data_9BFW
# 
_entry.id   9BFW 
# 
_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   9BFW         pdb_00009bfw 10.2210/pdb9bfw/pdb 
WWPDB D_1000283284 ?            ?                   
# 
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                        9BFW 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jyano@revmed.com 
_pdbx_contact_author.name_first         Jason 
_pdbx_contact_author.name_last          Yano 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9774-2611 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tomlinson, A.C.A.' 1 0000-0002-9663-773X 
'Knox, J.E.'        2 ?                   
'Yano, J.K.'        3 0000-0002-9774-2611 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                6041 
_citation.page_last                 6063 
_citation.title                     
;Discovery of Elironrasib (RMC-6291), a Potent and Orally Bioavailable, RAS(ON) G12C-Selective, Covalent Tricomplex Inhibitor for the Treatment of Patients with RAS G12C-Addicted Cancers.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02313 
_citation.pdbx_database_id_PubMed   39993169 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cregg, J.'         1  ? 
primary 'Pota, K.'          2  ? 
primary 'Tomlinson, A.C.A.' 3  ? 
primary 'Yano, J.'          4  ? 
primary 'Marquez, A.'       5  ? 
primary 'Liu, Y.'           6  ? 
primary 'Schulze, C.J.'     7  ? 
primary 'Seamon, K.J.'      8  ? 
primary 'Holderfield, M.'   9  ? 
primary 'Wei, X.'           10 ? 
primary 'Zhuang, Y.'        11 ? 
primary 'Yang, Y.C.'        12 ? 
primary 'Jiang, J.'         13 ? 
primary 'Huang, Y.'         14 ? 
primary 'Zhao, R.'          15 ? 
primary 'Ling, Y.'          16 ? 
primary 'Wang, Z.'          17 ? 
primary 'Flagella, M.'      18 ? 
primary 'Wang, Z.'          19 ? 
primary 'Singh, M.'         20 ? 
primary 'Knox, J.E.'        21 ? 
primary 'Nichols, R.'       22 ? 
primary 'Wildes, D.'        23 ? 
primary 'Smith, J.A.M.'     24 ? 
primary 'Koltun, E.S.'      25 ? 
primary 'Gill, A.L.'        26 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19382.811 1   3.6.5.2 ? ? ? 
2 polymer     man 'Peptidyl-prolyl cis-trans isomerase A' 18107.516 1   5.2.1.8 ? ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   1   ?       ? ? ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    1   ?       ? ? ? 
5 non-polymer syn '2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL' 209.240   1   ?       ? ? ? 
6 non-polymer syn 
;1-acetyl-N-[(2S)-1-{[(1M,8S,10R,14S,20S)-22-cyano-4-hydroxy-18,18-dimethyl-9,15-dioxo-16-oxa-10,20,28-triazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),2(29),3,5,21,23,26-heptaen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-N-methylazetidine-3-carboxamide (non-preferred name)
;
739.860   1   ?       ? ? ? 
7 water       nat water 18.015    549 ?       ? ? ? 
# 
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
;
A ? 
2 'polypeptide(L)' no no 
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSSFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
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 '2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL' BTB   
6 
;1-acetyl-N-[(2S)-1-{[(1M,8S,10R,14S,20S)-22-cyano-4-hydroxy-18,18-dimethyl-9,15-dioxo-16-oxa-10,20,28-triazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),2(29),3,5,21,23,26-heptaen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-N-methylazetidine-3-carboxamide (non-preferred name)
;
A1AOM 
7 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 
A1AOM non-polymer         . 
;1-acetyl-N-[(2S)-1-{[(1M,8S,10R,14S,20S)-22-cyano-4-hydroxy-18,18-dimethyl-9,15-dioxo-16-oxa-10,20,28-triazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),2(29),3,5,21,23,26-heptaen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-N-methylazetidine-3-carboxamide (non-preferred name)
;
?                 'C40 H49 N7 O7'     739.860 
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 
BTB   non-polymer         . '2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL' 'BIS-TRIS BUFFER' 'C8 H19 N O5' 
209.240 
CYS   'L-peptide linking' y CYSTEINE ?                 'C3 H7 N O2 S'      121.158 
GLN   'L-peptide linking' y GLUTAMINE ?                 'C5 H10 N2 O3'      146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'        147.129 
GLY   'peptide linking'   y GLYCINE ?                 'C2 H5 N O2'        75.067  
GNP   non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' ?                 'C10 H17 N6 O13 P3' 522.196 
HIS   'L-peptide linking' y HISTIDINE ?                 'C6 H10 N3 O2 1'    156.162 
HOH   non-polymer         . WATER ?                 'H2 O'              18.015  
ILE   'L-peptide linking' y ISOLEUCINE ?                 'C6 H13 N O2'       131.173 
LEU   'L-peptide linking' y LEUCINE ?                 'C6 H13 N O2'       131.173 
LYS   'L-peptide linking' y LYSINE ?                 'C6 H15 N2 O2 1'    147.195 
MET   'L-peptide linking' y METHIONINE ?                 'C5 H11 N O2 S'     149.211 
MG    non-polymer         . 'MAGNESIUM ION' ?                 'Mg 2'              24.305  
PHE   'L-peptide linking' y PHENYLALANINE ?                 'C9 H11 N O2'       165.189 
PRO   'L-peptide linking' y PROLINE ?                 'C5 H9 N O2'        115.130 
SER   'L-peptide linking' y SERINE ?                 'C3 H7 N O3'        105.093 
THR   'L-peptide linking' y THREONINE ?                 'C4 H9 N O3'        119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ?                 'C11 H12 N2 O2'     204.225 
TYR   'L-peptide linking' y TYROSINE ?                 'C9 H11 N O3'       181.189 
VAL   'L-peptide linking' y VALINE ?                 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   0   0   SER SER A . n 
A 1 2   MET 2   1   1   MET MET A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   GLU 4   3   3   GLU GLU A . n 
A 1 5   TYR 5   4   4   TYR TYR A . n 
A 1 6   LYS 6   5   5   LYS LYS A . n 
A 1 7   LEU 7   6   6   LEU LEU A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   VAL 9   8   8   VAL VAL A . n 
A 1 10  VAL 10  9   9   VAL VAL A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ALA 12  11  11  ALA ALA A . n 
A 1 13  CYS 13  12  12  CYS CYS A . n 
A 1 14  GLY 14  13  13  GLY GLY A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLY 16  15  15  GLY GLY A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  SER 18  17  17  SER SER A . n 
A 1 19  ALA 19  18  18  ALA ALA A . n 
A 1 20  LEU 20  19  19  LEU LEU A . n 
A 1 21  THR 21  20  20  THR THR A . n 
A 1 22  ILE 22  21  21  ILE ILE A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LEU 24  23  23  LEU LEU A . n 
A 1 25  ILE 25  24  24  ILE ILE A . n 
A 1 26  GLN 26  25  25  GLN GLN A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  HIS 28  27  27  HIS HIS A . n 
A 1 29  PHE 29  28  28  PHE PHE A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  ASP 31  30  30  ASP ASP A . n 
A 1 32  GLU 32  31  31  GLU GLU A . n 
A 1 33  TYR 33  32  32  TYR TYR A . n 
A 1 34  ASP 34  33  33  ASP ASP A . n 
A 1 35  PRO 35  34  34  PRO PRO A . n 
A 1 36  THR 36  35  35  THR THR A . n 
A 1 37  ILE 37  36  36  ILE ILE A . n 
A 1 38  GLU 38  37  37  GLU GLU A . n 
A 1 39  ASP 39  38  38  ASP ASP A . n 
A 1 40  SER 40  39  39  SER SER A . n 
A 1 41  TYR 41  40  40  TYR TYR A . n 
A 1 42  ARG 42  41  41  ARG ARG A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  GLN 44  43  43  GLN GLN A . n 
A 1 45  VAL 45  44  44  VAL VAL A . n 
A 1 46  VAL 46  45  45  VAL VAL A . n 
A 1 47  ILE 47  46  46  ILE ILE A . n 
A 1 48  ASP 48  47  47  ASP ASP A . n 
A 1 49  GLY 49  48  48  GLY GLY A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  THR 51  50  50  THR THR A . n 
A 1 52  SER 52  51  51  SER SER A . n 
A 1 53  LEU 53  52  52  LEU LEU A . n 
A 1 54  LEU 54  53  53  LEU LEU A . n 
A 1 55  ASP 55  54  54  ASP ASP A . n 
A 1 56  ILE 56  55  55  ILE ILE A . n 
A 1 57  LEU 57  56  56  LEU LEU A . n 
A 1 58  ASP 58  57  57  ASP ASP A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  ALA 60  59  59  ALA ALA A . n 
A 1 61  GLY 61  60  60  GLY GLY A . n 
A 1 62  GLN 62  61  61  GLN GLN A . n 
A 1 63  GLU 63  62  62  GLU GLU A . n 
A 1 64  GLU 64  63  63  GLU GLU A . n 
A 1 65  TYR 65  64  64  TYR TYR A . n 
A 1 66  SER 66  65  65  SER SER A . n 
A 1 67  ALA 67  66  66  ALA ALA A . n 
A 1 68  MET 68  67  67  MET MET A . n 
A 1 69  ARG 69  68  68  ARG ARG A . n 
A 1 70  ASP 70  69  69  ASP ASP A . n 
A 1 71  GLN 71  70  70  GLN GLN A . n 
A 1 72  TYR 72  71  71  TYR TYR A . n 
A 1 73  MET 73  72  72  MET MET A . n 
A 1 74  ARG 74  73  73  ARG ARG A . n 
A 1 75  THR 75  74  74  THR THR A . n 
A 1 76  GLY 76  75  75  GLY GLY A . n 
A 1 77  GLU 77  76  76  GLU GLU A . n 
A 1 78  GLY 78  77  77  GLY GLY A . n 
A 1 79  PHE 79  78  78  PHE PHE A . n 
A 1 80  LEU 80  79  79  LEU LEU A . n 
A 1 81  LEU 81  80  80  LEU LEU A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  PHE 83  82  82  PHE PHE A . n 
A 1 84  ALA 84  83  83  ALA ALA A . n 
A 1 85  ILE 85  84  84  ILE ILE A . n 
A 1 86  ASN 86  85  85  ASN ASN A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  THR 88  87  87  THR THR A . n 
A 1 89  LYS 89  88  88  LYS LYS A . n 
A 1 90  SER 90  89  89  SER SER A . n 
A 1 91  PHE 91  90  90  PHE PHE A . n 
A 1 92  GLU 92  91  91  GLU GLU A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  ILE 94  93  93  ILE ILE A . n 
A 1 95  HIS 95  94  94  HIS HIS A . n 
A 1 96  HIS 96  95  95  HIS HIS A . n 
A 1 97  TYR 97  96  96  TYR TYR A . n 
A 1 98  ARG 98  97  97  ARG ARG A . n 
A 1 99  GLU 99  98  98  GLU GLU A . n 
A 1 100 GLN 100 99  99  GLN GLN A . n 
A 1 101 ILE 101 100 100 ILE ILE A . n 
A 1 102 LYS 102 101 101 LYS LYS A . n 
A 1 103 ARG 103 102 102 ARG ARG A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 LYS 105 104 104 LYS LYS A . n 
A 1 106 ASP 106 105 105 ASP ASP A . n 
A 1 107 SER 107 106 106 SER SER A . n 
A 1 108 GLU 108 107 107 GLU GLU A . n 
A 1 109 ASP 109 108 108 ASP ASP A . n 
A 1 110 VAL 110 109 109 VAL VAL A . n 
A 1 111 PRO 111 110 110 PRO PRO A . n 
A 1 112 MET 112 111 111 MET MET A . n 
A 1 113 VAL 113 112 112 VAL VAL A . n 
A 1 114 LEU 114 113 113 LEU LEU A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 GLY 116 115 115 GLY GLY A . n 
A 1 117 ASN 117 116 116 ASN ASN A . n 
A 1 118 LYS 118 117 117 LYS LYS A . n 
A 1 119 SER 119 118 118 SER SER A . n 
A 1 120 ASP 120 119 119 ASP ASP A . n 
A 1 121 LEU 121 120 120 LEU LEU A . n 
A 1 122 PRO 122 121 121 PRO PRO A . n 
A 1 123 SER 123 122 122 SER SER A . n 
A 1 124 ARG 124 123 123 ARG ARG A . n 
A 1 125 THR 125 124 124 THR THR A . n 
A 1 126 VAL 126 125 125 VAL VAL A . n 
A 1 127 ASP 127 126 126 ASP ASP A . n 
A 1 128 THR 128 127 127 THR THR A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLN 130 129 129 GLN GLN A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 GLN 132 131 131 GLN GLN A . n 
A 1 133 ASP 133 132 132 ASP ASP A . n 
A 1 134 LEU 134 133 133 LEU LEU A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 ARG 136 135 135 ARG ARG A . n 
A 1 137 SER 137 136 136 SER SER A . n 
A 1 138 TYR 138 137 137 TYR TYR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ILE 140 139 139 ILE ILE A . n 
A 1 141 PRO 141 140 140 PRO PRO A . n 
A 1 142 PHE 142 141 141 PHE PHE A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 GLU 144 143 143 GLU GLU A . n 
A 1 145 THR 145 144 144 THR THR A . n 
A 1 146 SER 146 145 145 SER SER A . n 
A 1 147 ALA 147 146 146 ALA ALA A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 THR 149 148 148 THR THR A . n 
A 1 150 ARG 150 149 149 ARG ARG A . n 
A 1 151 GLN 151 150 150 GLN GLN A . n 
A 1 152 GLY 152 151 151 GLY GLY A . n 
A 1 153 VAL 153 152 152 VAL VAL A . n 
A 1 154 ASP 154 153 153 ASP ASP A . n 
A 1 155 ASP 155 154 154 ASP ASP A . n 
A 1 156 ALA 156 155 155 ALA ALA A . n 
A 1 157 PHE 157 156 156 PHE PHE A . n 
A 1 158 TYR 158 157 157 TYR TYR A . n 
A 1 159 THR 159 158 158 THR THR A . n 
A 1 160 LEU 160 159 159 LEU LEU A . n 
A 1 161 VAL 161 160 160 VAL VAL A . n 
A 1 162 ARG 162 161 161 ARG ARG A . n 
A 1 163 GLU 163 162 162 GLU GLU A . n 
A 1 164 ILE 164 163 163 ILE ILE A . n 
A 1 165 ARG 165 164 164 ARG ARG A . n 
A 1 166 LYS 166 165 165 LYS LYS A . n 
A 1 167 HIS 167 166 166 HIS HIS A . n 
A 1 168 LYS 168 167 167 LYS LYS A . n 
A 1 169 GLU 169 168 ?   ?   ?   A . n 
A 1 170 LYS 170 169 ?   ?   ?   A . n 
B 2 1   SER 1   0   0   SER SER D . n 
B 2 2   MET 2   1   1   MET MET D . n 
B 2 3   VAL 3   2   2   VAL VAL D . n 
B 2 4   ASN 4   3   3   ASN ASN D . n 
B 2 5   PRO 5   4   4   PRO PRO D . n 
B 2 6   THR 6   5   5   THR THR D . n 
B 2 7   VAL 7   6   6   VAL VAL D . n 
B 2 8   PHE 8   7   7   PHE PHE D . n 
B 2 9   PHE 9   8   8   PHE PHE D . n 
B 2 10  ASP 10  9   9   ASP ASP D . n 
B 2 11  ILE 11  10  10  ILE ILE D . n 
B 2 12  ALA 12  11  11  ALA ALA D . n 
B 2 13  VAL 13  12  12  VAL VAL D . n 
B 2 14  ASP 14  13  13  ASP ASP D . n 
B 2 15  GLY 15  14  14  GLY GLY D . n 
B 2 16  GLU 16  15  15  GLU GLU D . n 
B 2 17  PRO 17  16  16  PRO PRO D . n 
B 2 18  LEU 18  17  17  LEU LEU D . n 
B 2 19  GLY 19  18  18  GLY GLY D . n 
B 2 20  ARG 20  19  19  ARG ARG D . n 
B 2 21  VAL 21  20  20  VAL VAL D . n 
B 2 22  SER 22  21  21  SER SER D . n 
B 2 23  PHE 23  22  22  PHE PHE D . n 
B 2 24  GLU 24  23  23  GLU GLU D . n 
B 2 25  LEU 25  24  24  LEU LEU D . n 
B 2 26  PHE 26  25  25  PHE PHE D . n 
B 2 27  ALA 27  26  26  ALA ALA D . n 
B 2 28  ASP 28  27  27  ASP ASP D . n 
B 2 29  LYS 29  28  28  LYS LYS D . n 
B 2 30  VAL 30  29  29  VAL VAL D . n 
B 2 31  PRO 31  30  30  PRO PRO D . n 
B 2 32  LYS 32  31  31  LYS LYS D . n 
B 2 33  THR 33  32  32  THR THR D . n 
B 2 34  ALA 34  33  33  ALA ALA D . n 
B 2 35  GLU 35  34  34  GLU GLU D . n 
B 2 36  ASN 36  35  35  ASN ASN D . n 
B 2 37  PHE 37  36  36  PHE PHE D . n 
B 2 38  ARG 38  37  37  ARG ARG D . n 
B 2 39  ALA 39  38  38  ALA ALA D . n 
B 2 40  LEU 40  39  39  LEU LEU D . n 
B 2 41  SER 41  40  40  SER SER D . n 
B 2 42  THR 42  41  41  THR THR D . n 
B 2 43  GLY 43  42  42  GLY GLY D . n 
B 2 44  GLU 44  43  43  GLU GLU D . n 
B 2 45  LYS 45  44  44  LYS LYS D . n 
B 2 46  GLY 46  45  45  GLY GLY D . n 
B 2 47  PHE 47  46  46  PHE PHE D . n 
B 2 48  GLY 48  47  47  GLY GLY D . n 
B 2 49  TYR 49  48  48  TYR TYR D . n 
B 2 50  LYS 50  49  49  LYS LYS D . n 
B 2 51  GLY 51  50  50  GLY GLY D . n 
B 2 52  SER 52  51  51  SER SER D . n 
B 2 53  SER 53  52  52  SER SER D . n 
B 2 54  PHE 54  53  53  PHE PHE D . n 
B 2 55  HIS 55  54  54  HIS HIS D . n 
B 2 56  ARG 56  55  55  ARG ARG D . n 
B 2 57  ILE 57  56  56  ILE ILE D . n 
B 2 58  ILE 58  57  57  ILE ILE D . n 
B 2 59  PRO 59  58  58  PRO PRO D . n 
B 2 60  GLY 60  59  59  GLY GLY D . n 
B 2 61  PHE 61  60  60  PHE PHE D . n 
B 2 62  MET 62  61  61  MET MET D . n 
B 2 63  CYS 63  62  62  CYS CYS D . n 
B 2 64  GLN 64  63  63  GLN GLN D . n 
B 2 65  GLY 65  64  64  GLY GLY D . n 
B 2 66  GLY 66  65  65  GLY GLY D . n 
B 2 67  ASP 67  66  66  ASP ASP D . n 
B 2 68  PHE 68  67  67  PHE PHE D . n 
B 2 69  THR 69  68  68  THR THR D . n 
B 2 70  ARG 70  69  69  ARG ARG D . n 
B 2 71  HIS 71  70  70  HIS HIS D . n 
B 2 72  ASN 72  71  71  ASN ASN D . n 
B 2 73  GLY 73  72  72  GLY GLY D . n 
B 2 74  THR 74  73  73  THR THR D . n 
B 2 75  GLY 75  74  74  GLY GLY D . n 
B 2 76  GLY 76  75  75  GLY GLY D . n 
B 2 77  LYS 77  76  76  LYS LYS D . n 
B 2 78  SER 78  77  77  SER SER D . n 
B 2 79  ILE 79  78  78  ILE ILE D . n 
B 2 80  TYR 80  79  79  TYR TYR D . n 
B 2 81  GLY 81  80  80  GLY GLY D . n 
B 2 82  GLU 82  81  81  GLU GLU D . n 
B 2 83  LYS 83  82  82  LYS LYS D . n 
B 2 84  PHE 84  83  83  PHE PHE D . n 
B 2 85  GLU 85  84  84  GLU GLU D . n 
B 2 86  ASP 86  85  85  ASP ASP D . n 
B 2 87  GLU 87  86  86  GLU GLU D . n 
B 2 88  ASN 88  87  87  ASN ASN D . n 
B 2 89  PHE 89  88  88  PHE PHE D . n 
B 2 90  ILE 90  89  89  ILE ILE D . n 
B 2 91  LEU 91  90  90  LEU LEU D . n 
B 2 92  LYS 92  91  91  LYS LYS D . n 
B 2 93  HIS 93  92  92  HIS HIS D . n 
B 2 94  THR 94  93  93  THR THR D . n 
B 2 95  GLY 95  94  94  GLY GLY D . n 
B 2 96  PRO 96  95  95  PRO PRO D . n 
B 2 97  GLY 97  96  96  GLY GLY D . n 
B 2 98  ILE 98  97  97  ILE ILE D . n 
B 2 99  LEU 99  98  98  LEU LEU D . n 
B 2 100 SER 100 99  99  SER SER D . n 
B 2 101 MET 101 100 100 MET MET D . n 
B 2 102 ALA 102 101 101 ALA ALA D . n 
B 2 103 ASN 103 102 102 ASN ASN D . n 
B 2 104 ALA 104 103 103 ALA ALA D . n 
B 2 105 GLY 105 104 104 GLY GLY D . n 
B 2 106 PRO 106 105 105 PRO PRO D . n 
B 2 107 ASN 107 106 106 ASN ASN D . n 
B 2 108 THR 108 107 107 THR THR D . n 
B 2 109 ASN 109 108 108 ASN ASN D . n 
B 2 110 GLY 110 109 109 GLY GLY D . n 
B 2 111 SER 111 110 110 SER SER D . n 
B 2 112 GLN 112 111 111 GLN GLN D . n 
B 2 113 PHE 113 112 112 PHE PHE D . n 
B 2 114 PHE 114 113 113 PHE PHE D . n 
B 2 115 ILE 115 114 114 ILE ILE D . n 
B 2 116 CYS 116 115 115 CYS CYS D . n 
B 2 117 THR 117 116 116 THR THR D . n 
B 2 118 ALA 118 117 117 ALA ALA D . n 
B 2 119 LYS 119 118 118 LYS LYS D . n 
B 2 120 THR 120 119 119 THR THR D . n 
B 2 121 GLU 121 120 120 GLU GLU D . n 
B 2 122 TRP 122 121 121 TRP TRP D . n 
B 2 123 LEU 123 122 122 LEU LEU D . n 
B 2 124 ASP 124 123 123 ASP ASP D . n 
B 2 125 GLY 125 124 124 GLY GLY D . n 
B 2 126 LYS 126 125 125 LYS LYS D . n 
B 2 127 HIS 127 126 126 HIS HIS D . n 
B 2 128 VAL 128 127 127 VAL VAL D . n 
B 2 129 VAL 129 128 128 VAL VAL D . n 
B 2 130 PHE 130 129 129 PHE PHE D . n 
B 2 131 GLY 131 130 130 GLY GLY D . n 
B 2 132 LYS 132 131 131 LYS LYS D . n 
B 2 133 VAL 133 132 132 VAL VAL D . n 
B 2 134 LYS 134 133 133 LYS LYS D . n 
B 2 135 GLU 135 134 134 GLU GLU D . n 
B 2 136 GLY 136 135 135 GLY GLY D . n 
B 2 137 MET 137 136 136 MET MET D . n 
B 2 138 ASN 138 137 137 ASN ASN D . n 
B 2 139 ILE 139 138 138 ILE ILE D . n 
B 2 140 VAL 140 139 139 VAL VAL D . n 
B 2 141 GLU 141 140 140 GLU GLU D . n 
B 2 142 ALA 142 141 141 ALA ALA D . n 
B 2 143 MET 143 142 142 MET MET D . n 
B 2 144 GLU 144 143 143 GLU GLU D . n 
B 2 145 ARG 145 144 144 ARG ARG D . n 
B 2 146 PHE 146 145 145 PHE PHE D . n 
B 2 147 GLY 147 146 146 GLY GLY D . n 
B 2 148 SER 148 147 147 SER SER D . n 
B 2 149 ARG 149 148 148 ARG ARG D . n 
B 2 150 ASN 150 149 149 ASN ASN D . n 
B 2 151 GLY 151 150 150 GLY GLY D . n 
B 2 152 LYS 152 151 151 LYS LYS D . n 
B 2 153 THR 153 152 152 THR THR D . n 
B 2 154 SER 154 153 153 SER SER D . n 
B 2 155 LYS 155 154 154 LYS LYS D . n 
B 2 156 LYS 156 155 155 LYS LYS D . n 
B 2 157 ILE 157 156 156 ILE ILE D . n 
B 2 158 THR 158 157 157 THR THR D . n 
B 2 159 ILE 159 158 158 ILE ILE D . n 
B 2 160 ALA 160 159 159 ALA ALA D . n 
B 2 161 ASP 161 160 160 ASP ASP D . n 
B 2 162 CYS 162 161 161 CYS CYS D . n 
B 2 163 GLY 163 162 162 GLY GLY D . n 
B 2 164 GLN 164 163 163 GLN GLN D . n 
B 2 165 LEU 165 164 164 LEU LEU D . n 
B 2 166 GLU 166 165 165 GLU GLU D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AOM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AOM 
_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 
C 3 GNP   1   201 200  GNP   GNP A . 
D 4 MG    1   202 201  MG    MG  A . 
E 5 BTB   1   203 202  BTB   BTB A . 
F 6 A1AOM 1   204 7806 A1AOM RMC A . 
G 7 HOH   1   301 293  HOH   HOH A . 
G 7 HOH   2   302 334  HOH   HOH A . 
G 7 HOH   3   303 494  HOH   HOH A . 
G 7 HOH   4   304 282  HOH   HOH A . 
G 7 HOH   5   305 400  HOH   HOH A . 
G 7 HOH   6   306 446  HOH   HOH A . 
G 7 HOH   7   307 270  HOH   HOH A . 
G 7 HOH   8   308 307  HOH   HOH A . 
G 7 HOH   9   309 391  HOH   HOH A . 
G 7 HOH   10  310 96   HOH   HOH A . 
G 7 HOH   11  311 439  HOH   HOH A . 
G 7 HOH   12  312 554  HOH   HOH A . 
G 7 HOH   13  313 92   HOH   HOH A . 
G 7 HOH   14  314 434  HOH   HOH A . 
G 7 HOH   15  315 328  HOH   HOH A . 
G 7 HOH   16  316 137  HOH   HOH A . 
G 7 HOH   17  317 318  HOH   HOH A . 
G 7 HOH   18  318 113  HOH   HOH A . 
G 7 HOH   19  319 164  HOH   HOH A . 
G 7 HOH   20  320 427  HOH   HOH A . 
G 7 HOH   21  321 82   HOH   HOH A . 
G 7 HOH   22  322 16   HOH   HOH A . 
G 7 HOH   23  323 151  HOH   HOH A . 
G 7 HOH   24  324 486  HOH   HOH A . 
G 7 HOH   25  325 586  HOH   HOH A . 
G 7 HOH   26  326 63   HOH   HOH A . 
G 7 HOH   27  327 4    HOH   HOH A . 
G 7 HOH   28  328 134  HOH   HOH A . 
G 7 HOH   29  329 521  HOH   HOH A . 
G 7 HOH   30  330 297  HOH   HOH A . 
G 7 HOH   31  331 45   HOH   HOH A . 
G 7 HOH   32  332 195  HOH   HOH A . 
G 7 HOH   33  333 226  HOH   HOH A . 
G 7 HOH   34  334 581  HOH   HOH A . 
G 7 HOH   35  335 374  HOH   HOH A . 
G 7 HOH   36  336 153  HOH   HOH A . 
G 7 HOH   37  337 591  HOH   HOH A . 
G 7 HOH   38  338 130  HOH   HOH A . 
G 7 HOH   39  339 118  HOH   HOH A . 
G 7 HOH   40  340 24   HOH   HOH A . 
G 7 HOH   41  341 592  HOH   HOH A . 
G 7 HOH   42  342 197  HOH   HOH A . 
G 7 HOH   43  343 325  HOH   HOH A . 
G 7 HOH   44  344 7    HOH   HOH A . 
G 7 HOH   45  345 250  HOH   HOH A . 
G 7 HOH   46  346 85   HOH   HOH A . 
G 7 HOH   47  347 111  HOH   HOH A . 
G 7 HOH   48  348 132  HOH   HOH A . 
G 7 HOH   49  349 326  HOH   HOH A . 
G 7 HOH   50  350 8    HOH   HOH A . 
G 7 HOH   51  351 461  HOH   HOH A . 
G 7 HOH   52  352 58   HOH   HOH A . 
G 7 HOH   53  353 48   HOH   HOH A . 
G 7 HOH   54  354 114  HOH   HOH A . 
G 7 HOH   55  355 56   HOH   HOH A . 
G 7 HOH   56  356 373  HOH   HOH A . 
G 7 HOH   57  357 229  HOH   HOH A . 
G 7 HOH   58  358 40   HOH   HOH A . 
G 7 HOH   59  359 66   HOH   HOH A . 
G 7 HOH   60  360 129  HOH   HOH A . 
G 7 HOH   61  361 44   HOH   HOH A . 
G 7 HOH   62  362 60   HOH   HOH A . 
G 7 HOH   63  363 245  HOH   HOH A . 
G 7 HOH   64  364 41   HOH   HOH A . 
G 7 HOH   65  365 311  HOH   HOH A . 
G 7 HOH   66  366 588  HOH   HOH A . 
G 7 HOH   67  367 27   HOH   HOH A . 
G 7 HOH   68  368 379  HOH   HOH A . 
G 7 HOH   69  369 53   HOH   HOH A . 
G 7 HOH   70  370 32   HOH   HOH A . 
G 7 HOH   71  371 243  HOH   HOH A . 
G 7 HOH   72  372 315  HOH   HOH A . 
G 7 HOH   73  373 158  HOH   HOH A . 
G 7 HOH   74  374 200  HOH   HOH A . 
G 7 HOH   75  375 551  HOH   HOH A . 
G 7 HOH   76  376 304  HOH   HOH A . 
G 7 HOH   77  377 357  HOH   HOH A . 
G 7 HOH   78  378 157  HOH   HOH A . 
G 7 HOH   79  379 110  HOH   HOH A . 
G 7 HOH   80  380 188  HOH   HOH A . 
G 7 HOH   81  381 83   HOH   HOH A . 
G 7 HOH   82  382 69   HOH   HOH A . 
G 7 HOH   83  383 483  HOH   HOH A . 
G 7 HOH   84  384 218  HOH   HOH A . 
G 7 HOH   85  385 72   HOH   HOH A . 
G 7 HOH   86  386 553  HOH   HOH A . 
G 7 HOH   87  387 33   HOH   HOH A . 
G 7 HOH   88  388 180  HOH   HOH A . 
G 7 HOH   89  389 372  HOH   HOH A . 
G 7 HOH   90  390 28   HOH   HOH A . 
G 7 HOH   91  391 480  HOH   HOH A . 
G 7 HOH   92  392 170  HOH   HOH A . 
G 7 HOH   93  393 416  HOH   HOH A . 
G 7 HOH   94  394 6    HOH   HOH A . 
G 7 HOH   95  395 199  HOH   HOH A . 
G 7 HOH   96  396 12   HOH   HOH A . 
G 7 HOH   97  397 241  HOH   HOH A . 
G 7 HOH   98  398 105  HOH   HOH A . 
G 7 HOH   99  399 575  HOH   HOH A . 
G 7 HOH   100 400 139  HOH   HOH A . 
G 7 HOH   101 401 97   HOH   HOH A . 
G 7 HOH   102 402 509  HOH   HOH A . 
G 7 HOH   103 403 552  HOH   HOH A . 
G 7 HOH   104 404 349  HOH   HOH A . 
G 7 HOH   105 405 378  HOH   HOH A . 
G 7 HOH   106 406 91   HOH   HOH A . 
G 7 HOH   107 407 465  HOH   HOH A . 
G 7 HOH   108 408 149  HOH   HOH A . 
G 7 HOH   109 409 572  HOH   HOH A . 
G 7 HOH   110 410 347  HOH   HOH A . 
G 7 HOH   111 411 208  HOH   HOH A . 
G 7 HOH   112 412 366  HOH   HOH A . 
G 7 HOH   113 413 248  HOH   HOH A . 
G 7 HOH   114 414 333  HOH   HOH A . 
G 7 HOH   115 415 67   HOH   HOH A . 
G 7 HOH   116 416 415  HOH   HOH A . 
G 7 HOH   117 417 286  HOH   HOH A . 
G 7 HOH   118 418 86   HOH   HOH A . 
G 7 HOH   119 419 187  HOH   HOH A . 
G 7 HOH   120 420 444  HOH   HOH A . 
G 7 HOH   121 421 3    HOH   HOH A . 
G 7 HOH   122 422 172  HOH   HOH A . 
G 7 HOH   123 423 74   HOH   HOH A . 
G 7 HOH   124 424 191  HOH   HOH A . 
G 7 HOH   125 425 587  HOH   HOH A . 
G 7 HOH   126 426 146  HOH   HOH A . 
G 7 HOH   127 427 342  HOH   HOH A . 
G 7 HOH   128 428 205  HOH   HOH A . 
G 7 HOH   129 429 462  HOH   HOH A . 
G 7 HOH   130 430 143  HOH   HOH A . 
G 7 HOH   131 431 441  HOH   HOH A . 
G 7 HOH   132 432 394  HOH   HOH A . 
G 7 HOH   133 433 161  HOH   HOH A . 
G 7 HOH   134 434 289  HOH   HOH A . 
G 7 HOH   135 435 5    HOH   HOH A . 
G 7 HOH   136 436 145  HOH   HOH A . 
G 7 HOH   137 437 186  HOH   HOH A . 
G 7 HOH   138 438 210  HOH   HOH A . 
G 7 HOH   139 439 207  HOH   HOH A . 
G 7 HOH   140 440 115  HOH   HOH A . 
G 7 HOH   141 441 77   HOH   HOH A . 
G 7 HOH   142 442 103  HOH   HOH A . 
G 7 HOH   143 443 320  HOH   HOH A . 
G 7 HOH   144 444 147  HOH   HOH A . 
G 7 HOH   145 445 112  HOH   HOH A . 
G 7 HOH   146 446 29   HOH   HOH A . 
G 7 HOH   147 447 31   HOH   HOH A . 
G 7 HOH   148 448 65   HOH   HOH A . 
G 7 HOH   149 449 557  HOH   HOH A . 
G 7 HOH   150 450 43   HOH   HOH A . 
G 7 HOH   151 451 59   HOH   HOH A . 
G 7 HOH   152 452 55   HOH   HOH A . 
G 7 HOH   153 453 544  HOH   HOH A . 
G 7 HOH   154 454 263  HOH   HOH A . 
G 7 HOH   155 455 259  HOH   HOH A . 
G 7 HOH   156 456 574  HOH   HOH A . 
G 7 HOH   157 457 68   HOH   HOH A . 
G 7 HOH   158 458 290  HOH   HOH A . 
G 7 HOH   159 459 169  HOH   HOH A . 
G 7 HOH   160 460 306  HOH   HOH A . 
G 7 HOH   161 461 464  HOH   HOH A . 
G 7 HOH   162 462 433  HOH   HOH A . 
G 7 HOH   163 463 57   HOH   HOH A . 
G 7 HOH   164 464 344  HOH   HOH A . 
G 7 HOH   165 465 104  HOH   HOH A . 
G 7 HOH   166 466 276  HOH   HOH A . 
G 7 HOH   167 467 309  HOH   HOH A . 
G 7 HOH   168 468 37   HOH   HOH A . 
G 7 HOH   169 469 474  HOH   HOH A . 
G 7 HOH   170 470 160  HOH   HOH A . 
G 7 HOH   171 471 179  HOH   HOH A . 
G 7 HOH   172 472 356  HOH   HOH A . 
G 7 HOH   173 473 38   HOH   HOH A . 
G 7 HOH   174 474 2    HOH   HOH A . 
G 7 HOH   175 475 393  HOH   HOH A . 
G 7 HOH   176 476 204  HOH   HOH A . 
G 7 HOH   177 477 396  HOH   HOH A . 
G 7 HOH   178 478 358  HOH   HOH A . 
G 7 HOH   179 479 230  HOH   HOH A . 
G 7 HOH   180 480 580  HOH   HOH A . 
G 7 HOH   181 481 578  HOH   HOH A . 
G 7 HOH   182 482 267  HOH   HOH A . 
G 7 HOH   183 483 452  HOH   HOH A . 
G 7 HOH   184 484 508  HOH   HOH A . 
G 7 HOH   185 485 22   HOH   HOH A . 
G 7 HOH   186 486 408  HOH   HOH A . 
G 7 HOH   187 487 346  HOH   HOH A . 
G 7 HOH   188 488 19   HOH   HOH A . 
G 7 HOH   189 489 385  HOH   HOH A . 
G 7 HOH   190 490 538  HOH   HOH A . 
G 7 HOH   191 491 324  HOH   HOH A . 
G 7 HOH   192 492 492  HOH   HOH A . 
G 7 HOH   193 493 300  HOH   HOH A . 
G 7 HOH   194 494 582  HOH   HOH A . 
G 7 HOH   195 495 583  HOH   HOH A . 
G 7 HOH   196 496 559  HOH   HOH A . 
G 7 HOH   197 497 585  HOH   HOH A . 
G 7 HOH   198 498 605  HOH   HOH A . 
G 7 HOH   199 499 233  HOH   HOH A . 
G 7 HOH   200 500 314  HOH   HOH A . 
G 7 HOH   201 501 348  HOH   HOH A . 
G 7 HOH   202 502 401  HOH   HOH A . 
G 7 HOH   203 503 500  HOH   HOH A . 
G 7 HOH   204 504 303  HOH   HOH A . 
G 7 HOH   205 505 514  HOH   HOH A . 
G 7 HOH   206 506 383  HOH   HOH A . 
G 7 HOH   207 507 555  HOH   HOH A . 
G 7 HOH   208 508 288  HOH   HOH A . 
G 7 HOH   209 509 298  HOH   HOH A . 
G 7 HOH   210 510 550  HOH   HOH A . 
G 7 HOH   211 511 423  HOH   HOH A . 
G 7 HOH   212 512 252  HOH   HOH A . 
G 7 HOH   213 513 443  HOH   HOH A . 
G 7 HOH   214 514 361  HOH   HOH A . 
G 7 HOH   215 515 409  HOH   HOH A . 
G 7 HOH   216 516 371  HOH   HOH A . 
G 7 HOH   217 517 295  HOH   HOH A . 
G 7 HOH   218 518 292  HOH   HOH A . 
G 7 HOH   219 519 181  HOH   HOH A . 
G 7 HOH   220 520 351  HOH   HOH A . 
G 7 HOH   221 521 512  HOH   HOH A . 
G 7 HOH   222 522 411  HOH   HOH A . 
G 7 HOH   223 523 246  HOH   HOH A . 
G 7 HOH   224 524 410  HOH   HOH A . 
G 7 HOH   225 525 402  HOH   HOH A . 
G 7 HOH   226 526 176  HOH   HOH A . 
G 7 HOH   227 527 244  HOH   HOH A . 
G 7 HOH   228 528 455  HOH   HOH A . 
G 7 HOH   229 529 584  HOH   HOH A . 
G 7 HOH   230 530 89   HOH   HOH A . 
G 7 HOH   231 531 341  HOH   HOH A . 
G 7 HOH   232 532 431  HOH   HOH A . 
G 7 HOH   233 533 231  HOH   HOH A . 
G 7 HOH   234 534 212  HOH   HOH A . 
G 7 HOH   235 535 542  HOH   HOH A . 
G 7 HOH   236 536 174  HOH   HOH A . 
G 7 HOH   237 537 359  HOH   HOH A . 
G 7 HOH   238 538 377  HOH   HOH A . 
G 7 HOH   239 539 556  HOH   HOH A . 
G 7 HOH   240 540 365  HOH   HOH A . 
G 7 HOH   241 541 466  HOH   HOH A . 
G 7 HOH   242 542 225  HOH   HOH A . 
G 7 HOH   243 543 456  HOH   HOH A . 
G 7 HOH   244 544 470  HOH   HOH A . 
G 7 HOH   245 545 526  HOH   HOH A . 
G 7 HOH   246 546 499  HOH   HOH A . 
G 7 HOH   247 547 354  HOH   HOH A . 
G 7 HOH   248 548 506  HOH   HOH A . 
G 7 HOH   249 549 287  HOH   HOH A . 
G 7 HOH   250 550 603  HOH   HOH A . 
G 7 HOH   251 551 495  HOH   HOH A . 
G 7 HOH   252 552 589  HOH   HOH A . 
G 7 HOH   253 553 102  HOH   HOH A . 
G 7 HOH   254 554 445  HOH   HOH A . 
G 7 HOH   255 555 173  HOH   HOH A . 
G 7 HOH   256 556 541  HOH   HOH A . 
G 7 HOH   257 557 459  HOH   HOH A . 
G 7 HOH   258 558 49   HOH   HOH A . 
G 7 HOH   259 559 477  HOH   HOH A . 
G 7 HOH   260 560 419  HOH   HOH A . 
H 7 HOH   1   201 606  HOH   HOH D . 
H 7 HOH   2   202 360  HOH   HOH D . 
H 7 HOH   3   203 302  HOH   HOH D . 
H 7 HOH   4   204 272  HOH   HOH D . 
H 7 HOH   5   205 247  HOH   HOH D . 
H 7 HOH   6   206 177  HOH   HOH D . 
H 7 HOH   7   207 322  HOH   HOH D . 
H 7 HOH   8   208 390  HOH   HOH D . 
H 7 HOH   9   209 168  HOH   HOH D . 
H 7 HOH   10  210 94   HOH   HOH D . 
H 7 HOH   11  211 150  HOH   HOH D . 
H 7 HOH   12  212 251  HOH   HOH D . 
H 7 HOH   13  213 260  HOH   HOH D . 
H 7 HOH   14  214 387  HOH   HOH D . 
H 7 HOH   15  215 171  HOH   HOH D . 
H 7 HOH   16  216 327  HOH   HOH D . 
H 7 HOH   17  217 330  HOH   HOH D . 
H 7 HOH   18  218 417  HOH   HOH D . 
H 7 HOH   19  219 78   HOH   HOH D . 
H 7 HOH   20  220 576  HOH   HOH D . 
H 7 HOH   21  221 34   HOH   HOH D . 
H 7 HOH   22  222 152  HOH   HOH D . 
H 7 HOH   23  223 331  HOH   HOH D . 
H 7 HOH   24  224 76   HOH   HOH D . 
H 7 HOH   25  225 268  HOH   HOH D . 
H 7 HOH   26  226 535  HOH   HOH D . 
H 7 HOH   27  227 317  HOH   HOH D . 
H 7 HOH   28  228 496  HOH   HOH D . 
H 7 HOH   29  229 213  HOH   HOH D . 
H 7 HOH   30  230 47   HOH   HOH D . 
H 7 HOH   31  231 264  HOH   HOH D . 
H 7 HOH   32  232 573  HOH   HOH D . 
H 7 HOH   33  233 136  HOH   HOH D . 
H 7 HOH   34  234 451  HOH   HOH D . 
H 7 HOH   35  235 527  HOH   HOH D . 
H 7 HOH   36  236 203  HOH   HOH D . 
H 7 HOH   37  237 227  HOH   HOH D . 
H 7 HOH   38  238 135  HOH   HOH D . 
H 7 HOH   39  239 604  HOH   HOH D . 
H 7 HOH   40  240 79   HOH   HOH D . 
H 7 HOH   41  241 278  HOH   HOH D . 
H 7 HOH   42  242 220  HOH   HOH D . 
H 7 HOH   43  243 166  HOH   HOH D . 
H 7 HOH   44  244 269  HOH   HOH D . 
H 7 HOH   45  245 17   HOH   HOH D . 
H 7 HOH   46  246 202  HOH   HOH D . 
H 7 HOH   47  247 234  HOH   HOH D . 
H 7 HOH   48  248 75   HOH   HOH D . 
H 7 HOH   49  249 420  HOH   HOH D . 
H 7 HOH   50  250 120  HOH   HOH D . 
H 7 HOH   51  251 274  HOH   HOH D . 
H 7 HOH   52  252 182  HOH   HOH D . 
H 7 HOH   53  253 382  HOH   HOH D . 
H 7 HOH   54  254 280  HOH   HOH D . 
H 7 HOH   55  255 26   HOH   HOH D . 
H 7 HOH   56  256 569  HOH   HOH D . 
H 7 HOH   57  257 198  HOH   HOH D . 
H 7 HOH   58  258 11   HOH   HOH D . 
H 7 HOH   59  259 25   HOH   HOH D . 
H 7 HOH   60  260 395  HOH   HOH D . 
H 7 HOH   61  261 125  HOH   HOH D . 
H 7 HOH   62  262 73   HOH   HOH D . 
H 7 HOH   63  263 261  HOH   HOH D . 
H 7 HOH   64  264 39   HOH   HOH D . 
H 7 HOH   65  265 64   HOH   HOH D . 
H 7 HOH   66  266 599  HOH   HOH D . 
H 7 HOH   67  267 36   HOH   HOH D . 
H 7 HOH   68  268 192  HOH   HOH D . 
H 7 HOH   69  269 418  HOH   HOH D . 
H 7 HOH   70  270 133  HOH   HOH D . 
H 7 HOH   71  271 128  HOH   HOH D . 
H 7 HOH   72  272 283  HOH   HOH D . 
H 7 HOH   73  273 61   HOH   HOH D . 
H 7 HOH   74  274 380  HOH   HOH D . 
H 7 HOH   75  275 81   HOH   HOH D . 
H 7 HOH   76  276 88   HOH   HOH D . 
H 7 HOH   77  277 392  HOH   HOH D . 
H 7 HOH   78  278 294  HOH   HOH D . 
H 7 HOH   79  279 14   HOH   HOH D . 
H 7 HOH   80  280 30   HOH   HOH D . 
H 7 HOH   81  281 20   HOH   HOH D . 
H 7 HOH   82  282 21   HOH   HOH D . 
H 7 HOH   83  283 211  HOH   HOH D . 
H 7 HOH   84  284 9    HOH   HOH D . 
H 7 HOH   85  285 15   HOH   HOH D . 
H 7 HOH   86  286 190  HOH   HOH D . 
H 7 HOH   87  287 254  HOH   HOH D . 
H 7 HOH   88  288 84   HOH   HOH D . 
H 7 HOH   89  289 95   HOH   HOH D . 
H 7 HOH   90  290 70   HOH   HOH D . 
H 7 HOH   91  291 1    HOH   HOH D . 
H 7 HOH   92  292 206  HOH   HOH D . 
H 7 HOH   93  293 51   HOH   HOH D . 
H 7 HOH   94  294 332  HOH   HOH D . 
H 7 HOH   95  295 54   HOH   HOH D . 
H 7 HOH   96  296 189  HOH   HOH D . 
H 7 HOH   97  297 117  HOH   HOH D . 
H 7 HOH   98  298 214  HOH   HOH D . 
H 7 HOH   99  299 131  HOH   HOH D . 
H 7 HOH   100 300 235  HOH   HOH D . 
H 7 HOH   101 301 440  HOH   HOH D . 
H 7 HOH   102 302 155  HOH   HOH D . 
H 7 HOH   103 303 305  HOH   HOH D . 
H 7 HOH   104 304 196  HOH   HOH D . 
H 7 HOH   105 305 438  HOH   HOH D . 
H 7 HOH   106 306 46   HOH   HOH D . 
H 7 HOH   107 307 335  HOH   HOH D . 
H 7 HOH   108 308 355  HOH   HOH D . 
H 7 HOH   109 309 217  HOH   HOH D . 
H 7 HOH   110 310 108  HOH   HOH D . 
H 7 HOH   111 311 598  HOH   HOH D . 
H 7 HOH   112 312 397  HOH   HOH D . 
H 7 HOH   113 313 448  HOH   HOH D . 
H 7 HOH   114 314 316  HOH   HOH D . 
H 7 HOH   115 315 193  HOH   HOH D . 
H 7 HOH   116 316 124  HOH   HOH D . 
H 7 HOH   117 317 240  HOH   HOH D . 
H 7 HOH   118 318 570  HOH   HOH D . 
H 7 HOH   119 319 223  HOH   HOH D . 
H 7 HOH   120 320 127  HOH   HOH D . 
H 7 HOH   121 321 35   HOH   HOH D . 
H 7 HOH   122 322 257  HOH   HOH D . 
H 7 HOH   123 323 412  HOH   HOH D . 
H 7 HOH   124 324 600  HOH   HOH D . 
H 7 HOH   125 325 209  HOH   HOH D . 
H 7 HOH   126 326 101  HOH   HOH D . 
H 7 HOH   127 327 228  HOH   HOH D . 
H 7 HOH   128 328 178  HOH   HOH D . 
H 7 HOH   129 329 215  HOH   HOH D . 
H 7 HOH   130 330 156  HOH   HOH D . 
H 7 HOH   131 331 167  HOH   HOH D . 
H 7 HOH   132 332 369  HOH   HOH D . 
H 7 HOH   133 333 50   HOH   HOH D . 
H 7 HOH   134 334 18   HOH   HOH D . 
H 7 HOH   135 335 23   HOH   HOH D . 
H 7 HOH   136 336 525  HOH   HOH D . 
H 7 HOH   137 337 520  HOH   HOH D . 
H 7 HOH   138 338 116  HOH   HOH D . 
H 7 HOH   139 339 99   HOH   HOH D . 
H 7 HOH   140 340 201  HOH   HOH D . 
H 7 HOH   141 341 602  HOH   HOH D . 
H 7 HOH   142 342 184  HOH   HOH D . 
H 7 HOH   143 343 308  HOH   HOH D . 
H 7 HOH   144 344 122  HOH   HOH D . 
H 7 HOH   145 345 398  HOH   HOH D . 
H 7 HOH   146 346 493  HOH   HOH D . 
H 7 HOH   147 347 221  HOH   HOH D . 
H 7 HOH   148 348 71   HOH   HOH D . 
H 7 HOH   149 349 386  HOH   HOH D . 
H 7 HOH   150 350 262  HOH   HOH D . 
H 7 HOH   151 351 144  HOH   HOH D . 
H 7 HOH   152 352 10   HOH   HOH D . 
H 7 HOH   153 353 255  HOH   HOH D . 
H 7 HOH   154 354 364  HOH   HOH D . 
H 7 HOH   155 355 141  HOH   HOH D . 
H 7 HOH   156 356 343  HOH   HOH D . 
H 7 HOH   157 357 568  HOH   HOH D . 
H 7 HOH   158 358 353  HOH   HOH D . 
H 7 HOH   159 359 194  HOH   HOH D . 
H 7 HOH   160 360 106  HOH   HOH D . 
H 7 HOH   161 361 404  HOH   HOH D . 
H 7 HOH   162 362 482  HOH   HOH D . 
H 7 HOH   163 363 232  HOH   HOH D . 
H 7 HOH   164 364 52   HOH   HOH D . 
H 7 HOH   165 365 301  HOH   HOH D . 
H 7 HOH   166 366 98   HOH   HOH D . 
H 7 HOH   167 367 90   HOH   HOH D . 
H 7 HOH   168 368 219  HOH   HOH D . 
H 7 HOH   169 369 540  HOH   HOH D . 
H 7 HOH   170 370 481  HOH   HOH D . 
H 7 HOH   171 371 548  HOH   HOH D . 
H 7 HOH   172 372 80   HOH   HOH D . 
H 7 HOH   173 373 329  HOH   HOH D . 
H 7 HOH   174 374 238  HOH   HOH D . 
H 7 HOH   175 375 517  HOH   HOH D . 
H 7 HOH   176 376 529  HOH   HOH D . 
H 7 HOH   177 377 296  HOH   HOH D . 
H 7 HOH   178 378 42   HOH   HOH D . 
H 7 HOH   179 379 121  HOH   HOH D . 
H 7 HOH   180 380 323  HOH   HOH D . 
H 7 HOH   181 381 428  HOH   HOH D . 
H 7 HOH   182 382 524  HOH   HOH D . 
H 7 HOH   183 383 299  HOH   HOH D . 
H 7 HOH   184 384 463  HOH   HOH D . 
H 7 HOH   185 385 487  HOH   HOH D . 
H 7 HOH   186 386 100  HOH   HOH D . 
H 7 HOH   187 387 165  HOH   HOH D . 
H 7 HOH   188 388 469  HOH   HOH D . 
H 7 HOH   189 389 275  HOH   HOH D . 
H 7 HOH   190 390 565  HOH   HOH D . 
H 7 HOH   191 391 453  HOH   HOH D . 
H 7 HOH   192 392 185  HOH   HOH D . 
H 7 HOH   193 393 424  HOH   HOH D . 
H 7 HOH   194 394 563  HOH   HOH D . 
H 7 HOH   195 395 503  HOH   HOH D . 
H 7 HOH   196 396 87   HOH   HOH D . 
H 7 HOH   197 397 425  HOH   HOH D . 
H 7 HOH   198 398 490  HOH   HOH D . 
H 7 HOH   199 399 119  HOH   HOH D . 
H 7 HOH   200 400 154  HOH   HOH D . 
H 7 HOH   201 401 564  HOH   HOH D . 
H 7 HOH   202 402 539  HOH   HOH D . 
H 7 HOH   203 403 567  HOH   HOH D . 
H 7 HOH   204 404 126  HOH   HOH D . 
H 7 HOH   205 405 432  HOH   HOH D . 
H 7 HOH   206 406 107  HOH   HOH D . 
H 7 HOH   207 407 519  HOH   HOH D . 
H 7 HOH   208 408 337  HOH   HOH D . 
H 7 HOH   209 409 123  HOH   HOH D . 
H 7 HOH   210 410 370  HOH   HOH D . 
H 7 HOH   211 411 436  HOH   HOH D . 
H 7 HOH   212 412 159  HOH   HOH D . 
H 7 HOH   213 413 533  HOH   HOH D . 
H 7 HOH   214 414 281  HOH   HOH D . 
H 7 HOH   215 415 471  HOH   HOH D . 
H 7 HOH   216 416 577  HOH   HOH D . 
H 7 HOH   217 417 579  HOH   HOH D . 
H 7 HOH   218 418 338  HOH   HOH D . 
H 7 HOH   219 419 336  HOH   HOH D . 
H 7 HOH   220 420 502  HOH   HOH D . 
H 7 HOH   221 421 183  HOH   HOH D . 
H 7 HOH   222 422 476  HOH   HOH D . 
H 7 HOH   223 423 352  HOH   HOH D . 
H 7 HOH   224 424 236  HOH   HOH D . 
H 7 HOH   225 425 253  HOH   HOH D . 
H 7 HOH   226 426 237  HOH   HOH D . 
H 7 HOH   227 427 560  HOH   HOH D . 
H 7 HOH   228 428 291  HOH   HOH D . 
H 7 HOH   229 429 162  HOH   HOH D . 
H 7 HOH   230 430 284  HOH   HOH D . 
H 7 HOH   231 431 256  HOH   HOH D . 
H 7 HOH   232 432 430  HOH   HOH D . 
H 7 HOH   233 433 491  HOH   HOH D . 
H 7 HOH   234 434 497  HOH   HOH D . 
H 7 HOH   235 435 429  HOH   HOH D . 
H 7 HOH   236 436 489  HOH   HOH D . 
H 7 HOH   237 437 596  HOH   HOH D . 
H 7 HOH   238 438 566  HOH   HOH D . 
H 7 HOH   239 439 399  HOH   HOH D . 
H 7 HOH   240 440 140  HOH   HOH D . 
H 7 HOH   241 441 273  HOH   HOH D . 
H 7 HOH   242 442 442  HOH   HOH D . 
H 7 HOH   243 443 403  HOH   HOH D . 
H 7 HOH   244 444 528  HOH   HOH D . 
H 7 HOH   245 445 421  HOH   HOH D . 
H 7 HOH   246 446 467  HOH   HOH D . 
H 7 HOH   247 447 507  HOH   HOH D . 
H 7 HOH   248 448 216  HOH   HOH D . 
H 7 HOH   249 449 388  HOH   HOH D . 
H 7 HOH   250 450 414  HOH   HOH D . 
H 7 HOH   251 451 266  HOH   HOH D . 
H 7 HOH   252 452 473  HOH   HOH D . 
H 7 HOH   253 453 450  HOH   HOH D . 
H 7 HOH   254 454 561  HOH   HOH D . 
H 7 HOH   255 455 163  HOH   HOH D . 
H 7 HOH   256 456 224  HOH   HOH D . 
H 7 HOH   257 457 595  HOH   HOH D . 
H 7 HOH   258 458 458  HOH   HOH D . 
H 7 HOH   259 459 472  HOH   HOH D . 
H 7 HOH   260 460 523  HOH   HOH D . 
H 7 HOH   261 461 485  HOH   HOH D . 
H 7 HOH   262 462 593  HOH   HOH D . 
H 7 HOH   263 463 510  HOH   HOH D . 
H 7 HOH   264 464 513  HOH   HOH D . 
H 7 HOH   265 465 258  HOH   HOH D . 
H 7 HOH   266 466 363  HOH   HOH D . 
H 7 HOH   267 467 505  HOH   HOH D . 
H 7 HOH   268 468 375  HOH   HOH D . 
H 7 HOH   269 469 460  HOH   HOH D . 
H 7 HOH   270 470 279  HOH   HOH D . 
H 7 HOH   271 471 601  HOH   HOH D . 
H 7 HOH   272 472 242  HOH   HOH D . 
