494 0.20186 0.26167 0.05501  0.00652  0.01797  163 ILE A CG2   
2664 C CD1   . ILE B 164 ? 0.11228 0.10934 0.15654 0.03543  -0.00021 0.01133  163 ILE A CD1   
2665 N N     . ARG B 165 ? 0.24443 0.21861 0.27663 0.07083  0.00550  0.03757  164 ARG A N     
2666 C CA    . ARG B 165 ? 0.28860 0.26352 0.31981 0.08182  0.00544  0.04356  164 ARG A CA    
2667 C C     . ARG B 165 ? 0.31763 0.27204 0.34255 0.08284  0.01180  0.04833  164 ARG A C     
2668 O O     . ARG B 165 ? 0.38588 0.33298 0.41216 0.08787  0.01467  0.04924  164 ARG A O     
2669 C CB    . ARG B 165 ? 0.21955 0.21121 0.24692 0.08554  -0.00251 0.04663  164 ARG A CB    
2670 C CG    . ARG B 165 ? 0.18475 0.19814 0.22108 0.08327  -0.00994 0.04156  164 ARG A CG    
2671 C CD    . ARG B 165 ? 0.21874 0.24682 0.25090 0.08560  -0.01917 0.04279  164 ARG A CD    
2672 N NE    . ARG B 165 ? 0.19388 0.24306 0.23742 0.08207  -0.02705 0.03767  164 ARG A NE    
2673 C CZ    . ARG B 165 ? 0.21185 0.27368 0.25327 0.08084  -0.03665 0.03579  164 ARG A CZ    
2674 N NH1   . ARG B 165 ? 0.22398 0.28031 0.25022 0.08418  -0.03925 0.03848  164 ARG A NH1   
2675 N NH2   . ARG B 165 ? 0.19688 0.27679 0.25169 0.07555  -0.04342 0.03085  164 ARG A NH2   
2676 N N     . LYS B 166 ? 0.35178 0.29698 0.37085 0.07788  0.01452  0.05151  165 LYS A N     
2677 C CA    . LYS B 166 ? 0.37849 0.30510 0.39431 0.07706  0.02126  0.05643  165 LYS A CA    
2678 C C     . LYS B 166 ? 0.41942 0.33049 0.44186 0.07216  0.02573  0.05056  165 LYS A C     
2679 O O     . LYS B 166 ? 0.41577 0.31227 0.43771 0.07406  0.02982  0.05292  165 LYS A O     
2680 C CB    . LYS B 166 ? 0.45220 0.37540 0.46267 0.07205  0.02406  0.06115  165 LYS A CB    
2681 C CG    . LYS B 166 ? 0.47621 0.40920 0.47571 0.07873  0.02141  0.06801  165 LYS A CG    
2682 C CD    . LYS B 166 ? 0.49641 0.43345 0.49051 0.07449  0.02192  0.06921  165 LYS A CD    
2683 C CE    . LYS B 166 ? 0.58950 0.51368 0.58302 0.07018  0.03105  0.07555  165 LYS A CE    
2684 N NZ    . LYS B 166 ? 0.60731 0.51975 0.61330 0.06023  0.03541  0.07129  165 LYS A NZ    
2685 N N     . HIS B 167 ? 0.42279 0.33620 0.45077 0.06605  0.02469  0.04248  166 HIS A N     
2686 C CA    . HIS B 167 ? 0.40867 0.30818 0.44091 0.06161  0.02769  0.03488  166 HIS A CA    
2687 C C     . HIS B 167 ? 0.40859 0.30654 0.44114 0.07012  0.02806  0.03250  166 HIS A C     
2688 O O     . HIS B 167 ? 0.37163 0.25276 0.40386 0.07010  0.03122  0.02985  166 HIS A O     
2689 C CB    . HIS B 167 ? 0.35278 0.25800 0.38931 0.05414  0.02586  0.02647  166 HIS A CB    
2690 C CG    . HIS B 167 ? 0.36817 0.26224 0.40672 0.05117  0.02753  0.01674  166 HIS A CG    
2691 N ND1   . HIS B 167 ? 0.39075 0.29254 0.42906 0.05590  0.02662  0.01053  166 HIS A ND1   
2692 C CD2   . HIS B 167 ? 0.39946 0.27750 0.43915 0.04338  0.02910  0.01138  166 HIS A CD2   
2693 C CE1   . HIS B 167 ? 0.36784 0.25618 0.40511 0.05288  0.02837  0.00164  166 HIS A CE1   
2694 N NE2   . HIS B 167 ? 0.40692 0.28085 0.44517 0.04469  0.02891  0.00141  166 HIS A NE2   
2695 N N     . LYS B 168 ? 0.37325 0.28932 0.40734 0.07735  0.02462  0.03330  167 LYS A N     
2696 C CA    . LYS B 168 ? 0.42009 0.33814 0.45620 0.08608  0.02537  0.03179  167 LYS A CA    
2697 C C     . LYS B 168 ? 0.47781 0.38681 0.51042 0.09306  0.02695  0.03913  167 LYS A C     
2698 O O     . LYS B 168 ? 0.49105 0.39419 0.52486 0.09974  0.02912  0.03758  167 LYS A O     
2699 C CB    . LYS B 168 ? 0.36563 0.30872 0.40743 0.09059  0.02116  0.03132  167 LYS A CB    
2700 C CG    . LYS B 168 ? 0.33017 0.28190 0.37632 0.08528  0.02112  0.02416  167 LYS A CG    
2701 C CD    . LYS B 168 ? 0.32659 0.30171 0.38088 0.09025  0.01889  0.02366  167 LYS A CD    
2702 C CE    . LYS B 168 ? 0.28627 0.28003 0.34518 0.08347  0.01393  0.02307  167 LYS A CE    
2703 N NZ    . LYS B 168 ? 0.25112 0.26967 0.32147 0.08797  0.01159  0.02411  167 LYS A NZ    
2704 N N     . GLU B 169 ? 0.45975 0.36709 0.48743 0.09235  0.02652  0.04722  168 GLU A N     
2705 C CA    . GLU B 169 ? 0.45169 0.34691 0.47511 0.09836  0.02950  0.05478  168 GLU A CA    
2706 C C     . GLU B 169 ? 0.37106 0.24127 0.39491 0.09374  0.03501  0.05207  168 GLU A C     
2707 O O     . GLU B 169 ? 0.42358 0.28075 0.44596 0.09950  0.03797  0.05577  168 GLU A O     
2708 C CB    . GLU B 169 ? 0.48505 0.38381 0.50148 0.09861  0.02894  0.06415  168 GLU A CB    
2709 C CG    . GLU B 169 ? 0.51382 0.43576 0.52802 0.10388  0.02209  0.06661  168 GLU A CG    
2710 C CD    . GLU B 169 ? 0.58894 0.51366 0.59388 0.10289  0.02155  0.07347  168 GLU A CD    
2711 O OE1   . GLU B 169 ? 0.66544 0.57672 0.66791 0.09664  0.02712  0.07595  168 GLU A OE1   
2712 O OE2   . GLU B 169 ? 0.62769 0.56868 0.62806 0.10829  0.01554  0.07600  168 GLU A OE2   
2713 N N     . VAL C 3   ? 0.51032 0.50389 0.40195 -0.02017 0.11106  0.09048  2   VAL C N     
2714 C CA    . VAL C 3   ? 0.40798 0.40521 0.32583 -0.02807 0.11165  0.09182  2   VAL C CA    
2715 C C     . VAL C 3   ? 0.36316 0.36441 0.29980 -0.02513 0.10384  0.08408  2   VAL C C     
2716 O O     . VAL C 3   ? 0.37106 0.37568 0.32946 -0.03113 0.10271  0.08357  2   VAL C O     
2717 C CB    . VAL C 3   ? 0.47180 0.48561 0.40499 -0.03490 0.12403  0.09166  2   VAL C CB    
2718 C CG1   . VAL C 3   ? 0.62179 0.63075 0.53819 -0.04011 0.13246  0.10130  2   VAL C CG1   
2719 C CG2   . VAL C 3   ? 0.51559 0.54661 0.45434 -0.02866 0.12894  0.08191  2   VAL C CG2   
2720 N N     . ASN C 4   ? 0.34381 0.34484 0.27203 -0.01637 0.09831  0.07787  3   ASN C N     
2721 C CA    . ASN C 4   ? 0.27412 0.27743 0.21804 -0.01389 0.09071  0.07201  3   ASN C CA    
2722 C C     . ASN C 4   ? 0.25933 0.24850 0.20477 -0.01629 0.08195  0.07657  3   ASN C C     
2723 O O     . ASN C 4   ? 0.26358 0.23908 0.19070 -0.01437 0.07761  0.08203  3   ASN C O     
2724 C CB    . ASN C 4   ? 0.27658 0.28042 0.20926 -0.00455 0.08633  0.06523  3   ASN C CB    
2725 C CG    . ASN C 4   ? 0.25390 0.27257 0.19321 -0.00113 0.09329  0.05779  3   ASN C CG    
2726 O OD1   . ASN C 4   ? 0.25049 0.28246 0.21095 -0.00501 0.09874  0.05603  3   ASN C OD1   
2727 N ND2   . ASN C 4   ? 0.22838 0.24471 0.14990 0.00639  0.09236  0.05274  3   ASN C ND2   
2728 N N     . PRO C 5   ? 0.25161 0.24379 0.21848 -0.01991 0.07854  0.07392  4   PRO C N     
2729 C CA    . PRO C 5   ? 0.24037 0.21861 0.20919 -0.02166 0.07061  0.07700  4   PRO C CA    
2730 C C     . PRO C 5   ? 0.23854 0.20901 0.19588 -0.01369 0.06152  0.07549  4   PRO C C     
2731 O O     . PRO C 5   ? 0.21879 0.19613 0.17275 -0.00806 0.06034  0.07042  4   PRO C O     
2732 C CB    . PRO C 5   ? 0.25600 0.24205 0.25041 -0.02713 0.06944  0.07222  4   PRO C CB    
2733 C CG    . PRO C 5   ? 0.22595 0.23042 0.23093 -0.02496 0.07322  0.06567  4   PRO C CG    
2734 C CD    . PRO C 5   ? 0.22848 0.23722 0.21868 -0.02221 0.08119  0.06749  4   PRO C CD    
2735 N N     . THR C 6   ? 0.21005 0.16593 0.16186 -0.01311 0.05480  0.07982  5   THR C N     
2736 C CA    . THR C 6   ? 0.20761 0.15686 0.15355 -0.00617 0.04486  0.07831  5   THR C CA    
2737 C C     . THR C 6   ? 0.19227 0.13664 0.15519 -0.00824 0.03985  0.07634  5   THR C C     
2738 O O     . THR C 6   ? 0.22881 0.16514 0.19774 -0.01351 0.04097  0.07926  5   THR C O     
2739 C CB    . THR C 6   ? 0.23982 0.17695 0.16472 -0.00179 0.03961  0.08432  5   THR C CB    
2740 O OG1   . THR C 6   ? 0.33433 0.27552 0.24185 -0.00042 0.04454  0.08557  5   THR C OG1   
2741 C CG2   . THR C 6   ? 0.26328 0.19724 0.18488 0.00592  0.02827  0.08152  5   THR C CG2   
2742 N N     . VAL C 7   ? 0.17359 0.12299 0.14398 -0.00443 0.03364  0.06970  6   VAL C N     
2743 C CA    . VAL C 7   ? 0.17209 0.11748 0.15634 -0.00513 0.02791  0.06565  6   VAL C CA    
2744 C C     . VAL C 7   ? 0.17952 0.12169 0.15852 0.00242  0.01853  0.06334  6   VAL C C     
2745 O O     . VAL C 7   ? 0.19843 0.14530 0.16725 0.00701  0.01529  0.06197  6   VAL C O     
2746 C CB    . VAL C 7   ? 0.23073 0.18832 0.23186 -0.00875 0.02815  0.05683  6   VAL C CB    
2747 C CG1   . VAL C 7   ? 0.21581 0.17717 0.22769 -0.01688 0.03569  0.05865  6   VAL C CG1   
2748 C CG2   . VAL C 7   ? 0.20425 0.17408 0.20279 -0.00503 0.02662  0.05100  6   VAL C CG2   
2749 N N     . PHE C 8   ? 0.17699 0.11166 0.16437 0.00365  0.01413  0.06210  7   PHE C N     
2750 C CA    . PHE C 8   ? 0.20505 0.13859 0.19196 0.01094  0.00574  0.05974  7   PHE C CA    
2751 C C     . PHE C 8   ? 0.18114 0.12079 0.18339 0.01077  0.00353  0.05061  7   PHE C C     
2752 O O     . PHE C 8   ? 0.18693 0.12414 0.19821 0.00605  0.00671  0.04796  7   PHE C O     
2753 C CB    . PHE C 8   ? 0.24521 0.16271 0.22591 0.01536  0.00232  0.06776  7   PHE C CB    
2754 C CG    . PHE C 8   ? 0.19604 0.10200 0.18764 0.01320  0.00333  0.06706  7   PHE C CG    
2755 C CD1   . PHE C 8   ? 0.23370 0.13899 0.23675 0.01810  -0.00150 0.06108  7   PHE C CD1   
2756 C CD2   . PHE C 8   ? 0.21222 0.10926 0.20243 0.00585  0.00897  0.07042  7   PHE C CD2   
2757 C CE1   . PHE C 8   ? 0.18898 0.08309 0.19965 0.01646  -0.00063 0.05811  7   PHE C CE1   
2758 C CE2   . PHE C 8   ? 0.27070 0.15642 0.26949 0.00335  0.00893  0.06784  7   PHE C CE2   
2759 C CZ    . PHE C 8   ? 0.24733 0.13094 0.25539 0.00899  0.00412  0.06135  7   PHE C CZ    
2760 N N     . PHE C 9   ? 0.17273 0.12084 0.17735 0.01538  -0.00173 0.04562  8   PHE C N     
2761 C CA    . PHE C 9   ? 0.17801 0.13086 0.19510 0.01696  -0.00379 0.03825  8   PHE C CA    
2762 C C     . PHE C 9   ? 0.16894 0.11923 0.18844 0.02456  -0.00999 0.03923  8   PHE C C     
2763 O O     . PHE C 9   ? 0.14571 0.09986 0.15931 0.02829  -0.01494 0.04158  8   PHE C O     
2764 C CB    . PHE C 9   ? 0.10768 0.07448 0.12839 0.01553  -0.00384 0.03174  8   PHE C CB    
2765 C CG    . PHE C 9   ? 0.12923 0.10059 0.15060 0.00971  0.00091  0.02943  8   PHE C CG    
2766 C CD1   . PHE C 9   ? 0.17449 0.14061 0.19685 0.00517  0.00499  0.03151  8   PHE C CD1   
2767 C CD2   . PHE C 9   ? 0.16773 0.14894 0.19017 0.00874  0.00082  0.02517  8   PHE C CD2   
2768 C CE1   . PHE C 9   ? 0.13385 0.10700 0.15936 0.00050  0.00815  0.02894  8   PHE C CE1   
2769 C CE2   . PHE C 9   ? 0.16373 0.14938 0.18729 0.00483  0.00403  0.02336  8   PHE C CE2   
2770 C CZ    . PHE C 9   ? 0.12456 0.10734 0.15027 0.00106  0.00734  0.02502  8   PHE C CZ    
2771 N N     . ASP C 10  ? 0.15679 0.10174 0.18574 0.02725  -0.01024 0.03635  9   ASP C N     
2772 C CA    . ASP C 10  ? 0.14480 0.09167 0.18143 0.03543  -0.01563 0.03487  9   ASP C CA    
2773 C C     . ASP C 10  ? 0.14356 0.10447 0.19180 0.03511  -0.01393 0.02575  9   ASP C C     
2774 O O     . ASP C 10  ? 0.15215 0.11153 0.20491 0.03252  -0.00932 0.02032  9   ASP C O     
2775 C CB    . ASP C 10  ? 0.19842 0.12890 0.23780 0.04006  -0.01642 0.03765  9   ASP C CB    
2776 C CG    . ASP C 10  ? 0.24439 0.16104 0.27025 0.04116  -0.01855 0.04804  9   ASP C CG    
2777 O OD1   . ASP C 10  ? 0.22057 0.14254 0.23777 0.04385  -0.02322 0.05244  9   ASP C OD1   
2778 O OD2   . ASP C 10  ? 0.25600 0.15702 0.27733 0.03826  -0.01523 0.05079  9   ASP C OD2   
2779 N N     . ILE C 11  ? 0.11473 0.08910 0.16668 0.03698  -0.01756 0.02414  10  ILE C N     
2780 C CA    . ILE C 11  ? 0.12342 0.11220 0.18513 0.03517  -0.01512 0.01711  10  ILE C CA    
2781 C C     . ILE C 11  ? 0.10387 0.09794 0.18024 0.04206  -0.01599 0.01314  10  ILE C C     
2782 O O     . ILE C 11  ? 0.11333 0.10582 0.19393 0.04917  -0.02195 0.01616  10  ILE C O     
2783 C CB    . ILE C 11  ? 0.09684 0.09652 0.15667 0.03251  -0.01836 0.01729  10  ILE C CB    
2784 C CG1   . ILE C 11  ? 0.15531 0.14911 0.20034 0.02743  -0.01713 0.02084  10  ILE C CG1   
2785 C CG2   . ILE C 11  ? 0.11785 0.13067 0.18768 0.02935  -0.01483 0.01131  10  ILE C CG2   
2786 C CD1   . ILE C 11  ? 0.13470 0.12619 0.17708 0.02170  -0.01034 0.01878  10  ILE C CD1   
2787 N N     . ALA C 12  ? 0.11635 0.11701 0.20002 0.04063  -0.00995 0.00645  11  ALA C N     
2788 C CA    . ALA C 12  ? 0.11713 0.12494 0.21566 0.04725  -0.00836 0.00127  11  ALA C CA    
2789 C C     . ALA C 12  ? 0.09214 0.11789 0.19948 0.04390  -0.00397 -0.00340 11  ALA C C     
2790 O O     . ALA C 12  ? 0.10529 0.13311 0.20493 0.03640  -0.00042 -0.00373 11  ALA C O     
2791 C CB    . ALA C 12  ? 0.13907 0.13492 0.23669 0.04966  -0.00345 -0.00323 11  ALA C CB    
2792 N N     . VAL C 13  ? 0.09013 0.12904 0.21459 0.04960  -0.00417 -0.00647 12  VAL C N     
2793 C CA    . VAL C 13  ? 0.09042 0.14758 0.22640 0.04630  0.00146  -0.01062 12  VAL C CA    
2794 C C     . VAL C 13  ? 0.10732 0.16704 0.24851 0.05120  0.00875  -0.01655 12  VAL C C     
2795 O O     . VAL C 13  ? 0.10773 0.16858 0.25559 0.05855  0.00601  -0.01699 12  VAL C O     
2796 C CB    . VAL C 13  ? 0.13776 0.20935 0.28408 0.04562  -0.00479 -0.00869 12  VAL C CB    
2797 C CG1   . VAL C 13  ? 0.16249 0.25127 0.31961 0.04034  0.00220  -0.01212 12  VAL C CG1   
2798 C CG2   . VAL C 13  ? 0.09995 0.16727 0.23866 0.04173  -0.01278 -0.00385 12  VAL C CG2   
2799 N N     . ASP C 14  ? 0.11561 0.17573 0.25214 0.04764  0.01800  -0.02107 13  ASP C N     
2800 C CA    . ASP C 14  ? 0.14167 0.20183 0.27858 0.05228  0.02551  -0.02758 13  ASP C CA    
2801 C C     . ASP C 14  ? 0.11762 0.16209 0.25200 0.06026  0.02134  -0.02857 13  ASP C C     
2802 O O     . ASP C 14  ? 0.17955 0.22626 0.32027 0.06742  0.02323  -0.03187 13  ASP C O     
2803 C CB    . ASP C 14  ? 0.18373 0.26313 0.33402 0.05372  0.03001  -0.02929 13  ASP C CB    
2804 C CG    . ASP C 14  ? 0.18460 0.27644 0.33466 0.04492  0.03700  -0.02877 13  ASP C CG    
2805 O OD1   . ASP C 14  ? 0.19782 0.28266 0.33518 0.03922  0.04041  -0.02869 13  ASP C OD1   
2806 O OD2   . ASP C 14  ? 0.17021 0.27840 0.33270 0.04353  0.03916  -0.02806 13  ASP C OD2   
2807 N N     . GLY C 15  ? 0.11954 0.14759 0.24489 0.05891  0.01572  -0.02488 14  GLY C N     
2808 C CA    . GLY C 15  ? 0.15468 0.16454 0.27554 0.06450  0.01177  -0.02421 14  GLY C CA    
2809 C C     . GLY C 15  ? 0.16898 0.17698 0.29389 0.06997  0.00322  -0.01732 14  GLY C C     
2810 O O     . GLY C 15  ? 0.20071 0.19098 0.31925 0.07345  -0.00042 -0.01443 14  GLY C O     
2811 N N     . GLU C 16  ? 0.12648 0.15159 0.26089 0.07046  -0.00021 -0.01454 15  GLU C N     
2812 C CA    . GLU C 16  ? 0.13508 0.15859 0.27145 0.07622  -0.00910 -0.00834 15  GLU C CA    
2813 C C     . GLU C 16  ? 0.13020 0.14712 0.25591 0.07156  -0.01611 -0.00086 15  GLU C C     
2814 O O     . GLU C 16  ? 0.16780 0.19272 0.29269 0.06453  -0.01569 -0.00067 15  GLU C O     
2815 C CB    . GLU C 16  ? 0.13364 0.17879 0.28594 0.07949  -0.01064 -0.00948 15  GLU C CB    
2816 C CG    . GLU C 16  ? 0.14430 0.19571 0.30786 0.08698  -0.00481 -0.01521 15  GLU C CG    
2817 C CD    . GLU C 16  ? 0.16430 0.20080 0.32591 0.09704  -0.00868 -0.01297 15  GLU C CD    
2818 O OE1   . GLU C 16  ? 0.17083 0.19694 0.32521 0.09893  -0.01699 -0.00567 15  GLU C OE1   
2819 O OE2   . GLU C 16  ? 0.17582 0.21036 0.34218 0.10330  -0.00299 -0.01830 15  GLU C OE2   
2820 N N     . PRO C 17  ? 0.17244 0.17484 0.28914 0.07561  -0.02218 0.00571  16  PRO C N     
2821 C CA    . PRO C 17  ? 0.16639 0.16142 0.26979 0.07135  -0.02760 0.01314  16  PRO C CA    
2822 C C     . PRO C 17  ? 0.17806 0.19025 0.28570 0.06934  -0.03321 0.01409  16  PRO C C     
2823 O O     . PRO C 17  ? 0.17480 0.19917 0.29238 0.07414  -0.03752 0.01352  16  PRO C O     
2824 C CB    . PRO C 17  ? 0.20471 0.18290 0.29851 0.07751  -0.03205 0.02017  16  PRO C CB    
2825 C CG    . PRO C 17  ? 0.27928 0.24988 0.37928 0.08298  -0.02753 0.01564  16  PRO C CG    
2826 C CD    . PRO C 17  ? 0.19975 0.19026 0.31631 0.08426  -0.02342 0.00708  16  PRO C CD    
2827 N N     . LEU C 18  ? 0.12688 0.13994 0.22761 0.06200  -0.03328 0.01523  17  LEU C N     
2828 C CA    . LEU C 18  ? 0.16120 0.18626 0.26215 0.05923  -0.03965 0.01613  17  LEU C CA    
2829 C C     . LEU C 18  ? 0.17415 0.18786 0.25690 0.06033  -0.04667 0.02371  17  LEU C C     
2830 O O     . LEU C 18  ? 0.16434 0.18379 0.24601 0.06368  -0.05436 0.02574  17  LEU C O     
2831 C CB    . LEU C 18  ? 0.13233 0.16502 0.23610 0.05092  -0.03540 0.01250  17  LEU C CB    
2832 C CG    . LEU C 18  ? 0.11864 0.16415 0.22520 0.04635  -0.04062 0.01101  17  LEU C CG    
2833 C CD1   . LEU C 18  ? 0.09547 0.15892 0.22063 0.04794  -0.04185 0.00666  17  LEU C CD1   
2834 C CD2   . LEU C 18  ? 0.10555 0.15107 0.20512 0.03663  -0.03367 0.00873  17  LEU C CD2   
2835 N N     . GLY C 19  ? 0.16017 0.15826 0.22830 0.05726  -0.04356 0.02812  18  GLY C N     
2836 C CA    . GLY C 19  ? 0.14726 0.13368 0.19566 0.05779  -0.04767 0.03595  18  GLY C CA    
2837 C C     . GLY C 19  ? 0.16396 0.13832 0.19952 0.05117  -0.04078 0.03892  18  GLY C C     
2838 O O     . GLY C 19  ? 0.14008 0.11575 0.18115 0.04594  -0.03296 0.03426  18  GLY C O     
2839 N N     . ARG C 20  ? 0.15898 0.12321 0.17572 0.05081  -0.04248 0.04625  19  ARG C N     
2840 C CA    . ARG C 20  ? 0.15993 0.11470 0.16414 0.04400  -0.03414 0.04945  19  ARG C CA    
2841 C C     . ARG C 20  ? 0.19609 0.15820 0.18978 0.03928  -0.03324 0.04738  19  ARG C C     
2842 O O     . ARG C 20  ? 0.18783 0.15466 0.17445 0.04214  -0.04061 0.04737  19  ARG C O     
2843 C CB    . ARG C 20  ? 0.21349 0.15033 0.20383 0.04641  -0.03403 0.05991  19  ARG C CB    
2844 C CG    . ARG C 20  ? 0.21386 0.14289 0.19208 0.03888  -0.02493 0.06419  19  ARG C CG    
2845 C CD    . ARG C 20  ? 0.20954 0.12027 0.17772 0.03827  -0.02314 0.07229  19  ARG C CD    
2846 N NE    . ARG C 20  ? 0.23769 0.13972 0.21808 0.03829  -0.02063 0.06968  19  ARG C NE    
2847 C CZ    . ARG C 20  ? 0.27399 0.15991 0.24954 0.03480  -0.01710 0.07416  19  ARG C CZ    
2848 N NH1   . ARG C 20  ? 0.24947 0.12759 0.20996 0.03047  -0.01526 0.08240  19  ARG C NH1   
2849 N NH2   . ARG C 20  ? 0.22881 0.10692 0.21552 0.03510  -0.01540 0.07015  19  ARG C NH2   
2850 N N     . VAL C 21  ? 0.14334 0.10660 0.13688 0.03250  -0.02496 0.04477  20  VAL C N     
2851 C CA    . VAL C 21  ? 0.15010 0.11720 0.13298 0.02858  -0.02220 0.04332  20  VAL C CA    
2852 C C     . VAL C 21  ? 0.20570 0.16433 0.17964 0.02481  -0.01395 0.04880  20  VAL C C     
2853 O O     . VAL C 21  ? 0.19907 0.15469 0.18207 0.02149  -0.00880 0.04880  20  VAL C O     
2854 C CB    . VAL C 21  ? 0.14788 0.12563 0.14142 0.02444  -0.01975 0.03524  20  VAL C CB    
2855 C CG1   . VAL C 21  ? 0.17580 0.15539 0.15858 0.02167  -0.01702 0.03357  20  VAL C CG1   
2856 C CG2   . VAL C 21  ? 0.13973 0.12710 0.14566 0.02653  -0.02613 0.03000  20  VAL C CG2   
2857 N N     . SER C 22  ? 0.16163 0.11683 0.11812 0.02507  -0.01252 0.05312  21  SER C N     
2858 C CA    . SER C 22  ? 0.16790 0.11848 0.11789 0.02060  -0.00291 0.05788  21  SER C CA    
2859 C C     . SER C 22  ? 0.16166 0.12061 0.10719 0.01826  0.00188  0.05311  21  SER C C     
2860 O O     . SER C 22  ? 0.19491 0.15860 0.13492 0.02075  -0.00288 0.04803  21  SER C O     
2861 C CB    . SER C 22  ? 0.20689 0.14512 0.13929 0.02265  -0.00201 0.06847  21  SER C CB    
2862 O OG    . SER C 22  ? 0.26305 0.20147 0.17588 0.02674  -0.00608 0.06958  21  SER C OG    
2863 N N     . PHE C 23  ? 0.15883 0.11957 0.10821 0.01354  0.01105  0.05430  22  PHE C N     
2864 C CA    . PHE C 23  ? 0.15295 0.12220 0.10142 0.01226  0.01637  0.04960  22  PHE C CA    
2865 C C     . PHE C 23  ? 0.18475 0.15276 0.12438 0.00997  0.02645  0.05562  22  PHE C C     
2866 O O     . PHE C 23  ? 0.21147 0.17490 0.15577 0.00590  0.03122  0.06199  22  PHE C O     
2867 C CB    . PHE C 23  ? 0.14115 0.11861 0.10833 0.00903  0.01774  0.04363  22  PHE C CB    
2868 C CG    . PHE C 23  ? 0.15963 0.13844 0.13667 0.01008  0.01028  0.03877  22  PHE C CG    
2869 C CD1   . PHE C 23  ? 0.18291 0.16617 0.15976 0.01208  0.00580  0.03279  22  PHE C CD1   
2870 C CD2   . PHE C 23  ? 0.20640 0.18173 0.19330 0.00871  0.00864  0.03986  22  PHE C CD2   
2871 C CE1   . PHE C 23  ? 0.16835 0.15412 0.15510 0.01218  0.00065  0.02895  22  PHE C CE1   
2872 C CE2   . PHE C 23  ? 0.16215 0.14015 0.15808 0.00994  0.00353  0.03507  22  PHE C CE2   
2873 C CZ    . PHE C 23  ? 0.18521 0.16925 0.18133 0.01141  -0.00005 0.03011  22  PHE C CZ    
2874 N N     . GLU C 24  ? 0.17530 0.14686 0.10218 0.01238  0.03017  0.05344  23  GLU C N     
2875 C CA    . GLU C 24  ? 0.18903 0.16498 0.11312 0.01000  0.04221  0.05650  23  GLU C CA    
2876 C C     . GLU C 24  ? 0.20368 0.19192 0.14738 0.00799  0.04596  0.04995  23  GLU C C     
2877 O O     . GLU C 24  ? 0.16944 0.16152 0.11653 0.01109  0.04106  0.04220  23  GLU C O     
2878 C CB    . GLU C 24  ? 0.27568 0.25006 0.17598 0.01456  0.04547  0.05619  23  GLU C CB    
2879 C CG    . GLU C 24  ? 0.24566 0.22656 0.14445 0.01220  0.05910  0.05856  23  GLU C CG    
2880 C CD    . GLU C 24  ? 0.29522 0.27620 0.17275 0.01690  0.06160  0.05445  23  GLU C CD    
2881 O OE1   . GLU C 24  ? 0.29943 0.27338 0.15982 0.02185  0.05278  0.05136  23  GLU C OE1   
2882 O OE2   . GLU C 24  ? 0.28538 0.27404 0.16432 0.01545  0.07183  0.05354  23  GLU C OE2   
2883 N N     . LEU C 25  ? 0.16286 0.15687 0.12021 0.00260  0.05387  0.05335  24  LEU C N     
2884 C CA    . LEU C 25  ? 0.20964 0.21690 0.18664 0.00105  0.05673  0.04786  24  LEU C CA    
2885 C C     . LEU C 25  ? 0.17281 0.18986 0.14805 0.00219  0.06819  0.04796  24  LEU C C     
2886 O O     . LEU C 25  ? 0.19774 0.21429 0.16853 -0.00149 0.07585  0.05378  24  LEU C O     
2887 C CB    . LEU C 25  ? 0.15742 0.16716 0.15423 -0.00593 0.05649  0.04980  24  LEU C CB    
2888 C CG    . LEU C 25  ? 0.17860 0.17833 0.17761 -0.00702 0.04707  0.04960  24  LEU C CG    
2889 C CD1   . LEU C 25  ? 0.12529 0.12809 0.14370 -0.01365 0.04665  0.04885  24  LEU C CD1   
2890 C CD2   . LEU C 25  ? 0.13806 0.13742 0.13416 -0.00171 0.03832  0.04296  24  LEU C CD2   
2891 N N     . PHE C 26  ? 0.17239 0.19767 0.15188 0.00722  0.06816  0.04038  25  PHE C N     
2892 C CA    . PHE C 26  ? 0.16026 0.19486 0.13702 0.01067  0.07904  0.03864  25  PHE C CA    
2893 C C     . PHE C 26  ? 0.17990 0.22993 0.18084 0.00588  0.08493  0.03864  25  PHE C C     
2894 O O     . PHE C 26  ? 0.17669 0.23863 0.19116 0.00959  0.08632  0.03285  25  PHE C O     
2895 C CB    . PHE C 26  ? 0.17285 0.20737 0.14452 0.01871  0.07518  0.02950  25  PHE C CB    
2896 C CG    . PHE C 26  ? 0.16591 0.18607 0.11582 0.02211  0.06687  0.02709  25  PHE C CG    
2897 C CD1   . PHE C 26  ? 0.19588 0.20679 0.12500 0.02125  0.06743  0.03255  25  PHE C CD1   
2898 C CD2   . PHE C 26  ? 0.16684 0.18278 0.11740 0.02603  0.05809  0.01960  25  PHE C CD2   
2899 C CE1   . PHE C 26  ? 0.24754 0.24728 0.15835 0.02450  0.05821  0.02969  25  PHE C CE1   
2900 C CE2   . PHE C 26  ? 0.20171 0.20613 0.13507 0.02814  0.05004  0.01666  25  PHE C CE2   
2901 C CZ    . PHE C 26  ? 0.22469 0.22203 0.13894 0.02747  0.04949  0.02129  25  PHE C CZ    
2902 N N     . ALA C 27  ? 0.19075 0.23970 0.19711 -0.00247 0.08692  0.04460  26  ALA C N     
2903 C CA    . ALA C 27  ? 0.18676 0.25042 0.21516 -0.00822 0.09145  0.04388  26  ALA C CA    
2904 C C     . ALA C 27  ? 0.18732 0.26235 0.21461 -0.00556 0.10109  0.04126  26  ALA C C     
2905 O O     . ALA C 27  ? 0.16631 0.25770 0.21430 -0.00724 0.10404  0.03804  26  ALA C O     
2906 C CB    . ALA C 27  ? 0.17202 0.23020 0.20436 -0.01816 0.09209  0.05046  26  ALA C CB    
2907 N N     . ASP C 28  ? 0.18811 0.25544 0.19166 -0.00127 0.10552  0.04203  27  ASP C N     
2908 C CA    . ASP C 28  ? 0.24332 0.32121 0.24445 0.00170  0.11528  0.03860  27  ASP C CA    
2909 C C     . ASP C 28  ? 0.27025 0.35891 0.28346 0.01000  0.11441  0.02927  27  ASP C C     
2910 O O     . ASP C 28  ? 0.29750 0.40111 0.32230 0.01132  0.12166  0.02545  27  ASP C O     
2911 C CB    . ASP C 28  ? 0.22672 0.29266 0.19709 0.00469  0.11890  0.04066  27  ASP C CB    
2912 C CG    . ASP C 28  ? 0.25787 0.30976 0.20880 0.01238  0.11042  0.03704  27  ASP C CG    
2913 O OD1   . ASP C 28  ? 0.22209 0.27025 0.18092 0.01366  0.10182  0.03580  27  ASP C OD1   
2914 O OD2   . ASP C 28  ? 0.29596 0.34072 0.22292 0.01674  0.11219  0.03521  27  ASP C OD2   
2915 N N     . LYS C 29  ? 0.21813 0.29979 0.23012 0.01567  0.10556  0.02564  28  LYS C N     
2916 C CA    . LYS C 29  ? 0.25972 0.34811 0.28106 0.02428  0.10379  0.01726  28  LYS C CA    
2917 C C     . LYS C 29  ? 0.17125 0.26616 0.21529 0.02417  0.09546  0.01600  28  LYS C C     
2918 O O     . LYS C 29  ? 0.20513 0.30914 0.26281 0.03022  0.09414  0.01018  28  LYS C O     
2919 C CB    . LYS C 29  ? 0.28196 0.35559 0.28014 0.03258  0.10047  0.01242  28  LYS C CB    
2920 C CG    . LYS C 29  ? 0.33607 0.41114 0.32321 0.03913  0.10767  0.00559  28  LYS C CG    
2921 C CD    . LYS C 29  ? 0.42626 0.49208 0.38608 0.03728  0.11244  0.00827  28  LYS C CD    
2922 C CE    . LYS C 29  ? 0.48946 0.55477 0.43581 0.04454  0.11836  -0.00031 28  LYS C CE    
2923 N NZ    . LYS C 29  ? 0.49960 0.55390 0.41526 0.04376  0.12060  0.00120  28  LYS C NZ    
2924 N N     . VAL C 30  ? 0.13748 0.22723 0.18497 0.01793  0.08926  0.02104  29  VAL C N     
2925 C CA    . VAL C 30  ? 0.11880 0.21302 0.18424 0.01751  0.08025  0.01985  29  VAL C CA    
2926 C C     . VAL C 30  ? 0.15725 0.25457 0.23473 0.00685  0.07838  0.02467  29  VAL C C     
2927 O O     . VAL C 30  ? 0.13702 0.22531 0.21233 0.00336  0.07197  0.02736  29  VAL C O     
2928 C CB    . VAL C 30  ? 0.20216 0.28179 0.25484 0.02174  0.07135  0.01837  29  VAL C CB    
2929 C CG1   . VAL C 30  ? 0.20041 0.28424 0.26723 0.02517  0.06234  0.01448  29  VAL C CG1   
2930 C CG2   . VAL C 30  ? 0.17741 0.24567 0.20749 0.02878  0.07342  0.01467  29  VAL C CG2   
2931 N N     . PRO C 31  ? 0.14623 0.25607 0.23700 0.00134  0.08374  0.02522  30  PRO C N     
2932 C CA    . PRO C 31  ? 0.13779 0.24643 0.23536 -0.00966 0.08323  0.02996  30  PRO C CA    
2933 C C     . PRO C 31  ? 0.10704 0.21607 0.21819 -0.01348 0.07279  0.02863  30  PRO C C     
2934 O O     . PRO C 31  ? 0.13030 0.22796 0.23725 -0.01994 0.06994  0.03219  30  PRO C O     
2935 C CB    . PRO C 31  ? 0.13179 0.25724 0.24341 -0.01379 0.09114  0.02945  30  PRO C CB    
2936 C CG    . PRO C 31  ? 0.12888 0.26821 0.24924 -0.00425 0.09205  0.02273  30  PRO C CG    
2937 C CD    . PRO C 31  ? 0.13389 0.25886 0.23312 0.00471  0.09128  0.02147  30  PRO C CD    
2938 N N     . LYS C 32  ? 0.11304 0.23431 0.23964 -0.00952 0.06664  0.02341  31  LYS C N     
2939 C CA    . LYS C 32  ? 0.09457 0.21715 0.23265 -0.01356 0.05622  0.02164  31  LYS C CA    
2940 C C     . LYS C 32  ? 0.14858 0.25602 0.27432 -0.01129 0.04965  0.02258  31  LYS C C     
2941 O O     . LYS C 32  ? 0.09359 0.19470 0.22106 -0.01721 0.04379  0.02287  31  LYS C O     
2942 C CB    . LYS C 32  ? 0.12019 0.25981 0.27568 -0.00893 0.05024  0.01635  31  LYS C CB    
2943 C CG    . LYS C 32  ? 0.17814 0.33622 0.34786 -0.00900 0.05673  0.01459  31  LYS C CG    
2944 C CD    . LYS C 32  ? 0.21928 0.39257 0.40341 -0.00108 0.04984  0.00951  31  LYS C CD    
2945 C CE    . LYS C 32  ? 0.25253 0.44679 0.45284 -0.00014 0.05626  0.00736  31  LYS C CE    
2946 N NZ    . LYS C 32  ? 0.35868 0.56467 0.57404 -0.01154 0.05658  0.00873  31  LYS C NZ    
2947 N N     . THR C 33  ? 0.07606 0.17762 0.18935 -0.00274 0.05026  0.02223  32  THR C N     
2948 C CA    . THR C 33  ? 0.09100 0.17552 0.18711 -0.00094 0.04209  0.02132  32  THR C CA    
2949 C C     . THR C 33  ? 0.09514 0.16517 0.17710 -0.00572 0.04441  0.02547  32  THR C C     
2950 O O     . THR C 33  ? 0.08973 0.14987 0.16712 -0.00855 0.03800  0.02527  32  THR C O     
2951 C CB    . THR C 33  ? 0.09974 0.17919 0.18429 0.00839  0.04073  0.01856  32  THR C CB    
2952 O OG1   . THR C 33  ? 0.09466 0.18704 0.19334 0.01398  0.03912  0.01551  32  THR C OG1   
2953 C CG2   . THR C 33  ? 0.10364 0.16854 0.17490 0.00938  0.03218  0.01748  32  THR C CG2   
2954 N N     . ALA C 34  ? 0.10113 0.16994 0.17600 -0.00630 0.05376  0.02946  33  ALA C N     
2955 C CA    . ALA C 34  ? 0.09787 0.15235 0.15894 -0.01018 0.05531  0.03468  33  ALA C CA    
2956 C C     . ALA C 34  ? 0.14349 0.19618 0.21619 -0.01919 0.05426  0.03730  33  ALA C C     
2957 O O     . ALA C 34  ? 0.10149 0.13999 0.16582 -0.02127 0.05025  0.03933  33  ALA C O     
2958 C CB    . ALA C 34  ? 0.11296 0.16665 0.16210 -0.00893 0.06589  0.03925  33  ALA C CB    
2959 N N     . GLU C 35  ? 0.11022 0.17633 0.20172 -0.02421 0.05644  0.03592  34  GLU C N     
2960 C CA    . GLU C 35  ? 0.12725 0.18993 0.22789 -0.03330 0.05398  0.03631  34  GLU C CA    
2961 C C     . GLU C 35  ? 0.12075 0.17917 0.22686 -0.03448 0.04414  0.03216  34  GLU C C     
2962 O O     . GLU C 35  ? 0.11966 0.16589 0.22440 -0.03973 0.04138  0.03279  34  GLU C O     
2963 C CB    . GLU C 35  ? 0.10758 0.18662 0.22531 -0.03824 0.05706  0.03427  34  GLU C CB    
2964 C CG    . GLU C 35  ? 0.13658 0.21443 0.26645 -0.04798 0.05300  0.03290  34  GLU C CG    
2965 C CD    . GLU C 35  ? 0.14786 0.20737 0.26750 -0.05407 0.05612  0.03869  34  GLU C CD    
2966 O OE1   . GLU C 35  ? 0.17942 0.22966 0.28312 -0.05135 0.06222  0.04466  34  GLU C OE1   
2967 O OE2   . GLU C 35  ? 0.13717 0.19100 0.26408 -0.06136 0.05192  0.03708  34  GLU C OE2   
2968 N N     . ASN C 36  ? 0.08089 0.14759 0.19039 -0.02894 0.03803  0.02707  35  ASN C N     
2969 C CA    . ASN C 36  ? 0.10113 0.16151 0.20728 -0.02811 0.02787  0.02213  35  ASN C CA    
2970 C C     . ASN C 36  ? 0.11981 0.16184 0.20845 -0.02625 0.02645  0.02374  35  ASN C C     
2971 O O     . ASN C 36  ? 0.08209 0.11438 0.17044 -0.03018 0.02314  0.02242  35  ASN C O     
2972 C CB    . ASN C 36  ? 0.06895 0.13790 0.17485 -0.02076 0.02248  0.01820  35  ASN C CB    
2973 C CG    . ASN C 36  ? 0.07036 0.13397 0.17113 -0.01993 0.01300  0.01373  35  ASN C CG    
2974 O OD1   . ASN C 36  ? 0.06584 0.13023 0.17367 -0.02536 0.00841  0.01052  35  ASN C OD1   
2975 N ND2   . ASN C 36  ? 0.11310 0.17033 0.20050 -0.01356 0.01053  0.01336  35  ASN C ND2   
2976 N N     . PHE C 37  ? 0.07804 0.11542 0.15290 -0.02008 0.02883  0.02611  36  PHE C N     
2977 C CA    . PHE C 37  ? 0.08161 0.10457 0.14211 -0.01749 0.02646  0.02735  36  PHE C CA    
2978 C C     . PHE C 37  ? 0.09214 0.10388 0.15054 -0.02195 0.02960  0.03234  36  PHE C C     
2979 O O     . PHE C 37  ? 0.11166 0.11216 0.16601 -0.02177 0.02570  0.03171  36  PHE C O     
2980 C CB    . PHE C 37  ? 0.10470 0.12644 0.15248 -0.01093 0.02781  0.02844  36  PHE C CB    
2981 C CG    . PHE C 37  ? 0.10249 0.11378 0.13891 -0.00759 0.02326  0.02809  36  PHE C CG    
2982 C CD1   . PHE C 37  ? 0.12697 0.12839 0.15442 -0.00726 0.02433  0.03261  36  PHE C CD1   
2983 C CD2   . PHE C 37  ? 0.11890 0.13090 0.15423 -0.00472 0.01798  0.02376  36  PHE C CD2   
2984 C CE1   . PHE C 37  ? 0.13795 0.13235 0.15788 -0.00362 0.01935  0.03195  36  PHE C CE1   
2985 C CE2   . PHE C 37  ? 0.13723 0.14233 0.16538 -0.00222 0.01446  0.02323  36  PHE C CE2   
2986 C CZ    . PHE C 37  ? 0.11269 0.11004 0.13436 -0.00143 0.01475  0.02691  36  PHE C CZ    
2987 N N     . ARG C 38  ? 0.11857 0.13277 0.17983 -0.02572 0.03719  0.03766  37  ARG C N     
2988 C CA    . ARG C 38  ? 0.13047 0.13222 0.18978 -0.03084 0.04076  0.04391  37  ARG C CA    
2989 C C     . ARG C 38  ? 0.16377 0.15980 0.23459 -0.03695 0.03639  0.04044  37  ARG C C     
2990 O O     . ARG C 38  ? 0.12760 0.10796 0.19291 -0.03674 0.03357  0.04158  37  ARG C O     
2991 C CB    . ARG C 38  ? 0.13194 0.13967 0.19341 -0.03503 0.05004  0.04917  37  ARG C CB    
2992 C CG    . ARG C 38  ? 0.16287 0.15526 0.21423 -0.03850 0.05278  0.05590  37  ARG C CG    