H 7 HOH   273 473 531  HOH   HOH D . 
H 7 HOH   274 474 447  HOH   HOH D . 
H 7 HOH   275 475 277  HOH   HOH D . 
H 7 HOH   276 476 340  HOH   HOH D . 
H 7 HOH   277 477 271  HOH   HOH D . 
H 7 HOH   278 478 313  HOH   HOH D . 
H 7 HOH   279 479 449  HOH   HOH D . 
H 7 HOH   280 480 547  HOH   HOH D . 
H 7 HOH   281 481 516  HOH   HOH D . 
H 7 HOH   282 482 454  HOH   HOH D . 
H 7 HOH   283 483 350  HOH   HOH D . 
H 7 HOH   284 484 594  HOH   HOH D . 
H 7 HOH   285 485 376  HOH   HOH D . 
H 7 HOH   286 486 597  HOH   HOH D . 
H 7 HOH   287 487 426  HOH   HOH D . 
H 7 HOH   288 488 488  HOH   HOH D . 
H 7 HOH   289 489 422  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                   97.950 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BFW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     37.210 
_cell.length_a_esd                 ? 
_cell.length_b                     58.080 
_cell.length_b_esd                 ? 
_cell.length_c                     75.950 
_cell.length_c_esd                 ? 
_cell.volume                       162562.334 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_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                         9BFW 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BFW 
_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             2.17 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.27 
_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' 
_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 EIGER X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-04-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   .953 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'CLSI BEAMLINE 08ID-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        .953 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   08ID-1 
_diffrn_source.pdbx_synchrotron_site       CLSI 
# 
_reflns.B_iso_Wilson_estimate                          10.26 
_reflns.entry_id                                       9BFW 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.20 
_reflns.d_resolution_low                               35.07 
_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                                     99659 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.61 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          15.35 
_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                                .05144 
_reflns.pdbx_Rpim_I_all                                .02607 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .998 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              .04415 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.20 
_reflns_shell.d_res_low                                     1.243 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.98 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             9775 
_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                               .2368 
_reflns_shell.pdbx_Rpim_I_all                               .1258 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .947 
_reflns_shell.pdbx_CC_star                                  .986 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          98.16 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  .1992 
_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                               16.18 
_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                                 9BFW 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.20 
_refine.ls_d_res_low                             35.07 
_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                     99646 
_refine.ls_number_reflns_R_free                  4936 
_refine.ls_number_reflns_R_work                  94710 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.61 
_refine.ls_percent_reflns_R_free                 4.95 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1223 
_refine.ls_R_factor_R_free                       0.1475 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1210 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 12.9076 
_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                            0.0915 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.20 
_refine_hist.d_res_low                        35.07 
_refine_hist.number_atoms_solvent             549 
_refine_hist.number_atoms_total               3264 
_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        2614 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         101 
_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' ? 0.0051  ? 2926 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1709  ? 3973 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0829  ? 420  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0067  ? 519  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 13.9060 ? 1110 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.20 1.21  . . 148 3008 95.20 . . . . 0.1811 . . . . . . . . . . . 0.1884 
'X-RAY DIFFRACTION' 1.21 1.23  . . 154 3132 99.61 . . . . 0.1347 . . . . . . . . . . . 0.1948 
'X-RAY DIFFRACTION' 1.23 1.24  . . 162 3165 99.67 . . . . 0.1289 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 1.24 1.26  . . 160 3165 99.76 . . . . 0.1213 . . . . . . . . . . . 0.1649 
'X-RAY DIFFRACTION' 1.26 1.28  . . 186 3120 99.82 . . . . 0.1143 . . . . . . . . . . . 0.1496 
'X-RAY DIFFRACTION' 1.28 1.29  . . 169 3146 99.88 . . . . 0.1163 . . . . . . . . . . . 0.1475 
'X-RAY DIFFRACTION' 1.29 1.31  . . 162 3173 99.88 . . . . 0.1117 . . . . . . . . . . . 0.1485 
'X-RAY DIFFRACTION' 1.31 1.33  . . 152 3190 99.82 . . . . 0.1100 . . . . . . . . . . . 0.1561 
'X-RAY DIFFRACTION' 1.33 1.35  . . 164 3128 99.76 . . . . 0.1082 . . . . . . . . . . . 0.1446 
'X-RAY DIFFRACTION' 1.35 1.37  . . 152 3145 99.88 . . . . 0.1081 . . . . . . . . . . . 0.1501 
'X-RAY DIFFRACTION' 1.37 1.40  . . 159 3136 99.97 . . . . 0.1071 . . . . . . . . . . . 0.1401 
'X-RAY DIFFRACTION' 1.40 1.42  . . 166 3143 99.61 . . . . 0.1077 . . . . . . . . . . . 0.1463 
'X-RAY DIFFRACTION' 1.42 1.45  . . 176 3180 99.73 . . . . 0.1121 . . . . . . . . . . . 0.1393 
'X-RAY DIFFRACTION' 1.45 1.48  . . 177 3125 99.85 . . . . 0.1092 . . . . . . . . . . . 0.1281 
'X-RAY DIFFRACTION' 1.48 1.51  . . 154 3136 99.64 . . . . 0.1053 . . . . . . . . . . . 0.1319 
'X-RAY DIFFRACTION' 1.51 1.55  . . 151 3200 99.64 . . . . 0.1040 . . . . . . . . . . . 0.1391 
'X-RAY DIFFRACTION' 1.55 1.59  . . 177 3102 99.82 . . . . 0.1035 . . . . . . . . . . . 0.1388 
'X-RAY DIFFRACTION' 1.59 1.63  . . 169 3183 99.79 . . . . 0.1024 . . . . . . . . . . . 0.1377 
'X-RAY DIFFRACTION' 1.63 1.68  . . 167 3152 99.88 . . . . 0.1050 . . . . . . . . . . . 0.1365 
'X-RAY DIFFRACTION' 1.68 1.73  . . 152 3176 99.94 . . . . 0.1128 . . . . . . . . . . . 0.1484 
'X-RAY DIFFRACTION' 1.73 1.79  . . 171 3161 99.88 . . . . 0.1179 . . . . . . . . . . . 0.1440 
'X-RAY DIFFRACTION' 1.79 1.86  . . 153 3230 99.88 . . . . 0.1195 . . . . . . . . . . . 0.1580 
'X-RAY DIFFRACTION' 1.86 1.95  . . 165 3116 99.79 . . . . 0.1162 . . . . . . . . . . . 0.1594 
'X-RAY DIFFRACTION' 1.95 2.05  . . 176 3164 99.79 . . . . 0.1155 . . . . . . . . . . . 0.1523 
'X-RAY DIFFRACTION' 2.05 2.18  . . 169 3163 99.82 . . . . 0.1173 . . . . . . . . . . . 0.1396 
'X-RAY DIFFRACTION' 2.18 2.35  . . 168 3189 99.67 . . . . 0.1242 . . . . . . . . . . . 0.1481 
'X-RAY DIFFRACTION' 2.35 2.59  . . 160 3129 99.13 . . . . 0.1332 . . . . . . . . . . . 0.1469 
'X-RAY DIFFRACTION' 2.59 2.96  . . 168 3200 99.94 . . . . 0.1367 . . . . . . . . . . . 0.1636 
'X-RAY DIFFRACTION' 2.96 3.73  . . 170 3200 99.67 . . . . 0.1248 . . . . . . . . . . . 0.1458 
'X-RAY DIFFRACTION' 3.73 35.07 . . 179 3253 99.59 . . . . 0.1299 . . . . . . . . . . . 0.1385 
# 
_struct.entry_id                     9BFW 
_struct.title                        'Tri-complex of Compound-4, 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        9BFW 
_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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
G N N 7 ? 
H N N 7 ? 
# 
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 9BFW A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 2 9BFW 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 9BFW SER A 1   ? UNP P01116 ?   ?   'expression tag'      0   1 
1 9BFW CYS A 13  ? UNP P01116 GLY 12  'engineered mutation' 12  2 
1 9BFW SER A 52  ? UNP P01116 CYS 51  conflict              51  3 
1 9BFW LEU A 81  ? UNP P01116 CYS 80  conflict              80  4 
1 9BFW SER A 119 ? UNP P01116 CYS 118 conflict              118 5 
2 9BFW SER D 1   ? UNP P62937 ?   ?   'expression tag'      0   6 
2 9BFW SER D 53  ? UNP P62937 CYS 52  conflict              52  7 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 16  ? ASN A 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2 AA2 TYR A 65  ? ARG A 74  ? TYR A 64  ARG A 73  1 ? 10 
HELX_P HELX_P3 AA3 ASN A 87  ? ASP A 93  ? ASN A 86  ASP A 92  1 ? 7  
HELX_P HELX_P4 AA4 ASP A 93  ? ASP A 106 ? ASP A 92  ASP A 105 1 ? 14 
HELX_P HELX_P5 AA5 ASP A 127 ? GLY A 139 ? ASP A 126 GLY A 138 1 ? 13 
HELX_P HELX_P6 AA6 GLY A 152 ? LYS A 168 ? GLY A 151 LYS A 167 1 ? 17 
HELX_P HELX_P7 AA7 VAL B 30  ? GLY B 43  ? VAL D 29  GLY D 42  1 ? 14 
HELX_P HELX_P8 AA8 THR B 120 ? ASP B 124 ? THR D 119 ASP D 123 5 ? 5  
HELX_P HELX_P9 AA9 GLY B 136 ? ARG B 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 F A1AOM . C39 ? ? A CYS 12  A A1AOM 204 1_555 ? ? ? ? ? ? ? 1.650 ? ? 
metalc1 metalc ?    ? A SER 18 OG  ? ? ? 1_555 D MG    . MG  ? ? A SER 17  A MG    202 1_555 ? ? ? ? ? ? ? 2.084 ? ? 
metalc2 metalc ?    ? A THR 36 OG1 ? ? ? 1_555 D MG    . MG  ? ? A THR 35  A MG    202 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
metalc3 metalc ?    ? C GNP .  O1G ? ? ? 1_555 D MG    . MG  ? ? A GNP 201 A MG    202 1_555 ? ? ? ? ? ? ? 1.999 ? ? 
metalc4 metalc ?    ? C GNP .  O2B ? ? ? 1_555 D MG    . MG  ? ? A GNP 201 A MG    202 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc5 metalc ?    ? D MG  .  MG  ? ? ? 1_555 G HOH   . O   ? ? A MG  202 A HOH   327 1_555 ? ? ? ? ? ? ? 2.085 ? ? 
metalc6 metalc ?    ? D MG  .  MG  ? ? ? 1_555 G HOH   . O   ? ? A MG  202 A HOH   350 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 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 OG1 ? A THR 36 ? A THR 35  ? 1_555 83.9  ? 
2  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O1G ? C GNP .  ? A GNP 201 ? 1_555 173.5 ? 
3  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O1G ? C GNP .  ? A GNP 201 ? 1_555 90.0  ? 
4  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O2B ? C GNP .  ? A GNP 201 ? 1_555 90.9  ? 
5  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O2B ? C GNP .  ? A GNP 201 ? 1_555 173.5 ? 
6  O1G ? C GNP .  ? A GNP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O2B ? C GNP .  ? A GNP 201 ? 1_555 95.3  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 327 ? 1_555 86.5  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 327 ? 1_555 89.9  ? 
9  O1G ? C GNP .  ? A GNP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 327 ? 1_555 91.2  ? 
10 O2B ? C GNP .  ? A GNP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 327 ? 1_555 93.8  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 89.2  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 88.3  ? 
13 O1G ? C GNP .  ? A GNP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 92.9  ? 
14 O2B ? C GNP .  ? A GNP 201 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 87.5  ? 
15 O   ? G HOH .  ? A HOH 327 ? 1_555 MG ? D MG . ? A MG 202 ? 1_555 O   ? G HOH .  ? A HOH 350 ? 1_555 175.5 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      A1AOM 
_pdbx_modification_feature.label_asym_id                      F 
_pdbx_modification_feature.label_seq_id                       . 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      13 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       A1AOM 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        204 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       12 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               C39 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                CYS 
_pdbx_modification_feature.ref_pcm_id                         1 
_pdbx_modification_feature.ref_comp_id                        A1AOM 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 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 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 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 ASP A 39  ? ILE A 47  ? ASP A 38  ILE A 46  
AA1 2 GLU A 50  ? ASP A 58  ? GLU A 49  ASP A 57  
AA1 3 GLU A 4   ? GLY A 11  ? GLU A 3   GLY A 10  
AA1 4 GLY A 78  ? ALA A 84  ? GLY A 77  ALA A 83  
AA1 5 MET A 112 ? ASN A 117 ? MET A 111 ASN A 116 
AA1 6 PHE A 142 ? GLU A 144 ? PHE A 141 GLU A 143 
AA2 1 ARG B 56  ? ILE B 58  ? ARG D 55  ILE D 57  
AA2 2 MET B 62  ? GLY B 65  ? MET D 61  GLY D 64  
AA2 3 PHE B 113 ? CYS B 116 ? PHE D 112 CYS D 115 
AA2 4 ILE B 98  ? MET B 101 ? ILE D 97  MET D 100 
AA2 5 VAL B 129 ? GLU B 135 ? VAL D 128 GLU D 134 
AA2 6 GLU B 16  ? LEU B 25  ? GLU D 15  LEU D 24  
AA2 7 THR B 6   ? VAL B 13  ? THR D 5   VAL D 12  
AA2 8 ILE B 157 ? LEU B 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 ASP A 39  ? N ASP A 38  O ASP A 58  ? O ASP A 57  
AA1 2 3 O ASP A 55  ? O ASP A 54  N LEU A 7   ? N LEU A 6   
AA1 3 4 N VAL A 10  ? N VAL A 9   O VAL A 82  ? O VAL A 81  
AA1 4 5 N PHE A 83  ? N PHE A 82  O ASN A 117 ? O ASN A 116 
AA1 5 6 N LEU A 114 ? N LEU A 113 O ILE A 143 ? O ILE A 142 
AA2 1 2 N ARG B 56  ? N ARG D 55  O GLN B 64  ? O GLN D 63  
AA2 2 3 N CYS B 63  ? N CYS D 62  O ILE B 115 ? O ILE D 114 
AA2 3 4 O CYS B 116 ? O CYS D 115 N ILE B 98  ? N ILE D 97  
AA2 4 5 N LEU B 99  ? N LEU D 98  O GLY B 131 ? O GLY D 130 
AA2 5 6 O LYS B 134 ? O LYS D 133 N SER B 22  ? N SER D 21  
AA2 6 7 O LEU B 18  ? O LEU D 17  N ILE B 11  ? N ILE D 10  
AA2 7 8 N ASP B 10  ? N ASP D 9   O ASP B 161 ? O ASP D 160 
# 
_pdbx_entry_details.entry_id                   9BFW 
_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 A 36  ? ? -99.27  -66.09  
2 1 GLN A 61  ? ? 47.19   -137.43 
3 1 LYS A 117 ? ? 72.11   33.19   
4 1 PHE D 60  ? ? -129.88 -73.45  
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    N2 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    A1AOM 
_pdbx_validate_chiral.auth_seq_id     204 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 560 ? 6.70 . 
2 1 O ? D HOH 483 ? 5.89 . 
3 1 O ? D HOH 484 ? 5.96 . 
4 1 O ? D HOH 485 ? 6.01 . 
5 1 O ? D HOH 486 ? 6.15 . 
6 1 O ? D HOH 487 ? 6.37 . 
7 1 O ? D HOH 488 ? 6.63 . 
8 1 O ? D HOH 489 ? 6.88 . 
# 
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 GLU 168 ? A GLU 169 
2 1 Y 1 A LYS 169 ? A LYS 170 
# 
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 
A1AOM C1     C  N N 1   
A1AOM C10    C  N N 2   
A1AOM C11    C  N S 3   
A1AOM C12    C  N N 4   
A1AOM C13    C  N N 5   
A1AOM C14    C  N N 6   
A1AOM C15    C  N N 7   
A1AOM C16    C  N N 8   
A1AOM C17    C  N N 9   
A1AOM C18    C  Y N 10  
A1AOM C19    C  Y N 11  
A1AOM C2     C  N N 12  
A1AOM C20    C  N N 13  
A1AOM C21    C  N N 14  
A1AOM C22    C  Y N 15  
A1AOM C23    C  Y N 16  
A1AOM C24    C  Y N 17  
A1AOM C25    C  Y N 18  
A1AOM C26    C  Y N 19  
A1AOM C27    C  Y N 20  
A1AOM C28    C  Y N 21  
A1AOM C29    C  Y N 22  
A1AOM C3     C  N N 23  
A1AOM C30    C  Y N 24  
A1AOM C31    C  Y N 25  
A1AOM C32    C  Y N 26  
A1AOM C33    C  Y N 27  
A1AOM C34    C  N N 28  
A1AOM C35    C  N N 29  
A1AOM C36    C  N N 30  
A1AOM C37    C  N N 31  
A1AOM C38    C  N N 32  
A1AOM C39    C  N N 33  
A1AOM C4     C  N S 34  
A1AOM C40    C  N N 35  
A1AOM C5     C  N N 36  
A1AOM C6     C  N S 37  
A1AOM C7     C  N N 38  
A1AOM C8     C  N N 39  
A1AOM C9     C  N N 40  
A1AOM N1     N  N N 41  
A1AOM N2     N  N R 42  
A1AOM N3     N  Y N 43  
A1AOM N4     N  N N 44  
A1AOM N5     N  N N 45  
A1AOM N6     N  N N 46  
A1AOM N7     N  N N 47  
A1AOM O1     O  N N 48  
A1AOM O2     O  N N 49  
A1AOM O3     O  N N 50  
A1AOM O4     O  N N 51  
A1AOM O5     O  N N 52  
A1AOM O6     O  N N 53  
A1AOM O7     O  N N 54  
A1AOM H1     H  N N 55  
A1AOM H2     H  N N 56  
A1AOM H3     H  N N 57  
A1AOM H4     H  N N 58  
A1AOM H5     H  N N 59  
A1AOM H6     H  N N 60  
A1AOM H7     H  N N 61  
A1AOM H8     H  N N 62  
A1AOM H9     H  N N 63  
A1AOM H10    H  N N 64  
A1AOM H11    H  N N 65  
A1AOM H12    H  N N 66  
A1AOM H13    H  N N 67  
A1AOM H14    H  N N 68  
A1AOM H15    H  N N 69  
A1AOM H16    H  N N 70  
A1AOM H17    H  N N 71  
A1AOM H18    H  N N 72  
A1AOM H19    H  N N 73  
A1AOM H20    H  N N 74  
A1AOM H21    H  N N 75  
A1AOM H22    H  N N 76  
A1AOM H23    H  N N 77  
A1AOM H24    H  N N 78  
A1AOM H25    H  N N 79  
A1AOM H26    H  N N 80  
A1AOM H27    H  N N 81  
A1AOM H28    H  N N 82  
A1AOM H29    H  N N 83  
A1AOM H30    H  N N 84  
A1AOM H31    H  N N 85  
A1AOM H32    H  N N 86  
A1AOM H33    H  N N 87  
A1AOM H34    H  N N 88  
A1AOM H35    H  N N 89  
A1AOM H36    H  N N 90  
A1AOM H37    H  N N 91  
A1AOM H38    H  N N 92  
A1AOM H39    H  N N 93  
A1AOM H40    H  N N 94  
A1AOM H41    H  N N 95  
A1AOM H42    H  N N 96  
A1AOM H43    H  N N 97  
A1AOM H44    H  N N 98  
A1AOM H45    H  N N 99  
A1AOM H46    H  N N 100 
A1AOM H47    H  N N 101 
A1AOM H48    H  N N 102 
A1AOM H49    H  N N 103 
ALA   N      N  N N 104 
ALA   CA     C  N S 105 
ALA   C      C  N N 106 
ALA   O      O  N N 107 
ALA   CB     C  N N 108 
ALA   OXT    O  N N 109 
ALA   H      H  N N 110 
ALA   H2     H  N N 111 
ALA   HA     H  N N 112 
ALA   HB1    H  N N 113 
ALA   HB2    H  N N 114 
ALA   HB3    H  N N 115 
ALA   HXT    H  N N 116 
ARG   N      N  N N 117 
ARG   CA     C  N S 118 
ARG   C      C  N N 119 
ARG   O      O  N N 120 
ARG   CB     C  N N 121 
ARG   CG     C  N N 122 
ARG   CD     C  N N 123 
ARG   NE     N  N N 124 
ARG   CZ     C  N N 125 
ARG   NH1    N  N N 126 
ARG   NH2    N  N N 127 
ARG   OXT    O  N N 128 
ARG   H      H  N N 129 
ARG   H2     H  N N 130 
ARG   HA     H  N N 131 
ARG   HB2    H  N N 132 
ARG   HB3    H  N N 133 
ARG   HG2    H  N N 134 
ARG   HG3    H  N N 135 
ARG   HD2    H  N N 136 
ARG   HD3    H  N N 137 
ARG   HE     H  N N 138 
ARG   HH11   H  N N 139 
ARG   HH12   H  N N 140 
ARG   HH21   H  N N 141 
ARG   HH22   H  N N 142 
ARG   HXT    H  N N 143 
ASN   N      N  N N 144 
ASN   CA     C  N S 145 
ASN   C      C  N N 146 
ASN   O      O  N N 147 
ASN   CB     C  N N 148 
ASN   CG     C  N N 149 
ASN   OD1    O  N N 150 
ASN   ND2    N  N N 151 
ASN   OXT    O  N N 152 
ASN   H      H  N N 153 
ASN   H2     H  N N 154 
ASN   HA     H  N N 155 
ASN   HB2    H  N N 156 
ASN   HB3    H  N N 157 
ASN   HD21   H  N N 158 
ASN   HD22   H  N N 159 
ASN   HXT    H  N N 160 
ASP   N      N  N N 161 
ASP   CA     C  N S 162 
ASP   C      C  N N 163 
ASP   O      O  N N 164 
ASP   CB     C  N N 165 
ASP   CG     C  N N 166 
ASP   OD1    O  N N 167 
ASP   OD2    O  N N 168 
ASP   OXT    O  N N 169 
ASP   H      H  N N 170 
ASP   H2     H  N N 171 
ASP   HA     H  N N 172 
ASP   HB2    H  N N 173 
ASP   HB3    H  N N 174 
ASP   HD2    H  N N 175 
ASP   HXT    H  N N 176 
BTB   C1     C  N N 177 
BTB   O1     O  N N 178 
BTB   C2     C  N N 179 
BTB   C3     C  N N 180 
BTB   O3     O  N N 181 
BTB   C4     C  N N 182 
BTB   O4     O  N N 183 
BTB   N      N  N N 184 
BTB   C5     C  N N 185 
BTB   C6     C  N N 186 
BTB   O6     O  N N 187 
BTB   C7     C  N N 188 
BTB   C8     C  N N 189 
BTB   O8     O  N N 190 
BTB   H11    H  N N 191 
BTB   H12    H  N N 192 
BTB   HO1    H  N N 193 
BTB   H31    H  N N 194 
BTB   H32    H  N N 195 
BTB   HO3    H  N N 196 
BTB   H41    H  N N 197 
BTB   H42    H  N N 198 
BTB   HO4    H  N N 199 
BTB   H51    H  N N 200 
BTB   H52    H  N N 201 
BTB   H61    H  N N 202 
BTB   H62    H  N N 203 
BTB   HO6    H  N N 204 
BTB   H71    H  N N 205 
BTB   H72    H  N N 206 
BTB   H81    H  N N 207 
BTB   H82    H  N N 208 
BTB   HO8    H  N N 209 
CYS   N      N  N N 210 
CYS   CA     C  N R 211 
CYS   C      C  N N 212 
CYS   O      O  N N 213 
CYS   CB     C  N N 214 
CYS   SG     S  N N 215 
CYS   OXT    O  N N 216 
CYS   H      H  N N 217 
CYS   H2     H  N N 218 
CYS   HA     H  N N 219 
CYS   HB2    H  N N 220 
CYS   HB3    H  N N 221 
CYS   HG     H  N N 222 
CYS   HXT    H  N N 223 
GLN   N      N  N N 224 
GLN   CA     C  N S 225 
GLN   C      C  N N 226 
GLN   O      O  N N 227 
GLN   CB     C  N N 228 
GLN   CG     C  N N 229 
GLN   CD     C  N N 230 
GLN   OE1    O  N N 231 
GLN   NE2    N  N N 232 
GLN   OXT    O  N N 233 
GLN   H      H  N N 234 
GLN   H2     H  N N 235 
GLN   HA     H  N N 236 
GLN   HB2    H  N N 237 
GLN   HB3    H  N N 238 
GLN   HG2    H  N N 239 
GLN   HG3    H  N N 240 
GLN   HE21   H  N N 241 
GLN   HE22   H  N N 242 
GLN   HXT    H  N N 243 
GLU   N      N  N N 244 
GLU   CA     C  N S 245 
GLU   C      C  N N 246 
GLU   O      O  N N 247 
GLU   CB     C  N N 248 
GLU   CG     C  N N 249 
GLU   CD     C  N N 250 
GLU   OE1    O  N N 251 
GLU   OE2    O  N N 252 
GLU   OXT    O  N N 253 
GLU   H      H  N N 254 
GLU   H2     H  N N 255 
GLU   HA     H  N N 256 
GLU   HB2    H  N N 257 
GLU   HB3    H  N N 258 
GLU   HG2    H  N N 259 
GLU   HG3    H  N N 260 
GLU   HE2    H  N N 261 
GLU   HXT    H  N N 262 
GLY   N      N  N N 263 
GLY   CA     C  N N 264 
GLY   C      C  N N 265 
GLY   O      O  N N 266 
GLY   OXT    O  N N 267 
GLY   H      H  N N 268 
GLY   H2     H  N N 269 
GLY   HA2    H  N N 270 
GLY   HA3    H  N N 271 
GLY   HXT    H  N N 272 
GNP   PG     P  N N 273 
GNP   O1G    O  N N 274 
GNP   O2G    O  N N 275 
GNP   O3G    O  N N 276 
GNP   N3B    N  N N 277 
GNP   PB     P  N R 278 
GNP   O1B    O  N N 279 
GNP   O2B    O  N N 280 
GNP   O3A    O  N N 281 
GNP   PA     P  N S 282 
GNP   O1A    O  N N 283 
GNP   O2A    O  N N 284 
GNP   "O5'"  O  N N 285 
GNP   "C5'"  C  N N 286 
GNP   "C4'"  C  N R 287 
GNP   "O4'"  O  N N 288 
GNP   "C3'"  C  N S 289 
GNP   "O3'"  O  N N 290 
GNP   "C2'"  C  N R 291 
GNP   "O2'"  O  N N 292 
GNP   "C1'"  C  N R 293 
GNP   N9     N  Y N 294 
GNP   C8     C  Y N 295 
GNP   N7     N  Y N 296 
GNP   C5     C  Y N 297 
GNP   C6     C  Y N 298 
GNP   O6     O  N N 299 
GNP   N1     N  Y N 300 
GNP   C2     C  Y N 301 
GNP   N2     N  N N 302 
GNP   N3     N  Y N 303 
GNP   C4     C  Y N 304 
GNP   HOG2   H  N N 305 
GNP   HOG3   H  N N 306 
GNP   HNB3   H  N N 307 
GNP   HOB2   H  N N 308 
GNP   HOA2   H  N N 309 
GNP   "H5'2" H  N N 310 
GNP   "H5'1" H  N N 311 
GNP   "H4'"  H  N N 312 
GNP   "H3'"  H  N N 313 
GNP   "HO3'" H  N N 314 
GNP   "H2'"  H  N N 315 
GNP   "HO2'" H  N N 316 
GNP   "H1'"  H  N N 317 
GNP   H8     H  N N 318 
GNP   HN1    H  N N 319 
GNP   HN21   H  N N 320 
GNP   HN22   H  N N 321 
HIS   N      N  N N 322 
HIS   CA     C  N S 323 
HIS   C      C  N N 324 
HIS   O      O  N N 325 
HIS   CB     C  N N 326 
HIS   CG     C  Y N 327 
HIS   ND1    N  Y N 328 
HIS   CD2    C  Y N 329 
HIS   CE1    C  Y N 330 
HIS   NE2    N  Y N 331 
HIS   OXT    O  N N 332 
HIS   H      H  N N 333 
HIS   H2     H  N N 334 
HIS   HA     H  N N 335 
HIS   HB2    H  N N 336 
HIS   HB3    H  N N 337 
HIS   HD1    H  N N 338 
HIS   HD2    H  N N 339 
HIS   HE1    H  N N 340 
HIS   HE2    H  N N 341 
HIS   HXT    H  N N 342 
HOH   O      O  N N 343 
HOH   H1     H  N N 344 
HOH   H2     H  N N 345 
ILE   N      N  N N 346 
ILE   CA     C  N S 347 
ILE   C      C  N N 348 
ILE   O      O  N N 349 
ILE   CB     C  N S 350 
ILE   CG1    C  N N 351 
ILE   CG2    C  N N 352 
ILE   CD1    C  N N 353 
ILE   OXT    O  N N 354 
ILE   H      H  N N 355 
ILE   H2     H  N N 356 
ILE   HA     H  N N 357 
ILE   HB     H  N N 358 
ILE   HG12   H  N N 359 
ILE   HG13   H  N N 360 
ILE   HG21   H  N N 361 
ILE   HG22   H  N N 362 
ILE   HG23   H  N N 363 
ILE   HD11   H  N N 364 
ILE   HD12   H  N N 365 
ILE   HD13   H  N N 366 
ILE   HXT    H  N N 367 
LEU   N      N  N N 368 
LEU   CA     C  N S 369 
LEU   C      C  N N 370 
LEU   O      O  N N 371 
LEU   CB     C  N N 372 
LEU   CG     C  N N 373 
LEU   CD1    C  N N 374 
LEU   CD2    C  N N 375 
LEU   OXT    O  N N 376 
LEU   H      H  N N 377 
LEU   H2     H  N N 378 
LEU   HA     H  N N 379 
LEU   HB2    H  N N 380 
LEU   HB3    H  N N 381 
LEU   HG     H  N N 382 
LEU   HD11   H  N N 383 
LEU   HD12   H  N N 384 
LEU   HD13   H  N N 385 
LEU   HD21   H  N N 386 
LEU   HD22   H  N N 387 
LEU   HD23   H  N N 388 
LEU   HXT    H  N N 389 
LYS   N      N  N N 390 
LYS   CA     C  N S 391 
LYS   C      C  N N 392 
LYS   O      O  N N 393 
LYS   CB     C  N N 394 
LYS   CG     C  N N 395 
LYS   CD     C  N N 396 
LYS   CE     C  N N 397 
LYS   NZ     N  N N 398 
LYS   OXT    O  N N 399 
LYS   H      H  N N 400 
LYS   H2     H  N N 401 
LYS   HA     H  N N 402 
LYS   HB2    H  N N 403 
LYS   HB3    H  N N 404 
LYS   HG2    H  N N 405 
LYS   HG3    H  N N 406 
LYS   HD2    H  N N 407 
LYS   HD3    H  N N 408 
LYS   HE2    H  N N 409 
LYS   HE3    H  N N 410 
LYS   HZ1    H  N N 411 
LYS   HZ2    H  N N 412 
LYS   HZ3    H  N N 413 
LYS   HXT    H  N N 414 
MET   N      N  N N 415 
MET   CA     C  N S 416 
MET   C      C  N N 417 
MET   O      O  N N 418 
MET   CB     C  N N 419 
MET   CG     C  N N 420 
MET   SD     S  N N 421 
MET   CE     C  N N 422 
MET   OXT    O  N N 423 
MET   H      H  N N 424 
MET   H2     H  N N 425 
MET   HA     H  N N 426 
MET   HB2    H  N N 427 
MET   HB3    H  N N 428 
MET   HG2    H  N N 429 
MET   HG3    H  N N 430 
MET   HE1    H  N N 431 
MET   HE2    H  N N 432 
MET   HE3    H  N N 433 
MET   HXT    H  N N 434 
MG    MG     MG N N 435 
PHE   N      N  N N 436 
PHE   CA     C  N S 437 
PHE   C      C  N N 438 
PHE   O      O  N N 439 
PHE   CB     C  N N 440 
PHE   CG     C  Y N 441 
PHE   CD1    C  Y N 442 
PHE   CD2    C  Y N 443 
PHE   CE1    C  Y N 444 
PHE   CE2    C  Y N 445 
PHE   CZ     C  Y N 446 
PHE   OXT    O  N N 447 
PHE   H      H  N N 448 
PHE   H2     H  N N 449 
PHE   HA     H  N N 450 
PHE   HB2    H  N N 451 
PHE   HB3    H  N N 452 
PHE   HD1    H  N N 453 
PHE   HD2    H  N N 454 
PHE   HE1    H  N N 455 
PHE   HE2    H  N N 456 
PHE   HZ     H  N N 457 
PHE   HXT    H  N N 458 
PRO   N      N  N N 459 
PRO   CA     C  N S 460 
PRO   C      C  N N 461 
PRO   O      O  N N 462 
PRO   CB     C  N N 463 
PRO   CG     C  N N 464 
PRO   CD     C  N N 465 
PRO   OXT    O  N N 466 
PRO   H      H  N N 467 
PRO   HA     H  N N 468 
PRO   HB2    H  N N 469 
PRO   HB3    H  N N 470 
PRO   HG2    H  N N 471 
PRO   HG3    H  N N 472 
PRO   HD2    H  N N 473 
PRO   HD3    H  N N 474 
PRO   HXT    H  N N 475 
SER   N      N  N N 476 
SER   CA     C  N S 477 
SER   C      C  N N 478 
SER   O      O  N N 479 
SER   CB     C  N N 480 
SER   OG     O  N N 481 
SER   OXT    O  N N 482 
SER   H      H  N N 483 
SER   H2     H  N N 484 
SER   HA     H  N N 485 
SER   HB2    H  N N 486 
SER   HB3    H  N N 487 
SER   HG     H  N N 488 
SER   HXT    H  N N 489 
THR   N      N  N N 490 
THR   CA     C  N S 491 
THR   C      C  N N 492 
THR   O      O  N N 493 
THR   CB     C  N R 494 
THR   OG1    O  N N 495 
THR   CG2    C  N N 496 
THR   OXT    O  N N 497 
THR   H      H  N N 498 
THR   H2     H  N N 499 
THR   HA     H  N N 500 
THR   HB     H  N N 501 
THR   HG1    H  N N 502 
THR   HG21   H  N N 503 
THR   HG22   H  N N 504 
THR   HG23   H  N N 505 
THR   HXT    H  N N 506 
TRP   N      N  N N 507 
TRP   CA     C  N S 508 
TRP   C      C  N N 509 
TRP   O      O  N N 510 
TRP   CB     C  N N 511 
TRP   CG     C  Y N 512 
TRP   CD1    C  Y N 513 
TRP   CD2    C  Y N 514 
TRP   NE1    N  Y N 515 
TRP   CE2    C  Y N 516 
TRP   CE3    C  Y N 517 
TRP   CZ2    C  Y N 518 
TRP   CZ3    C  Y N 519 
TRP   CH2    C  Y N 520 
TRP   OXT    O  N N 521 
TRP   H      H  N N 522 
TRP   H2     H  N N 523 
TRP   HA     H  N N 524 
TRP   HB2    H  N N 525 
TRP   HB3    H  N N 526 
TRP   HD1    H  N N 527 
TRP   HE1    H  N N 528 
TRP   HE3    H  N N 529 
TRP   HZ2    H  N N 530 
TRP   HZ3    H  N N 531 
TRP   HH2    H  N N 532 
TRP   HXT    H  N N 533 
TYR   N      N  N N 534 
TYR   CA     C  N S 535 
TYR   C      C  N N 536 
TYR   O      O  N N 537 
TYR   CB     C  N N 538 
TYR   CG     C  Y N 539 
TYR   CD1    C  Y N 540 
TYR   CD2    C  Y N 541 
TYR   CE1    C  Y N 542 
TYR   CE2    C  Y N 543 
TYR   CZ     C  Y N 544 
TYR   OH     O  N N 545 
TYR   OXT    O  N N 546 
TYR   H      H  N N 547 
TYR   H2     H  N N 548 
TYR   HA     H  N N 549 
TYR   HB2    H  N N 550 
TYR   HB3    H  N N 551 
TYR   HD1    H  N N 552 
TYR   HD2    H  N N 553 
TYR   HE1    H  N N 554 
TYR   HE2    H  N N 555 
TYR   HH     H  N N 556 
TYR   HXT    H  N N 557 
VAL   N      N  N N 558 
VAL   CA     C  N S 559 
VAL   C      C  N N 560 
VAL   O      O  N N 561 
VAL   CB     C  N N 562 
VAL   CG1    C  N N 563 
VAL   CG2    C  N N 564 
VAL   OXT    O  N N 565 
VAL   H      H  N N 566 
VAL   H2     H  N N 567 
VAL   HA     H  N N 568 
VAL   HB     H  N N 569 
VAL   HG11   H  N N 570 
VAL   HG12   H  N N 571 
VAL   HG13   H  N N 572 
VAL   HG21   H  N N 573 
VAL   HG22   H  N N 574 
VAL   HG23   H  N N 575 
VAL   HXT    H  N N 576 
# 
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 
A1AOM C3    C2     sing N N 1   
A1AOM C1    C2     sing N N 2   
A1AOM C2    C4     sing N N 3   
A1AOM C34   N6     sing N N 4   
A1AOM O5    C5     doub N N 5   
A1AOM C4    C5     sing N N 6   
A1AOM C4    N6     sing N N 7   
A1AOM C5    N1     sing N N 8   
A1AOM N6    C35    sing N N 9   
A1AOM C8    N2     sing N N 10  
A1AOM C8    C9     sing N N 11  
A1AOM N1    C6     sing N N 12  
A1AOM O2    C12    doub N N 13  
A1AOM N5    N2     sing N N 14  
A1AOM N5    C11    sing N N 15  
A1AOM N2    C7     sing N N 16  
A1AOM C7    O3     doub N N 17  
A1AOM C7    C6     sing N N 18  
A1AOM C35   C36    sing N N 19  
A1AOM C35   O7     doub N N 20  
A1AOM C6    C21    sing N N 21  
A1AOM C36   C37    sing N N 22  
A1AOM C36   C40    sing N N 23  
A1AOM C12   C11    sing N N 24  
A1AOM C12   O1     sing N N 25  
A1AOM C10   C9     sing N N 26  
A1AOM C10   C11    sing N N 27  
A1AOM O4    C32    sing N N 28  
A1AOM C37   N7     sing N N 29  
A1AOM C33   C32    doub Y N 30  
A1AOM C33   C22    sing Y N 31  
A1AOM C32   C31    sing Y N 32  
A1AOM C13   O1     sing N N 33  
A1AOM C13   C14    sing N N 34  
A1AOM C40   N7     sing N N 35  
A1AOM C21   C22    sing N N 36  
A1AOM C22   C23    doub Y N 37  
A1AOM N7    C38    sing N N 38  
A1AOM C31   C24    doub Y N 39  
A1AOM C15   C14    sing N N 40  
A1AOM C16   C14    sing N N 41  
A1AOM C14   C17    sing N N 42  
A1AOM C23   C24    sing Y N 43  
A1AOM C24   C25    sing N N 44  
A1AOM C38   O6     doub N N 45  
A1AOM C38   C39    sing N N 46  
A1AOM C25   C26    doub Y N 47  
A1AOM C25   C30    sing Y N 48  
A1AOM C26   C27    sing Y N 49  
A1AOM C17   N3     sing N N 50  
A1AOM C30   C29    doub Y N 51  
A1AOM C27   N3     sing Y N 52  
A1AOM C27   C28    doub Y N 53  
A1AOM N3    C18    sing Y N 54  
A1AOM C28   C29    sing Y N 55  
A1AOM C28   C19    sing Y N 56  
A1AOM C18   C19    doub Y N 57  
A1AOM C19   C20    sing N N 58  
A1AOM C20   N4     trip N N 59  
A1AOM C1    H1     sing N N 60  
A1AOM C1    H2     sing N N 61  
A1AOM C1    H3     sing N N 62  
A1AOM C10   H4     sing N N 63  
A1AOM C10   H5     sing N N 64  
A1AOM C11   H6     sing N N 65  
A1AOM C13   H7     sing N N 66  
A1AOM C13   H8     sing N N 67  
A1AOM C15   H9     sing N N 68  
A1AOM C15   H10    sing N N 69  
A1AOM C15   H11    sing N N 70  
A1AOM C16   H12    sing N N 71  
A1AOM C16   H13    sing N N 72  
A1AOM C16   H14    sing N N 73  
A1AOM C17   H15    sing N N 74  
A1AOM C17   H16    sing N N 75  
A1AOM C18   H17    sing N N 76  
A1AOM C2    H18    sing N N 77  
A1AOM C21   H19    sing N N 78  
A1AOM C21   H20    sing N N 79  
A1AOM C23   H21    sing N N 80  
A1AOM C26   H22    sing N N 81  
A1AOM C29   H23    sing N N 82  
A1AOM C3    H24    sing N N 83  
A1AOM C3    H25    sing N N 84  
A1AOM C3    H26    sing N N 85  
A1AOM C30   H27    sing N N 86  
A1AOM C31   H28    sing N N 87  
A1AOM C33   H29    sing N N 88  
A1AOM C34   H30    sing N N 89  
A1AOM C34   H31    sing N N 90  
A1AOM C34   H32    sing N N 91  
A1AOM C36   H33    sing N N 92  
A1AOM C37   H34    sing N N 93  
A1AOM C37   H35    sing N N 94  
A1AOM C39   H36    sing N N 95  
A1AOM C39   H37    sing N N 96  
A1AOM C39   H38    sing N N 97  
A1AOM C4    H39    sing N N 98  
A1AOM C40   H40    sing N N 99  
A1AOM C40   H41    sing N N 100 
A1AOM C6    H42    sing N N 101 
A1AOM C8    H43    sing N N 102 
A1AOM C8    H44    sing N N 103 
A1AOM C9    H45    sing N N 104 
A1AOM C9    H46    sing N N 105 
A1AOM N1    H47    sing N N 106 
A1AOM N5    H48    sing N N 107 
A1AOM O4    H49    sing N N 108 
ALA   N     CA     sing N N 109 
ALA   N     H      sing N N 110 
ALA   N     H2     sing N N 111 
ALA   CA    C      sing N N 112 
ALA   CA    CB     sing N N 113 
ALA   CA    HA     sing N N 114 
ALA   C     O      doub N N 115 
ALA   C     OXT    sing N N 116 
ALA   CB    HB1    sing N N 117 
ALA   CB    HB2    sing N N 118 
ALA   CB    HB3    sing N N 119 
ALA   OXT   HXT    sing N N 120 
ARG   N     CA     sing N N 121 
ARG   N     H      sing N N 122 
ARG   N     H2     sing N N 123 
ARG   CA    C      sing N N 124 
ARG   CA    CB     sing N N 125 
ARG   CA    HA     sing N N 126 
ARG   C     O      doub N N 127 
ARG   C     OXT    sing N N 128 
ARG   CB    CG     sing N N 129 
ARG   CB    HB2    sing N N 130 
ARG   CB    HB3    sing N N 131 
ARG   CG    CD     sing N N 132 
ARG   CG    HG2    sing N N 133 
ARG   CG    HG3    sing N N 134 
ARG   CD    NE     sing N N 135 
ARG   CD    HD2    sing N N 136 
ARG   CD    HD3    sing N N 137 
ARG   NE    CZ     sing N N 138 
ARG   NE    HE     sing N N 139 
ARG   CZ    NH1    sing N N 140 
ARG   CZ    NH2    doub N N 141 
ARG   NH1   HH11   sing N N 142 
ARG   NH1   HH12   sing N N 143 
ARG   NH2   HH21   sing N N 144 
ARG   NH2   HH22   sing N N 145 
ARG   OXT   HXT    sing N N 146 
ASN   N     CA     sing N N 147 
ASN   N     H      sing N N 148 
ASN   N     H2     sing N N 149 
ASN   CA    C      sing N N 150 
ASN   CA    CB     sing N N 151 
ASN   CA    HA     sing N N 152 
ASN   C     O      doub N N 153 
ASN   C     OXT    sing N N 154 
ASN   CB    CG     sing N N 155 
ASN   CB    HB2    sing N N 156 
ASN   CB    HB3    sing N N 157 
ASN   CG    OD1    doub N N 158 
ASN   CG    ND2    sing N N 159 
ASN   ND2   HD21   sing N N 160 
ASN   ND2   HD22   sing N N 161 
ASN   OXT   HXT    sing N N 162 
ASP   N     CA     sing N N 163 
ASP   N     H      sing N N 164 
ASP   N     H2     sing N N 165 
ASP   CA    C      sing N N 166 
ASP   CA    CB     sing N N 167 
ASP   CA    HA     sing N N 168 
ASP   C     O      doub N N 169 
ASP   C     OXT    sing N N 170 
ASP   CB    CG     sing N N 171 
ASP   CB    HB2    sing N N 172 
ASP   CB    HB3    sing N N 173 
ASP   CG    OD1    doub N N 174 
ASP   CG    OD2    sing N N 175 
ASP   OD2   HD2    sing N N 176 
ASP   OXT   HXT    sing N N 177 
BTB   C1    O1     sing N N 178 
BTB   C1    C2     sing N N 179 
BTB   C1    H11    sing N N 180 
BTB   C1    H12    sing N N 181 
BTB   O1    HO1    sing N N 182 
BTB   C2    C3     sing N N 183 
BTB   C2    C4     sing N N 184 
BTB   C2    N      sing N N 185 
BTB   C3    O3     sing N N 186 
BTB   C3    H31    sing N N 187 
BTB   C3    H32    sing N N 188 
BTB   O3    HO3    sing N N 189 
BTB   C4    O4     sing N N 190 
BTB   C4    H41    sing N N 191 
BTB   C4    H42    sing N N 192 
BTB   O4    HO4    sing N N 193 
BTB   N     C5     sing N N 194 
BTB   N     C7     sing N N 195 
BTB   C5    C6     sing N N 196 
BTB   C5    H51    sing N N 197 
BTB   C5    H52    sing N N 198 
BTB   C6    O6     sing N N 199 
BTB   C6    H61    sing N N 200 
BTB   C6    H62    sing N N 201 
BTB   O6    HO6    sing N N 202 
BTB   C7    C8     sing N N 203 
BTB   C7    H71    sing N N 204 
BTB   C7    H72    sing N N 205 
BTB   C8    O8     sing N N 206 
BTB   C8    H81    sing N N 207 
BTB   C8    H82    sing N N 208 
BTB   O8    HO8    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 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BFW 
_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]   0.026874 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003753 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017218 
_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]   0.013294 
_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   ? 1.23400   43.72900  -9.05100  1.000 33.62415 ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 1   ? 1.28600   42.29200  -9.29700  1.000 32.63729 ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 1   ? -0.11900  41.70200  -9.37900  1.000 28.52103 ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 1   ? -1.08500  42.29600  -8.89200  1.000 31.75034 ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 1   ? 2.07300   41.58900  -8.19100  1.000 36.42938 ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? 1.37600   41.65300  -6.96000  1.000 38.93610 ? 0   SER   A OG    1 
ATOM   7    N  N     A MET   A 1 2   ? -0.23100  40.52700  -9.99500  0.500 24.47224 ? 1   MET   A N     1 
ATOM   8    N  N     B MET   A 1 2   ? -0.22800  40.53000  -9.99800  0.500 24.29833 ? 1   MET   A N     1 
ATOM   9    C  CA    A MET   A 1 2   ? -1.50100  39.82700  -10.13800 0.500 20.10016 ? 1   MET   A CA    1 
ATOM   10   C  CA    B MET   A 1 2   ? -1.49500  39.82600  -10.13500 0.500 19.75950 ? 1   MET   A CA    1 
ATOM   11   C  C     A MET   A 1 2   ? -1.38500  38.47200  -9.46100  0.500 16.53454 ? 1   MET   A C     1 
ATOM   12   C  C     B MET   A 1 2   ? -1.37000  38.47700  -9.44600  0.500 16.18039 ? 1   MET   A C     1 
ATOM   13   O  O     A MET   A 1 2   ? -0.57200  37.63500  -9.87000  0.500 17.44554 ? 1   MET   A O     1 
ATOM   14   O  O     B MET   A 1 2   ? -0.53600  37.65200  -9.83400  0.500 16.87504 ? 1   MET   A O     1 
ATOM   15   C  CB    A MET   A 1 2   ? -1.86900  39.65600  -11.61300 0.500 19.74329 ? 1   MET   A CB    1 
ATOM   16   C  CB    B MET   A 1 2   ? -1.85900  39.63300  -11.60700 0.500 19.34487 ? 1   MET   A CB    1 
ATOM   17   C  CG    A MET   A 1 2   ? -3.11500  38.82100  -11.84600 0.500 18.89896 ? 1   MET   A CG    1 
ATOM   18   C  CG    B MET   A 1 2   ? -3.24200  39.05100  -11.81700 0.500 18.20744 ? 1   MET   A CG    1 
ATOM   19   S  SD    A MET   A 1 2   ? -3.61100  38.76500  -13.57700 0.500 18.02319 ? 1   MET   A SD    1 
ATOM   20   S  SD    B MET   A 1 2   ? -3.62600  38.74300  -13.54800 0.500 17.14471 ? 1   MET   A SD    1 
ATOM   21   C  CE    A MET   A 1 2   ? -2.13800  38.07700  -14.32900 0.500 17.92531 ? 1   MET   A CE    1 
ATOM   22   C  CE    B MET   A 1 2   ? -3.16000  40.30500  -14.28200 0.500 17.00039 ? 1   MET   A CE    1 
ATOM   23   N  N     . THR   A 1 3   ? -2.19600  38.25700  -8.43000  1.000 14.51639 ? 2   THR   A N     1 
ATOM   24   C  CA    . THR   A 1 3   ? -2.19500  36.98200  -7.73100  1.000 13.34249 ? 2   THR   A CA    1 
ATOM   25   C  C     . THR   A 1 3   ? -2.87800  35.91700  -8.57900  1.000 11.92844 ? 2   THR   A C     1 
ATOM   26   O  O     . THR   A 1 3   ? -3.87100  36.18100  -9.26400  1.000 12.23965 ? 2   THR   A O     1 
ATOM   27   C  CB    . THR   A 1 3   ? -2.90400  37.14300  -6.38400  1.000 14.70582 ? 2   THR   A CB    1 
ATOM   28   O  OG1   . THR   A 1 3   ? -2.24600  38.16900  -5.63200  1.000 15.61032 ? 2   THR   A OG1   1 
ATOM   29   C  CG2   . THR   A 1 3   ? -2.87300  35.84800  -5.57800  1.000 15.32070 ? 2   THR   A CG2   1 
ATOM   30   N  N     A GLU   A 1 4   ? -2.33300  34.70800  -8.52800  0.500 12.66740 ? 3   GLU   A N     1 
ATOM   31   N  N     B GLU   A 1 4   ? -2.32200  34.71300  -8.54900  0.500 11.81804 ? 3   GLU   A N     1 
ATOM   32   C  CA    A GLU   A 1 4   ? -2.87200  33.55300  -9.22500  0.500 13.27481 ? 3   GLU   A CA    1 
ATOM   33   C  CA    B GLU   A 1 4   ? -2.88900  33.56300  -9.23300  0.500 11.79702 ? 3   GLU   A CA    1 
ATOM   34   C  C     A GLU   A 1 4   ? -3.53300  32.62700  -8.21300  0.500 12.35763 ? 3   GLU   A C     1 
ATOM   35   C  C     B GLU   A 1 4   ? -3.54300  32.64500  -8.21100  0.500 11.63591 ? 3   GLU   A C     1 
ATOM   36   O  O     A GLU   A 1 4   ? -3.00000  32.40800  -7.12000  0.500 13.93656 ? 3   GLU   A O     1 
ATOM   37   O  O     B GLU   A 1 4   ? -3.01700  32.45300  -7.10900  0.500 13.20442 ? 3   GLU   A O     1 
ATOM   38   C  CB    A GLU   A 1 4   ? -1.73900  32.80400  -9.92800  0.500 16.52373 ? 3   GLU   A CB    1 
ATOM   39   C  CB    B GLU   A 1 4   ? -1.79900  32.79800  -9.98800  0.500 13.99765 ? 3   GLU   A CB    1 
ATOM   40   C  CG    A GLU   A 1 4   ? -2.16900  31.61000  -10.75200 0.500 21.07099 ? 3   GLU   A CG    1 
ATOM   41   C  CG    B GLU   A 1 4   ? -2.28300  31.54200  -10.69300 0.500 18.27440 ? 3   GLU   A CG    1 
ATOM   42   C  CD    A GLU   A 1 4   ? -0.98300  30.80800  -11.24900 0.500 25.37032 ? 3   GLU   A CD    1 
ATOM   43   C  CD    B GLU   A 1 4   ? -1.18300  30.85800  -11.48300 0.500 22.20030 ? 3   GLU   A CD    1 
ATOM   44   O  OE1   A GLU   A 1 4   ? -0.25900  30.23500  -10.41100 0.500 27.44666 ? 3   GLU   A OE1   1 
ATOM   45   O  OE1   B GLU   A 1 4   ? -0.11100  31.47200  -11.67400 0.500 22.59980 ? 3   GLU   A OE1   1 
ATOM   46   O  OE2   A GLU   A 1 4   ? -0.76800  30.75800  -12.47700 0.500 25.79767 ? 3   GLU   A OE2   1 
ATOM   47   O  OE2   B GLU   A 1 4   ? -1.39000  29.70300  -11.90500 0.500 23.92898 ? 3   GLU   A OE2   1 
ATOM   48   N  N     . TYR   A 1 5   ? -4.69800  32.09400  -8.57700  1.000 10.75014 ? 4   TYR   A N     1 
ATOM   49   C  CA    . TYR   A 1 5   ? -5.44100  31.16200  -7.73600  1.000 10.93425 ? 4   TYR   A CA    1 
ATOM   50   C  C     . TYR   A 1 5   ? -5.64700  29.87000  -8.50800  1.000 10.72837 ? 4   TYR   A C     1 
ATOM   51   O  O     . TYR   A 1 5   ? -6.17800  29.88600  -9.62100  1.000 12.55752 ? 4   TYR   A O     1 
ATOM   52   C  CB    . TYR   A 1 5   ? -6.79800  31.75200  -7.32800  1.000 11.76051 ? 4   TYR   A CB    1 
ATOM   53   C  CG    . TYR   A 1 5   ? -6.65900  33.05600  -6.57600  1.000 11.41449 ? 4   TYR   A CG    1 
ATOM   54   C  CD1   . TYR   A 1 5   ? -6.45300  33.07300  -5.20000  1.000 13.66182 ? 4   TYR   A CD1   1 
ATOM   55   C  CD2   . TYR   A 1 5   ? -6.68400  34.27200  -7.24900  1.000 12.29661 ? 4   TYR   A CD2   1 
ATOM   56   C  CE1   . TYR   A 1 5   ? -6.30500  34.26800  -4.51100  1.000 13.85569 ? 4   TYR   A CE1   1 
ATOM   57   C  CE2   . TYR   A 1 5   ? -6.53700  35.47100  -6.56700  1.000 13.28434 ? 4   TYR   A CE2   1 
ATOM   58   C  CZ    . TYR   A 1 5   ? -6.34600  35.46100  -5.20300  1.000 13.70748 ? 4   TYR   A CZ    1 
ATOM   59   O  OH    . TYR   A 1 5   ? -6.18900  36.65400  -4.53700  1.000 16.59433 ? 4   TYR   A OH    1 
ATOM   60   N  N     . LYS   A 1 6   ? -5.22900  28.75900  -7.92000  1.000 10.20546 ? 5   LYS   A N     1 
ATOM   61   C  CA    . LYS   A 1 6   ? -5.35100  27.44500  -8.54800  1.000 10.55956 ? 5   LYS   A CA    1 
ATOM   62   C  C     . LYS   A 1 6   ? -6.61200  26.76600  -8.02700  1.000 9.62080  ? 5   LYS   A C     1 
ATOM   63   O  O     . LYS   A 1 6   ? -6.66300  26.33200  -6.86900  1.000 9.94002  ? 5   LYS   A O     1 
ATOM   64   C  CB    . LYS   A 1 6   ? -4.10000  26.61200  -8.28800  1.000 12.60256 ? 5   LYS   A CB    1 
ATOM   65   C  CG    . LYS   A 1 6   ? -2.86800  27.22100  -8.93900  1.000 15.74891 ? 5   LYS   A CG    1 
ATOM   66   C  CD    . LYS   A 1 6   ? -1.60900  26.41600  -8.68200  1.000 18.67278 ? 5   LYS   A CD    1 
ATOM   67   C  CE    . LYS   A 1 6   ? -0.39800  27.07000  -9.34400  1.000 21.61120 ? 5   LYS   A CE    1 
ATOM   68   N  NZ    . LYS   A 1 6   ? 0.86400   26.31400  -9.12400  1.000 25.12168 ? 5   LYS   A NZ    1 
ATOM   69   N  N     . LEU   A 1 7   ? -7.62900  26.68900  -8.88200  1.000 9.06302  ? 6   LEU   A N     1 
ATOM   70   C  CA    . LEU   A 1 7   ? -8.94100  26.16600  -8.52000  1.000 8.47398  ? 6   LEU   A CA    1 
ATOM   71   C  C     . LEU   A 1 7   ? -9.15100  24.83100  -9.21800  1.000 8.83902  ? 6   LEU   A C     1 
ATOM   72   O  O     . LEU   A 1 7   ? -8.82600  24.69100  -10.40200 1.000 12.07727 ? 6   LEU   A O     1 
ATOM   73   C  CB    . LEU   A 1 7   ? -10.03900 27.13300  -8.97200  1.000 8.92830  ? 6   LEU   A CB    1 
ATOM   74   C  CG    . LEU   A 1 7   ? -9.80700  28.61300  -8.66600  1.000 9.42671  ? 6   LEU   A CG    1 
ATOM   75   C  CD1   . LEU   A 1 7   ? -11.01600 29.42300  -9.10100  1.000 10.41878 ? 6   LEU   A CD1   1 
ATOM   76   C  CD2   . LEU   A 1 7   ? -9.51900  28.80900  -7.19300  1.000 10.36130 ? 6   LEU   A CD2   1 
ATOM   77   N  N     . VAL   A 1 8   ? -9.70100  23.85500  -8.49900  1.000 8.15344  ? 7   VAL   A N     1 
ATOM   78   C  CA    . VAL   A 1 8   ? -9.87700  22.50500  -9.02200  1.000 7.82822  ? 7   VAL   A CA    1 
ATOM   79   C  C     . VAL   A 1 8   ? -11.34800 22.12800  -8.89200  1.000 7.40699  ? 7   VAL   A C     1 
ATOM   80   O  O     . VAL   A 1 8   ? -11.94200 22.29200  -7.81900  1.000 8.70550  ? 7   VAL   A O     1 
ATOM   81   C  CB    . VAL   A 1 8   ? -8.97400  21.49200  -8.28900  1.000 8.06415  ? 7   VAL   A CB    1 
ATOM   82   C  CG1   . VAL   A 1 8   ? -9.11500  20.11400  -8.90800  1.000 8.98513  ? 7   VAL   A CG1   1 
ATOM   83   C  CG2   . VAL   A 1 8   ? -7.51300  21.94200  -8.32100  1.000 9.92819  ? 7   VAL   A CG2   1 
ATOM   84   N  N     . VAL   A 1 9   ? -11.92800 21.62000  -9.97900  1.000 7.41821  ? 8   VAL   A N     1 
ATOM   85   C  CA    . VAL   A 1 9   ? -13.34600 21.27700  -10.05500 1.000 7.56366  ? 8   VAL   A CA    1 
ATOM   86   C  C     . VAL   A 1 9   ? -13.45400 19.75500  -10.04100 1.000 6.79780  ? 8   VAL   A C     1 
ATOM   87   O  O     . VAL   A 1 9   ? -12.89300 19.08900  -10.92100 1.000 7.65134  ? 8   VAL   A O     1 
ATOM   88   C  CB    . VAL   A 1 9   ? -13.99300 21.87200  -11.31700 1.000 7.65808  ? 8   VAL   A CB    1 
ATOM   89   C  CG1   . VAL   A 1 9   ? -15.49100 21.65500  -11.28800 1.000 8.18609  ? 8   VAL   A CG1   1 
ATOM   90   C  CG2   . VAL   A 1 9   ? -13.67500 23.36600  -11.43900 1.000 8.84874  ? 8   VAL   A CG2   1 
ATOM   91   N  N     . VAL   A 1 10  ? -14.15200 19.20500  -9.03200  1.000 7.05195  ? 9   VAL   A N     1 
ATOM   92   C  CA    . VAL   A 1 10  ? -14.25800 17.76000  -8.83400  1.000 7.13376  ? 9   VAL   A CA    1 
ATOM   93   C  C     . VAL   A 1 10  ? -15.71800 17.36300  -8.63500  1.000 7.05999  ? 9   VAL   A C     1 
ATOM   94   O  O     . VAL   A 1 10  ? -16.56300 18.18700  -8.27500  1.000 7.70017  ? 9   VAL   A O     1 
ATOM   95   C  CB    . VAL   A 1 10  ? -13.39500 17.25400  -7.64900  1.000 7.36045  ? 9   VAL   A CB    1 
ATOM   96   C  CG1   . VAL   A 1 10  ? -11.94900 17.70600  -7.80600  1.000 8.92306  ? 9   VAL   A CG1   1 
ATOM   97   C  CG2   . VAL   A 1 10  ? -13.96800 17.70600  -6.30300  1.000 8.88271  ? 9   VAL   A CG2   1 
ATOM   98   N  N     . GLY   A 1 11  ? -16.00000 16.08400  -8.85600  1.000 7.08975  ? 10  GLY   A N     1 
ATOM   99   C  CA    . GLY   A 1 11  ? -17.34200 15.54900  -8.69700  1.000 7.64153  ? 10  GLY   A CA    1 
ATOM   100  C  C     . GLY   A 1 11  ? -17.59300 14.42400  -9.68000  1.000 7.32292  ? 10  GLY   A C     1 
ATOM   101  O  O     . GLY   A 1 11  ? -16.81100 14.17500  -10.59800 1.000 7.47715  ? 10  GLY   A O     1 
ATOM   102  N  N     . ALA   A 1 12  ? -18.70900 13.72900  -9.47000  1.000 7.75178  ? 11  ALA   A N     1 
ATOM   103  C  CA    . ALA   A 1 12  ? -19.04200 12.53100  -10.23700 1.000 8.16771  ? 11  ALA   A CA    1 
ATOM   104  C  C     . ALA   A 1 12  ? -19.28000 12.83500  -11.72300 1.000 7.82471  ? 11  ALA   A C     1 
ATOM   105  O  O     . ALA   A 1 12  ? -19.45800 13.98200  -12.14100 1.000 8.28714  ? 11  ALA   A O     1 
ATOM   106  C  CB    . ALA   A 1 12  ? -20.28700 11.87000  -9.64600  1.000 9.37521  ? 11  ALA   A CB    1 
ATOM   107  N  N     . CYS   A 1 13  ? -19.32300 11.76200  -12.51800 1.000 8.29618  ? 12  CYS   A N     1 
ATOM   108  C  CA    . CYS   A 1 13  ? -19.53700 11.88300  -13.95700 1.000 9.11271  ? 12  CYS   A CA    1 
ATOM   109  C  C     . CYS   A 1 13  ? -20.80800 12.64800  -14.27300 1.000 8.40551  ? 12  CYS   A C     1 
ATOM   110  O  O     . CYS   A 1 13  ? -21.87100 12.36900  -13.71400 1.000 8.85203  ? 12  CYS   A O     1 
ATOM   111  C  CB    . CYS   A 1 13  ? -19.71200 10.49300  -14.55900 1.000 12.86108 ? 12  CYS   A CB    1 
ATOM   112  S  SG    . CYS   A 1 13  ? -18.23400 9.56800   -14.83000 1.000 15.13195 ? 12  CYS   A SG    1 
ATOM   113  N  N     . GLY   A 1 14  ? -20.70700 13.57300  -15.22400 1.000 8.02485  ? 13  GLY   A N     1 
ATOM   114  C  CA    . GLY   A 1 14  ? -21.87000 14.17800  -15.83600 1.000 8.38227  ? 13  GLY   A CA    1 
ATOM   115  C  C     . GLY   A 1 14  ? -22.54500 15.26700  -15.03300 1.000 8.31896  ? 13  GLY   A C     1 
ATOM   116  O  O     . GLY   A 1 14  ? -23.58800 15.77400  -15.46400 1.000 9.23349  ? 13  GLY   A O     1 
ATOM   117  N  N     . VAL   A 1 15  ? -21.98400 15.66400  -13.88500 1.000 7.61240  ? 14  VAL   A N     1 
ATOM   118  C  CA    . VAL   A 1 15  ? -22.65000 16.64900  -13.03800 1.000 7.30926  ? 14  VAL   A CA    1 
ATOM   119  C  C     . VAL   A 1 15  ? -22.58800 18.05200  -13.61200 1.000 7.02639  ? 14  VAL   A C     1 
ATOM   120  O  O     . VAL   A 1 15  ? -23.35100 18.91900  -13.16900 1.000 7.75802  ? 14  VAL   A O     1 
ATOM   121  C  CB    . VAL   A 1 15  ? -22.11800 16.63400  -11.59100 1.000 8.00075  ? 14  VAL   A CB    1 
ATOM   122  C  CG1   . VAL   A 1 15  ? -22.37300 15.28800  -10.95000 1.000 8.44437  ? 14  VAL   A CG1   1 
ATOM   123  C  CG2   . VAL   A 1 15  ? -20.64400 17.02200  -11.52900 1.000 8.65564  ? 14  VAL   A CG2   1 
ATOM   124  N  N     . GLY   A 1 16  ? -21.68100 18.30200  -14.54900 1.000 7.45501  ? 15  GLY   A N     1 
ATOM   125  C  CA    . GLY   A 1 16  ? -21.50400 19.59800  -15.16100 1.000 7.60644  ? 15  GLY   A CA    1 
ATOM   126  C  C     . GLY   A 1 16  ? -20.22000 20.32700  -14.81200 1.000 7.45101  ? 15  GLY   A C     1 
ATOM   127  O  O     . GLY   A 1 16  ? -20.17500 21.55800  -14.95600 1.000 8.20749  ? 15  GLY   A O     1 
ATOM   128  N  N     . LYS   A 1 17  ? -19.17500 19.61700  -14.38000 1.000 7.28045  ? 16  LYS   A N     1 
ATOM   129  C  CA    . LYS   A 1 17  ? -17.90200 20.26700  -14.07600 1.000 7.41309  ? 16  LYS   A CA    1 
ATOM   130  C  C     . LYS   A 1 17  ? -17.38400 21.05000  -15.27500 1.000 7.36019  ? 16  LYS   A C     1 
ATOM   131  O  O     . LYS   A 1 17  ? -16.98100 22.21600  -15.15200 1.000 7.80045  ? 16  LYS   A O     1 
ATOM   132  C  CB    . LYS   A 1 17  ? -16.87400 19.21200  -13.66800 1.000 8.01853  ? 16  LYS   A CB    1 
ATOM   133  C  CG    . LYS   A 1 17  ? -17.27400 18.43600  -12.42700 1.000 8.79561  ? 16  LYS   A CG    1 
ATOM   134  C  CD    . LYS   A 1 17  ? -16.23500 17.39900  -11.99700 1.000 9.94851  ? 16  LYS   A CD    1 
ATOM   135  C  CE    . LYS   A 1 17  ? -16.05100 16.28200  -13.01000 1.000 9.81430  ? 16  LYS   A CE    1 
ATOM   136  N  NZ    . LYS   A 1 17  ? -17.28000 15.47200  -13.22000 1.000 8.41744  ? 16  LYS   A NZ    1 
ATOM   137  N  N     . SER   A 1 18  ? -17.37700 20.41600  -16.44600 1.000 7.69968  ? 17  SER   A N     1 
ATOM   138  C  CA    . SER   A 1 18  ? -16.84100 21.06700  -17.63400 1.000 8.02045  ? 17  SER   A CA    1 
ATOM   139  C  C     . SER   A 1 18  ? -17.75500 22.18100  -18.11600 1.000 7.90875  ? 17  SER   A C     1 
ATOM   140  O  O     . SER   A 1 18  ? -17.27900 23.24500  -18.51700 1.000 8.60031  ? 17  SER   A O     1 
ATOM   141  C  CB    . SER   A 1 18  ? -16.61400 20.03800  -18.73900 1.000 8.22214  ? 17  SER   A CB    1 
ATOM   142  O  OG    . SER   A 1 18  ? -15.67200 19.06100  -18.32000 1.000 8.05298  ? 17  SER   A OG    1 
ATOM   143  N  N     . ALA   A 1 19  ? -19.07000 21.95800  -18.08400 1.000 8.03013  ? 18  ALA   A N     1 
ATOM   144  C  CA    . ALA   A 1 19  ? -19.99400 22.99700  -18.51700 1.000 8.88852  ? 18  ALA   A CA    1 
ATOM   145  C  C     . ALA   A 1 19  ? -19.87400 24.23900  -17.64000 1.000 7.78243  ? 18  ALA   A C     1 
ATOM   146  O  O     . ALA   A 1 19  ? -19.94100 25.36800  -18.14400 1.000 8.35951  ? 18  ALA   A O     1 
ATOM   147  C  CB    . ALA   A 1 19  ? -21.42300 22.46100  -18.52600 1.000 9.62401  ? 18  ALA   A CB    1 
ATOM   148  N  N     . LEU   A 1 20  ? -19.68300 24.05400  -16.32800 1.000 7.97727  ? 19  LEU   A N     1 
ATOM   149  C  CA    . LEU   A 1 20  ? -19.48300 25.19700  -15.44300 1.000 8.46078  ? 19  LEU   A CA    1 
ATOM   150  C  C     . LEU   A 1 20  ? -18.19800 25.92900  -15.79300 1.000 8.48502  ? 19  LEU   A C     1 
ATOM   151  O  O     . LEU   A 1 20  ? -18.17600 27.16400  -15.89200 1.000 9.18198  ? 19  LEU   A O     1 
ATOM   152  C  CB    . LEU   A 1 20  ? -19.44400 24.72600  -13.99000 1.000 9.43236  ? 19  LEU   A CB    1 
ATOM   153  C  CG    . LEU   A 1 20  ? -20.78500 24.32600  -13.37100 1.000 8.90882  ? 19  LEU   A CG    1 
ATOM   154  C  CD1   . LEU   A 1 20  ? -20.57600 23.58800  -12.06300 1.000 10.25117 ? 19  LEU   A CD1   1 
ATOM   155  C  CD2   . LEU   A 1 20  ? -21.67500 25.55600  -13.16500 1.000 10.36488 ? 19  LEU   A CD2   1 
ATOM   156  N  N     . THR   A 1 21  ? -17.11400 25.17400  -15.99600 1.000 8.42723  ? 20  THR   A N     1 
ATOM   157  C  CA    . THR   A 1 21  ? -15.82700 25.76200  -16.34200 1.000 8.83219  ? 20  THR   A CA    1 
ATOM   158  C  C     . THR   A 1 21  ? -15.90200 26.51200  -17.66800 1.000 9.13189  ? 20  THR   A C     1 
ATOM   159  O  O     . THR   A 1 21  ? -15.40400 27.64000  -17.78200 1.000 10.21898 ? 20  THR   A O     1 
ATOM   160  C  CB    . THR   A 1 21  ? -14.78100 24.64600  -16.41200 1.000 9.68107  ? 20  THR   A CB    1 
ATOM   161  O  OG1   . THR   A 1 21  ? -14.68000 24.00300  -15.13300 1.000 10.33454 ? 20  THR   A OG1   1 
ATOM   162  C  CG2   . THR   A 1 21  ? -13.41900 25.19000  -16.80200 1.000 11.30755 ? 20  THR   A CG2   1 
ATOM   163  N  N     . ILE   A 1 22  ? -16.53600 25.90800  -18.68000 1.000 9.36193  ? 21  ILE   A N     1 
ATOM   164  C  CA    . ILE   A 1 22  ? -16.64900 26.54500  -19.99200 1.000 10.46472 ? 21  ILE   A CA    1 
ATOM   165  C  C     . ILE   A 1 22  ? -17.53800 27.78200  -19.93800 1.000 10.92046 ? 21  ILE   A C     1 
ATOM   166  O  O     . ILE   A 1 22  ? -17.29300 28.76200  -20.65200 1.000 11.12418 ? 21  ILE   A O     1 
ATOM   167  C  CB    . ILE   A 1 22  ? -17.10400 25.51500  -21.04400 1.000 11.76650 ? 21  ILE   A CB    1 
ATOM   168  C  CG1   . ILE   A 1 22  ? -16.00700 24.46900  -21.26500 1.000 13.12919 ? 21  ILE   A CG1   1 
ATOM   169  C  CG2   . ILE   A 1 22  ? -17.44900 26.18700  -22.37500 1.000 13.95838 ? 21  ILE   A CG2   1 
ATOM   170  C  CD1   . ILE   A 1 22  ? -14.68600 25.05000  -21.71700 1.000 17.76647 ? 21  ILE   A CD1   1 
ATOM   171  N  N     . GLN   A 1 23  ? -18.57500 27.78200  -19.09800 1.000 9.74882  ? 22  GLN   A N     1 
ATOM   172  C  CA    . GLN   A 1 23  ? -19.32200 29.02200  -18.90900 1.000 11.62616 ? 22  GLN   A CA    1 
ATOM   173  C  C     . GLN   A 1 23  ? -18.42500 30.12900  -18.37600 1.000 12.32826 ? 22  GLN   A C     1 
ATOM   174  O  O     . GLN   A 1 23  ? -18.48900 31.27000  -18.84400 1.000 13.97184 ? 22  GLN   A O     1 
ATOM   175  C  CB    . GLN   A 1 23  ? -20.50300 28.81300  -17.97000 1.000 12.34804 ? 22  GLN   A CB    1 
ATOM   176  C  CG    . GLN   A 1 23  ? -21.77600 28.44500  -18.67500 1.000 12.85072 ? 22  GLN   A CG    1 
ATOM   177  C  CD    . GLN   A 1 23  ? -22.39800 29.58600  -19.48000 1.000 13.29887 ? 22  GLN   A CD    1 
ATOM   178  O  OE1   . GLN   A 1 23  ? -21.76300 30.60100  -19.80000 1.000 15.45430 ? 22  GLN   A OE1   1 
ATOM   179  N  NE2   . GLN   A 1 23  ? -23.64500 29.39400  -19.84400 1.000 12.90095 ? 22  GLN   A NE2   1 
ATOM   180  N  N     . LEU   A 1 24  ? -17.57800 29.81200  -17.39800 1.000 11.52550 ? 23  LEU   A N     1 
ATOM   181  C  CA    . LEU   A 1 24  ? -16.66500 30.81200  -16.85900 1.000 13.02657 ? 23  LEU   A CA    1 
ATOM   182  C  C     . LEU   A 1 24  ? -15.65700 31.27900  -17.90900 1.000 13.54828 ? 23  LEU   A C     1 
ATOM   183  O  O     . LEU   A 1 24  ? -15.39200 32.48200  -18.03200 1.000 15.37902 ? 23  LEU   A O     1 
ATOM   184  C  CB    . LEU   A 1 24  ? -15.94700 30.25200  -15.63700 1.000 13.62617 ? 23  LEU   A CB    1 
ATOM   185  C  CG    . LEU   A 1 24  ? -15.12500 31.30300  -14.91100 1.000 17.20442 ? 23  LEU   A CG    1 
ATOM   186  C  CD1   . LEU   A 1 24  ? -16.02200 32.19600  -14.06500 1.000 19.28561 ? 23  LEU   A CD1   1 
ATOM   187  C  CD2   . LEU   A 1 24  ? -14.12200 30.62800  -14.06200 1.000 19.01354 ? 23  LEU   A CD2   1 
ATOM   188  N  N     . ILE   A 1 25  ? -15.07800 30.34500  -18.66900 1.000 14.07703 ? 24  ILE   A N     1 
ATOM   189  C  CA    . ILE   A 1 25  ? -13.97100 30.66800  -19.57200 1.000 14.44319 ? 24  ILE   A CA    1 
ATOM   190  C  C     . ILE   A 1 25  ? -14.48000 31.23900  -20.89400 1.000 15.58504 ? 24  ILE   A C     1 
ATOM   191  O  O     . ILE   A 1 25  ? -13.90300 32.19300  -21.43200 1.000 17.24016 ? 24  ILE   A O     1 
ATOM   192  C  CB    . ILE   A 1 25  ? -13.07700 29.43000  -19.80100 1.000 15.14548 ? 24  ILE   A CB    1 
ATOM   193  C  CG1   . ILE   A 1 25  ? -12.50800 28.88500  -18.48400 1.000 15.84817 ? 24  ILE   A CG1   1 
ATOM   194  C  CG2   . ILE   A 1 25  ? -11.95900 29.74200  -20.79600 1.000 16.95090 ? 24  ILE   A CG2   1 
ATOM   195  C  CD1   . ILE   A 1 25  ? -11.63300 29.84000  -17.73900 1.000 16.21251 ? 24  ILE   A CD1   1 
ATOM   196  N  N     . GLN   A 1 26  ? -15.54800 30.65300  -21.44900 1.000 15.88462 ? 25  GLN   A N     1 
ATOM   197  C  CA    . GLN   A 1 26  ? -15.98500 30.92600  -22.81400 1.000 15.85784 ? 25  GLN   A CA    1 
ATOM   198  C  C     . GLN   A 1 26  ? -17.40500 31.47100  -22.92300 1.000 16.24736 ? 25  GLN   A C     1 
ATOM   199  O  O     . GLN   A 1 26  ? -17.85800 31.73700  -24.04100 1.000 18.41696 ? 25  GLN   A O     1 
ATOM   200  C  CB    . GLN   A 1 26  ? -15.84900 29.66400  -23.68500 1.000 16.74128 ? 25  GLN   A CB    1 
ATOM   201  C  CG    . GLN   A 1 26  ? -14.42700 29.12100  -23.78800 1.000 18.40231 ? 25  GLN   A CG    1 
ATOM   202  C  CD    . GLN   A 1 26  ? -14.33800 27.84500  -24.60900 1.000 19.25675 ? 25  GLN   A CD    1 
ATOM   203  O  OE1   . GLN   A 1 26  ? -15.29500 27.44900  -25.27900 1.000 20.18017 ? 25  GLN   A OE1   1 
ATOM   204  N  NE2   . GLN   A 1 26  ? -13.18000 27.19500  -24.56400 1.000 20.70797 ? 25  GLN   A NE2   1 
ATOM   205  N  N     . ASN   A 1 27  ? -18.12900 31.61700  -21.81200 1.000 16.09824 ? 26  ASN   A N     1 
ATOM   206  C  CA    . ASN   A 1 27  ? -19.42000 32.31500  -21.79400 1.000 16.28662 ? 26  ASN   A CA    1 
ATOM   207  C  C     . ASN   A 1 27  ? -20.46500 31.68700  -22.71600 1.000 15.54889 ? 26  ASN   A C     1 
ATOM   208  O  O     . ASN   A 1 27  ? -21.24800 32.38400  -23.36300 1.000 17.31558 ? 26  ASN   A O     1 
ATOM   209  C  CB    . ASN   A 1 27  ? -19.25900 33.81000  -22.06300 1.000 20.20482 ? 26  ASN   A CB    1 
ATOM   210  C  CG    . ASN   A 1 27  ? -18.38100 34.47500  -21.04000 1.000 24.23138 ? 26  ASN   A CG    1 
ATOM   211  O  OD1   . ASN   A 1 27  ? -18.81900 34.76500  -19.93000 1.000 26.95151 ? 26  ASN   A OD1   1 
ATOM   212  N  ND2   . ASN   A 1 27  ? -17.12500 34.70700  -21.39900 1.000 27.23091 ? 26  ASN   A ND2   1 
ATOM   213  N  N     . HIS   A 1 28  ? -20.48900 30.35900  -22.77900 1.000 14.20406 ? 27  HIS   A N     1 
ATOM   214  C  CA    . HIS   A 1 28  ? -21.56100 29.68200  -23.49100 1.000 13.97100 ? 27  HIS   A CA    1 
ATOM   215  C  C     . HIS   A 1 28  ? -21.76900 28.30900  -22.87000 1.000 12.94897 ? 27  HIS   A C     1 
ATOM   216  O  O     . HIS   A 1 28  ? -20.94200 27.82100  -22.09100 1.000 12.73070 ? 27  HIS   A O     1 
ATOM   217  C  CB    . HIS   A 1 28  ? -21.28700 29.56400  -24.99500 1.000 17.48787 ? 27  HIS   A CB    1 
ATOM   218  C  CG    . HIS   A 1 28  ? -20.15300 28.65000  -25.32000 1.000 20.25297 ? 27  HIS   A CG    1 
ATOM   219  N  ND1   . HIS   A 1 28  ? -20.33700 27.35200  -25.74500 1.000 22.41914 ? 27  HIS   A ND1   1 
ATOM   220  C  CD2   . HIS   A 1 28  ? -18.81500 28.83900  -25.25500 1.000 20.10157 ? 27  HIS   A CD2   1 
ATOM   221  C  CE1   . HIS   A 1 28  ? -19.15900 26.78400  -25.93800 1.000 20.70780 ? 27  HIS   A CE1   1 
ATOM   222  N  NE2   . HIS   A 1 28  ? -18.21900 27.66500  -25.64500 1.000 22.12932 ? 27  HIS   A NE2   1 
ATOM   223  N  N     A PHE   A 1 29  ? -22.86700 27.67500  -23.28700 0.500 12.85777 ? 28  PHE   A N     1 
ATOM   224  N  N     B PHE   A 1 29  ? -22.90700 27.70300  -23.18100 0.500 13.40745 ? 28  PHE   A N     1 
ATOM   225  C  CA    A PHE   A 1 29  ? -23.27700 26.34700  -22.85200 0.500 11.90057 ? 28  PHE   A CA    1 
ATOM   226  C  CA    B PHE   A 1 29  ? -23.29600 26.43900  -22.56800 0.500 13.42280 ? 28  PHE   A CA    1 
ATOM   227  C  C     A PHE   A 1 29  ? -23.78200 25.56700  -24.05800 0.500 12.46085 ? 28  PHE   A C     1 
ATOM   228  C  C     B PHE   A 1 29  ? -23.05100 25.29100  -23.53600 0.500 16.06968 ? 28  PHE   A C     1 
ATOM   229  O  O     A PHE   A 1 29  ? -24.48900 26.11800  -24.90700 0.500 15.10855 ? 28  PHE   A O     1 
ATOM   230  O  O     B PHE   A 1 29  ? -23.49800 25.33900  -24.68400 0.500 16.63392 ? 28  PHE   A O     1 
ATOM   231  C  CB    A PHE   A 1 29  ? -24.41500 26.45800  -21.83200 0.500 11.48884 ? 28  PHE   A CB    1 
ATOM   232  C  CB    B PHE   A 1 29  ? -24.76600 26.46600  -22.14900 0.500 11.68821 ? 28  PHE   A CB    1 
ATOM   233  C  CG    A PHE   A 1 29  ? -25.06500 25.14200  -21.49400 0.500 10.72165 ? 28  PHE   A CG    1 
ATOM   234  C  CG    B PHE   A 1 29  ? -25.28500 25.13400  -21.67500 0.500 11.94930 ? 28  PHE   A CG    1 
ATOM   235  C  CD1   A PHE   A 1 29  ? -24.51700 24.30900  -20.52900 0.500 10.36389 ? 28  PHE   A CD1   1 
ATOM   236  C  CD1   B PHE   A 1 29  ? -24.70700 24.49200  -20.58800 0.500 12.53896 ? 28  PHE   A CD1   1 
ATOM   237  C  CD2   A PHE   A 1 29  ? -26.23800 24.75000  -22.12000 0.500 12.44511 ? 28  PHE   A CD2   1 
ATOM   238  C  CD2   B PHE   A 1 29  ? -26.36300 24.53100  -22.30800 0.500 13.52941 ? 28  PHE   A CD2   1 
ATOM   239  C  CE1   A PHE   A 1 29  ? -25.12200 23.10000  -20.20300 0.500 10.65171 ? 28  PHE   A CE1   1 
ATOM   240  C  CE1   B PHE   A 1 29  ? -25.19300 23.27000  -20.14300 0.500 12.77013 ? 28  PHE   A CE1   1 
ATOM   241  C  CE2   A PHE   A 1 29  ? -26.84500 23.54700  -21.80500 0.500 12.29708 ? 28  PHE   A CE2   1 
ATOM   242  C  CE2   B PHE   A 1 29  ? -26.85200 23.31200  -21.87000 0.500 13.74798 ? 28  PHE   A CE2   1 
ATOM   243  C  CZ    A PHE   A 1 29  ? -26.28800 22.72000  -20.84600 0.500 11.50934 ? 28  PHE   A CZ    1 
ATOM   244  C  CZ    B PHE   A 1 29  ? -26.26600 22.67900  -20.78700 0.500 13.22689 ? 28  PHE   A CZ    1 
ATOM   245  N  N     A VAL   A 1 30  ? -23.42800 24.28200  -24.12700 0.500 12.39077 ? 29  VAL   A N     1 
ATOM   246  N  N     B VAL   A 1 30  ? -22.34900 24.26200  -23.06900 0.500 17.53153 ? 29  VAL   A N     1 
ATOM   247  C  CA    A VAL   A 1 30  ? -23.91600 23.38300  -25.16500 0.500 14.86441 ? 29  VAL   A CA    1 
ATOM   248  C  CA    B VAL   A 1 30  ? -22.12600 23.04900  -23.85200 0.500 19.44109 ? 29  VAL   A CA    1 
ATOM   249  C  C     A VAL   A 1 30  ? -24.45200 22.11800  -24.51600 0.500 13.64914 ? 29  VAL   A C     1 
ATOM   250  C  C     B VAL   A 1 30  ? -23.26600 22.07400  -23.56000 0.500 19.74582 ? 29  VAL   A C     1 
ATOM   251  O  O     A VAL   A 1 30  ? -24.01400 21.71600  -23.43300 0.500 13.75174 ? 29  VAL   A O     1 
ATOM   252  O  O     B VAL   A 1 30  ? -23.41400 21.59200  -22.43500 0.500 20.07117 ? 29  VAL   A O     1 
ATOM   253  C  CB    A VAL   A 1 30  ? -22.83500 23.03400  -26.21300 0.500 17.61160 ? 29  VAL   A CB    1 
ATOM   254  C  CB    B VAL   A 1 30  ? -20.75100 22.42600  -23.56400 0.500 21.47865 ? 29  VAL   A CB    1 
ATOM   255  C  CG1   A VAL   A 1 30  ? -22.37900 24.27900  -26.93100 0.500 19.08668 ? 29  VAL   A CG1   1 
ATOM   256  C  CG1   B VAL   A 1 30  ? -19.63600 23.27500  -24.15900 0.500 21.44326 ? 29  VAL   A CG1   1 
ATOM   257  C  CG2   A VAL   A 1 30  ? -21.65600 22.34700  -25.55500 0.500 18.33392 ? 29  VAL   A CG2   1 
ATOM   258  C  CG2   B VAL   A 1 30  ? -20.52200 22.25100  -22.07100 0.500 23.36156 ? 29  VAL   A CG2   1 
ATOM   259  N  N     A ASP   A 1 31  ? -25.41800 21.49100  -25.18700 0.500 12.81272 ? 30  ASP   A N     1 
ATOM   260  N  N     B ASP   A 1 31  ? -24.08500 21.79300  -24.57600 0.500 20.81201 ? 30  ASP   A N     1 
ATOM   261  C  CA    A ASP   A 1 31  ? -25.93800 20.21900  -24.71100 0.500 13.29256 ? 30  ASP   A CA    1 
ATOM   262  C  CA    B ASP   A 1 31  ? -25.17500 20.82500  -24.46600 0.500 21.47865 ? 30  ASP   A CA    1 
ATOM   263  C  C     A ASP   A 1 31  ? -24.97900 19.06600  -24.97400 0.500 13.62789 ? 30  ASP   A C     1 
ATOM   264  C  C     B ASP   A 1 31  ? -24.69800 19.40000  -24.74700 0.500 19.82230 ? 30  ASP   A C     1 
ATOM   265  O  O     A ASP   A 1 31  ? -25.14300 18.00300  -24.36500 0.500 12.47600 ? 30  ASP   A O     1 
ATOM   266  O  O     B ASP   A 1 31  ? -25.01700 18.46700  -24.00400 0.500 20.81321 ? 30  ASP   A O     1 
ATOM   267  C  CB    A ASP   A 1 31  ? -27.30700 19.92900  -25.33300 0.500 14.73571 ? 30  ASP   A CB    1 
ATOM   268  C  CB    B ASP   A 1 31  ? -26.31500 21.21900  -25.41300 0.500 24.48769 ? 30  ASP   A CB    1 
ATOM   269  C  CG    A ASP   A 1 31  ? -28.39700 20.83300  -24.79100 0.500 18.13079 ? 30  ASP   A CG    1 
ATOM   270  C  CG    B ASP   A 1 31  ? -25.81500 21.83800  -26.71200 0.500 27.47306 ? 30  ASP   A CG    1 
ATOM   271  O  OD1   A ASP   A 1 31  ? -28.49800 20.97800  -23.55600 0.500 18.26043 ? 30  ASP   A OD1   1 
ATOM   272  O  OD1   B ASP   A 1 31  ? -24.67000 22.33700  -26.73800 0.500 29.97035 ? 30  ASP   A OD1   1 
ATOM   273  O  OD2   A ASP   A 1 31  ? -29.15100 21.40300  -25.60500 0.500 20.92187 ? 30  ASP   A OD2   1 
ATOM   274  O  OD2   B ASP   A 1 31  ? -26.57200 21.83700  -27.70800 0.500 26.70934 ? 30  ASP   A OD2   1 
ATOM   275  N  N     . GLU   A 1 32  ? -23.98700 19.23100  -25.85600 1.000 18.82723 ? 31  GLU   A N     1 
ATOM   276  C  CA    . GLU   A 1 32  ? -23.12900 18.09000  -26.14400 1.000 19.88043 ? 31  GLU   A CA    1 
ATOM   277  C  C     . GLU   A 1 32  ? -22.28400 17.70900  -24.92900 1.000 19.40616 ? 31  GLU   A C     1 
ATOM   278  O  O     . GLU   A 1 32  ? -21.86400 18.56600  -24.14400 1.000 20.78409 ? 31  GLU   A O     1 
ATOM   279  C  CB    . GLU   A 1 32  ? -22.22500 18.42500  -27.33700 1.000 23.73237 ? 31  GLU   A CB    1 
ATOM   280  C  CG    . GLU   A 1 32  ? -22.96400 18.59900  -28.67500 1.000 27.67433 ? 31  GLU   A CG    1 
ATOM   281  C  CD    . GLU   A 1 32  ? -23.53700 19.99900  -28.89000 1.000 31.26188 ? 31  GLU   A CD    1 
ATOM   282  O  OE1   . GLU   A 1 32  ? -22.78900 20.99100  -28.74700 1.000 32.61091 ? 31  GLU   A OE1   1 
ATOM   283  O  OE2   . GLU   A 1 32  ? -24.74200 20.10600  -29.21100 1.000 32.85978 ? 31  GLU   A OE2   1 
ATOM   284  N  N     . TYR   A 1 33  ? -22.05300 16.40500  -24.77500 1.000 18.73867 ? 32  TYR   A N     1 
ATOM   285  C  CA    . TYR   A 1 33  ? -21.26400 15.85300  -23.68100 1.000 19.65168 ? 32  TYR   A CA    1 
ATOM   286  C  C     . TYR   A 1 33  ? -19.94900 15.34800  -24.24200 1.000 19.43050 ? 32  TYR   A C     1 
ATOM   287  O  O     . TYR   A 1 33  ? -19.93100 14.38100  -25.01100 1.000 24.39830 ? 32  TYR   A O     1 
ATOM   288  C  CB    . TYR   A 1 33  ? -22.00100 14.69100  -23.01400 1.000 20.80013 ? 32  TYR   A CB    1 
ATOM   289  C  CG    . TYR   A 1 33  ? -21.16700 13.89000  -22.02900 1.000 20.05714 ? 32  TYR   A CG    1 
ATOM   290  C  CD1   . TYR   A 1 33  ? -20.28200 14.51500  -21.15800 1.000 17.32910 ? 32  TYR   A CD1   1 
ATOM   291  C  CD2   . TYR   A 1 33  ? -21.28400 12.50900  -21.95500 1.000 21.13651 ? 32  TYR   A CD2   1 
ATOM   292  C  CE1   . TYR   A 1 33  ? -19.53700 13.78900  -20.25300 1.000 16.86085 ? 32  TYR   A CE1   1 
ATOM   293  C  CE2   . TYR   A 1 33  ? -20.54400 11.77500  -21.05200 1.000 19.86086 ? 32  TYR   A CE2   1 
ATOM   294  C  CZ    . TYR   A 1 33  ? -19.67000 12.42200  -20.20300 1.000 17.60390 ? 32  TYR   A CZ    1 
ATOM   295  O  OH    . TYR   A 1 33  ? -18.93300 11.69600  -19.29900 1.000 18.25806 ? 32  TYR   A OH    1 
ATOM   296  N  N     . ASP   A 1 34  ? -18.85500 15.97800  -23.84000 1.000 15.79133 ? 33  ASP   A N     1 
ATOM   297  C  CA    . ASP   A 1 34  ? -17.52300 15.50800  -24.21100 1.000 16.64680 ? 33  ASP   A CA    1 
ATOM   298  C  C     . ASP   A 1 34  ? -16.79200 15.09600  -22.94400 1.000 12.67739 ? 33  ASP   A C     1 
ATOM   299  O  O     . ASP   A 1 34  ? -16.35100 15.96100  -22.16300 1.000 11.25167 ? 33  ASP   A O     1 
ATOM   300  C  CB    . ASP   A 1 34  ? -16.76400 16.59100  -24.96900 1.000 21.88167 ? 33  ASP   A CB    1 
ATOM   301  C  CG    . ASP   A 1 34  ? -17.38700 16.88200  -26.32700 1.000 28.59377 ? 33  ASP   A CG    1 
ATOM   302  O  OD1   . ASP   A 1 34  ? -18.07400 15.98600  -26.86700 1.000 29.73000 ? 33  ASP   A OD1   1 
ATOM   303  O  OD2   . ASP   A 1 34  ? -17.19600 17.99500  -26.85400 1.000 31.77120 ? 33  ASP   A OD2   1 
ATOM   304  N  N     . PRO   A 1 35  ? -16.67100 13.79800  -22.67400 1.000 12.35418 ? 34  PRO   A N     1 
ATOM   305  C  CA    . PRO   A 1 35  ? -16.12300 13.36400  -21.38300 1.000 11.17554 ? 34  PRO   A CA    1 
ATOM   306  C  C     . PRO   A 1 35  ? -14.68400 13.82000  -21.18300 1.000 10.09242 ? 34  PRO   A C     1 
ATOM   307  O  O     . PRO   A 1 35  ? -13.85900 13.77700  -22.09800 1.000 12.53273 ? 34  PRO   A O     1 
ATOM   308  C  CB    . PRO   A 1 35  ? -16.22400 11.83500  -21.45800 1.000 13.20868 ? 34  PRO   A CB    1 
ATOM   309  C  CG    . PRO   A 1 35  ? -17.32700 11.58000  -22.43700 1.000 15.53634 ? 34  PRO   A CG    1 
ATOM   310  C  CD    . PRO   A 1 35  ? -17.17100 12.66100  -23.46900 1.000 14.63966 ? 34  PRO   A CD    1 
ATOM   311  N  N     . THR   A 1 36  ? -14.38100 14.21700  -19.95400 1.000 8.33978  ? 35  THR   A N     1 
ATOM   312  C  CA    . THR   A 1 36  ? -13.07800 14.75200  -19.59000 1.000 8.12315  ? 35  THR   A CA    1 
ATOM   313  C  C     . THR   A 1 36  ? -12.16100 13.65700  -19.05800 1.000 8.02649  ? 35  THR   A C     1 
ATOM   314  O  O     . THR   A 1 36  ? -12.60800 12.71600  -18.39500 1.000 7.81254  ? 35  THR   A O     1 
ATOM   315  C  CB    . THR   A 1 36  ? -13.28000 15.80100  -18.49200 1.000 8.03132  ? 35  THR   A CB    1 
ATOM   316  O  OG1   . THR   A 1 36  ? -14.26000 16.74600  -18.92000 1.000 8.77086  ? 35  THR   A OG1   1 
ATOM   317  C  CG2   . THR   A 1 36  ? -11.98400 16.51700  -18.10700 1.000 9.86469  ? 35  THR   A CG2   1 
ATOM   318  N  N     . ILE   A 1 37  ? -10.86400 13.81300  -19.33200 1.000 7.96104  ? 36  ILE   A N     1 
ATOM   319  C  CA    . ILE   A 1 37  ? -9.81300  13.19400  -18.52900 1.000 8.24362  ? 36  ILE   A CA    1 
ATOM   320  C  C     . ILE   A 1 37  ? -9.27000  14.24900  -17.56300 1.000 8.04444  ? 36  ILE   A C     1 
ATOM   321  O  O     . ILE   A 1 37  ? -9.47000  14.14800  -16.34400 1.000 8.56436  ? 36  ILE   A O     1 
ATOM   322  C  CB    . ILE   A 1 37  ? -8.72700  12.53800  -19.40000 1.000 8.99377  ? 36  ILE   A CB    1 
ATOM   323  C  CG1   . ILE   A 1 37  ? -9.30800  11.28700  -20.08000 1.000 10.09264 ? 36  ILE   A CG1   1 
ATOM   324  C  CG2   . ILE   A 1 37  ? -7.51500  12.17200  -18.55600 1.000 9.44787  ? 36  ILE   A CG2   1 
ATOM   325  C  CD1   . ILE   A 1 37  ? -8.38600  10.63700  -21.10200 1.000 11.31011 ? 36  ILE   A CD1   1 
ATOM   326  N  N     . GLU   A 1 38  ? -8.62300  15.28900  -18.10100 1.000 8.20401  ? 37  GLU   A N     1 
ATOM   327  C  CA    . GLU   A 1 38  ? -8.32400  16.49800  -17.34400 1.000 8.19979  ? 37  GLU   A CA    1 
ATOM   328  C  C     . GLU   A 1 38  ? -8.09300  17.61200  -18.34600 1.000 8.33040  ? 37  GLU   A C     1 
ATOM   329  O  O     . GLU   A 1 38  ? -7.48000  17.38200  -19.38800 1.000 9.69329  ? 37  GLU   A O     1 
ATOM   330  C  CB    . GLU   A 1 38  ? -7.07000  16.33600  -16.47900 1.000 8.93387  ? 37  GLU   A CB    1 
ATOM   331  C  CG    . GLU   A 1 38  ? -6.85400  17.49300  -15.49200 1.000 11.11204 ? 37  GLU   A CG    1 
ATOM   332  C  CD    . GLU   A 1 38  ? -6.14300  18.72300  -16.06900 1.000 11.52786 ? 37  GLU   A CD    1 
ATOM   333  O  OE1   . GLU   A 1 38  ? -5.44500  18.60500  -17.10600 1.000 12.29296 ? 37  GLU   A OE1   1 
ATOM   334  O  OE2   . GLU   A 1 38  ? -6.27000  19.81200  -15.45200 1.000 13.61990 ? 37  GLU   A OE2   1 
ATOM   335  N  N     . ASP   A 1 39  ? -8.56400  18.81600  -18.02400 1.000 9.24341  ? 38  ASP   A N     1 
ATOM   336  C  CA    . ASP   A 1 39  ? -8.26100  19.97800  -18.84400 1.000 9.98364  ? 38  ASP   A CA    1 
ATOM   337  C  C     . ASP   A 1 39  ? -7.98600  21.17200  -17.95000 1.000 10.39961 ? 38  ASP   A C     1 
ATOM   338  O  O     . ASP   A 1 39  ? -8.68900  21.38800  -16.96200 1.000 11.71849 ? 38  ASP   A O     1 
ATOM   339  C  CB    . ASP   A 1 39  ? -9.40300  20.29300  -19.80700 1.000 12.10187 ? 38  ASP   A CB    1 
ATOM   340  C  CG    . ASP   A 1 39  ? -9.45500  19.31100  -20.95400 1.000 14.13721 ? 38  ASP   A CG    1 
ATOM   341  O  OD1   . ASP   A 1 39  ? -8.58700  19.38600  -21.85300 1.000 15.24061 ? 38  ASP   A OD1   1 
ATOM   342  O  OD2   . ASP   A 1 39  ? -10.33600 18.43400  -20.93000 1.000 16.10167 ? 38  ASP   A OD2   1 
ATOM   343  N  N     . SER   A 1 40  ? -6.96300  21.94400  -18.30400 1.000 10.62595 ? 39  SER   A N     1 
ATOM   344  C  CA    . SER   A 1 40  ? -6.55700  23.12000  -17.54900 1.000 11.65672 ? 39  SER   A CA    1 
ATOM   345  C  C     . SER   A 1 40  ? -6.82400  24.37800  -18.36400 1.000 11.04672 ? 39  SER   A C     1 
ATOM   346  O  O     . SER   A 1 40  ? -6.56600  24.41400  -19.57300 1.000 13.40944 ? 39  SER   A O     1 
ATOM   347  C  CB    . SER   A 1 40  ? -5.06500  23.05000  -17.22500 1.000 14.21050 ? 39  SER   A CB    1 
ATOM   348  O  OG    . SER   A 1 40  ? -4.77300  21.85200  -16.52200 1.000 17.27821 ? 39  SER   A OG    1 
ATOM   349  N  N     . TYR   A 1 41  ? -7.31200  25.41800  -17.69000 1.000 11.03013 ? 40  TYR   A N     1 
ATOM   350  C  CA    . TYR   A 1 41  ? -7.64000  26.68700  -18.31700 1.000 11.94453 ? 40  TYR   A CA    1 
ATOM   351  C  C     . TYR   A 1 41  ? -7.06700  27.81600  -17.47800 1.000 11.96784 ? 40  TYR   A C     1 
ATOM   352  O  O     . TYR   A 1 41  ? -6.84800  27.67100  -16.27400 1.000 14.06600 ? 40  TYR   A O     1 
ATOM   353  C  CB    . TYR   A 1 41  ? -9.16000  26.87700  -18.41100 1.000 12.49252 ? 40  TYR   A CB    1 
ATOM   354  C  CG    . TYR   A 1 41  ? -9.86400  25.77500  -19.16800 1.000 12.46570 ? 40  TYR   A CG    1 
ATOM   355  C  CD1   . TYR   A 1 41  ? -10.32600 24.63700  -18.51100 1.000 11.32444 ? 40  TYR   A CD1   1 
ATOM   356  C  CD2   . TYR   A 1 41  ? -10.05900 25.86300  -20.54300 1.000 15.19921 ? 40  TYR   A CD2   1 
ATOM   357  C  CE1   . TYR   A 1 41  ? -10.97400 23.62100  -19.20400 1.000 12.15228 ? 40  TYR   A CE1   1 
ATOM   358  C  CE2   . TYR   A 1 41  ? -10.70200 24.84800  -21.24700 1.000 15.78946 ? 40  TYR   A CE2   1 
ATOM   359  C  CZ    . TYR   A 1 41  ? -11.15800 23.73200  -20.56900 1.000 14.41734 ? 40  TYR   A CZ    1 
ATOM   360  O  OH    . TYR   A 1 41  ? -11.79800 22.72500  -21.25400 1.000 16.62289 ? 40  TYR   A OH    1 
ATOM   361  N  N     . ARG   A 1 42  ? -6.83300  28.95200  -18.12400 1.000 11.75143 ? 41  ARG   A N     1 
ATOM   362  C  CA    . ARG   A 1 42  ? -6.41500  30.16200  -17.43400 1.000 13.15867 ? 41  ARG   A CA    1 
ATOM   363  C  C     . ARG   A 1 42  ? -7.27100  31.32300  -17.90600 1.000 12.67990 ? 41  ARG   A C     1 
ATOM   364  O  O     . ARG   A 1 42  ? -7.54900  31.44700  -19.10300 1.000 15.76833 ? 41  ARG   A O     1 
ATOM   365  C  CB    . ARG   A 1 42  ? -4.94500  30.48100  -17.71700 1.000 16.39252 ? 41  ARG   A CB    1 
ATOM   366  C  CG    . ARG   A 1 42  ? -3.97000  29.65700  -16.90500 1.000 22.57951 ? 41  ARG   A CG    1 
ATOM   367  C  CD    . ARG   A 1 42  ? -2.55000  30.15600  -17.10300 1.000 29.58873 ? 41  ARG   A CD    1 
ATOM   368  N  NE    . ARG   A 1 42  ? -1.75200  29.98400  -15.89700 1.000 35.80425 ? 41  ARG   A NE    1 
ATOM   369  C  CZ    . ARG   A 1 42  ? -0.51700  30.44200  -15.74400 1.000 41.21753 ? 41  ARG   A CZ    1 
ATOM   370  N  NH1   . ARG   A 1 42  ? 0.09900   31.10400  -16.71000 1.000 43.43384 ? 41  ARG   A NH1   1 
ATOM   371  N  NH2   . ARG   A 1 42  ? 0.11400   30.23300  -14.59300 1.000 42.52456 ? 41  ARG   A NH2   1 
ATOM   372  N  N     . LYS   A 1 43  ? -7.68000  32.17400  -16.96600 1.000 11.79769 ? 42  LYS   A N     1 
ATOM   373  C  CA    . LYS   A 1 43  ? -8.45400  33.35300  -17.32400 1.000 12.60083 ? 42  LYS   A CA    1 
ATOM   374  C  C     . LYS   A 1 43  ? -8.24000  34.45100  -16.29700 1.000 11.08343 ? 42  LYS   A C     1 
ATOM   375  O  O     . LYS   A 1 43  ? -8.27500  34.20300  -15.08700 1.000 11.32230 ? 42  LYS   A O     1 
ATOM   376  C  CB    . LYS   A 1 43  ? -9.94700  33.04500  -17.44500 1.000 16.99761 ? 42  LYS   A CB    1 
ATOM   377  C  CG    . LYS   A 1 43  ? -10.74600 34.23400  -17.96000 1.000 19.30952 ? 42  LYS   A CG    1 
ATOM   378  C  CD    . LYS   A 1 43  ? -12.03100 33.80700  -18.62200 1.000 21.36711 ? 42  LYS   A CD    1 
ATOM   379  C  CE    . LYS   A 1 43  ? -12.83300 35.00600  -19.09800 1.000 21.76257 ? 42  LYS   A CE    1 
ATOM   380  N  NZ    . LYS   A 1 43  ? -14.12200 34.59100  -19.72700 1.000 24.15891 ? 42  LYS   A NZ    1 
ATOM   381  N  N     . GLN   A 1 44  ? -8.02600  35.66300  -16.79100 1.000 10.66070 ? 43  GLN   A N     1 
ATOM   382  C  CA    . GLN   A 1 44  ? -7.96400  36.83500  -15.93500 1.000 10.87401 ? 43  GLN   A CA    1 
ATOM   383  C  C     . GLN   A 1 44  ? -9.36300  37.36600  -15.66700 1.000 11.17792 ? 43  GLN   A C     1 
ATOM   384  O  O     . GLN   A 1 44  ? -10.19700 37.44700  -16.57300 1.000 12.07773 ? 43  GLN   A O     1 
ATOM   385  C  CB    . GLN   A 1 44  ? -7.10500  37.91700  -16.58200 1.000 11.72536 ? 43  GLN   A CB    1 