2993 C CD    . ARG C 38  ? 0.16046 0.15944 0.21705 -0.04539 0.06032  0.05882  37  ARG C CD    
2994 N NE    . ARG C 38  ? 0.16939 0.17892 0.24669 -0.05243 0.05865  0.05341  37  ARG C NE    
2995 C CZ    . ARG C 38  ? 0.18365 0.18427 0.26837 -0.05849 0.05406  0.05146  37  ARG C CZ    
2996 N NH1   . ARG C 38  ? 0.19577 0.17632 0.27021 -0.05801 0.05123  0.05456  37  ARG C NH1   
2997 N NH2   . ARG C 38  ? 0.15667 0.16864 0.25929 -0.06465 0.05163  0.04575  37  ARG C NH2   
2998 N N     . ALA C 39  ? 0.11997 0.12860 0.20712 -0.04195 0.03519  0.03553  38  ALA C N     
2999 C CA    . ALA C 39  ? 0.12747 0.13100 0.22427 -0.04839 0.03031  0.03061  38  ALA C CA    
3000 C C     . ALA C 39  ? 0.11457 0.11028 0.20522 -0.04399 0.02238  0.02420  38  ALA C C     
3001 O O     . ALA C 39  ? 0.14348 0.12559 0.23440 -0.04673 0.01965  0.02181  38  ALA C O     
3002 C CB    . ALA C 39  ? 0.11260 0.13356 0.22541 -0.05342 0.02874  0.02566  38  ALA C CB    
3003 N N     . LEU C 40  ? 0.11261 0.11586 0.19637 -0.03676 0.01904  0.02107  39  LEU C N     
3004 C CA    . LEU C 40  ? 0.13091 0.12767 0.20673 -0.03219 0.01315  0.01561  39  LEU C CA    
3005 C C     . LEU C 40  ? 0.11572 0.09715 0.18172 -0.02850 0.01417  0.01894  39  LEU C C     
3006 O O     . LEU C 40  ? 0.14634 0.11921 0.20992 -0.02672 0.01077  0.01440  39  LEU C O     
3007 C CB    . LEU C 40  ? 0.09713 0.10411 0.16760 -0.02606 0.01052  0.01326  39  LEU C CB    
3008 C CG    . LEU C 40  ? 0.10495 0.12660 0.18450 -0.02768 0.00740  0.00966  39  LEU C CG    
3009 C CD1   . LEU C 40  ? 0.12619 0.15437 0.19910 -0.02111 0.00530  0.00911  39  LEU C CD1   
3010 C CD2   . LEU C 40  ? 0.16662 0.18751 0.25140 -0.03229 0.00140  0.00271  39  LEU C CD2   
3011 N N     . SER C 41  ? 0.12315 0.10114 0.18328 -0.02687 0.01872  0.02665  40  SER C N     
3012 C CA    . SER C 41  ? 0.15964 0.12411 0.21030 -0.02227 0.01823  0.03058  40  SER C CA    
3013 C C     . SER C 41  ? 0.14138 0.09001 0.19544 -0.02645 0.01907  0.03301  40  SER C C     
3014 O O     . SER C 41  ? 0.16337 0.09979 0.21389 -0.02221 0.01617  0.03232  40  SER C O     
3015 C CB    . SER C 41  ? 0.17227 0.13792 0.21256 -0.01865 0.02151  0.03775  40  SER C CB    
3016 O OG    . SER C 41  ? 0.11610 0.09275 0.15266 -0.01422 0.01987  0.03458  40  SER C OG    
3017 N N     . THR C 42  ? 0.13875 0.08724 0.20117 -0.03480 0.02313  0.03569  41  THR C N     
3018 C CA    . THR C 42  ? 0.19458 0.12706 0.25955 -0.03969 0.02339  0.03700  41  THR C CA    
3019 C C     . THR C 42  ? 0.18575 0.11430 0.25943 -0.04277 0.01831  0.02693  41  THR C C     
3020 O O     . THR C 42  ? 0.22738 0.13984 0.29933 -0.04360 0.01668  0.02565  41  THR C O     
3021 C CB    . THR C 42  ? 0.20299 0.13872 0.27061 -0.04752 0.02882  0.04191  41  THR C CB    
3022 O OG1   . THR C 42  ? 0.17454 0.12669 0.25598 -0.05353 0.02858  0.03605  41  THR C OG1   
3023 C CG2   . THR C 42  ? 0.19268 0.13215 0.24935 -0.04469 0.03463  0.05092  41  THR C CG2   
3024 N N     . GLY C 43  ? 0.14401 0.08672 0.22421 -0.04378 0.01519  0.01926  42  GLY C N     
3025 C CA    . GLY C 43  ? 0.14790 0.08826 0.23448 -0.04756 0.00997  0.00896  42  GLY C CA    
3026 C C     . GLY C 43  ? 0.17277 0.11389 0.26846 -0.05734 0.00979  0.00733  42  GLY C C     
3027 O O     . GLY C 43  ? 0.23755 0.17276 0.33580 -0.06067 0.00493  -0.00122 42  GLY C O     
3028 N N     . GLU C 44  ? 0.16166 0.11053 0.26114 -0.06184 0.01500  0.01470  43  GLU C N     
3029 C CA    . GLU C 44  ? 0.17743 0.12487 0.28488 -0.07149 0.01575  0.01448  43  GLU C CA    
3030 C C     . GLU C 44  ? 0.19198 0.15397 0.31163 -0.07706 0.00998  0.00539  43  GLU C C     
3031 O O     . GLU C 44  ? 0.18849 0.14807 0.31551 -0.08555 0.00859  0.00295  43  GLU C O     
3032 C CB    . GLU C 44  ? 0.21765 0.17096 0.32572 -0.07475 0.02375  0.02450  43  GLU C CB    
3033 C CG    . GLU C 44  ? 0.16408 0.14017 0.27729 -0.07244 0.02651  0.02571  43  GLU C CG    
3034 C CD    . GLU C 44  ? 0.26013 0.23949 0.36900 -0.07312 0.03552  0.03539  43  GLU C CD    
3035 O OE1   . GLU C 44  ? 0.20641 0.17365 0.30071 -0.06790 0.03856  0.04208  43  GLU C OE1   
3036 O OE2   . GLU C 44  ? 0.17226 0.16651 0.29185 -0.07872 0.03927  0.03606  43  GLU C OE2   
3037 N N     . LYS C 45  ? 0.15789 0.13481 0.27943 -0.07263 0.00607  0.00071  44  LYS C N     
3038 C CA    . LYS C 45  ? 0.15321 0.14421 0.28377 -0.07620 -0.00128 -0.00792 44  LYS C CA    
3039 C C     . LYS C 45  ? 0.21430 0.19464 0.33843 -0.07524 -0.00916 -0.01849 44  LYS C C     
3040 O O     . LYS C 45  ? 0.17175 0.16180 0.29976 -0.07783 -0.01665 -0.02637 44  LYS C O     
3041 C CB    . LYS C 45  ? 0.16922 0.18114 0.30339 -0.07107 -0.00236 -0.00737 44  LYS C CB    
3042 C CG    . LYS C 45  ? 0.15164 0.17521 0.29071 -0.07039 0.00588  0.00156  44  LYS C CG    
3043 C CD    . LYS C 45  ? 0.17581 0.20801 0.32782 -0.07903 0.00822  0.00281  44  LYS C CD    
3044 C CE    . LYS C 45  ? 0.22905 0.27543 0.38566 -0.07747 0.01683  0.01013  44  LYS C CE    
3045 N NZ    . LYS C 45  ? 0.27210 0.32672 0.44164 -0.08656 0.02083  0.01216  44  LYS C NZ    
3046 N N     . GLY C 46  ? 0.20218 0.16325 0.31558 -0.07080 -0.00776 -0.01907 45  GLY C N     
3047 C CA    . GLY C 46  ? 0.25629 0.20692 0.36155 -0.06831 -0.01373 -0.02987 45  GLY C CA    
3048 C C     . GLY C 46  ? 0.25747 0.21275 0.35444 -0.06012 -0.01576 -0.03395 45  GLY C C     
3049 O O     . GLY C 46  ? 0.30560 0.25501 0.39310 -0.05728 -0.02016 -0.04369 45  GLY C O     
3050 N N     . PHE C 47  ? 0.16832 0.13522 0.26209 -0.05447 -0.01186 -0.02571 46  PHE C N     
3051 C CA    . PHE C 47  ? 0.13957 0.11130 0.21929 -0.04491 -0.01185 -0.02595 46  PHE C CA    
3052 C C     . PHE C 47  ? 0.13727 0.11253 0.21511 -0.04013 -0.00570 -0.01537 46  PHE C C     
3053 O O     . PHE C 47  ? 0.15078 0.12841 0.23681 -0.04391 -0.00186 -0.00841 46  PHE C O     
3054 C CB    . PHE C 47  ? 0.12924 0.11645 0.20607 -0.04415 -0.01800 -0.03075 46  PHE C CB    
3055 C CG    . PHE C 47  ? 0.17656 0.18030 0.26699 -0.04860 -0.01965 -0.02713 46  PHE C CG    
3056 C CD1   . PHE C 47  ? 0.16902 0.18362 0.26008 -0.04415 -0.01590 -0.01926 46  PHE C CD1   
3057 C CD2   . PHE C 47  ? 0.17294 0.18173 0.27679 -0.05710 -0.02503 -0.03236 46  PHE C CD2   
3058 C CE1   . PHE C 47  ? 0.13856 0.16938 0.24355 -0.04696 -0.01666 -0.01658 46  PHE C CE1   
3059 C CE2   . PHE C 47  ? 0.20469 0.23174 0.32446 -0.06075 -0.02632 -0.02934 46  PHE C CE2   
3060 C CZ    . PHE C 47  ? 0.14006 0.17813 0.26031 -0.05505 -0.02161 -0.02136 46  PHE C CZ    
3061 N N     . GLY C 48  ? 0.14267 0.11837 0.20947 -0.03220 -0.00451 -0.01450 47  GLY C N     
3062 C CA    . GLY C 48  ? 0.11124 0.09116 0.17556 -0.02793 -0.00026 -0.00599 47  GLY C CA    
3063 C C     . GLY C 48  ? 0.14009 0.11650 0.19484 -0.02039 0.00085  -0.00597 47  GLY C C     
3064 O O     . GLY C 48  ? 0.13327 0.10862 0.18271 -0.01790 -0.00082 -0.01227 47  GLY C O     
3065 N N     . TYR C 49  ? 0.13664 0.11219 0.18946 -0.01705 0.00383  0.00103  48  TYR C N     
3066 C CA    . TYR C 49  ? 0.11129 0.08845 0.15793 -0.01060 0.00433  0.00190  48  TYR C CA    
3067 C C     . TYR C 49  ? 0.12731 0.09482 0.17339 -0.00648 0.00445  -0.00064 48  TYR C C     
3068 O O     . TYR C 49  ? 0.09852 0.06986 0.14227 -0.00169 0.00478  -0.00215 48  TYR C O     
3069 C CB    . TYR C 49  ? 0.10044 0.08010 0.14489 -0.00859 0.00610  0.00925  48  TYR C CB    
3070 C CG    . TYR C 49  ? 0.10857 0.09859 0.15297 -0.01008 0.00671  0.01110  48  TYR C CG    
3071 C CD1   . TYR C 49  ? 0.13959 0.13756 0.18278 -0.00951 0.00482  0.00763  48  TYR C CD1   
3072 C CD2   . TYR C 49  ? 0.14821 0.13947 0.19307 -0.01139 0.00961  0.01657  48  TYR C CD2   
3073 C CE1   . TYR C 49  ? 0.12363 0.12992 0.16766 -0.00952 0.00496  0.00938  48  TYR C CE1   
3074 C CE2   . TYR C 49  ? 0.13080 0.13171 0.17669 -0.01148 0.01078  0.01742  48  TYR C CE2   
3075 C CZ    . TYR C 49  ? 0.09583 0.10393 0.14213 -0.01021 0.00806  0.01373  48  TYR C CZ    
3076 O OH    . TYR C 49  ? 0.09420 0.11074 0.14235 -0.00901 0.00892  0.01470  48  TYR C OH    
3077 N N     . LYS C 50  ? 0.16466 0.11978 0.21411 -0.00809 0.00446  -0.00093 49  LYS C N     
3078 C CA    . LYS C 50  ? 0.12004 0.06472 0.17002 -0.00245 0.00447  -0.00243 49  LYS C CA    
3079 C C     . LYS C 50  ? 0.15032 0.09765 0.19889 0.00077  0.00460  -0.01168 49  LYS C C     
3080 O O     . LYS C 50  ? 0.12694 0.07249 0.17414 -0.00278 0.00373  -0.01878 49  LYS C O     
3081 C CB    . LYS C 50  ? 0.15663 0.08440 0.21012 -0.00512 0.00439  -0.00096 49  LYS C CB    
3082 C CG    . LYS C 50  ? 0.22499 0.13989 0.27964 0.00245  0.00388  -0.00126 49  LYS C CG    
3083 C CD    . LYS C 50  ? 0.21857 0.11377 0.27569 -0.00056 0.00383  0.00217  49  LYS C CD    
3084 C CE    . LYS C 50  ? 0.34710 0.22791 0.40561 0.00824  0.00263  0.00273  49  LYS C CE    
3085 N NZ    . LYS C 50  ? 0.39191 0.25518 0.44716 0.00475  0.00250  0.00859  49  LYS C NZ    
3086 N N     . GLY C 51  ? 0.16226 0.11476 0.21109 0.00736  0.00575  -0.01180 50  GLY C N     
3087 C CA    . GLY C 51  ? 0.15913 0.11665 0.20655 0.01083  0.00792  -0.01954 50  GLY C CA    
3088 C C     . GLY C 51  ? 0.14280 0.11506 0.18611 0.00984  0.00942  -0.01892 50  GLY C C     
3089 O O     . GLY C 51  ? 0.15466 0.13322 0.19791 0.01337  0.01265  -0.02261 50  GLY C O     
3090 N N     . SER C 52  ? 0.13697 0.11445 0.17737 0.00526  0.00775  -0.01418 51  SER C N     
3091 C CA    . SER C 52  ? 0.12983 0.11803 0.16546 0.00417  0.00877  -0.01332 51  SER C CA    
3092 C C     . SER C 52  ? 0.11532 0.11007 0.15482 0.00707  0.00997  -0.00910 51  SER C C     
3093 O O     . SER C 52  ? 0.14260 0.13502 0.18783 0.01015  0.00886  -0.00646 51  SER C O     
3094 C CB    . SER C 52  ? 0.11364 0.10461 0.14634 -0.00046 0.00614  -0.01020 51  SER C CB    
3095 O OG    . SER C 52  ? 0.10855 0.09861 0.14506 -0.00109 0.00523  -0.00402 51  SER C OG    
3096 N N     . SER C 53  ? 0.10979 0.11233 0.14592 0.00585  0.01164  -0.00834 52  SER C N     
3097 C CA    . SER C 53  ? 0.12171 0.13124 0.16306 0.00738  0.01308  -0.00608 52  SER C CA    
3098 C C     . SER C 53  ? 0.10187 0.11370 0.14114 0.00472  0.01087  -0.00096 52  SER C C     
3099 O O     . SER C 53  ? 0.11445 0.12422 0.14775 0.00234  0.00941  0.00067  52  SER C O     
3100 C CB    . SER C 53  ? 0.16827 0.18427 0.20870 0.00760  0.01842  -0.00942 52  SER C CB    
3101 O OG    . SER C 53  ? 0.21208 0.22881 0.24264 0.00389  0.01906  -0.00774 52  SER C OG    
3102 N N     . PHE C 54  ? 0.10493 0.12127 0.15026 0.00556  0.01014  0.00088  53  PHE C N     
3103 C CA    . PHE C 54  ? 0.11030 0.12869 0.15390 0.00284  0.00888  0.00392  53  PHE C CA    
3104 C C     . PHE C 54  ? 0.09460 0.11830 0.13903 0.00039  0.01328  0.00319  53  PHE C C     
3105 O O     . PHE C 54  ? 0.09343 0.12413 0.14706 0.00061  0.01526  0.00199  53  PHE C O     
3106 C CB    . PHE C 54  ? 0.09791 0.11784 0.14682 0.00419  0.00484  0.00545  53  PHE C CB    
3107 C CG    . PHE C 54  ? 0.11000 0.12365 0.15378 0.00582  0.00141  0.00783  53  PHE C CG    
3108 C CD1   . PHE C 54  ? 0.10581 0.11525 0.15065 0.00882  0.00063  0.00826  53  PHE C CD1   
3109 C CD2   . PHE C 54  ? 0.11761 0.12861 0.15500 0.00445  -0.00025 0.00977  53  PHE C CD2   
3110 C CE1   . PHE C 54  ? 0.11775 0.12087 0.15688 0.00949  -0.00118 0.01169  53  PHE C CE1   
3111 C CE2   . PHE C 54  ? 0.12826 0.13450 0.16005 0.00587  -0.00164 0.01215  53  PHE C CE2   
3112 C CZ    . PHE C 54  ? 0.11029 0.11278 0.14269 0.00791  -0.00181 0.01368  53  PHE C CZ    
3113 N N     . HIS C 55  ? 0.11485 0.13577 0.15000 -0.00184 0.01491  0.00431  54  HIS C N     
3114 C CA    . HIS C 55  ? 0.12161 0.14535 0.15311 -0.00423 0.02010  0.00470  54  HIS C CA    
3115 C C     . HIS C 55  ? 0.10265 0.12631 0.13538 -0.00813 0.02072  0.00868  54  HIS C C     
3116 O O     . HIS C 55  ? 0.16074 0.18743 0.19305 -0.01111 0.02623  0.01002  54  HIS C O     
3117 C CB    . HIS C 55  ? 0.12679 0.14623 0.14522 -0.00427 0.02022  0.00461  54  HIS C CB    
3118 C CG    . HIS C 55  ? 0.13438 0.14863 0.14724 -0.00473 0.01548  0.00812  54  HIS C CG    
3119 N ND1   . HIS C 55  ? 0.11653 0.12885 0.13147 -0.00312 0.01104  0.00745  54  HIS C ND1   
3120 C CD2   . HIS C 55  ? 0.12623 0.13683 0.13251 -0.00616 0.01496  0.01250  54  HIS C CD2   
3121 C CE1   . HIS C 55  ? 0.12392 0.13356 0.13506 -0.00304 0.00823  0.01050  54  HIS C CE1   
3122 N NE2   . HIS C 55  ? 0.09108 0.09869 0.09662 -0.00440 0.00996  0.01357  54  HIS C NE2   
3123 N N     . ARG C 56  ? 0.08487 0.10434 0.11863 -0.00843 0.01583  0.01039  55  ARG C N     
3124 C CA    . ARG C 56  ? 0.07642 0.09246 0.11058 -0.01221 0.01552  0.01331  55  ARG C CA    
3125 C C     . ARG C 56  ? 0.07510 0.09139 0.11648 -0.01201 0.01050  0.01167  55  ARG C C     
3126 O O     . ARG C 56  ? 0.06809 0.07998 0.10511 -0.00908 0.00646  0.01125  55  ARG C O     
3127 C CB    . ARG C 56  ? 0.07556 0.08248 0.09833 -0.01192 0.01411  0.01675  55  ARG C CB    
3128 C CG    . ARG C 56  ? 0.11406 0.11380 0.13692 -0.01536 0.01348  0.01959  55  ARG C CG    
3129 C CD    . ARG C 56  ? 0.08890 0.07872 0.10155 -0.01295 0.01110  0.02288  55  ARG C CD    
3130 N NE    . ARG C 56  ? 0.09784 0.08557 0.10072 -0.01312 0.01382  0.02697  55  ARG C NE    
3131 C CZ    . ARG C 56  ? 0.14388 0.12376 0.13769 -0.01034 0.01117  0.03074  55  ARG C CZ    
3132 N NH1   . ARG C 56  ? 0.11372 0.08756 0.10878 -0.00706 0.00689  0.03047  55  ARG C NH1   
3133 N NH2   . ARG C 56  ? 0.11683 0.09495 0.09955 -0.01021 0.01277  0.03478  55  ARG C NH2   
3134 N N     . ILE C 57  ? 0.06662 0.08888 0.11893 -0.01525 0.01077  0.01057  56  ILE C N     
3135 C CA    . ILE C 57  ? 0.06718 0.09101 0.12609 -0.01513 0.00464  0.00817  56  ILE C CA    
3136 C C     . ILE C 57  ? 0.07383 0.09671 0.13902 -0.02170 0.00451  0.00834  56  ILE C C     
3137 O O     . ILE C 57  ? 0.07724 0.10852 0.15355 -0.02601 0.00864  0.00857  56  ILE C O     
3138 C CB    . ILE C 57  ? 0.06071 0.09504 0.13040 -0.01197 0.00280  0.00562  56  ILE C CB    
3139 C CG1   . ILE C 57  ? 0.05737 0.08926 0.12055 -0.00609 0.00292  0.00572  56  ILE C CG1   
3140 C CG2   . ILE C 57  ? 0.06228 0.09854 0.13711 -0.01179 -0.00504 0.00342  56  ILE C CG2   
3141 C CD1   . ILE C 57  ? 0.07541 0.11332 0.14699 -0.00151 -0.00053 0.00409  56  ILE C CD1   
3142 N N     . ILE C 58  ? 0.07697 0.08948 0.13574 -0.02269 0.00042  0.00793  57  ILE C N     
3143 C CA    . ILE C 58  ? 0.08612 0.09380 0.14988 -0.02953 -0.00029 0.00770  57  ILE C CA    
3144 C C     . ILE C 58  ? 0.12361 0.13198 0.19160 -0.02987 -0.00863 0.00236  57  ILE C C     
3145 O O     . ILE C 58  ? 0.09446 0.09484 0.15137 -0.02546 -0.01296 0.00030  57  ILE C O     
3146 C CB    . ILE C 58  ? 0.11608 0.10828 0.16812 -0.03015 0.00151  0.01104  57  ILE C CB    
3147 C CG1   . ILE C 58  ? 0.14856 0.14123 0.19509 -0.02982 0.00860  0.01654  57  ILE C CG1   
3148 C CG2   . ILE C 58  ? 0.13652 0.12009 0.19350 -0.03748 0.00015  0.01048  57  ILE C CG2   
3149 C CD1   . ILE C 58  ? 0.15580 0.13367 0.19100 -0.02988 0.00994  0.02135  57  ILE C CD1   
3150 N N     . PRO C 59  ? 0.09798 0.11678 0.18168 -0.03479 -0.01117 -0.00029 58  PRO C N     
3151 C CA    . PRO C 59  ? 0.11842 0.13912 0.20532 -0.03479 -0.02097 -0.00598 58  PRO C CA    
3152 C C     . PRO C 59  ? 0.13454 0.13895 0.21080 -0.03679 -0.02517 -0.00911 58  PRO C C     
3153 O O     . PRO C 59  ? 0.13984 0.13453 0.21723 -0.04280 -0.02208 -0.00789 58  PRO C O     
3154 C CB    . PRO C 59  ? 0.13639 0.17216 0.24576 -0.04160 -0.02207 -0.00789 58  PRO C CB    
3155 C CG    . PRO C 59  ? 0.10169 0.14763 0.21878 -0.04138 -0.01196 -0.00330 58  PRO C CG    
3156 C CD    . PRO C 59  ? 0.08790 0.11904 0.18766 -0.04029 -0.00505 0.00156  58  PRO C CD    
3157 N N     . GLY C 60  ? 0.12992 0.13039 0.19505 -0.03148 -0.03204 -0.01319 59  GLY C N     
3158 C CA    . GLY C 60  ? 0.18563 0.17049 0.23875 -0.03166 -0.03582 -0.01773 59  GLY C CA    
3159 C C     . GLY C 60  ? 0.13129 0.10414 0.16862 -0.02553 -0.03060 -0.01517 59  GLY C C     
3160 O O     . GLY C 60  ? 0.17226 0.13189 0.19891 -0.02382 -0.03277 -0.01943 59  GLY C O     
3161 N N     . PHE C 61  ? 0.13110 0.10858 0.16746 -0.02198 -0.02406 -0.00912 60  PHE C N     
3162 C CA    . PHE C 61  ? 0.11709 0.08618 0.14165 -0.01627 -0.01982 -0.00676 60  PHE C CA    
3163 C C     . PHE C 61  ? 0.11012 0.08736 0.13023 -0.01022 -0.01762 -0.00407 60  PHE C C     
3164 O O     . PHE C 61  ? 0.15677 0.13148 0.16686 -0.00524 -0.01866 -0.00597 60  PHE C O     
3165 C CB    . PHE C 61  ? 0.11321 0.07638 0.14007 -0.01887 -0.01439 -0.00172 60  PHE C CB    
3166 C CG    . PHE C 61  ? 0.13211 0.08301 0.16177 -0.02491 -0.01577 -0.00324 60  PHE C CG    
3167 C CD1   . PHE C 61  ? 0.16172 0.09644 0.18254 -0.02195 -0.01690 -0.00558 60  PHE C CD1   
3168 C CD2   . PHE C 61  ? 0.12955 0.08484 0.17191 -0.03364 -0.01547 -0.00245 60  PHE C CD2   
3169 C CE1   . PHE C 61  ? 0.20305 0.12330 0.22637 -0.02776 -0.01834 -0.00700 60  PHE C CE1   
3170 C CE2   . PHE C 61  ? 0.19655 0.13915 0.24257 -0.04067 -0.01637 -0.00336 60  PHE C CE2   
3171 C CZ    . PHE C 61  ? 0.19091 0.11453 0.22676 -0.03782 -0.01813 -0.00558 60  PHE C CZ    
3172 N N     . MET C 62  ? 0.10831 0.09455 0.13522 -0.01079 -0.01412 0.00003  61  MET C N     
3173 C CA    . MET C 62  ? 0.12194 0.11263 0.14455 -0.00575 -0.01181 0.00243  61  MET C CA    
3174 C C     . MET C 62  ? 0.11735 0.11736 0.14828 -0.00658 -0.00930 0.00490  61  MET C C     
3175 O O     . MET C 62  ? 0.09127 0.09502 0.13042 -0.01062 -0.00733 0.00552  61  MET C O     
3176 C CB    . MET C 62  ? 0.12554 0.11072 0.14144 -0.00265 -0.00802 0.00449  61  MET C CB    
3177 C CG    . MET C 62  ? 0.09442 0.08091 0.11354 -0.00426 -0.00418 0.00828  61  MET C CG    
3178 S SD    . MET C 62  ? 0.12267 0.10301 0.14543 -0.01015 -0.00334 0.00964  61  MET C SD    
3179 C CE    . MET C 62  ? 0.12403 0.11074 0.14792 -0.01123 0.00168  0.01410  61  MET C CE    
3180 N N     . CYS C 63  ? 0.06966 0.07264 0.09808 -0.00272 -0.00862 0.00625  62  CYS C N     
3181 C CA    . CYS C 63  ? 0.06331 0.07226 0.09741 -0.00213 -0.00577 0.00777  62  CYS C CA    
3182 C C     . CYS C 63  ? 0.06728 0.07339 0.09569 -0.00053 -0.00235 0.00965  62  CYS C C     
3183 O O     . CYS C 63  ? 0.09325 0.09674 0.11620 0.00186  -0.00272 0.01035  62  CYS C O     
3184 C CB    . CYS C 63  ? 0.08432 0.09705 0.12123 0.00099  -0.00886 0.00768  62  CYS C CB    
3185 S SG    . CYS C 63  ? 0.08836 0.10689 0.13303 0.00027  -0.01563 0.00506  62  CYS C SG    
3186 N N     . GLN C 64  ? 0.07846 0.08595 0.10817 -0.00203 0.00095  0.01037  63  GLN C N     
3187 C CA    . GLN C 64  ? 0.08852 0.09433 0.11356 -0.00108 0.00260  0.01153  63  GLN C CA    
3188 C C     . GLN C 64  ? 0.10995 0.11901 0.13700 -0.00088 0.00445  0.01055  63  GLN C C     
3189 O O     . GLN C 64  ? 0.10235 0.11458 0.13261 -0.00190 0.00656  0.00940  63  GLN C O     
3190 C CB    . GLN C 64  ? 0.09590 0.09823 0.11707 -0.00241 0.00344  0.01319  63  GLN C CB    
3191 C CG    . GLN C 64  ? 0.09269 0.09486 0.10971 -0.00076 0.00339  0.01436  63  GLN C CG    
3192 C CD    . GLN C 64  ? 0.10199 0.09912 0.11396 -0.00057 0.00293  0.01712  63  GLN C CD    
3193 O OE1   . GLN C 64  ? 0.11904 0.11037 0.13053 -0.00146 0.00272  0.01802  63  GLN C OE1   
3194 N NE2   . GLN C 64  ? 0.08293 0.08119 0.09064 0.00061  0.00205  0.01847  63  GLN C NE2   
3195 N N     . GLY C 65  ? 0.10013 0.10846 0.12597 0.00020  0.00411  0.01049  64  GLY C N     
3196 C CA    . GLY C 65  ? 0.08779 0.09678 0.11513 0.00011  0.00513  0.00843  64  GLY C CA    
3197 C C     . GLY C 65  ? 0.09843 0.10714 0.12446 -0.00064 0.00424  0.00811  64  GLY C C     
3198 O O     . GLY C 65  ? 0.09679 0.10664 0.12155 -0.00045 0.00322  0.00978  64  GLY C O     
3199 N N     . GLY C 66  ? 0.10374 0.11121 0.13135 -0.00140 0.00436  0.00538  65  GLY C N     
3200 C CA    . GLY C 66  ? 0.12008 0.12780 0.14970 -0.00334 0.00287  0.00455  65  GLY C CA    
3201 C C     . GLY C 66  ? 0.11213 0.12170 0.13858 -0.00475 0.00079  0.00086  65  GLY C C     
3202 O O     . GLY C 66  ? 0.14292 0.15461 0.17303 -0.00698 -0.00167 -0.00037 65  GLY C O     
3203 N N     . ASP C 67  ? 0.11516 0.12472 0.13481 -0.00383 0.00167  -0.00099 66  ASP C N     
3204 C CA    . ASP C 67  ? 0.13033 0.14078 0.14300 -0.00472 -0.00063 -0.00485 66  ASP C CA    
3205 C C     . ASP C 67  ? 0.12821 0.13422 0.14140 -0.00553 -0.00006 -0.01119 66  ASP C C     
3206 O O     . ASP C 67  ? 0.14309 0.14712 0.15207 -0.00379 0.00348  -0.01426 66  ASP C O     
3207 C CB    . ASP C 67  ? 0.09877 0.11008 0.10113 -0.00348 0.00116  -0.00328 66  ASP C CB    
3208 C CG    . ASP C 67  ? 0.09701 0.10855 0.08791 -0.00381 -0.00146 -0.00701 66  ASP C CG    
3209 O OD1   . ASP C 67  ? 0.14851 0.16006 0.14086 -0.00527 -0.00568 -0.01189 66  ASP C OD1   
3210 O OD2   . ASP C 67  ? 0.12727 0.13859 0.10694 -0.00302 0.00046  -0.00499 66  ASP C OD2   
3211 N N     . PHE C 68  ? 0.10184 0.10622 0.12094 -0.00832 -0.00325 -0.01364 67  PHE C N     
3212 C CA    . PHE C 68  ? 0.12788 0.12541 0.14720 -0.00958 -0.00362 -0.02057 67  PHE C CA    
3213 C C     . PHE C 68  ? 0.14729 0.14572 0.15917 -0.01168 -0.00847 -0.02730 67  PHE C C     
3214 O O     . PHE C 68  ? 0.13916 0.13066 0.15053 -0.01323 -0.00963 -0.03466 67  PHE C O     
3215 C CB    . PHE C 68  ? 0.12184 0.11396 0.15238 -0.01243 -0.00382 -0.01932 67  PHE C CB    
3216 C CG    . PHE C 68  ? 0.12657 0.12465 0.16462 -0.01679 -0.00706 -0.01681 67  PHE C CG    
3217 C CD1   . PHE C 68  ? 0.11375 0.11338 0.15468 -0.02138 -0.01214 -0.02234 67  PHE C CD1   
3218 C CD2   . PHE C 68  ? 0.08978 0.09283 0.13283 -0.01622 -0.00501 -0.00965 67  PHE C CD2   
3219 C CE1   . PHE C 68  ? 0.09924 0.10744 0.15076 -0.02543 -0.01488 -0.02012 67  PHE C CE1   
3220 C CE2   . PHE C 68  ? 0.11336 0.12381 0.16512 -0.01955 -0.00656 -0.00762 67  PHE C CE2   
3221 C CZ    . PHE C 68  ? 0.12712 0.14115 0.18467 -0.02427 -0.01135 -0.01256 67  PHE C CZ    
3222 N N     . THR C 69  ? 0.13419 0.13981 0.13937 -0.01140 -0.01206 -0.02536 68  THR C N     
3223 C CA    . THR C 69  ? 0.12487 0.13166 0.12063 -0.01279 -0.01812 -0.03177 68  THR C CA    
3224 C C     . THR C 69  ? 0.16237 0.16807 0.13953 -0.00946 -0.01579 -0.03343 68  THR C C     
3225 O O     . THR C 69  ? 0.16832 0.17045 0.13456 -0.00978 -0.01772 -0.04156 68  THR C O     
3226 C CB    . THR C 69  ? 0.17073 0.18678 0.17112 -0.01429 -0.02559 -0.02894 68  THR C CB    
3227 O OG1   . THR C 69  ? 0.15966 0.17991 0.15579 -0.01045 -0.02416 -0.02096 68  THR C OG1   
3228 C CG2   . THR C 69  ? 0.13795 0.15699 0.15756 -0.01836 -0.02652 -0.02758 68  THR C CG2   
3229 N N     . ARG C 70  ? 0.14896 0.15717 0.12145 -0.00671 -0.01144 -0.02608 69  ARG C N     
3230 C CA    . ARG C 70  ? 0.16832 0.17557 0.12338 -0.00442 -0.00731 -0.02607 69  ARG C CA    
3231 C C     . ARG C 70  ? 0.17086 0.17644 0.12855 -0.00271 0.00257  -0.02569 69  ARG C C     
3232 O O     . ARG C 70  ? 0.15125 0.15632 0.09644 -0.00121 0.00807  -0.02827 69  ARG C O     
3233 C CB    . ARG C 70  ? 0.14398 0.15434 0.09066 -0.00319 -0.00961 -0.01763 69  ARG C CB    
3234 C CG    . ARG C 70  ? 0.15205 0.16587 0.09390 -0.00324 -0.02037 -0.01804 69  ARG C CG    
3235 C CD    . ARG C 70  ? 0.25518 0.26715 0.17692 -0.00293 -0.02396 -0.02464 69  ARG C CD    
3236 N NE    . ARG C 70  ? 0.35205 0.36225 0.27821 -0.00555 -0.02699 -0.03570 69  ARG C NE    
3237 C CZ    . ARG C 70  ? 0.36776 0.38165 0.30411 -0.00846 -0.03646 -0.04002 69  ARG C CZ    
3238 N NH1   . ARG C 70  ? 0.36102 0.38280 0.30590 -0.00825 -0.04368 -0.03445 69  ARG C NH1   
3239 N NH2   . ARG C 70  ? 0.31753 0.32719 0.25704 -0.01168 -0.03858 -0.05046 69  ARG C NH2   
3240 N N     . HIS C 71  ? 0.12362 0.12924 0.09731 -0.00270 0.00482  -0.02286 70  HIS C N     
3241 C CA    . HIS C 71  ? 0.14766 0.15350 0.12780 -0.00066 0.01236  -0.02294 70  HIS C CA    
3242 C C     . HIS C 71  ? 0.19449 0.20467 0.16859 -0.00038 0.01826  -0.01773 70  HIS C C     
3243 O O     . HIS C 71  ? 0.14150 0.15424 0.11662 0.00114  0.02556  -0.01981 70  HIS C O     
3244 C CB    . HIS C 71  ? 0.19035 0.19203 0.16897 0.00150  0.01549  -0.03225 70  HIS C CB    
3245 C CG    . HIS C 71  ? 0.20463 0.19936 0.18723 0.00003  0.00963  -0.03811 70  HIS C CG    
3246 N ND1   . HIS C 71  ? 0.15194 0.14198 0.14882 0.00003  0.00866  -0.03729 70  HIS C ND1   
3247 C CD2   . HIS C 71  ? 0.20952 0.20069 0.18364 -0.00211 0.00416  -0.04473 70  HIS C CD2   
3248 C CE1   . HIS C 71  ? 0.19083 0.17411 0.18888 -0.00274 0.00374  -0.04263 70  HIS C CE1   
3249 N NE2   . HIS C 71  ? 0.16991 0.15434 0.15523 -0.00426 0.00050  -0.04790 70  HIS C NE2   
3250 N N     . ASN C 72  ? 0.12124 0.13220 0.09010 -0.00186 0.01548  -0.01075 71  ASN C N     
3251 C CA    . ASN C 72  ? 0.18104 0.19366 0.14411 -0.00274 0.02121  -0.00487 71  ASN C CA    
3252 C C     . ASN C 72  ? 0.18866 0.19997 0.15589 -0.00401 0.01835  0.00321  71  ASN C C     
3253 O O     . ASN C 72  ? 0.12661 0.13668 0.08776 -0.00556 0.02214  0.00890  71  ASN C O     
3254 C CB    . ASN C 72  ? 0.18495 0.19620 0.12715 -0.00264 0.02318  -0.00519 71  ASN C CB    
3255 C CG    . ASN C 72  ? 0.18070 0.18894 0.11158 -0.00222 0.01398  -0.00302 71  ASN C CG    
3256 O OD1   . ASN C 72  ? 0.16619 0.17449 0.10647 -0.00211 0.00727  -0.00078 71  ASN C OD1   
3257 N ND2   . ASN C 72  ? 0.26795 0.27441 0.17826 -0.00152 0.01369  -0.00390 71  ASN C ND2   
3258 N N     . GLY C 73  ? 0.15468 0.16540 0.13167 -0.00349 0.01259  0.00384  72  GLY C N     
3259 C CA    . GLY C 73  ? 0.10179 0.11044 0.08211 -0.00366 0.01011  0.00996  72  GLY C CA    
3260 C C     . GLY C 73  ? 0.12831 0.13505 0.10146 -0.00202 0.00376  0.01287  72  GLY C C     
3261 O O     . GLY C 73  ? 0.12493 0.12937 0.10192 -0.00089 0.00137  0.01709  72  GLY C O     
3262 N N     . THR C 74  ? 0.11529 0.12307 0.07844 -0.00128 0.00032  0.01019  73  THR C N     
3263 C CA    . THR C 74  ? 0.12306 0.13055 0.07962 0.00104  -0.00705 0.01326  73  THR C CA    
3264 C C     . THR C 74  ? 0.13458 0.14798 0.10004 0.00161  -0.01417 0.00861  73  THR C C     
3265 O O     . THR C 74  ? 0.13483 0.15087 0.10019 0.00413  -0.02111 0.01089  73  THR C O     
3266 C CB    . THR C 74  ? 0.15059 0.15541 0.08682 0.00161  -0.00767 0.01468  73  THR C CB    
3267 O OG1   . THR C 74  ? 0.15719 0.16496 0.08830 0.00073  -0.00878 0.00646  73  THR C OG1   
3268 C CG2   . THR C 74  ? 0.18953 0.18934 0.11730 -0.00028 0.00141  0.01968  73  THR C CG2   
3269 N N     . GLY C 75  ? 0.15313 0.16874 0.12745 -0.00067 -0.01275 0.00245  74  GLY C N     
3270 C CA    . GLY C 75  ? 0.14420 0.16483 0.12684 -0.00191 -0.01875 -0.00226 74  GLY C CA    
3271 C C     . GLY C 75  ? 0.16347 0.18661 0.16334 -0.00312 -0.01720 -0.00187 74  GLY C C     
3272 O O     . GLY C 75  ? 0.12847 0.15026 0.13301 -0.00177 -0.01340 0.00256  74  GLY C O     
3273 N N     . GLY C 76  ? 0.23589 0.26213 0.24446 -0.00615 -0.02014 -0.00669 75  GLY C N     
3274 C CA    . GLY C 76  ? 0.15022 0.17874 0.17392 -0.00820 -0.01815 -0.00592 75  GLY C CA    
3275 C C     . GLY C 76  ? 0.16885 0.20706 0.20358 -0.00997 -0.02411 -0.00724 75  GLY C C     
3276 O O     . GLY C 76  ? 0.20068 0.24429 0.23156 -0.00816 -0.03072 -0.00779 75  GLY C O     
3277 N N     . LYS C 77  ? 0.15550 0.19652 0.20438 -0.01358 -0.02191 -0.00740 76  LYS C N     
3278 C CA    . LYS C 77  ? 0.11953 0.17241 0.18321 -0.01620 -0.02638 -0.00861 76  LYS C CA    
3279 C C     . LYS C 77  ? 0.13211 0.18691 0.20948 -0.01937 -0.01984 -0.00571 76  LYS C C     
3280 O O     . LYS C 77  ? 0.12779 0.17261 0.20178 -0.02073 -0.01400 -0.00424 76  LYS C O     
3281 C CB    . LYS C 77  ? 0.18013 0.23471 0.24518 -0.02113 -0.03376 -0.01597 76  LYS C CB    
3282 C CG    . LYS C 77  ? 0.14515 0.18977 0.21212 -0.02710 -0.03101 -0.02040 76  LYS C CG    
3283 C CD    . LYS C 77  ? 0.19480 0.24250 0.26669 -0.03290 -0.03938 -0.02864 76  LYS C CD    
3284 C CE    . LYS C 77  ? 0.23952 0.27288 0.30858 -0.03764 -0.03767 -0.03474 76  LYS C CE    
3285 N NZ    . LYS C 77  ? 0.24359 0.27915 0.32109 -0.04514 -0.04585 -0.04348 76  LYS C NZ    
3286 N N     . SER C 78  ? 0.11291 0.18110 0.20533 -0.01980 -0.02059 -0.00438 77  SER C N     
3287 C CA    . SER C 78  ? 0.10929 0.18094 0.21382 -0.02269 -0.01294 -0.00089 77  SER C CA    
3288 C C     . SER C 78  ? 0.07289 0.14861 0.19247 -0.03181 -0.01401 -0.00403 77  SER C C     
3289 O O     . SER C 78  ? 0.08475 0.16137 0.20599 -0.03548 -0.02176 -0.00994 77  SER C O     
3290 C CB    . SER C 78  ? 0.10319 0.18775 0.21656 -0.01744 -0.01079 0.00232  77  SER C CB    
3291 O OG    . SER C 78  ? 0.06386 0.16491 0.19423 -0.01906 -0.01670 -0.00046 77  SER C OG    
3292 N N     . ILE C 79  ? 0.07269 0.15036 0.20281 -0.03604 -0.00603 -0.00011 78  ILE C N     
3293 C CA    . ILE C 79  ? 0.07955 0.16150 0.22678 -0.04608 -0.00616 -0.00223 78  ILE C CA    
3294 C C     . ILE C 79  ? 0.09446 0.19627 0.25655 -0.04677 -0.01020 -0.00448 78  ILE C C     
3295 O O     . ILE C 79  ? 0.09084 0.19641 0.26226 -0.05438 -0.01171 -0.00696 78  ILE C O     
3296 C CB    . ILE C 79  ? 0.08480 0.15882 0.23213 -0.05026 0.00467  0.00400  78  ILE C CB    
3297 C CG1   . ILE C 79  ? 0.10756 0.19261 0.25750 -0.04565 0.01271  0.00942  78  ILE C CG1   
3298 C CG2   . ILE C 79  ? 0.09762 0.15100 0.22821 -0.04831 0.00734  0.00647  78  ILE C CG2   
3299 C CD1   . ILE C 79  ? 0.10229 0.18292 0.25184 -0.05063 0.02269  0.01501  78  ILE C CD1   
3300 N N     . TYR C 80  ? 0.10689 0.22079 0.27085 -0.03861 -0.01242 -0.00361 79  TYR C N     
3301 C CA    . TYR C 80  ? 0.08497 0.21817 0.26263 -0.03739 -0.01638 -0.00528 79  TYR C CA    
3302 C C     . TYR C 80  ? 0.10493 0.24318 0.28015 -0.03433 -0.02985 -0.01015 79  TYR C C     
3303 O O     . TYR C 80  ? 0.14478 0.29899 0.33072 -0.03266 -0.03499 -0.01129 79  TYR C O     
3304 C CB    . TYR C 80  ? 0.09443 0.23761 0.27589 -0.02905 -0.00986 -0.00120 79  TYR C CB    
3305 C CG    . TYR C 80  ? 0.08571 0.22233 0.26369 -0.03022 0.00324  0.00373  79  TYR C CG    
3306 C CD1   . TYR C 80  ? 0.07744 0.21904 0.26440 -0.03751 0.01079  0.00539  79  TYR C CD1   
3307 C CD2   . TYR C 80  ? 0.08510 0.21041 0.24947 -0.02412 0.00776  0.00718  79  TYR C CD2   
3308 C CE1   . TYR C 80  ? 0.08021 0.21492 0.26046 -0.03815 0.02242  0.01045  79  TYR C CE1   
3309 C CE2   . TYR C 80  ? 0.13473 0.25349 0.29267 -0.02468 0.01883  0.01174  79  TYR C CE2   
3310 C CZ    . TYR C 80  ? 0.12477 0.24775 0.28954 -0.03146 0.02610  0.01344  79  TYR C CZ    
3311 O OH    . TYR C 80  ? 0.10127 0.21674 0.25625 -0.03158 0.03666  0.01848  79  TYR C OH    
3312 N N     . GLY C 81  ? 0.15371 0.27901 0.31409 -0.03318 -0.03560 -0.01278 80  GLY C N     
3313 C CA    . GLY C 81  ? 0.15710 0.28433 0.30821 -0.02834 -0.04762 -0.01622 80  GLY C CA    
3314 C C     . GLY C 81  ? 0.15005 0.26221 0.27780 -0.02104 -0.04595 -0.01324 80  GLY C C     
3315 O O     . GLY C 81  ? 0.14172 0.24191 0.26110 -0.02050 -0.03639 -0.00960 80  GLY C O     
3316 N N     . GLU C 82  ? 0.13729 0.24915 0.25206 -0.01535 -0.05498 -0.01408 81  GLU C N     
3317 C CA    . GLU C 82  ? 0.15846 0.25476 0.24883 -0.00972 -0.05251 -0.01080 81  GLU C CA    
3318 C C     . GLU C 82  ? 0.17062 0.26487 0.26066 -0.00305 -0.04509 -0.00399 81  GLU C C     
3319 O O     . GLU C 82  ? 0.18888 0.26958 0.26493 -0.00163 -0.03859 -0.00126 81  GLU C O     
3320 C CB    . GLU C 82  ? 0.22550 0.32154 0.30066 -0.00556 -0.06334 -0.01213 81  GLU C CB    
3321 C CG    . GLU C 82  ? 0.17645 0.26957 0.24368 -0.01156 -0.07023 -0.02021 81  GLU C CG    