ATOM   386  C  CG    . GLN   A 1 44  ? -5.66200  37.46900  -16.70100 1.000 14.15610 ? 43  GLN   A CG    1 
ATOM   387  C  CD    . GLN   A 1 44  ? -4.74900  38.53200  -17.26600 1.000 17.67802 ? 43  GLN   A CD    1 
ATOM   388  O  OE1   . GLN   A 1 44  ? -5.06600  39.71300  -17.23100 1.000 19.81407 ? 43  GLN   A OE1   1 
ATOM   389  N  NE2   . GLN   A 1 44  ? -3.60300  38.11300  -17.78500 1.000 19.20881 ? 43  GLN   A NE2   1 
ATOM   390  N  N     . VAL   A 1 45  ? -9.62400  37.69400  -14.40300 1.000 11.03124 ? 44  VAL   A N     1 
ATOM   391  C  CA    . VAL   A 1 45  ? -10.92000 38.18300  -13.95200 1.000 11.38945 ? 44  VAL   A CA    1 
ATOM   392  C  C     . VAL   A 1 45  ? -10.66500 39.33100  -12.98500 1.000 11.06822 ? 44  VAL   A C     1 
ATOM   393  O  O     . VAL   A 1 45  ? -9.54800  39.53500  -12.51400 1.000 14.18918 ? 44  VAL   A O     1 
ATOM   394  C  CB    . VAL   A 1 45  ? -11.74200 37.07600  -13.25300 1.000 14.43609 ? 44  VAL   A CB    1 
ATOM   395  C  CG1   . VAL   A 1 45  ? -11.97900 35.88100  -14.17900 1.000 16.37355 ? 44  VAL   A CG1   1 
ATOM   396  C  CG2   . VAL   A 1 45  ? -11.04000 36.63400  -11.98500 1.000 15.90756 ? 44  VAL   A CG2   1 
ATOM   397  N  N     . VAL   A 1 46  ? -11.70500 40.10300  -12.70500 1.000 10.32818 ? 45  VAL   A N     1 
ATOM   398  C  CA    . VAL   A 1 46  ? -11.66900 41.08700  -11.63100 1.000 10.45216 ? 45  VAL   A CA    1 
ATOM   399  C  C     . VAL   A 1 46  ? -12.63000 40.61800  -10.55300 1.000 9.79550  ? 45  VAL   A C     1 
ATOM   400  O  O     . VAL   A 1 46  ? -13.80000 40.33300  -10.84200 1.000 11.51722 ? 45  VAL   A O     1 
ATOM   401  C  CB    . VAL   A 1 46  ? -12.03700 42.49600  -12.12800 1.000 10.85047 ? 45  VAL   A CB    1 
ATOM   402  C  CG1   . VAL   A 1 46  ? -11.83500 43.50900  -11.01300 1.000 12.61390 ? 45  VAL   A CG1   1 
ATOM   403  C  CG2   . VAL   A 1 46  ? -11.20000 42.86800  -13.34700 1.000 11.94852 ? 45  VAL   A CG2   1 
ATOM   404  N  N     . ILE   A 1 47  ? -12.13300 40.51200  -9.32100  1.000 9.81913  ? 46  ILE   A N     1 
ATOM   405  C  CA    . ILE   A 1 47  ? -12.93200 40.09800  -8.17000  1.000 10.44875 ? 46  ILE   A CA    1 
ATOM   406  C  C     . ILE   A 1 47  ? -12.76500 41.16800  -7.10100  1.000 9.74397  ? 46  ILE   A C     1 
ATOM   407  O  O     . ILE   A 1 47  ? -11.63800 41.44700  -6.67400  1.000 10.09268 ? 46  ILE   A O     1 
ATOM   408  C  CB    . ILE   A 1 47  ? -12.50500 38.72300  -7.62700  1.000 11.28204 ? 46  ILE   A CB    1 
ATOM   409  C  CG1   . ILE   A 1 47  ? -12.67400 37.65300  -8.70300  1.000 12.42441 ? 46  ILE   A CG1   1 
ATOM   410  C  CG2   . ILE   A 1 47  ? -13.30700 38.38200  -6.37500  1.000 12.19864 ? 46  ILE   A CG2   1 
ATOM   411  C  CD1   . ILE   A 1 47  ? -12.05700 36.31600  -8.33700  1.000 13.87273 ? 46  ILE   A CD1   1 
ATOM   412  N  N     . ASP   A 1 48  ? -13.87600 41.77700  -6.68500  1.000 9.58838  ? 47  ASP   A N     1 
ATOM   413  C  CA    . ASP   A 1 48  ? -13.84300 42.83000  -5.66900  1.000 10.54393 ? 47  ASP   A CA    1 
ATOM   414  C  C     . ASP   A 1 48  ? -12.85400 43.93500  -6.03800  1.000 9.71385  ? 47  ASP   A C     1 
ATOM   415  O  O     . ASP   A 1 48  ? -12.14100 44.47000  -5.18500  1.000 10.79817 ? 47  ASP   A O     1 
ATOM   416  C  CB    . ASP   A 1 48  ? -13.55600 42.26700  -4.27300  1.000 10.83916 ? 47  ASP   A CB    1 
ATOM   417  C  CG    . ASP   A 1 48  ? -14.63200 41.31000  -3.78300  1.000 11.07653 ? 47  ASP   A CG    1 
ATOM   418  O  OD1   . ASP   A 1 48  ? -15.74700 41.30400  -4.34700  1.000 11.29737 ? 47  ASP   A OD1   1 
ATOM   419  O  OD2   . ASP   A 1 48  ? -14.34900 40.56700  -2.82100  1.000 11.43731 ? 47  ASP   A OD2   1 
ATOM   420  N  N     . GLY   A 1 49  ? -12.80000 44.27100  -7.33000  1.000 9.43566  ? 48  GLY   A N     1 
ATOM   421  C  CA    . GLY   A 1 49  ? -11.95500 45.34300  -7.80700  1.000 10.37597 ? 48  GLY   A CA    1 
ATOM   422  C  C     . GLY   A 1 49  ? -10.50400 44.98100  -8.03700  1.000 10.13414 ? 48  GLY   A C     1 
ATOM   423  O  O     . GLY   A 1 49  ? -9.72200  45.86300  -8.41200  1.000 11.58004 ? 48  GLY   A O     1 
ATOM   424  N  N     . GLU   A 1 50  ? -10.11200 43.72400  -7.83400  1.000 10.44414 ? 49  GLU   A N     1 
ATOM   425  C  CA    . GLU   A 1 50  ? -8.72000  43.30900  -7.96900  1.000 10.75747 ? 49  GLU   A CA    1 
ATOM   426  C  C     . GLU   A 1 50  ? -8.60500  42.32400  -9.12600  1.000 10.16565 ? 49  GLU   A C     1 
ATOM   427  O  O     . GLU   A 1 50  ? -9.25800  41.27500  -9.12000  1.000 11.03629 ? 49  GLU   A O     1 
ATOM   428  C  CB    . GLU   A 1 50  ? -8.19700  42.67600  -6.67400  1.000 11.39434 ? 49  GLU   A CB    1 
ATOM   429  C  CG    . GLU   A 1 50  ? -6.72500  42.27400  -6.78900  1.000 13.45576 ? 49  GLU   A CG    1 
ATOM   430  C  CD    . GLU   A 1 50  ? -6.08500  41.82600  -5.48500  1.000 14.26787 ? 49  GLU   A CD    1 
ATOM   431  O  OE1   . GLU   A 1 50  ? -6.55400  42.19800  -4.39100  1.000 15.35479 ? 49  GLU   A OE1   1 
ATOM   432  O  OE2   . GLU   A 1 50  ? -5.07800  41.09500  -5.56400  1.000 15.92163 ? 49  GLU   A OE2   1 
ATOM   433  N  N     . THR   A 1 51  ? -7.78100  42.65700  -10.11900 1.000 9.94858  ? 50  THR   A N     1 
ATOM   434  C  CA    . THR   A 1 51  ? -7.53400  41.71700  -11.20700 1.000 10.17025 ? 50  THR   A CA    1 
ATOM   435  C  C     . THR   A 1 51  ? -6.76300  40.51200  -10.68800 1.000 10.69721 ? 50  THR   A C     1 
ATOM   436  O  O     . THR   A 1 51  ? -5.74600  40.66000  -10.00400 1.000 11.49200 ? 50  THR   A O     1 
ATOM   437  C  CB    . THR   A 1 51  ? -6.74800  42.38100  -12.33500 1.000 10.84465 ? 50  THR   A CB    1 
ATOM   438  O  OG1   . THR   A 1 51  ? -7.48300  43.51500  -12.81100 1.000 11.94794 ? 50  THR   A OG1   1 
ATOM   439  C  CG2   . THR   A 1 51  ? -6.54300  41.40200  -13.49000 1.000 11.95441 ? 50  THR   A CG2   1 
ATOM   440  N  N     . SER   A 1 52  ? -7.24400  39.32200  -11.04000 1.000 10.06016 ? 51  SER   A N     1 
ATOM   441  C  CA    . SER   A 1 52  ? -6.70700  38.06400  -10.54300 1.000 12.46962 ? 51  SER   A CA    1 
ATOM   442  C  C     . SER   A 1 52  ? -6.60700  37.07900  -11.70200 1.000 11.12739 ? 51  SER   A C     1 
ATOM   443  O  O     . SER   A 1 52  ? -7.39800  37.12800  -12.64700 1.000 12.42190 ? 51  SER   A O     1 
ATOM   444  C  CB    . SER   A 1 52  ? -7.63000  37.48900  -9.45200  1.000 17.93363 ? 51  SER   A CB    1 
ATOM   445  O  OG    . SER   A 1 52  ? -7.96400  38.47300  -8.47800  1.000 22.11169 ? 51  SER   A OG    1 
ATOM   446  N  N     . LEU   A 1 53  ? -5.64800  36.16100  -11.61300 1.000 10.72473 ? 52  LEU   A N     1 
ATOM   447  C  CA    . LEU   A 1 53  ? -5.48800  35.10800  -12.61100 1.000 10.84339 ? 52  LEU   A CA    1 
ATOM   448  C  C     . LEU   A 1 53  ? -6.04200  33.81000  -12.03500 1.000 10.68392 ? 52  LEU   A C     1 
ATOM   449  O  O     . LEU   A 1 53  ? -5.58600  33.35000  -10.98300 1.000 11.83424 ? 52  LEU   A O     1 
ATOM   450  C  CB    . LEU   A 1 53  ? -4.01500  34.92900  -12.97500 1.000 11.30292 ? 52  LEU   A CB    1 
ATOM   451  C  CG    . LEU   A 1 53  ? -3.70300  33.81700  -13.98100 1.000 13.41741 ? 52  LEU   A CG    1 
ATOM   452  C  CD1   . LEU   A 1 53  ? -4.38500  34.06400  -15.32200 1.000 15.78586 ? 52  LEU   A CD1   1 
ATOM   453  C  CD2   . LEU   A 1 53  ? -2.19700  33.64900  -14.15500 1.000 15.95197 ? 52  LEU   A CD2   1 
ATOM   454  N  N     . LEU   A 1 54  ? -7.02500  33.22400  -12.71400 1.000 10.47166 ? 53  LEU   A N     1 
ATOM   455  C  CA    . LEU   A 1 54  ? -7.56600  31.93100  -12.31600 1.000 10.89745 ? 53  LEU   A CA    1 
ATOM   456  C  C     . LEU   A 1 54  ? -6.96600  30.83200  -13.17500 1.000 10.33348 ? 53  LEU   A C     1 
ATOM   457  O  O     . LEU   A 1 54  ? -6.99900  30.90700  -14.41000 1.000 12.32826 ? 53  LEU   A O     1 
ATOM   458  C  CB    . LEU   A 1 54  ? -9.08500  31.89600  -12.46400 1.000 11.00699 ? 53  LEU   A CB    1 
ATOM   459  C  CG    . LEU   A 1 54  ? -9.84300  33.02700  -11.78600 1.000 11.54219 ? 53  LEU   A CG    1 
ATOM   460  C  CD1   . LEU   A 1 54  ? -11.33300 32.73000  -11.86000 1.000 12.86794 ? 53  LEU   A CD1   1 
ATOM   461  C  CD2   . LEU   A 1 54  ? -9.37600  33.24200  -10.33900 1.000 13.09111 ? 53  LEU   A CD2   1 
ATOM   462  N  N     A ASP   A 1 55  ? -6.39600  29.82500  -12.52300 0.500 10.60809 ? 54  ASP   A N     1 
ATOM   463  N  N     B ASP   A 1 55  ? -6.40700  29.82500  -12.51500 0.500 9.64352  ? 54  ASP   A N     1 
ATOM   464  C  CA    A ASP   A 1 55  ? -6.06800  28.56200  -13.16700 0.500 11.56970 ? 54  ASP   A CA    1 
ATOM   465  C  CA    B ASP   A 1 55  ? -5.87900  28.62900  -13.15500 0.500 9.60080  ? 54  ASP   A CA    1 
ATOM   466  C  C     A ASP   A 1 55  ? -7.15900  27.58400  -12.75900 0.500 10.30455 ? 54  ASP   A C     1 
ATOM   467  C  C     B ASP   A 1 55  ? -6.80100  27.49900  -12.72100 0.500 9.27512  ? 54  ASP   A C     1 
ATOM   468  O  O     A ASP   A 1 55  ? -7.36000  27.35100  -11.56300 0.500 10.69058 ? 54  ASP   A O     1 
ATOM   469  O  O     B ASP   A 1 55  ? -6.75100  27.06200  -11.56600 0.500 9.53935  ? 54  ASP   A O     1 
ATOM   470  C  CB    A ASP   A 1 55  ? -4.71900  28.03700  -12.67600 0.500 14.93842 ? 54  ASP   A CB    1 
ATOM   471  C  CB    B ASP   A 1 55  ? -4.45000  28.39100  -12.67300 0.500 11.79403 ? 54  ASP   A CB    1 
ATOM   472  C  CG    A ASP   A 1 55  ? -3.55700  28.92600  -13.06100 0.500 19.25764 ? 54  ASP   A CG    1 
ATOM   473  C  CG    B ASP   A 1 55  ? -3.86900  27.07500  -13.15800 0.500 14.73368 ? 54  ASP   A CG    1 
ATOM   474  O  OD1   A ASP   A 1 55  ? -3.75100  29.89600  -13.82000 0.500 22.01970 ? 54  ASP   A OD1   1 
ATOM   475  O  OD1   B ASP   A 1 55  ? -4.45800  26.43800  -14.05400 0.500 15.85433 ? 54  ASP   A OD1   1 
ATOM   476  O  OD2   A ASP   A 1 55  ? -2.43600  28.64000  -12.59800 0.500 21.59553 ? 54  ASP   A OD2   1 
ATOM   477  O  OD2   B ASP   A 1 55  ? -2.81000  26.67200  -12.62900 0.500 17.75321 ? 54  ASP   A OD2   1 
ATOM   478  N  N     A ILE   A 1 56  ? -7.87200  27.02800  -13.73600 0.500 10.13388 ? 55  ILE   A N     1 
ATOM   479  N  N     B ILE   A 1 56  ? -7.64800  27.03400  -13.63700 0.500 9.21283  ? 55  ILE   A N     1 
ATOM   480  C  CA    A ILE   A 1 56  ? -8.94000  26.06400  -13.47500 0.500 9.79064  ? 55  ILE   A CA    1 
ATOM   481  C  CA    B ILE   A 1 56  ? -8.72400  26.10200  -13.31400 0.500 9.00884  ? 55  ILE   A CA    1 
ATOM   482  C  C     A ILE   A 1 56  ? -8.46900  24.69700  -13.94600 0.500 9.67706  ? 55  ILE   A C     1 
ATOM   483  C  C     B ILE   A 1 56  ? -8.40200  24.73500  -13.89200 0.500 8.46045  ? 55  ILE   A C     1 
ATOM   484  O  O     A ILE   A 1 56  ? -8.16200  24.51900  -15.13200 0.500 11.12352 ? 55  ILE   A O     1 
ATOM   485  O  O     B ILE   A 1 56  ? -8.17100  24.59900  -15.10000 0.500 9.21822  ? 55  ILE   A O     1 
ATOM   486  C  CB    A ILE   A 1 56  ? -10.24400 26.44000  -14.19700 0.500 11.40753 ? 55  ILE   A CB    1 
ATOM   487  C  CB    B ILE   A 1 56  ? -10.07800 26.60000  -13.83400 0.500 9.90647  ? 55  ILE   A CB    1 
ATOM   488  C  CG1   A ILE   A 1 56  ? -10.54400 27.93400  -14.07300 0.500 10.58264 ? 55  ILE   A CG1   1 
ATOM   489  C  CG1   B ILE   A 1 56  ? -10.39800 27.96000  -13.22700 0.500 10.34991 ? 55  ILE   A CG1   1 
ATOM   490  C  CG2   A ILE   A 1 56  ? -11.40500 25.61400  -13.64900 0.500 12.56600 ? 55  ILE   A CG2   1 
ATOM   491  C  CG2   B ILE   A 1 56  ? -11.17500 25.58600  -13.51800 0.500 10.74008 ? 55  ILE   A CG2   1 
ATOM   492  C  CD1   A ILE   A 1 56  ? -10.83900 28.37700  -12.67400 0.500 11.51074 ? 55  ILE   A CD1   1 
ATOM   493  C  CD1   B ILE   A 1 56  ? -11.44300 28.67800  -13.98500 0.500 11.27524 ? 55  ILE   A CD1   1 
ATOM   494  N  N     . LEU   A 1 57  ? -8.43800  23.72500  -13.03400 1.000 8.36075  ? 56  LEU   A N     1 
ATOM   495  C  CA    . LEU   A 1 57  ? -8.20700  22.33300  -13.39400 1.000 8.28596  ? 56  LEU   A CA    1 
ATOM   496  C  C     . LEU   A 1 57  ? -9.55100  21.62000  -13.33500 1.000 7.96486  ? 56  LEU   A C     1 
ATOM   497  O  O     . LEU   A 1 57  ? -10.13700 21.46800  -12.25400 1.000 9.38876  ? 56  LEU   A O     1 
ATOM   498  C  CB    . LEU   A 1 57  ? -7.21800  21.68200  -12.43700 1.000 9.87834  ? 56  LEU   A CB    1 
ATOM   499  C  CG    . LEU   A 1 57  ? -5.82800  22.30000  -12.28400 1.000 13.13887 ? 56  LEU   A CG    1 
ATOM   500  C  CD1   . LEU   A 1 57  ? -4.90300  21.28300  -11.63100 1.000 16.01369 ? 56  LEU   A CD1   1 
ATOM   501  C  CD2   . LEU   A 1 57  ? -5.22900  22.80100  -13.58200 1.000 17.98747 ? 56  LEU   A CD2   1 
ATOM   502  N  N     . ASP   A 1 58  ? -10.02000 21.17700  -14.49900 1.000 7.97602  ? 57  ASP   A N     1 
ATOM   503  C  CA    . ASP   A 1 58  ? -11.29300 20.48100  -14.65600 1.000 8.01188  ? 57  ASP   A CA    1 
ATOM   504  C  C     . ASP   A 1 58  ? -10.97600 18.98400  -14.69300 1.000 7.57624  ? 57  ASP   A C     1 
ATOM   505  O  O     . ASP   A 1 58  ? -10.29400 18.51600  -15.61300 1.000 9.45109  ? 57  ASP   A O     1 
ATOM   506  C  CB    . ASP   A 1 58  ? -11.91400 20.97100  -15.96400 1.000 8.89073  ? 57  ASP   A CB    1 
ATOM   507  C  CG    . ASP   A 1 58  ? -13.22700 20.30900  -16.29300 1.000 8.81926  ? 57  ASP   A CG    1 
ATOM   508  O  OD1   . ASP   A 1 58  ? -13.87100 19.76000  -15.37800 1.000 9.75205  ? 57  ASP   A OD1   1 
ATOM   509  O  OD2   . ASP   A 1 58  ? -13.61200 20.34800  -17.48800 1.000 10.33263 ? 57  ASP   A OD2   1 
ATOM   510  N  N     . THR   A 1 59  ? -11.42300 18.24500  -13.67000 1.000 8.10380  ? 58  THR   A N     1 
ATOM   511  C  CA    . THR   A 1 59  ? -10.99200 16.86600  -13.43700 1.000 7.87984  ? 58  THR   A CA    1 
ATOM   512  C  C     . THR   A 1 59  ? -12.09900 15.86300  -13.76100 1.000 7.17153  ? 58  THR   A C     1 
ATOM   513  O  O     . THR   A 1 59  ? -13.20500 16.22100  -14.16800 1.000 8.01524  ? 58  THR   A O     1 
ATOM   514  C  CB    . THR   A 1 59  ? -10.51300 16.66500  -11.99300 1.000 7.80701  ? 58  THR   A CB    1 
ATOM   515  O  OG1   . THR   A 1 59  ? -11.62900 16.70800  -11.09600 1.000 7.95820  ? 58  THR   A OG1   1 
ATOM   516  C  CG2   . THR   A 1 59  ? -9.47300  17.70600  -11.59700 1.000 9.26484  ? 58  THR   A CG2   1 
ATOM   517  N  N     . ALA   A 1 60  ? -11.78400 14.58500  -13.56400 1.000 7.58173  ? 59  ALA   A N     1 
ATOM   518  C  CA    . ALA   A 1 60  ? -12.70700 13.48400  -13.85900 1.000 7.52720  ? 59  ALA   A CA    1 
ATOM   519  C  C     . ALA   A 1 60  ? -12.16300 12.22200  -13.18900 1.000 8.23309  ? 59  ALA   A C     1 
ATOM   520  O  O     . ALA   A 1 60  ? -11.21000 12.28000  -12.40200 1.000 8.68718  ? 59  ALA   A O     1 
ATOM   521  C  CB    . ALA   A 1 60  ? -12.88400 13.30700  -15.36900 1.000 8.60686  ? 59  ALA   A CB    1 
ATOM   522  N  N     . GLY   A 1 61  ? -12.75400 11.06500  -13.50400 1.000 8.13291  ? 60  GLY   A N     1 
ATOM   523  C  CA    . GLY   A 1 61  ? -12.18400 9.77800   -13.15900 1.000 8.87227  ? 60  GLY   A CA    1 
ATOM   524  C  C     . GLY   A 1 61  ? -12.89900 9.02600   -12.05800 1.000 8.29972  ? 60  GLY   A C     1 
ATOM   525  O  O     . GLY   A 1 61  ? -12.67100 7.81500   -11.91100 1.000 9.32412  ? 60  GLY   A O     1 
ATOM   526  N  N     . GLN   A 1 62  ? -13.74900 9.69900   -11.27700 1.000 8.39677  ? 61  GLN   A N     1 
ATOM   527  C  CA    . GLN   A 1 62  ? -14.46800 9.07200   -10.17000 1.000 9.67368  ? 61  GLN   A CA    1 
ATOM   528  C  C     . GLN   A 1 62  ? -13.53200 8.23300   -9.30900  1.000 9.72014  ? 61  GLN   A C     1 
ATOM   529  O  O     . GLN   A 1 62  ? -12.41100 8.65500   -9.01400  1.000 10.11200 ? 61  GLN   A O     1 
ATOM   530  C  CB    . GLN   A 1 62  ? -15.67900 8.27500   -10.66300 1.000 10.46090 ? 61  GLN   A CB    1 
ATOM   531  C  CG    . GLN   A 1 62  ? -16.59300 9.10900   -11.52600 1.000 11.71049 ? 61  GLN   A CG    1 
ATOM   532  C  CD    . GLN   A 1 62  ? -17.92000 8.44000   -11.80100 1.000 12.59977 ? 61  GLN   A CD    1 
ATOM   533  O  OE1   . GLN   A 1 62  ? -18.98000 9.04600   -11.63400 1.000 11.90113 ? 61  GLN   A OE1   1 
ATOM   534  N  NE2   . GLN   A 1 62  ? -17.87100 7.19100   -12.25100 1.000 15.66103 ? 61  GLN   A NE2   1 
ATOM   535  N  N     . GLU   A 1 63  ? -13.97100 7.04300   -8.90400  1.000 10.19992 ? 62  GLU   A N     1 
ATOM   536  C  CA    . GLU   A 1 63  ? -13.15600 6.25400   -7.99000  1.000 11.75287 ? 62  GLU   A CA    1 
ATOM   537  C  C     . GLU   A 1 63  ? -12.10100 5.43900   -8.73400  1.000 10.26302 ? 62  GLU   A C     1 
ATOM   538  O  O     . GLU   A 1 63  ? -10.97300 5.29800   -8.24700  1.000 12.35478 ? 62  GLU   A O     1 
ATOM   539  C  CB    . GLU   A 1 63  ? -14.05100 5.36500   -7.12100  1.000 14.37338 ? 62  GLU   A CB    1 
ATOM   540  C  CG    . GLU   A 1 63  ? -14.94900 6.14900   -6.14700  1.000 19.75157 ? 62  GLU   A CG    1 
ATOM   541  C  CD    . GLU   A 1 63  ? -16.08600 6.90700   -6.84100  1.000 23.92665 ? 62  GLU   A CD    1 
ATOM   542  O  OE1   . GLU   A 1 63  ? -16.86200 6.26500   -7.58800  1.000 28.00236 ? 62  GLU   A OE1   1 
ATOM   543  O  OE2   . GLU   A 1 63  ? -16.19400 8.14400   -6.65800  1.000 22.12827 ? 62  GLU   A OE2   1 
ATOM   544  N  N     . GLU   A 1 64  ? -12.43900 4.91600   -9.91900  1.000 11.26007 ? 63  GLU   A N     1 
ATOM   545  C  CA    . GLU   A 1 64  ? -11.51900 4.03300   -10.63200 1.000 11.91594 ? 63  GLU   A CA    1 
ATOM   546  C  C     . GLU   A 1 64  ? -10.19700 4.72600   -10.94500 1.000 11.55127 ? 63  GLU   A C     1 
ATOM   547  O  O     . GLU   A 1 64  ? -9.14300  4.08500   -10.92100 1.000 13.18926 ? 63  GLU   A O     1 
ATOM   548  C  CB    . GLU   A 1 64  ? -12.16700 3.49100   -11.91100 1.000 12.33555 ? 63  GLU   A CB    1 
ATOM   549  C  CG    . GLU   A 1 64  ? -11.30800 2.45200   -12.62100 1.000 13.49940 ? 63  GLU   A CG    1 
ATOM   550  C  CD    . GLU   A 1 64  ? -11.96500 1.82400   -13.84000 1.000 13.45346 ? 63  GLU   A CD    1 
ATOM   551  O  OE1   . GLU   A 1 64  ? -13.16900 2.07100   -14.09800 1.000 14.27122 ? 63  GLU   A OE1   1 
ATOM   552  O  OE2   . GLU   A 1 64  ? -11.26000 1.07300   -14.55600 1.000 13.96980 ? 63  GLU   A OE2   1 
ATOM   553  N  N     . TYR   A 1 65  ? -10.22100 6.03400   -11.20800 1.000 11.07196 ? 64  TYR   A N     1 
ATOM   554  C  CA    . TYR   A 1 65  ? -9.01600  6.78400   -11.54900 1.000 10.71785 ? 64  TYR   A CA    1 
ATOM   555  C  C     . TYR   A 1 65  ? -8.64200  7.80600   -10.47300 1.000 10.22738 ? 64  TYR   A C     1 
ATOM   556  O  O     . TYR   A 1 65  ? -7.91400  8.77000   -10.74800 1.000 10.92790 ? 64  TYR   A O     1 
ATOM   557  C  CB    . TYR   A 1 65  ? -9.16500  7.41500   -12.93400 1.000 10.50254 ? 64  TYR   A CB    1 
ATOM   558  C  CG    . TYR   A 1 65  ? -9.52300  6.39100   -13.98900 1.000 9.78279  ? 64  TYR   A CG    1 
ATOM   559  C  CD1   . TYR   A 1 65  ? -8.52900  5.68200   -14.65700 1.000 10.87669 ? 64  TYR   A CD1   1 
ATOM   560  C  CD2   . TYR   A 1 65  ? -10.84900 6.09900   -14.28800 1.000 10.02406 ? 64  TYR   A CD2   1 
ATOM   561  C  CE1   . TYR   A 1 65  ? -8.83800  4.73500   -15.61200 1.000 10.69533 ? 64  TYR   A CE1   1 
ATOM   562  C  CE2   . TYR   A 1 65  ? -11.16800 5.13100   -15.23900 1.000 10.06187 ? 64  TYR   A CE2   1 
ATOM   563  C  CZ    . TYR   A 1 65  ? -10.15500 4.45700   -15.89700 1.000 10.77617 ? 64  TYR   A CZ    1 
ATOM   564  O  OH    . TYR   A 1 65  ? -10.44000 3.50400   -16.85200 1.000 11.10278 ? 64  TYR   A OH    1 
ATOM   565  N  N     . SER   A 1 66  ? -9.10200  7.58100   -9.24000  1.000 10.61984 ? 65  SER   A N     1 
ATOM   566  C  CA    A SER   A 1 66  ? -8.90600  8.56400   -8.17900  0.500 10.55067 ? 65  SER   A CA    1 
ATOM   567  C  CA    B SER   A 1 66  ? -8.90900  8.54700   -8.16200  0.500 11.78854 ? 65  SER   A CA    1 
ATOM   568  C  C     . SER   A 1 66  ? -7.43300  8.75900   -7.84400  1.000 11.05660 ? 65  SER   A C     1 
ATOM   569  O  O     . SER   A 1 66  ? -7.01300  9.88100   -7.53000  1.000 11.03010 ? 65  SER   A O     1 
ATOM   570  C  CB    A SER   A 1 66  ? -9.68700  8.16000   -6.93200  0.500 11.03998 ? 65  SER   A CB    1 
ATOM   571  C  CB    B SER   A 1 66  ? -9.66500  8.07100   -6.92200  0.500 14.94786 ? 65  SER   A CB    1 
ATOM   572  O  OG    A SER   A 1 66  ? -9.26100  6.89200   -6.47400  0.500 9.28327  ? 65  SER   A OG    1 
ATOM   573  O  OG    B SER   A 1 66  ? -9.44600  8.92300   -5.81700  0.500 16.79908 ? 65  SER   A OG    1 
ATOM   574  N  N     . ALA   A 1 67  ? -6.63200  7.68500   -7.88500  1.000 11.89714 ? 66  ALA   A N     1 
ATOM   575  C  CA    . ALA   A 1 67  ? -5.21300  7.81800   -7.54800  1.000 12.62644 ? 66  ALA   A CA    1 
ATOM   576  C  C     . ALA   A 1 67  ? -4.49700  8.75100   -8.51500  1.000 11.66701 ? 66  ALA   A C     1 
ATOM   577  O  O     . ALA   A 1 67  ? -3.61200  9.51700   -8.11200  1.000 12.94495 ? 66  ALA   A O     1 
ATOM   578  C  CB    . ALA   A 1 67  ? -4.53300  6.44800   -7.51300  1.000 15.51656 ? 66  ALA   A CB    1 
ATOM   579  N  N     A MET   A 1 68  ? -4.85100  8.68800   -9.80300  0.500 10.28479 ? 67  MET   A N     1 
ATOM   580  N  N     B MET   A 1 68  ? -4.87200  8.71200   -9.79200  0.500 11.36926 ? 67  MET   A N     1 
ATOM   581  C  CA    A MET   A 1 68  ? -4.28900  9.62700   -10.77200 0.500 10.17768 ? 67  MET   A CA    1 
ATOM   582  C  CA    B MET   A 1 68  ? -4.27000  9.62800   -10.75400 0.500 12.38892 ? 67  MET   A CA    1 
ATOM   583  C  C     A MET   A 1 68  ? -4.77700  11.04300  -10.50600 0.500 9.06058  ? 67  MET   A C     1 
ATOM   584  C  C     B MET   A 1 68  ? -4.79100  11.05000  -10.57000 0.500 10.36863 ? 67  MET   A C     1 
ATOM   585  O  O     A MET   A 1 68  ? -3.99300  12.00000  -10.56500 0.500 9.31315  ? 67  MET   A O     1 
ATOM   586  O  O     B MET   A 1 68  ? -4.03500  12.01800  -10.72200 0.500 10.49117 ? 67  MET   A O     1 
ATOM   587  C  CB    A MET   A 1 68  ? -4.64100  9.21400   -12.20000 0.500 10.45853 ? 67  MET   A CB    1 
ATOM   588  C  CB    B MET   A 1 68  ? -4.47400  9.10600   -12.17500 0.500 14.35061 ? 67  MET   A CB    1 
ATOM   589  C  CG    A MET   A 1 68  ? -4.12100  7.85700   -12.60400 0.500 11.42941 ? 67  MET   A CG    1 
ATOM   590  C  CG    B MET   A 1 68  ? -3.49900  7.99100   -12.51800 0.500 15.95326 ? 67  MET   A CG    1 
ATOM   591  S  SD    A MET   A 1 68  ? -5.36200  6.60400   -12.28100 0.500 12.70291 ? 67  MET   A SD    1 
ATOM   592  S  SD    B MET   A 1 68  ? -4.20100  6.66200   -13.51100 0.500 16.29226 ? 67  MET   A SD    1 
ATOM   593  C  CE    A MET   A 1 68  ? -4.31600  5.20400   -11.90900 0.500 13.53294 ? 67  MET   A CE    1 
ATOM   594  C  CE    B MET   A 1 68  ? -5.50400  6.09400   -12.42500 0.500 17.67298 ? 67  MET   A CE    1 
ATOM   595  N  N     . ARG   A 1 69  ? -6.07100  11.19700  -10.21200 1.000 9.31086  ? 68  ARG   A N     1 
ATOM   596  C  CA    . ARG   A 1 69  ? -6.61100  12.52600  -9.96000  1.000 8.72060  ? 68  ARG   A CA    1 
ATOM   597  C  C     . ARG   A 1 69  ? -5.96000  13.18400  -8.74500  1.000 8.63951  ? 68  ARG   A C     1 
ATOM   598  O  O     . ARG   A 1 69  ? -5.84400  14.41500  -8.71100  1.000 9.03898  ? 68  ARG   A O     1 
ATOM   599  C  CB    . ARG   A 1 69  ? -8.13400  12.47100  -9.83900  1.000 8.86678  ? 68  ARG   A CB    1 
ATOM   600  C  CG    . ARG   A 1 69  ? -8.75400  13.85100  -9.63800  1.000 8.64404  ? 68  ARG   A CG    1 
ATOM   601  C  CD    . ARG   A 1 69  ? -10.27300 13.82500  -9.52800  1.000 8.53242  ? 68  ARG   A CD    1 
ATOM   602  N  NE    . ARG   A 1 69  ? -10.73700 13.02200  -8.40200  1.000 8.31285  ? 68  ARG   A NE    1 
ATOM   603  C  CZ    . ARG   A 1 69  ? -11.23800 11.79700  -8.50800  1.000 8.14858  ? 68  ARG   A CZ    1 
ATOM   604  N  NH1   . ARG   A 1 69  ? -11.39100 11.20800  -9.68500  1.000 9.21108  ? 68  ARG   A NH1   1 
ATOM   605  N  NH2   . ARG   A 1 69  ? -11.57500 11.13900  -7.40100  1.000 9.42604  ? 68  ARG   A NH2   1 
ATOM   606  N  N     . ASP   A 1 70  ? -5.50000  12.39000  -7.76300  1.000 9.25651  ? 69  ASP   A N     1 
ATOM   607  C  CA    . ASP   A 1 70  ? -4.76500  12.94200  -6.62200  1.000 8.73508  ? 69  ASP   A CA    1 
ATOM   608  C  C     . ASP   A 1 70  ? -3.70000  13.93300  -7.07700  1.000 8.61770  ? 69  ASP   A C     1 
ATOM   609  O  O     . ASP   A 1 70  ? -3.47500  14.96300  -6.42900  1.000 8.96839  ? 69  ASP   A O     1 
ATOM   610  C  CB    . ASP   A 1 70  ? -4.00000  11.84100  -5.87900  1.000 10.04087 ? 69  ASP   A CB    1 
ATOM   611  C  CG    . ASP   A 1 70  ? -4.84100  11.01800  -4.90800  1.000 10.24564 ? 69  ASP   A CG    1 
ATOM   612  O  OD1   . ASP   A 1 70  ? -6.06200  11.21500  -4.75700  1.000 11.29193 ? 69  ASP   A OD1   1 
ATOM   613  O  OD2   . ASP   A 1 70  ? -4.22300  10.13300  -4.26900  1.000 12.62594 ? 69  ASP   A OD2   1 
ATOM   614  N  N     . GLN   A 1 71  ? -2.99000  13.60600  -8.16300  1.000 9.00106  ? 70  GLN   A N     1 
ATOM   615  C  CA    . GLN   A 1 71  ? -1.83700  14.40500  -8.57000  1.000 9.06882  ? 70  GLN   A CA    1 
ATOM   616  C  C     . GLN   A 1 71  ? -2.26100  15.78500  -9.06100  1.000 8.64018  ? 70  GLN   A C     1 
ATOM   617  O  O     . GLN   A 1 71  ? -1.55500  16.77500  -8.83000  1.000 9.18055  ? 70  GLN   A O     1 
ATOM   618  C  CB    . GLN   A 1 71  ? -1.04600  13.66700  -9.64700  1.000 10.92682 ? 70  GLN   A CB    1 
ATOM   619  C  CG    . GLN   A 1 71  ? -0.56600  12.29100  -9.21900  1.000 12.91610 ? 70  GLN   A CG    1 
ATOM   620  C  CD    . GLN   A 1 71  ? 0.31900   11.63200  -10.26500 1.000 14.41947 ? 70  GLN   A CD    1 
ATOM   621  O  OE1   . GLN   A 1 71  ? 0.87000   12.29800  -11.14400 1.000 15.22943 ? 70  GLN   A OE1   1 
ATOM   622  N  NE2   . GLN   A 1 71  ? 0.46100   10.31800  -10.17100 1.000 17.27772 ? 70  GLN   A NE2   1 
ATOM   623  N  N     . TYR   A 1 72  ? -3.40200  15.87300  -9.75100  1.000 9.09132  ? 71  TYR   A N     1 
ATOM   624  C  CA    . TYR   A 1 72  ? -3.91500  17.18200  -10.13400 1.000 9.11230  ? 71  TYR   A CA    1 
ATOM   625  C  C     . TYR   A 1 72  ? -4.45000  17.92900  -8.92200  1.000 8.62815  ? 71  TYR   A C     1 
ATOM   626  O  O     . TYR   A 1 72  ? -4.22800  19.13700  -8.77900  1.000 9.63116  ? 71  TYR   A O     1 
ATOM   627  C  CB    . TYR   A 1 72  ? -5.02200  17.04200  -11.18000 1.000 9.75338  ? 71  TYR   A CB    1 
ATOM   628  C  CG    . TYR   A 1 72  ? -4.55400  16.52800  -12.52100 1.000 9.91249  ? 71  TYR   A CG    1 
ATOM   629  C  CD1   . TYR   A 1 72  ? -3.83000  17.34000  -13.40100 1.000 10.31680 ? 71  TYR   A CD1   1 
ATOM   630  C  CD2   . TYR   A 1 72  ? -4.84900  15.23100  -12.92300 1.000 11.31505 ? 71  TYR   A CD2   1 
ATOM   631  C  CE1   . TYR   A 1 72  ? -3.41800  16.86300  -14.63800 1.000 10.44292 ? 71  TYR   A CE1   1 
ATOM   632  C  CE2   . TYR   A 1 72  ? -4.43500  14.75000  -14.14300 1.000 11.78348 ? 71  TYR   A CE2   1 
ATOM   633  C  CZ    . TYR   A 1 72  ? -3.71900  15.56600  -15.00100 1.000 11.38906 ? 71  TYR   A CZ    1 
ATOM   634  O  OH    . TYR   A 1 72  ? -3.30800  15.09600  -16.22800 1.000 13.55815 ? 71  TYR   A OH    1 
ATOM   635  N  N     . MET   A 1 73  ? -5.18300  17.23200  -8.05000  1.000 7.95298  ? 72  MET   A N     1 
ATOM   636  C  CA    . MET   A 1 73  ? -5.75500  17.88800  -6.87900  1.000 8.45409  ? 72  MET   A CA    1 
ATOM   637  C  C     . MET   A 1 73  ? -4.67800  18.44200  -5.95600  1.000 7.96690  ? 72  MET   A C     1 
ATOM   638  O  O     . MET   A 1 73  ? -4.89000  19.47500  -5.31100  1.000 8.85991  ? 72  MET   A O     1 
ATOM   639  C  CB    . MET   A 1 73  ? -6.70500  16.93600  -6.15700  1.000 8.85060  ? 72  MET   A CB    1 
ATOM   640  C  CG    . MET   A 1 73  ? -7.92700  16.61100  -6.99800  1.000 9.04093  ? 72  MET   A CG    1 
ATOM   641  S  SD    . MET   A 1 73  ? -8.98100  15.31700  -6.33200  1.000 8.93479  ? 72  MET   A SD    1 
ATOM   642  C  CE    . MET   A 1 73  ? -9.62100  16.14800  -4.87500  1.000 9.82580  ? 72  MET   A CE    1 
ATOM   643  N  N     . ARG   A 1 74  ? -3.51600  17.78800  -5.89500  1.000 8.66596  ? 73  ARG   A N     1 
ATOM   644  C  CA    . ARG   A 1 74  ? -2.42700  18.25700  -5.04600  1.000 9.46308  ? 73  ARG   A CA    1 
ATOM   645  C  C     . ARG   A 1 74  ? -1.95700  19.65900  -5.43400  1.000 9.78167  ? 73  ARG   A C     1 
ATOM   646  O  O     . ARG   A 1 74  ? -1.42700  20.38400  -4.58900  1.000 11.91244 ? 73  ARG   A O     1 
ATOM   647  C  CB    . ARG   A 1 74  ? -1.27600  17.24700  -5.09600  1.000 9.76436  ? 73  ARG   A CB    1 
ATOM   648  C  CG    . ARG   A 1 74  ? -0.19500  17.46200  -4.05600  1.000 11.77762 ? 73  ARG   A CG    1 
ATOM   649  C  CD    . ARG   A 1 74  ? 0.75500   16.27300  -4.00000  1.000 13.51195 ? 73  ARG   A CD    1 
ATOM   650  N  NE    . ARG   A 1 74  ? 0.20100   15.14000  -3.26600  1.000 14.52226 ? 73  ARG   A NE    1 
ATOM   651  C  CZ    . ARG   A 1 74  ? -0.13400  13.97800  -3.80900  1.000 13.24466 ? 73  ARG   A CZ    1 
ATOM   652  N  NH1   . ARG   A 1 74  ? -0.02100  13.76200  -5.11300  1.000 14.02326 ? 73  ARG   A NH1   1 
ATOM   653  N  NH2   . ARG   A 1 74  ? -0.58900  13.00300  -3.02300  1.000 16.41950 ? 73  ARG   A NH2   1 
ATOM   654  N  N     A THR   A 1 75  ? -2.14900  20.04400  -6.70600  0.500 8.43693  ? 74  THR   A N     1 
ATOM   655  N  N     B THR   A 1 75  ? -2.15000  20.06600  -6.68000  0.500 9.69244  ? 74  THR   A N     1 
ATOM   656  C  CA    A THR   A 1 75  ? -1.81900  21.38400  -7.19900  0.500 8.76054  ? 74  THR   A CA    1 
ATOM   657  C  CA    B THR   A 1 75  ? -1.75300  21.40500  -7.08700  0.500 10.84629 ? 74  THR   A CA    1 
ATOM   658  C  C     A THR   A 1 75  ? -2.76000  22.44600  -6.63700  0.500 8.90989  ? 74  THR   A C     1 
ATOM   659  C  C     B THR   A 1 75  ? -2.79300  22.46300  -6.74700  0.500 9.67014  ? 74  THR   A C     1 
ATOM   660  O  O     A THR   A 1 75  ? -2.36200  23.60600  -6.47400  0.500 9.36153  ? 74  THR   A O     1 
ATOM   661  O  O     B THR   A 1 75  ? -2.49500  23.65800  -6.85900  0.500 8.97914  ? 74  THR   A O     1 
ATOM   662  C  CB    A THR   A 1 75  ? -1.92600  21.38000  -8.73200  0.500 9.72215  ? 74  THR   A CB    1 
ATOM   663  C  CB    B THR   A 1 75  ? -1.48400  21.39800  -8.58300  0.500 13.43335 ? 74  THR   A CB    1 
ATOM   664  O  OG1   A THR   A 1 75  ? -1.01100  20.42500  -9.27300  0.500 10.08988 ? 74  THR   A OG1   1 
ATOM   665  O  OG1   B THR   A 1 75  ? -2.72600  21.49500  -9.27800  0.500 12.80540 ? 74  THR   A OG1   1 
ATOM   666  C  CG2   A THR   A 1 75  ? -1.61300  22.73700  -9.33300  0.500 8.97318  ? 74  THR   A CG2   1 
ATOM   667  C  CG2   B THR   A 1 75  ? -0.87000  20.08200  -8.94400  0.500 14.34350 ? 74  THR   A CG2   1 
ATOM   668  N  N     . GLY   A 1 76  ? -3.99800  22.07200  -6.33100  1.000 9.06831  ? 75  GLY   A N     1 
ATOM   669  C  CA    . GLY   A 1 76  ? -5.02500  23.05700  -6.07200  1.000 9.54346  ? 75  GLY   A CA    1 
ATOM   670  C  C     . GLY   A 1 76  ? -4.87400  23.77900  -4.74700  1.000 8.94355  ? 75  GLY   A C     1 
ATOM   671  O  O     . GLY   A 1 76  ? -4.41000  23.23400  -3.74800  1.000 10.38339 ? 75  GLY   A O     1 
ATOM   672  N  N     . GLU   A 1 77  ? -5.31500  25.03700  -4.75200  1.000 9.18721  ? 76  GLU   A N     1 
ATOM   673  C  CA    . GLU   A 1 77  ? -5.47300  25.82800  -3.54100  1.000 10.13010 ? 76  GLU   A CA    1 
ATOM   674  C  C     . GLU   A 1 77  ? -6.90700  25.84200  -3.03700  1.000 10.42920 ? 76  GLU   A C     1 
ATOM   675  O  O     . GLU   A 1 77  ? -7.12500  26.08500  -1.84800  1.000 13.38500 ? 76  GLU   A O     1 
ATOM   676  C  CB    . GLU   A 1 77  ? -5.04100  27.27200  -3.79600  1.000 11.71395 ? 76  GLU   A CB    1 
ATOM   677  C  CG    . GLU   A 1 77  ? -3.57300  27.44900  -4.09900  1.000 16.12313 ? 76  GLU   A CG    1 
ATOM   678  C  CD    . GLU   A 1 77  ? -3.27300  28.87200  -4.51000  1.000 21.28384 ? 76  GLU   A CD    1 
ATOM   679  O  OE1   . GLU   A 1 77  ? -3.64100  29.25400  -5.63300  1.000 20.29331 ? 76  GLU   A OE1   1 
ATOM   680  O  OE2   . GLU   A 1 77  ? -2.70800  29.63000  -3.69400  1.000 26.46606 ? 76  GLU   A OE2   1 
ATOM   681  N  N     . GLY   A 1 78  ? -7.88100  25.61500  -3.91000  1.000 9.24869  ? 77  GLY   A N     1 
ATOM   682  C  CA    . GLY   A 1 78  ? -9.27000  25.54600  -3.49500  1.000 9.36389  ? 77  GLY   A CA    1 
ATOM   683  C  C     . GLY   A 1 78  ? -10.03400 24.68800  -4.47600  1.000 8.21027  ? 77  GLY   A C     1 
ATOM   684  O  O     . GLY   A 1 78  ? -9.59800  24.48100  -5.61600  1.000 8.32291  ? 77  GLY   A O     1 
ATOM   685  N  N     . PHE   A 1 79  ? -11.19700 24.20100  -4.02700  1.000 7.46483  ? 78  PHE   A N     1 
ATOM   686  C  CA    . PHE   A 1 79  ? -11.93300 23.17700  -4.75800  1.000 7.20879  ? 78  PHE   A CA    1 
ATOM   687  C  C     . PHE   A 1 79  ? -13.41500 23.50300  -4.83900  1.000 7.10035  ? 78  PHE   A C     1 
ATOM   688  O  O     . PHE   A 1 79  ? -14.01500 23.95000  -3.85500  1.000 7.68705  ? 78  PHE   A O     1 
ATOM   689  C  CB    . PHE   A 1 79  ? -11.75400 21.81900  -4.05500  1.000 8.07838  ? 78  PHE   A CB    1 
ATOM   690  C  CG    . PHE   A 1 79  ? -10.32100 21.38500  -3.99000  1.000 7.80119  ? 78  PHE   A CG    1 
ATOM   691  C  CD1   . PHE   A 1 79  ? -9.46900  21.89200  -3.01500  1.000 8.79313  ? 78  PHE   A CD1   1 
ATOM   692  C  CD2   . PHE   A 1 79  ? -9.80000  20.51500  -4.94200  1.000 8.81988  ? 78  PHE   A CD2   1 
ATOM   693  C  CE1   . PHE   A 1 79  ? -8.13800  21.55200  -2.99400  1.000 9.46696  ? 78  PHE   A CE1   1 
ATOM   694  C  CE2   . PHE   A 1 79  ? -8.46100  20.16400  -4.91700  1.000 9.31509  ? 78  PHE   A CE2   1 
ATOM   695  C  CZ    . PHE   A 1 79  ? -7.63100  20.68100  -3.94400  1.000 9.60293  ? 78  PHE   A CZ    1 
ATOM   696  N  N     . LEU   A 1 80  ? -14.00100 23.25900  -6.01500  1.000 6.93028  ? 79  LEU   A N     1 
ATOM   697  C  CA    . LEU   A 1 80  ? -15.44800 23.16800  -6.15800  1.000 7.15478  ? 79  LEU   A CA    1 
ATOM   698  C  C     . LEU   A 1 80  ? -15.82900 21.69500  -6.10900  1.000 7.04341  ? 79  LEU   A C     1 
ATOM   699  O  O     . LEU   A 1 80  ? -15.32400 20.89300  -6.90400  1.000 8.06792  ? 79  LEU   A O     1 
ATOM   700  C  CB    . LEU   A 1 80  ? -15.92100 23.76400  -7.48100  1.000 7.87867  ? 79  LEU   A CB    1 
ATOM   701  C  CG    . LEU   A 1 80  ? -15.70500 25.25600  -7.72400  1.000 8.65612  ? 79  LEU   A CG    1 
ATOM   702  C  CD1   . LEU   A 1 80  ? -16.39200 25.67200  -9.02800  1.000 9.57244  ? 79  LEU   A CD1   1 
ATOM   703  C  CD2   . LEU   A 1 80  ? -16.21600 26.09900  -6.56600  1.000 8.70696  ? 79  LEU   A CD2   1 
ATOM   704  N  N     . LEU   A 1 81  ? -16.71500 21.34500  -5.18300  1.000 7.45710  ? 80  LEU   A N     1 
ATOM   705  C  CA    . LEU   A 1 81  ? -17.25100 19.99200  -5.06700  1.000 7.98030  ? 80  LEU   A CA    1 
ATOM   706  C  C     . LEU   A 1 81  ? -18.64000 20.02100  -5.69000  1.000 6.72652  ? 80  LEU   A C     1 
ATOM   707  O  O     . LEU   A 1 81  ? -19.56800 20.60300  -5.11800  1.000 7.98912  ? 80  LEU   A O     1 
ATOM   708  C  CB    . LEU   A 1 81  ? -17.32400 19.55900  -3.60300  1.000 10.53789 ? 80  LEU   A CB    1 
ATOM   709  C  CG    . LEU   A 1 81  ? -15.97700 19.34300  -2.89500  1.000 12.92471 ? 80  LEU   A CG    1 
ATOM   710  C  CD1   . LEU   A 1 81  ? -15.31800 20.65600  -2.49400  1.000 14.53952 ? 80  LEU   A CD1   1 
ATOM   711  C  CD2   . LEU   A 1 81  ? -16.10000 18.40800  -1.70000  1.000 14.90796 ? 80  LEU   A CD2   1 
ATOM   712  N  N     . VAL   A 1 82  ? -18.78300 19.42800  -6.87300  1.000 7.49648  ? 81  VAL   A N     1 
ATOM   713  C  CA    . VAL   A 1 82  ? -19.98600 19.58300  -7.68600  1.000 6.66636  ? 81  VAL   A CA    1 
ATOM   714  C  C     . VAL   A 1 82  ? -20.81300 18.30200  -7.64000  1.000 6.71324  ? 81  VAL   A C     1 
ATOM   715  O  O     . VAL   A 1 82  ? -20.29100 17.20400  -7.88500  1.000 7.36723  ? 81  VAL   A O     1 
ATOM   716  C  CB    . VAL   A 1 82  ? -19.63300 19.93200  -9.14300  1.000 7.18536  ? 81  VAL   A CB    1 
ATOM   717  C  CG1   . VAL   A 1 82  ? -20.89600 20.23700  -9.92900  1.000 8.31898  ? 81  VAL   A CG1   1 
ATOM   718  C  CG2   . VAL   A 1 82  ? -18.64600 21.09000  -9.20700  1.000 7.92201  ? 81  VAL   A CG2   1 
ATOM   719  N  N     . PHE   A 1 83  ? -22.10700 18.44400  -7.35800  1.000 7.02881  ? 82  PHE   A N     1 
ATOM   720  C  CA    . PHE   A 1 83  ? -23.08700 17.39700  -7.60700  1.000 7.17776  ? 82  PHE   A CA    1 
ATOM   721  C  C     . PHE   A 1 83  ? -24.18300 17.97300  -8.49300  1.000 7.11908  ? 82  PHE   A C     1 
ATOM   722  O  O     . PHE   A 1 83  ? -24.26200 19.18500  -8.69600  1.000 7.71666  ? 82  PHE   A O     1 
ATOM   723  C  CB    . PHE   A 1 83  ? -23.66400 16.81000  -6.30200  1.000 7.55233  ? 82  PHE   A CB    1 
ATOM   724  C  CG    . PHE   A 1 83  ? -24.58600 17.74800  -5.56600  1.000 7.56656  ? 82  PHE   A CG    1 
ATOM   725  C  CD1   . PHE   A 1 83  ? -24.08500 18.70700  -4.69500  1.000 7.70431  ? 82  PHE   A CD1   1 
ATOM   726  C  CD2   . PHE   A 1 83  ? -25.95800 17.66900  -5.74700  1.000 8.39851  ? 82  PHE   A CD2   1 
ATOM   727  C  CE1   . PHE   A 1 83  ? -24.94300 19.57000  -4.02900  1.000 8.34094  ? 82  PHE   A CE1   1 
ATOM   728  C  CE2   . PHE   A 1 83  ? -26.81300 18.53200  -5.10100  1.000 8.78545  ? 82  PHE   A CE2   1 
ATOM   729  C  CZ    . PHE   A 1 83  ? -26.31100 19.48100  -4.23800  1.000 8.66995  ? 82  PHE   A CZ    1 
ATOM   730  N  N     . ALA   A 1 84  ? -25.02100 17.10100  -9.05600  1.000 7.26101  ? 83  ALA   A N     1 
ATOM   731  C  CA    . ALA   A 1 84  ? -26.17700 17.53300  -9.83100  1.000 7.51250  ? 83  ALA   A CA    1 
ATOM   732  C  C     . ALA   A 1 84  ? -27.44900 17.20400  -9.05800  1.000 7.53350  ? 83  ALA   A C     1 
ATOM   733  O  O     . ALA   A 1 84  ? -27.56100 16.12900  -8.45500  1.000 7.61400  ? 83  ALA   A O     1 
ATOM   734  C  CB    . ALA   A 1 84  ? -26.21800 16.86300  -11.20700 1.000 8.32868  ? 83  ALA   A CB    1 
ATOM   735  N  N     . ILE   A 1 85  ? -28.42600 18.11600  -9.10000  1.000 7.49832  ? 84  ILE   A N     1 
ATOM   736  C  CA    . ILE   A 1 85  ? -29.60300 17.98900  -8.24100  1.000 7.64064  ? 84  ILE   A CA    1 
ATOM   737  C  C     . ILE   A 1 85  ? -30.49100 16.81600  -8.62200  1.000 7.48721  ? 84  ILE   A C     1 
ATOM   738  O  O     . ILE   A 1 85  ? -31.34900 16.41600  -7.82500  1.000 8.47031  ? 84  ILE   A O     1 
ATOM   739  C  CB    . ILE   A 1 85  ? -30.42100 19.29700  -8.17800  1.000 8.62072  ? 84  ILE   A CB    1 
ATOM   740  C  CG1   . ILE   A 1 85  ? -31.04500 19.63700  -9.54300  1.000 9.53012  ? 84  ILE   A CG1   1 
ATOM   741  C  CG2   . ILE   A 1 85  ? -29.56100 20.43400  -7.62800  1.000 9.76950  ? 84  ILE   A CG2   1 
ATOM   742  C  CD1   . ILE   A 1 85  ? -32.05600 20.77700  -9.49100  1.000 11.31215 ? 84  ILE   A CD1   1 
ATOM   743  N  N     . ASN   A 1 86  ? -30.31700 16.26500  -9.82200  1.000 7.84374  ? 85  ASN   A N     1 
ATOM   744  C  CA    . ASN   A 1 86  ? -31.06800 15.10900  -10.28700 1.000 8.71301  ? 85  ASN   A CA    1 
ATOM   745  C  C     . ASN   A 1 86  ? -30.23500 13.83200  -10.25800 1.000 8.66482  ? 85  ASN   A C     1 
ATOM   746  O  O     . ASN   A 1 86  ? -30.59500 12.85400  -10.91900 1.000 10.11674 ? 85  ASN   A O     1 
ATOM   747  C  CB    . ASN   A 1 86  ? -31.62000 15.36000  -11.69200 1.000 8.89061  ? 85  ASN   A CB    1 
ATOM   748  C  CG    . ASN   A 1 86  ? -30.53400 15.45000  -12.73600 1.000 8.65834  ? 85  ASN   A CG    1 
ATOM   749  O  OD1   . ASN   A 1 86  ? -29.39500 15.79200  -12.42200 1.000 9.38756  ? 85  ASN   A OD1   1 
ATOM   750  N  ND2   . ASN   A 1 86  ? -30.87600 15.15100  -13.98700 1.000 10.19926 ? 85  ASN   A ND2   1 
ATOM   751  N  N     . ASN   A 1 87  ? -29.13800 13.81500  -9.50500  1.000 8.33415  ? 86  ASN   A N     1 
ATOM   752  C  CA    . ASN   A 1 87  ? -28.22200 12.67300  -9.48300  1.000 8.47401  ? 86  ASN   A CA    1 
ATOM   753  C  C     . ASN   A 1 87  ? -27.86900 12.35900  -8.02800  1.000 7.92191  ? 86  ASN   A C     1 
ATOM   754  O  O     . ASN   A 1 87  ? -26.93800 12.92400  -7.44800  1.000 8.05766  ? 86  ASN   A O     1 
ATOM   755  C  CB    . ASN   A 1 87  ? -26.99300 12.98200  -10.34200 1.000 9.42259  ? 86  ASN   A CB    1 
ATOM   756  C  CG    . ASN   A 1 87  ? -26.01600 11.82700  -10.41400 1.000 9.75359  ? 86  ASN   A CG    1 
ATOM   757  O  OD1   . ASN   A 1 87  ? -26.05200 10.90800  -9.59700  1.000 10.24453 ? 86  ASN   A OD1   1 
ATOM   758  N  ND2   . ASN   A 1 87  ? -25.11100 11.88700  -11.38300 1.000 10.91890 ? 86  ASN   A ND2   1 
ATOM   759  N  N     . THR   A 1 88  ? -28.62300 11.43900  -7.43200  1.000 8.54857  ? 87  THR   A N     1 
ATOM   760  C  CA    . THR   A 1 88  ? -28.40400 11.05500  -6.03900  1.000 8.87484  ? 87  THR   A CA    1 
ATOM   761  C  C     . THR   A 1 88  ? -27.00000 10.51300  -5.80900  1.000 8.11457  ? 87  THR   A C     1 
ATOM   762  O  O     . THR   A 1 88  ? -26.35700 10.85400  -4.81000  1.000 8.36416  ? 87  THR   A O     1 
ATOM   763  C  CB    . THR   A 1 88  ? -29.45700 10.03000  -5.63300  1.000 10.63144 ? 87  THR   A CB    1 
ATOM   764  O  OG1   . THR   A 1 88  ? -30.72200 10.69400  -5.57900  1.000 12.29373 ? 87  THR   A OG1   1 
ATOM   765  C  CG2   . THR   A 1 88  ? -29.13100 9.40300   -4.27700  1.000 12.54607 ? 87  THR   A CG2   1 
ATOM   766  N  N     . LYS   A 1 89  ? -26.51400 9.64900   -6.70400  1.000 8.61364  ? 88  LYS   A N     1 
ATOM   767  C  CA    . LYS   A 1 89  ? -25.16200 9.12800   -6.54200  1.000 8.78213  ? 88  LYS   A CA    1 
ATOM   768  C  C     . LYS   A 1 89  ? -24.14800 10.25700  -6.43200  1.000 7.92963  ? 88  LYS   A C     1 
ATOM   769  O  O     . LYS   A 1 89  ? -23.24500 10.20500  -5.59200  1.000 8.45851  ? 88  LYS   A O     1 
ATOM   770  C  CB    . LYS   A 1 89  ? -24.80100 8.19300   -7.69300  1.000 11.18823 ? 88  LYS   A CB    1 
ATOM   771  C  CG    . LYS   A 1 89  ? -23.36700 7.70500   -7.60800  1.000 13.92145 ? 88  LYS   A CG    1 
ATOM   772  C  CD    . LYS   A 1 89  ? -23.04000 6.73000   -8.71600  1.000 17.22455 ? 88  LYS   A CD    1 
ATOM   773  C  CE    . LYS   A 1 89  ? -21.60900 6.21700   -8.59600  1.000 19.74275 ? 88  LYS   A CE    1 
ATOM   774  N  NZ    . LYS   A 1 89  ? -20.61600 7.30000   -8.85600  1.000 19.16819 ? 88  LYS   A NZ    1 
ATOM   775  N  N     . SER   A 1 90  ? -24.28800 11.29600  -7.26400  1.000 7.78192  ? 89  SER   A N     1 
ATOM   776  C  CA    . SER   A 1 90  ? -23.31600 12.38400  -7.22800  1.000 7.68746  ? 89  SER   A CA    1 
ATOM   777  C  C     . SER   A 1 90  ? -23.30300 13.09400  -5.88200  1.000 7.60305  ? 89  SER   A C     1 
ATOM   778  O  O     . SER   A 1 90  ? -22.23900 13.53300  -5.42900  1.000 8.55127  ? 89  SER   A O     1 
ATOM   779  C  CB    . SER   A 1 90  ? -23.53700 13.37500  -8.37000  1.000 7.98766  ? 89  SER   A CB    1 
ATOM   780  O  OG    . SER   A 1 90  ? -24.65200 14.23100  -8.17700  1.000 8.04753  ? 89  SER   A OG    1 
ATOM   781  N  N     . PHE   A 1 91  ? -24.46300 13.20400  -5.22400  1.000 7.90524  ? 90  PHE   A N     1 
ATOM   782  C  CA    . PHE   A 1 91  ? -24.49900 13.78800  -3.89100  1.000 7.68590  ? 90  PHE   A CA    1 
ATOM   783  C  C     . PHE   A 1 91  ? -23.87000 12.85100  -2.87000  1.000 7.78359  ? 90  PHE   A C     1 
ATOM   784  O  O     . PHE   A 1 91  ? -23.08600 13.28700  -2.01700  1.000 8.43249  ? 90  PHE   A O     1 
ATOM   785  C  CB    . PHE   A 1 91  ? -25.93000 14.14500  -3.49100  1.000 8.80699  ? 90  PHE   A CB    1 
ATOM   786  C  CG    . PHE   A 1 91  ? -26.01100 14.80900  -2.15300  1.000 9.80379  ? 90  PHE   A CG    1 
ATOM   787  C  CD1   . PHE   A 1 91  ? -25.71900 16.15600  -2.03200  1.000 10.52378 ? 90  PHE   A CD1   1 
ATOM   788  C  CD2   . PHE   A 1 91  ? -26.32300 14.08800  -1.00800  1.000 12.99250 ? 90  PHE   A CD2   1 
ATOM   789  C  CE1   . PHE   A 1 91  ? -25.75800 16.78300  -0.80800  1.000 13.56557 ? 90  PHE   A CE1   1 
ATOM   790  C  CE2   . PHE   A 1 91  ? -26.37100 14.71800  0.23400   1.000 15.75089 ? 90  PHE   A CE2   1 
ATOM   791  C  CZ    . PHE   A 1 91  ? -26.08700 16.06500  0.32800   1.000 15.49551 ? 90  PHE   A CZ    1 
ATOM   792  N  N     . GLU   A 1 92  ? -24.19900 11.55500  -2.93800  1.000 7.86114  ? 91  GLU   A N     1 
ATOM   793  C  CA    . GLU   A 1 92  ? -23.60300 10.59200  -2.01800  1.000 8.60648  ? 91  GLU   A CA    1 
ATOM   794  C  C     . GLU   A 1 92  ? -22.09000 10.52100  -2.17600  1.000 9.65663  ? 91  GLU   A C     1 
ATOM   795  O  O     . GLU   A 1 92  ? -21.38400 10.20000  -1.21300  1.000 11.90901 ? 91  GLU   A O     1 
ATOM   796  C  CB    . GLU   A 1 92  ? -24.24400 9.21600   -2.21300  1.000 9.24820  ? 91  GLU   A CB    1 
ATOM   797  C  CG    . GLU   A 1 92  ? -25.73100 9.19100   -1.92200  1.000 10.23541 ? 91  GLU   A CG    1 
ATOM   798  C  CD    . GLU   A 1 92  ? -26.04400 9.63500   -0.51100  1.000 10.09892 ? 91  GLU   A CD    1 
ATOM   799  O  OE1   . GLU   A 1 92  ? -25.30900 9.22700   0.41900   1.000 10.85800 ? 91  GLU   A OE1   1 
ATOM   800  O  OE2   . GLU   A 1 92  ? -27.02900 10.38000  -0.32000  1.000 12.12264 ? 91  GLU   A OE2   1 
ATOM   801  N  N     . ASP   A 1 93  ? -21.57600 10.81900  -3.37700  1.000 8.62989  ? 92  ASP   A N     1 
ATOM   802  C  CA    . ASP   A 1 93  ? -20.14300 10.78400  -3.65000  1.000 9.59917  ? 92  ASP   A CA    1 
ATOM   803  C  C     . ASP   A 1 93  ? -19.38300 11.97800  -3.08300  1.000 9.09089  ? 92  ASP   A C     1 
ATOM   804  O  O     . ASP   A 1 93  ? -18.15100 11.92500  -3.01500  1.000 9.49144  ? 92  ASP   A O     1 
ATOM   805  C  CB    . ASP   A 1 93  ? -19.89600 10.75700  -5.16000  1.000 10.98778 ? 92  ASP   A CB    1 
ATOM   806  C  CG    . ASP   A 1 93  ? -20.18800 9.41400   -5.79500  1.000 12.74083 ? 92  ASP   A CG    1 
ATOM   807  O  OD1   . ASP   A 1 93  ? -20.37500 8.41400   -5.06500  1.000 13.95454 ? 92  ASP   A OD1   1 
ATOM   808  O  OD2   . ASP   A 1 93  ? -20.22400 9.37000   -7.04800  1.000 14.81144 ? 92  ASP   A OD2   1 
ATOM   809  N  N     . ILE   A 1 94  ? -20.07000 13.06600  -2.70700  1.000 8.99158  ? 93  ILE   A N     1 
ATOM   810  C  CA    . ILE   A 1 94  ? -19.36800 14.27400  -2.26500  1.000 8.82774  ? 93  ILE   A CA    1 
ATOM   811  C  C     . ILE   A 1 94  ? -18.39300 13.95600  -1.14000  1.000 9.40536  ? 93  ILE   A C     1 
ATOM   812  O  O     . ILE   A 1 94  ? -17.25500 14.44100  -1.12600  1.000 9.61666  ? 93  ILE   A O     1 
ATOM   813  C  CB    . ILE   A 1 94  ? -20.36700 15.38300  -1.87600  1.000 8.26987  ? 93  ILE   A CB    1 
ATOM   814  C  CG1   . ILE   A 1 94  ? -21.09700 15.92500  -3.11500  1.000 8.91489  ? 93  ILE   A CG1   1 
ATOM   815  C  CG2   . ILE   A 1 94  ? -19.65900 16.50600  -1.12500  1.000 9.14287  ? 93  ILE   A CG2   1 
ATOM   816  C  CD1   . ILE   A 1 94  ? -20.21100 16.70700  -4.08300  1.000 9.48530  ? 93  ILE   A CD1   1 
ATOM   817  N  N     A HIS   A 1 95  ? -18.83400 13.12800  -0.18600  0.500 9.70483  ? 94  HIS   A N     1 
ATOM   818  N  N     B HIS   A 1 95  ? -18.80100 13.11100  -0.19000  0.500 10.91772 ? 94  HIS   A N     1 
ATOM   819  C  CA    A HIS   A 1 95  ? -17.99000 12.69900  0.92400   0.500 11.89380 ? 94  HIS   A CA    1 
ATOM   820  C  CA    B HIS   A 1 95  ? -17.91000 12.81000  0.92700   0.500 13.55848 ? 94  HIS   A CA    1 
ATOM   821  C  C     A HIS   A 1 95  ? -16.62900 12.19400  0.44600   0.500 11.59775 ? 94  HIS   A C     1 
ATOM   822  C  C     B HIS   A 1 95  ? -16.59000 12.19900  0.45100   0.500 12.52728 ? 94  HIS   A C     1 
ATOM   823  O  O     A HIS   A 1 95  ? -15.59300 12.53200  1.03000   0.500 11.82743 ? 94  HIS   A O     1 
ATOM   824  O  O     B HIS   A 1 95  ? -15.53700 12.45700  1.04700   0.500 12.84058 ? 94  HIS   A O     1 
ATOM   825  C  CB    A HIS   A 1 95  ? -18.72300 11.60300  1.70200   0.500 13.15802 ? 94  HIS   A CB    1 
ATOM   826  C  CB    B HIS   A 1 95  ? -18.60000 11.88100  1.92000   0.500 16.39190 ? 94  HIS   A CB    1 
ATOM   827  C  CG    A HIS   A 1 95  ? -17.83800 10.81700  2.60900   0.500 12.91714 ? 94  HIS   A CG    1 
ATOM   828  C  CG    B HIS   A 1 95  ? -18.50400 10.44500  1.53400   0.500 18.21170 ? 94  HIS   A CG    1 
ATOM   829  N  ND1   A HIS   A 1 95  ? -17.42000 11.29400  3.83200   0.500 12.82917 ? 94  HIS   A ND1   1 
ATOM   830  N  ND1   B HIS   A 1 95  ? -19.19400 9.92000   0.46400   0.500 18.69157 ? 94  HIS   A ND1   1 
ATOM   831  C  CD2   A HIS   A 1 95  ? -17.26400 9.60100   2.45900   0.500 12.26620 ? 94  HIS   A CD2   1 
ATOM   832  C  CD2   B HIS   A 1 95  ? -17.75800 9.43400   2.03700   0.500 19.18807 ? 94  HIS   A CD2   1 
ATOM   833  C  CE1   A HIS   A 1 95  ? -16.63600 10.39700  4.40400   0.500 12.34366 ? 94  HIS   A CE1   1 
ATOM   834  C  CE1   B HIS   A 1 95  ? -18.89100 8.64100   0.33600   0.500 19.30599 ? 94  HIS   A CE1   1 
ATOM   835  N  NE2   A HIS   A 1 95  ? -16.52700 9.36000   3.59200   0.500 12.23616 ? 94  HIS   A NE2   1 
ATOM   836  N  NE2   B HIS   A 1 95  ? -18.02700 8.31900   1.28300   0.500 21.13305 ? 94  HIS   A NE2   1 
ATOM   837  N  N     . HIS   A 1 96  ? -16.61900 11.38100  -0.61400  1.000 11.97845 ? 95  HIS   A N     1 
ATOM   838  C  CA    . HIS   A 1 96  ? -15.37000 10.84000  -1.15900  1.000 12.70766 ? 95  HIS   A CA    1 
ATOM   839  C  C     . HIS   A 1 96  ? -14.44300 11.95900  -1.60800  1.000 10.28800 ? 95  HIS   A C     1 
ATOM   840  O  O     . HIS   A 1 96  ? -13.23700 11.93200  -1.34100  1.000 10.09238 ? 95  HIS   A O     1 
ATOM   841  C  CB    . HIS   A 1 96  ? -15.64700 9.96900   -2.39200  1.000 17.00209 ? 95  HIS   A CB    1 
ATOM   842  C  CG    . HIS   A 1 96  ? -16.16200 8.59600   -2.10100  1.000 21.06374 ? 95  HIS   A CG    1 
ATOM   843  N  ND1   . HIS   A 1 96  ? -15.77100 7.85800   -1.00400  1.000 23.54473 ? 95  HIS   A ND1   1 
ATOM   844  C  CD2   . HIS   A 1 96  ? -17.01700 7.81000   -2.79700  1.000 23.75600 ? 95  HIS   A CD2   1 
ATOM   845  C  CE1   . HIS   A 1 96  ? -16.37700 6.68400   -1.02600  1.000 25.75594 ? 95  HIS   A CE1   1 
ATOM   846  N  NE2   . HIS   A 1 96  ? -17.13500 6.62800   -2.10700  1.000 24.67149 ? 95  HIS   A NE2   1 
ATOM   847  N  N     . TYR   A 1 97  ? -14.98400 12.93300  -2.34300  1.000 9.41632  ? 96  TYR   A N     1 
ATOM   848  C  CA    . TYR   A 1 97  ? -14.15200 14.02200  -2.84300  1.000 8.88965  ? 96  TYR   A CA    1 
ATOM   849  C  C     . TYR   A 1 97  ? -13.63900 14.87900  -1.69900  1.000 8.61669  ? 96  TYR   A C     1 
ATOM   850  O  O     . TYR   A 1 97  ? -12.48100 15.30400  -1.70900  1.000 9.55803  ? 96  TYR   A O     1 
ATOM   851  C  CB    . TYR   A 1 97  ? -14.92200 14.85900  -3.87700  1.000 9.27349  ? 96  TYR   A CB    1 
ATOM   852  C  CG    . TYR   A 1 97  ? -15.21600 14.07200  -5.13800  1.000 8.67499  ? 96  TYR   A CG    1 
ATOM   853  C  CD1   . TYR   A 1 97  ? -14.23800 13.88800  -6.10800  1.000 9.27157  ? 96  TYR   A CD1   1 
ATOM   854  C  CD2   . TYR   A 1 97  ? -16.45400 13.47600  -5.34100  1.000 8.94799  ? 96  TYR   A CD2   1 
ATOM   855  C  CE1   . TYR   A 1 97  ? -14.48300 13.14800  -7.25100  1.000 8.69599  ? 96  TYR   A CE1   1 
ATOM   856  C  CE2   . TYR   A 1 97  ? -16.71300 12.72500  -6.48100  1.000 9.47065  ? 96  TYR   A CE2   1 
ATOM   857  C  CZ    . TYR   A 1 97  ? -15.72200 12.56100  -7.43500  1.000 9.12886  ? 96  TYR   A CZ    1 
ATOM   858  O  OH    . TYR   A 1 97  ? -15.94400 11.81500  -8.57800  1.000 10.04795 ? 96  TYR   A OH    1 
ATOM   859  N  N     . ARG   A 1 98  ? -14.48700 15.13100  -0.69900  1.000 8.92158  ? 97  ARG   A N     1 
ATOM   860  C  CA    . ARG   A 1 98  ? -14.06300 15.86600  0.48800   1.000 10.50009 ? 97  ARG   A CA    1 
ATOM   861  C  C     . ARG   A 1 98  ? -12.90000 15.16700  1.17800   1.000 9.53568  ? 97  ARG   A C     1 
ATOM   862  O  O     . ARG   A 1 98  ? -11.90600 15.80400  1.55100   1.000 10.54742 ? 97  ARG   A O     1 
ATOM   863  C  CB    . ARG   A 1 98  ? -15.26000 16.00000  1.43100   1.000 13.44737 ? 97  ARG   A CB    1 
ATOM   864  C  CG    . ARG   A 1 98  ? -14.95100 16.42100  2.85800   1.000 17.17704 ? 97  ARG   A CG    1 
ATOM   865  C  CD    . ARG   A 1 98  ? -14.94700 17.91900  2.98700   1.000 18.24558 ? 97  ARG   A CD    1 
ATOM   866  N  NE    . ARG   A 1 98  ? -14.85300 18.34200  4.37900   1.000 18.95497 ? 97  ARG   A NE    1 
ATOM   867  C  CZ    . ARG   A 1 98  ? -14.77800 19.60700  4.76800   1.000 22.42251 ? 97  ARG   A CZ    1 
ATOM   868  N  NH1   . ARG   A 1 98  ? -14.78400 20.59900  3.89100   1.000 24.46121 ? 97  ARG   A NH1   1 
ATOM   869  N  NH2   . ARG   A 1 98  ? -14.70000 19.88300  6.06700   1.000 23.76641 ? 97  ARG   A NH2   1 
ATOM   870  N  N     . GLU   A 1 99  ? -13.01000 13.85100  1.36700   1.000 9.72308  ? 98  GLU   A N     1 
ATOM   871  C  CA    . GLU   A 1 99  ? -11.93400 13.11100  2.02000   1.000 10.55130 ? 98  GLU   A CA    1 
ATOM   872  C  C     . GLU   A 1 99  ? -10.67000 13.10600  1.16600   1.000 9.35204  ? 98  GLU   A C     1 
ATOM   873  O  O     . GLU   A 1 99  ? -9.55800  13.19000  1.69200   1.000 10.49711 ? 98  GLU   A O     1 
ATOM   874  C  CB    . GLU   A 1 99  ? -12.39300 11.68600  2.32600   1.000 12.53841 ? 98  GLU   A CB    1 
ATOM   875  C  CG    . GLU   A 1 99  ? -13.44600 11.61200  3.41600   1.000 16.42330 ? 98  GLU   A CG    1 
ATOM   876  C  CD    . GLU   A 1 99  ? -12.95400 12.17700  4.73800   1.000 23.69007 ? 98  GLU   A CD    1 
ATOM   877  O  OE1   . GLU   A 1 99  ? -11.90300 11.70900  5.23200   1.000 27.14287 ? 98  GLU   A OE1   1 
ATOM   878  O  OE2   . GLU   A 1 99  ? -13.60700 13.09500  5.27600   1.000 27.92043 ? 98  GLU   A OE2   1 
ATOM   879  N  N     . GLN   A 1 100 ? -10.82400 13.00500  -0.15700  1.000 9.52789  ? 99  GLN   A N     1 
ATOM   880  C  CA    . GLN   A 1 100 ? -9.66400  13.04200  -1.04300  1.000 9.22100  ? 99  GLN   A CA    1 
ATOM   881  C  C     . GLN   A 1 100 ? -8.93700  14.37800  -0.94000  1.000 8.97043  ? 99  GLN   A C     1 
ATOM   882  O  O     . GLN   A 1 100 ? -7.70200  14.42200  -0.88300  1.000 9.67406  ? 99  GLN   A O     1 
ATOM   883  C  CB    . GLN   A 1 100 ? -10.10100 12.76800  -2.48200  1.000 9.44799  ? 99  GLN   A CB    1 
ATOM   884  C  CG    . GLN   A 1 100 ? -8.96400  12.77000  -3.49100  1.000 9.46427  ? 99  GLN   A CG    1 
ATOM   885  C  CD    . GLN   A 1 100 ? -9.45000  12.43600  -4.88900  1.000 9.31868  ? 99  GLN   A CD    1 
ATOM   886  O  OE1   . GLN   A 1 100 ? -10.57500 12.78200  -5.26200  1.000 9.57447  ? 99  GLN   A OE1   1 
ATOM   887  N  NE2   . GLN   A 1 100 ? -8.61500  11.74800  -5.66600  1.000 9.64057  ? 99  GLN   A NE2   1 
ATOM   888  N  N     . ILE   A 1 101 ? -9.69000  15.48000  -0.89900  1.000 9.02885  ? 100 ILE   A N     1 
ATOM   889  C  CA    . ILE   A 1 101 ? -9.08100  16.80300  -0.75200  1.000 9.98652  ? 100 ILE   A CA    1 
ATOM   890  C  C     . ILE   A 1 101 ? -8.30000  16.89100  0.55400   1.000 10.36191 ? 100 ILE   A C     1 
ATOM   891  O  O     . ILE   A 1 101 ? -7.14200  17.32700  0.58000   1.000 11.35619 ? 100 ILE   A O     1 
ATOM   892  C  CB    . ILE   A 1 101 ? -10.15600 17.89900  -0.82600  1.000 9.51198  ? 100 ILE   A CB    1 
ATOM   893  C  CG1   . ILE   A 1 101 ? -10.74500 17.99400  -2.23000  1.000 9.55653  ? 100 ILE   A CG1   1 
ATOM   894  C  CG2   . ILE   A 1 101 ? -9.55100  19.23300  -0.41600  1.000 11.53871 ? 100 ILE   A CG2   1 
ATOM   895  C  CD1   . ILE   A 1 101 ? -12.06300 18.74300  -2.29400  1.000 10.23822 ? 100 ILE   A CD1   1 
ATOM   896  N  N     . LYS   A 1 102 ? -8.92800  16.49400  1.66600   1.000 11.21549 ? 101 LYS   A N     1 
ATOM   897  C  CA    . LYS   A 1 102 ? -8.25800  16.58000  2.96200   1.000 13.40447 ? 101 LYS   A CA    1 
ATOM   898  C  C     . LYS   A 1 102 ? -6.98600  15.74300  2.98000   1.000 13.40628 ? 101 LYS   A C     1 
ATOM   899  O  O     . LYS   A 1 102 ? -5.97300  16.15000  3.56000   1.000 14.56434 ? 101 LYS   A O     1 
ATOM   900  C  CB    . LYS   A 1 102 ? -9.22100  16.16300  4.07400   1.000 16.05643 ? 101 LYS   A CB    1 
ATOM   901  C  CG    . LYS   A 1 102 ? -10.32400 17.18800  4.31400   1.000 19.58254 ? 101 LYS   A CG    1 
ATOM   902  C  CD    . LYS   A 1 102 ? -11.50900 16.59900  5.06400   1.000 24.58824 ? 101 LYS   A CD    1 
ATOM   903  C  CE    . LYS   A 1 102 ? -11.09100 15.92600  6.35500   1.000 27.41590 ? 101 LYS   A CE    1 
ATOM   904  N  NZ    . LYS   A 1 102 ? -12.27600 15.44300  7.11800   1.000 28.79006 ? 101 LYS   A NZ    1 
ATOM   905  N  N     . ARG   A 1 103 ? -7.01300  14.58600  2.32100   1.000 13.15663 ? 102 ARG   A N     1 
ATOM   906  C  CA    . ARG   A 1 103 ? -5.84300  13.71800  2.27900   1.000 13.51764 ? 102 ARG   A CA    1 
ATOM   907  C  C     . ARG   A 1 103 ? -4.73300  14.31700  1.42100   1.000 13.28249 ? 102 ARG   A C     1 
ATOM   908  O  O     . ARG   A 1 103 ? -3.57700  14.40300  1.85600   1.000 14.12175 ? 102 ARG   A O     1 
ATOM   909  C  CB    . ARG   A 1 103 ? -6.25400  12.33700  1.76700   1.000 14.68132 ? 102 ARG   A CB    1 
ATOM   910  C  CG    . ARG   A 1 103 ? -5.09600  11.37500  1.63900   1.000 14.98329 ? 102 ARG   A CG    1 
ATOM   911  C  CD    . ARG   A 1 103 ? -5.55900  9.96900   1.27000   1.000 14.13863 ? 102 ARG   A CD    1 
ATOM   912  N  NE    . ARG   A 1 103 ? -6.42800  9.97000   0.09700   1.000 13.42890 ? 102 ARG   A NE    1 
ATOM   913  C  CZ    . ARG   A 1 103 ? -6.00300  10.08800  -1.15400  1.000 13.14618 ? 102 ARG   A CZ    1 
ATOM   914  N  NH1   . ARG   A 1 103 ? -4.71800  10.24600  -1.43500  1.000 13.50466 ? 102 ARG   A NH1   1 
ATOM   915  N  NH2   . ARG   A 1 103 ? -6.89000  10.05900  -2.14700  1.000 13.76579 ? 102 ARG   A NH2   1 
ATOM   916  N  N     . VAL   A 1 104 ? -5.05800  14.73500  0.19300   1.000 13.40582 ? 103 VAL   A N     1 
ATOM   917  C  CA    . VAL   A 1 104 ? -4.00800  15.21500  -0.70800  1.000 13.84202 ? 103 VAL   A CA    1 
ATOM   918  C  C     . VAL   A 1 104 ? -3.44900  16.56300  -0.26700  1.000 15.03592 ? 103 VAL   A C     1 
ATOM   919  O  O     . VAL   A 1 104 ? -2.26700  16.85000  -0.49300  1.000 17.17055 ? 103 VAL   A O     1 
ATOM   920  C  CB    . VAL   A 1 104 ? -4.42800  15.21400  -2.19400  1.000 15.75855 ? 103 VAL   A CB    1 
ATOM   921  C  CG1   . VAL   A 1 104 ? -4.92200  13.83300  -2.62100  1.000 15.67559 ? 103 VAL   A CG1   1 
ATOM   922  C  CG2   . VAL   A 1 104 ? -5.45000  16.30300  -2.49100  1.000 17.05315 ? 103 VAL   A CG2   1 
ATOM   923  N  N     . LYS   A 1 105 ? -4.27100  17.41700  0.33700   1.000 13.07215 ? 104 LYS   A N     1 
ATOM   924  C  CA    . LYS   A 1 105 ? -3.77600  18.67800  0.87200   1.000 14.15165 ? 104 LYS   A CA    1 
ATOM   925  C  C     . LYS   A 1 105 ? -3.22900  18.52500  2.28200   1.000 16.24726 ? 104 LYS   A C     1 
ATOM   926  O  O     . LYS   A 1 105 ? -2.63600  19.47300  2.81200   1.000 17.72281 ? 104 LYS   A O     1 
ATOM   927  C  CB    . LYS   A 1 105 ? -4.86300  19.75900  0.82600   1.000 13.53985 ? 104 LYS   A CB    1 
ATOM   928  C  CG    . LYS   A 1 105 ? -5.36600  20.06900  -0.57900  1.000 13.38745 ? 104 LYS   A CG    1 
ATOM   929  C  CD    . LYS   A 1 105 ? -4.23800  20.40800  -1.56300  1.000 13.95605 ? 104 LYS   A CD    1 
ATOM   930  C  CE    . LYS   A 1 105 ? -3.45600  21.64300  -1.16900  1.000 15.52066 ? 104 LYS   A CE    1 
ATOM   931  N  NZ    . LYS   A 1 105 ? -2.45400  21.98500  -2.22100  1.000 15.88764 ? 104 LYS   A NZ    1 
ATOM   932  N  N     . ASP   A 1 106 ? -3.40200  17.34800  2.88500   1.000 15.90143 ? 105 ASP   A N     1 
ATOM   933  C  CA    . ASP   A 1 106 ? -2.88300  17.05800  4.21900   1.000 17.13456 ? 105 ASP   A CA    1 
ATOM   934  C  C     . ASP   A 1 106 ? -3.32800  18.11900  5.22400   1.000 17.92504 ? 105 ASP   A C     1 
ATOM   935  O  O     . ASP   A 1 106 ? -2.53500  18.65500  6.00200   1.000 20.09757 ? 105 ASP   A O     1 
ATOM   936  C  CB    . ASP   A 1 106 ? -1.36000  16.89800  4.20400   1.000 20.49096 ? 105 ASP   A CB    1 
ATOM   937  C  CG    . ASP   A 1 106 ? -0.83700  16.19400  5.43600   1.000 23.03324 ? 105 ASP   A CG    1 
ATOM   938  O  OD1   . ASP   A 1 106 ? -1.57800  15.36400  6.00700   1.000 23.75971 ? 105 ASP   A OD1   1 
ATOM   939  O  OD2   . ASP   A 1 106 ? 0.31300   16.47900  5.83800   1.000 24.53261 ? 105 ASP   A OD2   1 
ATOM   940  N  N     . SER   A 1 107 ? -4.62100  18.42600  5.19600   1.000 17.24074 ? 106 SER   A N     1 
ATOM   941  C  CA    . SER   A 1 107 ? -5.14900  19.49300  6.03000   1.000 17.98227 ? 106 SER   A CA    1 
ATOM   942  C  C     . SER   A 1 107 ? -6.63400  19.27200  6.26200   1.000 18.41136 ? 106 SER   A C     1 
ATOM   943  O  O     . SER   A 1 107 ? -7.35300  18.79600  5.37900   1.000 18.16575 ? 106 SER   A O     1 
ATOM   944  C  CB    . SER   A 1 107 ? -4.93000  20.86500  5.38100   1.000 19.77191 ? 106 SER   A CB    1 
ATOM   945  O  OG    . SER   A 1 107 ? -5.55800  21.87900  6.14400   1.000 21.97549 ? 106 SER   A OG    1 
ATOM   946  N  N     . GLU   A 1 108 ? -7.08500  19.65100  7.45400   1.000 19.69655 ? 107 GLU   A N     1 
ATOM   947  C  CA    . GLU   A 1 108 ? -8.50000  19.63300  7.78800   1.000 22.87138 ? 107 GLU   A CA    1 
ATOM   948  C  C     . GLU   A 1 108 ? -9.21500  20.91400  7.38800   1.000 24.81046 ? 107 GLU   A C     1 
ATOM   949  O  O     . GLU   A 1 108 ? -10.44500 20.97700  7.49200   1.000 26.83820 ? 107 GLU   A O     1 
ATOM   950  C  CB    . GLU   A 1 108 ? -8.67500  19.41100  9.29400   1.000 24.97907 ? 107 GLU   A CB    1 
ATOM   951  C  CG    . GLU   A 1 108 ? -8.16600  18.06700  9.77000   1.000 29.23867 ? 107 GLU   A CG    1 
ATOM   952  C  CD    . GLU   A 1 108 ? -8.96400  16.91900  9.19000   1.000 33.87637 ? 107 GLU   A CD    1 
ATOM   953  O  OE1   . GLU   A 1 108 ? -10.21000 17.00500  9.19500   1.000 35.79312 ? 107 GLU   A OE1   1 
ATOM   954  O  OE2   . GLU   A 1 108 ? -8.34900  15.93900  8.72100   1.000 35.86739 ? 107 GLU   A OE2   1 
ATOM   955  N  N     . ASP   A 1 109 ? -8.47700  21.92700  6.93400   1.000 23.94842 ? 108 ASP   A N     1 
ATOM   956  C  CA    . ASP   A 1 109 ? -9.00800  23.26000  6.64500   1.000 25.09277 ? 108 ASP   A CA    1 
ATOM   957  C  C     . ASP   A 1 109 ? -8.52700  23.63000  5.24500   1.000 22.46920 ? 108 ASP   A C     1 
ATOM   958  O  O     . ASP   A 1 109 ? -7.46400  24.23800  5.08900   1.000 25.89678 ? 108 ASP   A O     1 
ATOM   959  C  CB    . ASP   A 1 109 ? -8.50300  24.24600  7.70300   1.000 30.04408 ? 108 ASP   A CB    1 
ATOM   960  C  CG    . ASP   A 1 109 ? -8.88400  25.68600  7.40100   1.000 36.03726 ? 108 ASP   A CG    1 
ATOM   961  O  OD1   . ASP   A 1 109 ? -9.87500  25.91100  6.67500   1.000 38.40030 ? 108 ASP   A OD1   1 
ATOM   962  O  OD2   . ASP   A 1 109 ? -8.18100  26.59600  7.89300   1.000 38.06734 ? 108 ASP   A OD2   1 
ATOM   963  N  N     . VAL   A 1 110 ? -9.29700  23.25600  4.22900   1.000 15.72416 ? 109 VAL   A N     1 
ATOM   964  C  CA    . VAL   A 1 110 ? -8.96500  23.52000  2.83600   1.000 12.93513 ? 109 VAL   A CA    1 
ATOM   965  C  C     . VAL   A 1 110 ? -10.08400 24.36300  2.23400   1.000 11.50095 ? 109 VAL   A C     1 
ATOM   966  O  O     . VAL   A 1 110 ? -11.25600 24.02700  2.41000   1.000 11.58070 ? 109 VAL   A O     1 
ATOM   967  C  CB    . VAL   A 1 110 ? -8.78800  22.22700  2.02000   1.000 12.23156 ? 109 VAL   A CB    1 
ATOM   968  C  CG1   . VAL   A 1 110 ? -8.42300  22.55000  0.58300   1.000 12.08823 ? 109 VAL   A CG1   1 
ATOM   969  C  CG2   . VAL   A 1 110 ? -7.74500  21.31600  2.65900   1.000 14.35311 ? 109 VAL   A CG2   1 
ATOM   970  N  N     . PRO   A 1 111 ? -9.77600  25.42900  1.49500   1.000 10.18061 ? 110 PRO   A N     1 
ATOM   971  C  CA    . PRO   A 1 111 ? -10.84200 26.20600  0.84300   1.000 10.23835 ? 110 PRO   A CA    1 
ATOM   972  C  C     . PRO   A 1 111 ? -11.65100 25.35500  -0.12800  1.000 8.73973  ? 110 PRO   A C     1 
ATOM   973  O  O     . PRO   A 1 111 ? -11.09800 24.70100  -1.01800  1.000 9.53705  ? 110 PRO   A O     1 
ATOM   974  C  CB    . PRO   A 1 111 ? -10.06900 27.31400  0.11700   1.000 10.70431 ? 110 PRO   A CB    1 
ATOM   975  C  CG    . PRO   A 1 111 ? -8.79200  27.46200  0.91100   1.000 11.95290 ? 110 PRO   A CG    1 
ATOM   976  C  CD    . PRO   A 1 111 ? -8.45100  26.06100  1.34600   1.000 11.71753 ? 110 PRO   A CD    1 
ATOM   977  N  N     . MET   A 1 112 ? -12.97400 25.36400  0.05300   1.000 8.84572  ? 111 MET   A N     1 
ATOM   978  C  CA    . MET   A 1 112 ? -13.87800 24.54600  -0.74600  1.000 9.76026  ? 111 MET   A CA    1 
ATOM   979  C  C     . MET   A 1 112 ? -15.24200 25.21600  -0.79400  1.000 8.07056  ? 111 MET   A C     1 
ATOM   980  O  O     . MET   A 1 112 ? -15.64200 25.92900  0.13500   1.000 9.18237  ? 111 MET   A O     1 
ATOM   981  C  CB    . MET   A 1 112 ? -14.13100 23.15800  -0.12100  1.000 13.01675 ? 111 MET   A CB    1 
ATOM   982  C  CG    . MET   A 1 112 ? -12.94400 22.24900  0.09900   1.000 13.76245 ? 111 MET   A CG    1 
ATOM   983  S  SD    . MET   A 1 112 ? -13.52500 20.71100  0.84600   1.000 15.53162 ? 111 MET   A SD    1 
ATOM   984  C  CE    . MET   A 1 112 ? -12.08900 20.27100  1.81600   1.000 19.38925 ? 111 MET   A CE    1 
ATOM   985  N  N     . VAL   A 1 113 ? -15.98000 24.92100  -1.86100  1.000 7.95276  ? 112 VAL   A N     1 
ATOM   986  C  CA    . VAL   A 1 113 ? -17.36500 25.35400  -2.02000  1.000 7.79249  ? 112 VAL   A CA    1 
ATOM   987  C  C     . VAL   A 1 113 ? -18.16000 24.16800  -2.54600  1.000 7.29157  ? 112 VAL   A C     1 
ATOM   988  O  O     . VAL   A 1 113 ? -17.71500 23.48600  -3.47600  1.000 8.25559  ? 112 VAL   A O     1 
ATOM   989  C  CB    . VAL   A 1 113 ? -17.46900 26.55000  -2.99200  1.000 8.34357  ? 112 VAL   A CB    1 
ATOM   990  C  CG1   . VAL   A 1 113 ? -18.92300 26.87300  -3.31900  1.000 9.70314  ? 112 VAL   A CG1   1 
ATOM   991  C  CG2   . VAL   A 1 113 ? -16.74900 27.76600  -2.42900  1.000 9.22053  ? 112 VAL   A CG2   1 
ATOM   992  N  N     . LEU   A 1 114 ? -19.32600 23.91200  -1.94700  1.000 7.44435  ? 113 LEU   A N     1 
ATOM   993  C  CA    . LEU   A 1 114 ? -20.24000 22.89200  -2.44500  1.000 7.36357  ? 113 LEU   A CA    1 
ATOM   994  C  C     . LEU   A 1 114 ? -21.13700 23.50700  -3.51100  1.000 7.55258  ? 113 LEU   A C     1 
ATOM   995  O  O     . LEU   A 1 114 ? -21.74000 24.56000  -3.28200  1.000 8.10889  ? 113 LEU   A O     1 
ATOM   996  C  CB    . LEU   A 1 114 ? -21.10100 22.34300  -1.30600  1.000 7.97525  ? 113 LEU   A CB    1 
ATOM   997  C  CG    . LEU   A 1 114 ? -22.04500 21.18700  -1.67000  1.000 8.68264  ? 113 LEU   A CG    1 
ATOM   998  C  CD1   . LEU   A 1 114 ? -21.27200 19.94500  -2.12200  1.000 9.15875  ? 113 LEU   A CD1   1 
ATOM   999  C  CD2   . LEU   A 1 114 ? -22.96800 20.85400  -0.49700  1.000 9.37738  ? 113 LEU   A CD2   1 
ATOM   1000 N  N     . VAL   A 1 115 ? -21.23300 22.84500  -4.66300  1.000 7.26796  ? 114 VAL   A N     1 
ATOM   1001 C  CA    . VAL   A 1 115 ? -21.95900 23.36100  -5.81800  1.000 6.88892  ? 114 VAL   A CA    1 
ATOM   1002 C  C     . VAL   A 1 115 ? -23.05400 22.37100  -6.19400  1.000 6.97716  ? 114 VAL   A C     1 
ATOM   1003 O  O     . VAL   A 1 115 ? -22.76500 21.21500  -6.53200  1.000 7.83358  ? 114 VAL   A O     1 
ATOM   1004 C  CB    . VAL   A 1 115 ? -21.02300 23.60500  -7.01200  1.000 7.37164  ? 114 VAL   A CB    1 
ATOM   1005 C  CG1   . VAL   A 1 115 ? -21.82300 24.00700  -8.25400  1.000 9.20171  ? 114 VAL   A CG1   1 
ATOM   1006 C  CG2   . VAL   A 1 115 ? -19.96900 24.64200  -6.65500  1.000 8.49863  ? 114 VAL   A CG2   1 
ATOM   1007 N  N     . GLY   A 1 116 ? -24.30500 22.83200  -6.15900  1.000 7.19138  ? 115 GLY   A N     1 
ATOM   1008 C  CA    . GLY   A 1 116 ? -25.44100 22.05400  -6.61500  1.000 7.70098  ? 115 GLY   A CA    1 
ATOM   1009 C  C     . GLY   A 1 116 ? -25.84900 22.48800  -8.00800  1.000 7.21528  ? 115 GLY   A C     1 
ATOM   1010 O  O     . GLY   A 1 116 ? -26.52500 23.51000  -8.17100  1.000 8.00361  ? 115 GLY   A O     1 
ATOM   1011 N  N     . ASN   A 1 117 ? -25.41100 21.74800  -9.02500  1.000 7.16868  ? 116 ASN   A N     1 
ATOM   1012 C  CA    . ASN   A 1 117 ? -25.58200 22.15500  -10.40900 1.000 7.45493  ? 116 ASN   A CA    1 
ATOM   1013 C  C     . ASN   A 1 117 ? -26.85200 21.56500  -11.02900 1.000 6.69418  ? 116 ASN   A C     1 
ATOM   1014 O  O     . ASN   A 1 117 ? -27.48600 20.65100  -10.48600 1.000 7.71711  ? 116 ASN   A O     1 
ATOM   1015 C  CB    . ASN   A 1 117 ? -24.33700 21.79000  -11.22700 1.000 7.33887  ? 116 ASN   A CB    1 
ATOM   1016 C  CG    . ASN   A 1 117 ? -24.31600 22.45200  -12.59200 1.000 7.43260  ? 116 ASN   A CG    1 
ATOM   1017 O  OD1   . ASN   A 1 117 ? -24.60200 23.64800  -12.71500 1.000 7.76565  ? 116 ASN   A OD1   1 
ATOM   1018 N  ND2   . ASN   A 1 117 ? -23.99700 21.67800  -13.62800 1.000 7.57529  ? 116 ASN   A ND2   1 
ATOM   1019 N  N     . LYS   A 1 118 ? -27.20200 22.10500  -12.20300 1.000 7.17099  ? 117 LYS   A N     1 
ATOM   1020 C  CA    . LYS   A 1 118 ? -28.40200 21.75600  -12.96300 1.000 7.56210  ? 117 LYS   A CA    1 
ATOM   1021 C  C     . LYS   A 1 118 ? -29.66600 22.29200  -12.30600 1.000 7.48010  ? 117 LYS   A C     1 
ATOM   1022 O  O     . LYS   A 1 118 ? -30.73400 21.69500  -12.40500 1.000 8.32207  ? 117 LYS   A O     1 
ATOM   1023 C  CB    . LYS   A 1 118 ? -28.49800 20.26700  -13.33600 1.000 8.19692  ? 117 LYS   A CB    1 
ATOM   1024 C  CG    . LYS   A 1 118 ? -27.19100 19.67800  -13.86200 1.000 8.31644  ? 117 LYS   A CG    1 
ATOM   1025 C  CD    . LYS   A 1 118 ? -27.40200 18.41200  -14.68600 1.000 8.44566  ? 117 LYS   A CD    1 
ATOM   1026 C  CE    . LYS   A 1 118 ? -26.07600 17.83200  -15.16600 1.000 8.91373  ? 117 LYS   A CE    1 
ATOM   1027 N  NZ    . LYS   A 1 118 ? -26.26900 16.60800  -15.97700 1.000 8.97191  ? 117 LYS   A NZ    1 
ATOM   1028 N  N     . SER   A 1 119 ? -29.55400 23.45400  -11.65900 1.000 7.82895  ? 118 SER   A N     1 
ATOM   1029 C  CA    . SER   A 1 119 ? -30.68500 24.03500  -10.94800 1.000 8.80604  ? 118 SER   A CA    1 
ATOM   1030 C  C     . SER   A 1 119 ? -31.78700 24.52600  -11.88400 1.000 9.16565  ? 118 SER   A C     1 
ATOM   1031 O  O     . SER   A 1 119 ? -32.86400 24.89000  -11.40400 1.000 10.58175 ? 118 SER   A O     1 
ATOM   1032 C  CB    . SER   A 1 119 ? -30.19400 25.15500  -10.02400 1.000 9.69733  ? 118 SER   A CB    1 
ATOM   1033 O  OG    . SER   A 1 119 ? -29.27500 24.65100  -9.06000  1.000 11.91602 ? 118 SER   A OG    1 
ATOM   1034 N  N     . ASP   A 1 120 ? -31.55500 24.52900  -13.19500 1.000 9.17184  ? 119 ASP   A N     1 
ATOM   1035 C  CA    . ASP   A 1 120 ? -32.58000 24.85000  -14.17800 1.000 9.87268  ? 119 ASP   A CA    1 
ATOM   1036 C  C     . ASP   A 1 120 ? -33.58500 23.72100  -14.37700 1.000 10.16675 ? 119 ASP   A C     1 
ATOM   1037 O  O     . ASP   A 1 120 ? -34.63500 23.95300  -14.97900 1.000 11.44512 ? 119 ASP   A O     1 
ATOM   1038 C  CB    . ASP   A 1 120 ? -31.91400 25.11800  -15.52700 1.000 10.13098 ? 119 ASP   A CB    1 
ATOM   1039 C  CG    . ASP   A 1 120 ? -31.05300 23.96000  -15.97100 1.000 9.64759  ? 119 ASP   A CG    1 
ATOM   1040 O  OD1   . ASP   A 1 120 ? -29.92100 23.83900  -15.45000 1.000 8.98448  ? 119 ASP   A OD1   1 
ATOM   1041 O  OD2   . ASP   A 1 120 ? -31.52100 23.14600  -16.80000 1.000 10.20012 ? 119 ASP   A OD2   1 
ATOM   1042 N  N     . LEU   A 1 121 ? -33.28900 22.50800  -13.91300 1.000 9.44430  ? 120 LEU   A N     1 
ATOM   1043 C  CA    . LEU   A 1 121 ? -34.11500 21.36200  -14.26500 1.000 9.62597  ? 120 LEU   A CA    1 
ATOM   1044 C  C     . LEU   A 1 121 ? -35.44600 21.39200  -13.52000 1.000 9.97528  ? 120 LEU   A C     1 
ATOM   1045 O  O     . LEU   A 1 121 ? -35.52500 21.86400  -12.38100 1.000 10.81832 ? 120 LEU   A O     1 
ATOM   1046 C  CB    . LEU   A 1 121 ? -33.38900 20.06200  -13.94200 1.000 10.48334 ? 120 LEU   A CB    1 
ATOM   1047 C  CG    . LEU   A 1 121 ? -32.20800 19.75100  -14.85600 1.000 11.01082 ? 120 LEU   A CG    1 
ATOM   1048 C  CD1   . LEU   A 1 121 ? -31.53300 18.46100  -14.38600 1.000 12.28079 ? 120 LEU   A CD1   1 
ATOM   1049 C  CD2   . LEU   A 1 121 ? -32.65000 19.63800  -16.32000 1.000 12.44106 ? 120 LEU   A CD2   1 
ATOM   1050 N  N     . PRO   A 1 122 ? -36.50800 20.87500  -14.14200 1.000 10.14602 ? 121 PRO   A N     1 
ATOM   1051 C  CA    . PRO   A 1 122 ? -37.82100 20.84800  -13.49200 1.000 10.89557 ? 121 PRO   A CA    1 
ATOM   1052 C  C     . PRO   A 1 122 ? -38.00200 19.72400  -12.49000 1.000 11.42727 ? 121 PRO   A C     1 
ATOM   1053 O  O     . PRO   A 1 122 ? -39.06000 19.65500  -11.85800 1.000 12.50278 ? 121 PRO   A O     1 
ATOM   1054 C  CB    . PRO   A 1 122 ? -38.77400 20.65700  -14.67800 1.000 12.16860 ? 121 PRO   A CB    1 
ATOM   1055 C  CG    . PRO   A 1 122 ? -37.97500 19.86600  -15.65300 1.000 12.42638 ? 121 PRO   A CG    1 
ATOM   1056 C  CD    . PRO   A 1 122 ? -36.57300 20.41100  -15.54000 1.000 11.67204 ? 121 PRO   A CD    1 
ATOM   1057 N  N     . SER   A 1 123 ? -37.02100 18.83900  -12.33100 1.000 11.37972 ? 122 SER   A N     1 
ATOM   1058 C  CA    . SER   A 1 123 ? -37.14600 17.73800  -11.39000 1.000 11.31921 ? 122 SER   A CA    1 
ATOM   1059 C  C     . SER   A 1 123 ? -35.81400 17.54700  -10.68300 1.000 10.82705 ? 122 SER   A C     1 
ATOM   1060 O  O     . SER   A 1 123 ? -34.75700 17.93900  -11.18900 1.000 12.58372 ? 122 SER   A O     1 
ATOM   1061 C  CB    . SER   A 1 123 ? -37.56500 16.44100  -12.08300 1.000 12.35472 ? 122 SER   A CB    1 
ATOM   1062 O  OG    . SER   A 1 123 ? -36.48900 15.90200  -12.82700 1.000 13.30559 ? 122 SER   A OG    1 
ATOM   1063 N  N     . ARG   A 1 124 ? -35.87900 16.95100  -9.49400  1.000 9.59154  ? 123 ARG   A N     1 
ATOM   1064 C  CA    . ARG   A 1 124 ? -34.67600 16.75100  -8.70000  1.000 9.61584  ? 123 ARG   A CA    1 
ATOM   1065 C  C     . ARG   A 1 124 ? -34.88500 15.59400  -7.73500  1.000 9.18634  ? 123 ARG   A C     1 
ATOM   1066 O  O     . ARG   A 1 124 ? -36.01400 15.29400  -7.33100  1.000 10.21506 ? 123 ARG   A O     1 
ATOM   1067 C  CB    . ARG   A 1 124 ? -34.29000 18.02500  -7.94700  1.000 11.75634 ? 123 ARG   A CB    1 
ATOM   1068 C  CG    . ARG   A 1 124 ? -35.35900 18.51000  -6.99800  1.000 11.64482 ? 123 ARG   A CG    1 
ATOM   1069 C  CD    . ARG   A 1 124 ? -34.98600 19.87200  -6.41800  1.000 13.18387 ? 123 ARG   A CD    1 
ATOM   1070 N  NE    . ARG   A 1 124 ? -33.73000 19.79600  -5.67800  1.000 13.88104 ? 123 ARG   A NE    1 
ATOM   1071 C  CZ    . ARG   A 1 124 ? -32.81500 20.75700  -5.58500  1.000 12.63503 ? 123 ARG   A CZ    1 
ATOM   1072 N  NH1   . ARG   A 1 124 ? -32.97100 21.93800  -6.16900  1.000 12.69723 ? 123 ARG   A NH1   1 
ATOM   1073 N  NH2   . ARG   A 1 124 ? -31.70800 20.52200  -4.89500  1.000 12.66244 ? 123 ARG   A NH2   1 
ATOM   1074 N  N     . THR   A 1 125 ? -33.77100 14.95400  -7.37100  1.000 8.96286  ? 124 THR   A N     1 
ATOM   1075 C  CA    . THR   A 1 125 ? -33.76800 13.82200  -6.45300  1.000 9.47930  ? 124 THR   A CA    1 
ATOM   1076 C  C     . THR   A 1 125 ? -33.06000 14.12900  -5.14400  1.000 10.29314 ? 124 THR   A C     1 
ATOM   1077 O  O     . THR   A 1 125 ? -33.18300 13.34600  -4.19300  1.000 12.09665 ? 124 THR   A O     1 
ATOM   1078 C  CB    . THR   A 1 125 ? -33.11300 12.59300  -7.10400  1.000 9.54445  ? 124 THR   A CB    1 
ATOM   1079 O  OG1   . THR   A 1 125 ? -31.77100 12.92500  -7.46000  1.000 10.75371 ? 124 THR   A OG1   1 
ATOM   1080 C  CG2   . THR   A 1 125 ? -33.87600 12.14400  -8.34600  1.000 11.65100 ? 124 THR   A CG2   1 
ATOM   1081 N  N     . VAL   A 1 126 ? -32.32700 15.23700  -5.07000  1.000 9.54319  ? 125 VAL   A N     1 
ATOM   1082 C  CA    . VAL   A 1 126 ? -31.59800 15.65000  -3.87700  1.000 10.46225 ? 125 VAL   A CA    1 
ATOM   1083 C  C     . VAL   A 1 126 ? -32.23700 16.93500  -3.37000  1.000 10.59509 ? 125 VAL   A C     1 
ATOM   1084 O  O     . VAL   A 1 126 ? -32.41500 17.88300  -4.14200  1.000 11.99883 ? 125 VAL   A O     1 
ATOM   1085 C  CB    . VAL   A 1 126 ? -30.11400 15.88300  -4.21000  1.000 11.69372 ? 125 VAL   A CB    1 
ATOM   1086 C  CG1   . VAL   A 1 126 ? -29.35500 16.35400  -2.97900  1.000 12.58933 ? 125 VAL   A CG1   1 
ATOM   1087 C  CG2   . VAL   A 1 126 ? -29.49900 14.60600  -4.77500  1.000 13.51575 ? 125 VAL   A CG2   1 
ATOM   1088 N  N     . ASP   A 1 127 ? -32.58900 16.96900  -2.08300  1.000 13.32233 ? 126 ASP   A N     1 
ATOM   1089 C  CA    . ASP   A 1 127 ? -33.19100 18.16700  -1.50000  1.000 15.90954 ? 126 ASP   A CA    1 
ATOM   1090 C  C     . ASP   A 1 127 ? -32.15700 19.26700  -1.32600  1.000 14.21377 ? 126 ASP   A C     1 
ATOM   1091 O  O     . ASP   A 1 127 ? -31.02800 19.00900  -0.91200  1.000 14.41355 ? 126 ASP   A O     1 
ATOM   1092 C  CB    . ASP   A 1 127 ? -33.69300 17.86500  -0.08900  1.000 20.64273 ? 126 ASP   A CB    1 
ATOM   1093 C  CG    . ASP   A 1 127 ? -34.95900 17.07200  -0.06700  1.000 24.11341 ? 126 ASP   A CG    1 
ATOM   1094 O  OD1   . ASP   A 1 127 ? -35.58600 16.91300  -1.12800  1.000 27.34087 ? 126 ASP   A OD1   1 
ATOM   1095 O  OD2   . ASP   A 1 127 ? -35.33200 16.61400  1.03300   1.000 26.10812 ? 126 ASP   A OD2   1 
ATOM   1096 N  N     . THR   A 1 128 ? -32.56000 20.51700  -1.56700  1.000 14.04907 ? 127 THR   A N     1 
ATOM   1097 C  CA    A THR   A 1 128 ? -31.66400 21.62900  -1.26300  0.500 13.61781 ? 127 THR   A CA    1 
ATOM   1098 C  CA    B THR   A 1 128 ? -31.67200 21.63500  -1.26000  0.500 15.63103 ? 127 THR   A CA    1 
ATOM   1099 C  C     . THR   A 1 128 ? -31.25500 21.61400  0.20600   1.000 13.44494 ? 127 THR   A C     1 
ATOM   1100 O  O     . THR   A 1 128 ? -30.09900 21.89900  0.53600   1.000 12.54541 ? 127 THR   A O     1 
ATOM   1101 C  CB    A THR   A 1 128 ? -32.30100 22.96300  -1.66700  0.500 12.90909 ? 127 THR   A CB    1 
ATOM   1102 C  CB    B THR   A 1 128 ? -32.34300 22.96600  -1.61000  0.500 19.06108 ? 127 THR   A CB    1 
ATOM   1103 O  OG1   A THR   A 1 128 ? -32.26800 23.08800  -3.09100  0.500 13.05679 ? 127 THR   A OG1   1 
ATOM   1104 O  OG1   B THR   A 1 128 ? -33.53300 23.12900  -0.83000  0.500 21.34109 ? 127 THR   A OG1   1 
ATOM   1105 C  CG2   A THR   A 1 128 ? -31.55400 24.14700  -1.05000  0.500 13.05527 ? 127 THR   A CG2   1 
ATOM   1106 C  CG2   B THR   A 1 128 ? -32.71500 23.00100  -3.06100  0.500 20.67427 ? 127 THR   A CG2   1 
ATOM   1107 N  N     . LYS   A 1 129 ? -32.18300 21.25100  1.10000   1.000 12.02415 ? 128 LYS   A N     1 
ATOM   1108 C  CA    . LYS   A 1 129 ? -31.86600 21.18700  2.52500   1.000 11.78619 ? 128 LYS   A CA    1 
ATOM   1109 C  C     . LYS   A 1 129 ? -30.75100 20.18500  2.82300   1.000 9.90743  ? 128 LYS   A C     1 
ATOM   1110 O  O     . LYS   A 1 129 ? -29.91700 20.42600  3.70300   1.000 10.42487 ? 128 LYS   A O     1 
ATOM   1111 C  CB    . LYS   A 1 129 ? -33.12500 20.85300  3.32500   1.000 14.28903 ? 128 LYS   A CB    1 
ATOM   1112 C  CG    . LYS   A 1 129 ? -32.90400 20.69200  4.81700   1.000 20.26715 ? 128 LYS   A CG    1 