3322 C CD    . GLU C 82  ? 0.22539 0.31756 0.27300 -0.00688 -0.08079 -0.02110 81  GLU C CD    
3323 O OE1   . GLU C 82  ? 0.22908 0.32048 0.26804 0.00096  -0.08211 -0.01414 81  GLU C OE1   
3324 O OE2   . GLU C 82  ? 0.16221 0.25286 0.20144 -0.01102 -0.08780 -0.02879 81  GLU C OE2   
3325 N N     . LYS C 83  ? 0.15927 0.26719 0.26533 0.00128  -0.04617 -0.00194 82  LYS C N     
3326 C CA    . LYS C 83  ? 0.14683 0.25225 0.25279 0.00812  -0.03931 0.00303  82  LYS C CA    
3327 C C     . LYS C 83  ? 0.11453 0.23605 0.24403 0.00827  -0.03453 0.00295  82  LYS C C     
3328 O O     . LYS C 83  ? 0.09221 0.22987 0.24053 0.00441  -0.03869 -0.00010 82  LYS C O     
3329 C CB    . LYS C 83  ? 0.15571 0.25765 0.25132 0.01732  -0.04565 0.00651  82  LYS C CB    
3330 C CG    . LYS C 83  ? 0.23906 0.35779 0.34888 0.02198  -0.05596 0.00569  82  LYS C CG    
3331 C CD    . LYS C 83  ? 0.28170 0.39345 0.37424 0.02838  -0.06590 0.00876  82  LYS C CD    
3332 C CE    . LYS C 83  ? 0.32180 0.41628 0.39843 0.03458  -0.06074 0.01473  82  LYS C CE    
3333 N NZ    . LYS C 83  ? 0.49371 0.57921 0.55198 0.04040  -0.06939 0.01949  82  LYS C NZ    
3334 N N     . PHE C 84  ? 0.11921 0.23688 0.24785 0.01247  -0.02542 0.00588  83  PHE C N     
3335 C CA    . PHE C 84  ? 0.11724 0.25077 0.26633 0.01474  -0.01958 0.00593  83  PHE C CA    
3336 C C     . PHE C 84  ? 0.10908 0.23684 0.25209 0.02471  -0.01490 0.00820  83  PHE C C     
3337 O O     . PHE C 84  ? 0.06447 0.17445 0.18794 0.02733  -0.01441 0.00999  83  PHE C O     
3338 C CB    . PHE C 84  ? 0.07583 0.21260 0.23357 0.00580  -0.00987 0.00571  83  PHE C CB    
3339 C CG    . PHE C 84  ? 0.09557 0.21440 0.23514 0.00409  -0.00147 0.00814  83  PHE C CG    
3340 C CD1   . PHE C 84  ? 0.12086 0.22402 0.24436 -0.00028 -0.00393 0.00797  83  PHE C CD1   
3341 C CD2   . PHE C 84  ? 0.06327 0.18231 0.20268 0.00685  0.00885  0.01011  83  PHE C CD2   
3342 C CE1   . PHE C 84  ? 0.09056 0.17946 0.19997 -0.00133 0.00259  0.01016  83  PHE C CE1   
3343 C CE2   . PHE C 84  ? 0.13610 0.23974 0.25862 0.00543  0.01494  0.01219  83  PHE C CE2   
3344 C CZ    . PHE C 84  ? 0.11641 0.20548 0.22502 0.00135  0.01126  0.01243  83  PHE C CZ    
3345 N N     . GLU C 85  ? 0.07377 0.21543 0.23189 0.02989  -0.01130 0.00693  84  GLU C N     
3346 C CA    . GLU C 85  ? 0.09689 0.23283 0.25035 0.04067  -0.00864 0.00736  84  GLU C CA    
3347 C C     . GLU C 85  ? 0.13439 0.25973 0.27822 0.04066  0.00275  0.00842  84  GLU C C     
3348 O O     . GLU C 85  ? 0.12398 0.24870 0.26586 0.03267  0.00967  0.00882  84  GLU C O     
3349 C CB    . GLU C 85  ? 0.11106 0.26402 0.28010 0.04686  -0.00857 0.00402  84  GLU C CB    
3350 C CG    . GLU C 85  ? 0.19295 0.36150 0.37585 0.04094  0.00080  0.00181  84  GLU C CG    
3351 C CD    . GLU C 85  ? 0.28426 0.47277 0.48339 0.04734  0.00048  -0.00025 84  GLU C CD    
3352 O OE1   . GLU C 85  ? 0.31672 0.50716 0.51657 0.05429  -0.00877 0.00226  84  GLU C OE1   
3353 O OE2   . GLU C 85  ? 0.31343 0.51432 0.52312 0.04515  0.01012  -0.00227 84  GLU C OE2   
3354 N N     . ASP C 86  ? 0.07680 0.19051 0.21070 0.04949  0.00379  0.00839  85  ASP C N     
3355 C CA    . ASP C 86  ? 0.07708 0.17883 0.19774 0.05021  0.01300  0.00734  85  ASP C CA    
3356 C C     . ASP C 86  ? 0.07976 0.19544 0.21193 0.05095  0.02329  0.00463  85  ASP C C     
3357 O O     . ASP C 86  ? 0.08667 0.21154 0.23011 0.05715  0.02330  0.00105  85  ASP C O     
3358 C CB    . ASP C 86  ? 0.08660 0.17162 0.19498 0.05899  0.01044  0.00664  85  ASP C CB    
3359 C CG    . ASP C 86  ? 0.09349 0.16309 0.18807 0.05650  0.00156  0.00973  85  ASP C CG    
3360 O OD1   . ASP C 86  ? 0.09662 0.15893 0.18035 0.04800  0.00190  0.01085  85  ASP C OD1   
3361 O OD2   . ASP C 86  ? 0.09494 0.15977 0.18952 0.06327  -0.00533 0.01141  85  ASP C OD2   
3362 N N     . GLU C 87  ? 0.07750 0.19290 0.20464 0.04400  0.03169  0.00596  86  GLU C N     
3363 C CA    . GLU C 87  ? 0.13363 0.26123 0.26857 0.04145  0.04143  0.00411  86  GLU C CA    
3364 C C     . GLU C 87  ? 0.10860 0.23302 0.23734 0.05029  0.04836  -0.00011 86  GLU C C     
3365 O O     . GLU C 87  ? 0.11745 0.25486 0.25950 0.05439  0.05126  -0.00404 86  GLU C O     
3366 C CB    . GLU C 87  ? 0.09874 0.22280 0.22608 0.03158  0.04790  0.00796  86  GLU C CB    
3367 C CG    . GLU C 87  ? 0.08985 0.22537 0.22358 0.02708  0.05802  0.00768  86  GLU C CG    
3368 C CD    . GLU C 87  ? 0.11478 0.24481 0.24181 0.01649  0.06215  0.01276  86  GLU C CD    
3369 O OE1   . GLU C 87  ? 0.11633 0.23306 0.23247 0.01397  0.05799  0.01577  86  GLU C OE1   
3370 O OE2   . GLU C 87  ? 0.11283 0.25148 0.24563 0.01083  0.06948  0.01389  86  GLU C OE2   
3371 N N     . ASN C 88  ? 0.09972 0.20713 0.20847 0.05341  0.05077  -0.00026 87  ASN C N     
3372 C CA    . ASN C 88  ? 0.13268 0.23300 0.23212 0.06187  0.05585  -0.00561 87  ASN C CA    
3373 C C     . ASN C 88  ? 0.12437 0.20320 0.20254 0.06461  0.05269  -0.00593 87  ASN C C     
3374 O O     . ASN C 88  ? 0.12839 0.19853 0.19865 0.05759  0.04663  -0.00233 87  ASN C O     
3375 C CB    . ASN C 88  ? 0.12465 0.23218 0.22057 0.05971  0.06801  -0.00733 87  ASN C CB    
3376 C CG    . ASN C 88  ? 0.15408 0.25356 0.23233 0.05242  0.07269  -0.00293 87  ASN C CG    
3377 O OD1   . ASN C 88  ? 0.15277 0.23590 0.21143 0.05438  0.07098  -0.00331 87  ASN C OD1   
3378 N ND2   . ASN C 88  ? 0.13297 0.24319 0.21773 0.04397  0.07829  0.00106  87  ASN C ND2   
3379 N N     . PHE C 89  ? 0.13125 0.19904 0.19877 0.07201  0.05472  -0.01177 88  PHE C N     
3380 C CA    . PHE C 89  ? 0.16186 0.20792 0.20819 0.07292  0.05108  -0.01389 88  PHE C CA    
3381 C C     . PHE C 89  ? 0.17776 0.21765 0.20606 0.07508  0.05937  -0.01900 88  PHE C C     
3382 O O     . PHE C 89  ? 0.19497 0.21782 0.20856 0.07922  0.05693  -0.02480 88  PHE C O     
3383 C CB    . PHE C 89  ? 0.14376 0.17654 0.19108 0.07999  0.04330  -0.01646 88  PHE C CB    
3384 C CG    . PHE C 89  ? 0.13168 0.16772 0.19107 0.07765  0.03415  -0.01074 88  PHE C CG    
3385 C CD1   . PHE C 89  ? 0.13265 0.16278 0.18560 0.06804  0.02783  -0.00600 88  PHE C CD1   
3386 C CD2   . PHE C 89  ? 0.18679 0.23153 0.26281 0.08356  0.03088  -0.01056 88  PHE C CD2   
3387 C CE1   . PHE C 89  ? 0.11328 0.14612 0.17424 0.06618  0.02006  -0.00130 88  PHE C CE1   
3388 C CE2   . PHE C 89  ? 0.13845 0.18610 0.22266 0.08215  0.02180  -0.00521 88  PHE C CE2   
3389 C CZ    . PHE C 89  ? 0.11561 0.15721 0.19131 0.07394  0.01695  -0.00062 88  PHE C CZ    
3390 N N     . ILE C 90  ? 0.16397 0.21609 0.19201 0.07057  0.06802  -0.01684 89  ILE C N     
3391 C CA    . ILE C 90  ? 0.17797 0.22488 0.18701 0.07167  0.07538  -0.02118 89  ILE C CA    
3392 C C     . ILE C 90  ? 0.18020 0.20833 0.16464 0.07051  0.07075  -0.02246 89  ILE C C     
3393 O O     . ILE C 90  ? 0.24515 0.26083 0.21248 0.07431  0.07055  -0.02964 89  ILE C O     
3394 C CB    . ILE C 90  ? 0.20290 0.26479 0.21475 0.06544  0.08501  -0.01655 89  ILE C CB    
3395 C CG1   . ILE C 90  ? 0.22321 0.30458 0.25949 0.06674  0.09000  -0.01764 89  ILE C CG1   
3396 C CG2   . ILE C 90  ? 0.19819 0.25283 0.18586 0.06593  0.09166  -0.01968 89  ILE C CG2   
3397 C CD1   . ILE C 90  ? 0.17682 0.27274 0.21812 0.05874  0.09900  -0.01253 89  ILE C CD1   
3398 N N     . LEU C 91  ? 0.18356 0.20889 0.16809 0.06166  0.06333  -0.01609 90  LEU C N     
3399 C CA    . LEU C 91  ? 0.18943 0.20027 0.15446 0.05700  0.05669  -0.01623 90  LEU C CA    
3400 C C     . LEU C 91  ? 0.20151 0.19933 0.16815 0.05609  0.04524  -0.01862 90  LEU C C     
3401 O O     . LEU C 91  ? 0.18774 0.18847 0.17019 0.05561  0.04122  -0.01607 90  LEU C O     
3402 C CB    . LEU C 91  ? 0.19702 0.21290 0.16144 0.04853  0.05666  -0.00774 90  LEU C CB    
3403 C CG    . LEU C 91  ? 0.24023 0.26696 0.20140 0.04877  0.06930  -0.00462 90  LEU C CG    
3404 C CD1   . LEU C 91  ? 0.26512 0.29630 0.22925 0.04046  0.07039  0.00462  90  LEU C CD1   
3405 C CD2   . LEU C 91  ? 0.28164 0.30004 0.21712 0.05352  0.07388  -0.00971 90  LEU C CD2   
3406 N N     . LYS C 92  ? 0.22330 0.20678 0.17300 0.05552  0.03992  -0.02348 91  LYS C N     
3407 C CA    . LYS C 92  ? 0.17644 0.14659 0.12749 0.05422  0.03047  -0.02653 91  LYS C CA    
3408 C C     . LYS C 92  ? 0.17993 0.14579 0.12614 0.04605  0.02241  -0.02352 91  LYS C C     
3409 O O     . LYS C 92  ? 0.18746 0.15819 0.12645 0.04279  0.02317  -0.01995 91  LYS C O     
3410 C CB    . LYS C 92  ? 0.19840 0.15445 0.13786 0.06053  0.03013  -0.03673 91  LYS C CB    
3411 C CG    . LYS C 92  ? 0.23583 0.19550 0.18215 0.07049  0.03803  -0.04074 91  LYS C CG    
3412 C CD    . LYS C 92  ? 0.24906 0.19173 0.18268 0.07706  0.03730  -0.05201 91  LYS C CD    
3413 C CE    . LYS C 92  ? 0.29489 0.24010 0.24122 0.08563  0.04234  -0.05507 91  LYS C CE    
3414 N NZ    . LYS C 92  ? 0.33300 0.26102 0.27018 0.08843  0.03993  -0.06497 91  LYS C NZ    
3415 N N     . HIS C 93  ? 0.17111 0.12802 0.12269 0.04296  0.01496  -0.02435 92  HIS C N     
3416 C CA    . HIS C 93  ? 0.16385 0.11830 0.11536 0.03541  0.00743  -0.02209 92  HIS C CA    
3417 C C     . HIS C 93  ? 0.24045 0.18444 0.17737 0.03480  0.00224  -0.02961 92  HIS C C     
3418 O O     . HIS C 93  ? 0.26391 0.19645 0.20137 0.03290  -0.00323 -0.03456 92  HIS C O     
3419 C CB    . HIS C 93  ? 0.18542 0.13634 0.14969 0.03186  0.00342  -0.01913 92  HIS C CB    
3420 C CG    . HIS C 93  ? 0.17052 0.13138 0.14705 0.03262  0.00682  -0.01260 92  HIS C CG    
3421 N ND1   . HIS C 93  ? 0.18051 0.14294 0.16274 0.03892  0.01050  -0.01284 92  HIS C ND1   
3422 C CD2   . HIS C 93  ? 0.15896 0.12912 0.14310 0.02828  0.00653  -0.00645 92  HIS C CD2   
3423 C CE1   . HIS C 93  ? 0.15796 0.13093 0.15093 0.03780  0.01139  -0.00701 92  HIS C CE1   
3424 N NE2   . HIS C 93  ? 0.15905 0.13590 0.15247 0.03117  0.00922  -0.00341 92  HIS C NE2   
3425 N N     . THR C 94  ? 0.20852 0.15590 0.13147 0.03617  0.00376  -0.03038 93  THR C N     
3426 C CA    . THR C 94  ? 0.23373 0.17172 0.13855 0.03761  -0.00052 -0.03888 93  THR C CA    
3427 C C     . THR C 94  ? 0.25382 0.19027 0.15649 0.03143  -0.01125 -0.03951 93  THR C C     
3428 O O     . THR C 94  ? 0.27901 0.20724 0.16826 0.03159  -0.01738 -0.04765 93  THR C O     
3429 C CB    . THR C 94  ? 0.29475 0.23668 0.18191 0.04292  0.00674  -0.03932 93  THR C CB    
3430 O OG1   . THR C 94  ? 0.23741 0.18994 0.12599 0.04020  0.00879  -0.02960 93  THR C OG1   
3431 C CG2   . THR C 94  ? 0.26158 0.20566 0.15173 0.04986  0.01750  -0.04133 93  THR C CG2   
3432 N N     . GLY C 95  ? 0.20342 0.14804 0.11933 0.02637  -0.01403 -0.03206 94  GLY C N     
3433 C CA    . GLY C 95  ? 0.19614 0.14227 0.11306 0.02148  -0.02387 -0.03259 94  GLY C CA    
3434 C C     . GLY C 95  ? 0.20163 0.15874 0.13001 0.01875  -0.02418 -0.02361 94  GLY C C     
3435 O O     . GLY C 95  ? 0.22455 0.18706 0.16130 0.01932  -0.01722 -0.01723 94  GLY C O     
3436 N N     . PRO C 96  ? 0.18392 0.14469 0.11390 0.01597  -0.03290 -0.02365 95  PRO C N     
3437 C CA    . PRO C 96  ? 0.18816 0.15854 0.13137 0.01400  -0.03360 -0.01625 95  PRO C CA    
3438 C C     . PRO C 96  ? 0.19285 0.16625 0.12875 0.01783  -0.02769 -0.00880 95  PRO C C     
3439 O O     . PRO C 96  ? 0.18703 0.15726 0.10485 0.02158  -0.02694 -0.00851 95  PRO C O     
3440 C CB    . PRO C 96  ? 0.19678 0.17068 0.14172 0.01195  -0.04510 -0.01920 95  PRO C CB    
3441 C CG    . PRO C 96  ? 0.20202 0.16839 0.14301 0.00940  -0.05040 -0.02867 95  PRO C CG    
3442 C CD    . PRO C 96  ? 0.23452 0.19116 0.15839 0.01400  -0.04337 -0.03161 95  PRO C CD    
3443 N N     . GLY C 97  ? 0.15398 0.13278 0.10331 0.01642  -0.02337 -0.00279 96  GLY C N     
3444 C CA    . GLY C 97  ? 0.18505 0.16562 0.13083 0.01849  -0.01786 0.00439  96  GLY C CA    
3445 C C     . GLY C 97  ? 0.18534 0.16620 0.13188 0.01911  -0.00794 0.00623  96  GLY C C     
3446 O O     . GLY C 97  ? 0.15185 0.13455 0.09837 0.01930  -0.00278 0.01218  96  GLY C O     
3447 N N     . ILE C 98  ? 0.15015 0.12914 0.09848 0.01947  -0.00546 0.00134  97  ILE C N     
3448 C CA    . ILE C 98  ? 0.16793 0.14957 0.12005 0.02093  0.00304  0.00270  97  ILE C CA    
3449 C C     . ILE C 98  ? 0.13664 0.12395 0.10464 0.01788  0.00461  0.00703  97  ILE C C     
3450 O O     . ILE C 98  ? 0.13204 0.11953 0.10894 0.01524  0.00045  0.00638  97  ILE C O     
3451 C CB    . ILE C 98  ? 0.15209 0.12924 0.10341 0.02335  0.00397  -0.00370 97  ILE C CB    
3452 C CG1   . ILE C 98  ? 0.18510 0.15630 0.11825 0.02722  0.00417  -0.00909 97  ILE C CG1   
3453 C CG2   . ILE C 98  ? 0.18541 0.16773 0.14725 0.02508  0.01071  -0.00201 97  ILE C CG2   
3454 C CD1   . ILE C 98  ? 0.17679 0.15164 0.10117 0.03121  0.01362  -0.00735 97  ILE C CD1   
3455 N N     . LEU C 99  ? 0.12176 0.11395 0.09319 0.01785  0.01094  0.01111  98  LEU C N     
3456 C CA    . LEU C 99  ? 0.11322 0.11046 0.09826 0.01485  0.01205  0.01419  98  LEU C CA    
3457 C C     . LEU C 99  ? 0.13619 0.13849 0.12924 0.01619  0.01587  0.01277  98  LEU C C     
3458 O O     . LEU C 99  ? 0.09708 0.10318 0.08874 0.01845  0.02171  0.01287  98  LEU C O     
3459 C CB    . LEU C 99  ? 0.10932 0.10773 0.09434 0.01283  0.01505  0.01971  98  LEU C CB    
3460 C CG    . LEU C 99  ? 0.14289 0.14501 0.14081 0.00922  0.01587  0.02188  98  LEU C CG    
3461 C CD1   . LEU C 99  ? 0.10166 0.10215 0.10473 0.00809  0.01010  0.02006  98  LEU C CD1   
3462 C CD2   . LEU C 99  ? 0.14144 0.14159 0.13817 0.00689  0.01943  0.02738  98  LEU C CD2   
3463 N N     . SER C 100 ? 0.11096 0.11393 0.11228 0.01524  0.01272  0.01173  99  SER C N     
3464 C CA    . SER C 100 ? 0.12953 0.13578 0.13733 0.01791  0.01393  0.01034  99  SER C CA    
3465 C C     . SER C 100 ? 0.12550 0.13590 0.14269 0.01528  0.01141  0.01214  99  SER C C     
3466 O O     . SER C 100 ? 0.10399 0.11236 0.12111 0.01186  0.00871  0.01305  99  SER C O     
3467 C CB    . SER C 100 ? 0.11504 0.11308 0.11761 0.02105  0.01142  0.00657  99  SER C CB    
3468 O OG    . SER C 100 ? 0.11465 0.11427 0.12274 0.02545  0.01250  0.00553  99  SER C OG    
3469 N N     . MET C 101 ? 0.09719 0.11409 0.12235 0.01748  0.01210  0.01217  100 MET C N     
3470 C CA    . MET C 101 ? 0.13093 0.15245 0.16320 0.01542  0.00873  0.01335  100 MET C CA    
3471 C C     . MET C 101 ? 0.12588 0.14074 0.15428 0.01681  0.00437  0.01352  100 MET C C     
3472 O O     . MET C 101 ? 0.09045 0.10073 0.11706 0.02124  0.00384  0.01288  100 MET C O     
3473 C CB    . MET C 101 ? 0.11248 0.14565 0.15633 0.01720  0.00986  0.01338  100 MET C CB    
3474 C CG    . MET C 101 ? 0.09180 0.13291 0.14241 0.01366  0.01467  0.01427  100 MET C CG    
3475 S SD    . MET C 101 ? 0.10862 0.14633 0.15861 0.00628  0.01265  0.01540  100 MET C SD    
3476 C CE    . MET C 101 ? 0.10994 0.15388 0.16760 0.00513  0.00599  0.01365  100 MET C CE    
3477 N N     . ALA C 102 ? 0.08135 0.09492 0.10810 0.01318  0.00181  0.01450  101 ALA C N     
3478 C CA    . ALA C 102 ? 0.11186 0.12030 0.13442 0.01393  -0.00138 0.01604  101 ALA C CA    
3479 C C     . ALA C 102 ? 0.12757 0.14233 0.15457 0.01691  -0.00473 0.01707  101 ALA C C     
3480 O O     . ALA C 102 ? 0.09104 0.11579 0.12632 0.01658  -0.00480 0.01587  101 ALA C O     
3481 C CB    . ALA C 102 ? 0.09717 0.10329 0.11542 0.00937  -0.00164 0.01649  101 ALA C CB    
3482 N N     . ASN C 103 ? 0.09855 0.10745 0.12050 0.01962  -0.00795 0.01966  102 ASN C N     
3483 C CA    . ASN C 103 ? 0.10446 0.11935 0.12986 0.02366  -0.01293 0.02111  102 ASN C CA    
3484 C C     . ASN C 103 ? 0.11716 0.12184 0.13195 0.02554  -0.01640 0.02561  102 ASN C C     
3485 O O     . ASN C 103 ? 0.11589 0.10914 0.12290 0.02328  -0.01387 0.02747  102 ASN C O     
3486 C CB    . ASN C 103 ? 0.13188 0.15345 0.16816 0.02987  -0.01257 0.01980  102 ASN C CB    
3487 C CG    . ASN C 103 ? 0.11698 0.12707 0.14968 0.03504  -0.01092 0.02021  102 ASN C CG    
3488 O OD1   . ASN C 103 ? 0.17867 0.17669 0.20321 0.03660  -0.01351 0.02345  102 ASN C OD1   
3489 N ND2   . ASN C 103 ? 0.10283 0.11551 0.14066 0.03751  -0.00621 0.01682  102 ASN C ND2   
3490 N N     . ALA C 104 ? 0.12974 0.13886 0.14449 0.02937  -0.02248 0.02772  103 ALA C N     
3491 C CA    . ALA C 104 ? 0.17234 0.17087 0.17528 0.03232  -0.02640 0.03355  103 ALA C CA    
3492 C C     . ALA C 104 ? 0.15254 0.14971 0.16095 0.04154  -0.03102 0.03594  103 ALA C C     
3493 O O     . ALA C 104 ? 0.18855 0.18447 0.19166 0.04624  -0.03790 0.04038  103 ALA C O     
3494 C CB    . ALA C 104 ? 0.15630 0.15867 0.14964 0.02997  -0.03084 0.03485  103 ALA C CB    
3495 N N     . GLY C 105 ? 0.14300 0.13965 0.16097 0.04498  -0.02736 0.03295  104 GLY C N     
3496 C CA    . GLY C 105 ? 0.14327 0.14043 0.16951 0.05496  -0.03054 0.03352  104 GLY C CA    
3497 C C     . GLY C 105 ? 0.14000 0.15649 0.18449 0.05786  -0.02919 0.02820  104 GLY C C     
3498 O O     . GLY C 105 ? 0.13049 0.15791 0.18018 0.05134  -0.02556 0.02462  104 GLY C O     
3499 N N     . PRO C 106 ? 0.12717 0.14807 0.18245 0.06785  -0.03167 0.02796  105 PRO C N     
3500 C CA    . PRO C 106 ? 0.17234 0.21296 0.24719 0.07090  -0.02837 0.02290  105 PRO C CA    
3501 C C     . PRO C 106 ? 0.10743 0.16808 0.19271 0.06510  -0.03144 0.02157  105 PRO C C     
3502 O O     . PRO C 106 ? 0.11214 0.17650 0.19536 0.06511  -0.04036 0.02420  105 PRO C O     
3503 C CB    . PRO C 106 ? 0.13165 0.17166 0.21564 0.07968  -0.03157 0.02354  105 PRO C CB    
3504 C CG    . PRO C 106 ? 0.18878 0.20437 0.25673 0.08196  -0.03300 0.02780  105 PRO C CG    
3505 C CD    . PRO C 106 ? 0.14574 0.15221 0.19648 0.07504  -0.03575 0.03212  105 PRO C CD    
3506 N N     . ASN C 107 ? 0.09564 0.16824 0.19131 0.06004  -0.02415 0.01743  106 ASN C N     
3507 C CA    . ASN C 107 ? 0.08713 0.17961 0.19757 0.05440  -0.02596 0.01535  106 ASN C CA    
3508 C C     . ASN C 107 ? 0.11421 0.20269 0.21352 0.04625  -0.03179 0.01630  106 ASN C C     
3509 O O     . ASN C 107 ? 0.09814 0.19829 0.20456 0.04495  -0.03989 0.01554  106 ASN C O     
3510 C CB    . ASN C 107 ? 0.09293 0.20090 0.22159 0.06068  -0.03172 0.01378  106 ASN C CB    
3511 C CG    . ASN C 107 ? 0.10192 0.21129 0.24054 0.06723  -0.02460 0.01119  106 ASN C CG    
3512 O OD1   . ASN C 107 ? 0.09139 0.20428 0.23178 0.06540  -0.01445 0.00800  106 ASN C OD1   
3513 N ND2   . ASN C 107 ? 0.17292 0.28034 0.31586 0.07518  -0.02808 0.01528  106 ASN C ND2   
3514 N N     . THR C 108 ? 0.08443 0.15686 0.16641 0.04098  -0.02786 0.01726  107 THR C N     
3515 C CA    . THR C 108 ? 0.10627 0.17453 0.17719 0.03385  -0.03149 0.01725  107 THR C CA    
3516 C C     . THR C 108 ? 0.10810 0.17222 0.17575 0.02569  -0.02409 0.01508  107 THR C C     
3517 O O     . THR C 108 ? 0.13959 0.19483 0.19466 0.02117  -0.02434 0.01516  107 THR C O     
3518 C CB    . THR C 108 ? 0.09554 0.14830 0.14725 0.03616  -0.03544 0.02154  107 THR C CB    
3519 O OG1   . THR C 108 ? 0.11112 0.14911 0.15423 0.03698  -0.02907 0.02337  107 THR C OG1   
3520 C CG2   . THR C 108 ? 0.17272 0.22829 0.22565 0.04465  -0.04456 0.02489  107 THR C CG2   
3521 N N     . ASN C 109 ? 0.08955 0.15995 0.16790 0.02423  -0.01723 0.01343  108 ASN C N     
3522 C CA    . ASN C 109 ? 0.06294 0.12845 0.13747 0.01726  -0.01113 0.01244  108 ASN C CA    
3523 C C     . ASN C 109 ? 0.09949 0.16873 0.17650 0.01023  -0.01456 0.01019  108 ASN C C     
3524 O O     . ASN C 109 ? 0.08268 0.16428 0.17201 0.00889  -0.01917 0.00828  108 ASN C O     
3525 C CB    . ASN C 109 ? 0.08661 0.15832 0.17051 0.01706  -0.00310 0.01208  108 ASN C CB    
3526 C CG    . ASN C 109 ? 0.09938 0.16612 0.17916 0.02427  0.00083  0.01257  108 ASN C CG    
3527 O OD1   . ASN C 109 ? 0.11317 0.16644 0.17951 0.02476  0.00233  0.01307  108 ASN C OD1   
3528 N ND2   . ASN C 109 ? 0.07811 0.15619 0.17059 0.02992  0.00239  0.01170  108 ASN C ND2   
3529 N N     . GLY C 110 ? 0.06745 0.12618 0.13388 0.00586  -0.01252 0.00973  109 GLY C N     
3530 C CA    . GLY C 110 ? 0.08590 0.14452 0.15267 -0.00028 -0.01502 0.00657  109 GLY C CA    
3531 C C     . GLY C 110 ? 0.07589 0.12711 0.14122 -0.00458 -0.00880 0.00666  109 GLY C C     
3532 O O     . GLY C 110 ? 0.10769 0.16274 0.18211 -0.00680 -0.00413 0.00786  109 GLY C O     
3533 N N     . SER C 111 ? 0.08550 0.12639 0.13955 -0.00538 -0.00833 0.00586  110 SER C N     
3534 C CA    . SER C 111 ? 0.08577 0.11879 0.13769 -0.00737 -0.00334 0.00673  110 SER C CA    
3535 C C     . SER C 111 ? 0.08613 0.11219 0.12862 -0.00393 -0.00089 0.00892  110 SER C C     
3536 O O     . SER C 111 ? 0.07641 0.09791 0.11790 -0.00413 0.00253  0.01058  110 SER C O     
3537 C CB    . SER C 111 ? 0.09418 0.12155 0.14473 -0.01125 -0.00471 0.00288  110 SER C CB    
3538 O OG    . SER C 111 ? 0.11161 0.13721 0.15314 -0.00983 -0.00807 -0.00004 110 SER C OG    
3539 N N     . GLN C 112 ? 0.05876 0.08355 0.09436 -0.00118 -0.00289 0.00926  111 GLN C N     
3540 C CA    . GLN C 112 ? 0.05786 0.07647 0.08696 0.00042  -0.00070 0.01080  111 GLN C CA    
3541 C C     . GLN C 112 ? 0.08230 0.10023 0.11246 0.00269  0.00154  0.01280  111 GLN C C     
3542 O O     . GLN C 112 ? 0.07712 0.09940 0.11119 0.00478  0.00167  0.01342  111 GLN C O     
3543 C CB    . GLN C 112 ? 0.08452 0.10079 0.10622 0.00171  -0.00238 0.01163  111 GLN C CB    
3544 C CG    . GLN C 112 ? 0.09297 0.10867 0.10927 -0.00014 -0.00315 0.00931  111 GLN C CG    
3545 C CD    . GLN C 112 ? 0.10364 0.11577 0.11080 0.00047  -0.00245 0.01159  111 GLN C CD    
3546 O OE1   . GLN C 112 ? 0.10336 0.11188 0.11012 0.00066  -0.00020 0.01404  111 GLN C OE1   
3547 N NE2   . GLN C 112 ? 0.11474 0.12735 0.11375 0.00034  -0.00447 0.01089  111 GLN C NE2   
3548 N N     . PHE C 113 ? 0.07274 0.08582 0.09945 0.00273  0.00309  0.01321  112 PHE C N     
3549 C CA    . PHE C 113 ? 0.07197 0.08313 0.09664 0.00465  0.00475  0.01407  112 PHE C CA    
3550 C C     . PHE C 113 ? 0.07454 0.08068 0.09484 0.00470  0.00355  0.01355  112 PHE C C     
3551 O O     . PHE C 113 ? 0.08834 0.09408 0.10930 0.00298  0.00282  0.01307  112 PHE C O     
3552 C CB    . PHE C 113 ? 0.07463 0.08626 0.10056 0.00357  0.00720  0.01535  112 PHE C CB    
3553 C CG    . PHE C 113 ? 0.11651 0.12435 0.14206 0.00199  0.00633  0.01549  112 PHE C CG    
3554 C CD1   . PHE C 113 ? 0.12850 0.13652 0.15846 -0.00038 0.00601  0.01439  112 PHE C CD1   
3555 C CD2   . PHE C 113 ? 0.06496 0.06917 0.08630 0.00342  0.00510  0.01592  112 PHE C CD2   
3556 C CE1   . PHE C 113 ? 0.10011 0.10373 0.13041 -0.00046 0.00543  0.01380  112 PHE C CE1   
3557 C CE2   . PHE C 113 ? 0.09492 0.09680 0.11796 0.00342  0.00379  0.01594  112 PHE C CE2   
3558 C CZ    . PHE C 113 ? 0.14808 0.14920 0.17567 0.00192  0.00444  0.01493  112 PHE C CZ    
3559 N N     . PHE C 114 ? 0.07984 0.08289 0.09614 0.00648  0.00353  0.01306  113 PHE C N     
3560 C CA    . PHE C 114 ? 0.10273 0.10219 0.11671 0.00564  0.00130  0.01185  113 PHE C CA    
3561 C C     . PHE C 114 ? 0.09131 0.08871 0.09946 0.00742  0.00065  0.01119  113 PHE C C     
3562 O O     . PHE C 114 ? 0.10889 0.10612 0.11288 0.00973  0.00313  0.01133  113 PHE C O     
3563 C CB    . PHE C 114 ? 0.08320 0.07821 0.09638 0.00501  0.00007  0.01090  113 PHE C CB    
3564 C CG    . PHE C 114 ? 0.14014 0.13074 0.14960 0.00830  0.00046  0.00982  113 PHE C CG    
3565 C CD1   . PHE C 114 ? 0.11228 0.10529 0.12372 0.01097  0.00186  0.01111  113 PHE C CD1   
3566 C CD2   . PHE C 114 ? 0.09981 0.08402 0.10454 0.00910  -0.00115 0.00677  113 PHE C CD2   
3567 C CE1   . PHE C 114 ? 0.11482 0.10443 0.12472 0.01542  0.00246  0.00976  113 PHE C CE1   
3568 C CE2   . PHE C 114 ? 0.12606 0.10477 0.12715 0.01315  -0.00034 0.00467  113 PHE C CE2   
3569 C CZ    . PHE C 114 ? 0.12595 0.10768 0.13023 0.01680  0.00188  0.00638  113 PHE C CZ    
3570 N N     . ILE C 115 ? 0.09698 0.09396 0.10491 0.00660  -0.00261 0.01054  114 ILE C N     
3571 C CA    . ILE C 115 ? 0.08105 0.07543 0.08116 0.00836  -0.00545 0.00944  114 ILE C CA    
3572 C C     . ILE C 115 ? 0.10059 0.09170 0.09998 0.00705  -0.00926 0.00528  114 ILE C C     
3573 O O     . ILE C 115 ? 0.09366 0.08696 0.10114 0.00394  -0.01153 0.00446  114 ILE C O     
3574 C CB    . ILE C 115 ? 0.10244 0.09878 0.10376 0.00893  -0.00846 0.01147  114 ILE C CB    
3575 C CG1   . ILE C 115 ? 0.12537 0.12229 0.12909 0.00923  -0.00477 0.01541  114 ILE C CG1   
3576 C CG2   . ILE C 115 ? 0.11110 0.10450 0.10138 0.01139  -0.01251 0.01104  114 ILE C CG2   
3577 C CD1   . ILE C 115 ? 0.09565 0.09307 0.10368 0.01042  -0.00786 0.01714  114 ILE C CD1   
3578 N N     . CYS C 116 ? 0.11417 0.09986 0.10440 0.00910  -0.00955 0.00224  115 CYS C N     
3579 C CA    . CYS C 116 ? 0.13039 0.11066 0.11940 0.00730  -0.01406 -0.00273 115 CYS C CA    
3580 C C     . CYS C 116 ? 0.16758 0.15038 0.15623 0.00589  -0.02104 -0.00474 115 CYS C C     
3581 O O     . CYS C 116 ? 0.11962 0.10419 0.10056 0.00879  -0.02275 -0.00331 115 CYS C O     
3582 C CB    . CYS C 116 ? 0.11632 0.08886 0.09423 0.01081  -0.01279 -0.00692 115 CYS C CB    
3583 S SG    . CYS C 116 ? 0.17572 0.14722 0.15603 0.01430  -0.00566 -0.00507 115 CYS C SG    
3584 N N     . THR C 117 ? 0.13474 0.11768 0.13193 0.00131  -0.02540 -0.00780 116 THR C N     
3585 C CA    . THR C 117 ? 0.12777 0.11385 0.12617 -0.00028 -0.03376 -0.01146 116 THR C CA    
3586 C C     . THR C 117 ? 0.19482 0.17203 0.18675 -0.00226 -0.03866 -0.01875 116 THR C C     
3587 O O     . THR C 117 ? 0.14787 0.12742 0.14093 -0.00439 -0.04715 -0.02325 116 THR C O     
3588 C CB    . THR C 117 ? 0.13284 0.12897 0.14953 -0.00466 -0.03552 -0.01014 116 THR C CB    
3589 O OG1   . THR C 117 ? 0.16807 0.16151 0.19366 -0.01008 -0.03173 -0.01031 116 THR C OG1   
3590 C CG2   . THR C 117 ? 0.13883 0.14223 0.16022 -0.00158 -0.03149 -0.00447 116 THR C CG2   
3591 N N     . ALA C 118 ? 0.14827 0.11519 0.13373 -0.00112 -0.03411 -0.02051 117 ALA C N     
3592 C CA    . ALA C 118 ? 0.17803 0.13309 0.15517 -0.00167 -0.03765 -0.02825 117 ALA C CA    
3593 C C     . ALA C 118 ? 0.20803 0.15484 0.17417 0.00445  -0.03067 -0.02859 117 ALA C C     
3594 O O     . ALA C 118 ? 0.21550 0.16675 0.18439 0.00731  -0.02382 -0.02258 117 ALA C O     
3595 C CB    . ALA C 118 ? 0.21046 0.16022 0.20047 -0.00924 -0.03994 -0.03058 117 ALA C CB    
3596 N N     . LYS C 119 ? 0.17834 0.11380 0.13278 0.00666  -0.03273 -0.03644 118 LYS C N     
3597 C CA    . LYS C 119 ? 0.24453 0.17129 0.19254 0.01262  -0.02607 -0.03811 118 LYS C CA    
3598 C C     . LYS C 119 ? 0.22448 0.14679 0.18583 0.01040  -0.02294 -0.03383 118 LYS C C     
3599 O O     . LYS C 119 ? 0.26084 0.17715 0.23057 0.00382  -0.02688 -0.03465 118 LYS C O     
3600 C CB    . LYS C 119 ? 0.23835 0.15146 0.17213 0.01505  -0.02960 -0.04906 118 LYS C CB    
3601 C CG    . LYS C 119 ? 0.26870 0.17287 0.19421 0.02332  -0.02253 -0.05285 118 LYS C CG    
3602 C CD    . LYS C 119 ? 0.32519 0.21505 0.23480 0.02552  -0.02679 -0.06539 118 LYS C CD    
3603 C CE    . LYS C 119 ? 0.40729 0.29016 0.30633 0.03559  -0.01884 -0.07064 118 LYS C CE    
3604 N NZ    . LYS C 119 ? 0.48254 0.35307 0.39227 0.03765  -0.01671 -0.07124 118 LYS C NZ    
3605 N N     . THR C 120 ? 0.21837 0.14438 0.18205 0.01551  -0.01597 -0.02862 119 THR C N     
3606 C CA    . THR C 120 ? 0.23488 0.15680 0.20834 0.01497  -0.01355 -0.02363 119 THR C CA    
3607 C C     . THR C 120 ? 0.20217 0.11824 0.17217 0.02372  -0.00899 -0.02529 119 THR C C     
3608 O O     . THR C 120 ? 0.19739 0.12171 0.17277 0.02745  -0.00483 -0.01986 119 THR C O     
3609 C CB    . THR C 120 ? 0.20021 0.13539 0.18305 0.01229  -0.01119 -0.01494 119 THR C CB    
3610 O OG1   . THR C 120 ? 0.18024 0.12667 0.16087 0.01687  -0.00708 -0.01268 119 THR C OG1   
3611 C CG2   . THR C 120 ? 0.17934 0.12077 0.16809 0.00471  -0.01499 -0.01371 119 THR C CG2   
3612 N N     . GLU C 121 ? 0.21612 0.11823 0.17818 0.02714  -0.01025 -0.03348 120 GLU C N     
3613 C CA    . GLU C 121 ? 0.24029 0.13824 0.19858 0.03725  -0.00529 -0.03700 120 GLU C CA    
3614 C C     . GLU C 121 ? 0.24566 0.13811 0.21352 0.04107  -0.00400 -0.03188 120 GLU C C     
3615 O O     . GLU C 121 ? 0.22107 0.11662 0.19099 0.05025  0.00047  -0.03236 120 GLU C O     
3616 C CB    . GLU C 121 ? 0.28462 0.16695 0.23069 0.04029  -0.00723 -0.04849 120 GLU C CB    
3617 C CG    . GLU C 121 ? 0.34811 0.20905 0.29629 0.03672  -0.01259 -0.05214 120 GLU C CG    
3618 C CD    . GLU C 121 ? 0.38197 0.24032 0.33221 0.02485  -0.01988 -0.05283 120 GLU C CD    
3619 O OE1   . GLU C 121 ? 0.39420 0.26745 0.34414 0.02039  -0.02156 -0.05071 120 GLU C OE1   
3620 O OE2   . GLU C 121 ? 0.54383 0.38501 0.49729 0.01991  -0.02399 -0.05539 120 GLU C OE2   
3621 N N     . TRP C 122 ? 0.19872 0.08398 0.17262 0.03456  -0.00767 -0.02654 121 TRP C N     
3622 C CA    . TRP C 122 ? 0.21572 0.09515 0.19604 0.03838  -0.00721 -0.02007 121 TRP C CA    
3623 C C     . TRP C 122 ? 0.19580 0.09391 0.18291 0.04125  -0.00442 -0.01273 121 TRP C C     
3624 O O     . TRP C 122 ? 0.18431 0.08052 0.17613 0.04635  -0.00475 -0.00768 121 TRP C O     
3625 C CB    . TRP C 122 ? 0.24007 0.10674 0.22289 0.02966  -0.01081 -0.01519 121 TRP C CB    
3626 C CG    . TRP C 122 ? 0.22332 0.10350 0.21012 0.01994  -0.01119 -0.01012 121 TRP C CG    
3627 C CD1   . TRP C 122 ? 0.22596 0.11677 0.21723 0.01797  -0.00968 -0.00145 121 TRP C CD1   
3628 C CD2   . TRP C 122 ? 0.21415 0.09867 0.20102 0.01175  -0.01358 -0.01416 121 TRP C CD2   
3629 N NE1   . TRP C 122 ? 0.21888 0.12000 0.21329 0.00956  -0.00986 -0.00018 121 TRP C NE1   
3630 C CE2   . TRP C 122 ? 0.22997 0.12801 0.22299 0.00575  -0.01254 -0.00746 121 TRP C CE2   
3631 C CE3   . TRP C 122 ? 0.21734 0.09568 0.19955 0.00931  -0.01720 -0.02332 121 TRP C CE3   
3632 C CZ2   . TRP C 122 ? 0.20956 0.11640 0.20649 -0.00176 -0.01464 -0.00920 121 TRP C CZ2   
3633 C CZ3   . TRP C 122 ? 0.28221 0.16964 0.26769 0.00125  -0.02053 -0.02475 121 TRP C CZ3   
3634 C CH2   . TRP C 122 ? 0.18023 0.08212 0.17416 -0.00387 -0.01907 -0.01749 121 TRP C CH2   
3635 N N     . LEU C 123 ? 0.16584 0.08093 0.15344 0.03809  -0.00249 -0.01204 122 LEU C N     
3636 C CA    . LEU C 123 ? 0.20251 0.13478 0.19700 0.03976  -0.00013 -0.00644 122 LEU C CA    
3637 C C     . LEU C 123 ? 0.17029 0.11282 0.16697 0.04786  0.00476  -0.00967 122 LEU C C     
3638 O O     . LEU C 123 ? 0.16735 0.12392 0.17259 0.04997  0.00644  -0.00567 122 LEU C O     
3639 C CB    . LEU C 123 ? 0.13439 0.07772 0.12939 0.03171  -0.00038 -0.00358 122 LEU C CB    
3640 C CG    . LEU C 123 ? 0.13536 0.07345 0.13124 0.02363  -0.00359 0.00014  122 LEU C CG    
3641 C CD1   . LEU C 123 ? 0.14449 0.09404 0.14191 0.01761  -0.00346 0.00143  122 LEU C CD1   
3642 C CD2   . LEU C 123 ? 0.14408 0.07976 0.14314 0.02408  -0.00447 0.00684  122 LEU C CD2   
3643 N N     . ASP C 124 ? 0.16309 0.09936 0.15239 0.05208  0.00722  -0.01721 123 ASP C N     
3644 C CA    . ASP C 124 ? 0.18349 0.12926 0.17449 0.06037  0.01371  -0.02085 123 ASP C CA    
3645 C C     . ASP C 124 ? 0.16760 0.11765 0.17113 0.06864  0.01433  -0.01844 123 ASP C C     
3646 O O     . ASP C 124 ? 0.19286 0.12865 0.19733 0.07261  0.01043  -0.01842 123 ASP C O     
3647 C CB    . ASP C 124 ? 0.18707 0.12090 0.16587 0.06502  0.01586  -0.03050 123 ASP C CB    
3648 C CG    . ASP C 124 ? 0.25491 0.18702 0.22019 0.05848  0.01471  -0.03366 123 ASP C CG    
3649 O OD1   . ASP C 124 ? 0.19359 0.13547 0.16022 0.05138  0.01346  -0.02801 123 ASP C OD1   
3650 O OD2   . ASP C 124 ? 0.23636 0.15648 0.18923 0.06106  0.01438  -0.04231 123 ASP C OD2   