ATOM   1113 C  CD    . LYS   A 1 129 ? -32.40300 21.97500  5.45500   1.000 27.48547 ? 128 LYS   A CD    1 
ATOM   1114 C  CE    . LYS   A 1 129 ? -32.85900 22.07100  6.89800   1.000 32.44862 ? 128 LYS   A CE    1 
ATOM   1115 N  NZ    . LYS   A 1 129 ? -32.73800 20.76000  7.58500   1.000 35.45342 ? 128 LYS   A NZ    1 
ATOM   1116 N  N     . GLN   A 1 130 ? -30.72600 19.04700  2.11700   1.000 9.79677  ? 129 GLN   A N     1 
ATOM   1117 C  CA    . GLN   A 1 130 ? -29.62800 18.09700  2.29600   1.000 10.86125 ? 129 GLN   A CA    1 
ATOM   1118 C  C     . GLN   A 1 130 ? -28.29300 18.75100  1.99900   1.000 9.61556  ? 129 GLN   A C     1 
ATOM   1119 O  O     . GLN   A 1 130 ? -27.31000 18.53000  2.71500   1.000 10.32051 ? 129 GLN   A O     1 
ATOM   1120 C  CB    . GLN   A 1 130 ? -29.77200 16.92700  1.33200   1.000 12.89033 ? 129 GLN   A CB    1 
ATOM   1121 C  CG    . GLN   A 1 130 ? -30.82800 15.92300  1.65200   1.000 13.38295 ? 129 GLN   A CG    1 
ATOM   1122 C  CD    . GLN   A 1 130 ? -30.86700 14.85600  0.57700   1.000 12.96738 ? 129 GLN   A CD    1 
ATOM   1123 O  OE1   . GLN   A 1 130 ? -31.73300 14.86900  -0.29400  1.000 12.94683 ? 129 GLN   A OE1   1 
ATOM   1124 N  NE2   . GLN   A 1 130 ? -29.89000 13.95100  0.60900   1.000 13.37071 ? 129 GLN   A NE2   1 
ATOM   1125 N  N     . ALA   A 1 131 ? -28.22900 19.51600  0.90500   1.000 10.13438 ? 130 ALA   A N     1 
ATOM   1126 C  CA    . ALA   A 1 131 ? -26.97600 20.15200  0.51700   1.000 10.50125 ? 130 ALA   A CA    1 
ATOM   1127 C  C     . ALA   A 1 131 ? -26.60600 21.26100  1.48600   1.000 10.25608 ? 130 ALA   A C     1 
ATOM   1128 O  O     . ALA   A 1 131 ? -25.43600 21.40500  1.85700   1.000 10.75484 ? 130 ALA   A O     1 
ATOM   1129 C  CB    . ALA   A 1 131 ? -27.06500 20.68300  -0.91400  1.000 12.27309 ? 130 ALA   A CB    1 
ATOM   1130 N  N     . GLN   A 1 132 ? -27.59000 22.05500  1.91300   1.000 10.60260 ? 131 GLN   A N     1 
ATOM   1131 C  CA    . GLN   A 1 132 ? -27.30700 23.07600  2.91200   1.000 10.47033 ? 131 GLN   A CA    1 
ATOM   1132 C  C     . GLN   A 1 132 ? -26.77200 22.44900  4.18900   1.000 10.02898 ? 131 GLN   A C     1 
ATOM   1133 O  O     . GLN   A 1 132 ? -25.82000 22.96100  4.78700   1.000 11.00613 ? 131 GLN   A O     1 
ATOM   1134 C  CB    . GLN   A 1 132 ? -28.56400 23.89100  3.20700   1.000 12.35539 ? 131 GLN   A CB    1 
ATOM   1135 C  CG    . GLN   A 1 132 ? -29.03600 24.73100  2.03500   1.000 14.51718 ? 131 GLN   A CG    1 
ATOM   1136 C  CD    . GLN   A 1 132 ? -30.39100 25.35700  2.27600   1.000 18.06284 ? 131 GLN   A CD    1 
ATOM   1137 O  OE1   . GLN   A 1 132 ? -31.18300 24.86500  3.07700   1.000 19.62284 ? 131 GLN   A OE1   1 
ATOM   1138 N  NE2   . GLN   A 1 132 ? -30.66100 26.45300  1.58800   1.000 19.41042 ? 131 GLN   A NE2   1 
ATOM   1139 N  N     . ASP   A 1 133 ? -27.37800 21.33800  4.62700   1.000 9.87859  ? 132 ASP   A N     1 
ATOM   1140 C  CA    . ASP   A 1 133 ? -26.92200 20.68000  5.85100   1.000 9.94167  ? 132 ASP   A CA    1 
ATOM   1141 C  C     . ASP   A 1 133 ? -25.52500 20.09700  5.68300   1.000 9.95075  ? 132 ASP   A C     1 
ATOM   1142 O  O     . ASP   A 1 133 ? -24.71500 20.13700  6.61900   1.000 10.55415 ? 132 ASP   A O     1 
ATOM   1143 C  CB    . ASP   A 1 133 ? -27.89300 19.57100  6.24600   1.000 11.51944 ? 132 ASP   A CB    1 
ATOM   1144 C  CG    . ASP   A 1 133 ? -29.20600 20.09600  6.80100   1.000 13.82749 ? 132 ASP   A CG    1 
ATOM   1145 O  OD1   . ASP   A 1 133 ? -29.34100 21.31100  7.06900   1.000 15.86108 ? 132 ASP   A OD1   1 
ATOM   1146 O  OD2   . ASP   A 1 133 ? -30.11600 19.26400  6.96600   1.000 14.46107 ? 132 ASP   A OD2   1 
ATOM   1147 N  N     . LEU   A 1 134 ? -25.23400 19.51700  4.51300   1.000 9.45919  ? 133 LEU   A N     1 
ATOM   1148 C  CA    . LEU   A 1 134 ? -23.89600 18.98000  4.26800   1.000 9.38864  ? 133 LEU   A CA    1 
ATOM   1149 C  C     . LEU   A 1 134 ? -22.85000 20.09000  4.28400   1.000 10.00196 ? 133 LEU   A C     1 
ATOM   1150 O  O     . LEU   A 1 134 ? -21.81700 19.98000  4.95700   1.000 10.38822 ? 133 LEU   A O     1 
ATOM   1151 C  CB    . LEU   A 1 134 ? -23.86700 18.20700  2.94900   1.000 9.42623  ? 133 LEU   A CB    1 
ATOM   1152 C  CG    . LEU   A 1 134 ? -22.51800 17.59000  2.57900   1.000 9.67204  ? 133 LEU   A CG    1 
ATOM   1153 C  CD1   . LEU   A 1 134 ? -22.04600 16.63200  3.66700   1.000 11.35664 ? 133 LEU   A CD1   1 
ATOM   1154 C  CD2   . LEU   A 1 134 ? -22.60500 16.89300  1.23200   1.000 11.06258 ? 133 LEU   A CD2   1 
ATOM   1155 N  N     . ALA   A 1 135 ? -23.10500 21.17900  3.55000   1.000 9.77938  ? 134 ALA   A N     1 
ATOM   1156 C  CA    . ALA   A 1 135 ? -22.15800 22.29000  3.53000   1.000 9.89130  ? 134 ALA   A CA    1 
ATOM   1157 C  C     . ALA   A 1 135 ? -21.94800 22.86100  4.92600   1.000 9.18377  ? 134 ALA   A C     1 
ATOM   1158 O  O     . ALA   A 1 135 ? -20.81300 23.15500  5.31900   1.000 10.20493 ? 134 ALA   A O     1 
ATOM   1159 C  CB    . ALA   A 1 135 ? -22.63100 23.38000  2.56800   1.000 10.39253 ? 134 ALA   A CB    1 
ATOM   1160 N  N     A ARG   A 1 136 ? -23.02900 23.02200  5.69500   0.500 9.59682  ? 135 ARG   A N     1 
ATOM   1161 N  N     B ARG   A 1 136 ? -23.03400 23.02300  5.68900   0.500 9.98843  ? 135 ARG   A N     1 
ATOM   1162 C  CA    A ARG   A 1 136 ? -22.88500 23.52400  7.05800   0.500 10.68521 ? 135 ARG   A CA    1 
ATOM   1163 C  CA    B ARG   A 1 136 ? -22.90900 23.51200  7.05900   0.500 11.26968 ? 135 ARG   A CA    1 
ATOM   1164 C  C     A ARG   A 1 136 ? -22.03100 22.58400  7.90400   0.500 11.00590 ? 135 ARG   A C     1 
ATOM   1165 C  C     B ARG   A 1 136 ? -22.03100 22.58400  7.89100   0.500 11.34876 ? 135 ARG   A C     1 
ATOM   1166 O  O     A ARG   A 1 136 ? -21.19700 23.03500  8.69700   0.500 12.11399 ? 135 ARG   A O     1 
ATOM   1167 O  O     B ARG   A 1 136 ? -21.18200 23.04600  8.66200   0.500 12.28924 ? 135 ARG   A O     1 
ATOM   1168 C  CB    A ARG   A 1 136 ? -24.26100 23.75800  7.68700   0.500 11.46154 ? 135 ARG   A CB    1 
ATOM   1169 C  CB    B ARG   A 1 136 ? -24.29700 23.65900  7.68700   0.500 12.36255 ? 135 ARG   A CB    1 
ATOM   1170 C  CG    A ARG   A 1 136 ? -24.21700 24.10600  9.16900   0.500 12.00197 ? 135 ARG   A CG    1 
ATOM   1171 C  CG    B ARG   A 1 136 ? -24.29700 24.30500  9.06600   0.500 13.18287 ? 135 ARG   A CG    1 
ATOM   1172 C  CD    A ARG   A 1 136 ? -25.56000 24.62600  9.68200   0.500 13.20013 ? 135 ARG   A CD    1 
ATOM   1173 C  CD    B ARG   A 1 136 ? -25.70700 24.38100  9.66100   0.500 15.98611 ? 135 ARG   A CD    1 
ATOM   1174 N  NE    A ARG   A 1 136 ? -25.77900 26.01500  9.29600   0.500 13.93852 ? 135 ARG   A NE    1 
ATOM   1175 N  NE    B ARG   A 1 136 ? -26.65600 25.01600  8.75400   0.500 18.35316 ? 135 ARG   A NE    1 
ATOM   1176 C  CZ    A ARG   A 1 136 ? -26.59600 26.84900  9.92400   0.500 14.26379 ? 135 ARG   A CZ    1 
ATOM   1177 C  CZ    B ARG   A 1 136 ? -27.60900 24.37100  8.09400   0.500 20.42160 ? 135 ARG   A CZ    1 
ATOM   1178 N  NH1   A ARG   A 1 136 ? -27.31900 26.46100  10.96200  0.500 15.43642 ? 135 ARG   A NH1   1 
ATOM   1179 N  NH1   B ARG   A 1 136 ? -27.80800 23.07300  8.26100   0.500 21.23093 ? 135 ARG   A NH1   1 
ATOM   1180 N  NH2   A ARG   A 1 136 ? -26.67700 28.11100  9.51100   0.500 14.02189 ? 135 ARG   A NH2   1 
ATOM   1181 N  NH2   B ARG   A 1 136 ? -28.38500 25.04500  7.25000   0.500 21.57030 ? 135 ARG   A NH2   1 
ATOM   1182 N  N     . SER   A 1 137 ? -22.20300 21.26800  7.72500   1.000 10.91195 ? 136 SER   A N     1 
ATOM   1183 C  CA    . SER   A 1 137 ? -21.41300 20.30800  8.49400   1.000 11.98854 ? 136 SER   A CA    1 
ATOM   1184 C  C     . SER   A 1 137 ? -19.93400 20.37600  8.13600   1.000 13.04031 ? 136 SER   A C     1 
ATOM   1185 O  O     . SER   A 1 137 ? -19.07700 20.02300  8.95500   1.000 14.94594 ? 136 SER   A O     1 
ATOM   1186 C  CB    . SER   A 1 137 ? -21.95700 18.88700  8.30400   1.000 12.01742 ? 136 SER   A CB    1 
ATOM   1187 O  OG    . SER   A 1 137 ? -21.53600 18.30700  7.07800   1.000 12.79369 ? 136 SER   A OG    1 
ATOM   1188 N  N     . TYR   A 1 138 ? -19.61600 20.82100  6.92400   1.000 11.74118 ? 137 TYR   A N     1 
ATOM   1189 C  CA    . TYR   A 1 138 ? -18.23700 21.01600  6.50200   1.000 11.76735 ? 137 TYR   A CA    1 
ATOM   1190 C  C     . TYR   A 1 138 ? -17.71600 22.41900  6.79100   1.000 11.86676 ? 137 TYR   A C     1 
ATOM   1191 O  O     . TYR   A 1 138 ? -16.51300 22.65700  6.63500   1.000 13.88539 ? 137 TYR   A O     1 
ATOM   1192 C  CB    . TYR   A 1 138 ? -18.12200 20.80200  4.99100   1.000 12.38332 ? 137 TYR   A CB    1 
ATOM   1193 C  CG    . TYR   A 1 138 ? -18.30900 19.38300  4.47700   1.000 11.64041 ? 137 TYR   A CG    1 
ATOM   1194 C  CD1   . TYR   A 1 138 ? -18.19700 18.27000  5.31200   1.000 12.67803 ? 137 TYR   A CD1   1 
ATOM   1195 C  CD2   . TYR   A 1 138 ? -18.57000 19.16200  3.12800   1.000 12.42609 ? 137 TYR   A CD2   1 
ATOM   1196 C  CE1   . TYR   A 1 138 ? -18.34500 16.98000  4.80100   1.000 13.23182 ? 137 TYR   A CE1   1 
ATOM   1197 C  CE2   . TYR   A 1 138 ? -18.71900 17.89400  2.61800   1.000 12.63547 ? 137 TYR   A CE2   1 
ATOM   1198 C  CZ    . TYR   A 1 138 ? -18.61500 16.80500  3.45100   1.000 12.55904 ? 137 TYR   A CZ    1 
ATOM   1199 O  OH    . TYR   A 1 138 ? -18.76600 15.55000  2.90500   1.000 14.31153 ? 137 TYR   A OH    1 
ATOM   1200 N  N     . GLY   A 1 139 ? -18.58800 23.35200  7.16300   1.000 11.59839 ? 138 GLY   A N     1 
ATOM   1201 C  CA    . GLY   A 1 139 ? -18.19600 24.74000  7.33700   1.000 12.83530 ? 138 GLY   A CA    1 
ATOM   1202 C  C     . GLY   A 1 139 ? -17.85400 25.46600  6.05100   1.000 11.91822 ? 138 GLY   A C     1 
ATOM   1203 O  O     . GLY   A 1 139 ? -16.95700 26.31800  6.05500   1.000 13.55886 ? 138 GLY   A O     1 
ATOM   1204 N  N     . ILE   A 1 140 ? -18.55100 25.16500  4.95500   1.000 10.58266 ? 139 ILE   A N     1 
ATOM   1205 C  CA    . ILE   A 1 140 ? -18.20700 25.74100  3.65400   1.000 10.23364 ? 139 ILE   A CA    1 
ATOM   1206 C  C     . ILE   A 1 140 ? -19.45900 26.32200  3.01000   1.000 9.20752  ? 139 ILE   A C     1 
ATOM   1207 O  O     . ILE   A 1 140 ? -20.58800 25.92100  3.33000   1.000 10.38945 ? 139 ILE   A O     1 
ATOM   1208 C  CB    . ILE   A 1 140 ? -17.54200 24.70200  2.71500   1.000 9.94458  ? 139 ILE   A CB    1 
ATOM   1209 C  CG1   . ILE   A 1 140 ? -18.54100 23.62000  2.28200   1.000 10.36217 ? 139 ILE   A CG1   1 
ATOM   1210 C  CG2   . ILE   A 1 140 ? -16.30800 24.10300  3.36100   1.000 10.83178 ? 139 ILE   A CG2   1 
ATOM   1211 C  CD1   . ILE   A 1 140 ? -17.97200 22.58400  1.32000   1.000 10.01140 ? 139 ILE   A CD1   1 
ATOM   1212 N  N     . PRO   A 1 141 ? -19.28500 27.25000  2.06600   1.000 9.18628  ? 140 PRO   A N     1 
ATOM   1213 C  CA    . PRO   A 1 141 ? -20.44000 27.78500  1.33700   1.000 9.78393  ? 140 PRO   A CA    1 
ATOM   1214 C  C     . PRO   A 1 141 ? -21.09100 26.73000  0.45800   1.000 9.21416  ? 140 PRO   A C     1 
ATOM   1215 O  O     . PRO   A 1 141 ? -20.44700 25.78500  -0.01100  1.000 9.28770  ? 140 PRO   A O     1 
ATOM   1216 C  CB    . PRO   A 1 141 ? -19.83000 28.89600  0.47000   1.000 10.59341 ? 140 PRO   A CB    1 
ATOM   1217 C  CG    . PRO   A 1 141 ? -18.54500 29.26300  1.15300   1.000 11.53104 ? 140 PRO   A CG    1 
ATOM   1218 C  CD    . PRO   A 1 141 ? -18.04200 27.96900  1.73000   1.000 10.36580 ? 140 PRO   A CD    1 
ATOM   1219 N  N     . PHE   A 1 142 ? -22.38100 26.93300  0.20000   1.000 8.98179  ? 141 PHE   A N     1 
ATOM   1220 C  CA    . PHE   A 1 142 ? -23.14900 26.14500  -0.75700  1.000 9.17478  ? 141 PHE   A CA    1 
ATOM   1221 C  C     . PHE   A 1 142 ? -23.76800 27.09600  -1.77200  1.000 8.70381  ? 141 PHE   A C     1 
ATOM   1222 O  O     . PHE   A 1 142 ? -24.44900 28.05600  -1.39100  1.000 10.00307 ? 141 PHE   A O     1 
ATOM   1223 C  CB    . PHE   A 1 142 ? -24.26000 25.34900  -0.06100  1.000 10.01680 ? 141 PHE   A CB    1 
ATOM   1224 C  CG    . PHE   A 1 142 ? -25.23400 24.72100  -1.02400  1.000 9.41432  ? 141 PHE   A CG    1 
ATOM   1225 C  CD1   . PHE   A 1 142 ? -24.78500 23.86500  -2.02300  1.000 9.30854  ? 141 PHE   A CD1   1 
ATOM   1226 C  CD2   . PHE   A 1 142 ? -26.58700 25.01100  -0.96100  1.000 11.74041 ? 141 PHE   A CD2   1 
ATOM   1227 C  CE1   . PHE   A 1 142 ? -25.65900 23.29800  -2.92800  1.000 9.36827  ? 141 PHE   A CE1   1 
ATOM   1228 C  CE2   . PHE   A 1 142 ? -27.47000 24.44100  -1.86700  1.000 12.63135 ? 141 PHE   A CE2   1 
ATOM   1229 C  CZ    . PHE   A 1 142 ? -27.00200 23.58600  -2.85500  1.000 11.30198 ? 141 PHE   A CZ    1 
ATOM   1230 N  N     . ILE   A 1 143 ? -23.54300 26.82900  -3.05600  1.000 8.02496  ? 142 ILE   A N     1 
ATOM   1231 C  CA    . ILE   A 1 143 ? -24.04600 27.67000  -4.13400  1.000 9.17244  ? 142 ILE   A CA    1 
ATOM   1232 C  C     . ILE   A 1 143 ? -24.81100 26.80900  -5.13500  1.000 7.98275  ? 142 ILE   A C     1 
ATOM   1233 O  O     . ILE   A 1 143 ? -24.30200 25.78400  -5.60700  1.000 8.45371  ? 142 ILE   A O     1 
ATOM   1234 C  CB    . ILE   A 1 143 ? -22.91100 28.47600  -4.79700  1.000 10.05885 ? 142 ILE   A CB    1 
ATOM   1235 C  CG1   . ILE   A 1 143 ? -22.31300 29.43000  -3.74800  1.000 13.94381 ? 142 ILE   A CG1   1 
ATOM   1236 C  CG2   . ILE   A 1 143 ? -23.42500 29.25800  -6.00500  1.000 11.11406 ? 142 ILE   A CG2   1 
ATOM   1237 C  CD1   . ILE   A 1 143 ? -21.13500 30.23200  -4.19400  1.000 16.22626 ? 142 ILE   A CD1   1 
ATOM   1238 N  N     . GLU   A 1 144 ? -26.03600 27.22500  -5.44600  1.000 8.43463  ? 143 GLU   A N     1 
ATOM   1239 C  CA    . GLU   A 1 144 ? -26.85400 26.60000  -6.47800  1.000 8.73654  ? 143 GLU   A CA    1 
ATOM   1240 C  C     . GLU   A 1 144 ? -26.49200 27.18600  -7.83600  1.000 8.22143  ? 143 GLU   A C     1 
ATOM   1241 O  O     . GLU   A 1 144 ? -26.48200 28.41000  -8.00500  1.000 10.40380 ? 143 GLU   A O     1 
ATOM   1242 C  CB    . GLU   A 1 144 ? -28.33300 26.85400  -6.19400  1.000 10.16446 ? 143 GLU   A CB    1 
ATOM   1243 C  CG    . GLU   A 1 144 ? -28.76400 26.35000  -4.83400  1.000 11.72413 ? 143 GLU   A CG    1 
ATOM   1244 C  CD    . GLU   A 1 144 ? -30.23700 26.58900  -4.55900  1.000 15.32043 ? 143 GLU   A CD    1 
ATOM   1245 O  OE1   . GLU   A 1 144 ? -31.07900 26.13200  -5.36200  1.000 15.61948 ? 143 GLU   A OE1   1 
ATOM   1246 O  OE2   . GLU   A 1 144 ? -30.55900 27.23100  -3.53400  1.000 19.23794 ? 143 GLU   A OE2   1 
ATOM   1247 N  N     . THR   A 1 145 ? -26.19600 26.32100  -8.80600  1.000 7.75649  ? 144 THR   A N     1 
ATOM   1248 C  CA    . THR   A 1 145 ? -25.75900 26.78600  -10.11200 1.000 7.79407  ? 144 THR   A CA    1 
ATOM   1249 C  C     . THR   A 1 145 ? -26.55900 26.12700  -11.22500 1.000 7.71330  ? 144 THR   A C     1 
ATOM   1250 O  O     . THR   A 1 145 ? -27.13900 25.04800  -11.05800 1.000 7.62196  ? 144 THR   A O     1 
ATOM   1251 C  CB    . THR   A 1 145 ? -24.26300 26.51100  -10.37100 1.000 7.77428  ? 144 THR   A CB    1 
ATOM   1252 O  OG1   . THR   A 1 145 ? -24.02500 25.10100  -10.38100 1.000 7.66169  ? 144 THR   A OG1   1 
ATOM   1253 C  CG2   . THR   A 1 145 ? -23.38300 27.15800  -9.31600  1.000 8.76154  ? 144 THR   A CG2   1 
ATOM   1254 N  N     . SER   A 1 146 ? -26.52500 26.77700  -12.38600 1.000 8.44376  ? 145 SER   A N     1 
ATOM   1255 C  CA    . SER   A 1 146 ? -26.89900 26.15600  -13.65000 1.000 8.30077  ? 145 SER   A CA    1 
ATOM   1256 C  C     . SER   A 1 146 ? -25.89400 26.59400  -14.70100 1.000 8.38116  ? 145 SER   A C     1 
ATOM   1257 O  O     . SER   A 1 146 ? -25.81600 27.78200  -15.02200 1.000 8.60211  ? 145 SER   A O     1 
ATOM   1258 C  CB    . SER   A 1 146 ? -28.30500 26.56500  -14.08700 1.000 8.29906  ? 145 SER   A CB    1 
ATOM   1259 O  OG    . SER   A 1 146 ? -28.53300 26.13700  -15.41900 1.000 8.83712  ? 145 SER   A OG    1 
ATOM   1260 N  N     . ALA   A 1 147 ? -25.12900 25.64900  -15.24800 1.000 8.10527  ? 146 ALA   A N     1 
ATOM   1261 C  CA    . ALA   A 1 147 ? -24.28800 25.98900  -16.39200 1.000 9.04277  ? 146 ALA   A CA    1 
ATOM   1262 C  C     . ALA   A 1 147 ? -25.12800 26.36500  -17.60200 1.000 9.37659  ? 146 ALA   A C     1 
ATOM   1263 O  O     . ALA   A 1 147 ? -24.65000 27.08700  -18.48400 1.000 11.27630 ? 146 ALA   A O     1 
ATOM   1264 C  CB    . ALA   A 1 147 ? -23.34900 24.83200  -16.73500 1.000 10.02103 ? 146 ALA   A CB    1 
ATOM   1265 N  N     . LYS   A 1 148 ? -26.37800 25.90800  -17.64900 1.000 9.29346  ? 147 LYS   A N     1 
ATOM   1266 C  CA    . LYS   A 1 148 ? -27.22700 26.18700  -18.80100 1.000 11.03129 ? 147 LYS   A CA    1 
ATOM   1267 C  C     . LYS   A 1 148 ? -27.65700 27.65000  -18.83400 1.000 11.15010 ? 147 LYS   A C     1 
ATOM   1268 O  O     . LYS   A 1 148 ? -27.55500 28.31000  -19.87300 1.000 13.80452 ? 147 LYS   A O     1 
ATOM   1269 C  CB    . LYS   A 1 148 ? -28.43000 25.24200  -18.80800 1.000 12.38809 ? 147 LYS   A CB    1 
ATOM   1270 C  CG    . LYS   A 1 148 ? -29.35600 25.43700  -19.99400 1.000 14.98328 ? 147 LYS   A CG    1 
ATOM   1271 C  CD    . LYS   A 1 148 ? -30.44600 24.37900  -20.01300 1.000 16.91095 ? 147 LYS   A CD    1 
ATOM   1272 C  CE    . LYS   A 1 148 ? -31.41300 24.57900  -21.17600 1.000 20.46633 ? 147 LYS   A CE    1 
ATOM   1273 N  NZ    . LYS   A 1 148 ? -32.44100 23.49700  -21.21800 1.000 23.29143 ? 147 LYS   A NZ    1 
ATOM   1274 N  N     . THR   A 1 149 ? -28.14200 28.17400  -17.70700 1.000 10.43739 ? 148 THR   A N     1 
ATOM   1275 C  CA    . THR   A 1 149 ? -28.60900 29.55700  -17.63900 1.000 11.21476 ? 148 THR   A CA    1 
ATOM   1276 C  C     . THR   A 1 149 ? -27.55400 30.52300  -17.13000 1.000 11.51398 ? 148 THR   A C     1 
ATOM   1277 O  O     . THR   A 1 149 ? -27.78400 31.73800  -17.17000 1.000 13.55465 ? 148 THR   A O     1 
ATOM   1278 C  CB    . THR   A 1 149 ? -29.81000 29.67400  -16.70100 1.000 11.87369 ? 148 THR   A CB    1 
ATOM   1279 O  OG1   . THR   A 1 149 ? -29.37400 29.40400  -15.36600 1.000 11.36754 ? 148 THR   A OG1   1 
ATOM   1280 C  CG2   . THR   A 1 149 ? -30.91700 28.71600  -17.09700 1.000 12.72947 ? 148 THR   A CG2   1 
ATOM   1281 N  N     . ARG   A 1 150 ? -26.42700 30.01700  -16.63600 1.000 10.56412 ? 149 ARG   A N     1 
ATOM   1282 C  CA    . ARG   A 1 150 ? -25.32700 30.75000  -16.00200 1.000 11.27040 ? 149 ARG   A CA    1 
ATOM   1283 C  C     . ARG   A 1 150 ? -25.63600 31.15500  -14.55700 1.000 10.51239 ? 149 ARG   A C     1 
ATOM   1284 O  O     . ARG   A 1 150 ? -24.78500 31.79000  -13.91300 1.000 12.16102 ? 149 ARG   A O     1 
ATOM   1285 C  CB    . ARG   A 1 150 ? -24.77400 31.92700  -16.83000 1.000 13.36814 ? 149 ARG   A CB    1 
ATOM   1286 C  CG    . ARG   A 1 150 ? -23.25100 31.99200  -16.81200 1.000 15.88221 ? 149 ARG   A CG    1 
ATOM   1287 C  CD    . ARG   A 1 150 ? -22.67700 32.91700  -17.88800 1.000 18.40785 ? 149 ARG   A CD    1 
ATOM   1288 N  NE    . ARG   A 1 150 ? -21.21900 32.97300  -17.80600 1.000 19.67601 ? 149 ARG   A NE    1 
ATOM   1289 C  CZ    . ARG   A 1 150 ? -20.56300 33.65600  -16.87800 1.000 19.27577 ? 149 ARG   A CZ    1 
ATOM   1290 N  NH1   . ARG   A 1 150 ? -21.20200 34.39300  -15.98600 1.000 19.97393 ? 149 ARG   A NH1   1 
ATOM   1291 N  NH2   . ARG   A 1 150 ? -19.23500 33.58700  -16.83400 1.000 20.15216 ? 149 ARG   A NH2   1 
ATOM   1292 N  N     . GLN   A 1 151 ? -26.79500 30.77700  -14.01100 1.000 10.80576 ? 150 GLN   A N     1 
ATOM   1293 C  CA    . GLN   A 1 151 ? -27.10300 31.03300  -12.60500 1.000 11.34506 ? 150 GLN   A CA    1 
ATOM   1294 C  C     . GLN   A 1 151 ? -25.96200 30.56400  -11.71200 1.000 9.82751  ? 150 GLN   A C     1 
ATOM   1295 O  O     . GLN   A 1 151 ? -25.54800 29.40400  -11.77200 1.000 9.54822  ? 150 GLN   A O     1 
ATOM   1296 C  CB    . GLN   A 1 151 ? -28.38100 30.27800  -12.20800 1.000 13.64812 ? 150 GLN   A CB    1 
ATOM   1297 C  CG    . GLN   A 1 151 ? -28.65700 30.21900  -10.68800 1.000 15.22943 ? 150 GLN   A CG    1 
ATOM   1298 C  CD    . GLN   A 1 151 ? -29.75000 29.22100  -10.30500 1.000 18.01535 ? 150 GLN   A CD    1 
ATOM   1299 O  OE1   . GLN   A 1 151 ? -30.27200 28.49400  -11.15300 1.000 21.25719 ? 150 GLN   A OE1   1 
ATOM   1300 N  NE2   . GLN   A 1 151 ? -30.08100 29.16700  -9.01800  1.000 20.66322 ? 150 GLN   A NE2   1 
ATOM   1301 N  N     . GLY   A 1 152 ? -25.45700 31.47000  -10.87400 1.000 10.15729 ? 151 GLY   A N     1 
ATOM   1302 C  CA    . GLY   A 1 152 ? -24.50500 31.10400  -9.84500  1.000 9.46236  ? 151 GLY   A CA    1 
ATOM   1303 C  C     . GLY   A 1 152 ? -23.08700 30.80600  -10.29300 1.000 9.09002  ? 151 GLY   A C     1 
ATOM   1304 O  O     . GLY   A 1 152 ? -22.24500 30.53600  -9.43500  1.000 9.53781  ? 151 GLY   A O     1 
ATOM   1305 N  N     . VAL   A 1 153 ? -22.78400 30.84800  -11.59400 1.000 9.08174  ? 152 VAL   A N     1 
ATOM   1306 C  CA    . VAL   A 1 153 ? -21.47400 30.39300  -12.07100 1.000 10.03053 ? 152 VAL   A CA    1 
ATOM   1307 C  C     . VAL   A 1 153 ? -20.35700 31.29900  -11.55800 1.000 9.73655  ? 152 VAL   A C     1 
ATOM   1308 O  O     . VAL   A 1 153 ? -19.38700 30.83100  -10.94700 1.000 9.98307  ? 152 VAL   A O     1 
ATOM   1309 C  CB    . VAL   A 1 153 ? -21.45800 30.27000  -13.60500 1.000 10.56910 ? 152 VAL   A CB    1 
ATOM   1310 C  CG1   . VAL   A 1 153 ? -20.04400 29.96400  -14.09300 1.000 12.92617 ? 152 VAL   A CG1   1 
ATOM   1311 C  CG2   . VAL   A 1 153 ? -22.43900 29.19600  -14.05400 1.000 11.84467 ? 152 VAL   A CG2   1 
ATOM   1312 N  N     . ASP   A 1 154 ? -20.45400 32.60500  -11.82700 1.000 9.44606  ? 153 ASP   A N     1 
ATOM   1313 C  CA    . ASP   A 1 154 ? -19.43700 33.51600  -11.31600 1.000 10.93777 ? 153 ASP   A CA    1 
ATOM   1314 C  C     . ASP   A 1 154 ? -19.36600 33.45100  -9.79800  1.000 9.80244  ? 153 ASP   A C     1 
ATOM   1315 O  O     . ASP   A 1 154 ? -18.27600 33.45900  -9.21800  1.000 10.66339 ? 153 ASP   A O     1 
ATOM   1316 C  CB    . ASP   A 1 154 ? -19.72800 34.95000  -11.75500 1.000 13.27362 ? 153 ASP   A CB    1 
ATOM   1317 C  CG    . ASP   A 1 154 ? -19.51000 35.17600  -13.23500 1.000 16.82158 ? 153 ASP   A CG    1 
ATOM   1318 O  OD1   . ASP   A 1 154 ? -18.73800 34.43000  -13.86800 1.000 19.59026 ? 153 ASP   A OD1   1 
ATOM   1319 O  OD2   . ASP   A 1 154 ? -20.10800 36.13100  -13.76400 1.000 20.98411 ? 153 ASP   A OD2   1 
ATOM   1320 N  N     . ASP   A 1 155 ? -20.52200 33.38500  -9.13800  1.000 9.47272  ? 154 ASP   A N     1 
ATOM   1321 C  CA    . ASP   A 1 155 ? -20.54700 33.34100  -7.68000  1.000 9.52296  ? 154 ASP   A CA    1 
ATOM   1322 C  C     . ASP   A 1 155 ? -19.77500 32.13300  -7.14700  1.000 9.25933  ? 154 ASP   A C     1 
ATOM   1323 O  O     . ASP   A 1 155 ? -19.03400 32.24700  -6.16500  1.000 9.14397  ? 154 ASP   A O     1 
ATOM   1324 C  CB    . ASP   A 1 155 ? -22.00100 33.33600  -7.20700  1.000 10.99039 ? 154 ASP   A CB    1 
ATOM   1325 C  CG    . ASP   A 1 155 ? -22.15200 33.57500  -5.71700  1.000 11.82730 ? 154 ASP   A CG    1 
ATOM   1326 O  OD1   . ASP   A 1 155 ? -21.24900 34.15300  -5.08000  1.000 12.71615 ? 154 ASP   A OD1   1 
ATOM   1327 O  OD2   . ASP   A 1 155 ? -23.21100 33.18900  -5.18500  1.000 14.26854 ? 154 ASP   A OD2   1 
ATOM   1328 N  N     . ALA   A 1 156 ? -19.91700 30.96900  -7.78700  1.000 8.91774  ? 155 ALA   A N     1 
ATOM   1329 C  CA    . ALA   A 1 156 ? -19.22000 29.78000  -7.29300  1.000 8.69664  ? 155 ALA   A CA    1 
ATOM   1330 C  C     . ALA   A 1 156 ? -17.70400 29.96400  -7.34900  1.000 8.01862  ? 155 ALA   A C     1 
ATOM   1331 O  O     . ALA   A 1 156 ? -17.00000 29.71700  -6.36400  1.000 8.49901  ? 155 ALA   A O     1 
ATOM   1332 C  CB    . ALA   A 1 156 ? -19.64800 28.54700  -8.09100  1.000 9.20962  ? 155 ALA   A CB    1 
ATOM   1333 N  N     . PHE   A 1 157 ? -17.18200 30.40500  -8.49900  1.000 8.24872  ? 156 PHE   A N     1 
ATOM   1334 C  CA    . PHE   A 1 157 ? -15.73600 30.56600  -8.64300  1.000 8.12188  ? 156 PHE   A CA    1 
ATOM   1335 C  C     . PHE   A 1 157 ? -15.21000 31.73200  -7.81200  1.000 8.43640  ? 156 PHE   A C     1 
ATOM   1336 O  O     . PHE   A 1 157 ? -14.15000 31.61600  -7.18900  1.000 8.85461  ? 156 PHE   A O     1 
ATOM   1337 C  CB    . PHE   A 1 157 ? -15.36700 30.72100  -10.11800 1.000 8.53571  ? 156 PHE   A CB    1 
ATOM   1338 C  CG    . PHE   A 1 157 ? -15.46800 29.43700  -10.90900 1.000 8.85759  ? 156 PHE   A CG    1 
ATOM   1339 C  CD1   . PHE   A 1 157 ? -14.42500 28.51800  -10.89900 1.000 9.83350  ? 156 PHE   A CD1   1 
ATOM   1340 C  CD2   . PHE   A 1 157 ? -16.59700 29.14600  -11.66200 1.000 9.80326  ? 156 PHE   A CD2   1 
ATOM   1341 C  CE1   . PHE   A 1 157 ? -14.49900 27.34600  -11.63100 1.000 10.26160 ? 156 PHE   A CE1   1 
ATOM   1342 C  CE2   . PHE   A 1 157 ? -16.67700 27.97000  -12.39800 1.000 10.17099 ? 156 PHE   A CE2   1 
ATOM   1343 C  CZ    . PHE   A 1 157 ? -15.62500 27.06800  -12.37700 1.000 10.03699 ? 156 PHE   A CZ    1 
ATOM   1344 N  N     . TYR   A 1 158 ? -15.91700 32.86900  -7.80800  1.000 8.22839  ? 157 TYR   A N     1 
ATOM   1345 C  CA    . TYR   A 1 158 ? -15.43600 34.02600  -7.05100  1.000 8.71645  ? 157 TYR   A CA    1 
ATOM   1346 C  C     . TYR   A 1 158 ? -15.50400 33.76800  -5.55200  1.000 7.97231  ? 157 TYR   A C     1 
ATOM   1347 O  O     . TYR   A 1 158 ? -14.59400 34.15800  -4.80600  1.000 8.71331  ? 157 TYR   A O     1 
ATOM   1348 C  CB    . TYR   A 1 158 ? -16.22900 35.29000  -7.39800  1.000 10.20520 ? 157 TYR   A CB    1 
ATOM   1349 C  CG    . TYR   A 1 158 ? -16.06400 35.84600  -8.80200  1.000 11.07397 ? 157 TYR   A CG    1 
ATOM   1350 C  CD1   . TYR   A 1 158 ? -15.38300 35.15700  -9.80200  1.000 12.57933 ? 157 TYR   A CD1   1 
ATOM   1351 C  CD2   . TYR   A 1 158 ? -16.59000 37.09500  -9.11800  1.000 14.11802 ? 157 TYR   A CD2   1 
ATOM   1352 C  CE1   . TYR   A 1 158 ? -15.24500 35.70700  -11.09300 1.000 13.55402 ? 157 TYR   A CE1   1 
ATOM   1353 C  CE2   . TYR   A 1 158 ? -16.46800 37.63800  -10.38300 1.000 16.57238 ? 157 TYR   A CE2   1 
ATOM   1354 C  CZ    . TYR   A 1 158 ? -15.79700 36.94400  -11.36600 1.000 15.76830 ? 157 TYR   A CZ    1 
ATOM   1355 O  OH    . TYR   A 1 158 ? -15.67800 37.49800  -12.62300 1.000 18.47809 ? 157 TYR   A OH    1 
ATOM   1356 N  N     . THR   A 1 159 ? -16.57000 33.10300  -5.09000  1.000 8.48121  ? 158 THR   A N     1 
ATOM   1357 C  CA    . THR   A 1 159 ? -16.63200 32.73200  -3.67900  1.000 8.85346  ? 158 THR   A CA    1 
ATOM   1358 C  C     . THR   A 1 159 ? -15.44800 31.86100  -3.29600  1.000 8.40903  ? 158 THR   A C     1 
ATOM   1359 O  O     . THR   A 1 159 ? -14.84700 32.04400  -2.23000  1.000 8.98823  ? 158 THR   A O     1 
ATOM   1360 C  CB    . THR   A 1 159 ? -17.95900 32.03900  -3.35600  1.000 9.17299  ? 158 THR   A CB    1 
ATOM   1361 O  OG1   . THR   A 1 159 ? -19.03500 32.97100  -3.51100  1.000 9.64843  ? 158 THR   A OG1   1 
ATOM   1362 C  CG2   . THR   A 1 159 ? -17.96800 31.50200  -1.93400  1.000 9.93086  ? 158 THR   A CG2   1 
ATOM   1363 N  N     . LEU   A 1 160 ? -15.09300 30.90500  -4.15500  1.000 8.21368  ? 159 LEU   A N     1 
ATOM   1364 C  CA    . LEU   A 1 160 ? -13.94900 30.05200  -3.85500  1.000 8.08717  ? 159 LEU   A CA    1 
ATOM   1365 C  C     . LEU   A 1 160 ? -12.66600 30.87400  -3.72300  1.000 8.62079  ? 159 LEU   A C     1 
ATOM   1366 O  O     . LEU   A 1 160 ? -11.86600 30.63900  -2.80900  1.000 9.19392  ? 159 LEU   A O     1 
ATOM   1367 C  CB    . LEU   A 1 160 ? -13.81700 28.95400  -4.90800  1.000 8.57451  ? 159 LEU   A CB    1 
ATOM   1368 C  CG    . LEU   A 1 160 ? -12.65000 27.99100  -4.67900  1.000 8.39725  ? 159 LEU   A CG    1 
ATOM   1369 C  CD1   . LEU   A 1 160 ? -12.73500 27.28900  -3.32000  1.000 9.09902  ? 159 LEU   A CD1   1 
ATOM   1370 C  CD2   . LEU   A 1 160 ? -12.59500 26.96700  -5.80500  1.000 9.20398  ? 159 LEU   A CD2   1 
ATOM   1371 N  N     . VAL   A 1 161 ? -12.46600 31.86600  -4.59900  1.000 8.57688  ? 160 VAL   A N     1 
ATOM   1372 C  CA    . VAL   A 1 161 ? -11.30900 32.75100  -4.45300  1.000 8.62259  ? 160 VAL   A CA    1 
ATOM   1373 C  C     . VAL   A 1 161 ? -11.32900 33.45700  -3.09900  1.000 9.31804  ? 160 VAL   A C     1 
ATOM   1374 O  O     . VAL   A 1 161 ? -10.30300 33.53200  -2.41100  1.000 10.44936 ? 160 VAL   A O     1 
ATOM   1375 C  CB    . VAL   A 1 161 ? -11.20700 33.74600  -5.62600  1.000 9.27029  ? 160 VAL   A CB    1 
ATOM   1376 C  CG1   . VAL   A 1 161 ? -10.14400 34.81300  -5.32100  1.000 12.02455 ? 160 VAL   A CG1   1 
ATOM   1377 C  CG2   . VAL   A 1 161 ? -10.88300 33.00000  -6.92700  1.000 10.61849 ? 160 VAL   A CG2   1 
ATOM   1378 N  N     . ARG   A 1 162 ? -12.49200 33.97000  -2.68400  1.000 9.45445  ? 161 ARG   A N     1 
ATOM   1379 C  CA    . ARG   A 1 162 ? -12.55700 34.63700  -1.38600  1.000 10.10682 ? 161 ARG   A CA    1 
ATOM   1380 C  C     . ARG   A 1 162 ? -12.24800 33.66800  -0.24800  1.000 9.46509  ? 161 ARG   A C     1 
ATOM   1381 O  O     . ARG   A 1 162 ? -11.61000 34.04500  0.74300   1.000 11.01546 ? 161 ARG   A O     1 
ATOM   1382 C  CB    . ARG   A 1 162 ? -13.91500 35.31500  -1.18400  1.000 9.95308  ? 161 ARG   A CB    1 
ATOM   1383 C  CG    . ARG   A 1 162 ? -14.23200 36.38600  -2.20700  1.000 9.83883  ? 161 ARG   A CG    1 
ATOM   1384 C  CD    . ARG   A 1 162 ? -15.41100 37.24600  -1.75800  1.000 10.59073 ? 161 ARG   A CD    1 
ATOM   1385 N  NE    . ARG   A 1 162 ? -15.84700 38.13800  -2.82800  1.000 10.80600 ? 161 ARG   A NE    1 
ATOM   1386 C  CZ    . ARG   A 1 162 ? -16.68800 37.79500  -3.79600  1.000 10.41795 ? 161 ARG   A CZ    1 
ATOM   1387 N  NH1   . ARG   A 1 162 ? -17.29700 36.61600  -3.80400  1.000 11.75270 ? 161 ARG   A NH1   1 
ATOM   1388 N  NH2   . ARG   A 1 162 ? -16.91900 38.65200  -4.78400  1.000 11.40074 ? 161 ARG   A NH2   1 
ATOM   1389 N  N     . GLU   A 1 163 ? -12.68900 32.41000  -0.37000  1.000 10.18040 ? 162 GLU   A N     1 
ATOM   1390 C  CA    . GLU   A 1 163 ? -12.33700 31.41000  0.63600   1.000 10.25245 ? 162 GLU   A CA    1 
ATOM   1391 C  C     . GLU   A 1 163 ? -10.82900 31.20800  0.70700   1.000 10.81465 ? 162 GLU   A C     1 
ATOM   1392 O  O     . GLU   A 1 163 ? -10.26400 31.06000  1.79800   1.000 12.12868 ? 162 GLU   A O     1 
ATOM   1393 C  CB    . GLU   A 1 163 ? -13.04300 30.08200  0.35200   1.000 10.51934 ? 162 GLU   A CB    1 
ATOM   1394 C  CG    . GLU   A 1 163 ? -14.54600 30.13100  0.46800   1.000 11.35227 ? 162 GLU   A CG    1 
ATOM   1395 C  CD    . GLU   A 1 163 ? -15.00800 30.48700  1.86400   1.000 12.87067 ? 162 GLU   A CD    1 
ATOM   1396 O  OE1   . GLU   A 1 163 ? -14.83100 29.66600  2.79100   1.000 13.88473 ? 162 GLU   A OE1   1 
ATOM   1397 O  OE2   . GLU   A 1 163 ? -15.54500 31.59900  2.03600   1.000 15.60145 ? 162 GLU   A OE2   1 
ATOM   1398 N  N     . ILE   A 1 164 ? -10.16000 31.16800  -0.44900  1.000 11.04781 ? 163 ILE   A N     1 
ATOM   1399 C  CA    . ILE   A 1 164 ? -8.70300  31.05300  -0.44400  1.000 12.16320 ? 163 ILE   A CA    1 
ATOM   1400 C  C     . ILE   A 1 164 ? -8.08100  32.25100  0.25600   1.000 14.21255 ? 163 ILE   A C     1 
ATOM   1401 O  O     . ILE   A 1 164 ? -7.17400  32.10500  1.08500   1.000 16.48580 ? 163 ILE   A O     1 
ATOM   1402 C  CB    . ILE   A 1 164 ? -8.17200  30.87800  -1.87900  1.000 11.35862 ? 163 ILE   A CB    1 
ATOM   1403 C  CG1   . ILE   A 1 164 ? -8.65300  29.54800  -2.46600  1.000 11.23540 ? 163 ILE   A CG1   1 
ATOM   1404 C  CG2   . ILE   A 1 164 ? -6.64400  30.97000  -1.90200  1.000 12.80318 ? 163 ILE   A CG2   1 
ATOM   1405 C  CD1   . ILE   A 1 164 ? -8.41700  29.44000  -3.95300  1.000 11.60381 ? 163 ILE   A CD1   1 
ATOM   1406 N  N     . ARG   A 1 165 ? -8.56400  33.45100  -0.05500  1.000 13.71001 ? 164 ARG   A N     1 
ATOM   1407 C  CA    . ARG   A 1 165 ? -7.98300  34.64700  0.54400   1.000 15.00062 ? 164 ARG   A CA    1 
ATOM   1408 C  C     . ARG   A 1 165 ? -8.17800  34.68500  2.05400   1.000 17.32910 ? 164 ARG   A C     1 
ATOM   1409 O  O     . ARG   A 1 165 ? -7.32400  35.21100  2.77500   1.000 20.78352 ? 164 ARG   A O     1 
ATOM   1410 C  CB    . ARG   A 1 165 ? -8.56400  35.89600  -0.11000  1.000 15.01219 ? 164 ARG   A CB    1 
ATOM   1411 C  CG    . ARG   A 1 165 ? -8.28000  35.98000  -1.59000  1.000 15.86521 ? 164 ARG   A CG    1 
ATOM   1412 C  CD    . ARG   A 1 165 ? -8.53100  37.36100  -2.09600  1.000 18.06244 ? 164 ARG   A CD    1 
ATOM   1413 N  NE    . ARG   A 1 165 ? -7.65700  38.27900  -1.37700  1.000 21.47558 ? 164 ARG   A NE    1 
ATOM   1414 C  CZ    . ARG   A 1 165 ? -7.12300  39.37400  -1.89300  1.000 23.84624 ? 164 ARG   A CZ    1 
ATOM   1415 N  NH1   . ARG   A 1 165 ? -7.41600  39.77500  -3.11700  1.000 27.10424 ? 164 ARG   A NH1   1 
ATOM   1416 N  NH2   . ARG   A 1 165 ? -6.26400  40.07900  -1.16300  1.000 25.65130 ? 164 ARG   A NH2   1 
ATOM   1417 N  N     . LYS   A 1 166 ? -9.28200  34.13600  2.55500   1.000 17.77156 ? 165 LYS   A N     1 
ATOM   1418 C  CA    . LYS   A 1 166 ? -9.48300  34.07200  3.99600   1.000 20.31441 ? 165 LYS   A CA    1 
ATOM   1419 C  C     . LYS   A 1 166 ? -8.62400  33.00800  4.66200   1.000 24.73723 ? 165 LYS   A C     1 
ATOM   1420 O  O     . LYS   A 1 166 ? -8.34100  33.11500  5.86000   1.000 27.17905 ? 165 LYS   A O     1 
ATOM   1421 C  CB    . LYS   A 1 166 ? -10.95600 33.83000  4.30700   1.000 19.53242 ? 165 LYS   A CB    1 
ATOM   1422 C  CG    . LYS   A 1 166 ? -11.82500 35.01600  3.93600   1.000 20.10040 ? 165 LYS   A CG    1 
ATOM   1423 C  CD    . LYS   A 1 166 ? -13.24900 34.82400  4.37900   1.000 21.23597 ? 165 LYS   A CD    1 
ATOM   1424 C  CE    . LYS   A 1 166 ? -13.91600 33.75800  3.56100   1.000 20.67659 ? 165 LYS   A CE    1 
ATOM   1425 N  NZ    . LYS   A 1 166 ? -15.36100 33.63100  3.88800   1.000 21.06826 ? 165 LYS   A NZ    1 
ATOM   1426 N  N     . HIS   A 1 167 ? -8.19200  31.99500  3.91200   1.000 26.77813 ? 166 HIS   A N     1 
ATOM   1427 C  CA    . HIS   A 1 167 ? -7.37600  30.93400  4.49200   1.000 33.37042 ? 166 HIS   A CA    1 
ATOM   1428 C  C     . HIS   A 1 167 ? -5.94700  31.40300  4.72400   1.000 38.85008 ? 166 HIS   A C     1 
ATOM   1429 O  O     . HIS   A 1 167 ? -5.33600  31.06700  5.74500   1.000 40.72398 ? 166 HIS   A O     1 
ATOM   1430 C  CB    . HIS   A 1 167 ? -7.39800  29.71400  3.57200   1.000 36.33800 ? 166 HIS   A CB    1 
ATOM   1431 C  CG    . HIS   A 1 167 ? -6.45600  28.62500  3.98100   1.000 39.60538 ? 166 HIS   A CG    1 
ATOM   1432 N  ND1   . HIS   A 1 167 ? -6.74300  27.73400  4.99200   1.000 40.51804 ? 166 HIS   A ND1   1 
ATOM   1433 C  CD2   . HIS   A 1 167 ? -5.23400  28.28000  3.51000   1.000 41.76586 ? 166 HIS   A CD2   1 
ATOM   1434 C  CE1   . HIS   A 1 167 ? -5.73800  26.88700  5.12700   1.000 41.29844 ? 166 HIS   A CE1   1 
ATOM   1435 N  NE2   . HIS   A 1 167 ? -4.81000  27.19700  4.24000   1.000 42.19181 ? 166 HIS   A NE2   1 
ATOM   1436 N  N     . LYS   A 1 168 ? -5.39900  32.17300  3.78800   1.000 42.59463 ? 167 LYS   A N     1 
ATOM   1437 C  CA    . LYS   A 1 168 ? -4.02400  32.65100  3.87400   1.000 46.20756 ? 167 LYS   A CA    1 
ATOM   1438 C  C     . LYS   A 1 168 ? -3.82300  33.52300  5.10900   1.000 48.42815 ? 167 LYS   A C     1 
ATOM   1439 O  O     . LYS   A 1 168 ? -2.69600  33.88100  5.44800   1.000 49.96204 ? 167 LYS   A O     1 
ATOM   1440 C  CB    . LYS   A 1 168 ? -3.66000  33.44900  2.62100   1.000 47.28186 ? 167 LYS   A CB    1 
ATOM   1441 C  CG    . LYS   A 1 168 ? -3.90000  32.72500  1.30700   1.000 47.79011 ? 167 LYS   A CG    1 
ATOM   1442 C  CD    . LYS   A 1 168 ? -3.69400  33.67700  0.13700   1.000 47.88016 ? 167 LYS   A CD    1 
ATOM   1443 C  CE    . LYS   A 1 168 ? -3.60100  32.93900  -1.18800  1.000 47.35852 ? 167 LYS   A CE    1 
ATOM   1444 N  NZ    . LYS   A 1 168 ? -3.29700  33.87200  -2.31100  1.000 46.33094 ? 167 LYS   A NZ    1 
ATOM   1445 N  N     . SER   B 2 1   ? -10.87100 -27.96900 -34.42700 1.000 13.80007 ? 0   SER   D N     1 
ATOM   1446 C  CA    . SER   B 2 1   ? -9.79300  -27.18100 -33.82400 1.000 14.48492 ? 0   SER   D CA    1 
ATOM   1447 C  C     . SER   B 2 1   ? -9.66100  -25.80600 -34.48600 1.000 16.31572 ? 0   SER   D C     1 
ATOM   1448 O  O     . SER   B 2 1   ? -9.86200  -25.68200 -35.69900 1.000 18.51121 ? 0   SER   D O     1 
ATOM   1449 C  CB    . SER   B 2 1   ? -8.46900  -27.92900 -33.96400 1.000 15.35413 ? 0   SER   D CB    1 
ATOM   1450 O  OG    . SER   B 2 1   ? -8.18900  -28.18000 -35.33400 1.000 14.50137 ? 0   SER   D OG    1 
ATOM   1451 N  N     . MET   B 2 2   ? -9.31000  -24.78400 -33.69800 1.000 15.98903 ? 1   MET   D N     1 
ATOM   1452 C  CA    . MET   B 2 2   ? -9.08900  -23.43500 -34.22800 1.000 16.43419 ? 1   MET   D CA    1 
ATOM   1453 C  C     . MET   B 2 2   ? -7.98400  -22.74100 -33.43600 1.000 15.61450 ? 1   MET   D C     1 
ATOM   1454 O  O     . MET   B 2 2   ? -8.10500  -22.56000 -32.22100 1.000 17.94028 ? 1   MET   D O     1 
ATOM   1455 C  CB    . MET   B 2 2   ? -10.37600 -22.59100 -34.18000 1.000 17.91291 ? 1   MET   D CB    1 
ATOM   1456 C  CG    . MET   B 2 2   ? -11.53700 -23.08100 -35.06100 1.000 17.94372 ? 1   MET   D CG    1 
ATOM   1457 S  SD    . MET   B 2 2   ? -11.30700 -22.90600 -36.84800 1.000 17.79697 ? 1   MET   D SD    1 
ATOM   1458 C  CE    . MET   B 2 2   ? -11.69200 -21.17400 -37.07300 1.000 20.05725 ? 1   MET   D CE    1 
ATOM   1459 N  N     . VAL   B 2 3   ? -6.92400  -22.31900 -34.12900 1.000 15.65870 ? 2   VAL   D N     1 
ATOM   1460 C  CA    . VAL   B 2 3   ? -5.86900  -21.51600 -33.51500 1.000 14.84720 ? 2   VAL   D CA    1 
ATOM   1461 C  C     . VAL   B 2 3   ? -6.41100  -20.11900 -33.21600 1.000 12.74079 ? 2   VAL   D C     1 
ATOM   1462 O  O     . VAL   B 2 3   ? -7.32200  -19.63000 -33.89300 1.000 13.39753 ? 2   VAL   D O     1 
ATOM   1463 C  CB    . VAL   B 2 3   ? -4.67900  -21.47100 -34.49700 1.000 16.79110 ? 2   VAL   D CB    1 
ATOM   1464 C  CG1   . VAL   B 2 3   ? -3.59700  -20.50000 -34.05100 1.000 19.90872 ? 2   VAL   D CG1   1 
ATOM   1465 C  CG2   . VAL   B 2 3   ? -4.09200  -22.87000 -34.68200 1.000 18.50706 ? 2   VAL   D CG2   1 
ATOM   1466 N  N     . ASN   B 2 4   ? -5.86700  -19.47700 -32.18000 1.000 11.18421 ? 3   ASN   D N     1 
ATOM   1467 C  CA    . ASN   B 2 4   ? -6.24000  -18.10000 -31.87800 1.000 10.63539 ? 3   ASN   D CA    1 
ATOM   1468 C  C     . ASN   B 2 4   ? -6.08100  -17.22900 -33.12700 1.000 10.51035 ? 3   ASN   D C     1 
ATOM   1469 O  O     . ASN   B 2 4   ? -5.05000  -17.31300 -33.80700 1.000 12.03374 ? 3   ASN   D O     1 
ATOM   1470 C  CB    . ASN   B 2 4   ? -5.34500  -17.54600 -30.76700 1.000 10.99234 ? 3   ASN   D CB    1 
ATOM   1471 C  CG    . ASN   B 2 4   ? -5.74900  -18.01900 -29.38000 1.000 11.14669 ? 3   ASN   D CG    1 
ATOM   1472 O  OD1   . ASN   B 2 4   ? -6.84400  -18.54400 -29.17500 1.000 12.11212 ? 3   ASN   D OD1   1 
ATOM   1473 N  ND2   . ASN   B 2 4   ? -4.86400  -17.80900 -28.41200 1.000 12.28036 ? 3   ASN   D ND2   1 
ATOM   1474 N  N     . PRO   B 2 5   ? -7.06100  -16.39000 -33.45700 1.000 10.85429 ? 4   PRO   D N     1 
ATOM   1475 C  CA    . PRO   B 2 5   ? -6.95800  -15.57800 -34.67600 1.000 11.68865 ? 4   PRO   D CA    1 