3651 N N     . GLY C 125 ? 0.18287 0.15231 0.19654 0.07163  0.01915  -0.01658 124 GLY C N     
3652 C CA    . GLY C 125 ? 0.17129 0.14860 0.19943 0.07993  0.01885  -0.01468 124 GLY C CA    
3653 C C     . GLY C 125 ? 0.21616 0.19765 0.25204 0.07643  0.01202  -0.00678 124 GLY C C     
3654 O O     . GLY C 125 ? 0.17478 0.16549 0.22345 0.08310  0.01011  -0.00452 124 GLY C O     
3655 N N     . LYS C 126 ? 0.15837 0.13471 0.18698 0.06658  0.00826  -0.00286 125 LYS C N     
3656 C CA    . LYS C 126 ? 0.13195 0.11123 0.16415 0.06276  0.00243  0.00407  125 LYS C CA    
3657 C C     . LYS C 126 ? 0.11874 0.11002 0.15166 0.05366  0.00304  0.00659  125 LYS C C     
3658 O O     . LYS C 126 ? 0.16380 0.16292 0.20184 0.05174  -0.00073 0.01078  125 LYS C O     
3659 C CB    . LYS C 126 ? 0.16603 0.12504 0.18864 0.06007  -0.00244 0.00702  125 LYS C CB    
3660 C CG    . LYS C 126 ? 0.30372 0.24651 0.32524 0.06881  -0.00410 0.00549  125 LYS C CG    
3661 C CD    . LYS C 126 ? 0.41675 0.33918 0.42971 0.06464  -0.00857 0.01039  125 LYS C CD    
3662 C CE    . LYS C 126 ? 0.44593 0.35335 0.46007 0.07257  -0.01091 0.01097  125 LYS C CE    
3663 N NZ    . LYS C 126 ? 0.44782 0.37011 0.47350 0.08010  -0.01288 0.01381  125 LYS C NZ    
3664 N N     . HIS C 127 ? 0.11156 0.10336 0.13859 0.04853  0.00699  0.00401  126 HIS C N     
3665 C CA    . HIS C 127 ? 0.09879 0.10051 0.12694 0.04114  0.00816  0.00607  126 HIS C CA    
3666 C C     . HIS C 127 ? 0.11674 0.12748 0.14610 0.04190  0.01500  0.00349  126 HIS C C     
3667 O O     . HIS C 127 ? 0.10806 0.11241 0.12950 0.04504  0.01833  -0.00062 126 HIS C O     
3668 C CB    . HIS C 127 ? 0.10887 0.10087 0.12755 0.03394  0.00574  0.00696  126 HIS C CB    
3669 C CG    . HIS C 127 ? 0.10987 0.09449 0.12701 0.03190  0.00097  0.01051  126 HIS C CG    
3670 N ND1   . HIS C 127 ? 0.09736 0.08726 0.11579 0.02716  -0.00097 0.01396  126 HIS C ND1   
3671 C CD2   . HIS C 127 ? 0.10956 0.08089 0.12285 0.03403  -0.00164 0.01141  126 HIS C CD2   
3672 C CE1   . HIS C 127 ? 0.10756 0.08896 0.12188 0.02652  -0.00398 0.01718  126 HIS C CE1   
3673 N NE2   . HIS C 127 ? 0.11326 0.08282 0.12479 0.03026  -0.00447 0.01634  126 HIS C NE2   
3674 N N     . VAL C 128 ? 0.09879 0.12358 0.13724 0.03881  0.01726  0.00579  127 VAL C N     
3675 C CA    . VAL C 128 ? 0.09082 0.12471 0.13102 0.03842  0.02503  0.00504  127 VAL C CA    
3676 C C     . VAL C 128 ? 0.10911 0.13612 0.13659 0.03276  0.02626  0.00605  127 VAL C C     
3677 O O     . VAL C 128 ? 0.11529 0.14165 0.14305 0.02675  0.02310  0.00900  127 VAL C O     
3678 C CB    . VAL C 128 ? 0.09654 0.14755 0.15344 0.03606  0.02678  0.00744  127 VAL C CB    
3679 C CG1   . VAL C 128 ? 0.08581 0.14567 0.14466 0.03333  0.03606  0.00836  127 VAL C CG1   
3680 C CG2   . VAL C 128 ? 0.08477 0.14472 0.15558 0.04332  0.02472  0.00609  127 VAL C CG2   
3681 N N     . VAL C 129 ? 0.11675 0.13868 0.13259 0.03546  0.03063  0.00326  128 VAL C N     
3682 C CA    . VAL C 129 ? 0.12076 0.13758 0.12359 0.03153  0.03167  0.00462  128 VAL C CA    
3683 C C     . VAL C 129 ? 0.15134 0.17816 0.15753 0.02876  0.03919  0.00873  128 VAL C C     
3684 O O     . VAL C 129 ? 0.12669 0.16308 0.13892 0.03186  0.04673  0.00800  128 VAL C O     
3685 C CB    . VAL C 129 ? 0.12722 0.13373 0.11378 0.03570  0.03203  -0.00063 128 VAL C CB    
3686 C CG1   . VAL C 129 ? 0.17746 0.17981 0.14911 0.03270  0.03223  0.00115  128 VAL C CG1   
3687 C CG2   . VAL C 129 ? 0.12309 0.11812 0.10781 0.03653  0.02446  -0.00429 128 VAL C CG2   
3688 N N     . PHE C 130 ? 0.10501 0.12946 0.10804 0.02293  0.03778  0.01326  129 PHE C N     
3689 C CA    . PHE C 130 ? 0.14547 0.17719 0.15305 0.01894  0.04472  0.01827  129 PHE C CA    
3690 C C     . PHE C 130 ? 0.11560 0.13890 0.10935 0.01573  0.04501  0.02297  129 PHE C C     
3691 O O     . PHE C 130 ? 0.16066 0.18700 0.15714 0.01153  0.05078  0.02839  129 PHE C O     
3692 C CB    . PHE C 130 ? 0.13685 0.17686 0.16327 0.01414  0.04268  0.02018  129 PHE C CB    
3693 C CG    . PHE C 130 ? 0.14817 0.18071 0.17423 0.01042  0.03459  0.02100  129 PHE C CG    
3694 C CD1   . PHE C 130 ? 0.13084 0.15993 0.15744 0.01245  0.02755  0.01775  129 PHE C CD1   
3695 C CD2   . PHE C 130 ? 0.12622 0.15467 0.15148 0.00510  0.03480  0.02521  129 PHE C CD2   
3696 C CE1   . PHE C 130 ? 0.13912 0.16279 0.16537 0.00931  0.02171  0.01816  129 PHE C CE1   
3697 C CE2   . PHE C 130 ? 0.11216 0.13431 0.13780 0.00282  0.02826  0.02498  129 PHE C CE2   
3698 C CZ    . PHE C 130 ? 0.11233 0.13311 0.13853 0.00493  0.02207  0.02117  129 PHE C CZ    
3699 N N     . GLY C 131 ? 0.12592 0.13884 0.10614 0.01738  0.03859  0.02142  130 GLY C N     
3700 C CA    . GLY C 131 ? 0.16362 0.16890 0.13061 0.01580  0.03744  0.02615  130 GLY C CA    
3701 C C     . GLY C 131 ? 0.17169 0.16854 0.12526 0.01881  0.02950  0.02248  130 GLY C C     
3702 O O     . GLY C 131 ? 0.15323 0.14908 0.10748 0.02128  0.02591  0.01619  130 GLY C O     
3703 N N     . LYS C 132 ? 0.14360 0.13403 0.08588 0.01842  0.02615  0.02667  131 LYS C N     
3704 C CA    . LYS C 132 ? 0.14877 0.13332 0.08122 0.02070  0.01690  0.02308  131 LYS C CA    
3705 C C     . LYS C 132 ? 0.15174 0.13193 0.08204 0.01983  0.01131  0.02875  131 LYS C C     
3706 O O     . LYS C 132 ? 0.16937 0.14739 0.09804 0.01838  0.01569  0.03604  131 LYS C O     
3707 C CB    . LYS C 132 ? 0.16838 0.14911 0.08042 0.02484  0.01783  0.01932  131 LYS C CB    
3708 C CG    . LYS C 132 ? 0.18879 0.16605 0.08220 0.02602  0.02276  0.02606  131 LYS C CG    
3709 C CD    . LYS C 132 ? 0.25069 0.22317 0.12013 0.03064  0.02196  0.02107  131 LYS C CD    
3710 C CE    . LYS C 132 ? 0.24538 0.21328 0.09238 0.03200  0.02659  0.02895  131 LYS C CE    
3711 N NZ    . LYS C 132 ? 0.36163 0.32643 0.18362 0.03671  0.03021  0.02369  131 LYS C NZ    
3712 N N     . VAL C 133 ? 0.14903 0.12789 0.08077 0.02071  0.00166  0.02545  132 VAL C N     
3713 C CA    . VAL C 133 ? 0.15389 0.12945 0.08424 0.02171  -0.00477 0.03023  132 VAL C CA    
3714 C C     . VAL C 133 ? 0.19997 0.16916 0.10804 0.02493  -0.00511 0.03519  132 VAL C C     
3715 O O     . VAL C 133 ? 0.19992 0.16770 0.09191 0.02724  -0.00594 0.03132  132 VAL C O     
3716 C CB    . VAL C 133 ? 0.14702 0.12554 0.08582 0.02213  -0.01486 0.02507  132 VAL C CB    
3717 C CG1   . VAL C 133 ? 0.17318 0.14925 0.10789 0.02535  -0.02287 0.02942  132 VAL C CG1   
3718 C CG2   . VAL C 133 ? 0.12675 0.11047 0.08592 0.01888  -0.01335 0.02278  132 VAL C CG2   
3719 N N     . LYS C 134 ? 0.18545 0.14932 0.09095 0.02534  -0.00459 0.04377  133 LYS C N     
3720 C CA    . LYS C 134 ? 0.21129 0.16725 0.09374 0.02853  -0.00497 0.05082  133 LYS C CA    
3721 C C     . LYS C 134 ? 0.22891 0.18202 0.10795 0.03298  -0.01815 0.05217  133 LYS C C     
3722 O O     . LYS C 134 ? 0.28680 0.23991 0.15119 0.03640  -0.02610 0.04875  133 LYS C O     
3723 C CB    . LYS C 134 ? 0.21873 0.16877 0.10018 0.02574  0.00478  0.06086  133 LYS C CB    
3724 C CG    . LYS C 134 ? 0.28941 0.23186 0.14931 0.02669  0.00688  0.06854  133 LYS C CG    
3725 C CD    . LYS C 134 ? 0.33939 0.27563 0.20702 0.02181  0.01305  0.07738  133 LYS C CD    
3726 C CE    . LYS C 134 ? 0.29562 0.23336 0.15652 0.01698  0.02565  0.08064  133 LYS C CE    
3727 N NZ    . LYS C 134 ? 0.49854 0.43112 0.33670 0.01857  0.02449  0.08549  133 LYS C NZ    
3728 N N     . GLU C 135 ? 0.21251 0.16374 0.10589 0.03336  -0.02119 0.05625  134 GLU C N     
3729 C CA    . GLU C 135 ? 0.23428 0.18559 0.13025 0.03848  -0.03390 0.05680  134 GLU C CA    
3730 C C     . GLU C 135 ? 0.22501 0.18580 0.14749 0.03714  -0.03731 0.04982  134 GLU C C     
3731 O O     . GLU C 135 ? 0.18989 0.15276 0.12691 0.03295  -0.02980 0.04799  134 GLU C O     
3732 C CB    . GLU C 135 ? 0.25566 0.19807 0.14879 0.04026  -0.03450 0.06670  134 GLU C CB    
3733 C CG    . GLU C 135 ? 0.35657 0.29380 0.22695 0.04028  -0.03340 0.07221  134 GLU C CG    
3734 C CD    . GLU C 135 ? 0.55818 0.48489 0.42626 0.03901  -0.02944 0.08291  134 GLU C CD    
3735 O OE1   . GLU C 135 ? 0.61522 0.53708 0.49242 0.03452  -0.02057 0.08556  134 GLU C OE1   
3736 O OE2   . GLU C 135 ? 0.60541 0.52851 0.46289 0.04221  -0.03565 0.08852  134 GLU C OE2   
3737 N N     . GLY C 136 ? 0.20434 0.17175 0.13292 0.04060  -0.04873 0.04587  135 GLY C N     
3738 C CA    . GLY C 136 ? 0.19454 0.17202 0.14838 0.03957  -0.05113 0.04006  135 GLY C CA    
3739 C C     . GLY C 136 ? 0.15868 0.14585 0.12211 0.03452  -0.05052 0.03067  135 GLY C C     
3740 O O     . GLY C 136 ? 0.17059 0.16451 0.15318 0.03177  -0.04754 0.02694  135 GLY C O     
3741 N N     . MET C 137 ? 0.17473 0.16156 0.12437 0.03330  -0.05309 0.02666  136 MET C N     
3742 C CA    . MET C 137 ? 0.18085 0.17494 0.14079 0.02868  -0.05444 0.01780  136 MET C CA    
3743 C C     . MET C 137 ? 0.18881 0.19414 0.16872 0.02876  -0.06318 0.01416  136 MET C C     
3744 O O     . MET C 137 ? 0.16251 0.17472 0.15783 0.02379  -0.06181 0.00857  136 MET C O     
3745 C CB    . MET C 137 ? 0.24164 0.23169 0.18276 0.02823  -0.05752 0.01297  136 MET C CB    
3746 C CG    . MET C 137 ? 0.24984 0.23364 0.18081 0.02612  -0.04668 0.01193  136 MET C CG    
3747 S SD    . MET C 137 ? 0.23672 0.22466 0.18896 0.02063  -0.03889 0.00845  136 MET C SD    
3748 C CE    . MET C 137 ? 0.31056 0.30353 0.27436 0.01665  -0.04752 -0.00034 136 MET C CE    
3749 N N     . ASN C 138 ? 0.16012 0.16783 0.14068 0.03448  -0.07203 0.01770  137 ASN C N     
3750 C CA    . ASN C 138 ? 0.15431 0.17573 0.15737 0.03528  -0.08021 0.01409  137 ASN C CA    
3751 C C     . ASN C 138 ? 0.14866 0.17556 0.17339 0.03444  -0.07227 0.01467  137 ASN C C     
3752 O O     . ASN C 138 ? 0.14100 0.18072 0.18708 0.03163  -0.07322 0.00974  137 ASN C O     
3753 C CB    . ASN C 138 ? 0.18928 0.21277 0.18784 0.04160  -0.08991 0.01758  137 ASN C CB    
3754 C CG    . ASN C 138 ? 0.18742 0.20285 0.18222 0.04768  -0.08595 0.02672  137 ASN C CG    
3755 O OD1   . ASN C 138 ? 0.18100 0.18332 0.16107 0.04802  -0.07895 0.03227  137 ASN C OD1   
3756 N ND2   . ASN C 138 ? 0.18230 0.20526 0.19074 0.05230  -0.09027 0.02826  137 ASN C ND2   
3757 N N     . ILE C 139 ? 0.16547 0.18273 0.18462 0.03609  -0.06373 0.02014  138 ILE C N     
3758 C CA    . ILE C 139 ? 0.11945 0.13974 0.15518 0.03498  -0.05556 0.01946  138 ILE C CA    
3759 C C     . ILE C 139 ? 0.12051 0.14351 0.16042 0.02731  -0.04762 0.01475  138 ILE C C     
3760 O O     . ILE C 139 ? 0.12144 0.15293 0.17791 0.02495  -0.04377 0.01144  138 ILE C O     
3761 C CB    . ILE C 139 ? 0.13819 0.14568 0.16589 0.03823  -0.05003 0.02596  138 ILE C CB    
3762 C CG1   . ILE C 139 ? 0.14266 0.14437 0.16403 0.04631  -0.05826 0.03221  138 ILE C CG1   
3763 C CG2   . ILE C 139 ? 0.11249 0.12205 0.15542 0.03739  -0.04246 0.02376  138 ILE C CG2   
3764 C CD1   . ILE C 139 ? 0.14332 0.15691 0.18315 0.05165  -0.06511 0.02979  138 ILE C CD1   
3765 N N     . VAL C 140 ? 0.15570 0.17128 0.18009 0.02390  -0.04470 0.01469  139 VAL C N     
3766 C CA    . VAL C 140 ? 0.10116 0.11774 0.12838 0.01773  -0.03858 0.01083  139 VAL C CA    
3767 C C     . VAL C 140 ? 0.12095 0.14718 0.16115 0.01386  -0.04308 0.00535  139 VAL C C     
3768 O O     . VAL C 140 ? 0.15500 0.18576 0.20660 0.00939  -0.03789 0.00328  139 VAL C O     
3769 C CB    . VAL C 140 ? 0.10338 0.11069 0.11240 0.01656  -0.03563 0.01134  139 VAL C CB    
3770 C CG1   . VAL C 140 ? 0.11256 0.11974 0.12413 0.01141  -0.03155 0.00713  139 VAL C CG1   
3771 C CG2   . VAL C 140 ? 0.11355 0.11356 0.11427 0.01843  -0.02917 0.01689  139 VAL C CG2   
3772 N N     . GLU C 141 ? 0.13125 0.16057 0.16944 0.01503  -0.05295 0.00309  140 GLU C N     
3773 C CA    . GLU C 141 ? 0.10567 0.14535 0.15917 0.01036  -0.05836 -0.00249 140 GLU C CA    
3774 C C     . GLU C 141 ? 0.10780 0.16143 0.18521 0.01055  -0.05685 -0.00261 140 GLU C C     
3775 O O     . GLU C 141 ? 0.13521 0.19706 0.22812 0.00435  -0.05419 -0.00589 140 GLU C O     
3776 C CB    . GLU C 141 ? 0.14779 0.18895 0.19444 0.01215  -0.07109 -0.00543 140 GLU C CB    
3777 C CG    . GLU C 141 ? 0.16585 0.19399 0.18846 0.01168  -0.07206 -0.00728 140 GLU C CG    
3778 C CD    . GLU C 141 ? 0.20998 0.23773 0.21951 0.01534  -0.08471 -0.00936 140 GLU C CD    
3779 O OE1   . GLU C 141 ? 0.24312 0.28061 0.26216 0.01911  -0.09373 -0.00818 140 GLU C OE1   
3780 O OE2   . GLU C 141 ? 0.32331 0.34107 0.31227 0.01512  -0.08601 -0.01249 140 GLU C OE2   
3781 N N     . ALA C 142 ? 0.09975 0.15557 0.18053 0.01766  -0.05769 0.00100  141 ALA C N     
3782 C CA    . ALA C 142 ? 0.09918 0.16770 0.20226 0.01920  -0.05431 0.00018  141 ALA C CA    
3783 C C     . ALA C 142 ? 0.07603 0.14266 0.18174 0.01477  -0.04155 -0.00000 141 ALA C C     
3784 O O     . ALA C 142 ? 0.12861 0.20670 0.25133 0.01102  -0.03693 -0.00263 141 ALA C O     
3785 C CB    . ALA C 142 ? 0.12453 0.19193 0.22854 0.02891  -0.05768 0.00398  141 ALA C CB    
3786 N N     . MET C 143 ? 0.10878 0.16177 0.19764 0.01490  -0.03578 0.00289  142 MET C N     
3787 C CA    . MET C 143 ? 0.09914 0.15001 0.18812 0.01108  -0.02542 0.00266  142 MET C CA    
3788 C C     . MET C 143 ? 0.10157 0.15564 0.19441 0.00324  -0.02291 0.00043  142 MET C C     
3789 O O     . MET C 143 ? 0.07287 0.13284 0.17475 -0.00021 -0.01588 -0.00036 142 MET C O     
3790 C CB    . MET C 143 ? 0.11459 0.15172 0.18604 0.01192  -0.02171 0.00571  142 MET C CB    
3791 C CG    . MET C 143 ? 0.11334 0.14441 0.18057 0.01829  -0.02310 0.00879  142 MET C CG    
3792 S SD    . MET C 143 ? 0.19485 0.21165 0.24277 0.01737  -0.02005 0.01269  142 MET C SD    
3793 C CE    . MET C 143 ? 0.13712 0.15432 0.18627 0.01227  -0.01177 0.01043  142 MET C CE    
3794 N N     . GLU C 144 ? 0.06962 0.11865 0.15463 0.00041  -0.02837 -0.00059 143 GLU C N     
3795 C CA    . GLU C 144 ? 0.10893 0.15698 0.19636 -0.00714 -0.02660 -0.00253 143 GLU C CA    
3796 C C     . GLU C 144 ? 0.14521 0.20778 0.25430 -0.01182 -0.02602 -0.00477 143 GLU C C     
3797 O O     . GLU C 144 ? 0.09301 0.15586 0.20700 -0.01846 -0.01981 -0.00444 143 GLU C O     
3798 C CB    . GLU C 144 ? 0.12608 0.16581 0.20199 -0.00820 -0.03392 -0.00487 143 GLU C CB    
3799 C CG    . GLU C 144 ? 0.15817 0.19224 0.23457 -0.01563 -0.03294 -0.00729 143 GLU C CG    
3800 C CD    . GLU C 144 ? 0.19707 0.22255 0.26177 -0.01566 -0.04080 -0.01143 143 GLU C CD    
3801 O OE1   . GLU C 144 ? 0.17893 0.20884 0.24181 -0.01211 -0.04914 -0.01336 143 GLU C OE1   
3802 O OE2   . GLU C 144 ? 0.17943 0.19307 0.23556 -0.01842 -0.03885 -0.01284 143 GLU C OE2   
3803 N N     . ARG C 145 ? 0.13792 0.21325 0.26098 -0.00816 -0.03182 -0.00641 144 ARG C N     
3804 C CA    . ARG C 145 ? 0.09844 0.19108 0.24597 -0.01257 -0.03090 -0.00891 144 ARG C CA    
3805 C C     . ARG C 145 ? 0.13573 0.23525 0.29214 -0.01296 -0.01859 -0.00742 144 ARG C C     
3806 O O     . ARG C 145 ? 0.14690 0.25718 0.31680 -0.01829 -0.01360 -0.00838 144 ARG C O     
3807 C CB    . ARG C 145 ? 0.10895 0.21376 0.26784 -0.00712 -0.04065 -0.01101 144 ARG C CB    
3808 C CG    . ARG C 145 ? 0.16073 0.26021 0.30998 -0.00703 -0.05340 -0.01313 144 ARG C CG    
3809 C CD    . ARG C 145 ? 0.12005 0.23060 0.27663 -0.00229 -0.06211 -0.01443 144 ARG C CD    
3810 N NE    . ARG C 145 ? 0.23040 0.33464 0.37402 -0.00269 -0.07391 -0.01685 144 ARG C NE    
3811 C CZ    . ARG C 145 ? 0.21448 0.30996 0.33997 0.00482  -0.08121 -0.01468 144 ARG C CZ    
3812 N NH1   . ARG C 145 ? 0.10922 0.20148 0.22976 0.01340  -0.07895 -0.00957 144 ARG C NH1   
3813 N NH2   . ARG C 145 ? 0.18218 0.27047 0.29240 0.00350  -0.09024 -0.01760 144 ARG C NH2   
3814 N N     . PHE C 146 ? 0.10145 0.19257 0.24495 -0.00747 -0.01294 -0.00511 145 PHE C N     
3815 C CA    . PHE C 146 ? 0.08617 0.18168 0.23347 -0.00756 -0.00142 -0.00468 145 PHE C CA    
3816 C C     . PHE C 146 ? 0.09767 0.18409 0.23314 -0.01462 0.00640  -0.00209 145 PHE C C     
3817 O O     . PHE C 146 ? 0.13111 0.22050 0.26649 -0.01543 0.01617  -0.00144 145 PHE C O     
3818 C CB    . PHE C 146 ? 0.09569 0.18527 0.23445 0.00109  0.00033  -0.00443 145 PHE C CB    
3819 C CG    . PHE C 146 ? 0.08556 0.18369 0.23741 0.00928  -0.00533 -0.00621 145 PHE C CG    
3820 C CD1   . PHE C 146 ? 0.11178 0.22264 0.27798 0.01237  -0.00013 -0.00882 145 PHE C CD1   
3821 C CD2   . PHE C 146 ? 0.13027 0.22090 0.27452 0.01436  -0.01548 -0.00453 145 PHE C CD2   
3822 C CE1   . PHE C 146 ? 0.13957 0.25494 0.31290 0.02071  -0.00563 -0.00974 145 PHE C CE1   
3823 C CE2   . PHE C 146 ? 0.13031 0.22655 0.28420 0.02274  -0.02146 -0.00495 145 PHE C CE2   
3824 C CZ    . PHE C 146 ? 0.16653 0.27405 0.33347 0.02580  -0.01646 -0.00751 145 PHE C CZ    
3825 N N     . GLY C 147 ? 0.10221 0.17716 0.22690 -0.01903 0.00229  -0.00068 146 GLY C N     
3826 C CA    . GLY C 147 ? 0.11526 0.17971 0.22840 -0.02453 0.00830  0.00254  146 GLY C CA    
3827 C C     . GLY C 147 ? 0.09730 0.16734 0.22272 -0.03381 0.01273  0.00346  146 GLY C C     
3828 O O     . GLY C 147 ? 0.09422 0.17953 0.24001 -0.03659 0.01249  0.00107  146 GLY C O     
3829 N N     . SER C 148 ? 0.10217 0.15951 0.21585 -0.03877 0.01670  0.00738  147 SER C N     
3830 C CA    . SER C 148 ? 0.09512 0.15363 0.21800 -0.04876 0.02191  0.00984  147 SER C CA    
3831 C C     . SER C 148 ? 0.12045 0.15865 0.22713 -0.05211 0.02150  0.01391  147 SER C C     
3832 O O     . SER C 148 ? 0.11190 0.13815 0.20187 -0.04608 0.01788  0.01444  147 SER C O     
3833 C CB    . SER C 148 ? 0.09622 0.16485 0.22166 -0.05014 0.03329  0.01231  147 SER C CB    
3834 O OG    . SER C 148 ? 0.17692 0.23787 0.28551 -0.04624 0.03937  0.01570  147 SER C OG    
3835 N N     . ARG C 149 ? 0.11040 0.14466 0.22159 -0.06127 0.02531  0.01686  148 ARG C N     
3836 C CA    . ARG C 149 ? 0.19654 0.20973 0.29473 -0.06475 0.02465  0.02100  148 ARG C CA    
3837 C C     . ARG C 149 ? 0.16068 0.16257 0.23850 -0.05855 0.02785  0.02623  148 ARG C C     
3838 O O     . ARG C 149 ? 0.24136 0.22749 0.30651 -0.05501 0.02279  0.02688  148 ARG C O     
3839 C CB    . ARG C 149 ? 0.21306 0.22298 0.31233 -0.07404 0.02980  0.02480  148 ARG C CB    
3840 C CG    . ARG C 149 ? 0.28529 0.30192 0.40049 -0.08132 0.02540  0.02007  148 ARG C CG    
3841 C CD    . ARG C 149 ? 0.24973 0.25766 0.36261 -0.09122 0.03070  0.02560  148 ARG C CD    
3842 N NE    . ARG C 149 ? 0.27999 0.26271 0.37986 -0.09283 0.02695  0.02728  148 ARG C NE    
3843 C CZ    . ARG C 149 ? 0.32228 0.28777 0.40542 -0.09305 0.03144  0.03520  148 ARG C CZ    
3844 N NH1   . ARG C 149 ? 0.25406 0.22479 0.33014 -0.09296 0.03982  0.04262  148 ARG C NH1   
3845 N NH2   . ARG C 149 ? 0.27918 0.22141 0.35159 -0.09250 0.02693  0.03549  148 ARG C NH2   
3846 N N     . ASN C 150 ? 0.12288 0.13276 0.19613 -0.05663 0.03585  0.02935  149 ASN C N     
3847 C CA    . ASN C 150 ? 0.15929 0.15943 0.21165 -0.05092 0.03761  0.03379  149 ASN C CA    
3848 C C     . ASN C 150 ? 0.18973 0.19657 0.23704 -0.04164 0.03400  0.02915  149 ASN C C     
3849 O O     . ASN C 150 ? 0.19417 0.19786 0.22700 -0.03724 0.03575  0.03138  149 ASN C O     
3850 C CB    . ASN C 150 ? 0.20924 0.20971 0.25436 -0.05526 0.04846  0.04074  149 ASN C CB    
3851 C CG    . ASN C 150 ? 0.18187 0.20179 0.23526 -0.05492 0.05521  0.03731  149 ASN C CG    
3852 O OD1   . ASN C 150 ? 0.18116 0.21351 0.24713 -0.05105 0.05317  0.03089  149 ASN C OD1   
3853 N ND2   . ASN C 150 ? 0.25288 0.27516 0.29845 -0.05810 0.06306  0.04190  149 ASN C ND2   
3854 N N     . GLY C 151 ? 0.12089 0.13601 0.17936 -0.03887 0.02840  0.02295  150 GLY C N     
3855 C CA    . GLY C 151 ? 0.14458 0.16327 0.19874 -0.03095 0.02477  0.01933  150 GLY C CA    
3856 C C     . GLY C 151 ? 0.14677 0.17813 0.20581 -0.02824 0.02972  0.01681  150 GLY C C     
3857 O O     . GLY C 151 ? 0.12822 0.16179 0.18621 -0.02223 0.02633  0.01343  150 GLY C O     
3858 N N     . LYS C 152 ? 0.14767 0.18673 0.21189 -0.03233 0.03823  0.01828  151 LYS C N     
3859 C CA    . LYS C 152 ? 0.18176 0.23266 0.25042 -0.02867 0.04390  0.01474  151 LYS C CA    
3860 C C     . LYS C 152 ? 0.14096 0.20385 0.22883 -0.02581 0.03981  0.00953  151 LYS C C     
3861 O O     . LYS C 152 ? 0.11159 0.17989 0.21402 -0.02997 0.03663  0.00915  151 LYS C O     
3862 C CB    . LYS C 152 ? 0.22433 0.28180 0.29399 -0.03375 0.05553  0.01758  151 LYS C CB    
3863 C CG    . LYS C 152 ? 0.23408 0.27966 0.28129 -0.03524 0.05979  0.02339  151 LYS C CG    
3864 C CD    . LYS C 152 ? 0.27075 0.31375 0.30239 -0.02800 0.05897  0.02010  151 LYS C CD    
3865 C CE    . LYS C 152 ? 0.30787 0.33975 0.31592 -0.02873 0.06113  0.02577  151 LYS C CE    
3866 N NZ    . LYS C 152 ? 0.36428 0.39518 0.35789 -0.02265 0.06001  0.02131  151 LYS C NZ    
3867 N N     . THR C 153 ? 0.13131 0.19767 0.21929 -0.01862 0.03912  0.00543  152 THR C N     
3868 C CA    . THR C 153 ? 0.16456 0.24022 0.26899 -0.01428 0.03397  0.00146  152 THR C CA    
3869 C C     . THR C 153 ? 0.14537 0.23742 0.26631 -0.01255 0.04153  -0.00191 152 THR C C     
3870 O O     . THR C 153 ? 0.13360 0.22756 0.24848 -0.01180 0.05090  -0.00283 152 THR C O     
3871 C CB    . THR C 153 ? 0.16548 0.23282 0.26155 -0.00710 0.02755  -0.00028 152 THR C CB    
3872 O OG1   . THR C 153 ? 0.16751 0.23153 0.25380 -0.00359 0.03289  -0.00230 152 THR C OG1   
3873 C CG2   . THR C 153 ? 0.12629 0.18067 0.20929 -0.00872 0.02106  0.00274  152 THR C CG2   
3874 N N     . SER C 154 ? 0.10076 0.20528 0.24223 -0.01154 0.03703  -0.00408 153 SER C N     
3875 C CA    . SER C 154 ? 0.10708 0.22623 0.26113 -0.00935 0.04151  -0.00664 153 SER C CA    
3876 C C     . SER C 154 ? 0.16314 0.28395 0.31875 0.00105  0.04218  -0.01103 153 SER C C     
3877 O O     . SER C 154 ? 0.15942 0.29057 0.32205 0.00410  0.04848  -0.01349 153 SER C O     
3878 C CB    . SER C 154 ? 0.13287 0.26297 0.30418 -0.01210 0.03432  -0.00691 153 SER C CB    
3879 O OG    . SER C 154 ? 0.11666 0.24178 0.28906 -0.00866 0.02232  -0.00761 153 SER C OG    
3880 N N     . LYS C 155 ? 0.15902 0.26919 0.30847 0.00655  0.03596  -0.01188 154 LYS C N     
3881 C CA    . LYS C 155 ? 0.13595 0.24176 0.28284 0.01565  0.03698  -0.01580 154 LYS C CA    
3882 C C     . LYS C 155 ? 0.12397 0.21154 0.25076 0.01572  0.03421  -0.01449 154 LYS C C     
3883 O O     . LYS C 155 ? 0.14284 0.22252 0.25879 0.01017  0.03011  -0.01027 154 LYS C O     
3884 C CB    . LYS C 155 ? 0.08174 0.19146 0.24090 0.02331  0.02844  -0.01682 154 LYS C CB    
3885 C CG    . LYS C 155 ? 0.14013 0.26720 0.31607 0.02437  0.03011  -0.01812 154 LYS C CG    
3886 C CD    . LYS C 155 ? 0.20969 0.33860 0.39512 0.03378  0.02179  -0.01896 154 LYS C CD    
3887 C CE    . LYS C 155 ? 0.18961 0.33603 0.39228 0.03747  0.02534  -0.02126 154 LYS C CE    
3888 N NZ    . LYS C 155 ? 0.25016 0.41061 0.46711 0.03290  0.01912  -0.01933 154 LYS C NZ    
3889 N N     . LYS C 156 ? 0.09654 0.17616 0.21670 0.02175  0.03591  -0.01825 155 LYS C N     
3890 C CA    . LYS C 156 ? 0.15019 0.21270 0.25108 0.02089  0.03270  -0.01724 155 LYS C CA    
3891 C C     . LYS C 156 ? 0.16359 0.21724 0.26419 0.02325  0.02269  -0.01381 155 LYS C C     
3892 O O     . LYS C 156 ? 0.10065 0.15311 0.20980 0.03009  0.01930  -0.01502 155 LYS C O     
3893 C CB    . LYS C 156 ? 0.11366 0.16997 0.20759 0.02535  0.03791  -0.02348 155 LYS C CB    
3894 C CG    . LYS C 156 ? 0.27721 0.31715 0.35437 0.02363  0.03359  -0.02309 155 LYS C CG    
3895 C CD    . LYS C 156 ? 0.24534 0.28065 0.30829 0.02272  0.03918  -0.02848 155 LYS C CD    
3896 C CE    . LYS C 156 ? 0.16164 0.18549 0.20993 0.01821  0.03374  -0.02644 155 LYS C CE    
3897 N NZ    . LYS C 156 ? 0.33286 0.34979 0.36859 0.01877  0.03601  -0.03349 155 LYS C NZ    
3898 N N     . ILE C 157 ? 0.11307 0.15984 0.20294 0.01818  0.01842  -0.00928 156 ILE C N     
3899 C CA    . ILE C 157 ? 0.08290 0.12150 0.16938 0.01954  0.01045  -0.00542 156 ILE C CA    
3900 C C     . ILE C 157 ? 0.14810 0.17325 0.22178 0.01895  0.01035  -0.00513 156 ILE C C     
3901 O O     . ILE C 157 ? 0.17265 0.19513 0.23655 0.01424  0.01230  -0.00474 156 ILE C O     
3902 C CB    . ILE C 157 ? 0.06098 0.10158 0.14480 0.01466  0.00646  -0.00160 156 ILE C CB    
3903 C CG1   . ILE C 157 ? 0.07552 0.13000 0.17317 0.01266  0.00709  -0.00266 156 ILE C CG1   
3904 C CG2   . ILE C 157 ? 0.09561 0.12930 0.17505 0.01705  -0.00102 0.00193  156 ILE C CG2   
3905 C CD1   . ILE C 157 ? 0.09098 0.15490 0.20505 0.01880  0.00406  -0.00456 156 ILE C CD1   
3906 N N     . THR C 158 ? 0.10113 0.11764 0.17564 0.02349  0.00767  -0.00499 157 THR C N     
3907 C CA    . THR C 158 ? 0.10224 0.10633 0.16734 0.02163  0.00779  -0.00510 157 THR C CA    
3908 C C     . THR C 158 ? 0.10625 0.10057 0.16828 0.02250  0.00300  0.00050  157 THR C C     
3909 O O     . THR C 158 ? 0.12621 0.12103 0.19223 0.02664  -0.00102 0.00390  157 THR C O     
3910 C CB    . THR C 158 ? 0.10525 0.10379 0.17177 0.02476  0.01118  -0.01144 157 THR C CB    
3911 O OG1   . THR C 158 ? 0.13738 0.13384 0.21383 0.03224  0.00962  -0.01207 157 THR C OG1   
3912 C CG2   . THR C 158 ? 0.11417 0.12163 0.17922 0.02342  0.01730  -0.01690 157 THR C CG2   
3913 N N     . ILE C 159 ? 0.10532 0.09128 0.16005 0.01832  0.00355  0.00150  158 ILE C N     
3914 C CA    . ILE C 159 ? 0.10237 0.07737 0.15349 0.01782  0.00133  0.00690  158 ILE C CA    
3915 C C     . ILE C 159 ? 0.14331 0.10634 0.19798 0.02074  0.00174  0.00424  158 ILE C C     
3916 O O     . ILE C 159 ? 0.13903 0.09569 0.19229 0.01703  0.00354  0.00041  158 ILE C O     
3917 C CB    . ILE C 159 ? 0.12319 0.09756 0.16813 0.01126  0.00258  0.00890  158 ILE C CB    
3918 C CG1   . ILE C 159 ? 0.09116 0.07590 0.13289 0.00965  0.00234  0.01028  158 ILE C CG1   
3919 C CG2   . ILE C 159 ? 0.11630 0.08066 0.15803 0.00972  0.00220  0.01511  158 ILE C CG2   
3920 C CD1   . ILE C 159 ? 0.10844 0.09491 0.14625 0.00459  0.00378  0.01121  158 ILE C CD1   
3921 N N     . ALA C 160 ? 0.14068 0.10017 0.20061 0.02785  -0.00069 0.00574  159 ALA C N     
3922 C CA    . ALA C 160 ? 0.16582 0.11210 0.22980 0.03200  -0.00031 0.00259  159 ALA C CA    
3923 C C     . ALA C 160 ? 0.20273 0.13150 0.26159 0.02815  -0.00090 0.00758  159 ALA C C     
3924 O O     . ALA C 160 ? 0.15885 0.07483 0.21943 0.02747  0.00033  0.00320  159 ALA C O     
3925 C CB    . ALA C 160 ? 0.14369 0.09106 0.21626 0.04195  -0.00336 0.00339  159 ALA C CB    
3926 N N     . ASP C 161 ? 0.17569 0.10308 0.22815 0.02539  -0.00235 0.01643  160 ASP C N     
3927 C CA    . ASP C 161 ? 0.19761 0.11035 0.24537 0.02015  -0.00120 0.02246  160 ASP C CA    
3928 C C     . ASP C 161 ? 0.19297 0.11394 0.23347 0.01465  0.00021  0.02835  160 ASP C C     
3929 O O     . ASP C 161 ? 0.15421 0.08771 0.19193 0.01680  -0.00129 0.02893  160 ASP C O     
3930 C CB    . ASP C 161 ? 0.17550 0.07108 0.22196 0.02617  -0.00402 0.02954  160 ASP C CB    
3931 C CG    . ASP C 161 ? 0.26172 0.14073 0.30276 0.01943  -0.00161 0.03340  160 ASP C CG    
3932 O OD1   . ASP C 161 ? 0.23642 0.11505 0.28125 0.01110  0.00165  0.02936  160 ASP C OD1   
3933 O OD2   . ASP C 161 ? 0.31242 0.17894 0.34548 0.02230  -0.00334 0.04026  160 ASP C OD2   
3934 N N     . CYS C 162 ? 0.15155 0.06575 0.19009 0.00731  0.00347  0.03202  161 CYS C N     
3935 C CA    . CYS C 162 ? 0.18066 0.10295 0.21339 0.00254  0.00628  0.03712  161 CYS C CA    
3936 C C     . CYS C 162 ? 0.20178 0.11399 0.23523 -0.00513 0.01066  0.04234  161 CYS C C     
3937 O O     . CYS C 162 ? 0.19066 0.09184 0.23079 -0.00862 0.01095  0.03956  161 CYS C O     
3938 C CB    . CYS C 162 ? 0.14747 0.08681 0.18287 -0.00016 0.00709  0.03066  161 CYS C CB    
3939 S SG    . CYS C 162 ? 0.18730 0.12949 0.23181 -0.00554 0.00747  0.02062  161 CYS C SG    
3940 N N     . GLY C 163 ? 0.18734 0.10315 0.21400 -0.00797 0.01447  0.04959  162 GLY C N     
3941 C CA    . GLY C 163 ? 0.21234 0.12144 0.23924 -0.01575 0.01981  0.05514  162 GLY C CA    
3942 C C     . GLY C 163 ? 0.23197 0.14707 0.24763 -0.01627 0.02431  0.06253  162 GLY C C     
3943 O O     . GLY C 163 ? 0.17286 0.09658 0.18205 -0.01118 0.02344  0.06310  162 GLY C O     
3944 N N     . GLN C 164 ? 0.19454 0.10464 0.20725 -0.02258 0.02913  0.06754  163 GLN C N     
3945 C CA    . GLN C 164 ? 0.25333 0.16918 0.25513 -0.02385 0.03486  0.07387  163 GLN C CA    
3946 C C     . GLN C 164 ? 0.29232 0.19339 0.27667 -0.02051 0.03321  0.08245  163 GLN C C     
3947 O O     . GLN C 164 ? 0.37696 0.26270 0.36091 -0.02275 0.03163  0.08553  163 GLN C O     
3948 C CB    . GLN C 164 ? 0.21087 0.13453 0.22216 -0.03359 0.04213  0.07384  163 GLN C CB    
3949 C CG    . GLN C 164 ? 0.28719 0.22021 0.28904 -0.03441 0.04948  0.07872  163 GLN C CG    
3950 C CD    . GLN C 164 ? 0.21239 0.15931 0.22841 -0.04281 0.05651  0.07662  163 GLN C CD    
3951 O OE1   . GLN C 164 ? 0.23101 0.18249 0.26427 -0.04790 0.05467  0.07083  163 GLN C OE1   
3952 N NE2   . GLN C 164 ? 0.21877 0.17325 0.22759 -0.04405 0.06416  0.08080  163 GLN C NE2   
3953 N N     . LEU C 165 ? 0.27178 0.17679 0.24095 -0.01518 0.03298  0.08608  164 LEU C N     
3954 C CA    . LEU C 165 ? 0.35560 0.24827 0.30645 -0.01156 0.02996  0.09433  164 LEU C CA    
3955 C C     . LEU C 165 ? 0.46039 0.35226 0.40275 -0.01846 0.03834  0.10145  164 LEU C C     
3956 O O     . LEU C 165 ? 0.42917 0.33455 0.36972 -0.02049 0.04524  0.10021  164 LEU C O     
3957 C CB    . LEU C 165 ? 0.40521 0.30293 0.34315 -0.00256 0.02400  0.09386  164 LEU C CB    
3958 C CG    . LEU C 165 ? 0.35313 0.24929 0.29647 0.00549  0.01395  0.08933  164 LEU C CG    
3959 C CD1   . LEU C 165 ? 0.40080 0.30231 0.33065 0.01311  0.00726  0.08956  164 LEU C CD1   
3960 C CD2   . LEU C 165 ? 0.38858 0.26845 0.33491 0.00730  0.00858  0.09206  164 LEU C CD2   
3961 N N     . GLU C 166 ? 0.50513 0.38104 0.44282 -0.02184 0.03789  0.10878  165 GLU C N     
3962 C CA    . GLU C 166 ? 0.60608 0.47740 0.53325 -0.02829 0.04492  0.11806  165 GLU C CA    
3963 C C     . GLU C 166 ? 0.61297 0.46562 0.54451 -0.03409 0.04390  0.12321  165 GLU C C     
3964 O O     . GLU C 166 ? 0.61760 0.46310 0.56196 -0.03393 0.03934  0.11766  165 GLU C O     
3965 C CB    . GLU C 166 ? 0.67270 0.56105 0.60700 -0.03550 0.05607  0.11574  165 GLU C CB    
3966 C CG    . GLU C 166 ? 0.66719 0.55590 0.58623 -0.03942 0.06409  0.12469  165 GLU C CG    
3967 C CD    . GLU C 166 ? 0.75511 0.66427 0.67468 -0.03986 0.07280  0.12027  165 GLU C CD    
3968 O OE1   . GLU C 166 ? 0.75552 0.67487 0.67647 -0.03314 0.06982  0.11251  165 GLU C OE1   
3969 O OE2   . GLU C 166 ? 0.83435 0.74930 0.75343 -0.04682 0.08276  0.12447  165 GLU C OE2   
3970 O OXT   . GLU C 166 ? 0.63057 0.47396 0.55246 -0.03921 0.04779  0.13290  165 GLU C OXT   
3971 N N     . SER D 1   ? 0.30458 0.31929 0.23585 -0.03620 -0.03790 0.08168  0   SER D N     
3972 C CA    . SER D 1   ? 0.36701 0.38605 0.29482 -0.03481 -0.04398 0.07819  0   SER D CA    
3973 C C     . SER D 1   ? 0.36423 0.37999 0.30128 -0.03155 -0.05413 0.08487  0   SER D C     
3974 O O     . SER D 1   ? 0.32639 0.33494 0.27766 -0.02716 -0.05691 0.08902  0   SER D O     
3975 C CB    . SER D 1   ? 0.27840 0.29936 0.21677 -0.02972 -0.04165 0.06732  0   SER D CB    
3976 O OG    . SER D 1   ? 0.33995 0.36583 0.27754 -0.02931 -0.04861 0.06512  0   SER D OG    
3977 N N     . MET D 2   ? 0.36402 0.38490 0.29337 -0.03345 -0.05959 0.08502  1   MET D N     
3978 C CA    . MET D 2   ? 0.28780 0.30777 0.22712 -0.02973 -0.06928 0.09082  1   MET D CA    
3979 C C     . MET D 2   ? 0.25085 0.27374 0.20927 -0.02221 -0.07284 0.08623  1   MET D C     
3980 O O     . MET D 2   ? 0.31465 0.33642 0.28626 -0.01682 -0.07930 0.09024  1   MET D O     
3981 C CB    . MET D 2   ? 0.28433 0.30995 0.20929 -0.03478 -0.07432 0.09291  1   MET D CB    
3982 C CG    . MET D 2   ? 0.36466 0.38851 0.27142 -0.04184 -0.07173 0.09862  1   MET D CG    
3983 S SD    . MET D 2   ? 0.39035 0.40444 0.30531 -0.04051 -0.07640 0.11149  1   MET D SD    
3984 C CE    . MET D 2   ? 0.29391 0.31102 0.20476 -0.04132 -0.08833 0.11903  1   MET D CE    
3985 N N     . VAL D 3   ? 0.25023 0.27765 0.21047 -0.02174 -0.06854 0.07775  2   VAL D N     
3986 C CA    . VAL D 3   ? 0.20704 0.23976 0.18500 -0.01571 -0.07074 0.07277  2   VAL D CA    
3987 C C     . VAL D 3   ? 0.24382 0.27374 0.23117 -0.01202 -0.06468 0.06792  2   VAL D C     
3988 O O     . VAL D 3   ? 0.21999 0.25054 0.22542 -0.00497 -0.06537 0.06589  2   VAL D O     
3989 C CB    . VAL D 3   ? 0.24519 0.28766 0.21805 -0.01962 -0.07304 0.06704  2   VAL D CB    
3990 C CG1   . VAL D 3   ? 0.20295 0.24454 0.15655 -0.02661 -0.06713 0.06101  2   VAL D CG1   
3991 C CG2   . VAL D 3   ? 0.19294 0.24279 0.18472 -0.01471 -0.07367 0.06176  2   VAL D CG2   
3992 N N     . ASN D 4   ? 0.20557 0.23180 0.18199 -0.01587 -0.05583 0.06300  3   ASN D N     
3993 C CA    . ASN D 4   ? 0.17580 0.19931 0.16180 -0.01223 -0.04773 0.05466  3   ASN D CA    
3994 C C     . ASN D 4   ? 0.18809 0.20277 0.17946 -0.01003 -0.04494 0.05805  3   ASN D C     
3995 O O     . ASN D 4   ? 0.14694 0.15760 0.12876 -0.01433 -0.04453 0.06458  3   ASN D O     
3996 C CB    . ASN D 4   ? 0.15194 0.17655 0.12678 -0.01632 -0.03998 0.04632  3   ASN D CB    
3997 C CG    . ASN D 4   ? 0.16278 0.19347 0.13520 -0.01842 -0.04246 0.04080  3   ASN D CG    
3998 O OD1   . ASN D 4   ? 0.13881 0.17501 0.12282 -0.01596 -0.04780 0.04144  3   ASN D OD1   
3999 N ND2   . ASN D 4   ? 0.14629 0.17624 0.10428 -0.02310 -0.03859 0.03511  3   ASN D ND2   
4000 N N     . PRO D 5   ? 0.16839 0.18034 0.17433 -0.00418 -0.04321 0.05378  4   PRO D N     
4001 C CA    . PRO D 5   ? 0.14096 0.14324 0.15223 -0.00263 -0.04143 0.05582  4   PRO D CA    
4002 C C     . PRO D 5   ? 0.20043 0.20158 0.20484 -0.00699 -0.03329 0.05238  4   PRO D C     
4003 O O     . PRO D 5   ? 0.14027 0.14681 0.14038 -0.00823 -0.02797 0.04560  4   PRO D O     
4004 C CB    . PRO D 5   ? 0.17129 0.17263 0.19820 0.00487  -0.04154 0.04989  4   PRO D CB    
4005 C CG    . PRO D 5   ? 0.22172 0.23406 0.25041 0.00571  -0.03994 0.04348  4   PRO D CG    
4006 C CD    . PRO D 5   ? 0.14839 0.16663 0.16635 0.00072  -0.04363 0.04752  4   PRO D CD    
4007 N N     . THR D 6   ? 0.14514 0.13920 0.14952 -0.00947 -0.03287 0.05768  5   THR D N     
4008 C CA    . THR D 6   ? 0.13361 0.12841 0.13509 -0.01353 -0.02570 0.05559  5   THR D CA    
4009 C C     . THR D 6   ? 0.14831 0.13548 0.16141 -0.01099 -0.02566 0.05312  5   THR D C     
4010 O O     . THR D 6   ? 0.14199 0.11947 0.16053 -0.00986 -0.03108 0.05801  5   THR D O     
4011 C CB    . THR D 6   ? 0.17844 0.17377 0.16947 -0.02083 -0.02483 0.06450  5   THR D CB    
4012 O OG1   . THR D 6   ? 0.20922 0.21138 0.18690 -0.02346 -0.02525 0.06601  5   THR D OG1   
4013 C CG2   . THR D 6   ? 0.20735 0.20716 0.19813 -0.02478 -0.01668 0.06211  5   THR D CG2   
4014 N N     . VAL D 7   ? 0.13972 0.13019 0.15619 -0.01010 -0.02032 0.04550  6   VAL D N     
4015 C CA    . VAL D 7   ? 0.10695 0.09108 0.13216 -0.00897 -0.02045 0.04254  6   VAL D CA    
4016 C C     . VAL D 7   ? 0.14533 0.13374 0.17009 -0.01422 -0.01547 0.04289  6   VAL D C     
4017 O O     . VAL D 7   ? 0.10383 0.10131 0.12294 -0.01645 -0.01046 0.04258  6   VAL D O     
4018 C CB    . VAL D 7   ? 0.15027 0.13531 0.18103 -0.00308 -0.01991 0.03370  6   VAL D CB    
4019 C CG1   . VAL D 7   ? 0.13417 0.11705 0.16879 0.00237  -0.02453 0.03367  6   VAL D CG1   
4020 C CG2   . VAL D 7   ? 0.11962 0.11387 0.14640 -0.00301 -0.01509 0.02872  6   VAL D CG2   
4021 N N     . PHE D 8   ? 0.14445 0.12655 0.17589 -0.01621 -0.01706 0.04325  7   PHE D N     
4022 C CA    . PHE D 8   ? 0.14885 0.13674 0.18315 -0.02159 -0.01329 0.04410  7   PHE D CA    
4023 C C     . PHE D 8   ? 0.13686 0.12291 0.17845 -0.01996 -0.01417 0.03737  7   PHE D C     
4024 O O     . PHE D 8   ? 0.15546 0.13158 0.19957 -0.01687 -0.01848 0.03385  7   PHE D O     
4025 C CB    . PHE D 8   ? 0.15225 0.13582 0.18701 -0.02931 -0.01514 0.05362  7   PHE D CB    
4026 C CG    . PHE D 8   ? 0.17442 0.14237 0.21523 -0.03023 -0.02192 0.05482  7   PHE D CG    
4027 C CD1   . PHE D 8   ? 0.19225 0.14713 0.23188 -0.02728 -0.02799 0.05827  7   PHE D CD1   
4028 C CD2   . PHE D 8   ? 0.20462 0.17055 0.25272 -0.03395 -0.02282 0.05221  7   PHE D CD2   
4029 C CE1   . PHE D 8   ? 0.21603 0.15417 0.26145 -0.02717 -0.03430 0.05824  7   PHE D CE1   
4030 C CE2   . PHE D 8   ? 0.17228 0.12164 0.22471 -0.03502 -0.02942 0.05181  7   PHE D CE2   
4031 C CZ    . PHE D 8   ? 0.19650 0.13101 0.24749 -0.03129 -0.03486 0.05445  7   PHE D CZ    
4032 N N     . PHE D 9   ? 0.10327 0.09958 0.14814 -0.02184 -0.01014 0.03544  8   PHE D N     
4033 C CA    . PHE D 9   ? 0.16210 0.15857 0.21393 -0.02267 -0.01192 0.03133  8   PHE D CA    
4034 C C     . PHE D 9   ? 0.10931 0.11182 0.16776 -0.03037 -0.01107 0.03673  8   PHE D C     
4035 O O     . PHE D 9   ? 0.13373 0.14851 0.19274 -0.03235 -0.00553 0.03993  8   PHE D O     
4036 C CB    . PHE D 9   ? 0.11519 0.12047 0.16793 -0.01841 -0.00911 0.02556  8   PHE D CB    
4037 C CG    . PHE D 9   ? 0.09470 0.09620 0.14205 -0.01223 -0.00963 0.02022  8   PHE D CG    
4038 C CD1   . PHE D 9   ? 0.10327 0.09591 0.14741 -0.00972 -0.01238 0.01922  8   PHE D CD1   
4039 C CD2   . PHE D 9   ? 0.08206 0.08967 0.12895 -0.00905 -0.00745 0.01660  8   PHE D CD2   
4040 C CE1   . PHE D 9   ? 0.08570 0.07835 0.12655 -0.00481 -0.01202 0.01461  8   PHE D CE1   
4041 C CE2   . PHE D 9   ? 0.09508 0.10027 0.13720 -0.00498 -0.00767 0.01276  8   PHE D CE2   
4042 C CZ    . PHE D 9   ? 0.08947 0.08841 0.12878 -0.00324 -0.00958 0.01169  8   PHE D CZ    
4043 N N     . ASP D 10  ? 0.10311 0.09816 0.16686 -0.03489 -0.01618 0.03702  9   ASP D N     
4044 C CA    . ASP D 10  ? 0.10674 0.10993 0.17945 -0.04303 -0.01613 0.04122  9   ASP D CA    
4045 C C     . ASP D 10  ? 0.10769 0.11879 0.18659 -0.04122 -0.01735 0.03522  9   ASP D C     
4046 O O     . ASP D 10  ? 0.10149 0.10299 0.17906 -0.04007 -0.02286 0.02976  9   ASP D O     
4047 C CB    . ASP D 10  ? 0.12213 0.11126 0.19696 -0.05063 -0.02221 0.04578  9   ASP D CB    
4048 C CG    . ASP D 10  ? 0.13247 0.11614 0.20221 -0.05412 -0.02130 0.05486  9   ASP D CG    
4049 O OD1   . ASP D 10  ? 0.17488 0.17204 0.24225 -0.05552 -0.01484 0.05974  9   ASP D OD1   
4050 O OD2   . ASP D 10  ? 0.19390 0.16034 0.25985 -0.05387 -0.02677 0.05583  9   ASP D OD2   
4051 N N     . ILE D 11  ? 0.09091 0.11961 0.17586 -0.04021 -0.01216 0.03592  10  ILE D N     
4052 C CA    . ILE D 11  ? 0.08507 0.12298 0.17638 -0.03702 -0.01337 0.03155  10  ILE D CA    
4053 C C     . ILE D 11  ? 0.09840 0.14405 0.20207 -0.04488 -0.01749 0.03415  10  ILE D C     
4054 O O     . ILE D 11  ? 0.13366 0.18862 0.24512 -0.05167 -0.01477 0.04027  10  ILE D O     
4055 C CB    . ILE D 11  ? 0.09175 0.14377 0.18538 -0.03099 -0.00626 0.03087  10  ILE D CB    
4056 C CG1   . ILE D 11  ? 0.09726 0.14142 0.17832 -0.02500 -0.00280 0.02854  10  ILE D CG1   
4057 C CG2   . ILE D 11  ? 0.12862 0.18828 0.22935 -0.02678 -0.00879 0.02742  10  ILE D CG2   
4058 C CD1   . ILE D 11  ? 0.06880 0.10278 0.14293 -0.01963 -0.00662 0.02309  10  ILE D CD1   
4059 N N     . ALA D 12  ? 0.09445 0.13799 0.19982 -0.04468 -0.02408 0.02984  11  ALA D N     
4060 C CA    . ALA D 12  ? 0.12351 0.17418 0.23910 -0.05184 -0.02945 0.03119  11  ALA D CA    
4061 C C     . ALA D 12  ? 0.08700 0.15172 0.20968 -0.04745 -0.03114 0.02926  11  ALA D C     
4062 O O     . ALA D 12  ? 0.09077 0.15352 0.20848 -0.04045 -0.03168 0.02587  11  ALA D O     
4063 C CB    . ALA D 12  ? 0.12829 0.16056 0.23617 -0.05653 -0.03749 0.02725  11  ALA D CB    
4064 N N     . VAL D 13  ? 0.09142 0.16921 0.22404 -0.05092 -0.03178 0.03149  12  VAL D N     
4065 C CA    . VAL D 13  ? 0.08885 0.17986 0.22950 -0.04715 -0.03467 0.03055  12  VAL D CA    
4066 C C     . VAL D 13  ? 0.10081 0.18919 0.24170 -0.05435 -0.04323 0.02942  12  VAL D C     
4067 O O     . VAL D 13  ? 0.12587 0.21873 0.27310 -0.06150 -0.04314 0.03207  12  VAL D O     
4068 C CB    . VAL D 13  ? 0.08486 0.19629 0.23920 -0.04374 -0.02744 0.03345  12  VAL D CB    
4069 C CG1   . VAL D 13  ? 0.08531 0.20944 0.24942 -0.03967 -0.03186 0.03280  12  VAL D CG1   
4070 C CG2   . VAL D 13  ? 0.07575 0.18842 0.22774 -0.03630 -0.01894 0.03314  12  VAL D CG2   
4071 N N     . ASP D 14  ? 0.14297 0.22423 0.27612 -0.05300 -0.05057 0.02548  13  ASP D N     
4072 C CA    . ASP D 14  ? 0.15180 0.22746 0.28113 -0.06001 -0.05911 0.02285  13  ASP D CA    
4073 C C     . ASP D 14  ? 0.17218 0.23474 0.29776 -0.06801 -0.05933 0.02238  13  ASP D C     
4074 O O     . ASP D 14  ? 0.14038 0.20520 0.27105 -0.07552 -0.06285 0.02340  13  ASP D O     
4075 C CB    . ASP D 14  ? 0.19057 0.28439 0.33304 -0.06158 -0.06251 0.02558  13  ASP D CB    
4076 C CG    . ASP D 14  ? 0.16903 0.27151 0.31291 -0.05369 -0.06519 0.02579  13  ASP D CG    
4077 O OD1   . ASP D 14  ? 0.19943 0.29195 0.33112 -0.04916 -0.06666 0.02321  13  ASP D OD1   
4078 O OD2   . ASP D 14  ? 0.20111 0.32048 0.35864 -0.05205 -0.06616 0.02882  13  ASP D OD2   
4079 N N     . GLY D 15  ? 0.14809 0.19652 0.26533 -0.06620 -0.05567 0.02130  14  GLY D N     
4080 C CA    . GLY D 15  ? 0.15798 0.19057 0.27037 -0.07215 -0.05629 0.02111  14  GLY D CA    
4081 C C     . GLY D 15  ? 0.21355 0.25237 0.33409 -0.07616 -0.05041 0.02840  14  GLY D C     
4082 O O     . GLY D 15  ? 0.18519 0.20898 0.30043 -0.07980 -0.05039 0.02960  14  GLY D O     
4083 N N     . GLU D 16  ? 0.13129 0.19148 0.26401 -0.07534 -0.04533 0.03315  15  GLU D N     
4084 C CA    . GLU D 16  ? 0.14726 0.21563 0.28648 -0.07953 -0.03872 0.03974  15  GLU D CA    
4085 C C     . GLU D 16  ? 0.13059 0.19913 0.26546 -0.07383 -0.03058 0.04199  15  GLU D C     
4086 O O     . GLU D 16  ? 0.11050 0.18534 0.24554 -0.06581 -0.02768 0.03969  15  GLU D O     
4087 C CB    . GLU D 16  ? 0.13269 0.22523 0.28741 -0.08117 -0.03618 0.04261  15  GLU D CB    
4088 C CG    . GLU D 16  ? 0.14570 0.23989 0.30615 -0.08885 -0.04410 0.04189  15  GLU D CG    
4089 C CD    . GLU D 16  ? 0.16321 0.24534 0.32113 -0.09916 -0.04618 0.04496  15  GLU D CD    
4090 O OE1   . GLU D 16  ? 0.16822 0.24829 0.32433 -0.10115 -0.04006 0.04995  15  GLU D OE1   
4091 O OE2   . GLU D 16  ? 0.17673 0.25111 0.33392 -0.10548 -0.05423 0.04253  15  GLU D OE2   
4092 N N     . PRO D 17  ? 0.17977 0.24146 0.31038 -0.07812 -0.02717 0.04682  16  PRO D N     
4093 C CA    . PRO D 17  ? 0.14646 0.20755 0.27087 -0.07353 -0.02010 0.04921  16  PRO D CA    
4094 C C     . PRO D 17  ? 0.13580 0.21966 0.26810 -0.06902 -0.01135 0.05010  16  PRO D C     
4095 O O     . PRO D 17  ? 0.17058 0.27061 0.31251 -0.07269 -0.00767 0.05272  16  PRO D O     
4096 C CB    . PRO D 17  ? 0.14451 0.19594 0.26363 -0.08068 -0.01938 0.05552  16  PRO D CB    
4097 C CG    . PRO D 17  ? 0.20940 0.24978 0.33007 -0.08764 -0.02743 0.05475  16  PRO D CG    
4098 C CD    . PRO D 17  ? 0.19917 0.25367 0.33013 -0.08774 -0.02995 0.05094  16  PRO D CD    
4099 N N     . LEU D 18  ? 0.10214 0.18694 0.23058 -0.06078 -0.00771 0.04738  17  LEU D N     
4100 C CA    . LEU D 18  ? 0.11670 0.21979 0.25004 -0.05537 0.00159  0.04718  17  LEU D CA    
4101 C C     . LEU D 18  ? 0.14886 0.25039 0.27232 -0.05667 0.00889  0.05099  17  LEU D C     
4102 O O     . LEU D 18  ? 0.12971 0.24490 0.25575 -0.05902 0.01630  0.05345  17  LEU D O     
4103 C CB    . LEU D 18  ? 0.08240 0.18749 0.21723 -0.04535 0.00128  0.04176  17  LEU D CB    
4104 C CG    . LEU D 18  ? 0.15465 0.27545 0.29420 -0.03741 0.01032  0.03945  17  LEU D CG    
4105 C CD1   . LEU D 18  ? 0.11201 0.25204 0.26581 -0.03784 0.01318  0.03929  17  LEU D CD1   
4106 C CD2   . LEU D 18  ? 0.11404 0.23084 0.25299 -0.02782 0.00835  0.03472  17  LEU D CD2   
4107 N N     . GLY D 19  ? 0.10695 0.19218 0.21867 -0.05537 0.00664  0.05146  18  GLY D N     
4108 C CA    . GLY D 19  ? 0.10484 0.18662 0.20481 -0.05679 0.01169  0.05566  18  GLY D CA    
4109 C C     . GLY D 19  ? 0.10097 0.16574 0.18965 -0.05193 0.00811  0.05363  18  GLY D C     
4110 O O     . GLY D 19  ? 0.09490 0.14981 0.18315 -0.04669 0.00255  0.04763  18  GLY D O     
4111 N N     . ARG D 20  ? 0.10753 0.16806 0.18398 -0.05251 0.01116  0.05726  19  ARG D N     
4112 C CA    . ARG D 20  ? 0.10752 0.15107 0.17159 -0.04709 0.00705  0.05482  19  ARG D CA    
4113 C C     . ARG D 20  ? 0.13461 0.18376 0.19039 -0.03953 0.01265  0.04938  19  ARG D C     
4114 O O     . ARG D 20  ? 0.15992 0.22144 0.21220 -0.04080 0.02009  0.05078  19  ARG D O     
4115 C CB    . ARG D 20  ? 0.12161 0.15360 0.17781 -0.05325 0.00368  0.06356  19  ARG D CB    
4116 C CG    . ARG D 20  ? 0.14442 0.16171 0.19011 -0.04708 -0.00076 0.06171  19  ARG D CG    
4117 C CD    . ARG D 20  ? 0.14569 0.14977 0.18632 -0.05256 -0.00616 0.07126  19  ARG D CD    
4118 N NE    . ARG D 20  ? 0.19433 0.18360 0.24229 -0.05444 -0.01359 0.07116  19  ARG D NE    
4119 C CZ    . ARG D 20  ? 0.19982 0.17301 0.24441 -0.05454 -0.02012 0.07458  19  ARG D CZ    
4120 N NH1   . ARG D 20  ? 0.22960 0.20014 0.26501 -0.05451 -0.02099 0.08088  19  ARG D NH1   
4121 N NH2   . ARG D 20  ? 0.21486 0.17453 0.26520 -0.05435 -0.02615 0.07107  19  ARG D NH2   
4122 N N     . VAL D 21  ? 0.09422 0.13424 0.14638 -0.03226 0.00924  0.04293  20  VAL D N     
4123 C CA    . VAL D 21  ? 0.12924 0.17007 0.17226 -0.02616 0.01250  0.03804  20  VAL D CA    
4124 C C     . VAL D 21  ? 0.11635 0.14430 0.14979 -0.02524 0.00741  0.03968  20  VAL D C     
4125 O O     . VAL D 21  ? 0.12917 0.14661 0.16546 -0.02379 0.00137  0.03889  20  VAL D O     
4126 C CB    . VAL D 21  ? 0.09562 0.13789 0.14345 -0.01925 0.01262  0.03022  20  VAL D CB    
4127 C CG1   . VAL D 21  ? 0.09554 0.13657 0.13384 -0.01414 0.01542  0.02527  20  VAL D CG1   
4128 C CG2   . VAL D 21  ? 0.11701 0.17305 0.17747 -0.01942 0.01632  0.02946  20  VAL D CG2   
4129 N N     . SER D 22  ? 0.10172 0.13130 0.12407 -0.02608 0.00967  0.04183  21  SER D N     
4130 C CA    . SER D 22  ? 0.14366 0.16369 0.15804 -0.02455 0.00431  0.04351  21  SER D CA    
4131 C C     . SER D 22  ? 0.14788 0.16969 0.15543 -0.01969 0.00588  0.03672  21  SER D C     
4132 O O     . SER D 22  ? 0.12071 0.15009 0.12527 -0.01872 0.01186  0.03224  21  SER D O     
4133 C CB    . SER D 22  ? 0.14214 0.16102 0.14800 -0.03058 0.00300  0.05302  21  SER D CB    
4134 O OG    . SER D 22  ? 0.18664 0.21578 0.18178 -0.03303 0.00933  0.05313  21  SER D OG    
4135 N N     . PHE D 23  ? 0.09905 0.11378 0.10521 -0.01661 0.00037  0.03568  22  PHE D N     
4136 C CA    . PHE D 23  ? 0.09543 0.11084 0.09677 -0.01319 0.00043  0.02973  22  PHE D CA    
4137 C C     . PHE D 23  ? 0.11319 0.12631 0.10733 -0.01402 -0.00474 0.03341  22  PHE D C     
4138 O O     . PHE D 23  ? 0.14758 0.15560 0.14613 -0.01334 -0.01026 0.03812  22  PHE D O     
4139 C CB    . PHE D 23  ? 0.09392 0.10598 0.10324 -0.00873 -0.00146 0.02440  22  PHE D CB    
4140 C CG    . PHE D 23  ? 0.10086 0.11439 0.11806 -0.00774 0.00115  0.02173  22  PHE D CG    
4141 C CD1   . PHE D 23  ? 0.12141 0.13174 0.14595 -0.00865 -0.00128 0.02392  22  PHE D CD1   
4142 C CD2   . PHE D 23  ? 0.11400 0.13121 0.13157 -0.00574 0.00508  0.01684  22  PHE D CD2   
4143 C CE1   . PHE D 23  ? 0.10627 0.11896 0.13790 -0.00841 -0.00015 0.02165  22  PHE D CE1   
4144 C CE2   . PHE D 23  ? 0.15322 0.17281 0.17911 -0.00452 0.00622  0.01533  22  PHE D CE2   
4145 C CZ    . PHE D 23  ? 0.11956 0.13776 0.15228 -0.00625 0.00338  0.01791  22  PHE D CZ    
4146 N N     . GLU D 24  ? 0.11206 0.12847 0.09582 -0.01508 -0.00367 0.03080  23  GLU D N     
4147 C CA    . GLU D 24  ? 0.11348 0.12905 0.09256 -0.01530 -0.00997 0.03271  23  GLU D CA    
4148 C C     . GLU D 24  ? 0.12956 0.14436 0.11573 -0.01158 -0.01172 0.02674  23  GLU D C     
4149 O O     . GLU D 24  ? 0.10747 0.12243 0.09311 -0.01074 -0.00782 0.02017  23  GLU D O     
4150 C CB    . GLU D 24  ? 0.17089 0.19018 0.13414 -0.01938 -0.00928 0.03236  23  GLU D CB    
4151 C CG    . GLU D 24  ? 0.14177 0.16164 0.10097 -0.02030 -0.01732 0.03474  23  GLU D CG    
4152 C CD    . GLU D 24  ? 0.23223 0.25539 0.17320 -0.02559 -0.01802 0.03530  23  GLU D CD    
4153 O OE1   . GLU D 24  ? 0.30153 0.32678 0.23258 -0.02885 -0.01276 0.03706  23  GLU D OE1   
4154 O OE2   . GLU D 24  ? 0.25918 0.28388 0.19552 -0.02703 -0.02379 0.03387  23  GLU D OE2   
4155 N N     . LEU D 25  ? 0.10712 0.12135 0.10054 -0.00928 -0.01751 0.02939  24  LEU D N     
4156 C CA    . LEU D 25  ? 0.10196 0.11823 0.10262 -0.00661 -0.01885 0.02478  24  LEU D CA    
4157 C C     . LEU D 25  ? 0.09744 0.11856 0.09394 -0.00875 -0.02394 0.02568  24  LEU D C     
4158 O O     . LEU D 25  ? 0.10458 0.12741 0.10066 -0.00898 -0.02962 0.03175  24  LEU D O     
4159 C CB    . LEU D 25  ? 0.09571 0.11057 0.10897 -0.00196 -0.02073 0.02558  24  LEU D CB    
4160 C CG    . LEU D 25  ? 0.08335 0.09253 0.10046 -0.00077 -0.01775 0.02536  24  LEU D CG    
4161 C CD1   . LEU D 25  ? 0.08075 0.08742 0.10853 0.00403  -0.01973 0.02401  24  LEU D CD1   
4162 C CD2   . LEU D 25  ? 0.09820 0.10764 0.11310 -0.00189 -0.01219 0.02045  24  LEU D CD2   
4163 N N     . PHE D 26  ? 0.09598 0.11873 0.08961 -0.01075 -0.02276 0.02015  25  PHE D N     
4164 C CA    . PHE D 26  ? 0.13947 0.16630 0.12672 -0.01483 -0.02761 0.01986  25  PHE D CA    
4165 C C     . PHE D 26  ? 0.13514 0.16980 0.13505 -0.01323 -0.03295 0.02186  25  PHE D C     
4166 O O     . PHE D 26  ? 0.13912 0.17770 0.14292 -0.01529 -0.03340 0.01839  25  PHE D O     
4167 C CB    . PHE D 26  ? 0.15510 0.17815 0.13415 -0.01821 -0.02442 0.01265  25  PHE D CB    
4168 C CG    . PHE D 26  ? 0.14415 0.16166 0.11197 -0.01868 -0.01864 0.00957  25  PHE D CG    
4169 C CD1   . PHE D 26  ? 0.19750 0.21642 0.15503 -0.02055 -0.01872 0.01316  25  PHE D CD1   
4170 C CD2   . PHE D 26  ? 0.14107 0.15297 0.10920 -0.01715 -0.01308 0.00349  25  PHE D CD2   
4171 C CE1   . PHE D 26  ? 0.24791 0.26475 0.19605 -0.02095 -0.01203 0.00994  25  PHE D CE1   
4172 C CE2   . PHE D 26  ? 0.17924 0.18833 0.13984 -0.01633 -0.00719 0.00010  25  PHE D CE2   
4173 C CZ    . PHE D 26  ? 0.20307 0.21565 0.15378 -0.01829 -0.00600 0.00288  25  PHE D CZ    
4174 N N     . ALA D 27  ? 0.11833 0.15552 0.12567 -0.00948 -0.03703 0.02787  26  ALA D N     
4175 C CA    . ALA D 27  ? 0.12939 0.17603 0.15130 -0.00627 -0.04184 0.02973  26  ALA D CA    
4176 C C     . ALA D 27  ? 0.13729 0.19277 0.15694 -0.01104 -0.04885 0.03140  26  ALA D C     
4177 O O     . ALA D 27  ? 0.13419 0.20062 0.16642 -0.01039 -0.05152 0.03094  26  ALA D O     
4178 C CB    . ALA D 27  ? 0.10680 0.15179 0.13771 -0.00001 -0.04517 0.03542  26  ALA D CB    
4179 N N     . ASP D 28  ? 0.11885 0.17102 0.12250 -0.01634 -0.05183 0.03316  27  ASP D N     
4180 C CA    . ASP D 28  ? 0.16001 0.21979 0.15884 -0.02219 -0.05944 0.03408  27  ASP D CA    
4181 C C     . ASP D 28  ? 0.16980 0.23243 0.17044 -0.02694 -0.05770 0.02709  27  ASP D C     
4182 O O     . ASP D 28  ? 0.14474 0.21791 0.15150 -0.03065 -0.06430 0.02808  27  ASP D O     
4183 C CB    . ASP D 28  ? 0.15203 0.20646 0.12935 -0.02768 -0.06168 0.03570  27  ASP D CB    
4184 C CG    . ASP D 28  ? 0.19913 0.24271 0.16244 -0.02928 -0.05223 0.02917  27  ASP D CG    
4185 O OD1   . ASP D 28  ? 0.15832 0.19759 0.12871 -0.02612 -0.04507 0.02438  27  ASP D OD1   
4186 O OD2   . ASP D 28  ? 0.24184 0.28223 0.18705 -0.03356 -0.05206 0.02897  27  ASP D OD2   
4187 N N     . LYS D 29  ? 0.12345 0.17715 0.12018 -0.02714 -0.04959 0.02084  28  LYS D N     
4188 C CA    . LYS D 29  ? 0.15709 0.21003 0.15423 -0.03221 -0.04815 0.01511  28  LYS D CA    
4189 C C     . LYS D 29  ? 0.14341 0.19850 0.15427 -0.02895 -0.04262 0.01381  28  LYS D C     
4190 O O     . LYS D 29  ? 0.16199 0.22077 0.17759 -0.03374 -0.04305 0.01182  28  LYS D O     
4191 C CB    . LYS D 29  ? 0.15341 0.19265 0.13299 -0.03583 -0.04428 0.00862  28  LYS D CB    
4192 C CG    . LYS D 29  ? 0.21338 0.25084 0.17588 -0.04060 -0.04903 0.00800  28  LYS D CG    
4193 C CD    . LYS D 29  ? 0.30372 0.32793 0.24960 -0.04238 -0.04348 -0.00008 28  LYS D CD    
4194 C CE    . LYS D 29  ? 0.36639 0.38973 0.29263 -0.04722 -0.04722 -0.00157 28  LYS D CE    
4195 N NZ    . LYS D 29  ? 0.45461 0.48610 0.38071 -0.05404 -0.05793 0.00064  28  LYS D NZ    
4196 N N     . VAL D 30  ? 0.12260 0.17526 0.13877 -0.02197 -0.03768 0.01496  29  VAL D N     
4197 C CA    . VAL D 30  ? 0.09517 0.14969 0.12135 -0.01922 -0.03232 0.01326  29  VAL D CA    
4198 C C     . VAL D 30  ? 0.08050 0.14112 0.11876 -0.01158 -0.03181 0.01603  29  VAL D C     
4199 O O     . VAL D 30  ? 0.07248 0.12647 0.11070 -0.00713 -0.02722 0.01490  29  VAL D O     
4200 C CB    . VAL D 30  ? 0.12646 0.16811 0.14430 -0.01908 -0.02620 0.00948  29  VAL D CB    
4201 C CG1   . VAL D 30  ? 0.09423 0.13698 0.11682 -0.02150 -0.02315 0.00772  29  VAL D CG1   
4202 C CG2   . VAL D 30  ? 0.12764 0.15931 0.13077 -0.02311 -0.02682 0.00650  29  VAL D CG2   
4203 N N     . PRO D 31  ? 0.07768 0.15085 0.12743 -0.00969 -0.03680 0.01925  30  PRO D N     
4204 C CA    . PRO D 31  ? 0.10179 0.17774 0.16253 -0.00116 -0.03748 0.02164  30  PRO D CA    
4205 C C     . PRO D 31  ? 0.07556 0.15247 0.14449 0.00406  -0.03069 0.01767  30  PRO D C     
4206 O O     . PRO D 31  ? 0.13245 0.20158 0.20236 0.00993  -0.02934 0.01748  30  PRO D O     
4207 C CB    . PRO D 31  ? 0.10015 0.19157 0.17347 -0.00033 -0.04470 0.02552  30  PRO D CB    
4208 C CG    . PRO D 31  ? 0.11581 0.21614 0.18871 -0.00890 -0.04545 0.02377  30  PRO D CG    
4209 C CD    . PRO D 31  ? 0.08222 0.16731 0.13618 -0.01521 -0.04293 0.02087  30  PRO D CD    
4210 N N     . LYS D 32  ? 0.06419 0.15016 0.13821 0.00146  -0.02659 0.01464  31  LYS D N     
4211 C CA    . LYS D 32  ? 0.08349 0.17183 0.16347 0.00627  -0.02007 0.01068  31  LYS D CA    
4212 C C     . LYS D 32  ? 0.09474 0.16749 0.16263 0.00607  -0.01604 0.00835  31  LYS D C     
4213 O O     . LYS D 32  ? 0.09972 0.16809 0.16943 0.01163  -0.01334 0.00575  31  LYS D O     
4214 C CB    . LYS D 32  ? 0.11549 0.21839 0.20193 0.00206  -0.01609 0.00905  31  LYS D CB    
4215 C CG    . LYS D 32  ? 0.19888 0.32272 0.30297 0.00401  -0.01818 0.01037  31  LYS D CG    
4216 C CD    . LYS D 32  ? 0.31488 0.45443 0.42597 0.00073  -0.01137 0.00814  31  LYS D CD    
4217 C CE    . LYS D 32  ? 0.38026 0.51656 0.48911 0.00666  -0.00346 0.00290  31  LYS D CE    
4218 N NZ    . LYS D 32  ? 0.31127 0.45592 0.41708 0.00060  0.00382  0.00151  31  LYS D NZ    
4219 N N     . THR D 33  ? 0.06906 0.13338 0.12527 -0.00013 -0.01605 0.00885  32  THR D N     
4220 C CA    . THR D 33  ? 0.07139 0.12325 0.11823 -0.00033 -0.01272 0.00710  32  THR D CA    
4221 C C     . THR D 33  ? 0.11089 0.15318 0.15430 0.00312  -0.01433 0.00845  32  THR D C     
4222 O O     . THR D 33  ? 0.09850 0.13443 0.14079 0.00573  -0.01200 0.00688  32  THR D O     
4223 C CB    . THR D 33  ? 0.06049 0.10655 0.09815 -0.00683 -0.01250 0.00700  32  THR D CB    
4224 O OG1   . THR D 33  ? 0.06715 0.12147 0.10825 -0.01168 -0.01187 0.00707  32  THR D OG1   
4225 C CG2   . THR D 33  ? 0.07510 0.11077 0.10609 -0.00621 -0.00933 0.00553  32  THR D CG2   
4226 N N     . ALA D 34  ? 0.08913 0.13063 0.13013 0.00216  -0.01865 0.01182  33  ALA D N     
4227 C CA    . ALA D 34  ? 0.06788 0.10162 0.10602 0.00445  -0.02031 0.01470  33  ALA D CA    
4228 C C     . ALA D 34  ? 0.09447 0.12737 0.14223 0.01080  -0.02112 0.01482  33  ALA D C     
4229 O O     . ALA D 34  ? 0.08729 0.11130 0.13347 0.01229  -0.02008 0.01475  33  ALA D O     
4230 C CB    . ALA D 34  ? 0.07498 0.10969 0.10779 0.00175  -0.02533 0.01919  33  ALA D CB    
4231 N N     . GLU D 35  ? 0.08823 0.13038 0.14692 0.01468  -0.02308 0.01456  34  GLU D N     
4232 C CA    . GLU D 35  ? 0.07252 0.11281 0.14128 0.02219  -0.02378 0.01329  34  GLU D CA    
4233 C C     . GLU D 35  ? 0.13969 0.17536 0.20748 0.02398  -0.01822 0.00699  34  GLU D C     
4234 O O     . GLU D 35  ? 0.10203 0.12777 0.17121 0.02770  -0.01885 0.00565  34  GLU D O     
4235 C CB    . GLU D 35  ? 0.10833 0.16254 0.19113 0.02690  -0.02599 0.01322  34  GLU D CB    
4236 C CG    . GLU D 35  ? 0.09785 0.15152 0.19288 0.03635  -0.02516 0.00930  34  GLU D CG    
4237 C CD    . GLU D 35  ? 0.13730 0.17627 0.23338 0.04063  -0.03071 0.01331  34  GLU D CD    
4238 O OE1   . GLU D 35  ? 0.12413 0.15752 0.21307 0.03632  -0.03580 0.02074  34  GLU D OE1   
4239 O OE2   . GLU D 35  ? 0.12603 0.15838 0.22936 0.04797  -0.03003 0.00897  34  GLU D OE2   
4240 N N     . ASN D 36  ? 0.11553 0.15741 0.18008 0.02065  -0.01346 0.00341  35  ASN D N     
4241 C CA    . ASN D 36  ? 0.10390 0.14151 0.16440 0.02095  -0.00901 -0.00172 35  ASN D CA    
4242 C C     . ASN D 36  ? 0.13745 0.16141 0.19068 0.01917  -0.01021 -0.00055 35  ASN D C     
4243 O O     . ASN D 36  ? 0.10932 0.12557 0.16366 0.02214  -0.01052 -0.00339 35  ASN D O     
4244 C CB    . ASN D 36  ? 0.10705 0.15179 0.16261 0.01576  -0.00507 -0.00294 35  ASN D CB    
4245 C CG    . ASN D 36  ? 0.11088 0.15248 0.16067 0.01539  -0.00132 -0.00725 35  ASN D CG    
4246 O OD1   . ASN D 36  ? 0.09304 0.13700 0.14597 0.01973  0.00103  -0.01231 35  ASN D OD1   
4247 N ND2   . ASN D 36  ? 0.10874 0.14505 0.14986 0.01048  -0.00105 -0.00558 35  ASN D ND2   
4248 N N     . PHE D 37  ? 0.06341 0.08465 0.10984 0.01422  -0.01095 0.00327  36  PHE D N     
4249 C CA    . PHE D 37  ? 0.08682 0.09884 0.12819 0.01205  -0.01128 0.00478  36  PHE D CA    
4250 C C     . PHE D 37  ? 0.10906 0.11348 0.15377 0.01417  -0.01481 0.00764  36  PHE D C     
4251 O O     . PHE D 37  ? 0.10959 0.10620 0.15411 0.01379  -0.01521 0.00675  36  PHE D O     
4252 C CB    . PHE D 37  ? 0.11340 0.12594 0.14824 0.00760  -0.01066 0.00767  36  PHE D CB    
4253 C CG    . PHE D 37  ? 0.08672 0.09416 0.11813 0.00540  -0.00938 0.00842  36  PHE D CG    
4254 C CD1   . PHE D 37  ? 0.07521 0.07885 0.10600 0.00410  -0.01061 0.01237  36  PHE D CD1   
4255 C CD2   . PHE D 37  ? 0.10059 0.10824 0.13022 0.00436  -0.00724 0.00598  36  PHE D CD2   
4256 C CE1   . PHE D 37  ? 0.12081 0.12295 0.15061 0.00164  -0.00890 0.01332  36  PHE D CE1   
4257 C CE2   . PHE D 37  ? 0.09252 0.09806 0.12173 0.00286  -0.00645 0.00689  36  PHE D CE2   
4258 C CZ    . PHE D 37  ? 0.08592 0.08970 0.11595 0.00147  -0.00688 0.01025  36  PHE D CZ    
4259 N N     . ARG D 38  ? 0.07512 0.08135 0.12321 0.01597  -0.01828 0.01160  37  ARG D N     
4260 C CA    . ARG D 38  ? 0.11470 0.11216 0.16614 0.01802  -0.02278 0.01588  37  ARG D CA    
4261 C C     . ARG D 38  ? 0.14645 0.13693 0.20466 0.02332  -0.02320 0.01078  37  ARG D C     
4262 O O     . ARG D 38  ? 0.13945 0.11814 0.19739 0.02244  -0.02523 0.01178  37  ARG D O     
4263 C CB    . ARG D 38  ? 0.08893 0.09070 0.14390 0.02002  -0.02760 0.02125  37  ARG D CB    
4264 C CG    . ARG D 38  ? 0.10144 0.09258 0.15804 0.02099  -0.03348 0.02837  37  ARG D CG    
4265 C CD    . ARG D 38  ? 0.13508 0.13042 0.19872 0.02543  -0.03980 0.03328  37  ARG D CD    
4266 N NE    . ARG D 38  ? 0.10886 0.10955 0.18560 0.03365  -0.03937 0.02714  37  ARG D NE    
4267 C CZ    . ARG D 38  ? 0.13497 0.12653 0.21990 0.04024  -0.03990 0.02315  37  ARG D CZ    
4268 N NH1   . ARG D 38  ? 0.12425 0.09939 0.20555 0.03864  -0.04192 0.02544  37  ARG D NH1   
4269 N NH2   . ARG D 38  ? 0.15579 0.15538 0.25072 0.04743  -0.03716 0.01587  37  ARG D NH2   
4270 N N     . ALA D 39  ? 0.11219 0.10998 0.17667 0.02861  -0.02124 0.00499  38  ALA D N     
4271 C CA    . ALA D 39  ? 0.09934 0.09063 0.16989 0.03488  -0.02112 -0.00152 38  ALA D CA    
4272 C C     . ALA D 39  ? 0.14393 0.12834 0.20749 0.03171  -0.01842 -0.00712 38  ALA D C     
4273 O O     . ALA D 39  ? 0.12436 0.09639 0.18922 0.03383  -0.02039 -0.01079 38  ALA D O     
4274 C CB    . ALA D 39  ? 0.14652 0.15094 0.22565 0.04123  -0.01821 -0.00683 38  ALA D CB    
4275 N N     . LEU D 40  ? 0.10037 0.09173 0.15655 0.02641  -0.01482 -0.00765 39  LEU D N     
4276 C CA    . LEU D 40  ? 0.10203 0.08822 0.15173 0.02278  -0.01369 -0.01141 39  LEU D CA    
4277 C C     . LEU D 40  ? 0.09414 0.06991 0.14240 0.01815  -0.01729 -0.00659 39  LEU D C     
4278 O O     . LEU D 40  ? 0.12848 0.09699 0.17457 0.01588  -0.01853 -0.00987 39  LEU D O     
4279 C CB    . LEU D 40  ? 0.09726 0.09324 0.14065 0.01877  -0.01004 -0.01159 39  LEU D CB    
4280 C CG    . LEU D 40  ? 0.08792 0.09517 0.13132 0.02096  -0.00585 -0.01580 39  LEU D CG    
4281 C CD1   . LEU D 40  ? 0.07216 0.08607 0.10912 0.01574  -0.00369 -0.01332 39  LEU D CD1   
4282 C CD2   . LEU D 40  ? 0.13747 0.14300 0.17951 0.02446  -0.00385 -0.02445 39  LEU D CD2   
4283 N N     . SER D 41  ? 0.11721 0.09317 0.16619 0.01587  -0.01901 0.00125  40  SER D N     
4284 C CA    . SER D 41  ? 0.10792 0.07639 0.15593 0.01061  -0.02147 0.00671  40  SER D CA    
4285 C C     . SER D 41  ? 0.12539 0.07961 0.17794 0.01218  -0.02637 0.00780  40  SER D C     
4286 O O     . SER D 41  ? 0.14236 0.08796 0.19479 0.00735  -0.02862 0.00920  40  SER D O     
4287 C CB    . SER D 41  ? 0.11439 0.08873 0.15948 0.00714  -0.02077 0.01441  40  SER D CB    
4288 O OG    . SER D 41  ? 0.10281 0.08716 0.14385 0.00564  -0.01668 0.01280  40  SER D OG    
4289 N N     . THR D 42  ? 0.15197 0.10329 0.20967 0.01872  -0.02862 0.00755  41  THR D N     
4290 C CA    . THR D 42  ? 0.16202 0.09704 0.22501 0.02159  -0.03393 0.00790  41  THR D CA    
4291 C C     . THR D 42  ? 0.16362 0.09089 0.22819 0.02585  -0.03339 -0.00343 41  THR D C     
4292 O O     . THR D 42  ? 0.20986 0.12101 0.27659 0.02626  -0.03758 -0.00477 41  THR D O     
4293 C CB    . THR D 42  ? 0.16105 0.09520 0.23093 0.02839  -0.03761 0.01211  41  THR D CB    
4294 O OG1   . THR D 42  ? 0.16860 0.11156 0.24388 0.03662  -0.03454 0.00370  41  THR D OG1   
4295 C CG2   . THR D 42  ? 0.21631 0.16009 0.28247 0.02445  -0.03827 0.02209  41  THR D CG2   
4296 N N     . GLY D 43  ? 0.15287 0.09131 0.21481 0.02833  -0.02816 -0.01153 42  GLY D N     
4297 C CA    . GLY D 43  ? 0.17245 0.10537 0.23366 0.03260  -0.02682 -0.02320 42  GLY D CA    
4298 C C     . GLY D 43  ? 0.20047 0.12888 0.27006 0.04300  -0.02728 -0.02872 42  GLY D C     
4299 O O     . GLY D 43  ? 0.19570 0.11813 0.26274 0.04605  -0.02569 -0.03837 42  GLY D O     
4300 N N     . GLU D 44  ? 0.19895 0.13412 0.27544 0.04695  -0.02818 -0.02195 43  GLU D N     
4301 C CA    . GLU D 44  ? 0.16608 0.09973 0.24931 0.05518  -0.02830 -0.02440 43  GLU D CA    
4302 C C     . GLU D 44  ? 0.24611 0.19166 0.33165 0.06218  -0.02148 -0.03545 43  GLU D C     
4303 O O     . GLU D 44  ? 0.21735 0.16048 0.30831 0.06956  -0.02055 -0.03968 43  GLU D O     
4304 C CB    . GLU D 44  ? 0.22345 0.16353 0.31310 0.05690  -0.03165 -0.01396 43  GLU D CB    
4305 C CG    . GLU D 44  ? 0.19544 0.15506 0.28689 0.05593  -0.02901 -0.01103 43  GLU D CG    
4306 C CD    . GLU D 44  ? 0.24307 0.20696 0.33755 0.05509  -0.03393 0.00016  43  GLU D CD    
4307 O OE1   . GLU D 44  ? 0.17029 0.12706 0.25881 0.04835  -0.03787 0.00870  43  GLU D OE1   
4308 O OE2   . GLU D 44  ? 0.19956 0.17472 0.30197 0.06081  -0.03382 0.00049  43  GLU D OE2   