ATOM   1476 C  C     . PRO   B 2 5   ? -5.92600  -14.46700 -34.55800 1.000 10.94815 ? 4   PRO   D C     1 
ATOM   1477 O  O     . PRO   B 2 5   ? -5.55800  -14.01800 -33.46800 1.000 11.27838 ? 4   PRO   D O     1 
ATOM   1478 C  CB    . PRO   B 2 5   ? -8.36800  -15.00000 -34.85600 1.000 14.85518 ? 4   PRO   D CB    1 
ATOM   1479 C  CG    . PRO   B 2 5   ? -9.05700  -15.20000 -33.58200 1.000 14.66608 ? 4   PRO   D CG    1 
ATOM   1480 C  CD    . PRO   B 2 5   ? -8.36200  -16.25000 -32.78400 1.000 11.22757 ? 4   PRO   D CD    1 
ATOM   1481 N  N     . THR   B 2 6   ? -5.45900  -14.03100 -35.72700 1.000 11.24683 ? 5   THR   D N     1 
ATOM   1482 C  CA    . THR   B 2 6   ? -4.54000  -12.91000 -35.86100 1.000 11.77776 ? 5   THR   D CA    1 
ATOM   1483 C  C     . THR   B 2 6   ? -5.21800  -11.83400 -36.69600 1.000 11.29156 ? 5   THR   D C     1 
ATOM   1484 O  O     . THR   B 2 6   ? -5.72900  -12.12200 -37.78200 1.000 13.10601 ? 5   THR   D O     1 
ATOM   1485 C  CB    . THR   B 2 6   ? -3.26400  -13.35200 -36.59000 1.000 14.84915 ? 5   THR   D CB    1 
ATOM   1486 O  OG1   . THR   B 2 6   ? -2.66900  -14.46700 -35.91700 1.000 16.85073 ? 5   THR   D OG1   1 
ATOM   1487 C  CG2   . THR   B 2 6   ? -2.26400  -12.21000 -36.65500 1.000 15.81537 ? 5   THR   D CG2   1 
ATOM   1488 N  N     . VAL   B 2 7   ? -5.22800  -10.60100 -36.19800 1.000 11.09134 ? 6   VAL   D N     1 
ATOM   1489 C  CA    . VAL   B 2 7   ? -5.77400  -9.49500  -36.97300 1.000 11.64660 ? 6   VAL   D CA    1 
ATOM   1490 C  C     . VAL   B 2 7   ? -4.72200  -8.40000  -37.09500 1.000 11.36811 ? 6   VAL   D C     1 
ATOM   1491 O  O     . VAL   B 2 7   ? -3.74200  -8.36300  -36.35200 1.000 12.04352 ? 6   VAL   D O     1 
ATOM   1492 C  CB    . VAL   B 2 7   ? -7.10400  -8.95600  -36.41400 1.000 14.71134 ? 6   VAL   D CB    1 
ATOM   1493 C  CG1   . VAL   B 2 7   ? -8.17400  -10.04700 -36.44800 1.000 16.46264 ? 6   VAL   D CG1   1 
ATOM   1494 C  CG2   . VAL   B 2 7   ? -6.91400  -8.44000  -35.02400 1.000 14.98333 ? 6   VAL   D CG2   1 
ATOM   1495 N  N     . PHE   B 2 8   ? -4.91700  -7.51600  -38.07100 1.000 12.45020 ? 7   PHE   D N     1 
ATOM   1496 C  CA    . PHE   B 2 8   ? -3.98300  -6.42100  -38.29800 1.000 13.01893 ? 7   PHE   D CA    1 
ATOM   1497 C  C     . PHE   B 2 8   ? -4.71900  -5.09700  -38.41300 1.000 11.69543 ? 7   PHE   D C     1 
ATOM   1498 O  O     . PHE   B 2 8   ? -5.86700  -5.04300  -38.86400 1.000 11.27715 ? 7   PHE   D O     1 
ATOM   1499 C  CB    . PHE   B 2 8   ? -3.14600  -6.62200  -39.58000 1.000 14.47122 ? 7   PHE   D CB    1 
ATOM   1500 C  CG    . PHE   B 2 8   ? -3.91600  -6.40200  -40.85900 1.000 14.31810 ? 7   PHE   D CG    1 
ATOM   1501 C  CD1   . PHE   B 2 8   ? -4.59100  -7.44700  -41.47200 1.000 15.77241 ? 7   PHE   D CD1   1 
ATOM   1502 C  CD2   . PHE   B 2 8   ? -3.96500  -5.14400  -41.45000 1.000 15.87934 ? 7   PHE   D CD2   1 
ATOM   1503 C  CE1   . PHE   B 2 8   ? -5.29700  -7.24500  -42.64700 1.000 16.85385 ? 7   PHE   D CE1   1 
ATOM   1504 C  CE2   . PHE   B 2 8   ? -4.67300  -4.93400  -42.62000 1.000 17.22570 ? 7   PHE   D CE2   1 
ATOM   1505 C  CZ    . PHE   B 2 8   ? -5.33800  -5.98700  -43.22200 1.000 18.08259 ? 7   PHE   D CZ    1 
ATOM   1506 N  N     . PHE   B 2 9   ? -4.02100  -4.03000  -38.02000 1.000 11.78752 ? 8   PHE   D N     1 
ATOM   1507 C  CA    . PHE   B 2 9   ? -4.39000  -2.65400  -38.32900 1.000 11.81497 ? 8   PHE   D CA    1 
ATOM   1508 C  C     . PHE   B 2 9   ? -3.24700  -2.04000  -39.12600 1.000 11.96817 ? 8   PHE   D C     1 
ATOM   1509 O  O     . PHE   B 2 9   ? -2.08300  -2.14800  -38.72400 1.000 13.18662 ? 8   PHE   D O     1 
ATOM   1510 C  CB    . PHE   B 2 9   ? -4.48300  -1.78900  -37.06400 1.000 11.04746 ? 8   PHE   D CB    1 
ATOM   1511 C  CG    . PHE   B 2 9   ? -5.62900  -2.10600  -36.12300 1.000 10.52443 ? 8   PHE   D CG    1 
ATOM   1512 C  CD1   . PHE   B 2 9   ? -6.67600  -2.95600  -36.46100 1.000 11.10961 ? 8   PHE   D CD1   1 
ATOM   1513 C  CD2   . PHE   B 2 9   ? -5.64300  -1.50400  -34.87100 1.000 10.24637 ? 8   PHE   D CD2   1 
ATOM   1514 C  CE1   . PHE   B 2 9   ? -7.71600  -3.19200  -35.54900 1.000 10.13145 ? 8   PHE   D CE1   1 
ATOM   1515 C  CE2   . PHE   B 2 9   ? -6.66400  -1.73600  -33.96800 1.000 9.96211  ? 8   PHE   D CE2   1 
ATOM   1516 C  CZ    . PHE   B 2 9   ? -7.70000  -2.58100  -34.30100 1.000 10.20560 ? 8   PHE   D CZ    1 
ATOM   1517 N  N     . ASP   B 2 10  ? -3.56900  -1.37100  -40.22800 1.000 12.10709 ? 9   ASP   D N     1 
ATOM   1518 C  CA    . ASP   B 2 10  ? -2.62600  -0.49000  -40.90800 1.000 13.79483 ? 9   ASP   D CA    1 
ATOM   1519 C  C     . ASP   B 2 10  ? -2.89700  0.93200   -40.42300 1.000 12.68879 ? 9   ASP   D C     1 
ATOM   1520 O  O     . ASP   B 2 10  ? -3.98600  1.47000   -40.65200 1.000 13.50877 ? 9   ASP   D O     1 
ATOM   1521 C  CB    . ASP   B 2 10  ? -2.79400  -0.59300  -42.42200 1.000 16.02904 ? 9   ASP   D CB    1 
ATOM   1522 C  CG    . ASP   B 2 10  ? -2.21500  -1.87900  -42.98000 1.000 18.24160 ? 9   ASP   D CG    1 
ATOM   1523 O  OD1   . ASP   B 2 10  ? -1.20000  -2.35500  -42.43200 1.000 18.30715 ? 9   ASP   D OD1   1 
ATOM   1524 O  OD2   . ASP   B 2 10  ? -2.77000  -2.41800  -43.96100 1.000 21.24969 ? 9   ASP   D OD2   1 
ATOM   1525 N  N     . ILE   B 2 11  ? -1.91700  1.52400   -39.73300 1.000 13.65627 ? 10  ILE   D N     1 
ATOM   1526 C  CA    . ILE   B 2 11  ? -2.08000  2.81000   -39.05500 1.000 12.98788 ? 10  ILE   D CA    1 
ATOM   1527 C  C     . ILE   B 2 11  ? -1.59600  3.92800   -39.96700 1.000 12.80636 ? 10  ILE   D C     1 
ATOM   1528 O  O     . ILE   B 2 11  ? -0.56400  3.79600   -40.63300 1.000 13.94587 ? 10  ILE   D O     1 
ATOM   1529 C  CB    . ILE   B 2 11  ? -1.29200  2.82700   -37.72800 1.000 14.02554 ? 10  ILE   D CB    1 
ATOM   1530 C  CG1   . ILE   B 2 11  ? -1.72700  1.68600   -36.81000 1.000 14.36033 ? 10  ILE   D CG1   1 
ATOM   1531 C  CG2   . ILE   B 2 11  ? -1.41700  4.18200   -37.01900 1.000 13.70546 ? 10  ILE   D CG2   1 
ATOM   1532 C  CD1   . ILE   B 2 11  ? -3.14700  1.78700   -36.32500 1.000 14.89840 ? 10  ILE   D CD1   1 
ATOM   1533 N  N     . ALA   B 2 12  ? -2.32500  5.04300   -39.97300 1.000 12.27666 ? 11  ALA   D N     1 
ATOM   1534 C  CA    . ALA   B 2 12  ? -1.93800  6.24600   -40.69300 1.000 12.64459 ? 11  ALA   D CA    1 
ATOM   1535 C  C     . ALA   B 2 12  ? -1.93700  7.43800   -39.74100 1.000 11.73194 ? 11  ALA   D C     1 
ATOM   1536 O  O     . ALA   B 2 12  ? -2.66400  7.46100   -38.74000 1.000 11.06379 ? 11  ALA   D O     1 
ATOM   1537 C  CB    . ALA   B 2 12  ? -2.87300  6.51600   -41.88100 1.000 14.67230 ? 11  ALA   D CB    1 
ATOM   1538 N  N     . VAL   B 2 13  ? -1.10800  8.42600   -40.07000 1.000 11.92453 ? 12  VAL   D N     1 
ATOM   1539 C  CA    . VAL   B 2 13  ? -0.92000  9.63400   -39.27400 1.000 12.19236 ? 12  VAL   D CA    1 
ATOM   1540 C  C     . VAL   B 2 13  ? -1.21700  10.80600  -40.20000 1.000 12.07676 ? 12  VAL   D C     1 
ATOM   1541 O  O     . VAL   B 2 13  ? -0.47400  11.04200  -41.16100 1.000 13.25448 ? 12  VAL   D O     1 
ATOM   1542 C  CB    . VAL   B 2 13  ? 0.51000   9.73000   -38.72300 1.000 13.46126 ? 12  VAL   D CB    1 
ATOM   1543 C  CG1   . VAL   B 2 13  ? 0.69800   11.04300  -37.97200 1.000 14.97718 ? 12  VAL   D CG1   1 
ATOM   1544 C  CG2   . VAL   B 2 13  ? 0.84200   8.53700   -37.83600 1.000 15.50507 ? 12  VAL   D CG2   1 
ATOM   1545 N  N     . ASP   B 2 14  ? -2.30000  11.53900  -39.92600 1.000 12.35360 ? 13  ASP   D N     1 
ATOM   1546 C  CA    . ASP   B 2 14  ? -2.76100  12.59600  -40.83000 1.000 13.12614 ? 13  ASP   D CA    1 
ATOM   1547 C  C     . ASP   B 2 14  ? -2.81400  12.10100  -42.27800 1.000 14.34442 ? 13  ASP   D C     1 
ATOM   1548 O  O     . ASP   B 2 14  ? -2.43600  12.80700  -43.21600 1.000 16.62869 ? 13  ASP   D O     1 
ATOM   1549 C  CB    . ASP   B 2 14  ? -1.93100  13.88000  -40.69400 1.000 13.71458 ? 13  ASP   D CB    1 
ATOM   1550 C  CG    . ASP   B 2 14  ? -2.29200  14.67800  -39.45400 1.000 13.71997 ? 13  ASP   D CG    1 
ATOM   1551 O  OD1   . ASP   B 2 14  ? -3.40200  14.49400  -38.91400 1.000 13.63239 ? 13  ASP   D OD1   1 
ATOM   1552 O  OD2   . ASP   B 2 14  ? -1.47300  15.51900  -39.02900 1.000 16.64895 ? 13  ASP   D OD2   1 
ATOM   1553 N  N     . GLY   B 2 15  ? -3.26300  10.85300  -42.45800 1.000 14.88905 ? 14  GLY   D N     1 
ATOM   1554 C  CA    . GLY   B 2 15  ? -3.40200  10.26900  -43.77700 1.000 17.37475 ? 14  GLY   D CA    1 
ATOM   1555 C  C     . GLY   B 2 15  ? -2.16100  9.60800   -44.34400 1.000 19.84294 ? 14  GLY   D C     1 
ATOM   1556 O  O     . GLY   B 2 15  ? -2.25100  8.96000   -45.39600 1.000 24.40179 ? 14  GLY   D O     1 
ATOM   1557 N  N     . GLU   B 2 16  ? -1.01400  9.75000   -43.70100 1.000 18.62056 ? 15  GLU   D N     1 
ATOM   1558 C  CA    . GLU   B 2 16  ? 0.23300   9.18400   -44.20900 1.000 21.10621 ? 15  GLU   D CA    1 
ATOM   1559 C  C     . GLU   B 2 16  ? 0.47200   7.82700   -43.56400 1.000 19.85903 ? 15  GLU   D C     1 
ATOM   1560 O  O     . GLU   B 2 16  ? 0.41100   7.72100   -42.33600 1.000 19.41255 ? 15  GLU   D O     1 
ATOM   1561 C  CB    . GLU   B 2 16  ? 1.39600   10.10700  -43.86700 1.000 24.14819 ? 15  GLU   D CB    1 
ATOM   1562 C  CG    . GLU   B 2 16  ? 2.77200   9.56100   -44.21500 1.000 30.68143 ? 15  GLU   D CG    1 
ATOM   1563 C  CD    . GLU   B 2 16  ? 3.89600   10.51800  -43.84100 1.000 36.03428 ? 15  GLU   D CD    1 
ATOM   1564 O  OE1   . GLU   B 2 16  ? 3.89800   11.02000  -42.69500 1.000 37.35239 ? 15  GLU   D OE1   1 
ATOM   1565 O  OE2   . GLU   B 2 16  ? 4.77400   10.77200  -44.69800 1.000 38.62938 ? 15  GLU   D OE2   1 
ATOM   1566 N  N     . PRO   B 2 17  ? 0.75100   6.77600   -44.33600 1.000 19.71677 ? 16  PRO   D N     1 
ATOM   1567 C  CA    . PRO   B 2 17  ? 0.95800   5.45700   -43.72400 1.000 19.14612 ? 16  PRO   D CA    1 
ATOM   1568 C  C     . PRO   B 2 17  ? 2.09400   5.48200   -42.71100 1.000 19.00966 ? 16  PRO   D C     1 
ATOM   1569 O  O     . PRO   B 2 17  ? 3.15000   6.07700   -42.94500 1.000 20.56612 ? 16  PRO   D O     1 
ATOM   1570 C  CB    . PRO   B 2 17  ? 1.29400   4.55800   -44.92000 1.000 21.36257 ? 16  PRO   D CB    1 
ATOM   1571 C  CG    . PRO   B 2 17  ? 0.70200   5.26400   -46.09900 1.000 23.72803 ? 16  PRO   D CG    1 
ATOM   1572 C  CD    . PRO   B 2 17  ? 0.85900   6.72500   -45.80500 1.000 21.97643 ? 16  PRO   D CD    1 
ATOM   1573 N  N     . LEU   B 2 18  ? 1.85700   4.84300   -41.56700 1.000 17.34330 ? 17  LEU   D N     1 
ATOM   1574 C  CA    . LEU   B 2 18  ? 2.86700   4.68500   -40.53000 1.000 17.38306 ? 17  LEU   D CA    1 
ATOM   1575 C  C     . LEU   B 2 18  ? 3.39500   3.25600   -40.48200 1.000 17.82530 ? 17  LEU   D C     1 
ATOM   1576 O  O     . LEU   B 2 18  ? 4.60200   3.03400   -40.61700 1.000 20.08435 ? 17  LEU   D O     1 
ATOM   1577 C  CB    . LEU   B 2 18  ? 2.30900   5.11500   -39.16400 1.000 17.10227 ? 17  LEU   D CB    1 
ATOM   1578 C  CG    . LEU   B 2 18  ? 3.23900   4.98000   -37.95300 1.000 17.49430 ? 17  LEU   D CG    1 
ATOM   1579 C  CD1   . LEU   B 2 18  ? 4.42900   5.92700   -38.06200 1.000 20.29315 ? 17  LEU   D CD1   1 
ATOM   1580 C  CD2   . LEU   B 2 18  ? 2.48000   5.21500   -36.65400 1.000 17.80749 ? 17  LEU   D CD2   1 
ATOM   1581 N  N     . GLY   B 2 19  ? 2.52100   2.27300   -40.30700 1.000 16.66619 ? 18  GLY   D N     1 
ATOM   1582 C  CA    . GLY   B 2 19  ? 2.94000   0.88500   -40.31500 1.000 16.72747 ? 18  GLY   D CA    1 
ATOM   1583 C  C     . GLY   B 2 19  ? 1.80700   -0.01100  -39.86400 1.000 16.25698 ? 18  GLY   D C     1 
ATOM   1584 O  O     . GLY   B 2 19  ? 0.69300   0.44400   -39.57800 1.000 16.65476 ? 18  GLY   D O     1 
ATOM   1585 N  N     . ARG   B 2 20  ? 2.11600   -1.30500  -39.79400 1.000 17.12524 ? 19  ARG   D N     1 
ATOM   1586 C  CA    . ARG   B 2 20  ? 1.14700   -2.33600  -39.44600 1.000 16.59332 ? 19  ARG   D CA    1 
ATOM   1587 C  C     . ARG   B 2 20  ? 1.36700   -2.83000  -38.02100 1.000 15.71027 ? 19  ARG   D C     1 
ATOM   1588 O  O     . ARG   B 2 20  ? 2.50300   -3.08100  -37.60600 1.000 17.62697 ? 19  ARG   D O     1 
ATOM   1589 C  CB    . ARG   B 2 20  ? 1.23100   -3.52100  -40.41600 1.000 18.37203 ? 19  ARG   D CB    1 
ATOM   1590 C  CG    . ARG   B 2 20  ? 0.32500   -4.68800  -40.05500 1.000 19.42578 ? 19  ARG   D CG    1 
ATOM   1591 C  CD    . ARG   B 2 20  ? 0.22900   -5.69400  -41.19400 1.000 20.10646 ? 19  ARG   D CD    1 
ATOM   1592 N  NE    . ARG   B 2 20  ? -0.52900  -5.16400  -42.32100 1.000 20.68650 ? 19  ARG   D NE    1 
ATOM   1593 C  CZ    . ARG   B 2 20  ? -0.97600  -5.89100  -43.33500 1.000 22.00375 ? 19  ARG   D CZ    1 
ATOM   1594 N  NH1   . ARG   B 2 20  ? -0.72500  -7.19100  -43.42100 1.000 22.37429 ? 19  ARG   D NH1   1 
ATOM   1595 N  NH2   . ARG   B 2 20  ? -1.69700  -5.30300  -44.28500 1.000 24.26059 ? 19  ARG   D NH2   1 
ATOM   1596 N  N     . VAL   B 2 21  ? 0.27300   -2.96900  -37.27700 1.000 14.22850 ? 20  VAL   D N     1 
ATOM   1597 C  CA    . VAL   B 2 21  ? 0.26400   -3.64600  -35.98600 1.000 13.22358 ? 20  VAL   D CA    1 
ATOM   1598 C  C     . VAL   B 2 21  ? -0.59900  -4.89000  -36.12900 1.000 12.99122 ? 20  VAL   D C     1 
ATOM   1599 O  O     . VAL   B 2 21  ? -1.71400  -4.81600  -36.65900 1.000 13.60325 ? 20  VAL   D O     1 
ATOM   1600 C  CB    . VAL   B 2 21  ? -0.30300  -2.73800  -34.87800 1.000 13.82150 ? 20  VAL   D CB    1 
ATOM   1601 C  CG1   . VAL   B 2 21  ? -0.25100  -3.45100  -33.52500 1.000 13.97322 ? 20  VAL   D CG1   1 
ATOM   1602 C  CG2   . VAL   B 2 21  ? 0.43100   -1.40800  -34.83200 1.000 14.52725 ? 20  VAL   D CG2   1 
ATOM   1603 N  N     . SER   B 2 22  ? -0.09300  -6.03000  -35.66400 1.000 12.14274 ? 21  SER   D N     1 
ATOM   1604 C  CA    . SER   B 2 22  ? -0.89500  -7.24500  -35.63400 1.000 12.70916 ? 21  SER   D CA    1 
ATOM   1605 C  C     . SER   B 2 22  ? -1.11300  -7.68800  -34.19500 1.000 12.02581 ? 21  SER   D C     1 
ATOM   1606 O  O     . SER   B 2 22  ? -0.33500  -7.35200  -33.29900 1.000 12.44007 ? 21  SER   D O     1 
ATOM   1607 C  CB    . SER   B 2 22  ? -0.26200  -8.37600  -36.45000 1.000 14.40193 ? 21  SER   D CB    1 
ATOM   1608 O  OG    . SER   B 2 22  ? 0.94100   -8.81500  -35.85600 1.000 15.84982 ? 21  SER   D OG    1 
ATOM   1609 N  N     . PHE   B 2 23  ? -2.18400  -8.45900  -33.99600 1.000 11.23794 ? 22  PHE   D N     1 
ATOM   1610 C  CA    . PHE   B 2 23  ? -2.61900  -8.88000  -32.67300 1.000 10.70358 ? 22  PHE   D CA    1 
ATOM   1611 C  C     . PHE   B 2 23  ? -2.99000  -10.35200 -32.70500 1.000 11.11226 ? 22  PHE   D C     1 
ATOM   1612 O  O     . PHE   B 2 23  ? -3.62900  -10.81800 -33.65400 1.000 11.83057 ? 22  PHE   D O     1 
ATOM   1613 C  CB    . PHE   B 2 23  ? -3.88900  -8.13900  -32.22800 1.000 10.86477 ? 22  PHE   D CB    1 
ATOM   1614 C  CG    . PHE   B 2 23  ? -3.80800  -6.64000  -32.35200 1.000 10.94714 ? 22  PHE   D CG    1 
ATOM   1615 C  CD1   . PHE   B 2 23  ? -3.34700  -5.85700  -31.29800 1.000 11.01210 ? 22  PHE   D CD1   1 
ATOM   1616 C  CD2   . PHE   B 2 23  ? -4.21600  -6.00300  -33.51800 1.000 11.10898 ? 22  PHE   D CD2   1 
ATOM   1617 C  CE1   . PHE   B 2 23  ? -3.29000  -4.46900  -31.41000 1.000 11.20640 ? 22  PHE   D CE1   1 
ATOM   1618 C  CE2   . PHE   B 2 23  ? -4.16100  -4.62300  -33.63400 1.000 11.69677 ? 22  PHE   D CE2   1 
ATOM   1619 C  CZ    . PHE   B 2 23  ? -3.70000  -3.85900  -32.57800 1.000 11.26593 ? 22  PHE   D CZ    1 
ATOM   1620 N  N     . GLU   B 2 24  ? -2.61200  -11.06800 -31.64700 1.000 9.95593  ? 23  GLU   D N     1 
ATOM   1621 C  CA    . GLU   B 2 24  ? -3.19700  -12.36400 -31.33600 1.000 10.26790 ? 23  GLU   D CA    1 
ATOM   1622 C  C     . GLU   B 2 24  ? -4.41300  -12.12500 -30.45000 1.000 9.05033  ? 23  GLU   D C     1 
ATOM   1623 O  O     . GLU   B 2 24  ? -4.33200  -11.37500 -29.47200 1.000 10.12522 ? 23  GLU   D O     1 
ATOM   1624 C  CB    . GLU   B 2 24  ? -2.20200  -13.24300 -30.57500 1.000 11.39277 ? 23  GLU   D CB    1 
ATOM   1625 C  CG    . GLU   B 2 24  ? -2.79800  -14.59200 -30.17900 1.000 11.98349 ? 23  GLU   D CG    1 
ATOM   1626 C  CD    . GLU   B 2 24  ? -1.85200  -15.47900 -29.39000 1.000 14.41368 ? 23  GLU   D CD    1 
ATOM   1627 O  OE1   . GLU   B 2 24  ? -0.67100  -15.11800 -29.20600 1.000 17.24590 ? 23  GLU   D OE1   1 
ATOM   1628 O  OE2   . GLU   B 2 24  ? -2.30300  -16.54600 -28.93000 1.000 14.59141 ? 23  GLU   D OE2   1 
ATOM   1629 N  N     . LEU   B 2 25  ? -5.53500  -12.75800 -30.78400 1.000 8.94877  ? 24  LEU   D N     1 
ATOM   1630 C  CA    . LEU   B 2 25  ? -6.75400  -12.66300 -29.99100 1.000 9.58231  ? 24  LEU   D CA    1 
ATOM   1631 C  C     . LEU   B 2 25  ? -6.93100  -13.96800 -29.22500 1.000 9.09063  ? 24  LEU   D C     1 
ATOM   1632 O  O     . LEU   B 2 25  ? -6.91700  -15.04800 -29.82900 1.000 10.00262 ? 24  LEU   D O     1 
ATOM   1633 C  CB    . LEU   B 2 25  ? -7.96700  -12.39700 -30.88600 1.000 9.35707  ? 24  LEU   D CB    1 
ATOM   1634 C  CG    . LEU   B 2 25  ? -7.81600  -11.22400 -31.86900 1.000 9.58440  ? 24  LEU   D CG    1 
ATOM   1635 C  CD1   . LEU   B 2 25  ? -9.09500  -11.03600 -32.67400 1.000 10.84217 ? 24  LEU   D CD1   1 
ATOM   1636 C  CD2   . LEU   B 2 25  ? -7.44500  -9.92600  -31.14800 1.000 11.07566 ? 24  LEU   D CD2   1 
ATOM   1637 N  N     . PHE   B 2 26  ? -7.10100  -13.87200 -27.90000 1.000 9.84806  ? 25  PHE   D N     1 
ATOM   1638 C  CA    . PHE   B 2 26  ? -7.11200  -15.04600 -27.01900 1.000 10.35451 ? 25  PHE   D CA    1 
ATOM   1639 C  C     . PHE   B 2 26  ? -8.49700  -15.69600 -27.00600 1.000 9.82495  ? 25  PHE   D C     1 
ATOM   1640 O  O     . PHE   B 2 26  ? -9.18400  -15.76900 -25.98300 1.000 11.29685 ? 25  PHE   D O     1 
ATOM   1641 C  CB    . PHE   B 2 26  ? -6.67300  -14.65200 -25.61700 1.000 10.70297 ? 25  PHE   D CB    1 
ATOM   1642 C  CG    . PHE   B 2 26  ? -5.31400  -14.00900 -25.55700 1.000 11.39173 ? 25  PHE   D CG    1 
ATOM   1643 C  CD1   . PHE   B 2 26  ? -4.25700  -14.49300 -26.31100 1.000 13.28227 ? 25  PHE   D CD1   1 
ATOM   1644 C  CD2   . PHE   B 2 26  ? -5.09300  -12.92400 -24.72400 1.000 12.05143 ? 25  PHE   D CD2   1 
ATOM   1645 C  CE1   . PHE   B 2 26  ? -2.99900  -13.89800 -26.23400 1.000 13.72811 ? 25  PHE   D CE1   1 
ATOM   1646 C  CE2   . PHE   B 2 26  ? -3.84300  -12.33000 -24.63900 1.000 13.16841 ? 25  PHE   D CE2   1 
ATOM   1647 C  CZ    . PHE   B 2 26  ? -2.79700  -12.81700 -25.39400 1.000 14.02741 ? 25  PHE   D CZ    1 
ATOM   1648 N  N     . ALA   B 2 27  ? -8.87800  -16.22500 -28.17200 1.000 9.98457  ? 26  ALA   D N     1 
ATOM   1649 C  CA    . ALA   B 2 27  ? -10.16200 -16.90500 -28.29800 1.000 10.89556 ? 26  ALA   D CA    1 
ATOM   1650 C  C     . ALA   B 2 27  ? -10.24100 -18.12000 -27.38800 1.000 10.92847 ? 26  ALA   D C     1 
ATOM   1651 O  O     . ALA   B 2 27  ? -11.34200 -18.52400 -26.99000 1.000 11.88753 ? 26  ALA   D O     1 
ATOM   1652 C  CB    . ALA   B 2 27  ? -10.38300 -17.32500 -29.75000 1.000 12.84364 ? 26  ALA   D CB    1 
ATOM   1653 N  N     . ASP   B 2 28  ? -9.08900  -18.71800 -27.05400 1.000 10.87308 ? 27  ASP   D N     1 
ATOM   1654 C  CA    . ASP   B 2 28  ? -9.06900  -19.87700 -26.17000 1.000 12.11008 ? 27  ASP   D CA    1 
ATOM   1655 C  C     . ASP   B 2 28  ? -9.52900  -19.55200 -24.75400 1.000 13.14938 ? 27  ASP   D C     1 
ATOM   1656 O  O     . ASP   B 2 28  ? -9.99900  -20.45400 -24.05300 1.000 16.20809 ? 27  ASP   D O     1 
ATOM   1657 C  CB    . ASP   B 2 28  ? -7.68900  -20.55300 -26.17300 1.000 14.38038 ? 27  ASP   D CB    1 
ATOM   1658 C  CG    . ASP   B 2 28  ? -6.52600  -19.58100 -25.93900 1.000 16.25616 ? 27  ASP   D CG    1 
ATOM   1659 O  OD1   . ASP   B 2 28  ? -6.73300  -18.37900 -25.69600 1.000 16.22898 ? 27  ASP   D OD1   1 
ATOM   1660 O  OD2   . ASP   B 2 28  ? -5.36600  -20.03800 -26.01900 1.000 20.48331 ? 27  ASP   D OD2   1 
ATOM   1661 N  N     . LYS   B 2 29  ? -9.42200  -18.29600 -24.31700 1.000 11.29869 ? 28  LYS   D N     1 
ATOM   1662 C  CA    . LYS   B 2 29  ? -9.81800  -17.92000 -22.96800 1.000 12.23963 ? 28  LYS   D CA    1 
ATOM   1663 C  C     . LYS   B 2 29  ? -10.97400 -16.93700 -22.90500 1.000 9.81893  ? 28  LYS   D C     1 
ATOM   1664 O  O     . LYS   B 2 29  ? -11.69900 -16.92900 -21.90300 1.000 10.56242 ? 28  LYS   D O     1 
ATOM   1665 C  CB    . LYS   B 2 29  ? -8.61600  -17.37500 -22.18300 1.000 15.41257 ? 28  LYS   D CB    1 
ATOM   1666 C  CG    . LYS   B 2 29  ? -7.58300  -18.46000 -21.87000 1.000 17.58708 ? 28  LYS   D CG    1 
ATOM   1667 C  CD    . LYS   B 2 29  ? -6.45300  -17.92800 -21.01500 1.000 19.33112 ? 28  LYS   D CD    1 
ATOM   1668 C  CE    . LYS   B 2 29  ? -5.40600  -18.99700 -20.76100 1.000 20.47418 ? 28  LYS   D CE    1 
ATOM   1669 N  NZ    . LYS   B 2 29  ? -4.81500  -19.46300 -22.03700 1.000 21.47777 ? 28  LYS   D NZ    1 
ATOM   1670 N  N     . VAL   B 2 30  ? -11.16000 -16.10900 -23.93000 1.000 9.75792  ? 29  VAL   D N     1 
ATOM   1671 C  CA    . VAL   B 2 30  ? -12.26400 -15.14600 -23.98200 1.000 9.87831  ? 29  VAL   D CA    1 
ATOM   1672 C  C     . VAL   B 2 30  ? -12.87200 -15.18200 -25.37700 1.000 9.62017  ? 29  VAL   D C     1 
ATOM   1673 O  O     . VAL   B 2 30  ? -12.72400 -14.22700 -26.16200 1.000 9.56816  ? 29  VAL   D O     1 
ATOM   1674 C  CB    . VAL   B 2 30  ? -11.85400 -13.71900 -23.57500 1.000 12.66487 ? 29  VAL   D CB    1 
ATOM   1675 C  CG1   . VAL   B 2 30  ? -11.88600 -13.56000 -22.05900 1.000 15.58803 ? 29  VAL   D CG1   1 
ATOM   1676 C  CG2   . VAL   B 2 30  ? -10.51300 -13.34600 -24.14000 1.000 14.72159 ? 29  VAL   D CG2   1 
ATOM   1677 N  N     . PRO   B 2 31  ? -13.55300 -16.27200 -25.72900 1.000 10.03370 ? 30  PRO   D N     1 
ATOM   1678 C  CA    . PRO   B 2 31  ? -13.99700 -16.43000 -27.12500 1.000 9.96124  ? 30  PRO   D CA    1 
ATOM   1679 C  C     . PRO   B 2 31  ? -14.96500 -15.36500 -27.60300 1.000 9.51497  ? 30  PRO   D C     1 
ATOM   1680 O  O     . PRO   B 2 31  ? -14.86800 -14.91900 -28.75600 1.000 9.47009  ? 30  PRO   D O     1 
ATOM   1681 C  CB    . PRO   B 2 31  ? -14.65400 -17.81900 -27.12700 1.000 10.74262 ? 30  PRO   D CB    1 
ATOM   1682 C  CG    . PRO   B 2 31  ? -14.96600 -18.09800 -25.67500 1.000 11.51951 ? 30  PRO   D CG    1 
ATOM   1683 C  CD    . PRO   B 2 31  ? -13.84400 -17.46700 -24.92000 1.000 10.51696 ? 30  PRO   D CD    1 
ATOM   1684 N  N     . LYS   B 2 32  ? -15.92100 -14.95800 -26.76900 1.000 9.64475  ? 31  LYS   D N     1 
ATOM   1685 C  CA    A LYS   B 2 32  ? -16.92000 -14.00000 -27.23200 0.500 10.55042 ? 31  LYS   D CA    1 
ATOM   1686 C  CA    B LYS   B 2 32  ? -16.92500 -13.99800 -27.21800 0.500 9.12283  ? 31  LYS   D CA    1 
ATOM   1687 C  C     . LYS   B 2 32  ? -16.30600 -12.62500 -27.45200 1.000 9.11678  ? 31  LYS   D C     1 
ATOM   1688 O  O     . LYS   B 2 32  ? -16.65400 -11.93200 -28.42100 1.000 8.98810  ? 31  LYS   D O     1 
ATOM   1689 C  CB    A LYS   B 2 32  ? -18.08100 -13.92200 -26.24300 0.500 13.12926 ? 31  LYS   D CB    1 
ATOM   1690 C  CB    B LYS   B 2 32  ? -18.04900 -13.91600 -26.18700 0.500 8.90102  ? 31  LYS   D CB    1 
ATOM   1691 C  CG    A LYS   B 2 32  ? -18.81400 -15.23800 -26.06500 0.500 15.95711 ? 31  LYS   D CG    1 
ATOM   1692 C  CG    B LYS   B 2 32  ? -19.22800 -13.07900 -26.61500 0.500 9.11316  ? 31  LYS   D CG    1 
ATOM   1693 C  CD    A LYS   B 2 32  ? -19.81300 -15.15800 -24.92200 0.500 19.44732 ? 31  LYS   D CD    1 
ATOM   1694 C  CD    B LYS   B 2 32  ? -20.37200 -13.18700 -25.62000 0.500 10.97767 ? 31  LYS   D CD    1 
ATOM   1695 C  CE    A LYS   B 2 32  ? -20.28300 -16.53800 -24.50100 0.500 21.80306 ? 31  LYS   D CE    1 
ATOM   1696 C  CE    B LYS   B 2 32  ? -21.56400 -12.35800 -26.06600 0.500 13.00223 ? 31  LYS   D CE    1 
ATOM   1697 N  NZ    A LYS   B 2 32  ? -21.17200 -16.47300 -23.31200 0.500 22.27806 ? 31  LYS   D NZ    1 
ATOM   1698 N  NZ    B LYS   B 2 32  ? -22.72700 -12.54700 -25.15200 0.500 15.66716 ? 31  LYS   D NZ    1 
ATOM   1699 N  N     . THR   B 2 33  ? -15.38900 -12.22400 -26.57100 1.000 8.16346  ? 32  THR   D N     1 
ATOM   1700 C  CA    . THR   B 2 33  ? -14.74800 -10.92200 -26.69400 1.000 8.64448  ? 32  THR   D CA    1 
ATOM   1701 C  C     . THR   B 2 33  ? -13.77000 -10.91800 -27.86300 1.000 7.49384  ? 32  THR   D C     1 
ATOM   1702 O  O     . THR   B 2 33  ? -13.71200 -9.95300  -28.63700 1.000 8.43334  ? 32  THR   D O     1 
ATOM   1703 C  CB    . THR   B 2 33  ? -14.06800 -10.58000 -25.36400 1.000 8.67054  ? 32  THR   D CB    1 
ATOM   1704 O  OG1   . THR   B 2 33  ? -15.02200 -10.68400 -24.29700 1.000 8.86144  ? 32  THR   D OG1   1 
ATOM   1705 C  CG2   . THR   B 2 33  ? -13.50200 -9.17300  -25.38300 1.000 9.14080  ? 32  THR   D CG2   1 
ATOM   1706 N  N     . ALA   B 2 34  ? -13.01800 -12.00800 -28.02500 1.000 8.51655  ? 33  ALA   D N     1 
ATOM   1707 C  CA    . ALA   B 2 34  ? -12.11900 -12.12300 -29.16700 1.000 8.57569  ? 33  ALA   D CA    1 
ATOM   1708 C  C     . ALA   B 2 34  ? -12.89200 -12.07800 -30.47800 1.000 8.43349  ? 33  ALA   D C     1 
ATOM   1709 O  O     . ALA   B 2 34  ? -12.46700 -11.42200 -31.44100 1.000 9.15371  ? 33  ALA   D O     1 
ATOM   1710 C  CB    . ALA   B 2 34  ? -11.31100 -13.41600 -29.06300 1.000 9.97879  ? 33  ALA   D CB    1 
ATOM   1711 N  N     . GLU   B 2 35  ? -14.02800 -12.78000 -30.53600 1.000 8.70321  ? 34  GLU   D N     1 
ATOM   1712 C  CA    . GLU   B 2 35  ? -14.79100 -12.85000 -31.77900 1.000 9.26166  ? 34  GLU   D CA    1 
ATOM   1713 C  C     . GLU   B 2 35  ? -15.33600 -11.48200 -32.16600 1.000 8.57504  ? 34  GLU   D C     1 
ATOM   1714 O  O     . GLU   B 2 35  ? -15.36100 -11.12900 -33.35400 1.000 8.81677  ? 34  GLU   D O     1 
ATOM   1715 C  CB    . GLU   B 2 35  ? -15.91600 -13.87900 -31.65100 1.000 9.58949  ? 34  GLU   D CB    1 
ATOM   1716 C  CG    . GLU   B 2 35  ? -16.85300 -13.93300 -32.84200 1.000 10.93180 ? 34  GLU   D CG    1 
ATOM   1717 C  CD    . GLU   B 2 35  ? -16.18900 -14.35100 -34.15500 1.000 11.81664 ? 34  GLU   D CD    1 
ATOM   1718 O  OE1   . GLU   B 2 35  ? -15.01900 -14.79700 -34.16500 1.000 12.42056 ? 34  GLU   D OE1   1 
ATOM   1719 O  OE2   . GLU   B 2 35  ? -16.85500 -14.23400 -35.19900 1.000 15.49111 ? 34  GLU   D OE2   1 
ATOM   1720 N  N     . ASN   B 2 36  ? -15.78100 -10.70200 -31.17800 1.000 8.29084  ? 35  ASN   D N     1 
ATOM   1721 C  CA    . ASN   B 2 36  ? -16.25500 -9.34800  -31.45100 1.000 8.60675  ? 35  ASN   D CA    1 
ATOM   1722 C  C     . ASN   B 2 36  ? -15.16800 -8.51900  -32.12500 1.000 8.42285  ? 35  ASN   D C     1 
ATOM   1723 O  O     . ASN   B 2 36  ? -15.39600 -7.90700  -33.17700 1.000 8.90160  ? 35  ASN   D O     1 
ATOM   1724 C  CB    . ASN   B 2 36  ? -16.71200 -8.72200  -30.12800 1.000 9.11911  ? 35  ASN   D CB    1 
ATOM   1725 C  CG    . ASN   B 2 36  ? -17.22300 -7.30500  -30.28000 1.000 8.62364  ? 35  ASN   D CG    1 
ATOM   1726 O  OD1   . ASN   B 2 36  ? -18.22400 -7.05600  -30.95600 1.000 9.54798  ? 35  ASN   D OD1   1 
ATOM   1727 N  ND2   . ASN   B 2 36  ? -16.55900 -6.36700  -29.60600 1.000 9.29313  ? 35  ASN   D ND2   1 
ATOM   1728 N  N     . PHE   B 2 37  ? -13.97100 -8.50000  -31.54000 1.000 8.48464  ? 36  PHE   D N     1 
ATOM   1729 C  CA    . PHE   B 2 37  ? -12.88200 -7.71000  -32.10200 1.000 8.59090  ? 36  PHE   D CA    1 
ATOM   1730 C  C     . PHE   B 2 37  ? -12.47800 -8.22800  -33.47800 1.000 7.87724  ? 36  PHE   D C     1 
ATOM   1731 O  O     . PHE   B 2 37  ? -12.19700 -7.43800  -34.39100 1.000 8.43114  ? 36  PHE   D O     1 
ATOM   1732 C  CB    . PHE   B 2 37  ? -11.70500 -7.74200  -31.13200 1.000 8.92719  ? 36  PHE   D CB    1 
ATOM   1733 C  CG    . PHE   B 2 37  ? -10.57400 -6.81000  -31.48600 1.000 8.14980  ? 36  PHE   D CG    1 
ATOM   1734 C  CD1   . PHE   B 2 37  ? -10.53700 -5.51600  -30.98300 1.000 9.08744  ? 36  PHE   D CD1   1 
ATOM   1735 C  CD2   . PHE   B 2 37  ? -9.52600  -7.24000  -32.28600 1.000 9.60523  ? 36  PHE   D CD2   1 
ATOM   1736 C  CE1   . PHE   B 2 37  ? -9.47100  -4.68100  -31.27900 1.000 10.19241 ? 36  PHE   D CE1   1 
ATOM   1737 C  CE2   . PHE   B 2 37  ? -8.47000  -6.40400  -32.58700 1.000 11.22951 ? 36  PHE   D CE2   1 
ATOM   1738 C  CZ    . PHE   B 2 37  ? -8.44300  -5.12800  -32.08200 1.000 10.74377 ? 36  PHE   D CZ    1 
ATOM   1739 N  N     . ARG   B 2 38  ? -12.46100 -9.55600  -33.65400 1.000 8.46232  ? 37  ARG   D N     1 
ATOM   1740 C  CA    . ARG   B 2 38  ? -12.11700 -10.14100 -34.94800 1.000 8.97899  ? 37  ARG   D CA    1 
ATOM   1741 C  C     . ARG   B 2 38  ? -13.08700 -9.68900  -36.03300 1.000 8.83337  ? 37  ARG   D C     1 
ATOM   1742 O  O     . ARG   B 2 38  ? -12.66900 -9.21800  -37.09800 1.000 9.52345  ? 37  ARG   D O     1 
ATOM   1743 C  CB    . ARG   B 2 38  ? -12.12200 -11.67000 -34.85000 1.000 9.57176  ? 37  ARG   D CB    1 
ATOM   1744 C  CG    . ARG   B 2 38  ? -11.57800 -12.34300 -36.10800 1.000 9.84225  ? 37  ARG   D CG    1 
ATOM   1745 C  CD    . ARG   B 2 38  ? -12.04500 -13.79500 -36.24400 1.000 11.02152 ? 37  ARG   D CD    1 
ATOM   1746 N  NE    . ARG   B 2 38  ? -13.49200 -13.88100 -36.40300 1.000 11.84037 ? 37  ARG   D NE    1 
ATOM   1747 C  CZ    . ARG   B 2 38  ? -14.14400 -13.55300 -37.51200 1.000 12.31630 ? 37  ARG   D CZ    1 
ATOM   1748 N  NH1   . ARG   B 2 38  ? -13.50200 -13.20200 -38.61900 1.000 13.46769 ? 37  ARG   D NH1   1 
ATOM   1749 N  NH2   . ARG   B 2 38  ? -15.47600 -13.55300 -37.50600 1.000 13.22629 ? 37  ARG   D NH2   1 
ATOM   1750 N  N     . ALA   B 2 39  ? -14.39300 -9.82900  -35.77900 1.000 8.92588  ? 38  ALA   D N     1 
ATOM   1751 C  CA    . ALA   B 2 39  ? -15.39200 -9.46800  -36.78300 1.000 9.32528  ? 38  ALA   D CA    1 
ATOM   1752 C  C     . ALA   B 2 39  ? -15.41300 -7.96200  -37.05300 1.000 9.47358  ? 38  ALA   D C     1 
ATOM   1753 O  O     . ALA   B 2 39  ? -15.64800 -7.53400  -38.19000 1.000 9.68332  ? 38  ALA   D O     1 
ATOM   1754 C  CB    . ALA   B 2 39  ? -16.76900 -9.96400  -36.34800 1.000 9.89042  ? 38  ALA   D CB    1 
ATOM   1755 N  N     . LEU   B 2 40  ? -15.18500 -7.13800  -36.02500 1.000 9.21346  ? 39  LEU   D N     1 
ATOM   1756 C  CA    . LEU   B 2 40  ? -15.10300 -5.69900  -36.25100 1.000 8.99986  ? 39  LEU   D CA    1 
ATOM   1757 C  C     . LEU   B 2 40  ? -13.86900 -5.33700  -37.07000 1.000 8.54209  ? 39  LEU   D C     1 
ATOM   1758 O  O     . LEU   B 2 40  ? -13.88500 -4.35100  -37.81900 1.000 9.89954  ? 39  LEU   D O     1 
ATOM   1759 C  CB    . LEU   B 2 40  ? -15.11500 -4.96400  -34.91400 1.000 8.96720  ? 39  LEU   D CB    1 
ATOM   1760 C  CG    . LEU   B 2 40  ? -16.43000 -5.07900  -34.13800 1.000 8.69132  ? 39  LEU   D CG    1 
ATOM   1761 C  CD1   . LEU   B 2 40  ? -16.26400 -4.52900  -32.73100 1.000 9.98791  ? 39  LEU   D CD1   1 
ATOM   1762 C  CD2   . LEU   B 2 40  ? -17.57800 -4.38300  -34.87200 1.000 11.00408 ? 39  LEU   D CD2   1 
ATOM   1763 N  N     . SER   B 2 41  ? -12.80200 -6.13200  -36.95300 1.000 9.13558  ? 40  SER   D N     1 
ATOM   1764 C  CA    . SER   B 2 41  ? -11.59300 -5.89200  -37.73100 1.000 9.41098  ? 40  SER   D CA    1 
ATOM   1765 C  C     . SER   B 2 41  ? -11.76300 -6.28300  -39.19600 1.000 9.76919  ? 40  SER   D C     1 
ATOM   1766 O  O     . SER   B 2 41  ? -11.21400 -5.61700  -40.07900 1.000 11.90815 ? 40  SER   D O     1 
ATOM   1767 C  CB    . SER   B 2 41  ? -10.41200 -6.63600  -37.10700 1.000 10.42008 ? 40  SER   D CB    1 
ATOM   1768 O  OG    . SER   B 2 41  ? -10.10400 -6.11600  -35.82400 1.000 10.32604 ? 40  SER   D OG    1 
ATOM   1769 N  N     . THR   B 2 42  ? -12.49600 -7.36100  -39.48700 1.000 10.48723 ? 41  THR   D N     1 
ATOM   1770 C  CA    . THR   B 2 42  ? -12.73400 -7.69800  -40.88700 1.000 11.11754 ? 41  THR   D CA    1 
ATOM   1771 C  C     . THR   B 2 42  ? -13.84100 -6.86100  -41.50700 1.000 11.47305 ? 41  THR   D C     1 
ATOM   1772 O  O     . THR   B 2 42  ? -13.89700 -6.75100  -42.73600 1.000 13.03007 ? 41  THR   D O     1 
ATOM   1773 C  CB    . THR   B 2 42  ? -13.14000 -9.15900  -41.05000 1.000 12.32081 ? 41  THR   D CB    1 
ATOM   1774 O  OG1   . THR   B 2 42  ? -14.41400 -9.35300  -40.42500 1.000 11.81306 ? 41  THR   D OG1   1 
ATOM   1775 C  CG2   . THR   B 2 42  ? -12.09400 -10.09500 -40.44900 1.000 12.70647 ? 41  THR   D CG2   1 
ATOM   1776 N  N     . GLY   B 2 43  ? -14.73400 -6.30300  -40.69200 1.000 11.17545 ? 42  GLY   D N     1 
ATOM   1777 C  CA    . GLY   B 2 43  ? -15.88500 -5.58500  -41.20100 1.000 11.80048 ? 42  GLY   D CA    1 
ATOM   1778 C  C     . GLY   B 2 43  ? -16.96600 -6.46600  -41.78400 1.000 12.66816 ? 42  GLY   D C     1 
ATOM   1779 O  O     . GLY   B 2 43  ? -17.86600 -5.96000  -42.46100 1.000 13.26703 ? 42  GLY   D O     1 
ATOM   1780 N  N     . GLU   B 2 44  ? -16.92900 -7.77200  -41.50400 1.000 12.82331 ? 43  GLU   D N     1 
ATOM   1781 C  CA    . GLU   B 2 44  ? -17.77800 -8.72700  -42.21100 1.000 13.08606 ? 43  GLU   D CA    1 
ATOM   1782 C  C     . GLU   B 2 44  ? -19.26100 -8.57800  -41.89200 1.000 13.84418 ? 43  GLU   D C     1 
ATOM   1783 O  O     . GLU   B 2 44  ? -20.09000 -9.08000  -42.65500 1.000 15.51447 ? 43  GLU   D O     1 
ATOM   1784 C  CB    . GLU   B 2 44  ? -17.30100 -10.15600 -41.94500 1.000 14.38774 ? 43  GLU   D CB    1 
ATOM   1785 C  CG    . GLU   B 2 44  ? -17.41500 -10.58800 -40.49400 1.000 14.48736 ? 43  GLU   D CG    1 
ATOM   1786 C  CD    . GLU   B 2 44  ? -16.61000 -11.83400 -40.20500 1.000 13.50101 ? 43  GLU   D CD    1 
ATOM   1787 O  OE1   . GLU   B 2 44  ? -15.38600 -11.83300 -40.46100 1.000 14.92201 ? 43  GLU   D OE1   1 
ATOM   1788 O  OE2   . GLU   B 2 44  ? -17.19800 -12.83100 -39.73800 1.000 14.95525 ? 43  GLU   D OE2   1 
ATOM   1789 N  N     . LYS   B 2 45  ? -19.62500 -7.90900  -40.80000 1.000 13.32716 ? 44  LYS   D N     1 
ATOM   1790 C  CA    . LYS   B 2 45  ? -21.03400 -7.64700  -40.52600 1.000 14.57123 ? 44  LYS   D CA    1 
ATOM   1791 C  C     . LYS   B 2 45  ? -21.52200 -6.30600  -41.07400 1.000 14.25299 ? 44  LYS   D C     1 
ATOM   1792 O  O     . LYS   B 2 45  ? -22.68100 -5.94000  -40.84600 1.000 15.12373 ? 44  LYS   D O     1 
ATOM   1793 C  CB    . LYS   B 2 45  ? -21.34800 -7.81000  -39.03900 1.000 17.26308 ? 44  LYS   D CB    1 
ATOM   1794 C  CG    . LYS   B 2 45  ? -21.46100 -9.29300  -38.62700 1.000 20.37617 ? 44  LYS   D CG    1 
ATOM   1795 C  CD    . LYS   B 2 45  ? -22.04100 -9.45700  -37.22900 1.000 23.07701 ? 44  LYS   D CD    1 
ATOM   1796 C  CE    . LYS   B 2 45  ? -22.25300 -10.92700 -36.86900 1.000 23.15542 ? 44  LYS   D CE    1 
ATOM   1797 N  NZ    . LYS   B 2 45  ? -23.34600 -11.59800 -37.65000 1.000 23.74857 ? 44  LYS   D NZ    1 
ATOM   1798 N  N     . GLY   B 2 46  ? -20.68800 -5.59700  -41.83100 1.000 13.91591 ? 45  GLY   D N     1 
ATOM   1799 C  CA    . GLY   B 2 46  ? -21.08400 -4.35000  -42.45000 1.000 14.70095 ? 45  GLY   D CA    1 
ATOM   1800 C  C     . GLY   B 2 46  ? -20.70700 -3.11400  -41.67300 1.000 14.25702 ? 45  GLY   D C     1 
ATOM   1801 O  O     . GLY   B 2 46  ? -21.02900 -2.00700  -42.11200 1.000 15.19021 ? 45  GLY   D O     1 
ATOM   1802 N  N     . PHE   B 2 47  ? -20.04600 -3.26900  -40.53200 1.000 12.35202 ? 46  PHE   D N     1 
ATOM   1803 C  CA    . PHE   B 2 47  ? -19.55600 -2.15400  -39.73900 1.000 12.08280 ? 46  PHE   D CA    1 
ATOM   1804 C  C     . PHE   B 2 47  ? -18.31400 -2.63900  -39.00900 1.000 10.89033 ? 46  PHE   D C     1 
ATOM   1805 O  O     . PHE   B 2 47  ? -18.07400 -3.84500  -38.90100 1.000 11.68066 ? 46  PHE   D O     1 
ATOM   1806 C  CB    . PHE   B 2 47  ? -20.61800 -1.64800  -38.75200 1.000 13.20332 ? 46  PHE   D CB    1 
ATOM   1807 C  CG    . PHE   B 2 47  ? -21.21800 -2.73000  -37.89000 1.000 12.85122 ? 46  PHE   D CG    1 
ATOM   1808 C  CD1   . PHE   B 2 47  ? -20.61900 -3.11300  -36.69500 1.000 12.81254 ? 46  PHE   D CD1   1 
ATOM   1809 C  CD2   . PHE   B 2 47  ? -22.39400 -3.36200  -38.27200 1.000 14.47510 ? 46  PHE   D CD2   1 
ATOM   1810 C  CE1   . PHE   B 2 47  ? -21.18100 -4.11300  -35.90600 1.000 13.99656 ? 46  PHE   D CE1   1 
ATOM   1811 C  CE2   . PHE   B 2 47  ? -22.96000 -4.35200  -37.48600 1.000 15.47229 ? 46  PHE   D CE2   1 
ATOM   1812 C  CZ    . PHE   B 2 47  ? -22.35400 -4.72700  -36.30400 1.000 14.85896 ? 46  PHE   D CZ    1 
ATOM   1813 N  N     . GLY   B 2 48  ? -17.52300 -1.70000  -38.50600 1.000 10.71658 ? 47  GLY   D N     1 
ATOM   1814 C  CA    . GLY   B 2 48  ? -16.31800 -2.09400  -37.80100 1.000 10.89631 ? 47  GLY   D CA    1 
ATOM   1815 C  C     . GLY   B 2 48  ? -15.27900 -0.98700  -37.79900 1.000 9.62293  ? 47  GLY   D C     1 
ATOM   1816 O  O     . GLY   B 2 48  ? -15.59200 0.18400   -38.00500 1.000 10.80295 ? 47  GLY   D O     1 
ATOM   1817 N  N     . TYR   B 2 49  ? -14.03800 -1.39500  -37.55200 1.000 9.56750  ? 48  TYR   D N     1 
ATOM   1818 C  CA    . TYR   B 2 49  ? -12.98900 -0.44600  -37.19300 1.000 9.22597  ? 48  TYR   D CA    1 
ATOM   1819 C  C     . TYR   B 2 49  ? -12.42800 0.35800   -38.36600 1.000 9.17936  ? 48  TYR   D C     1 
ATOM   1820 O  O     . TYR   B 2 49  ? -11.84100 1.42000   -38.13200 1.000 10.47507 ? 48  TYR   D O     1 
ATOM   1821 C  CB    . TYR   B 2 49  ? -11.84800 -1.18200  -36.50000 1.000 9.36168  ? 48  TYR   D CB    1 
ATOM   1822 C  CG    . TYR   B 2 49  ? -12.20300 -1.79500  -35.16300 1.000 8.44449  ? 48  TYR   D CG    1 
ATOM   1823 C  CD1   . TYR   B 2 49  ? -12.92500 -1.08100  -34.21200 1.000 8.75236  ? 48  TYR   D CD1   1 
ATOM   1824 C  CD2   . TYR   B 2 49  ? -11.79200 -3.08500  -34.84300 1.000 8.40632  ? 48  TYR   D CD2   1 
ATOM   1825 C  CE1   . TYR   B 2 49  ? -13.22900 -1.63000  -32.98000 1.000 8.70724  ? 48  TYR   D CE1   1 
ATOM   1826 C  CE2   . TYR   B 2 49  ? -12.09500 -3.64700  -33.62200 1.000 8.62481  ? 48  TYR   D CE2   1 
ATOM   1827 C  CZ    . TYR   B 2 49  ? -12.81200 -2.92000  -32.68800 1.000 8.12373  ? 48  TYR   D CZ    1 
ATOM   1828 O  OH    . TYR   B 2 49  ? -13.09800 -3.50300  -31.47500 1.000 8.39176  ? 48  TYR   D OH    1 
ATOM   1829 N  N     . LYS   B 2 50  ? -12.56000 -0.11100  -39.60700 1.000 10.00827 ? 49  LYS   D N     1 
ATOM   1830 C  CA    . LYS   B 2 50  ? -11.85600 0.53700   -40.70700 1.000 10.48888 ? 49  LYS   D CA    1 
ATOM   1831 C  C     . LYS   B 2 50  ? -12.24500 2.00700   -40.82700 1.000 11.33099 ? 49  LYS   D C     1 
ATOM   1832 O  O     . LYS   B 2 50  ? -13.43000 2.34800   -40.90600 1.000 12.36536 ? 49  LYS   D O     1 
ATOM   1833 C  CB    . LYS   B 2 50  ? -12.14500 -0.18400  -42.02000 1.000 11.80820 ? 49  LYS   D CB    1 
ATOM   1834 C  CG    . LYS   B 2 50  ? -11.39800 0.42400   -43.19700 1.000 13.81932 ? 49  LYS   D CG    1 
ATOM   1835 C  CD    . LYS   B 2 50  ? -11.64200 -0.34600  -44.48500 1.000 15.63928 ? 49  LYS   D CD    1 
ATOM   1836 C  CE    . LYS   B 2 50  ? -10.89700 0.29200   -45.64700 1.000 17.16567 ? 49  LYS   D CE    1 
ATOM   1837 N  NZ    . LYS   B 2 50  ? -11.26600 -0.34100  -46.93800 1.000 18.35923 ? 49  LYS   D NZ    1 
ATOM   1838 N  N     . GLY   B 2 51  ? -11.23100 2.88300   -40.82800 1.000 11.22034 ? 50  GLY   D N     1 
ATOM   1839 C  CA    . GLY   B 2 51  ? -11.43200 4.31300   -40.93700 1.000 11.79725 ? 50  GLY   D CA    1 