4309 N N     . LYS D 45  ? 0.19825 0.15715 0.27981 0.05998  -0.01634 -0.03990 44  LYS D N     
4310 C CA    . LYS D 45  ? 0.16176 0.13343 0.24315 0.06478  -0.00886 -0.05001 44  LYS D CA    
4311 C C     . LYS D 45  ? 0.18686 0.14872 0.25787 0.06376  -0.00663 -0.06088 44  LYS D C     
4312 O O     . LYS D 45  ? 0.23169 0.20313 0.29994 0.06718  0.00006  -0.06969 44  LYS D O     
4313 C CB    . LYS D 45  ? 0.14673 0.13907 0.22756 0.06190  -0.00402 -0.04916 44  LYS D CB    
4314 C CG    . LYS D 45  ? 0.19196 0.19555 0.28110 0.06116  -0.00631 -0.03890 44  LYS D CG    
4315 C CD    . LYS D 45  ? 0.18826 0.19715 0.28898 0.06857  -0.00686 -0.03722 44  LYS D CD    
4316 C CE    . LYS D 45  ? 0.28109 0.30537 0.38914 0.06684  -0.00887 -0.02834 44  LYS D CE    
4317 N NZ    . LYS D 45  ? 0.24323 0.27227 0.36272 0.07354  -0.01125 -0.02480 44  LYS D NZ    
4318 N N     . GLY D 46  ? 0.22581 0.16984 0.29041 0.05824  -0.01205 -0.06006 45  GLY D N     
4319 C CA    . GLY D 46  ? 0.19004 0.12429 0.24358 0.05561  -0.01140 -0.06988 45  GLY D CA    
4320 C C     . GLY D 46  ? 0.22388 0.16245 0.26685 0.04776  -0.01114 -0.07155 45  GLY D C     
4321 O O     . GLY D 46  ? 0.22559 0.15861 0.25737 0.04448  -0.01095 -0.07964 45  GLY D O     
4322 N N     . PHE D 47  ? 0.18451 0.13489 0.22793 0.04251  -0.01084 -0.06101 46  PHE D N     
4323 C CA    . PHE D 47  ? 0.18676 0.14421 0.21950 0.03341  -0.01038 -0.05744 46  PHE D CA    
4324 C C     . PHE D 47  ? 0.15119 0.11385 0.18827 0.02897  -0.01228 -0.04462 46  PHE D C     
4325 O O     . PHE D 47  ? 0.16697 0.13172 0.21288 0.03262  -0.01270 -0.03929 46  PHE D O     
4326 C CB    . PHE D 47  ? 0.14867 0.12204 0.17327 0.03353  -0.00355 -0.06264 46  PHE D CB    
4327 C CG    . PHE D 47  ? 0.14914 0.13844 0.18162 0.03842  0.00194  -0.06044 46  PHE D CG    
4328 C CD1   . PHE D 47  ? 0.15635 0.15638 0.19068 0.03416  0.00241  -0.05040 46  PHE D CD1   
4329 C CD2   . PHE D 47  ? 0.15862 0.15283 0.19740 0.04723  0.00661  -0.06896 46  PHE D CD2   
4330 C CE1   . PHE D 47  ? 0.15163 0.16644 0.19366 0.03732  0.00651  -0.04833 46  PHE D CE1   
4331 C CE2   . PHE D 47  ? 0.18513 0.19685 0.23327 0.05100  0.01136  -0.06645 46  PHE D CE2   
4332 C CZ    . PHE D 47  ? 0.13535 0.15715 0.18488 0.04534  0.01086  -0.05582 46  PHE D CZ    
4333 N N     . GLY D 48  ? 0.13157 0.09637 0.16245 0.02133  -0.01377 -0.03999 47  GLY D N     
4334 C CA    . GLY D 48  ? 0.12266 0.09199 0.15706 0.01771  -0.01478 -0.02949 47  GLY D CA    
4335 C C     . GLY D 48  ? 0.14160 0.11006 0.17212 0.01039  -0.01748 -0.02574 47  GLY D C     
4336 O O     . GLY D 48  ? 0.15088 0.11793 0.17512 0.00754  -0.01882 -0.03043 47  GLY D O     
4337 N N     . TYR D 49  ? 0.12796 0.09839 0.16256 0.00755  -0.01832 -0.01734 48  TYR D N     
4338 C CA    . TYR D 49  ? 0.13226 0.10687 0.16620 0.00186  -0.01941 -0.01271 48  TYR D CA    
4339 C C     . TYR D 49  ? 0.14026 0.10724 0.17647 -0.00321 -0.02404 -0.01241 48  TYR D C     
4340 O O     . TYR D 49  ? 0.12501 0.09737 0.16158 -0.00762 -0.02545 -0.01032 48  TYR D O     
4341 C CB    . TYR D 49  ? 0.08518 0.06547 0.12248 0.00115  -0.01751 -0.00518 48  TYR D CB    
4342 C CG    . TYR D 49  ? 0.10453 0.09293 0.13947 0.00402  -0.01382 -0.00472 48  TYR D CG    
4343 C CD1   . TYR D 49  ? 0.11222 0.10613 0.14246 0.00405  -0.01221 -0.00732 48  TYR D CD1   
4344 C CD2   . TYR D 49  ? 0.10599 0.09620 0.14283 0.00557  -0.01272 -0.00097 48  TYR D CD2   
4345 C CE1   . TYR D 49  ? 0.09792 0.09815 0.12639 0.00522  -0.00935 -0.00623 48  TYR D CE1   
4346 C CE2   . TYR D 49  ? 0.07991 0.07705 0.11491 0.00693  -0.01024 -0.00072 48  TYR D CE2   
4347 C CZ    . TYR D 49  ? 0.11121 0.11298 0.14254 0.00652  -0.00844 -0.00332 48  TYR D CZ    
4348 O OH    . TYR D 49  ? 0.09056 0.09818 0.12042 0.00648  -0.00644 -0.00241 48  TYR D OH    
4349 N N     . LYS D 50  ? 0.15354 0.10822 0.19255 -0.00294 -0.02697 -0.01375 49  LYS D N     
4350 C CA    . LYS D 50  ? 0.15155 0.09824 0.19364 -0.00956 -0.03192 -0.01213 49  LYS D CA    
4351 C C     . LYS D 50  ? 0.13715 0.08465 0.17455 -0.01322 -0.03484 -0.01813 49  LYS D C     
4352 O O     . LYS D 50  ? 0.15423 0.09725 0.18468 -0.01019 -0.03500 -0.02693 49  LYS D O     
4353 C CB    . LYS D 50  ? 0.14658 0.07630 0.19147 -0.00834 -0.03545 -0.01338 49  LYS D CB    
4354 C CG    . LYS D 50  ? 0.19336 0.11300 0.24214 -0.01694 -0.04118 -0.01021 49  LYS D CG    
4355 C CD    . LYS D 50  ? 0.22224 0.12324 0.27428 -0.01551 -0.04499 -0.00909 49  LYS D CD    
4356 C CE    . LYS D 50  ? 0.25878 0.15363 0.31403 -0.02494 -0.04908 -0.00246 49  LYS D CE    
4357 N NZ    . LYS D 50  ? 0.27303 0.15363 0.32879 -0.02212 -0.05118 0.00008  49  LYS D NZ    
4358 N N     . GLY D 51  ? 0.17427 0.12930 0.21541 -0.01964 -0.03702 -0.01340 50  GLY D N     
4359 C CA    . GLY D 51  ? 0.15538 0.11323 0.19305 -0.02403 -0.04133 -0.01733 50  GLY D CA    
4360 C C     . GLY D 51  ? 0.12037 0.09223 0.15472 -0.02230 -0.03940 -0.01602 50  GLY D C     
4361 O O     . GLY D 51  ? 0.14835 0.12584 0.18242 -0.02667 -0.04393 -0.01592 50  GLY D O     
4362 N N     . SER D 52  ? 0.11050 0.08741 0.14251 -0.01646 -0.03375 -0.01467 51  SER D N     
4363 C CA    . SER D 52  ? 0.12778 0.11509 0.15625 -0.01490 -0.03226 -0.01280 51  SER D CA    
4364 C C     . SER D 52  ? 0.11512 0.11223 0.15328 -0.01658 -0.03250 -0.00535 51  SER D C     
4365 O O     . SER D 52  ? 0.13503 0.13305 0.18206 -0.01906 -0.03235 -0.00155 51  SER D O     
4366 C CB    . SER D 52  ? 0.09634 0.08513 0.12021 -0.00931 -0.02650 -0.01357 51  SER D CB    
4367 O OG    . SER D 52  ? 0.09109 0.08119 0.12156 -0.00724 -0.02304 -0.00875 51  SER D OG    
4368 N N     . SER D 53  ? 0.12163 0.12634 0.15830 -0.01520 -0.03282 -0.00310 52  SER D N     
4369 C CA    . SER D 53  ? 0.13855 0.15314 0.18562 -0.01568 -0.03389 0.00264  52  SER D CA    
4370 C C     . SER D 53  ? 0.08849 0.10675 0.13636 -0.01053 -0.02918 0.00567  52  SER D C     
4371 O O     . SER D 53  ? 0.09041 0.10458 0.12984 -0.00793 -0.02646 0.00407  52  SER D O     
4372 C CB    . SER D 53  ? 0.13645 0.15632 0.18376 -0.01875 -0.04106 0.00332  52  SER D CB    
4373 O OG    . SER D 53  ? 0.20105 0.22016 0.23769 -0.01666 -0.04201 0.00287  52  SER D OG    
4374 N N     . PHE D 54  ? 0.12885 0.15522 0.18774 -0.00932 -0.02801 0.00966  53  PHE D N     
4375 C CA    . PHE D 54  ? 0.09997 0.12921 0.16083 -0.00422 -0.02508 0.01182  53  PHE D CA    
4376 C C     . PHE D 54  ? 0.10295 0.13628 0.16596 -0.00346 -0.03107 0.01433  53  PHE D C     
4377 O O     . PHE D 54  ? 0.11747 0.16004 0.19230 -0.00377 -0.03430 0.01694  53  PHE D O     
4378 C CB    . PHE D 54  ? 0.09889 0.13488 0.17003 -0.00231 -0.01998 0.01355  53  PHE D CB    
4379 C CG    . PHE D 54  ? 0.09217 0.12337 0.15814 -0.00244 -0.01441 0.01228  53  PHE D CG    
4380 C CD1   . PHE D 54  ? 0.05992 0.08887 0.12569 -0.00677 -0.01438 0.01251  53  PHE D CD1   
4381 C CD2   . PHE D 54  ? 0.09975 0.12778 0.16084 0.00136  -0.01018 0.01125  53  PHE D CD2   
4382 C CE1   . PHE D 54  ? 0.08777 0.11228 0.14869 -0.00679 -0.01051 0.01265  53  PHE D CE1   
4383 C CE2   . PHE D 54  ? 0.08974 0.11440 0.14559 0.00078  -0.00628 0.01058  53  PHE D CE2   
4384 C CZ    . PHE D 54  ? 0.09766 0.12095 0.15343 -0.00306 -0.00662 0.01173  53  PHE D CZ    
4385 N N     . HIS D 55  ? 0.11422 0.14176 0.16611 -0.00300 -0.03299 0.01421  54  HIS D N     
4386 C CA    . HIS D 55  ? 0.10765 0.13732 0.15768 -0.00353 -0.04000 0.01753  54  HIS D CA    
4387 C C     . HIS D 55  ? 0.11688 0.14767 0.17382 0.00186  -0.04075 0.02216  54  HIS D C     
4388 O O     . HIS D 55  ? 0.10759 0.14248 0.16876 0.00253  -0.04772 0.02654  54  HIS D O     
4389 C CB    . HIS D 55  ? 0.13436 0.15774 0.16738 -0.00656 -0.04136 0.01585  54  HIS D CB    
4390 C CG    . HIS D 55  ? 0.13723 0.15461 0.16300 -0.00457 -0.03599 0.01586  54  HIS D CG    
4391 N ND1   . HIS D 55  ? 0.12561 0.13995 0.14971 -0.00397 -0.02953 0.01184  54  HIS D ND1   
4392 C CD2   . HIS D 55  ? 0.15138 0.16527 0.17184 -0.00374 -0.03688 0.02005  54  HIS D CD2   
4393 C CE1   . HIS D 55  ? 0.13288 0.14359 0.15143 -0.00318 -0.02659 0.01303  54  HIS D CE1   
4394 N NE2   . HIS D 55  ? 0.10145 0.11108 0.11736 -0.00342 -0.03075 0.01800  54  HIS D NE2   
4395 N N     . ARG D 56  ? 0.08158 0.10819 0.13995 0.00585  -0.03448 0.02115  55  ARG D N     
4396 C CA    . ARG D 56  ? 0.08045 0.10452 0.14447 0.01155  -0.03496 0.02413  55  ARG D CA    
4397 C C     . ARG D 56  ? 0.11974 0.14688 0.19395 0.01619  -0.02814 0.02111  55  ARG D C     
4398 O O     . ARG D 56  ? 0.09257 0.11465 0.16060 0.01577  -0.02219 0.01766  55  ARG D O     
4399 C CB    . ARG D 56  ? 0.10420 0.11687 0.15546 0.01076  -0.03488 0.02552  55  ARG D CB    
4400 C CG    . ARG D 56  ? 0.13491 0.14106 0.19153 0.01635  -0.03670 0.02884  55  ARG D CG    
4401 C CD    . ARG D 56  ? 0.12380 0.11765 0.16799 0.01383  -0.03613 0.03041  55  ARG D CD    
4402 N NE    . ARG D 56  ? 0.10908 0.10141 0.14186 0.00841  -0.04147 0.03560  55  ARG D NE    
4403 C CZ    . ARG D 56  ? 0.18046 0.16450 0.20208 0.00441  -0.04162 0.03876  55  ARG D CZ    
4404 N NH1   . ARG D 56  ? 0.11734 0.09289 0.13831 0.00490  -0.03763 0.03705  55  ARG D NH1   
4405 N NH2   . ARG D 56  ? 0.15745 0.14221 0.16775 -0.00100 -0.04599 0.04386  55  ARG D NH2   
4406 N N     . ILE D 57  ? 0.08789 0.12471 0.17771 0.02053  -0.02899 0.02237  56  ILE D N     
4407 C CA    . ILE D 57  ? 0.07209 0.11482 0.17193 0.02510  -0.02163 0.01903  56  ILE D CA    
4408 C C     . ILE D 57  ? 0.12694 0.16956 0.23800 0.03375  -0.02322 0.02010  56  ILE D C     
4409 O O     . ILE D 57  ? 0.10550 0.15571 0.22738 0.03597  -0.02926 0.02402  56  ILE D O     
4410 C CB    . ILE D 57  ? 0.09391 0.15175 0.20469 0.02209  -0.01953 0.01899  56  ILE D CB    
4411 C CG1   . ILE D 57  ? 0.06221 0.11653 0.16194 0.01406  -0.01898 0.01802  56  ILE D CG1   
4412 C CG2   . ILE D 57  ? 0.07632 0.14239 0.19631 0.02646  -0.01083 0.01582  56  ILE D CG2   
4413 C CD1   . ILE D 57  ? 0.10585 0.17230 0.21543 0.00935  -0.01816 0.01905  56  ILE D CD1   
4414 N N     . ILE D 58  ? 0.11704 0.14978 0.22441 0.03843  -0.01850 0.01635  57  ILE D N     
4415 C CA    . ILE D 58  ? 0.11869 0.14804 0.23631 0.04765  -0.01972 0.01608  57  ILE D CA    
4416 C C     . ILE D 58  ? 0.10439 0.13919 0.22827 0.05326  -0.01004 0.00884  57  ILE D C     
4417 O O     . ILE D 58  ? 0.09725 0.12335 0.21081 0.05237  -0.00436 0.00369  57  ILE D O     
4418 C CB    . ILE D 58  ? 0.10492 0.11428 0.21148 0.04821  -0.02412 0.01791  57  ILE D CB    
4419 C CG1   . ILE D 58  ? 0.11052 0.11674 0.20783 0.04132  -0.03243 0.02511  57  ILE D CG1   
4420 C CG2   . ILE D 58  ? 0.12079 0.12397 0.23278 0.05632  -0.02534 0.01729  57  ILE D CG2   
4421 C CD1   . ILE D 58  ? 0.14350 0.13180 0.23026 0.04037  -0.03760 0.02936  57  ILE D CD1   
4422 N N     . PRO D 59  ? 0.09889 0.14838 0.23552 0.05771  -0.00775 0.00792  58  PRO D N     
4423 C CA    . PRO D 59  ? 0.16069 0.21830 0.30218 0.06273  0.00237  0.00083  58  PRO D CA    
4424 C C     . PRO D 59  ? 0.16133 0.20201 0.29541 0.06926  0.00531  -0.00529 58  PRO D C     
4425 O O     . PRO D 59  ? 0.12688 0.15378 0.25919 0.07315  -0.00073 -0.00334 58  PRO D O     
4426 C CB    . PRO D 59  ? 0.20569 0.28123 0.36303 0.06731  0.00186  0.00220  58  PRO D CB    
4427 C CG    . PRO D 59  ? 0.12625 0.20719 0.28661 0.06074  -0.00731 0.00986  58  PRO D CG    
4428 C CD    . PRO D 59  ? 0.14271 0.20364 0.28951 0.05779  -0.01434 0.01324  58  PRO D CD    
4429 N N     . GLY D 60  ? 0.13947 0.18023 0.26763 0.06938  0.01437  -0.01252 59  GLY D N     
4430 C CA    . GLY D 60  ? 0.15393 0.17725 0.27209 0.07377  0.01726  -0.01976 59  GLY D CA    
4431 C C     . GLY D 60  ? 0.15500 0.15936 0.25907 0.06787  0.01378  -0.01994 59  GLY D C     
4432 O O     . GLY D 60  ? 0.17187 0.16058 0.26606 0.06973  0.01555  -0.02646 59  GLY D O     
4433 N N     . PHE D 61  ? 0.12386 0.12911 0.22181 0.05906  0.00859  -0.01270 60  PHE D N     
4434 C CA    . PHE D 61  ? 0.13751 0.12700 0.21850 0.05179  0.00479  -0.01127 60  PHE D CA    
4435 C C     . PHE D 61  ? 0.11443 0.11081 0.18545 0.04238  0.00604  -0.00884 60  PHE D C     
4436 O O     . PHE D 61  ? 0.15158 0.14491 0.21141 0.03888  0.01006  -0.01297 60  PHE D O     
4437 C CB    . PHE D 61  ? 0.13406 0.11258 0.21598 0.05147  -0.00458 -0.00429 60  PHE D CB    
4438 C CG    . PHE D 61  ? 0.13862 0.10378 0.22758 0.06020  -0.00740 -0.00605 60  PHE D CG    
4439 C CD1   . PHE D 61  ? 0.15283 0.09814 0.23134 0.05961  -0.00779 -0.01018 60  PHE D CD1   
4440 C CD2   . PHE D 61  ? 0.14375 0.11678 0.24389 0.06629  -0.00964 -0.00288 60  PHE D CD2   
4441 C CE1   . PHE D 61  ? 0.17544 0.10779 0.25457 0.06523  -0.00988 -0.01098 60  PHE D CE1   
4442 C CE2   . PHE D 61  ? 0.17196 0.13308 0.27365 0.07284  -0.01186 -0.00347 60  PHE D CE2   
4443 C CZ    . PHE D 61  ? 0.17782 0.11779 0.26893 0.07247  -0.01173 -0.00754 60  PHE D CZ    
4444 N N     . MET D 62  ? 0.09786 0.10268 0.17250 0.03840  0.00212  -0.00253 61  MET D N     
4445 C CA    . MET D 62  ? 0.11445 0.12254 0.18005 0.03041  0.00234  -0.00054 61  MET D CA    
4446 C C     . MET D 62  ? 0.12721 0.14625 0.19997 0.02764  -0.00082 0.00431  61  MET D C     
4447 O O     . MET D 62  ? 0.11946 0.14292 0.20248 0.03065  -0.00495 0.00728  61  MET D O     
4448 C CB    . MET D 62  ? 0.08566 0.08157 0.13878 0.02553  -0.00141 0.00088  61  MET D CB    
4449 C CG    . MET D 62  ? 0.08423 0.07827 0.13704 0.02303  -0.00813 0.00672  61  MET D CG    
4450 S SD    . MET D 62  ? 0.15928 0.14660 0.22010 0.02906  -0.01378 0.01009  61  MET D SD    
4451 C CE    . MET D 62  ? 0.09891 0.09292 0.15955 0.02474  -0.02065 0.01699  61  MET D CE    
4452 N N     . CYS D 63  ? 0.08694 0.10972 0.15433 0.02179  0.00050  0.00501  62  CYS D N     
4453 C CA    . CYS D 63  ? 0.07197 0.10012 0.14168 0.01732  -0.00347 0.00857  62  CYS D CA    
4454 C C     . CYS D 63  ? 0.09621 0.11591 0.15388 0.01297  -0.00613 0.00893  62  CYS D C     
4455 O O     . CYS D 63  ? 0.08289 0.09930 0.13328 0.01102  -0.00324 0.00722  62  CYS D O     
4456 C CB    . CYS D 63  ? 0.10505 0.14310 0.17951 0.01422  0.00019  0.00900  62  CYS D CB    
4457 S SG    . CYS D 63  ? 0.09448 0.14731 0.18396 0.01842  0.00566  0.00831  62  CYS D SG    
4458 N N     . GLN D 64  ? 0.10560 0.12330 0.16135 0.01145  -0.01157 0.01117  63  GLN D N     
4459 C CA    . GLN D 64  ? 0.06383 0.07548 0.10866 0.00801  -0.01304 0.01092  63  GLN D CA    
4460 C C     . GLN D 64  ? 0.08222 0.09671 0.12557 0.00438  -0.01587 0.01078  63  GLN D C     
4461 O O     . GLN D 64  ? 0.09038 0.10944 0.13898 0.00368  -0.01983 0.01234  63  GLN D O     
4462 C CB    . GLN D 64  ? 0.09185 0.09735 0.13178 0.00844  -0.01625 0.01326  63  GLN D CB    
4463 C CG    . GLN D 64  ? 0.08082 0.08292 0.10992 0.00438  -0.01644 0.01319  63  GLN D CG    
4464 C CD    . GLN D 64  ? 0.09558 0.09178 0.11958 0.00341  -0.01939 0.01702  63  GLN D CD    
4465 O OE1   . GLN D 64  ? 0.08992 0.08072 0.11781 0.00643  -0.02054 0.01871  63  GLN D OE1   
4466 N NE2   . GLN D 64  ? 0.15089 0.14776 0.16607 -0.00079 -0.02061 0.01847  63  GLN D NE2   
4467 N N     . GLY D 65  ? 0.06481 0.07649 0.10156 0.00226  -0.01423 0.00846  64  GLY D N     
4468 C CA    . GLY D 65  ? 0.08827 0.10001 0.12265 -0.00046 -0.01660 0.00662  64  GLY D CA    
4469 C C     . GLY D 65  ? 0.07748 0.08597 0.10412 -0.00089 -0.01467 0.00367  64  GLY D C     
4470 O O     . GLY D 65  ? 0.10720 0.11493 0.13030 -0.00018 -0.01243 0.00417  64  GLY D O     
4471 N N     . GLY D 66  ? 0.10006 0.10681 0.12490 -0.00205 -0.01570 0.00029  65  GLY D N     
4472 C CA    . GLY D 66  ? 0.09981 0.10481 0.12038 -0.00095 -0.01332 -0.00344 65  GLY D CA    
4473 C C     . GLY D 66  ? 0.12234 0.12787 0.13473 -0.00191 -0.01388 -0.00746 65  GLY D C     
4474 O O     . GLY D 66  ? 0.15211 0.15820 0.16218 -0.00014 -0.01095 -0.01144 65  GLY D O     
4475 N N     . ASP D 67  ? 0.08354 0.09010 0.09137 -0.00450 -0.01745 -0.00665 66  ASP D N     
4476 C CA    . ASP D 67  ? 0.11038 0.11804 0.10735 -0.00624 -0.01781 -0.01076 66  ASP D CA    
4477 C C     . ASP D 67  ? 0.10227 0.10498 0.09799 -0.00672 -0.02006 -0.01744 66  ASP D C     
4478 O O     . ASP D 67  ? 0.12210 0.12324 0.11792 -0.00980 -0.02548 -0.01715 66  ASP D O     
4479 C CB    . ASP D 67  ? 0.11619 0.12657 0.10686 -0.00942 -0.02185 -0.00615 66  ASP D CB    
4480 C CG    . ASP D 67  ? 0.11269 0.12518 0.08909 -0.01232 -0.02215 -0.00982 66  ASP D CG    
4481 O OD1   . ASP D 67  ? 0.12411 0.13653 0.09592 -0.01115 -0.01818 -0.01723 66  ASP D OD1   
4482 O OD2   . ASP D 67  ? 0.12353 0.13807 0.09282 -0.01555 -0.02631 -0.00525 66  ASP D OD2   
4483 N N     . PHE D 68  ? 0.11970 0.11977 0.11484 -0.00365 -0.01640 -0.02374 67  PHE D N     
4484 C CA    . PHE D 68  ? 0.16002 0.15230 0.15338 -0.00345 -0.01852 -0.03144 67  PHE D CA    
4485 C C     . PHE D 68  ? 0.20313 0.19673 0.18393 -0.00307 -0.01618 -0.04001 67  PHE D C     
4486 O O     . PHE D 68  ? 0.14479 0.13049 0.12257 -0.00216 -0.01742 -0.04857 67  PHE D O     
4487 C CB    . PHE D 68  ? 0.16281 0.14841 0.16609 0.00069  -0.01717 -0.03269 67  PHE D CB    
4488 C CG    . PHE D 68  ? 0.16371 0.15428 0.16995 0.00596  -0.01141 -0.03344 67  PHE D CG    
4489 C CD1   . PHE D 68  ? 0.15918 0.15075 0.16194 0.01008  -0.00765 -0.04181 67  PHE D CD1   
4490 C CD2   . PHE D 68  ? 0.11040 0.10558 0.12342 0.00680  -0.00980 -0.02636 67  PHE D CD2   
4491 C CE1   . PHE D 68  ? 0.16015 0.15934 0.16840 0.01494  -0.00252 -0.04210 67  PHE D CE1   
4492 C CE2   . PHE D 68  ? 0.14151 0.14270 0.15825 0.01077  -0.00561 -0.02670 67  PHE D CE2   
4493 C CZ    . PHE D 68  ? 0.11750 0.12165 0.13302 0.01481  -0.00208 -0.03405 67  PHE D CZ    
4494 N N     . THR D 69  ? 0.17083 0.17372 0.14335 -0.00425 -0.01280 -0.03813 68  THR D N     
4495 C CA    . THR D 69  ? 0.18253 0.18922 0.14148 -0.00455 -0.00929 -0.04609 68  THR D CA    
4496 C C     . THR D 69  ? 0.19408 0.20304 0.13833 -0.01097 -0.01387 -0.04460 68  THR D C     
4497 O O     . THR D 69  ? 0.23900 0.24613 0.17061 -0.01249 -0.01435 -0.05329 68  THR D O     
4498 C CB    . THR D 69  ? 0.18268 0.20048 0.14161 -0.00214 -0.00111 -0.04543 68  THR D CB    
4499 O OG1   . THR D 69  ? 0.15884 0.18275 0.11616 -0.00642 -0.00180 -0.03508 68  THR D OG1   
4500 C CG2   . THR D 69  ? 0.22123 0.23845 0.19517 0.00417  0.00223  -0.04620 68  THR D CG2   
4501 N N     . ARG D 70  ? 0.15114 0.16360 0.09637 -0.01450 -0.01766 -0.03400 69  ARG D N     
4502 C CA    . ARG D 70  ? 0.18369 0.19815 0.11684 -0.02039 -0.02403 -0.03030 69  ARG D CA    
4503 C C     . ARG D 70  ? 0.15820 0.16844 0.09955 -0.02245 -0.03310 -0.02604 69  ARG D C     
4504 O O     . ARG D 70  ? 0.17013 0.18123 0.10242 -0.02725 -0.04017 -0.02535 69  ARG D O     
4505 C CB    . ARG D 70  ? 0.16016 0.18150 0.08847 -0.02293 -0.02294 -0.02037 69  ARG D CB    
4506 C CG    . ARG D 70  ? 0.22897 0.25800 0.14907 -0.02303 -0.01397 -0.02247 69  ARG D CG    
4507 C CD    . ARG D 70  ? 0.30556 0.33832 0.20743 -0.02544 -0.01139 -0.03172 69  ARG D CD    
4508 N NE    . ARG D 70  ? 0.47412 0.50400 0.36333 -0.03073 -0.02024 -0.03084 69  ARG D NE    
4509 C CZ    . ARG D 70  ? 0.49309 0.52673 0.37058 -0.03670 -0.02512 -0.02155 69  ARG D CZ    
4510 N NH1   . ARG D 70  ? 0.39974 0.43853 0.27612 -0.03869 -0.02189 -0.01200 69  ARG D NH1   
4511 N NH2   . ARG D 70  ? 0.45227 0.48387 0.31911 -0.04127 -0.03435 -0.02126 69  ARG D NH2   
4512 N N     . HIS D 71  ? 0.14288 0.15042 0.10105 -0.01940 -0.03308 -0.02258 70  HIS D N     
4513 C CA    . HIS D 71  ? 0.13907 0.14516 0.10770 -0.02129 -0.04019 -0.01904 70  HIS D CA    
4514 C C     . HIS D 71  ? 0.19348 0.20560 0.16256 -0.02353 -0.04626 -0.00984 70  HIS D C     
4515 O O     . HIS D 71  ? 0.16365 0.17778 0.13676 -0.02664 -0.05403 -0.00780 70  HIS D O     
4516 C CB    . HIS D 71  ? 0.15253 0.15291 0.11684 -0.02489 -0.04516 -0.02705 70  HIS D CB    
4517 C CG    . HIS D 71  ? 0.17868 0.17078 0.14132 -0.02187 -0.04000 -0.03693 70  HIS D CG    
4518 N ND1   . HIS D 71  ? 0.15467 0.14058 0.13062 -0.01908 -0.03821 -0.03716 70  HIS D ND1   
4519 C CD2   . HIS D 71  ? 0.18833 0.17737 0.13789 -0.02071 -0.03637 -0.04688 70  HIS D CD2   
4520 C CE1   . HIS D 71  ? 0.17426 0.15242 0.14656 -0.01583 -0.03462 -0.04628 70  HIS D CE1   
4521 N NE2   . HIS D 71  ? 0.18271 0.16303 0.13965 -0.01627 -0.03296 -0.05308 70  HIS D NE2   
4522 N N     . ASN D 72  ? 0.13589 0.15080 0.10184 -0.02210 -0.04340 -0.00384 71  ASN D N     
4523 C CA    . ASN D 72  ? 0.14946 0.16785 0.11608 -0.02336 -0.04986 0.00549  71  ASN D CA    
4524 C C     . ASN D 72  ? 0.18461 0.20222 0.15750 -0.01986 -0.04634 0.01254  71  ASN D C     
4525 O O     . ASN D 72  ? 0.17099 0.18910 0.14164 -0.02062 -0.05113 0.02049  71  ASN D O     
4526 C CB    . ASN D 72  ? 0.17823 0.19878 0.12555 -0.02870 -0.05443 0.00628  71  ASN D CB    
4527 C CG    . ASN D 72  ? 0.18807 0.20920 0.12129 -0.02977 -0.04708 0.00524  71  ASN D CG    
4528 O OD1   . ASN D 72  ? 0.17427 0.19450 0.11343 -0.02651 -0.03938 0.00448  71  ASN D OD1   
4529 N ND2   . ASN D 72  ? 0.23207 0.25609 0.14634 -0.03501 -0.04948 0.00540  71  ASN D ND2   
4530 N N     . GLY D 73  ? 0.16929 0.18467 0.14920 -0.01638 -0.03896 0.01002  72  GLY D N     
4531 C CA    . GLY D 73  ? 0.14922 0.16250 0.13445 -0.01375 -0.03612 0.01540  72  GLY D CA    
4532 C C     . GLY D 73  ? 0.11695 0.12976 0.09137 -0.01612 -0.03176 0.01678  72  GLY D C     
4533 O O     . GLY D 73  ? 0.16515 0.17486 0.14356 -0.01496 -0.02950 0.02059  72  GLY D O     
4534 N N     . THR D 74  ? 0.12695 0.14321 0.08778 -0.01984 -0.03017 0.01336  73  THR D N     
4535 C CA    . THR D 74  ? 0.13329 0.15231 0.08416 -0.02316 -0.02530 0.01527  73  THR D CA    
4536 C C     . THR D 74  ? 0.18746 0.21126 0.13810 -0.02187 -0.01691 0.00710  73  THR D C     
4537 O O     . THR D 74  ? 0.13597 0.16458 0.08243 -0.02437 -0.01175 0.00871  73  THR D O     
4538 C CB    . THR D 74  ? 0.16997 0.19204 0.10358 -0.02903 -0.02888 0.01890  73  THR D CB    
4539 O OG1   . THR D 74  ? 0.16255 0.18887 0.08640 -0.03012 -0.02717 0.00974  73  THR D OG1   
4540 C CG2   . THR D 74  ? 0.21352 0.23167 0.14826 -0.02965 -0.03903 0.02712  73  THR D CG2   
4541 N N     . GLY D 75  ? 0.12446 0.14730 0.08062 -0.01816 -0.01574 -0.00103 74  GLY D N     
4542 C CA    . GLY D 75  ? 0.13891 0.16575 0.09509 -0.01576 -0.00891 -0.00931 74  GLY D CA    
4543 C C     . GLY D 75  ? 0.15298 0.17815 0.12354 -0.01103 -0.00600 -0.01057 74  GLY D C     
4544 O O     . GLY D 75  ? 0.14400 0.16618 0.12251 -0.01047 -0.00757 -0.00491 74  GLY D O     
4545 N N     . GLY D 76  ? 0.20612 0.23273 0.17964 -0.00724 -0.00203 -0.01844 75  GLY D N     
4546 C CA    . GLY D 76  ? 0.13807 0.16400 0.12417 -0.00282 0.00016  -0.01915 75  GLY D CA    
4547 C C     . GLY D 76  ? 0.16055 0.19607 0.14898 -0.00058 0.00672  -0.02277 75  GLY D C     
4548 O O     . GLY D 76  ? 0.14355 0.18787 0.12429 -0.00361 0.01065  -0.02289 75  GLY D O     
4549 N N     . LYS D 77  ? 0.09623 0.13130 0.09578 0.00455  0.00782  -0.02518 76  LYS D N     
4550 C CA    . LYS D 77  ? 0.12015 0.16643 0.12603 0.00766  0.01338  -0.02804 76  LYS D CA    
4551 C C     . LYS D 77  ? 0.12075 0.16459 0.13975 0.01209  0.01140  -0.02641 76  LYS D C     
4552 O O     . LYS D 77  ? 0.13047 0.16324 0.15199 0.01354  0.00689  -0.02536 76  LYS D O     
4553 C CB    . LYS D 77  ? 0.16878 0.21943 0.17120 0.01167  0.01799  -0.03800 76  LYS D CB    
4554 C CG    . LYS D 77  ? 0.18494 0.22370 0.19132 0.01778  0.01520  -0.04500 76  LYS D CG    
4555 C CD    . LYS D 77  ? 0.22561 0.26781 0.22808 0.02257  0.02037  -0.05672 76  LYS D CD    
4556 C CE    . LYS D 77  ? 0.22010 0.24689 0.22645 0.02843  0.01665  -0.06401 76  LYS D CE    
4557 N NZ    . LYS D 77  ? 0.30363 0.33257 0.30912 0.03546  0.02213  -0.07703 76  LYS D NZ    
4558 N N     . SER D 78  ? 0.11283 0.16827 0.14009 0.01343  0.01452  -0.02544 77  SER D N     
4559 C CA    . SER D 78  ? 0.09012 0.14512 0.12915 0.01712  0.01181  -0.02300 77  SER D CA    
4560 C C     . SER D 78  ? 0.10500 0.16343 0.15383 0.02557  0.01354  -0.02948 77  SER D C     
4561 O O     . SER D 78  ? 0.09251 0.15555 0.13935 0.02867  0.01821  -0.03694 77  SER D O     
4562 C CB    . SER D 78  ? 0.12828 0.19369 0.17166 0.01286  0.01230  -0.01725 77  SER D CB    
4563 O OG    . SER D 78  ? 0.07385 0.15580 0.12494 0.01487  0.01726  -0.02014 77  SER D OG    
4564 N N     . ILE D 79  ? 0.10166 0.15779 0.16095 0.02958  0.00958  -0.02663 78  ILE D N     
4565 C CA    . ILE D 79  ? 0.08669 0.14644 0.15832 0.03870  0.01019  -0.03151 78  ILE D CA    
4566 C C     . ILE D 79  ? 0.09663 0.17776 0.17808 0.04077  0.01559  -0.03336 78  ILE D C     
4567 O O     . ILE D 79  ? 0.12376 0.21120 0.21711 0.04960  0.01753  -0.03884 78  ILE D O     
4568 C CB    . ILE D 79  ? 0.10114 0.15230 0.18103 0.04212  0.00318  -0.02619 78  ILE D CB    
4569 C CG1   . ILE D 79  ? 0.08135 0.14267 0.16556 0.03797  0.00069  -0.01832 78  ILE D CG1   
4570 C CG2   . ILE D 79  ? 0.09761 0.12964 0.16869 0.03909  -0.00136 -0.02379 78  ILE D CG2   
4571 C CD1   . ILE D 79  ? 0.12651 0.18477 0.22018 0.04227  -0.00593 -0.01330 78  ILE D CD1   
4572 N N     . TYR D 80  ? 0.07986 0.17248 0.15753 0.03290  0.01820  -0.02911 79  TYR D N     
4573 C CA    . TYR D 80  ? 0.15600 0.27122 0.24348 0.03263  0.02359  -0.02970 79  TYR D CA    
4574 C C     . TYR D 80  ? 0.09711 0.22247 0.17636 0.02985  0.03212  -0.03481 79  TYR D C     
4575 O O     . TYR D 80  ? 0.13287 0.27928 0.22014 0.02905  0.03809  -0.03558 79  TYR D O     
4576 C CB    . TYR D 80  ? 0.11671 0.23868 0.20605 0.02419  0.02044  -0.02096 79  TYR D CB    
4577 C CG    . TYR D 80  ? 0.14873 0.26037 0.24150 0.02513  0.01208  -0.01570 79  TYR D CG    
4578 C CD1   . TYR D 80  ? 0.15225 0.26893 0.25988 0.03286  0.00851  -0.01560 79  TYR D CD1   
4579 C CD2   . TYR D 80  ? 0.08325 0.18067 0.16427 0.01858  0.00778  -0.01075 79  TYR D CD2   
4580 C CE1   . TYR D 80  ? 0.16721 0.27491 0.27576 0.03283  0.00054  -0.00986 79  TYR D CE1   
4581 C CE2   . TYR D 80  ? 0.12192 0.21118 0.20403 0.01893  0.00105  -0.00632 79  TYR D CE2   
4582 C CZ    . TYR D 80  ? 0.16442 0.25878 0.25926 0.02552  -0.00269 -0.00551 79  TYR D CZ    
4583 O OH    . TYR D 80  ? 0.16838 0.25512 0.26233 0.02512  -0.00971 -0.00021 79  TYR D OH    
4584 N N     . GLY D 81  ? 0.09378 0.20624 0.15723 0.02770  0.03269  -0.03782 80  GLY D N     
4585 C CA    . GLY D 81  ? 0.11746 0.23780 0.16835 0.02229  0.03923  -0.04019 80  GLY D CA    
4586 C C     . GLY D 81  ? 0.12916 0.23531 0.16384 0.01381  0.03482  -0.03424 80  GLY D C     
4587 O O     . GLY D 81  ? 0.13274 0.22404 0.16705 0.01321  0.02786  -0.02990 80  GLY D O     
4588 N N     . GLU D 82  ? 0.12966 0.24133 0.15094 0.00722  0.03894  -0.03362 81  GLU D N     
4589 C CA    . GLU D 82  ? 0.14884 0.24721 0.15536 0.00024  0.03405  -0.02795 81  GLU D CA    
4590 C C     . GLU D 82  ? 0.17020 0.26283 0.18019 -0.00517 0.02866  -0.01799 81  GLU D C     
4591 O O     . GLU D 82  ? 0.14836 0.22594 0.15411 -0.00608 0.02253  -0.01470 81  GLU D O     
4592 C CB    . GLU D 82  ? 0.20504 0.31146 0.19602 -0.00629 0.03890  -0.02775 81  GLU D CB    
4593 C CG    . GLU D 82  ? 0.17152 0.27974 0.15422 -0.00139 0.04337  -0.03912 81  GLU D CG    
4594 C CD    . GLU D 82  ? 0.27128 0.38782 0.23526 -0.00860 0.04800  -0.03890 81  GLU D CD    
4595 O OE1   . GLU D 82  ? 0.19046 0.30970 0.14781 -0.01781 0.04685  -0.02841 81  GLU D OE1   
4596 O OE2   . GLU D 82  ? 0.22451 0.34385 0.17938 -0.00525 0.05248  -0.04931 81  GLU D OE2   
4597 N N     . LYS D 83  ? 0.15212 0.25695 0.17022 -0.00888 0.03087  -0.01368 82  LYS D N     
4598 C CA    . LYS D 83  ? 0.15679 0.25547 0.17695 -0.01471 0.02585  -0.00549 82  LYS D CA    
4599 C C     . LYS D 83  ? 0.14275 0.25091 0.17850 -0.01278 0.02538  -0.00517 82  LYS D C     
4600 O O     . LYS D 83  ? 0.10502 0.22897 0.15101 -0.00856 0.02999  -0.00941 82  LYS D O     
4601 C CB    . LYS D 83  ? 0.18974 0.29191 0.20128 -0.02514 0.02714  0.00176  82  LYS D CB    
4602 C CG    . LYS D 83  ? 0.36544 0.46851 0.36195 -0.02809 0.03016  0.00145  82  LYS D CG    
4603 C CD    . LYS D 83  ? 0.38875 0.47317 0.37428 -0.03037 0.02324  0.00633  82  LYS D CD    
4604 C CE    . LYS D 83  ? 0.36418 0.44585 0.33672 -0.02883 0.02347  0.00259  82  LYS D CE    
4605 N NZ    . LYS D 83  ? 0.31364 0.37928 0.27883 -0.03053 0.01576  0.00811  82  LYS D NZ    
4606 N N     . PHE D 84  ? 0.13829 0.23730 0.17606 -0.01552 0.01954  -0.00048 83  PHE D N     
4607 C CA    . PHE D 84  ? 0.18916 0.29812 0.23940 -0.01663 0.01792  0.00131  83  PHE D CA    
4608 C C     . PHE D 84  ? 0.14467 0.24470 0.19087 -0.02500 0.01305  0.00730  83  PHE D C     
4609 O O     . PHE D 84  ? 0.08655 0.16991 0.12246 -0.02688 0.01010  0.00925  83  PHE D O     
4610 C CB    . PHE D 84  ? 0.18603 0.29368 0.24593 -0.00774 0.01476  -0.00204 83  PHE D CB    
4611 C CG    . PHE D 84  ? 0.13730 0.22576 0.19070 -0.00558 0.00925  -0.00128 83  PHE D CG    
4612 C CD1   . PHE D 84  ? 0.08097 0.15755 0.12670 -0.00185 0.00951  -0.00399 83  PHE D CD1   
4613 C CD2   . PHE D 84  ? 0.06317 0.14728 0.11860 -0.00736 0.00392  0.00175  83  PHE D CD2   
4614 C CE1   . PHE D 84  ? 0.14050 0.20274 0.18229 -0.00028 0.00526  -0.00296 83  PHE D CE1   
4615 C CE2   . PHE D 84  ? 0.13196 0.20123 0.18137 -0.00548 0.00026  0.00219  83  PHE D CE2   
4616 C CZ    . PHE D 84  ? 0.08877 0.14773 0.13217 -0.00195 0.00124  0.00014  83  PHE D CZ    
4617 N N     . GLU D 85  ? 0.12650 0.23820 0.18190 -0.02990 0.01197  0.00979  84  GLU D N     
4618 C CA    . GLU D 85  ? 0.07605 0.18027 0.12733 -0.03964 0.00787  0.01483  84  GLU D CA    
4619 C C     . GLU D 85  ? 0.11193 0.19868 0.15881 -0.03777 0.00141  0.01407  84  GLU D C     
4620 O O     . GLU D 85  ? 0.13732 0.22234 0.18706 -0.03032 -0.00034 0.01104  84  GLU D O     
4621 C CB    . GLU D 85  ? 0.10271 0.22607 0.16573 -0.04683 0.00822  0.01760  84  GLU D CB    
4622 C CG    . GLU D 85  ? 0.15092 0.28531 0.22717 -0.04185 0.00511  0.01540  84  GLU D CG    
4623 C CD    . GLU D 85  ? 0.26413 0.41565 0.35171 -0.04717 0.00524  0.01761  84  GLU D CD    
4624 O OE1   . GLU D 85  ? 0.25576 0.41342 0.34178 -0.05257 0.01005  0.01978  84  GLU D OE1   
4625 O OE2   . GLU D 85  ? 0.32036 0.47677 0.41666 -0.04545 0.00011  0.01728  84  GLU D OE2   
4626 N N     . ASP D 86  ? 0.12020 0.19321 0.15936 -0.04474 -0.00196 0.01688  85  ASP D N     
4627 C CA    . ASP D 86  ? 0.09636 0.15404 0.13060 -0.04386 -0.00722 0.01516  85  ASP D CA    
4628 C C     . ASP D 86  ? 0.11418 0.18167 0.15606 -0.04525 -0.01101 0.01427  85  ASP D C     
4629 O O     . ASP D 86  ? 0.09174 0.16801 0.13886 -0.05343 -0.01295 0.01661  85  ASP D O     
4630 C CB    . ASP D 86  ? 0.09479 0.13576 0.12044 -0.05092 -0.00992 0.01753  85  ASP D CB    
4631 C CG    . ASP D 86  ? 0.13929 0.17022 0.15772 -0.04878 -0.00774 0.01947  85  ASP D CG    
4632 O OD1   . ASP D 86  ? 0.11669 0.14458 0.13333 -0.04059 -0.00632 0.01683  85  ASP D OD1   
4633 O OD2   . ASP D 86  ? 0.15560 0.18206 0.17028 -0.05579 -0.00804 0.02434  85  ASP D OD2   
4634 N N     . GLU D 87  ? 0.08333 0.14977 0.12589 -0.03798 -0.01269 0.01168  86  GLU D N     
4635 C CA    . GLU D 87  ? 0.08479 0.16247 0.13504 -0.03806 -0.01703 0.01187  86  GLU D CA    
4636 C C     . GLU D 87  ? 0.10241 0.17310 0.14687 -0.04634 -0.02301 0.01178  86  GLU D C     
4637 O O     . GLU D 87  ? 0.12006 0.20301 0.17206 -0.05280 -0.02664 0.01355  86  GLU D O     
4638 C CB    . GLU D 87  ? 0.11283 0.18825 0.16303 -0.02891 -0.01794 0.01047  86  GLU D CB    
4639 C CG    . GLU D 87  ? 0.09747 0.18351 0.15491 -0.02808 -0.02369 0.01199  86  GLU D CG    
4640 C CD    . GLU D 87  ? 0.07869 0.16382 0.13857 -0.01872 -0.02425 0.01228  86  GLU D CD    
4641 O OE1   . GLU D 87  ? 0.06815 0.14134 0.12105 -0.01454 -0.02089 0.01076  86  GLU D OE1   
4642 O OE2   . GLU D 87  ? 0.06765 0.16389 0.13721 -0.01586 -0.02862 0.01457  86  GLU D OE2   
4643 N N     . ASN D 88  ? 0.13941 0.19115 0.17101 -0.04621 -0.02416 0.00913  87  ASN D N     
4644 C CA    . ASN D 88  ? 0.13272 0.17377 0.15602 -0.05373 -0.02924 0.00705  87  ASN D CA    
4645 C C     . ASN D 88  ? 0.13012 0.15007 0.14106 -0.05090 -0.02735 0.00339  87  ASN D C     
4646 O O     . ASN D 88  ? 0.13888 0.15531 0.14893 -0.04352 -0.02299 0.00327  87  ASN D O     
4647 C CB    . ASN D 88  ? 0.10774 0.15477 0.13000 -0.05475 -0.03519 0.00604  87  ASN D CB    
4648 C CG    . ASN D 88  ? 0.16575 0.20795 0.18124 -0.04659 -0.03434 0.00451  87  ASN D CG    
4649 O OD1   . ASN D 88  ? 0.15044 0.17759 0.15458 -0.04430 -0.03212 0.00093  87  ASN D OD1   
4650 N ND2   . ASN D 88  ? 0.12473 0.18026 0.14803 -0.04227 -0.03626 0.00759  87  ASN D ND2   
4651 N N     . PHE D 89  ? 0.15970 0.16597 0.16185 -0.05662 -0.03096 -0.00011 88  PHE D N     
4652 C CA    . PHE D 89  ? 0.17606 0.16265 0.16753 -0.05295 -0.02930 -0.00498 88  PHE D CA    
4653 C C     . PHE D 89  ? 0.15585 0.13583 0.13631 -0.05372 -0.03227 -0.01117 88  PHE D C     
4654 O O     . PHE D 89  ? 0.22129 0.18418 0.19231 -0.05483 -0.03291 -0.01704 88  PHE D O     
4655 C CB    . PHE D 89  ? 0.20030 0.17195 0.19010 -0.05789 -0.03006 -0.00449 88  PHE D CB    
4656 C CG    . PHE D 89  ? 0.16614 0.14382 0.16354 -0.05763 -0.02691 0.00205  88  PHE D CG    
4657 C CD1   . PHE D 89  ? 0.12598 0.10459 0.12465 -0.04891 -0.02230 0.00315  88  PHE D CD1   
4658 C CD2   . PHE D 89  ? 0.17282 0.15647 0.17550 -0.06692 -0.02856 0.00719  88  PHE D CD2   
4659 C CE1   . PHE D 89  ? 0.15733 0.14165 0.16047 -0.04922 -0.01974 0.00861  88  PHE D CE1   
4660 C CE2   . PHE D 89  ? 0.15837 0.14864 0.16564 -0.06728 -0.02500 0.01316  88  PHE D CE2   
4661 C CZ    . PHE D 89  ? 0.12962 0.11984 0.13621 -0.05831 -0.02075 0.01356  88  PHE D CZ    
4662 N N     . ILE D 90  ? 0.14004 0.13306 0.12089 -0.05270 -0.03416 -0.01008 89  ILE D N     
4663 C CA    . ILE D 90  ? 0.17545 0.16413 0.14349 -0.05445 -0.03734 -0.01521 89  ILE D CA    
4664 C C     . ILE D 90  ? 0.18185 0.15896 0.13973 -0.04744 -0.03178 -0.02052 89  ILE D C     
4665 O O     . ILE D 90  ? 0.18347 0.14903 0.12841 -0.04920 -0.03237 -0.02793 89  ILE D O     
4666 C CB    . ILE D 90  ? 0.18398 0.18974 0.15501 -0.05451 -0.04131 -0.01083 89  ILE D CB    
4667 C CG1   . ILE D 90  ? 0.14561 0.16516 0.12804 -0.06165 -0.04739 -0.00654 89  ILE D CG1   
4668 C CG2   . ILE D 90  ? 0.18957 0.19110 0.14435 -0.05619 -0.04418 -0.01531 89  ILE D CG2   
4669 C CD1   . ILE D 90  ? 0.19087 0.22892 0.18118 -0.05922 -0.05139 -0.00085 89  ILE D CD1   
4670 N N     . LEU D 91  ? 0.14360 0.12490 0.10732 -0.03961 -0.02628 -0.01733 90  LEU D N     
4671 C CA    . LEU D 91  ? 0.14586 0.12081 0.10327 -0.03296 -0.02048 -0.02116 90  LEU D CA    
4672 C C     . LEU D 91  ? 0.19794 0.16038 0.15834 -0.02922 -0.01688 -0.02392 90  LEU D C     
4673 O O     . LEU D 91  ? 0.18317 0.14470 0.15217 -0.03010 -0.01771 -0.01994 90  LEU D O     
4674 C CB    . LEU D 91  ? 0.13178 0.11800 0.09475 -0.02756 -0.01747 -0.01565 90  LEU D CB    
4675 C CG    . LEU D 91  ? 0.13215 0.12892 0.09173 -0.02987 -0.02141 -0.01194 90  LEU D CG    
4676 C CD1   . LEU D 91  ? 0.14679 0.15136 0.11398 -0.02464 -0.01906 -0.00585 90  LEU D CD1   
4677 C CD2   . LEU D 91  ? 0.19795 0.19077 0.14077 -0.03228 -0.02151 -0.01706 90  LEU D CD2   
4678 N N     . LYS D 92  ? 0.19137 0.14489 0.14469 -0.02480 -0.01282 -0.03056 91  LYS D N     
4679 C CA    . LYS D 92  ? 0.19762 0.13824 0.15460 -0.02028 -0.01045 -0.03352 91  LYS D CA    
4680 C C     . LYS D 92  ? 0.18349 0.12878 0.14525 -0.01156 -0.00399 -0.03351 91  LYS D C     
4681 O O     . LYS D 92  ? 0.15000 0.10642 0.10986 -0.00998 -0.00085 -0.03235 91  LYS D O     
4682 C CB    . LYS D 92  ? 0.21774 0.14124 0.16465 -0.02217 -0.01193 -0.04293 91  LYS D CB    
4683 C CG    . LYS D 92  ? 0.29967 0.21882 0.24194 -0.03257 -0.01925 -0.04298 91  LYS D CG    
4684 C CD    . LYS D 92  ? 0.37643 0.27470 0.30904 -0.03512 -0.02170 -0.05270 91  LYS D CD    
4685 C CE    . LYS D 92  ? 0.47221 0.36685 0.40158 -0.04726 -0.02994 -0.05192 91  LYS D CE    
4686 N NZ    . LYS D 92  ? 0.50082 0.40638 0.44323 -0.05226 -0.03284 -0.04065 91  LYS D NZ    
4687 N N     . HIS D 93  ? 0.18475 0.12173 0.15366 -0.00648 -0.00276 -0.03380 92  HIS D N     
4688 C CA    . HIS D 93  ? 0.18707 0.12909 0.16345 0.00178  0.00253  -0.03364 92  HIS D CA    
4689 C C     . HIS D 93  ? 0.20648 0.14272 0.17693 0.00682  0.00743  -0.04348 92  HIS D C     
4690 O O     . HIS D 93  ? 0.25912 0.18236 0.23194 0.01166  0.00768  -0.04861 92  HIS D O     
4691 C CB    . HIS D 93  ? 0.16072 0.09765 0.14772 0.00490  0.00039  -0.02884 92  HIS D CB    
4692 C CG    . HIS D 93  ? 0.15600 0.09828 0.14647 -0.00051 -0.00361 -0.02056 92  HIS D CG    
4693 N ND1   . HIS D 93  ? 0.15325 0.08989 0.14017 -0.00786 -0.00816 -0.01873 92  HIS D ND1   
4694 C CD2   . HIS D 93  ? 0.13026 0.08402 0.12715 0.00008  -0.00325 -0.01439 92  HIS D CD2   
4695 C CE1   . HIS D 93  ? 0.15258 0.09840 0.14408 -0.01085 -0.00953 -0.01183 92  HIS D CE1   
4696 N NE2   . HIS D 93  ? 0.15863 0.11381 0.15540 -0.00587 -0.00673 -0.00967 92  HIS D NE2   
4697 N N     . THR D 94  ? 0.17261 0.11846 0.13467 0.00571  0.01137  -0.04623 93  THR D N     
4698 C CA    . THR D 94  ? 0.19942 0.14138 0.15166 0.00886  0.01669  -0.05681 93  THR D CA    
4699 C C     . THR D 94  ? 0.20870 0.16094 0.16830 0.01709  0.02517  -0.05889 93  THR D C     
4700 O O     . THR D 94  ? 0.26040 0.21012 0.21395 0.02153  0.03109  -0.06886 93  THR D O     
4701 C CB    . THR D 94  ? 0.30896 0.25618 0.24477 0.00188  0.01621  -0.05883 93  THR D CB    
4702 O OG1   . THR D 94  ? 0.24729 0.21067 0.18567 -0.00068 0.01659  -0.04955 93  THR D OG1   
4703 C CG2   . THR D 94  ? 0.23736 0.17404 0.16533 -0.00627 0.00783  -0.05964 93  THR D CG2   
4704 N N     . GLY D 95  ? 0.19364 0.15833 0.16586 0.01883  0.02616  -0.05041 94  GLY D N     
4705 C CA    . GLY D 95  ? 0.16588 0.14231 0.14778 0.02570  0.03361  -0.05154 94  GLY D CA    
4706 C C     . GLY D 95  ? 0.15533 0.14665 0.14786 0.02411  0.03354  -0.04143 94  GLY D C     
4707 O O     . GLY D 95  ? 0.18247 0.17326 0.17658 0.01932  0.02750  -0.03383 94  GLY D O     
4708 N N     . PRO D 96  ? 0.20243 0.20777 0.20282 0.02798  0.04057  -0.04170 95  PRO D N     
4709 C CA    . PRO D 96  ? 0.16242 0.18101 0.17400 0.02591  0.04010  -0.03252 95  PRO D CA    
4710 C C     . PRO D 96  ? 0.15491 0.17737 0.15681 0.01742  0.03791  -0.02605 95  PRO D C     
4711 O O     . PRO D 96  ? 0.18919 0.21168 0.17657 0.01361  0.03991  -0.02832 95  PRO D O     
4712 C CB    . PRO D 96  ? 0.16408 0.19819 0.18496 0.03079  0.04908  -0.03529 95  PRO D CB    
4713 C CG    . PRO D 96  ? 0.21152 0.23854 0.23008 0.03847  0.05365  -0.04664 95  PRO D CG    
4714 C CD    . PRO D 96  ? 0.18506 0.19536 0.18527 0.03436  0.04956  -0.05102 95  PRO D CD    
4715 N N     . GLY D 97  ? 0.14443 0.16949 0.15423 0.01468  0.03317  -0.01805 96  GLY D N     
4716 C CA    . GLY D 97  ? 0.10671 0.13326 0.11037 0.00803  0.02983  -0.01149 96  GLY D CA    
4717 C C     . GLY D 97  ? 0.11805 0.13436 0.11690 0.00558  0.02251  -0.01002 96  GLY D C     
4718 O O     . GLY D 97  ? 0.11906 0.13644 0.11749 0.00184  0.01873  -0.00421 96  GLY D O     
4719 N N     . ILE D 98  ? 0.11023 0.11684 0.10662 0.00758  0.02042  -0.01496 97  ILE D N     
4720 C CA    . ILE D 98  ? 0.10779 0.10728 0.10069 0.00429  0.01411  -0.01329 97  ILE D CA    
4721 C C     . ILE D 98  ? 0.12083 0.12182 0.12329 0.00425  0.01048  -0.00775 97  ILE D C     
4722 O O     . ILE D 98  ? 0.10111 0.10250 0.11227 0.00746  0.01077  -0.00713 97  ILE D O     
4723 C CB    . ILE D 98  ? 0.11394 0.10207 0.10298 0.00524  0.01254  -0.01909 97  ILE D CB    
4724 C CG1   . ILE D 98  ? 0.14713 0.13226 0.12315 0.00380  0.01492  -0.02573 97  ILE D CG1   
4725 C CG2   . ILE D 98  ? 0.10794 0.09111 0.09789 0.00152  0.00635  -0.01587 97  ILE D CG2   
4726 C CD1   . ILE D 98  ? 0.16037 0.14861 0.12630 -0.00252 0.01147  -0.02325 97  ILE D CD1   
4727 N N     . LEU D 99  ? 0.08458 0.08676 0.08533 0.00087  0.00678  -0.00406 98  LEU D N     
4728 C CA    . LEU D 99  ? 0.10206 0.10548 0.10979 0.00081  0.00376  -0.00031 98  LEU D CA    
4729 C C     . LEU D 99  ? 0.10143 0.10112 0.10788 -0.00092 0.00045  -0.00089 98  LEU D C     
4730 O O     . LEU D 99  ? 0.11922 0.11934 0.12110 -0.00370 -0.00153 -0.00108 98  LEU D O     
4731 C CB    . LEU D 99  ? 0.08854 0.09632 0.09712 -0.00076 0.00248  0.00391  98  LEU D CB    
4732 C CG    . LEU D 99  ? 0.11093 0.11896 0.12587 -0.00021 -0.00035 0.00606  98  LEU D CG    
4733 C CD1   . LEU D 99  ? 0.11250 0.12093 0.13359 0.00132  0.00057  0.00601  98  LEU D CD1   
4734 C CD2   . LEU D 99  ? 0.12757 0.13685 0.14323 -0.00106 -0.00242 0.00973  98  LEU D CD2   
4735 N N     . SER D 100 ? 0.09581 0.09313 0.10638 -0.00001 -0.00049 -0.00042 99  SER D N     
4736 C CA    . SER D 100 ? 0.13038 0.12451 0.13935 -0.00274 -0.00281 -0.00034 99  SER D CA    
4737 C C     . SER D 100 ? 0.09611 0.09312 0.10904 -0.00283 -0.00381 0.00228  99  SER D C     
4738 O O     . SER D 100 ? 0.10273 0.10121 0.11897 -0.00047 -0.00343 0.00314  99  SER D O     
4739 C CB    . SER D 100 ? 0.12140 0.10614 0.12755 -0.00253 -0.00290 -0.00288 99  SER D CB    
4740 O OG    . SER D 100 ? 0.12098 0.10149 0.12555 -0.00659 -0.00552 -0.00167 99  SER D OG    
4741 N N     . MET D 101 ? 0.10347 0.10234 0.11568 -0.00620 -0.00501 0.00335  100 MET D N     
4742 C CA    . MET D 101 ? 0.10056 0.10379 0.11444 -0.00674 -0.00495 0.00510  100 MET D CA    
4743 C C     . MET D 101 ? 0.11320 0.11059 0.12479 -0.00782 -0.00608 0.00727  100 MET D C     
4744 O O     . MET D 101 ? 0.10487 0.09526 0.11405 -0.01029 -0.00738 0.00820  100 MET D O     
4745 C CB    . MET D 101 ? 0.10743 0.11833 0.12256 -0.01000 -0.00470 0.00560  100 MET D CB    
4746 C CG    . MET D 101 ? 0.06301 0.08129 0.08258 -0.00779 -0.00453 0.00441  100 MET D CG    
4747 S SD    . MET D 101 ? 0.09492 0.11378 0.11734 -0.00263 -0.00373 0.00310  100 MET D SD    
4748 C CE    . MET D 101 ? 0.07390 0.09844 0.09604 -0.00306 -0.00166 0.00185  100 MET D CE    
4749 N N     . ALA D 102 ? 0.09198 0.09141 0.10381 -0.00644 -0.00640 0.00837  101 ALA D N     
4750 C CA    . ALA D 102 ? 0.12102 0.11631 0.12970 -0.00808 -0.00856 0.01191  101 ALA D CA    
4751 C C     . ALA D 102 ? 0.13692 0.13714 0.14120 -0.01326 -0.00768 0.01411  101 ALA D C     
4752 O O     . ALA D 102 ? 0.14401 0.15305 0.14950 -0.01387 -0.00498 0.01183  101 ALA D O     
4753 C CB    . ALA D 102 ? 0.10815 0.10469 0.11806 -0.00528 -0.01027 0.01242  101 ALA D CB    
4754 N N     . ASN D 103 ? 0.09247 0.08752 0.09220 -0.01699 -0.00988 0.01897  102 ASN D N     
4755 C CA    . ASN D 103 ? 0.11651 0.11822 0.11157 -0.02324 -0.00814 0.02186  102 ASN D CA    
4756 C C     . ASN D 103 ? 0.10874 0.10431 0.09682 -0.02735 -0.01142 0.02881  102 ASN D C     
4757 O O     . ASN D 103 ? 0.15714 0.14247 0.14551 -0.02459 -0.01578 0.03138  102 ASN D O     
4758 C CB    . ASN D 103 ? 0.10675 0.11087 0.10469 -0.02751 -0.00664 0.02154  102 ASN D CB    
4759 C CG    . ASN D 103 ? 0.13276 0.12297 0.13011 -0.03006 -0.01025 0.02393  102 ASN D CG    
4760 O OD1   . ASN D 103 ? 0.14230 0.12261 0.13561 -0.03229 -0.01345 0.02904  102 ASN D OD1   
4761 N ND2   . ASN D 103 ? 0.11298 0.10133 0.11376 -0.02967 -0.01031 0.02014  102 ASN D ND2   
4762 N N     . ALA D 104 ? 0.11542 0.11836 0.09769 -0.03394 -0.00927 0.03231  103 ALA D N     
4763 C CA    . ALA D 104 ? 0.15898 0.15708 0.13256 -0.03994 -0.01231 0.04071  103 ALA D CA    
4764 C C     . ALA D 104 ? 0.16666 0.16272 0.13928 -0.04862 -0.01194 0.04608  103 ALA D C     
4765 O O     . ALA D 104 ? 0.15672 0.15760 0.12172 -0.05648 -0.01095 0.05256  103 ALA D O     
4766 C CB    . ALA D 104 ? 0.17333 0.18267 0.13777 -0.04191 -0.01001 0.04118  103 ALA D CB    
4767 N N     . GLY D 105 ? 0.13670 0.12564 0.11629 -0.04818 -0.01293 0.04359  104 GLY D N     
4768 C CA    . GLY D 105 ? 0.16936 0.15611 0.14942 -0.05716 -0.01328 0.04759  104 GLY D CA    
4769 C C     . GLY D 105 ? 0.13473 0.13563 0.12232 -0.05819 -0.00893 0.04193  104 GLY D C     
4770 O O     . GLY D 105 ? 0.12114 0.13085 0.11336 -0.05105 -0.00612 0.03516  104 GLY D O     
4771 N N     . PRO D 106 ? 0.14188 0.14501 0.13156 -0.06743 -0.00912 0.04524  105 PRO D N     
4772 C CA    . PRO D 106 ? 0.15742 0.17499 0.15610 -0.06856 -0.00645 0.04050  105 PRO D CA    
4773 C C     . PRO D 106 ? 0.13992 0.17999 0.14301 -0.06453 0.00011  0.03684  105 PRO D C     
4774 O O     . PRO D 106 ? 0.19230 0.24246 0.19090 -0.06700 0.00426  0.03974  105 PRO D O     
4775 C CB    . PRO D 106 ? 0.17086 0.18917 0.17046 -0.08127 -0.00793 0.04669  105 PRO D CB    
4776 C CG    . PRO D 106 ? 0.21069 0.20504 0.20211 -0.08283 -0.01366 0.05141  105 PRO D CG    
4777 C CD    . PRO D 106 ? 0.21529 0.20450 0.20021 -0.07708 -0.01353 0.05358  105 PRO D CD    
4778 N N     . ASN D 107 ? 0.10876 0.15592 0.11999 -0.05810 0.00086  0.03027  106 ASN D N     
4779 C CA    . ASN D 107 ? 0.10115 0.16928 0.12003 -0.05397 0.00635  0.02624  106 ASN D CA    
4780 C C     . ASN D 107 ? 0.09850 0.16982 0.11163 -0.04816 0.01037  0.02387  106 ASN D C     
4781 O O     . ASN D 107 ? 0.09995 0.18796 0.11445 -0.04870 0.01628  0.02272  106 ASN D O     
4782 C CB    . ASN D 107 ? 0.10559 0.19265 0.13152 -0.06271 0.00967  0.02965  106 ASN D CB    
4783 C CG    . ASN D 107 ? 0.11944 0.20340 0.15109 -0.06953 0.00454  0.03157  106 ASN D CG    
4784 O OD1   . ASN D 107 ? 0.13173 0.21253 0.16802 -0.06476 0.00097  0.02736  106 ASN D OD1   
4785 N ND2   . ASN D 107 ? 0.12010 0.20052 0.14861 -0.07900 0.00314  0.03710  106 ASN D ND2   
4786 N N     . THR D 108 ? 0.09713 0.15327 0.10394 -0.04268 0.00725  0.02253  107 THR D N     
4787 C CA    . THR D 108 ? 0.10105 0.15812 0.10188 -0.03757 0.00936  0.01969  107 THR D CA    
4788 C C     . THR D 108 ? 0.14730 0.19744 0.15150 -0.02853 0.00733  0.01406  107 THR D C     
4789 O O     . THR D 108 ? 0.15086 0.19391 0.14955 -0.02523 0.00575  0.01301  107 THR D O     
4790 C CB    . THR D 108 ? 0.12029 0.16744 0.10932 -0.04174 0.00676  0.02559  107 THR D CB    
4791 O OG1   . THR D 108 ? 0.12409 0.15354 0.11281 -0.04078 0.00065  0.02826  107 THR D OG1   
4792 C CG2   . THR D 108 ? 0.12003 0.17479 0.10424 -0.05190 0.00917  0.03239  107 THR D CG2   
4793 N N     . ASN D 109 ? 0.09943 0.15205 0.11264 -0.02515 0.00681  0.01108  108 ASN D N     
4794 C CA    . ASN D 109 ? 0.09455 0.14120 0.11051 -0.01769 0.00510  0.00694  108 ASN D CA    
4795 C C     . ASN D 109 ? 0.13374 0.18660 0.15042 -0.01252 0.00817  0.00191  108 ASN D C     
4796 O O     . ASN D 109 ? 0.16302 0.22877 0.18330 -0.01211 0.01241  -0.00051 108 ASN D O     
4797 C CB    . ASN D 109 ? 0.07051 0.11839 0.09412 -0.01608 0.00318  0.00609  108 ASN D CB    
4798 C CG    . ASN D 109 ? 0.10747 0.14780 0.12885 -0.02123 0.00001  0.00920  108 ASN D CG    
4799 O OD1   . ASN D 109 ? 0.11609 0.14385 0.13306 -0.02014 -0.00237 0.00943  108 ASN D OD1   
4800 N ND2   . ASN D 109 ? 0.09933 0.14753 0.12438 -0.02696 -0.00003 0.01113  108 ASN D ND2   
4801 N N     . GLY D 110 ? 0.09569 0.13952 0.10940 -0.00867 0.00610  -0.00014 109 GLY D N     
4802 C CA    . GLY D 110 ? 0.11427 0.16000 0.12780 -0.00405 0.00781  -0.00581 109 GLY D CA    
4803 C C     . GLY D 110 ? 0.10537 0.14269 0.12350 0.00076  0.00472  -0.00768 109 GLY D C     
4804 O O     . GLY D 110 ? 0.09443 0.13347 0.12034 0.00393  0.00435  -0.00830 109 GLY D O     
4805 N N     . SER D 111 ? 0.11422 0.14312 0.12790 0.00068  0.00199  -0.00770 110 SER D N     
4806 C CA    . SER D 111 ? 0.09858 0.11982 0.11641 0.00331  -0.00095 -0.00792 110 SER D CA    
4807 C C     . SER D 111 ? 0.06977 0.08525 0.08626 0.00126  -0.00375 -0.00390 110 SER D C     
4808 O O     . SER D 111 ? 0.07312 0.08474 0.09376 0.00244  -0.00515 -0.00282 110 SER D O     
4809 C CB    . SER D 111 ? 0.09737 0.11491 0.11443 0.00577  -0.00168 -0.01324 110 SER D CB    
4810 O OG    . SER D 111 ? 0.09471 0.11205 0.10340 0.00307  -0.00233 -0.01469 110 SER D OG    
4811 N N     . GLN D 112 ? 0.07217 0.08744 0.08363 -0.00155 -0.00457 -0.00129 111 GLN D N     
4812 C CA    . GLN D 112 ? 0.07936 0.08999 0.09226 -0.00181 -0.00724 0.00202  111 GLN D CA    
4813 C C     . GLN D 112 ? 0.09438 0.10308 0.11065 -0.00124 -0.00629 0.00381  111 GLN D C     
4814 O O     . GLN D 112 ? 0.10731 0.11756 0.12262 -0.00261 -0.00486 0.00417  111 GLN D O     
4815 C CB    . GLN D 112 ? 0.09899 0.10874 0.10643 -0.00420 -0.00954 0.00519  111 GLN D CB    
4816 C CG    . GLN D 112 ? 0.10707 0.11853 0.10883 -0.00554 -0.01165 0.00352  111 GLN D CG    
4817 C CD    . GLN D 112 ? 0.09591 0.10582 0.09335 -0.00766 -0.01598 0.00858  111 GLN D CD    
4818 O OE1   . GLN D 112 ? 0.10657 0.11319 0.10960 -0.00609 -0.01835 0.01226  111 GLN D OE1   
4819 N NE2   . GLN D 112 ? 0.13017 0.14266 0.11748 -0.01092 -0.01707 0.00882  111 GLN D NE2   
4820 N N     . PHE D 113 ? 0.07078 0.07705 0.09089 0.00031  -0.00703 0.00461  112 PHE D N     
4821 C CA    . PHE D 113 ? 0.08338 0.08797 0.10507 0.00111  -0.00557 0.00488  112 PHE D CA    
4822 C C     . PHE D 113 ? 0.10128 0.10416 0.12630 0.00294  -0.00600 0.00586  112 PHE D C     
4823 O O     . PHE D 113 ? 0.11881 0.12310 0.14665 0.00345  -0.00812 0.00700  112 PHE D O     
4824 C CB    . PHE D 113 ? 0.07102 0.07733 0.09481 0.00176  -0.00454 0.00415  112 PHE D CB    
4825 C CG    . PHE D 113 ? 0.06906 0.07594 0.09687 0.00219  -0.00529 0.00457  112 PHE D CG    
4826 C CD1   . PHE D 113 ? 0.07179 0.07821 0.10013 0.00193  -0.00697 0.00320  112 PHE D CD1   
4827 C CD2   . PHE D 113 ? 0.09008 0.09833 0.12133 0.00250  -0.00418 0.00584  112 PHE D CD2   
4828 C CE1   . PHE D 113 ? 0.09691 0.10250 0.12894 0.00101  -0.00862 0.00352  112 PHE D CE1   
4829 C CE2   . PHE D 113 ? 0.10326 0.11346 0.13950 0.00145  -0.00510 0.00698  112 PHE D CE2   
4830 C CZ    . PHE D 113 ? 0.11322 0.12121 0.14974 0.00021  -0.00791 0.00604  112 PHE D CZ    
4831 N N     . PHE D 114 ? 0.08484 0.08564 0.11000 0.00415  -0.00407 0.00492  113 PHE D N     
4832 C CA    . PHE D 114 ? 0.08630 0.08765 0.11666 0.00728  -0.00306 0.00466  113 PHE D CA    
4833 C C     . PHE D 114 ? 0.08888 0.09174 0.11828 0.00803  0.00087  0.00237  113 PHE D C     
4834 O O     . PHE D 114 ? 0.09375 0.09414 0.11684 0.00621  0.00161  0.00099  113 PHE D O     
4835 C CB    . PHE D 114 ? 0.09652 0.09166 0.12742 0.00935  -0.00496 0.00523  113 PHE D CB    
4836 C CG    . PHE D 114 ? 0.10538 0.09233 0.13003 0.00801  -0.00462 0.00353  113 PHE D CG    
4837 C CD1   . PHE D 114 ? 0.09308 0.07837 0.11206 0.00346  -0.00608 0.00490  113 PHE D CD1   
4838 C CD2   . PHE D 114 ? 0.08497 0.06627 0.10992 0.01112  -0.00282 0.00009  113 PHE D CD2   
4839 C CE1   . PHE D 114 ? 0.08459 0.06275 0.09881 0.00078  -0.00658 0.00381  113 PHE D CE1   
4840 C CE2   . PHE D 114 ? 0.11237 0.08416 0.13100 0.00899  -0.00348 -0.00209 113 PHE D CE2   
4841 C CZ    . PHE D 114 ? 0.10826 0.07860 0.12178 0.00317  -0.00579 0.00028  113 PHE D CZ    
4842 N N     . ILE D 115 ? 0.08532 0.09394 0.12100 0.01013  0.00329  0.00230  114 ILE D N     
4843 C CA    . ILE D 115 ? 0.09849 0.11066 0.13274 0.01084  0.00820  0.00011  114 ILE D CA    
4844 C C     . ILE D 115 ? 0.10659 0.11742 0.14460 0.01603  0.01068  -0.00354 114 ILE D C     
4845 O O     . ILE D 115 ? 0.11431 0.12991 0.16269 0.01947  0.01031  -0.00253 114 ILE D O     
4846 C CB    . ILE D 115 ? 0.09368 0.11521 0.13324 0.00889  0.01017  0.00295  114 ILE D CB    
4847 C CG1   . ILE D 115 ? 0.07900 0.09883 0.11627 0.00479  0.00670  0.00622  114 ILE D CG1   
4848 C CG2   . ILE D 115 ? 0.10330 0.12999 0.13935 0.00859  0.01600  0.00141  114 ILE D CG2   
4849 C CD1   . ILE D 115 ? 0.08478 0.11067 0.12872 0.00188  0.00658  0.00975  114 ILE D CD1   
4850 N N     . CYS D 116 ? 0.09031 0.09474 0.12060 0.01687  0.01281  -0.00812 115 CYS D N     
4851 C CA    . CYS D 116 ? 0.11899 0.11954 0.15235 0.02278  0.01537  -0.01320 115 CYS D CA    
4852 C C     . CYS D 116 ? 0.15840 0.17110 0.19846 0.02635  0.02207  -0.01553 115 CYS D C     
4853 O O     . CYS D 116 ? 0.16179 0.18223 0.19681 0.02287  0.02615  -0.01526 115 CYS D O     
4854 C CB    . CYS D 116 ? 0.13838 0.12775 0.16011 0.02185  0.01584  -0.01882 115 CYS D CB    
4855 S SG    . CYS D 116 ? 0.15082 0.12804 0.16644 0.01673  0.00872  -0.01597 115 CYS D SG    
4856 N N     . THR D 117 ? 0.16551 0.18067 0.21746 0.03330  0.02318  -0.01733 116 THR D N     
4857 C CA    . THR D 117 ? 0.15501 0.18314 0.21510 0.03806  0.03084  -0.02108 116 THR D CA    
4858 C C     . THR D 117 ? 0.22773 0.24786 0.28551 0.04529  0.03497  -0.03033 116 THR D C     
4859 O O     . THR D 117 ? 0.17068 0.20125 0.23710 0.05160  0.04197  -0.03515 116 THR D O     
4860 C CB    . THR D 117 ? 0.17968 0.22047 0.25865 0.04146  0.02941  -0.01663 116 THR D CB    
4861 O OG1   . THR D 117 ? 0.15347 0.18467 0.23941 0.04702  0.02316  -0.01593 116 THR D OG1   
4862 C CG2   . THR D 117 ? 0.13548 0.18299 0.21571 0.03373  0.02537  -0.00888 116 THR D CG2   
4863 N N     . ALA D 118 ? 0.19434 0.19638 0.24089 0.04422  0.03097  -0.03335 117 ALA D N     
4864 C CA    . ALA D 118 ? 0.18661 0.17563 0.22931 0.05028  0.03304  -0.04271 117 ALA D CA    
4865 C C     . ALA D 118 ? 0.17452 0.14591 0.20177 0.04377  0.02747  -0.04345 117 ALA D C     
4866 O O     . ALA D 118 ? 0.20238 0.17281 0.22645 0.03680  0.02184  -0.03608 117 ALA D O     
4867 C CB    . ALA D 118 ? 0.19517 0.17882 0.25373 0.05993  0.03025  -0.04309 117 ALA D CB    
4868 N N     . LYS D 119 ? 0.20605 0.16428 0.22424 0.04597  0.02922  -0.05291 118 LYS D N     
4869 C CA    . LYS D 119 ? 0.22971 0.16997 0.23574 0.03968  0.02285  -0.05380 118 LYS D CA    
4870 C C     . LYS D 119 ? 0.23328 0.16197 0.24745 0.03990  0.01481  -0.04684 118 LYS D C     
4871 O O     . LYS D 119 ? 0.25722 0.18132 0.28325 0.04805  0.01393  -0.04692 118 LYS D O     
4872 C CB    . LYS D 119 ? 0.24677 0.17314 0.24243 0.04252  0.02577  -0.06647 118 LYS D CB    
4873 C CG    . LYS D 119 ? 0.26543 0.17598 0.24588 0.03368  0.01985  -0.06876 118 LYS D CG    
4874 C CD    . LYS D 119 ? 0.31945 0.21221 0.29167 0.03793  0.02174  -0.08244 118 LYS D CD    
4875 C CE    . LYS D 119 ? 0.41063 0.28686 0.36753 0.02812  0.01516  -0.08575 118 LYS D CE    
4876 N NZ    . LYS D 119 ? 0.44034 0.29959 0.38754 0.03140  0.01785  -0.09795 118 LYS D NZ    
4877 N N     . THR D 120 ? 0.20946 0.13497 0.21779 0.03097  0.00894  -0.04015 119 THR D N     
4878 C CA    . THR D 120 ? 0.21421 0.12989 0.22719 0.02902  0.00167  -0.03260 119 THR D CA    
4879 C C     . THR D 120 ? 0.21118 0.11335 0.21318 0.02009  -0.00317 -0.03270 119 THR D C     
4880 O O     . THR D 120 ? 0.20128 0.10742 0.20141 0.01252  -0.00675 -0.02548 119 THR D O     
4881 C CB    . THR D 120 ? 0.18348 0.11295 0.20252 0.02626  -0.00036 -0.02267 119 THR D CB    
4882 O OG1   . THR D 120 ? 0.16309 0.10175 0.17467 0.01858  0.00023  -0.02066 119 THR D OG1   
4883 C CG2   . THR D 120 ? 0.15892 0.10274 0.19000 0.03342  0.00323  -0.02170 119 THR D CG2   
4884 N N     . GLU D 121 ? 0.20204 0.08868 0.19723 0.02088  -0.00313 -0.04151 120 GLU D N     
4885 C CA    . GLU D 121 ? 0.24530 0.12092 0.22945 0.01107  -0.00759 -0.04298 120 GLU D CA    
4886 C C     . GLU D 121 ? 0.24070 0.10379 0.22721 0.00520  -0.01491 -0.03488 120 GLU D C     
4887 O O     . GLU D 121 ? 0.25734 0.11712 0.23738 -0.00503 -0.01881 -0.03294 120 GLU D O     
4888 C CB    . GLU D 121 ? 0.25110 0.11164 0.22613 0.01316  -0.00605 -0.05579 120 GLU D CB    
4889 C CG    . GLU D 121 ? 0.33733 0.17538 0.31694 0.01948  -0.00850 -0.05963 120 GLU D CG    
4890 C CD    . GLU D 121 ? 0.42364 0.26791 0.41558 0.03267  -0.00288 -0.06061 120 GLU D CD    
4891 O OE1   . GLU D 121 ? 0.34787 0.21080 0.34490 0.03774  0.00243  -0.06135 120 GLU D OE1   
4892 O OE2   . GLU D 121 ? 0.45422 0.28599 0.45136 0.03741  -0.00373 -0.05978 120 GLU D OE2   
4893 N N     . TRP D 122 ? 0.29655 0.15350 0.29227 0.01079  -0.01721 -0.02940 121 TRP D N     
4894 C CA    . TRP D 122 ? 0.25866 0.10609 0.25511 0.00392  -0.02399 -0.01953 121 TRP D CA    
4895 C C     . TRP D 122 ? 0.22341 0.08922 0.21898 -0.00427 -0.02405 -0.01076 121 TRP D C     
4896 O O     . TRP D 122 ? 0.22383 0.08539 0.21775 -0.01242 -0.02843 -0.00291 121 TRP D O     
4897 C CB    . TRP D 122 ? 0.24789 0.08879 0.25359 0.01171  -0.02631 -0.01403 121 TRP D CB    
4898 C CG    . TRP D 122 ? 0.27571 0.13343 0.29040 0.01864  -0.02419 -0.01044 121 TRP D CG    
4899 C CD1   . TRP D 122 ? 0.21395 0.08448 0.23045 0.01482  -0.02604 -0.00046 121 TRP D CD1   
4900 C CD2   . TRP D 122 ? 0.23738 0.10492 0.26002 0.02949  -0.01866 -0.01690 121 TRP D CD2   
4901 N NE1   . TRP D 122 ? 0.20330 0.08935 0.22825 0.02219  -0.02302 -0.00038 121 TRP D NE1   
4902 C CE2   . TRP D 122 ? 0.23776 0.12320 0.26763 0.03104  -0.01840 -0.00973 121 TRP D CE2   
4903 C CE3   . TRP D 122 ? 0.25284 0.11720 0.27670 0.03749  -0.01329 -0.02817 121 TRP D CE3   
4904 C CZ2   . TRP D 122 ? 0.23727 0.13750 0.27724 0.03956  -0.01370 -0.01271 121 TRP D CZ2   
4905 C CZ3   . TRP D 122 ? 0.25664 0.13688 0.29050 0.04662  -0.00761 -0.03123 121 TRP D CZ3   
4906 C CH2   . TRP D 122 ? 0.26931 0.16747 0.31198 0.04723  -0.00814 -0.02305 121 TRP D CH2   
4907 N N     . LEU D 123 ? 0.18009 0.06590 0.17670 -0.00245 -0.01909 -0.01201 122 LEU D N     
4908 C CA    . LEU D 123 ? 0.16984 0.07221 0.16600 -0.00895 -0.01872 -0.00567 122 LEU D CA    
4909 C C     . LEU D 123 ? 0.18960 0.09695 0.17966 -0.01690 -0.01873 -0.00836 122 LEU D C     
4910 O O     . LEU D 123 ? 0.17697 0.09786 0.16802 -0.02217 -0.01862 -0.00355 122 LEU D O     
4911 C CB    . LEU D 123 ? 0.16030 0.07977 0.16165 -0.00308 -0.01457 -0.00494 122 LEU D CB    
4912 C CG    . LEU D 123 ? 0.14519 0.06325 0.15421 0.00446  -0.01529 -0.00199 122 LEU D CG    
4913 C CD1   . LEU D 123 ? 0.12845 0.06363 0.14239 0.00811  -0.01173 -0.00153 122 LEU D CD1   
4914 C CD2   . LEU D 123 ? 0.16356 0.07607 0.17256 0.00046  -0.02045 0.00681  122 LEU D CD2   
4915 N N     . ASP D 124 ? 0.19973 0.09730 0.18377 -0.01756 -0.01903 -0.01633 123 ASP D N     
4916 C CA    . ASP D 124 ? 0.21669 0.11887 0.19482 -0.02592 -0.02072 -0.01849 123 ASP D CA    
4917 C C     . ASP D 124 ? 0.23276 0.13451 0.21239 -0.03622 -0.02520 -0.01142 123 ASP D C     
4918 O O     . ASP D 124 ? 0.20469 0.09175 0.18479 -0.03891 -0.02849 -0.00808 123 ASP D O     
4919 C CB    . ASP D 124 ? 0.21948 0.10726 0.18870 -0.02614 -0.02163 -0.02870 123 ASP D CB    
4920 C CG    . ASP D 124 ? 0.25726 0.15025 0.22334 -0.01758 -0.01587 -0.03603 123 ASP D CG    
4921 O OD1   . ASP D 124 ? 0.18689 0.09516 0.15846 -0.01273 -0.01188 -0.03227 123 ASP D OD1   
4922 O OD2   . ASP D 124 ? 0.27829 0.16003 0.23591 -0.01628 -0.01520 -0.04575 123 ASP D OD2   
4923 N N     . GLY D 125 ? 0.21769 0.13621 0.19880 -0.04211 -0.02538 -0.00864 124 GLY D N     
4924 C CA    . GLY D 125 ? 0.17948 0.10241 0.16360 -0.05232 -0.02843 -0.00211 124 GLY D CA    
4925 C C     . GLY D 125 ? 0.19335 0.12497 0.18300 -0.05215 -0.02636 0.00634  124 GLY D C     
4926 O O     . GLY D 125 ? 0.18005 0.11891 0.17241 -0.06084 -0.02747 0.01226  124 GLY D O     
4927 N N     . LYS D 126 ? 0.16716 0.09935 0.15826 -0.04322 -0.02337 0.00706  125 LYS D N     
4928 C CA    . LYS D 126 ? 0.14530 0.08546 0.13927 -0.04298 -0.02180 0.01423  125 LYS D CA    
4929 C C     . LYS D 126 ? 0.15293 0.10956 0.15038 -0.03636 -0.01754 0.01331  125 LYS D C     
4930 O O     . LYS D 126 ? 0.14026 0.10794 0.13933 -0.03766 -0.01570 0.01771  125 LYS D O     
4931 C CB    . LYS D 126 ? 0.21379 0.13770 0.20630 -0.03948 -0.02414 0.01746  125 LYS D CB    
4932 C CG    . LYS D 126 ? 0.26770 0.17135 0.25699 -0.04569 -0.02923 0.01940  125 LYS D CG    
4933 C CD    . LYS D 126 ? 0.40605 0.31507 0.39439 -0.05811 -0.03070 0.02748  125 LYS D CD    
4934 C CE    . LYS D 126 ? 0.32543 0.21619 0.31104 -0.06217 -0.03520 0.03129  125 LYS D CE    
4935 N NZ    . LYS D 126 ? 0.39936 0.27646 0.38487 -0.05353 -0.03722 0.03328  125 LYS D NZ    
4936 N N     . HIS D 127 ? 0.12077 0.07852 0.11857 -0.02978 -0.01589 0.00760  126 HIS D N     
4937 C CA    . HIS D 127 ? 0.12865 0.09906 0.12977 -0.02401 -0.01264 0.00680  126 HIS D CA    
4938 C C     . HIS D 127 ? 0.11603 0.09364 0.11712 -0.02403 -0.01213 0.00303  126 HIS D C     
4939 O O     . HIS D 127 ? 0.17275 0.14274 0.16946 -0.02438 -0.01326 -0.00119 126 HIS D O     
4940 C CB    . HIS D 127 ? 0.11647 0.08149 0.11864 -0.01634 -0.01155 0.00546  126 HIS D CB    
4941 C CG    . HIS D 127 ? 0.13585 0.09651 0.13873 -0.01576 -0.01318 0.01038  126 HIS D CG    
4942 N ND1   . HIS D 127 ? 0.12274 0.09241 0.12724 -0.01416 -0.01230 0.01320  126 HIS D ND1   
4943 C CD2   . HIS D 127 ? 0.13436 0.08176 0.13571 -0.01695 -0.01648 0.01337  126 HIS D CD2   
4944 C CE1   . HIS D 127 ? 0.13623 0.09996 0.13932 -0.01481 -0.01509 0.01807  126 HIS D CE1   
4945 N NE2   . HIS D 127 ? 0.12083 0.07080 0.12257 -0.01629 -0.01782 0.01892  126 HIS D NE2   
4946 N N     . VAL D 128 ? 0.10422 0.09583 0.10959 -0.02352 -0.01082 0.00435  127 VAL D N     
4947 C CA    . VAL D 128 ? 0.11122 0.10997 0.11720 -0.02361 -0.01173 0.00245  127 VAL D CA    
4948 C C     . VAL D 128 ? 0.13163 0.12873 0.13557 -0.01765 -0.01007 0.00024  127 VAL D C     
4949 O O     . VAL D 128 ? 0.10309 0.10404 0.11054 -0.01330 -0.00807 0.00144  127 VAL D O     
4950 C CB    . VAL D 128 ? 0.13159 0.14562 0.14491 -0.02453 -0.01154 0.00487  127 VAL D CB    
4951 C CG1   . VAL D 128 ? 0.10550 0.12625 0.12036 -0.02297 -0.01361 0.00411  127 VAL D CG1   
4952 C CG2   . VAL D 128 ? 0.09741 0.11605 0.11327 -0.03200 -0.01280 0.00715  127 VAL D CG2   
4953 N N     . VAL D 129 ? 0.11935 0.11098 0.11691 -0.01828 -0.01087 -0.00314 128 VAL D N     
4954 C CA    . VAL D 129 ? 0.10773 0.10013 0.10205 -0.01434 -0.00885 -0.00470 128 VAL D CA    
4955 C C     . VAL D 129 ? 0.10918 0.11158 0.10499 -0.01503 -0.01091 -0.00191 128 VAL D C     
4956 O O     . VAL D 129 ? 0.10934 0.11604 0.10500 -0.01916 -0.01464 -0.00129 128 VAL D O     
4957 C CB    . VAL D 129 ? 0.12105 0.10450 0.10610 -0.01502 -0.00827 -0.01020 128 VAL D CB    
4958 C CG1   . VAL D 129 ? 0.10715 0.09437 0.08717 -0.01244 -0.00547 -0.01132 128 VAL D CG1   
4959 C CG2   . VAL D 129 ? 0.13178 0.10397 0.11759 -0.01244 -0.00661 -0.01293 128 VAL D CG2   
4960 N N     . PHE D 130 ? 0.08259 0.08850 0.08067 -0.01125 -0.00922 0.00026  129 PHE D N     
4961 C CA    . PHE D 130 ? 0.13187 0.14518 0.13253 -0.01103 -0.01205 0.00393  129 PHE D CA    
4962 C C     . PHE D 130 ? 0.14407 0.15714 0.14153 -0.00915 -0.01083 0.00618  129 PHE D C     
4963 O O     . PHE D 130 ? 0.12698 0.14400 0.12709 -0.00845 -0.01379 0.01038  129 PHE D O     
4964 C CB    . PHE D 130 ? 0.10985 0.12890 0.12100 -0.00876 -0.01248 0.00598  129 PHE D CB    
4965 C CG    . PHE D 130 ? 0.09652 0.11282 0.11112 -0.00508 -0.00936 0.00594  129 PHE D CG    
4966 C CD1   . PHE D 130 ? 0.09720 0.11004 0.11193 -0.00513 -0.00712 0.00419  129 PHE D CD1   
4967 C CD2   . PHE D 130 ? 0.11718 0.13361 0.13460 -0.00225 -0.00963 0.00816  129 PHE D CD2   
4968 C CE1   . PHE D 130 ? 0.10018 0.11135 0.11759 -0.00246 -0.00542 0.00424  129 PHE D CE1   
4969 C CE2   . PHE D 130 ? 0.13978 0.15337 0.16015 -0.00005 -0.00763 0.00770  129 PHE D CE2   
4970 C CZ    . PHE D 130 ? 0.09188 0.10367 0.11215 -0.00018 -0.00564 0.00552  129 PHE D CZ    
4971 N N     . GLY D 131 ? 0.11998 0.12911 0.11289 -0.00831 -0.00668 0.00409  130 GLY D N     
4972 C CA    . GLY D 131 ? 0.11354 0.12441 0.10396 -0.00791 -0.00492 0.00721  130 GLY D CA    
4973 C C     . GLY D 131 ? 0.16136 0.17083 0.14687 -0.00734 0.00065  0.00357  130 GLY D C     
4974 O O     . GLY D 131 ? 0.13305 0.13840 0.11726 -0.00627 0.00254  -0.00177 130 GLY D O     
4975 N N     . LYS D 132 ? 0.13959 0.15270 0.12300 -0.00806 0.00332  0.00678  131 LYS D N     
4976 C CA    . LYS D 132 ? 0.11840 0.13398 0.09915 -0.00715 0.00987  0.00357  131 LYS D CA    
4977 C C     . LYS D 132 ? 0.13306 0.15433 0.11787 -0.00851 0.01216  0.00948  131 LYS D C     
4978 O O     . LYS D 132 ? 0.10959 0.13103 0.09288 -0.01142 0.00856  0.01603  131 LYS D O     
4979 C CB    . LYS D 132 ? 0.12435 0.14003 0.09064 -0.00927 0.01210  -0.00087 131 LYS D CB    
4980 C CG    . LYS D 132 ? 0.25998 0.28070 0.21596 -0.01397 0.01141  0.00489  131 LYS D CG    
4981 C CD    . LYS D 132 ? 0.31062 0.33126 0.24903 -0.01727 0.01184  0.00055  131 LYS D CD    
4982 C CE    . LYS D 132 ? 0.27162 0.29690 0.19949 -0.02271 0.00863  0.00889  131 LYS D CE    
4983 N NZ    . LYS D 132 ? 0.39374 0.41949 0.30213 -0.02701 0.00758  0.00526  131 LYS D NZ    
4984 N N     . VAL D 133 ? 0.09895 0.12479 0.09010 -0.00651 0.01764  0.00754  132 VAL D N     
4985 C CA    . VAL D 133 ? 0.09985 0.13288 0.09540 -0.00920 0.02054  0.01304  132 VAL D CA    
4986 C C     . VAL D 133 ? 0.16132 0.19895 0.14389 -0.01392 0.02324  0.01621  132 VAL D C     
4987 O O     . VAL D 133 ? 0.15137 0.19084 0.12312 -0.01357 0.02716  0.01081  132 VAL D O     
4988 C CB    . VAL D 133 ? 0.09664 0.13695 0.10281 -0.00605 0.02616  0.00987  132 VAL D CB    
4989 C CG1   . VAL D 133 ? 0.13640 0.18707 0.14657 -0.01038 0.03020  0.01557  132 VAL D CG1   
4990 C CG2   . VAL D 133 ? 0.10459 0.14085 0.12271 -0.00281 0.02196  0.00917  132 VAL D CG2   
4991 N N     . LYS D 134 ? 0.13852 0.17693 0.12106 -0.01872 0.02073  0.02500  133 LYS D N     
4992 C CA    . LYS D 134 ? 0.15797 0.20073 0.12765 -0.02460 0.02235  0.03083  133 LYS D CA    
4993 C C     . LYS D 134 ? 0.15967 0.21352 0.13386 -0.02823 0.02969  0.03431  133 LYS D C     
4994 O O     . LYS D 134 ? 0.22925 0.29319 0.19751 -0.02849 0.03806  0.03021  133 LYS D O     
4995 C CB    . LYS D 134 ? 0.16829 0.20334 0.13549 -0.02776 0.01358  0.03987  133 LYS D CB    
4996 C CG    . LYS D 134 ? 0.25212 0.29035 0.20524 -0.03458 0.01344  0.04827  133 LYS D CG    
4997 C CD    . LYS D 134 ? 0.26683 0.29583 0.21945 -0.03631 0.00321  0.05781  133 LYS D CD    
4998 C CE    . LYS D 134 ? 0.30562 0.33732 0.24344 -0.04404 0.00229  0.06837  133 LYS D CE    
4999 N NZ    . LYS D 134 ? 0.27812 0.29972 0.21729 -0.04532 -0.00843 0.07931  133 LYS D NZ    
5000 N N     . GLU D 135 ? 0.16837 0.22105 0.15362 -0.03116 0.02689  0.04128  134 GLU D N     
5001 C CA    . GLU D 135 ? 0.17750 0.24218 0.17092 -0.03525 0.03332  0.04461  134 GLU D CA    
5002 C C     . GLU D 135 ? 0.11993 0.18634 0.13143 -0.03095 0.03307  0.04018  134 GLU D C     
5003 O O     . GLU D 135 ? 0.10871 0.16451 0.12552 -0.02704 0.02644  0.03771  134 GLU D O     
5004 C CB    . GLU D 135 ? 0.22122 0.28387 0.21341 -0.04416 0.03004  0.05708  134 GLU D CB    
5005 C CG    . GLU D 135 ? 0.32827 0.39282 0.30197 -0.05001 0.03121  0.06360  134 GLU D CG    
5006 C CD    . GLU D 135 ? 0.54115 0.59786 0.51410 -0.05726 0.02507  0.07567  134 GLU D CD    
5007 O OE1   . GLU D 135 ? 0.62266 0.67183 0.60897 -0.05821 0.02004  0.07884  134 GLU D OE1   
5008 O OE2   . GLU D 135 ? 0.63180 0.68794 0.59101 -0.06100 0.02443  0.08035  134 GLU D OE2   
5009 N N     . GLY D 136 ? 0.15827 0.23977 0.17907 -0.03180 0.04049  0.03927  135 GLY D N     
5010 C CA    . GLY D 136 ? 0.11404 0.19994 0.15301 -0.02915 0.03947  0.03704  135 GLY D CA    
5011 C C     . GLY D 136 ? 0.15875 0.24761 0.20364 -0.01979 0.04210  0.02728  135 GLY D C     
5012 O O     . GLY D 136 ? 0.13471 0.22253 0.19224 -0.01666 0.03803  0.02560  135 GLY D O     
5013 N N     . MET D 137 ? 0.12763 0.21889 0.16306 -0.01539 0.04811  0.02080  136 MET D N     
5014 C CA    . MET D 137 ? 0.13308 0.22531 0.17533 -0.00621 0.05033  0.01177  136 MET D CA    
5015 C C     . MET D 137 ? 0.11647 0.22521 0.17844 -0.00390 0.05456  0.01163  136 MET D C     
5016 O O     . MET D 137 ? 0.10573 0.21311 0.17936 0.00264  0.05154  0.00803  136 MET D O     
5017 C CB    . MET D 137 ? 0.18709 0.27855 0.21551 -0.00245 0.05658  0.00394  136 MET D CB    
5018 C CG    . MET D 137 ? 0.23500 0.31915 0.26718 0.00706  0.05609  -0.00547 136 MET D CG    
5019 S SD    . MET D 137 ? 0.17444 0.23847 0.20439 0.00830  0.04451  -0.00498 136 MET D SD    
5020 C CE    . MET D 137 ? 0.22193 0.28422 0.26600 0.01824  0.04442  -0.01143 136 MET D CE    
5021 N N     . ASN D 138 ? 0.10558 0.23097 0.17225 -0.00972 0.06101  0.01644  137 ASN D N     
5022 C CA    . ASN D 138 ? 0.12475 0.26876 0.21307 -0.00829 0.06446  0.01712  137 ASN D CA    
5023 C C     . ASN D 138 ? 0.10971 0.24856 0.21104 -0.01017 0.05419  0.02152  137 ASN D C     
5024 O O     . ASN D 138 ? 0.08404 0.23338 0.20352 -0.00587 0.05332  0.02012  137 ASN D O     
5025 C CB    . ASN D 138 ? 0.13689 0.29386 0.22528 -0.01618 0.07123  0.02144  137 ASN D CB    
5026 C CG    . ASN D 138 ? 0.17382 0.32405 0.25680 -0.02786 0.06528  0.03204  137 ASN D CG    
5027 O OD1   . ASN D 138 ? 0.17274 0.30942 0.24259 -0.03083 0.06017  0.03581  137 ASN D OD1   
5028 N ND2   . ASN D 138 ? 0.21420 0.37302 0.30793 -0.03434 0.06547  0.03676  137 ASN D ND2   
5029 N N     . ILE D 139 ? 0.08710 0.20982 0.17926 -0.01602 0.04601  0.02631  138 ILE D N     
5030 C CA    . ILE D 139 ? 0.08392 0.20004 0.18526 -0.01785 0.03639  0.02882  138 ILE D CA    
5031 C C     . ILE D 139 ? 0.09164 0.19769 0.19314 -0.00898 0.03145  0.02260  138 ILE D C     
5032 O O     . ILE D 139 ? 0.07809 0.18683 0.19154 -0.00733 0.02614  0.02264  138 ILE D O     
5033 C CB    . ILE D 139 ? 0.12313 0.22445 0.21485 -0.02584 0.02988  0.03466  138 ILE D CB    
5034 C CG1   . ILE D 139 ? 0.09159 0.20133 0.18272 -0.03568 0.03401  0.04262  138 ILE D CG1   
5035 C CG2   . ILE D 139 ? 0.10254 0.19601 0.20176 -0.02756 0.02034  0.03533  138 ILE D CG2   
5036 C CD1   . ILE D 139 ? 0.11590 0.24213 0.22291 -0.04024 0.03608  0.04498  138 ILE D CD1   
5037 N N     . VAL D 140 ? 0.07386 0.16846 0.16170 -0.00404 0.03260  0.01779  139 VAL D N     
5038 C CA    . VAL D 140 ? 0.09059 0.17573 0.17807 0.00349  0.02862  0.01268  139 VAL D CA    
5039 C C     . VAL D 140 ? 0.12372 0.22081 0.22614 0.01075  0.03177  0.00939  139 VAL D C     
5040 O O     . VAL D 140 ? 0.08357 0.17901 0.19476 0.01450  0.02587  0.00936  139 VAL D O     
5041 C CB    . VAL D 140 ? 0.08501 0.15708 0.15576 0.00591  0.02973  0.00845  139 VAL D CB    
5042 C CG1   . VAL D 140 ? 0.10284 0.16554 0.17366 0.01290  0.02651  0.00365  139 VAL D CG1   
5043 C CG2   . VAL D 140 ? 0.07508 0.13610 0.13478 0.00019  0.02481  0.01215  139 VAL D CG2   
5044 N N     . GLU D 141 ? 0.11674 0.22709 0.22262 0.01290  0.04109  0.00684  140 GLU D N     
5045 C CA    . GLU D 141 ? 0.10425 0.22796 0.22698 0.02119  0.04501  0.00310  140 GLU D CA    
5046 C C     . GLU D 141 ? 0.13865 0.27694 0.28175 0.01897  0.04061  0.00863  140 GLU D C     
5047 O O     . GLU D 141 ? 0.12245 0.26244 0.27622 0.02549  0.03604  0.00671  140 GLU D O     
5048 C CB    . GLU D 141 ? 0.11076 0.24791 0.23248 0.02347  0.05731  -0.00151 140 GLU D CB    
5049 C CG    . GLU D 141 ? 0.09762 0.21964 0.19824 0.02588  0.06062  -0.00829 140 GLU D CG    
5050 C CD    . GLU D 141 ? 0.22428 0.35863 0.31723 0.02473  0.07252  -0.01204 140 GLU D CD    
5051 O OE1   . GLU D 141 ? 0.20524 0.35683 0.30690 0.01992  0.07786  -0.00809 140 GLU D OE1   
5052 O OE2   . GLU D 141 ? 0.24009 0.36412 0.31658 0.02736  0.07570  -0.01915 140 GLU D OE2   
5053 N N     . ALA D 142 ? 0.07078 0.21555 0.21490 0.00861  0.03957  0.01489  141 ALA D N     
5054 C CA    . ALA D 142 ? 0.06957 0.22245 0.22675 0.00427  0.03284  0.01844  141 ALA D CA    
5055 C C     . ALA D 142 ? 0.08504 0.22552 0.24234 0.00509  0.02147  0.02009  141 ALA D C     
5056 O O     . ALA D 142 ? 0.07117 0.21681 0.23858 0.00701  0.01540  0.02037  141 ALA D O     
5057 C CB    . ALA D 142 ? 0.07300 0.23063 0.22865 -0.00783 0.03368  0.02427  141 ALA D CB    
5058 N N     . MET D 143 ? 0.08037 0.20286 0.22279 0.00326  0.01801  0.02028  142 MET D N     
5059 C CA    . MET D 143 ? 0.12422 0.23338 0.26206 0.00403  0.00813  0.02025  142 MET D CA    
5060 C C     . MET D 143 ? 0.14171 0.25033 0.28527 0.01380  0.00620  0.01758  142 MET D C     
5061 O O     . MET D 143 ? 0.11549 0.22549 0.26629 0.01477  -0.00183 0.01974  142 MET D O     
5062 C CB    . MET D 143 ? 0.15995 0.24936 0.27771 0.00175  0.00650  0.01881  142 MET D CB    
5063 C CG    . MET D 143 ? 0.08058 0.16631 0.19195 -0.00678 0.00672  0.02183  142 MET D CG    
5064 S SD    . MET D 143 ? 0.15266 0.21818 0.24357 -0.00674 0.00575  0.01971  142 MET D SD    
5065 C CE    . MET D 143 ? 0.08354 0.13930 0.17110 -0.00319 -0.00185 0.01698  142 MET D CE    
5066 N N     . GLU D 144 ? 0.14574 0.25132 0.28537 0.02082  0.01290  0.01300  143 GLU D N     
5067 C CA    . GLU D 144 ? 0.18889 0.28921 0.33230 0.03044  0.01099  0.01020  143 GLU D CA    
5068 C C     . GLU D 144 ? 0.10399 0.21709 0.26326 0.03442  0.00733  0.01162  143 GLU D C     
5069 O O     . GLU D 144 ? 0.16659 0.27257 0.32680 0.03959  0.00076  0.01231  143 GLU D O     
5070 C CB    . GLU D 144 ? 0.15227 0.24826 0.28914 0.03636  0.01984  0.00367  143 GLU D CB    
5071 C CG    . GLU D 144 ? 0.13692 0.22163 0.27448 0.04599  0.01811  -0.00025 143 GLU D CG    
5072 C CD    . GLU D 144 ? 0.19841 0.27957 0.32935 0.05106  0.02740  -0.00827 143 GLU D CD    
5073 O OE1   . GLU D 144 ? 0.18102 0.27488 0.31168 0.04850  0.03590  -0.01018 143 GLU D OE1   
5074 O OE2   . GLU D 144 ? 0.21949 0.28482 0.34438 0.05670  0.02603  -0.01257 143 GLU D OE2   
5075 N N     . ARG D 145 ? 0.15290 0.28392 0.32243 0.03104  0.01078  0.01249  144 ARG D N     
5076 C CA    . ARG D 145 ? 0.11654 0.26113 0.30071 0.03436  0.00720  0.01333  144 ARG D CA    
5077 C C     . ARG D 145 ? 0.18397 0.32648 0.36959 0.02932  -0.00431 0.01860  144 ARG D C     
5078 O O     . ARG D 145 ? 0.12374 0.27591 0.32070 0.03236  -0.00904 0.01994  144 ARG D O     
5079 C CB    . ARG D 145 ? 0.18849 0.35432 0.38387 0.03118  0.01460  0.01236  144 ARG D CB    
5080 C CG    . ARG D 145 ? 0.20668 0.37942 0.40329 0.03854  0.02575  0.00567  144 ARG D CG    
5081 C CD    . ARG D 145 ? 0.28947 0.47537 0.48623 0.03048  0.03507  0.00541  144 ARG D CD    
5082 N NE    . ARG D 145 ? 0.37523 0.56348 0.56644 0.03586  0.04619  -0.00174 144 ARG D NE    
5083 C CZ    . ARG D 145 ? 0.32282 0.51353 0.50520 0.02902  0.05509  -0.00224 144 ARG D CZ    
5084 N NH1   . ARG D 145 ? 0.26148 0.45194 0.43950 0.01710  0.05384  0.00510  144 ARG D NH1   
5085 N NH2   . ARG D 145 ? 0.26253 0.45400 0.43870 0.03404  0.06504  -0.01005 144 ARG D NH2   
5086 N N     . PHE D 146 ? 0.12297 0.25376 0.29718 0.02193  -0.00902 0.02113  145 PHE D N     
5087 C CA    . PHE D 146 ? 0.10732 0.23490 0.27964 0.01694  -0.01975 0.02479  145 PHE D CA    
5088 C C     . PHE D 146 ? 0.10246 0.21554 0.26571 0.02143  -0.02650 0.02570  145 PHE D C     
5089 O O     . PHE D 146 ? 0.11741 0.22796 0.27713 0.01779  -0.03548 0.02861  145 PHE D O     
5090 C CB    . PHE D 146 ? 0.06704 0.18982 0.23137 0.00616  -0.02174 0.02614  145 PHE D CB    
5091 C CG    . PHE D 146 ? 0.10166 0.23746 0.27451 -0.00079 -0.01806 0.02722  145 PHE D CG    
5092 C CD1   . PHE D 146 ? 0.10931 0.25738 0.29312 -0.00417 -0.02286 0.02909  145 PHE D CD1   
5093 C CD2   . PHE D 146 ? 0.12781 0.26356 0.29731 -0.00453 -0.01009 0.02696  145 PHE D CD2   
5094 C CE1   . PHE D 146 ? 0.15443 0.31419 0.34629 -0.01150 -0.01958 0.03046  145 PHE D CE1   
5095 C CE2   . PHE D 146 ? 0.09729 0.24397 0.27335 -0.01189 -0.00682 0.02897  145 PHE D CE2   
5096 C CZ    . PHE D 146 ? 0.13521 0.29366 0.32272 -0.01554 -0.01146 0.03059  145 PHE D CZ    
5097 N N     . GLY D 147 ? 0.13163 0.23471 0.28989 0.02848  -0.02248 0.02333  146 GLY D N     
5098 C CA    . GLY D 147 ? 0.09369 0.18205 0.24286 0.03190  -0.02852 0.02497  146 GLY D CA    
5099 C C     . GLY D 147 ? 0.10044 0.19120 0.25821 0.03994  -0.03177 0.02630  146 GLY D C     
5100 O O     . GLY D 147 ? 0.12408 0.22997 0.29599 0.04275  -0.03079 0.02608  146 GLY D O     
5101 N N     . SER D 148 ? 0.17684 0.25239 0.32617 0.04356  -0.03584 0.02802  147 SER D N     
5102 C CA    . SER D 148 ? 0.11089 0.18486 0.26667 0.05125  -0.04014 0.03029  147 SER D CA    
5103 C C     . SER D 148 ? 0.17549 0.22887 0.31993 0.05458  -0.04110 0.03072  147 SER D C     
5104 O O     . SER D 148 ? 0.11404 0.15635 0.24634 0.05058  -0.03870 0.02927  147 SER D O     
5105 C CB    . SER D 148 ? 0.14048 0.22056 0.29832 0.04777  -0.05032 0.03636  147 SER D CB    
5106 O OG    . SER D 148 ? 0.13853 0.20708 0.27985 0.04056  -0.05630 0.03993  147 SER D OG    
5107 N N     . ARG D 149 ? 0.13449 0.18275 0.28337 0.06153  -0.04531 0.03328  148 ARG D N     
5108 C CA    . ARG D 149 ? 0.22766 0.25530 0.36711 0.06464  -0.04647 0.03404  148 ARG D CA    
5109 C C     . ARG D 149 ? 0.15034 0.16530 0.27255 0.05591  -0.05162 0.03891  148 ARG D C     
5110 O O     . ARG D 149 ? 0.21462 0.21345 0.32663 0.05513  -0.04993 0.03801  148 ARG D O     
5111 C CB    . ARG D 149 ? 0.18369 0.20821 0.33117 0.07262  -0.05194 0.03771  148 ARG D CB    
5112 C CG    . ARG D 149 ? 0.32835 0.35093 0.48534 0.08352  -0.04530 0.03138  148 ARG D CG    
5113 C CD    . ARG D 149 ? 0.30870 0.32990 0.47553 0.09188  -0.05159 0.03573  148 ARG D CD    
5114 N NE    . ARG D 149 ? 0.26797 0.27556 0.42435 0.08697  -0.06155 0.04457  148 ARG D NE    
5115 C CZ    . ARG D 149 ? 0.27486 0.26072 0.42191 0.08781  -0.06368 0.04659  148 ARG D CZ    
5116 N NH1   . ARG D 149 ? 0.27203 0.24549 0.41851 0.09354  -0.05709 0.03982  148 ARG D NH1   
5117 N NH2   . ARG D 149 ? 0.22601 0.20237 0.36359 0.08224  -0.07268 0.05558  148 ARG D NH2   
5118 N N     . ASN D 150 ? 0.14097 0.16281 0.25903 0.04910  -0.05815 0.04404  149 ASN D N     
5119 C CA    . ASN D 150 ? 0.15584 0.16758 0.25632 0.04087  -0.06264 0.04858  149 ASN D CA    
5120 C C     . ASN D 150 ? 0.16636 0.18318 0.25951 0.03352  -0.05953 0.04561  149 ASN D C     
5121 O O     . ASN D 150 ? 0.12959 0.14286 0.20855 0.02626  -0.06339 0.04883  149 ASN D O     
5122 C CB    . ASN D 150 ? 0.15575 0.16893 0.25222 0.03799  -0.07242 0.05624  149 ASN D CB    
5123 C CG    . ASN D 150 ? 0.20832 0.23836 0.31050 0.03461  -0.07593 0.05639  149 ASN D CG    
5124 O OD1   . ASN D 150 ? 0.20062 0.24138 0.31026 0.03387  -0.07103 0.05121  149 ASN D OD1   
5125 N ND2   . ASN D 150 ? 0.23105 0.26308 0.32897 0.03169  -0.08474 0.06255  149 ASN D ND2   
5126 N N     . GLY D 151 ? 0.11500 0.14040 0.21709 0.03523  -0.05247 0.03958  150 GLY D N     
5127 C CA    . GLY D 151 ? 0.16764 0.19687 0.26439 0.02910  -0.04939 0.03672  150 GLY D CA    
5128 C C     . GLY D 151 ? 0.14451 0.18682 0.24403 0.02349  -0.05280 0.03706  150 GLY D C     
5129 O O     . GLY D 151 ? 0.12549 0.17199 0.22400 0.01928  -0.04895 0.03343  150 GLY D O     
5130 N N     . LYS D 152 ? 0.11263 0.16029 0.21456 0.02274  -0.05988 0.04094  151 LYS D N     
5131 C CA    . LYS D 152 ? 0.17169 0.22991 0.27454 0.01626  -0.06394 0.04067  151 LYS D CA    
5132 C C     . LYS D 152 ? 0.15007 0.22123 0.26840 0.01687  -0.05835 0.03700  151 LYS D C     
5133 O O     . LYS D 152 ? 0.14085 0.21818 0.27258 0.02364  -0.05401 0.03619  151 LYS D O     
5134 C CB    . LYS D 152 ? 0.18455 0.24660 0.28778 0.01566  -0.07289 0.04564  151 LYS D CB    
5135 C CG    . LYS D 152 ? 0.22600 0.27698 0.31088 0.01225  -0.07896 0.05013  151 LYS D CG    
5136 C CD    . LYS D 152 ? 0.31176 0.35946 0.37960 0.00379  -0.07927 0.04722  151 LYS D CD    
5137 C CE    . LYS D 152 ? 0.36446 0.40371 0.41223 -0.00055 -0.08412 0.05137  151 LYS D CE    
5138 N NZ    . LYS D 152 ? 0.29956 0.33665 0.32988 -0.00804 -0.08313 0.04688  151 LYS D NZ    
5139 N N     . THR D 153 ? 0.11499 0.19003 0.23069 0.00941  -0.05839 0.03464  152 THR D N     
5140 C CA    . THR D 153 ? 0.11700 0.20317 0.24514 0.00766  -0.05305 0.03216  152 THR D CA    
5141 C C     . THR D 153 ? 0.12700 0.22459 0.26277 0.00313  -0.05899 0.03374  152 THR D C     
5142 O O     . THR D 153 ? 0.10341 0.19796 0.23007 -0.00184 -0.06710 0.03490  152 THR D O     
5143 C CB    . THR D 153 ? 0.08738 0.16848 0.20856 0.00201  -0.04893 0.02884  152 THR D CB    
5144 O OG1   . THR D 153 ? 0.13604 0.21113 0.24473 -0.00542 -0.05569 0.02788  152 THR D OG1   
5145 C CG2   . THR D 153 ? 0.08094 0.15054 0.19300 0.00643  -0.04250 0.02676  152 THR D CG2   
5146 N N     . SER D 154 ? 0.13837 0.24985 0.29040 0.00468  -0.05473 0.03351  153 SER D N     
5147 C CA    . SER D 154 ? 0.11957 0.24456 0.28250 0.00126  -0.05997 0.03532  153 SER D CA    
5148 C C     . SER D 154 ? 0.10353 0.23059 0.26508 -0.00931 -0.06084 0.03384  153 SER D C     
5149 O O     . SER D 154 ? 0.14235 0.27762 0.30937 -0.01438 -0.06704 0.03505  153 SER D O     
5150 C CB    . SER D 154 ? 0.11422 0.25493 0.29639 0.00842  -0.05489 0.03561  153 SER D CB    
5151 O OG    . SER D 154 ? 0.13524 0.27852 0.32093 0.00965  -0.04416 0.03263  153 SER D OG    
5152 N N     . LYS D 155 ? 0.12142 0.24030 0.27582 -0.01274 -0.05524 0.03136  154 LYS D N     
5153 C CA    . LYS D 155 ? 0.09042 0.20455 0.23933 -0.02267 -0.05677 0.02964  154 LYS D CA    
5154 C C     . LYS D 155 ? 0.08657 0.18394 0.21950 -0.02364 -0.05552 0.02671  154 LYS D C     
5155 O O     . LYS D 155 ? 0.08068 0.17300 0.20939 -0.01721 -0.05201 0.02653  154 LYS D O     
5156 C CB    . LYS D 155 ? 0.08838 0.21307 0.24963 -0.02632 -0.05013 0.03051  154 LYS D CB    
5157 C CG    . LYS D 155 ? 0.11547 0.25879 0.29358 -0.02637 -0.05204 0.03284  154 LYS D CG    
5158 C CD    . LYS D 155 ? 0.22333 0.37816 0.41280 -0.03215 -0.04610 0.03401  154 LYS D CD    
5159 C CE    . LYS D 155 ? 0.27299 0.44821 0.48063 -0.03230 -0.04869 0.03595  154 LYS D CE    
5160 N NZ    . LYS D 155 ? 0.32715 0.51832 0.54876 -0.03493 -0.04023 0.03707  154 LYS D NZ    
5161 N N     . LYS D 156 ? 0.13391 0.22209 0.25800 -0.03156 -0.05894 0.02393  155 LYS D N     
5162 C CA    . LYS D 156 ? 0.10167 0.17418 0.21128 -0.03264 -0.05838 0.02007  155 LYS D CA    
5163 C C     . LYS D 156 ? 0.12444 0.19501 0.23808 -0.03219 -0.05007 0.02061  155 LYS D C     
5164 O O     . LYS D 156 ? 0.08591 0.15845 0.20529 -0.03757 -0.04794 0.02187  155 LYS D O     
5165 C CB    . LYS D 156 ? 0.16511 0.22717 0.26376 -0.04048 -0.06491 0.01550  155 LYS D CB    
5166 C CG    . LYS D 156 ? 0.31174 0.35789 0.39328 -0.04054 -0.06602 0.00967  155 LYS D CG    
5167 C CD    . LYS D 156 ? 0.38618 0.43190 0.45610 -0.03662 -0.06924 0.00918  155 LYS D CD    
5168 C CE    . LYS D 156 ? 0.36659 0.39771 0.41557 -0.03796 -0.06975 0.00151  155 LYS D CE    
5169 N NZ    . LYS D 156 ? 0.22230 0.24211 0.26715 -0.03551 -0.06187 -0.00260 155 LYS D NZ    
5170 N N     . ILE D 157 ? 0.08416 0.14815 0.18979 -0.02532 -0.04383 0.01937  156 ILE D N     
5171 C CA    . ILE D 157 ? 0.07176 0.13289 0.17683 -0.02367 -0.03503 0.01968  156 ILE D CA    
5172 C C     . ILE D 157 ? 0.11008 0.15384 0.19909 -0.02416 -0.03430 0.01546  156 ILE D C     
5173 O O     . ILE D 157 ? 0.11739 0.15423 0.19552 -0.01979 -0.03405 0.01264  156 ILE D O     
5174 C CB    . ILE D 157 ? 0.09550 0.16207 0.20340 -0.01540 -0.02845 0.02064  156 ILE D CB    
5175 C CG1   . ILE D 157 ? 0.06300 0.14621 0.18764 -0.01236 -0.03013 0.02373  156 ILE D CG1   
5176 C CG2   . ILE D 157 ? 0.07977 0.14590 0.18677 -0.01495 -0.01986 0.02111  156 ILE D CG2   
5177 C CD1   . ILE D 157 ? 0.11413 0.21201 0.25369 -0.01724 -0.02845 0.02660  156 ILE D CD1   
5178 N N     . THR D 158 ? 0.09396 0.13078 0.18217 -0.02940 -0.03417 0.01533  157 THR D N     
5179 C CA    . THR D 158 ? 0.09330 0.11380 0.16858 -0.02881 -0.03460 0.01072  157 THR D CA    
5180 C C     . THR D 158 ? 0.09588 0.11057 0.17019 -0.02854 -0.02954 0.01298  157 THR D C     
5181 O O     . THR D 158 ? 0.09291 0.11488 0.17508 -0.03139 -0.02639 0.01824  157 THR D O     
5182 C CB    . THR D 158 ? 0.10853 0.12000 0.18046 -0.03478 -0.04194 0.00667  157 THR D CB    
5183 O OG1   . THR D 158 ? 0.13697 0.15050 0.21920 -0.04257 -0.04433 0.01052  157 THR D OG1   
5184 C CG2   . THR D 158 ? 0.19721 0.21400 0.26659 -0.03545 -0.04792 0.00434  157 THR D CG2   
5185 N N     . ILE D 159 ? 0.12778 0.13068 0.19214 -0.02483 -0.02865 0.00921  158 ILE D N     
5186 C CA    . ILE D 159 ? 0.09003 0.08493 0.15248 -0.02443 -0.02617 0.01132  158 ILE D CA    
5187 C C     . ILE D 159 ? 0.15182 0.13412 0.21502 -0.02967 -0.03164 0.01007  158 ILE D C     
5188 O O     . ILE D 159 ? 0.16098 0.13160 0.21800 -0.02743 -0.03447 0.00371  158 ILE D O     
5189 C CB    . ILE D 159 ? 0.10909 0.09933 0.16338 -0.01756 -0.02329 0.00814  158 ILE D CB    
5190 C CG1   . ILE D 159 ? 0.09590 0.09636 0.14902 -0.01358 -0.01918 0.00871  158 ILE D CG1   
5191 C CG2   . ILE D 159 ? 0.09176 0.07448 0.14504 -0.01687 -0.02219 0.01128  158 ILE D CG2   
5192 C CD1   . ILE D 159 ? 0.07334 0.07046 0.11880 -0.00832 -0.01734 0.00510  158 ILE D CD1   
5193 N N     . ALA D 160 ? 0.11505 0.09985 0.18618 -0.03703 -0.03298 0.01586  159 ALA D N     
5194 C CA    . ALA D 160 ? 0.13636 0.10787 0.20913 -0.04371 -0.03918 0.01531  159 ALA D CA    
5195 C C     . ALA D 160 ? 0.20989 0.16410 0.27797 -0.04125 -0.03988 0.01557  159 ALA D C     
5196 O O     . ALA D 160 ? 0.14829 0.08581 0.21435 -0.04261 -0.04530 0.01099  159 ALA D O     
5197 C CB    . ALA D 160 ? 0.13143 0.11194 0.21507 -0.05342 -0.04008 0.02289  159 ALA D CB    
5198 N N     . ASP D 161 ? 0.13630 0.09386 0.20277 -0.03751 -0.03505 0.02068  160 ASP D N     
5199 C CA    . ASP D 161 ? 0.14213 0.08557 0.20511 -0.03396 -0.03625 0.02218  160 ASP D CA    
5200 C C     . ASP D 161 ? 0.15433 0.10685 0.21322 -0.02738 -0.03075 0.02399  160 ASP D C     
5201 O O     . ASP D 161 ? 0.13877 0.10628 0.19785 -0.02772 -0.02587 0.02617  160 ASP D O     
5202 C CB    . ASP D 161 ? 0.14965 0.08441 0.21622 -0.04188 -0.03930 0.03128  160 ASP D CB    
5203 C CG    . ASP D 161 ? 0.22729 0.14496 0.28998 -0.03689 -0.04258 0.03120  160 ASP D CG    
5204 O OD1   . ASP D 161 ? 0.20705 0.11673 0.26782 -0.02874 -0.04379 0.02333  160 ASP D OD1   
5205 O OD2   . ASP D 161 ? 0.21232 0.12568 0.27439 -0.04089 -0.04384 0.03891  160 ASP D OD2   
5206 N N     . CYS D 162 ? 0.15862 0.10197 0.21451 -0.02110 -0.03192 0.02248  161 CYS D N     
5207 C CA    . CYS D 162 ? 0.12158 0.07300 0.17386 -0.01598 -0.02808 0.02455  161 CYS D CA    
5208 C C     . CYS D 162 ? 0.15672 0.09625 0.20916 -0.01115 -0.03177 0.02602  161 CYS D C     
5209 O O     . CYS D 162 ? 0.14076 0.06601 0.19602 -0.00930 -0.03623 0.02245  161 CYS D O     
5210 C CB    . CYS D 162 ? 0.10537 0.06692 0.15493 -0.01071 -0.02429 0.01744  161 CYS D CB    
5211 S SG    . CYS D 162 ? 0.16112 0.11593 0.20969 -0.00589 -0.02624 0.00650  161 CYS D SG    
5212 N N     . GLY D 163 ? 0.14131 0.08656 0.19098 -0.00902 -0.03041 0.03110  162 GLY D N     
5213 C CA    . GLY D 163 ? 0.20378 0.14015 0.25502 -0.00408 -0.03480 0.03407  162 GLY D CA    
5214 C C     . GLY D 163 ? 0.14590 0.09151 0.19235 -0.00413 -0.03371 0.04081  162 GLY D C     
5215 O O     . GLY D 163 ? 0.12972 0.08812 0.17119 -0.00644 -0.02869 0.04044  162 GLY D O     
5216 N N     . GLN D 164 ? 0.15348 0.09176 0.20131 -0.00139 -0.03911 0.04680  163 GLN D N     
5217 C CA    . GLN D 164 ? 0.15674 0.10293 0.19908 -0.00163 -0.03997 0.05357  163 GLN D CA    
5218 C C     . GLN D 164 ? 0.20661 0.14731 0.24340 -0.00900 -0.04307 0.06565  163 GLN D C     
5219 O O     . GLN D 164 ? 0.22474 0.15429 0.26429 -0.01020 -0.04635 0.06728  163 GLN D O     
5220 C CB    . GLN D 164 ? 0.16410 0.10977 0.21263 0.00727  -0.04451 0.05209  163 GLN D CB    
5221 C CG    . GLN D 164 ? 0.15171 0.10918 0.19452 0.00687  -0.04537 0.05666  163 GLN D CG    
5222 C CD    . GLN D 164 ? 0.19293 0.15423 0.24452 0.01548  -0.04955 0.05450  163 GLN D CD    
5223 O OE1   . GLN D 164 ? 0.18509 0.14397 0.24621 0.02236  -0.04876 0.04674  163 GLN D OE1   
5224 N NE2   . GLN D 164 ? 0.21996 0.18945 0.26717 0.01443  -0.05277 0.05994  163 GLN D NE2   
5225 N N     . LEU D 165 ? 0.15583 0.10722 0.18270 -0.01400 -0.04037 0.07118  164 LEU D N     
5226 C CA    . LEU D 165 ? 0.19965 0.15082 0.21813 -0.02165 -0.04114 0.08101  164 LEU D CA    
5227 C C     . LEU D 165 ? 0.28686 0.23812 0.30060 -0.01944 -0.04671 0.08635  164 LEU D C     
5228 O O     . LEU D 165 ? 0.35588 0.31545 0.36635 -0.01622 -0.04729 0.08483  164 LEU D O     
5229 C CB    . LEU D 165 ? 0.22871 0.19273 0.23783 -0.02916 -0.03361 0.08325  164 LEU D CB    
5230 C CG    . LEU D 165 ? 0.23072 0.19848 0.24538 -0.03270 -0.02735 0.07838  164 LEU D CG    
5231 C CD1   . LEU D 165 ? 0.22469 0.20832 0.23128 -0.03816 -0.01881 0.07871  164 LEU D CD1   
5232 C CD2   . LEU D 165 ? 0.30036 0.25716 0.32110 -0.03704 -0.03068 0.08208  164 LEU D CD2   
5233 P PG    . GNP E .   ? 0.10907 0.10212 0.12193 -0.02232 0.02076  0.02269  201 GNP B PG    
5234 O O1G   . GNP E .   ? 0.11597 0.10209 0.12346 -0.01681 0.01683  0.02169  201 GNP B O1G   
5235 O O2G   . GNP E .   ? 0.11800 0.12289 0.13209 -0.02015 0.02363  0.02169  201 GNP B O2G   
5236 O O3G   . GNP E .   ? 0.12256 0.10933 0.13243 -0.02713 0.02404  0.02902  201 GNP B O3G   
5237 N N3B   . GNP E .   ? 0.10555 0.10038 0.12726 -0.02671 0.01837  0.01793  201 GNP B N3B   
5238 P PB    . GNP E .   ? 0.09748 0.09561 0.12041 -0.02481 0.01486  0.01143  201 GNP B PB    
5239 O O1B   . GNP E .   ? 0.10113 0.11199 0.12730 -0.02384 0.01455  0.01134  201 GNP B O1B   
5240 O O2B   . GNP E .   ? 0.09754 0.08941 0.11621 -0.01896 0.01352  0.00958  201 GNP B O2B   
5241 O O3A   . GNP E .   ? 0.12535 0.11903 0.15111 -0.03140 0.01319  0.00740  201 GNP B O3A   
5242 P PA    . GNP E .   ? 0.11770 0.09735 0.14114 -0.03132 0.01274  0.00235  201 GNP B PA    
5243 O O1A   . GNP E .   ? 0.12216 0.10430 0.14294 -0.02744 0.01224  -0.00360 201 GNP B O1A   
5244 O O2A   . GNP E .   ? 0.16153 0.12852 0.18448 -0.02852 0.01372  0.00662  201 GNP B O2A   
5245 O "O5'" . GNP E .   ? 0.12281 0.10108 0.14814 -0.04045 0.01139  -0.00098 201 GNP B "O5'" 
5246 C "C5'" . GNP E .   ? 0.12794 0.10701 0.15833 -0.04709 0.01172  0.00381  201 GNP B "C5'" 
5247 C "C4'" . GNP E .   ? 0.17866 0.14978 0.20924 -0.05572 0.00963  -0.00159 201 GNP B "C4'" 
5248 O "O4'" . GNP E .   ? 0.17535 0.15620 0.20395 -0.05974 0.00580  -0.00657 201 GNP B "O4'" 
5249 C "C3'" . GNP E .   ? 0.18083 0.13272 0.20708 -0.05392 0.01082  -0.00771 201 GNP B "C3'" 
5250 O "O3'" . GNP E .   ? 0.25987 0.19954 0.28802 -0.06241 0.01024  -0.00897 201 GNP B "O3'" 
5251 C "C2'" . GNP E .   ? 0.18369 0.13861 0.20371 -0.05304 0.01002  -0.01679 201 GNP B "C2'" 
5252 O "O2'" . GNP E .   ? 0.27509 0.21454 0.29097 -0.05579 0.01130  -0.02623 201 GNP B "O2'" 
5253 C "C1'" . GNP E .   ? 0.17490 0.14466 0.19524 -0.06079 0.00570  -0.01585 201 GNP B "C1'" 
5254 N N9    . GNP E .   ? 0.16044 0.14009 0.17440 -0.05915 0.00398  -0.01908 201 GNP B N9    
5255 C C8    . GNP E .   ? 0.14671 0.13347 0.15989 -0.05103 0.00551  -0.01669 201 GNP B C8    
5256 N N7    . GNP E .   ? 0.12823 0.12192 0.13456 -0.05269 0.00341  -0.01948 201 GNP B N7    
5257 C C5    . GNP E .   ? 0.16241 0.15366 0.16312 -0.06244 -0.00008 -0.02435 201 GNP B C5    
5258 C C6    . GNP E .   ? 0.20264 0.19818 0.19184 -0.06964 -0.00431 -0.02844 201 GNP B C6    
5259 O O6    . GNP E .   ? 0.14809 0.15019 0.13028 -0.06837 -0.00513 -0.02778 201 GNP B O6    
5260 N N1    . GNP E .   ? 0.19634 0.18679 0.18131 -0.08001 -0.00813 -0.03316 201 GNP B N1    
5261 C C2    . GNP E .   ? 0.18546 0.16724 0.17773 -0.08343 -0.00760 -0.03389 201 GNP B C2    
5262 N N2    . GNP E .   ? 0.19178 0.16874 0.17840 -0.09495 -0.01220 -0.03932 201 GNP B N2    
5263 N N3    . GNP E .   ? 0.17486 0.15230 0.17813 -0.07691 -0.00326 -0.02909 201 GNP B N3    
5264 C C4    . GNP E .   ? 0.15043 0.13301 0.15652 -0.06660 0.00014  -0.02465 201 GNP B C4    
5332 P PG    . GNP H .   ? 0.10353 0.08586 0.11716 0.01066  -0.01976 0.01698  201 GNP A PG    
5333 O O1G   . GNP H .   ? 0.11104 0.08950 0.12496 0.00488  -0.01816 0.01741  201 GNP A O1G   
5334 O O2G   . GNP H .   ? 0.09921 0.09471 0.11580 0.00977  -0.02084 0.01371  201 GNP A O2G   
5335 O O3G   . GNP H .   ? 0.11469 0.09392 0.12399 0.01568  -0.02026 0.02306  201 GNP A O3G   
5336 N N3B   . GNP H .   ? 0.10549 0.08004 0.12024 0.01336  -0.01961 0.01349  201 GNP A N3B   
5337 P PB    . GNP H .   ? 0.11752 0.09003 0.13336 0.01004  -0.01933 0.00827  201 GNP A PB    
5338 O O1B   . GNP H .   ? 0.11497 0.09838 0.13421 0.01027  -0.01840 0.00620  201 GNP A O1B   
5339 O O2B   . GNP H .   ? 0.14649 0.11618 0.16349 0.00385  -0.01967 0.00816  201 GNP A O2B   
5340 O O3A   . GNP H .   ? 0.12163 0.08257 0.13333 0.01482  -0.01955 0.00571  201 GNP A O3A   
5341 P PA    . GNP H .   ? 0.13751 0.08230 0.14575 0.01277  -0.02147 0.00332  201 GNP A PA    
5342 O O1A   . GNP H .   ? 0.13931 0.08588 0.14824 0.00797  -0.02336 -0.00115 201 GNP A O1A   
5343 O O2A   . GNP H .   ? 0.14272 0.07995 0.15203 0.01052  -0.02138 0.00837  201 GNP A O2A   
5344 O "O5'" . GNP H .   ? 0.17022 0.10694 0.17270 0.02096  -0.02085 0.00061  201 GNP A "O5'" 
5345 C "C5'" . GNP H .   ? 0.14154 0.07847 0.14388 0.02813  -0.01904 0.00454  201 GNP A "C5'" 
5346 C "C4'" . GNP H .   ? 0.15600 0.07956 0.15153 0.03585  -0.01840 0.00082  201 GNP A "C4'" 
5347 O "O4'" . GNP H .   ? 0.17147 0.10070 0.16366 0.03893  -0.01692 -0.00393 201 GNP A "O4'" 
5348 C "C3'" . GNP H .   ? 0.17316 0.07540 0.16374 0.03288  -0.02118 -0.00298 201 GNP A "C3'" 
5349 O "O3'" . GNP H .   ? 0.19164 0.07895 0.17694 0.04143  -0.02004 -0.00323 201 GNP A "O3'" 
5350 C "C2'" . GNP H .   ? 0.17509 0.07684 0.16104 0.03057  -0.02338 -0.01081 201 GNP A "C2'" 
5351 O "O2'" . GNP H .   ? 0.25309 0.13512 0.23153 0.03112  -0.02669 -0.01797 201 GNP A "O2'" 
5352 C "C1'" . GNP H .   ? 0.20023 0.11438 0.18370 0.03888  -0.01935 -0.01094 201 GNP A "C1'" 
5353 N N9    . GNP H .   ? 0.16036 0.08309 0.14130 0.03698  -0.01957 -0.01427 201 GNP A N9    
5354 C C8    . GNP H .   ? 0.14554 0.07928 0.13225 0.02962  -0.02067 -0.01257 201 GNP A C8    
5355 N N7    . GNP H .   ? 0.14477 0.08324 0.12654 0.03112  -0.02028 -0.01526 201 GNP A N7    
5356 C C5    . GNP H .   ? 0.17444 0.10520 0.14561 0.04000  -0.01861 -0.01922 201 GNP A C5    
5357 C C6    . GNP H .   ? 0.17466 0.10603 0.13425 0.04668  -0.01683 -0.02280 201 GNP A C6    
5358 O O6    . GNP H .   ? 0.16519 0.10389 0.12231 0.04557  -0.01680 -0.02239 201 GNP A O6    
5359 N N1    . GNP H .   ? 0.19291 0.11458 0.14230 0.05632  -0.01459 -0.02662 201 GNP A N1    
5360 C C2    . GNP H .   ? 0.21248 0.12404 0.16335 0.05955  -0.01424 -0.02687 201 GNP A C2    
5361 N N2    . GNP H .   ? 0.22495 0.12687 0.16441 0.07052  -0.01145 -0.03123 201 GNP A N2    
5362 N N3    . GNP H .   ? 0.18726 0.09787 0.14906 0.05347  -0.01606 -0.02262 201 GNP A N3    
5363 C C4    . GNP H .   ? 0.18175 0.10257 0.15270 0.04380  -0.01810 -0.01909 201 GNP A C4    
# 