ATOM   1840 C  C     . GLY   B 2 51  ? -11.54600 5.04800   -39.61900 1.000 11.48636 ? 50  GLY   D C     1 
ATOM   1841 O  O     . GLY   B 2 51  ? -11.48500 6.28400   -39.61000 1.000 12.45700 ? 50  GLY   D O     1 
ATOM   1842 N  N     . SER   B 2 52  ? -11.71300 4.33500   -38.51000 1.000 10.48191 ? 51  SER   D N     1 
ATOM   1843 C  CA    . SER   B 2 52  ? -11.85400 4.97500   -37.21300 1.000 9.84962  ? 51  SER   D CA    1 
ATOM   1844 C  C     . SER   B 2 52  ? -10.49400 5.45000   -36.69800 1.000 9.68855  ? 51  SER   D C     1 
ATOM   1845 O  O     . SER   B 2 52  ? -9.43900  5.08800   -37.22200 1.000 11.36190 ? 51  SER   D O     1 
ATOM   1846 C  CB    . SER   B 2 52  ? -12.55700 4.03700   -36.22900 1.000 10.18309 ? 51  SER   D CB    1 
ATOM   1847 O  OG    . SER   B 2 52  ? -11.76000 2.90800   -35.89200 1.000 10.40744 ? 51  SER   D OG    1 
ATOM   1848 N  N     . SER   B 2 53  ? -10.52200 6.28600   -35.66200 1.000 9.75094  ? 52  SER   D N     1 
ATOM   1849 C  CA    . SER   B 2 53  ? -9.29900  6.88600   -35.15500 1.000 10.26739 ? 52  SER   D CA    1 
ATOM   1850 C  C     . SER   B 2 53  ? -9.01400  6.43300   -33.72700 1.000 8.75614  ? 52  SER   D C     1 
ATOM   1851 O  O     . SER   B 2 53  ? -9.87700  5.88700   -33.03000 1.000 10.47664 ? 52  SER   D O     1 
ATOM   1852 C  CB    . SER   B 2 53  ? -9.35300  8.41700   -35.21000 1.000 14.93166 ? 52  SER   D CB    1 
ATOM   1853 O  OG    . SER   B 2 53  ? -10.25900 8.92100   -34.26000 1.000 17.38805 ? 52  SER   D OG    1 
ATOM   1854 N  N     . PHE   B 2 54  ? -7.77800  6.67000   -33.29600 1.000 8.38239  ? 53  PHE   D N     1 
ATOM   1855 C  CA    . PHE   B 2 54  ? -7.39600  6.51100   -31.89500 1.000 9.00483  ? 53  PHE   D CA    1 
ATOM   1856 C  C     . PHE   B 2 54  ? -7.62400  7.86300   -31.23700 1.000 9.05974  ? 53  PHE   D C     1 
ATOM   1857 O  O     . PHE   B 2 54  ? -6.83100  8.79700   -31.41000 1.000 10.52063 ? 53  PHE   D O     1 
ATOM   1858 C  CB    . PHE   B 2 54  ? -5.94700  6.05100   -31.78000 1.000 10.01660 ? 53  PHE   D CB    1 
ATOM   1859 C  CG    . PHE   B 2 54  ? -5.76900  4.57900   -32.01800 1.000 9.52318  ? 53  PHE   D CG    1 
ATOM   1860 C  CD1   . PHE   B 2 54  ? -5.67800  4.05900   -33.30100 1.000 10.62651 ? 53  PHE   D CD1   1 
ATOM   1861 C  CD2   . PHE   B 2 54  ? -5.74500  3.70200   -30.94700 1.000 9.78488  ? 53  PHE   D CD2   1 
ATOM   1862 C  CE1   . PHE   B 2 54  ? -5.53500  2.68400   -33.49600 1.000 11.42698 ? 53  PHE   D CE1   1 
ATOM   1863 C  CE2   . PHE   B 2 54  ? -5.61700  2.33900   -31.13600 1.000 10.66048 ? 53  PHE   D CE2   1 
ATOM   1864 C  CZ    . PHE   B 2 54  ? -5.50300  1.83200   -32.40500 1.000 11.70305 ? 53  PHE   D CZ    1 
ATOM   1865 N  N     . HIS   B 2 55  ? -8.73200  7.97900   -30.50400 1.000 9.36758  ? 54  HIS   D N     1 
ATOM   1866 C  CA    . HIS   B 2 55  ? -9.13900  9.27600   -29.98200 1.000 9.37433  ? 54  HIS   D CA    1 
ATOM   1867 C  C     . HIS   B 2 55  ? -8.44900  9.63300   -28.67400 1.000 8.92697  ? 54  HIS   D C     1 
ATOM   1868 O  O     . HIS   B 2 55  ? -8.43900  10.80800  -28.30100 1.000 10.26504 ? 54  HIS   D O     1 
ATOM   1869 C  CB    . HIS   B 2 55  ? -10.66500 9.35600   -29.85400 1.000 10.32646 ? 54  HIS   D CB    1 
ATOM   1870 C  CG    . HIS   B 2 55  ? -11.24400 8.35800   -28.90800 1.000 9.80018  ? 54  HIS   D CG    1 
ATOM   1871 N  ND1   . HIS   B 2 55  ? -11.34900 7.01600   -29.21400 1.000 10.39685 ? 54  HIS   D ND1   1 
ATOM   1872 C  CD2   . HIS   B 2 55  ? -11.74200 8.50300   -27.65800 1.000 11.53463 ? 54  HIS   D CD2   1 
ATOM   1873 C  CE1   . HIS   B 2 55  ? -11.89300 6.38000   -28.19000 1.000 10.67998 ? 54  HIS   D CE1   1 
ATOM   1874 N  NE2   . HIS   B 2 55  ? -12.13500 7.25700   -27.23100 1.000 12.15048 ? 54  HIS   D NE2   1 
ATOM   1875 N  N     . ARG   B 2 56  ? -7.86700  8.66500   -27.97100 1.000 8.37828  ? 55  ARG   D N     1 
ATOM   1876 C  CA    . ARG   B 2 56  ? -7.08100  8.93600   -26.77000 1.000 8.56616  ? 55  ARG   D CA    1 
ATOM   1877 C  C     . ARG   B 2 56  ? -5.74900  8.22100   -26.88800 1.000 8.90206  ? 55  ARG   D C     1 
ATOM   1878 O  O     . ARG   B 2 56  ? -5.71300  6.99800   -27.04600 1.000 10.73430 ? 55  ARG   D O     1 
ATOM   1879 C  CB    . ARG   B 2 56  ? -7.79200  8.43800   -25.51400 1.000 9.87672  ? 55  ARG   D CB    1 
ATOM   1880 C  CG    . ARG   B 2 56  ? -9.01500  9.23500   -25.13600 1.000 9.81264  ? 55  ARG   D CG    1 
ATOM   1881 C  CD    . ARG   B 2 56  ? -9.73800  8.58100   -23.97100 1.000 10.67075 ? 55  ARG   D CD    1 
ATOM   1882 N  NE    . ARG   B 2 56  ? -10.89000 9.37100   -23.54900 1.000 11.72218 ? 55  ARG   D NE    1 
ATOM   1883 C  CZ    . ARG   B 2 56  ? -11.61500 9.12300   -22.46600 1.000 10.98860 ? 55  ARG   D CZ    1 
ATOM   1884 N  NH1   . ARG   B 2 56  ? -11.31900 8.12700   -21.64600 1.000 11.26119 ? 55  ARG   D NH1   1 
ATOM   1885 N  NH2   . ARG   B 2 56  ? -12.65800 9.89900   -22.19200 1.000 13.17248 ? 55  ARG   D NH2   1 
ATOM   1886 N  N     . ILE   B 2 57  ? -4.65700  8.96800   -26.79200 1.000 8.06954  ? 56  ILE   D N     1 
ATOM   1887 C  CA    . ILE   B 2 57  ? -3.32500  8.37500   -26.73000 1.000 8.52369  ? 56  ILE   D CA    1 
ATOM   1888 C  C     . ILE   B 2 57  ? -2.62800  9.00300   -25.53300 1.000 8.38777  ? 56  ILE   D C     1 
ATOM   1889 O  O     . ILE   B 2 57  ? -2.39900  10.21700  -25.51300 1.000 8.92462  ? 56  ILE   D O     1 
ATOM   1890 C  CB    . ILE   B 2 57  ? -2.52600  8.58600   -28.02300 1.000 9.32774  ? 56  ILE   D CB    1 
ATOM   1891 C  CG1   . ILE   B 2 57  ? -3.21300  7.86500   -29.19000 1.000 10.25537 ? 56  ILE   D CG1   1 
ATOM   1892 C  CG2   . ILE   B 2 57  ? -1.08200  8.10800   -27.84500 1.000 9.92621  ? 56  ILE   D CG2   1 
ATOM   1893 C  CD1   . ILE   B 2 57  ? -2.50600  8.02800   -30.51300 1.000 11.63145 ? 56  ILE   D CD1   1 
ATOM   1894 N  N     . ILE   B 2 58  ? -2.32500  8.19000   -24.52800 1.000 8.41999  ? 57  ILE   D N     1 
ATOM   1895 C  CA    . ILE   B 2 58  ? -1.71100  8.64100   -23.28400 1.000 8.40486  ? 57  ILE   D CA    1 
ATOM   1896 C  C     . ILE   B 2 58  ? -0.33200  8.00600   -23.18300 1.000 9.14946  ? 57  ILE   D C     1 
ATOM   1897 O  O     . ILE   B 2 58  ? -0.20400  6.81800   -22.87300 1.000 9.77119  ? 57  ILE   D O     1 
ATOM   1898 C  CB    . ILE   B 2 58  ? -2.56600  8.28900   -22.05100 1.000 9.55993  ? 57  ILE   D CB    1 
ATOM   1899 C  CG1   . ILE   B 2 58  ? -4.01000  8.79900   -22.18000 1.000 11.32422 ? 57  ILE   D CG1   1 
ATOM   1900 C  CG2   . ILE   B 2 58  ? -1.89800  8.85100   -20.79300 1.000 10.68670 ? 57  ILE   D CG2   1 
ATOM   1901 C  CD1   . ILE   B 2 58  ? -4.97900  7.83200   -22.83400 1.000 12.27012 ? 57  ILE   D CD1   1 
ATOM   1902 N  N     . PRO   B 2 59  ? 0.73000   8.76900   -23.44500 1.000 9.74393  ? 58  PRO   D N     1 
ATOM   1903 C  CA    . PRO   B 2 59  ? 2.07800   8.19000   -23.42000 1.000 11.17054 ? 58  PRO   D CA    1 
ATOM   1904 C  C     . PRO   B 2 59  ? 2.37800   7.57400   -22.06300 1.000 11.56878 ? 58  PRO   D C     1 
ATOM   1905 O  O     . PRO   B 2 59  ? 2.07100   8.14500   -21.01300 1.000 12.65670 ? 58  PRO   D O     1 
ATOM   1906 C  CB    . PRO   B 2 59  ? 2.98300   9.39600   -23.70300 1.000 12.35749 ? 58  PRO   D CB    1 
ATOM   1907 C  CG    . PRO   B 2 59  ? 2.11600   10.32700  -24.48500 1.000 12.69030 ? 58  PRO   D CG    1 
ATOM   1908 C  CD    . PRO   B 2 59  ? 0.74500   10.17700  -23.87900 1.000 11.02812 ? 58  PRO   D CD    1 
ATOM   1909 N  N     . GLY   B 2 60  ? 2.98700   6.39200   -22.09500 1.000 12.01760 ? 59  GLY   D N     1 
ATOM   1910 C  CA    . GLY   B 2 60  ? 3.28400   5.65000   -20.89200 1.000 13.65350 ? 59  GLY   D CA    1 
ATOM   1911 C  C     . GLY   B 2 60  ? 2.14400   4.80500   -20.37300 1.000 12.16315 ? 59  GLY   D C     1 
ATOM   1912 O  O     . GLY   B 2 60  ? 2.33200   4.07700   -19.39200 1.000 13.51459 ? 59  GLY   D O     1 
ATOM   1913 N  N     . PHE   B 2 61  ? 0.97100   4.87000   -21.00100 1.000 9.74507  ? 60  PHE   D N     1 
ATOM   1914 C  CA    . PHE   B 2 61  ? -0.20400  4.15500   -20.51400 1.000 10.13401 ? 60  PHE   D CA    1 
ATOM   1915 C  C     . PHE   B 2 61  ? -0.89000  3.33600   -21.60400 1.000 9.09555  ? 60  PHE   D C     1 
ATOM   1916 O  O     . PHE   B 2 61  ? -0.78700  2.10200   -21.59400 1.000 10.05014 ? 60  PHE   D O     1 
ATOM   1917 C  CB    . PHE   B 2 61  ? -1.16800  5.11100   -19.80800 1.000 10.56218 ? 60  PHE   D CB    1 
ATOM   1918 C  CG    . PHE   B 2 61  ? -0.63700  5.62900   -18.49700 1.000 11.50797 ? 60  PHE   D CG    1 
ATOM   1919 C  CD1   . PHE   B 2 61  ? 0.19600   6.74100   -18.45700 1.000 13.44316 ? 60  PHE   D CD1   1 
ATOM   1920 C  CD2   . PHE   B 2 61  ? -0.94000  4.98700   -17.30200 1.000 14.19789 ? 60  PHE   D CD2   1 
ATOM   1921 C  CE1   . PHE   B 2 61  ? 0.69800   7.20500   -17.25400 1.000 15.57512 ? 60  PHE   D CE1   1 
ATOM   1922 C  CE2   . PHE   B 2 61  ? -0.44100  5.45600   -16.09400 1.000 17.77156 ? 60  PHE   D CE2   1 
ATOM   1923 C  CZ    . PHE   B 2 61  ? 0.37700   6.56200   -16.07600 1.000 17.50545 ? 60  PHE   D CZ    1 
ATOM   1924 N  N     . MET   B 2 62  ? -1.59400  3.97400   -22.54100 1.000 8.99551  ? 61  MET   D N     1 
ATOM   1925 C  CA    . MET   B 2 62  ? -2.30200  3.20300   -23.55700 1.000 8.89012  ? 61  MET   D CA    1 
ATOM   1926 C  C     . MET   B 2 62  ? -2.75100  4.09600   -24.70500 1.000 8.34756  ? 61  MET   D C     1 
ATOM   1927 O  O     . MET   B 2 62  ? -2.79800  5.32400   -24.59000 1.000 9.10513  ? 61  MET   D O     1 
ATOM   1928 C  CB    . MET   B 2 62  ? -3.52700  2.47800   -22.98300 1.000 9.33226  ? 61  MET   D CB    1 
ATOM   1929 C  CG    . MET   B 2 62  ? -4.72600  3.37200   -22.66800 1.000 10.25489 ? 61  MET   D CG    1 
ATOM   1930 S  SD    . MET   B 2 62  ? -4.57900  4.30800   -21.13700 1.000 11.00669 ? 61  MET   D SD    1 
ATOM   1931 C  CE    . MET   B 2 62  ? -4.48700  2.99000   -19.93400 1.000 11.59628 ? 61  MET   D CE    1 
ATOM   1932 N  N     . CYS   B 2 63  ? -3.13000  3.43300   -25.80300 1.000 8.65703  ? 62  CYS   D N     1 
ATOM   1933 C  CA    A CYS   B 2 63  ? -3.78500  4.03500   -26.96600 0.500 7.17877  ? 62  CYS   D CA    1 
ATOM   1934 C  CA    B CYS   B 2 63  ? -3.82200  4.08600   -26.90300 0.500 12.09866 ? 62  CYS   D CA    1 
ATOM   1935 C  C     . CYS   B 2 63  ? -5.19000  3.44300   -27.06400 1.000 8.22902  ? 62  CYS   D C     1 
ATOM   1936 O  O     . CYS   B 2 63  ? -5.32000  2.21600   -27.16300 1.000 9.73764  ? 62  CYS   D O     1 
ATOM   1937 C  CB    A CYS   B 2 63  ? -3.01500  3.66700   -28.23700 0.500 6.87593  ? 62  CYS   D CB    1 
ATOM   1938 C  CB    B CYS   B 2 63  ? -3.02200  4.07200   -28.20500 0.500 18.73432 ? 62  CYS   D CB    1 
ATOM   1939 S  SG    A CYS   B 2 63  ? -1.28900  4.24100   -28.29700 0.500 6.55721  ? 62  CYS   D SG    1 
ATOM   1940 S  SG    B CYS   B 2 63  ? -2.67000  2.45900   -28.81900 0.500 23.63211 ? 62  CYS   D SG    1 
ATOM   1941 N  N     . GLN   B 2 64  ? -6.22000  4.28700   -27.05800 1.000 7.72788  ? 63  GLN   D N     1 
ATOM   1942 C  CA    . GLN   B 2 64  ? -7.60600  3.84300   -27.08700 1.000 8.09037  ? 63  GLN   D CA    1 
ATOM   1943 C  C     . GLN   B 2 64  ? -8.26500  4.22700   -28.40700 1.000 7.85101  ? 63  GLN   D C     1 
ATOM   1944 O  O     . GLN   B 2 64  ? -8.11500  5.35500   -28.88900 1.000 8.85431  ? 63  GLN   D O     1 
ATOM   1945 C  CB    . GLN   B 2 64  ? -8.38100  4.45600   -25.92000 1.000 8.25539  ? 63  GLN   D CB    1 
ATOM   1946 C  CG    . GLN   B 2 64  ? -9.84100  4.04900   -25.84800 1.000 8.49951  ? 63  GLN   D CG    1 
ATOM   1947 C  CD    . GLN   B 2 64  ? -10.51500 4.61200   -24.60500 1.000 8.77689  ? 63  GLN   D CD    1 
ATOM   1948 O  OE1   . GLN   B 2 64  ? -9.84600  4.95300   -23.62800 1.000 10.76927 ? 63  GLN   D OE1   1 
ATOM   1949 N  NE2   . GLN   B 2 64  ? -11.84000 4.72200   -24.63600 1.000 8.80965  ? 63  GLN   D NE2   1 
ATOM   1950 N  N     . GLY   B 2 65  ? -9.01800  3.29400   -28.97500 1.000 8.14010  ? 64  GLY   D N     1 
ATOM   1951 C  CA    . GLY   B 2 65  ? -9.74700  3.53200   -30.20200 1.000 8.88032  ? 64  GLY   D CA    1 
ATOM   1952 C  C     . GLY   B 2 65  ? -11.02100 2.71900   -30.28300 1.000 8.24780  ? 64  GLY   D C     1 
ATOM   1953 O  O     . GLY   B 2 65  ? -11.53600 2.23900   -29.26600 1.000 8.73605  ? 64  GLY   D O     1 
ATOM   1954 N  N     . GLY   B 2 66  ? -11.54500 2.56700   -31.49300 1.000 9.16775  ? 65  GLY   D N     1 
ATOM   1955 C  CA    . GLY   B 2 66  ? -12.68400 1.70900   -31.72500 1.000 9.79935  ? 65  GLY   D CA    1 
ATOM   1956 C  C     . GLY   B 2 66  ? -14.03700 2.38400   -31.79200 1.000 10.27826 ? 65  GLY   D C     1 
ATOM   1957 O  O     . GLY   B 2 66  ? -15.03900 1.68100   -31.95000 1.000 10.89265 ? 65  GLY   D O     1 
ATOM   1958 N  N     . ASP   B 2 67  ? -14.11500 3.70800   -31.68400 1.000 9.75359  ? 66  ASP   D N     1 
ATOM   1959 C  CA    . ASP   B 2 67  ? -15.40300 4.39800   -31.79900 1.000 10.10616 ? 66  ASP   D CA    1 
ATOM   1960 C  C     . ASP   B 2 67  ? -15.65100 4.73300   -33.26500 1.000 9.99680  ? 66  ASP   D C     1 
ATOM   1961 O  O     . ASP   B 2 67  ? -15.20700 5.76800   -33.76700 1.000 11.74848 ? 66  ASP   D O     1 
ATOM   1962 C  CB    . ASP   B 2 67  ? -15.45000 5.64700   -30.92900 1.000 11.70215 ? 66  ASP   D CB    1 
ATOM   1963 C  CG    . ASP   B 2 67  ? -16.80900 6.32900   -30.97400 1.000 12.14788 ? 66  ASP   D CG    1 
ATOM   1964 O  OD1   . ASP   B 2 67  ? -17.65600 5.91400   -31.80200 1.000 13.05206 ? 66  ASP   D OD1   1 
ATOM   1965 O  OD2   . ASP   B 2 67  ? -17.03200 7.27500   -30.18500 1.000 12.20763 ? 66  ASP   D OD2   1 
ATOM   1966 N  N     . PHE   B 2 68  ? -16.40000 3.87200   -33.94800 1.000 10.82796 ? 67  PHE   D N     1 
ATOM   1967 C  CA    . PHE   B 2 68  ? -16.76900 4.09400   -35.33900 1.000 11.38459 ? 67  PHE   D CA    1 
ATOM   1968 C  C     . PHE   B 2 68  ? -18.18600 4.64100   -35.50600 1.000 11.99275 ? 67  PHE   D C     1 
ATOM   1969 O  O     . PHE   B 2 68  ? -18.68800 4.66900   -36.63400 1.000 14.19207 ? 67  PHE   D O     1 
ATOM   1970 C  CB    . PHE   B 2 68  ? -16.56000 2.81900   -36.17500 1.000 11.21261 ? 67  PHE   D CB    1 
ATOM   1971 C  CG    . PHE   B 2 68  ? -17.30600 1.62100   -35.66200 1.000 10.63928 ? 67  PHE   D CG    1 
ATOM   1972 C  CD1   . PHE   B 2 68  ? -18.63300 1.41500   -36.00300 1.000 11.23005 ? 67  PHE   D CD1   1 
ATOM   1973 C  CD2   . PHE   B 2 68  ? -16.68200 0.69100   -34.84700 1.000 11.22949 ? 67  PHE   D CD2   1 
ATOM   1974 C  CE1   . PHE   B 2 68  ? -19.32500 0.31300   -35.53600 1.000 12.80804 ? 67  PHE   D CE1   1 
ATOM   1975 C  CE2   . PHE   B 2 68  ? -17.37200 -0.41800  -34.38100 1.000 12.74995 ? 67  PHE   D CE2   1 
ATOM   1976 C  CZ    . PHE   B 2 68  ? -18.69300 -0.60300  -34.72700 1.000 14.09870 ? 67  PHE   D CZ    1 
ATOM   1977 N  N     . THR   B 2 69  ? -18.84800 5.08800   -34.42300 1.000 11.37561 ? 68  THR   D N     1 
ATOM   1978 C  CA    . THR   B 2 69  ? -20.19700 5.64100   -34.55700 1.000 12.72678 ? 68  THR   D CA    1 
ATOM   1979 C  C     . THR   B 2 69  ? -20.40300 7.06600   -34.06000 1.000 14.28742 ? 68  THR   D C     1 
ATOM   1980 O  O     . THR   B 2 69  ? -21.37400 7.69800   -34.48300 1.000 15.06119 ? 68  THR   D O     1 
ATOM   1981 C  CB    . THR   B 2 69  ? -21.27200 4.76900   -33.88300 1.000 13.72177 ? 68  THR   D CB    1 
ATOM   1982 O  OG1   . THR   B 2 69  ? -21.16800 4.88200   -32.45800 1.000 13.50681 ? 68  THR   D OG1   1 
ATOM   1983 C  CG2   . THR   B 2 69  ? -21.17900 3.30500   -34.32300 1.000 15.19436 ? 68  THR   D CG2   1 
ATOM   1984 N  N     A ARG   B 2 70  ? -19.56200 7.57900   -33.16300 0.500 15.78497 ? 69  ARG   D N     1 
ATOM   1985 N  N     B ARG   B 2 70  ? -19.55100 7.58500   -33.18100 0.500 15.89035 ? 69  ARG   D N     1 
ATOM   1986 C  CA    A ARG   B 2 70  ? -19.76200 8.91600   -32.61500 0.500 18.27371 ? 69  ARG   D CA    1 
ATOM   1987 C  CA    B ARG   B 2 70  ? -19.75800 8.91900   -32.63500 0.500 18.56332 ? 69  ARG   D CA    1 
ATOM   1988 C  C     A ARG   B 2 70  ? -18.49200 9.74400   -32.76000 0.500 20.73895 ? 69  ARG   D C     1 
ATOM   1989 C  C     B ARG   B 2 70  ? -18.48400 9.74400   -32.74300 0.500 20.83385 ? 69  ARG   D C     1 
ATOM   1990 O  O     A ARG   B 2 70  ? -17.40600 9.21800   -33.01500 0.500 21.49728 ? 69  ARG   D O     1 
ATOM   1991 O  O     B ARG   B 2 70  ? -17.39000 9.21600   -32.95700 0.500 21.54294 ? 69  ARG   D O     1 
ATOM   1992 C  CB    A ARG   B 2 70  ? -20.20000 8.88700   -31.14100 0.500 19.52995 ? 69  ARG   D CB    1 
ATOM   1993 C  CB    B ARG   B 2 70  ? -20.25100 8.87700   -31.18200 0.500 20.23480 ? 69  ARG   D CB    1 
ATOM   1994 C  CG    A ARG   B 2 70  ? -21.46900 8.09200   -30.86800 0.500 22.57248 ? 69  ARG   D CG    1 
ATOM   1995 C  CG    B ARG   B 2 70  ? -21.55200 8.11700   -31.00500 0.500 23.33389 ? 69  ARG   D CG    1 
ATOM   1996 C  CD    A ARG   B 2 70  ? -22.68200 8.96700   -30.62200 0.500 26.41330 ? 69  ARG   D CD    1 
ATOM   1997 C  CD    B ARG   B 2 70  ? -22.74000 9.03100   -30.78100 0.500 27.49466 ? 69  ARG   D CD    1 
ATOM   1998 N  NE    A ARG   B 2 70  ? -23.42700 9.21900   -31.84800 0.500 27.84839 ? 69  ARG   D NE    1 
ATOM   1999 N  NE    B ARG   B 2 70  ? -23.47300 8.63200   -29.58500 0.500 29.84129 ? 69  ARG   D NE    1 
ATOM   2000 C  CZ    A ARG   B 2 70  ? -24.40000 8.44600   -32.30900 0.500 28.24716 ? 69  ARG   D CZ    1 
ATOM   2001 C  CZ    B ARG   B 2 70  ? -23.30300 9.17400   -28.38700 0.500 31.05564 ? 69  ARG   D CZ    1 
ATOM   2002 N  NH1   A ARG   B 2 70  ? -24.77800 7.35100   -31.66900 0.500 28.27686 ? 69  ARG   D NH1   1 
ATOM   2003 N  NH1   B ARG   B 2 70  ? -22.47000 10.18300  -28.19700 0.500 31.06166 ? 69  ARG   D NH1   1 
ATOM   2004 N  NH2   A ARG   B 2 70  ? -25.00900 8.77800   -33.44300 0.500 29.09599 ? 69  ARG   D NH2   1 
ATOM   2005 N  NH2   B ARG   B 2 70  ? -23.98500 8.68900   -27.35400 0.500 32.48584 ? 69  ARG   D NH2   1 
ATOM   2006 N  N     . HIS   B 2 71  ? -18.64600 11.05900  -32.58300 1.000 22.45128 ? 70  HIS   D N     1 
ATOM   2007 C  CA    . HIS   B 2 71  ? -17.55700 12.01200  -32.75600 1.000 24.99108 ? 70  HIS   D CA    1 
ATOM   2008 C  C     . HIS   B 2 71  ? -16.78100 12.30800  -31.47900 1.000 26.05320 ? 70  HIS   D C     1 
ATOM   2009 O  O     . HIS   B 2 71  ? -15.74800 12.98100  -31.54900 1.000 28.74183 ? 70  HIS   D O     1 
ATOM   2010 C  CB    . HIS   B 2 71  ? -18.09500 13.34600  -33.30100 1.000 26.73429 ? 70  HIS   D CB    1 
ATOM   2011 C  CG    . HIS   B 2 71  ? -18.73900 14.21500  -32.26200 1.000 27.17466 ? 70  HIS   D CG    1 
ATOM   2012 N  ND1   . HIS   B 2 71  ? -18.04700 15.18500  -31.56500 1.000 27.94743 ? 70  HIS   D ND1   1 
ATOM   2013 C  CD2   . HIS   B 2 71  ? -20.01100 14.26100  -31.80100 1.000 28.34858 ? 70  HIS   D CD2   1 
ATOM   2014 C  CE1   . HIS   B 2 71  ? -18.86500 15.78600  -30.72000 1.000 29.43076 ? 70  HIS   D CE1   1 
ATOM   2015 N  NE2   . HIS   B 2 71  ? -20.06200 15.24200  -30.83900 1.000 30.70792 ? 70  HIS   D NE2   1 
ATOM   2016 N  N     . ASN   B 2 72  ? -17.25100 11.85300  -30.31800 1.000 23.15416 ? 71  ASN   D N     1 
ATOM   2017 C  CA    . ASN   B 2 72  ? -16.69800 12.28400  -29.03700 1.000 21.52895 ? 71  ASN   D CA    1 
ATOM   2018 C  C     . ASN   B 2 72  ? -16.22600 11.11700  -28.17200 1.000 18.95058 ? 71  ASN   D C     1 
ATOM   2019 O  O     . ASN   B 2 72  ? -16.13600 11.25700  -26.94900 1.000 19.51454 ? 71  ASN   D O     1 
ATOM   2020 C  CB    . ASN   B 2 72  ? -17.73100 13.11500  -28.27600 1.000 22.40382 ? 71  ASN   D CB    1 
ATOM   2021 C  CG    . ASN   B 2 72  ? -18.97500 12.32700  -27.95500 1.000 22.65510 ? 71  ASN   D CG    1 
ATOM   2022 O  OD1   . ASN   B 2 72  ? -19.15500 11.20700  -28.44200 1.000 21.88474 ? 71  ASN   D OD1   1 
ATOM   2023 N  ND2   . ASN   B 2 72  ? -19.84900 12.90200  -27.13800 1.000 23.64840 ? 71  ASN   D ND2   1 
ATOM   2024 N  N     . GLY   B 2 73  ? -15.94100 9.96200   -28.77100 1.000 15.62831 ? 72  GLY   D N     1 
ATOM   2025 C  CA    . GLY   B 2 73  ? -15.45200 8.84400   -27.98700 1.000 13.76741 ? 72  GLY   D CA    1 
ATOM   2026 C  C     . GLY   B 2 73  ? -16.48700 8.17000   -27.11800 1.000 10.39655 ? 72  GLY   D C     1 
ATOM   2027 O  O     . GLY   B 2 73  ? -16.13000 7.40900   -26.21100 1.000 10.57555 ? 72  GLY   D O     1 
ATOM   2028 N  N     . THR   B 2 74  ? -17.76700 8.40700   -27.37400 1.000 9.96270  ? 73  THR   D N     1 
ATOM   2029 C  CA    . THR   B 2 74  ? -18.83100 7.77900   -26.60500 1.000 11.31561 ? 73  THR   D CA    1 
ATOM   2030 C  C     . THR   B 2 74  ? -19.51200 6.64900   -27.36400 1.000 11.03800 ? 73  THR   D C     1 
ATOM   2031 O  O     . THR   B 2 74  ? -20.43400 6.02500   -26.82900 1.000 14.89520 ? 73  THR   D O     1 
ATOM   2032 C  CB    . THR   B 2 74  ? -19.87600 8.82300   -26.19800 1.000 14.36547 ? 73  THR   D CB    1 
ATOM   2033 O  OG1   . THR   B 2 74  ? -20.45600 9.38700   -27.38000 1.000 17.36078 ? 73  THR   D OG1   1 
ATOM   2034 C  CG2   . THR   B 2 74  ? -19.23000 9.91800   -25.36500 1.000 15.46990 ? 73  THR   D CG2   1 
ATOM   2035 N  N     . GLY   B 2 75  ? -19.09800 6.37600   -28.59700 1.000 11.33946 ? 74  GLY   D N     1 
ATOM   2036 C  CA    . GLY   B 2 75  ? -19.82700 5.43600   -29.42500 1.000 11.42664 ? 74  GLY   D CA    1 
ATOM   2037 C  C     . GLY   B 2 75  ? -19.15000 4.10500   -29.65800 1.000 12.19254 ? 74  GLY   D C     1 
ATOM   2038 O  O     . GLY   B 2 75  ? -18.35600 3.62500   -28.83600 1.000 12.18450 ? 74  GLY   D O     1 
ATOM   2039 N  N     . GLY   B 2 76  ? -19.46200 3.51400   -30.80400 1.000 12.81087 ? 75  GLY   D N     1 
ATOM   2040 C  CA    . GLY   B 2 76  ? -19.12300 2.13700   -31.08800 1.000 12.35998 ? 75  GLY   D CA    1 
ATOM   2041 C  C     . GLY   B 2 76  ? -20.23100 1.18100   -30.67800 1.000 11.95192 ? 75  GLY   D C     1 
ATOM   2042 O  O     . GLY   B 2 76  ? -21.11200 1.50000   -29.88500 1.000 15.08956 ? 75  GLY   D O     1 
ATOM   2043 N  N     . LYS   B 2 77  ? -20.17700 -0.02100  -31.24000 1.000 10.94571 ? 76  LYS   D N     1 
ATOM   2044 C  CA    . LYS   B 2 77  ? -21.14200 -1.05700  -30.91700 1.000 11.18065 ? 76  LYS   D CA    1 
ATOM   2045 C  C     . LYS   B 2 77  ? -20.50600 -2.41100  -31.17600 1.000 10.00192 ? 76  LYS   D C     1 
ATOM   2046 O  O     . LYS   B 2 77  ? -19.59200 -2.54500  -31.99800 1.000 10.27288 ? 76  LYS   D O     1 
ATOM   2047 C  CB    . LYS   B 2 77  ? -22.44100 -0.91800  -31.71600 1.000 13.03184 ? 76  LYS   D CB    1 
ATOM   2048 C  CG    . LYS   B 2 77  ? -22.26900 -1.02300  -33.21500 1.000 13.86481 ? 76  LYS   D CG    1 
ATOM   2049 C  CD    . LYS   B 2 77  ? -23.61300 -0.96000  -33.93400 1.000 16.06411 ? 76  LYS   D CD    1 
ATOM   2050 C  CE    . LYS   B 2 77  ? -23.43000 -0.86000  -35.44700 1.000 18.10344 ? 76  LYS   D CE    1 
ATOM   2051 N  NZ    . LYS   B 2 77  ? -24.72900 -0.69000  -36.16500 1.000 20.00186 ? 76  LYS   D NZ    1 
ATOM   2052 N  N     . SER   B 2 78  ? -20.97900 -3.40600  -30.43800 1.000 9.75108  ? 77  SER   D N     1 
ATOM   2053 C  CA    . SER   B 2 78  ? -20.50300 -4.76500  -30.60800 1.000 9.44037  ? 77  SER   D CA    1 
ATOM   2054 C  C     . SER   B 2 78  ? -21.26100 -5.45300  -31.73900 1.000 9.86626  ? 77  SER   D C     1 
ATOM   2055 O  O     . SER   B 2 78  ? -22.21200 -4.91400  -32.31100 1.000 11.78074 ? 77  SER   D O     1 
ATOM   2056 C  CB    . SER   B 2 78  ? -20.69100 -5.55000  -29.31500 1.000 10.49490 ? 77  SER   D CB    1 
ATOM   2057 O  OG    . SER   B 2 78  ? -22.01400 -6.04100  -29.20500 1.000 12.37851 ? 77  SER   D OG    1 
ATOM   2058 N  N     . ILE   B 2 79  ? -20.82900 -6.67800  -32.05300 1.000 9.50384  ? 78  ILE   D N     1 
ATOM   2059 C  CA    . ILE   B 2 79  ? -21.53100 -7.50800  -33.03100 1.000 10.34418 ? 78  ILE   D CA    1 
ATOM   2060 C  C     . ILE   B 2 79  ? -22.73900 -8.21800  -32.44300 1.000 11.26620 ? 78  ILE   D C     1 
ATOM   2061 O  O     . ILE   B 2 79  ? -23.40900 -8.97200  -33.16400 1.000 12.65665 ? 78  ILE   D O     1 
ATOM   2062 C  CB    . ILE   B 2 79  ? -20.57000 -8.52800  -33.67500 1.000 10.60295 ? 78  ILE   D CB    1 
ATOM   2063 C  CG1   . ILE   B 2 79  ? -20.06600 -9.53400  -32.63100 1.000 10.69029 ? 78  ILE   D CG1   1 
ATOM   2064 C  CG2   . ILE   B 2 79  ? -19.42100 -7.80300  -34.37600 1.000 11.50369 ? 78  ILE   D CG2   1 
ATOM   2065 C  CD1   . ILE   B 2 79  ? -19.33900 -10.74000 -33.22700 1.000 11.67387 ? 78  ILE   D CD1   1 
ATOM   2066 N  N     . TYR   B 2 80  ? -23.04400 -8.00400  -31.16100 1.000 11.61768 ? 79  TYR   D N     1 
ATOM   2067 C  CA    . TYR   B 2 80  ? -24.06500 -8.77700  -30.46600 1.000 12.84459 ? 79  TYR   D CA    1 
ATOM   2068 C  C     . TYR   B 2 80  ? -25.42000 -8.07000  -30.35400 1.000 17.64795 ? 79  TYR   D C     1 
ATOM   2069 O  O     . TYR   B 2 80  ? -26.29400 -8.55100  -29.62400 1.000 20.25829 ? 79  TYR   D O     1 
ATOM   2070 C  CB    . TYR   B 2 80  ? -23.53600 -9.25400  -29.10700 1.000 12.19170 ? 79  TYR   D CB    1 
ATOM   2071 C  CG    . TYR   B 2 80  ? -22.28900 -10.10900 -29.26800 1.000 11.13959 ? 79  TYR   D CG    1 
ATOM   2072 C  CD1   . TYR   B 2 80  ? -22.32700 -11.29300 -30.00500 1.000 11.48724 ? 79  TYR   D CD1   1 
ATOM   2073 C  CD2   . TYR   B 2 80  ? -21.07200 -9.72600  -28.70800 1.000 10.20488 ? 79  TYR   D CD2   1 
ATOM   2074 C  CE1   . TYR   B 2 80  ? -21.19500 -12.06600 -30.17300 1.000 11.41430 ? 79  TYR   D CE1   1 
ATOM   2075 C  CE2   . TYR   B 2 80  ? -19.93700 -10.50000 -28.86900 1.000 10.36092 ? 79  TYR   D CE2   1 
ATOM   2076 C  CZ    . TYR   B 2 80  ? -20.00400 -11.66800 -29.60800 1.000 10.76236 ? 79  TYR   D CZ    1 
ATOM   2077 O  OH    . TYR   B 2 80  ? -18.89800 -12.46300 -29.80200 1.000 10.99496 ? 79  TYR   D OH    1 
ATOM   2078 N  N     . GLY   B 2 81  ? -25.62700 -6.96700  -31.07800 1.000 17.39273 ? 80  GLY   D N     1 
ATOM   2079 C  CA    . GLY   B 2 81  ? -26.90100 -6.27000  -31.07500 1.000 19.56956 ? 80  GLY   D CA    1 
ATOM   2080 C  C     . GLY   B 2 81  ? -27.15100 -5.41000  -29.85900 1.000 19.65261 ? 80  GLY   D C     1 
ATOM   2081 O  O     . GLY   B 2 81  ? -28.21500 -4.78000  -29.77200 1.000 21.95569 ? 80  GLY   D O     1 
ATOM   2082 N  N     . GLU   B 2 82  ? -26.19900 -5.35600  -28.93100 1.000 19.76930 ? 81  GLU   D N     1 
ATOM   2083 C  CA    . GLU   B 2 82  ? -26.31300 -4.65800  -27.65800 1.000 22.13159 ? 81  GLU   D CA    1 
ATOM   2084 C  C     . GLU   B 2 82  ? -24.93500 -4.69100  -27.01600 1.000 18.49386 ? 81  GLU   D C     1 
ATOM   2085 O  O     . GLU   B 2 82  ? -24.09800 -5.52500  -27.37200 1.000 18.98861 ? 81  GLU   D O     1 
ATOM   2086 C  CB    . GLU   B 2 82  ? -27.31200 -5.36900  -26.74200 1.000 30.26058 ? 81  GLU   D CB    1 
ATOM   2087 C  CG    . GLU   B 2 82  ? -26.90100 -6.80600  -26.43400 1.000 37.45798 ? 81  GLU   D CG    1 
ATOM   2088 C  CD    . GLU   B 2 82  ? -27.95100 -7.58100  -25.66800 1.000 43.56801 ? 81  GLU   D CD    1 
ATOM   2089 O  OE1   . GLU   B 2 82  ? -29.07600 -7.06500  -25.50400 1.000 45.99623 ? 81  GLU   D OE1   1 
ATOM   2090 O  OE2   . GLU   B 2 82  ? -27.64900 -8.71200  -25.23100 1.000 45.20894 ? 81  GLU   D OE2   1 
ATOM   2091 N  N     . LYS   B 2 83  ? -24.70000 -3.77200  -26.07500 1.000 18.10921 ? 82  LYS   D N     1 
ATOM   2092 C  CA    . LYS   B 2 83  ? -23.52300 -3.87000  -25.22000 1.000 16.00937 ? 82  LYS   D CA    1 
ATOM   2093 C  C     . LYS   B 2 83  ? -23.50900 -5.24100  -24.57000 1.000 15.92925 ? 82  LYS   D C     1 
ATOM   2094 O  O     . LYS   B 2 83  ? -24.56300 -5.79700  -24.24600 1.000 19.75084 ? 82  LYS   D O     1 
ATOM   2095 C  CB    . LYS   B 2 83  ? -23.59300 -2.80000  -24.13300 1.000 18.52051 ? 82  LYS   D CB    1 
ATOM   2096 C  CG    . LYS   B 2 83  ? -23.39600 -1.38800  -24.65000 1.000 23.45052 ? 82  LYS   D CG    1 
ATOM   2097 C  CD    . LYS   B 2 83  ? -22.05900 -1.27600  -25.35700 1.000 28.63096 ? 82  LYS   D CD    1 
ATOM   2098 C  CE    . LYS   B 2 83  ? -21.57000 0.15600   -25.43000 1.000 32.04540 ? 82  LYS   D CE    1 
ATOM   2099 N  NZ    . LYS   B 2 83  ? -21.68800 0.71600   -26.80500 1.000 34.40958 ? 82  LYS   D NZ    1 
ATOM   2100 N  N     . PHE   B 2 84  ? -22.32100 -5.80500  -24.39200 1.000 12.42987 ? 83  PHE   D N     1 
ATOM   2101 C  CA    . PHE   B 2 84  ? -22.25200 -7.16600  -23.89400 1.000 11.75193 ? 83  PHE   D CA    1 
ATOM   2102 C  C     . PHE   B 2 84  ? -21.51600 -7.27500  -22.56600 1.000 10.53489 ? 83  PHE   D C     1 
ATOM   2103 O  O     . PHE   B 2 84  ? -20.75200 -6.39100  -22.16400 1.000 10.87215 ? 83  PHE   D O     1 
ATOM   2104 C  CB    . PHE   B 2 84  ? -21.77200 -8.19300  -24.94400 1.000 11.22113 ? 83  PHE   D CB    1 
ATOM   2105 C  CG    . PHE   B 2 84  ? -20.32700 -8.05000  -25.37400 1.000 10.50503 ? 83  PHE   D CG    1 
ATOM   2106 C  CD1   . PHE   B 2 84  ? -19.95000 -7.05900  -26.26700 1.000 10.70429 ? 83  PHE   D CD1   1 
ATOM   2107 C  CD2   . PHE   B 2 84  ? -19.36300 -8.95500  -24.94000 1.000 11.03956 ? 83  PHE   D CD2   1 
ATOM   2108 C  CE1   . PHE   B 2 84  ? -18.63800 -6.94700  -26.69800 1.000 10.46423 ? 83  PHE   D CE1   1 
ATOM   2109 C  CE2   . PHE   B 2 84  ? -18.05100 -8.85400  -25.36900 1.000 11.08468 ? 83  PHE   D CE2   1 
ATOM   2110 C  CZ    . PHE   B 2 84  ? -17.68200 -7.84700  -26.25000 1.000 11.09088 ? 83  PHE   D CZ    1 
ATOM   2111 N  N     A GLU   B 2 85  ? -21.76200 -8.39600  -21.89900 0.500 10.70170 ? 84  GLU   D N     1 
ATOM   2112 N  N     B GLU   B 2 85  ? -21.78400 -8.38500  -21.88100 0.500 11.56415 ? 84  GLU   D N     1 
ATOM   2113 C  CA    A GLU   B 2 85  ? -21.27900 -8.61800  -20.54700 0.500 10.97561 ? 84  GLU   D CA    1 
ATOM   2114 C  CA    B GLU   B 2 85  ? -21.26500 -8.62000  -20.54400 0.500 12.74970 ? 84  GLU   D CA    1 
ATOM   2115 C  C     A GLU   B 2 85  ? -19.76500 -8.79600  -20.52100 0.500 10.08992 ? 84  GLU   D C     1 
ATOM   2116 C  C     B GLU   B 2 85  ? -19.74300 -8.70000  -20.55100 0.500 11.13192 ? 84  GLU   D C     1 
ATOM   2117 O  O     A GLU   B 2 85  ? -19.15000 -9.25200  -21.49100 0.500 10.73696 ? 84  GLU   D O     1 
ATOM   2118 O  O     B GLU   B 2 85  ? -19.10500 -8.99800  -21.56700 0.500 12.23217 ? 84  GLU   D O     1 
ATOM   2119 C  CB    A GLU   B 2 85  ? -21.94500 -9.87100  -19.97800 0.500 12.95111 ? 84  GLU   D CB    1 
ATOM   2120 C  CB    B GLU   B 2 85  ? -21.80400 -9.94100  -19.98900 0.500 16.40161 ? 84  GLU   D CB    1 
ATOM   2121 C  CG    A GLU   B 2 85  ? -21.52000 -11.17700 -20.65000 0.500 15.72414 ? 84  GLU   D CG    1 
ATOM   2122 C  CG    B GLU   B 2 85  ? -23.28400 -9.93900  -19.64200 0.500 20.83552 ? 84  GLU   D CG    1 
ATOM   2123 C  CD    A GLU   B 2 85  ? -22.22700 -11.47200 -21.97900 0.500 18.09875 ? 84  GLU   D CD    1 
ATOM   2124 C  CD    B GLU   B 2 85  ? -23.75300 -11.26700 -19.06500 0.500 24.71349 ? 84  GLU   D CD    1 
ATOM   2125 O  OE1   A GLU   B 2 85  ? -23.09500 -10.68100 -22.42000 0.500 19.45890 ? 84  GLU   D OE1   1 
ATOM   2126 O  OE1   B GLU   B 2 85  ? -23.26600 -12.32400 -19.52000 0.500 26.20182 ? 84  GLU   D OE1   1 
ATOM   2127 O  OE2   A GLU   B 2 85  ? -21.90200 -12.51600 -22.58700 0.500 18.69768 ? 84  GLU   D OE2   1 
ATOM   2128 O  OE2   B GLU   B 2 85  ? -24.60300 -11.25100 -18.15100 0.500 26.76784 ? 84  GLU   D OE2   1 
ATOM   2129 N  N     . ASP   B 2 86  ? -19.16400 -8.42600  -19.38700 1.000 9.78941  ? 85  ASP   D N     1 
ATOM   2130 C  CA    . ASP   B 2 86  ? -17.77000 -8.76000  -19.14000 1.000 10.18872 ? 85  ASP   D CA    1 
ATOM   2131 C  C     . ASP   B 2 86  ? -17.65700 -10.27900 -19.11500 1.000 9.80829  ? 85  ASP   D C     1 
ATOM   2132 O  O     . ASP   B 2 86  ? -18.22800 -10.93700 -18.23800 1.000 11.69525 ? 85  ASP   D O     1 
ATOM   2133 C  CB    . ASP   B 2 86  ? -17.29900 -8.16100  -17.81800 1.000 9.93374  ? 85  ASP   D CB    1 
ATOM   2134 C  CG    . ASP   B 2 86  ? -17.30600 -6.64500  -17.82800 1.000 9.94798  ? 85  ASP   D CG    1 
ATOM   2135 O  OD1   . ASP   B 2 86  ? -16.81000 -6.05100  -18.81400 1.000 9.57463  ? 85  ASP   D OD1   1 
ATOM   2136 O  OD2   . ASP   B 2 86  ? -17.81000 -6.04100  -16.85300 1.000 10.82558 ? 85  ASP   D OD2   1 
ATOM   2137 N  N     . GLU   B 2 87  ? -16.94300 -10.83800 -20.09100 1.000 9.42867  ? 86  GLU   D N     1 
ATOM   2138 C  CA    . GLU   B 2 87  ? -16.94800 -12.28300 -20.28900 1.000 9.50303  ? 86  GLU   D CA    1 
ATOM   2139 C  C     . GLU   B 2 87  ? -16.27200 -13.00200 -19.12400 1.000 9.84751  ? 86  GLU   D C     1 
ATOM   2140 O  O     . GLU   B 2 87  ? -16.83000 -13.94900 -18.55400 1.000 10.80855 ? 86  GLU   D O     1 
ATOM   2141 C  CB    . GLU   B 2 87  ? -16.26900 -12.59400 -21.62000 1.000 9.38354  ? 86  GLU   D CB    1 
ATOM   2142 C  CG    . GLU   B 2 87  ? -16.32300 -14.04900 -22.01100 1.000 10.33478 ? 86  GLU   D CG    1 
ATOM   2143 C  CD    . GLU   B 2 87  ? -15.83100 -14.30100 -23.42700 1.000 10.22751 ? 86  GLU   D CD    1 
ATOM   2144 O  OE1   . GLU   B 2 87  ? -15.26600 -13.37200 -24.05300 1.000 9.91595  ? 86  GLU   D OE1   1 
ATOM   2145 O  OE2   . GLU   B 2 87  ? -16.02100 -15.43300 -23.92400 1.000 11.05669 ? 86  GLU   D OE2   1 
ATOM   2146 N  N     . ASN   B 2 88  ? -15.07300 -12.56400 -18.75800 1.000 9.38014  ? 87  ASN   D N     1 
ATOM   2147 C  CA    . ASN   B 2 88  ? -14.36300 -13.02700 -17.57200 1.000 9.81954  ? 87  ASN   D CA    1 
ATOM   2148 C  C     . ASN   B 2 88  ? -13.19300 -12.07800 -17.35800 1.000 9.28078  ? 87  ASN   D C     1 
ATOM   2149 O  O     . ASN   B 2 88  ? -12.86800 -11.25900 -18.22600 1.000 9.75160  ? 87  ASN   D O     1 
ATOM   2150 C  CB    . ASN   B 2 88  ? -13.88800 -14.48300 -17.68900 1.000 9.77793  ? 87  ASN   D CB    1 
ATOM   2151 C  CG    . ASN   B 2 88  ? -12.89400 -14.68600 -18.80500 1.000 9.95437  ? 87  ASN   D CG    1 
ATOM   2152 O  OD1   . ASN   B 2 88  ? -11.80300 -14.10400 -18.80200 1.000 9.69506  ? 87  ASN   D OD1   1 
ATOM   2153 N  ND2   . ASN   B 2 88  ? -13.24800 -15.52900 -19.75900 1.000 10.61448 ? 87  ASN   D ND2   1 
ATOM   2154 N  N     . PHE   B 2 89  ? -12.56900 -12.19400 -16.19000 1.000 9.53595  ? 88  PHE   D N     1 
ATOM   2155 C  CA    . PHE   B 2 89  ? -11.37100 -11.43300 -15.85600 1.000 9.06556  ? 88  PHE   D CA    1 
ATOM   2156 C  C     . PHE   B 2 89  ? -10.18700 -12.36000 -15.61100 1.000 9.31378  ? 88  PHE   D C     1 
ATOM   2157 O  O     . PHE   B 2 89  ? -9.34300  -12.11600 -14.74700 1.000 9.93944  ? 88  PHE   D O     1 
ATOM   2158 C  CB    . PHE   B 2 89  ? -11.62200 -10.48000 -14.68800 1.000 10.25334 ? 88  PHE   D CB    1 
ATOM   2159 C  CG    . PHE   B 2 89  ? -12.65700 -9.44000  -14.99100 1.000 9.77273  ? 88  PHE   D CG    1 
ATOM   2160 C  CD1   . PHE   B 2 89  ? -12.37500 -8.40500  -15.87600 1.000 10.05978 ? 88  PHE   D CD1   1 
ATOM   2161 C  CD2   . PHE   B 2 89  ? -13.91200 -9.49900  -14.41700 1.000 10.51835 ? 88  PHE   D CD2   1 
ATOM   2162 C  CE1   . PHE   B 2 89  ? -13.32000 -7.44700  -16.16900 1.000 10.37548 ? 88  PHE   D CE1   1 
ATOM   2163 C  CE2   . PHE   B 2 89  ? -14.86200 -8.53100  -14.70500 1.000 10.98321 ? 88  PHE   D CE2   1 
ATOM   2164 C  CZ    . PHE   B 2 89  ? -14.56200 -7.50700  -15.58600 1.000 10.62592 ? 88  PHE   D CZ    1 
ATOM   2165 N  N     . ILE   B 2 90  ? -10.09800 -13.43400 -16.39800 1.000 9.28396  ? 89  ILE   D N     1 
ATOM   2166 C  CA    . ILE   B 2 90  ? -8.99200  -14.37500 -16.23600 1.000 9.76437  ? 89  ILE   D CA    1 
ATOM   2167 C  C     . ILE   B 2 90  ? -7.65400  -13.66900 -16.41100 1.000 9.15848  ? 89  ILE   D C     1 
ATOM   2168 O  O     . ILE   B 2 90  ? -6.73600  -13.83200 -15.59800 1.000 10.13372 ? 89  ILE   D O     1 
ATOM   2169 C  CB    . ILE   B 2 90  ? -9.13400  -15.55100 -17.21900 1.000 10.56944 ? 89  ILE   D CB    1 
ATOM   2170 C  CG1   . ILE   B 2 90  ? -10.33000 -16.42700 -16.84100 1.000 10.60903 ? 89  ILE   D CG1   1 
ATOM   2171 C  CG2   . ILE   B 2 90  ? -7.84300  -16.36700 -17.27000 1.000 11.74382 ? 89  ILE   D CG2   1 
ATOM   2172 C  CD1   . ILE   B 2 90  ? -10.74200 -17.39300 -17.93600 1.000 12.54814 ? 89  ILE   D CD1   1 
ATOM   2173 N  N     . LEU   B 2 91  ? -7.52700  -12.87700 -17.47300 1.000 9.41671  ? 90  LEU   D N     1 
ATOM   2174 C  CA    . LEU   B 2 91  ? -6.25600  -12.30600 -17.89800 1.000 9.56091  ? 90  LEU   D CA    1 
ATOM   2175 C  C     . LEU   B 2 91  ? -6.07000  -10.90100 -17.33400 1.000 9.96856  ? 90  LEU   D C     1 
ATOM   2176 O  O     . LEU   B 2 91  ? -7.03200  -10.16000 -17.11400 1.000 10.69540 ? 90  LEU   D O     1 
ATOM   2177 C  CB    . LEU   B 2 91  ? -6.16000  -12.28000 -19.42600 1.000 10.42831 ? 90  LEU   D CB    1 
ATOM   2178 C  CG    . LEU   B 2 91  ? -6.21800  -13.66300 -20.07700 1.000 11.27315 ? 90  LEU   D CG    1 
ATOM   2179 C  CD1   . LEU   B 2 91  ? -6.28100  -13.49800 -21.58100 1.000 12.54518 ? 90  LEU   D CD1   1 
ATOM   2180 C  CD2   . LEU   B 2 91  ? -5.01300  -14.49700 -19.66400 1.000 13.52751 ? 90  LEU   D CD2   1 
ATOM   2181 N  N     . LYS   B 2 92  ? -4.80900  -10.53600 -17.12400 1.000 10.47912 ? 91  LYS   D N     1 
ATOM   2182 C  CA    . LYS   B 2 92  ? -4.45100  -9.28200  -16.48200 1.000 10.74920 ? 91  LYS   D CA    1 
ATOM   2183 C  C     . LYS   B 2 92  ? -3.68600  -8.36400  -17.42900 1.000 9.69776  ? 91  LYS   D C     1 
ATOM   2184 O  O     . LYS   B 2 92  ? -3.17100  -8.78000  -18.47600 1.000 10.32274 ? 91  LYS   D O     1 
ATOM   2185 C  CB    . LYS   B 2 92  ? -3.59100  -9.52700  -15.23300 1.000 13.12721 ? 91  LYS   D CB    1 
ATOM   2186 C  CG    . LYS   B 2 92  ? -4.13700  -10.57700 -14.29500 1.000 17.24709 ? 91  LYS   D CG    1 
ATOM   2187 C  CD    . LYS   B 2 92  ? -5.53200  -10.26000 -13.84200 1.000 21.73084 ? 91  LYS   D CD    1 
ATOM   2188 C  CE    . LYS   B 2 92  ? -6.03900  -11.36100 -12.93700 1.000 23.60858 ? 91  LYS   D CE    1 
ATOM   2189 N  NZ    . LYS   B 2 92  ? -7.50600  -11.26400 -12.75900 1.000 22.09282 ? 91  LYS   D NZ    1 
ATOM   2190 N  N     . HIS   B 2 93  ? -3.61000  -7.09300  -17.02400 1.000 9.97075  ? 92  HIS   D N     1 
ATOM   2191 C  CA    . HIS   B 2 93  ? -2.89400  -6.06200  -17.77800 1.000 9.97273  ? 92  HIS   D CA    1 
ATOM   2192 C  C     . HIS   B 2 93  ? -1.43200  -6.12100  -17.34600 1.000 10.75730 ? 92  HIS   D C     1 
ATOM   2193 O  O     . HIS   B 2 93  ? -0.97500  -5.38200  -16.47300 1.000 13.34823 ? 92  HIS   D O     1 
ATOM   2194 C  CB    . HIS   B 2 93  ? -3.50200  -4.68500  -17.51200 1.000 10.41807 ? 92  HIS   D CB    1 
ATOM   2195 C  CG    . HIS   B 2 93  ? -4.95400  -4.57100  -17.87600 1.000 8.83280  ? 92  HIS   D CG    1 
ATOM   2196 N  ND1   . HIS   B 2 93  ? -5.96600  -5.03000  -17.05800 1.000 8.68323  ? 92  HIS   D ND1   1 
ATOM   2197 C  CD2   . HIS   B 2 93  ? -5.56400  -4.04700  -18.96800 1.000 8.98924  ? 92  HIS   D CD2   1 
ATOM   2198 C  CE1   . HIS   B 2 93  ? -7.13400  -4.80600  -17.63800 1.000 8.50890  ? 92  HIS   D CE1   1 
ATOM   2199 N  NE2   . HIS   B 2 93  ? -6.92000  -4.20500  -18.79500 1.000 8.37248  ? 92  HIS   D NE2   1 
ATOM   2200 N  N     . THR   B 2 94  ? -0.68700  -7.04100  -17.96500 1.000 11.02618 ? 93  THR   D N     1 
ATOM   2201 C  CA    . THR   B 2 94  ? 0.62500   -7.43800  -17.46700 1.000 12.24580 ? 93  THR   D CA    1 
ATOM   2202 C  C     . THR   B 2 94  ? 1.77700   -6.60200  -18.00600 1.000 11.83983 ? 93  THR   D C     1 
ATOM   2203 O  O     . THR   B 2 94  ? 2.87000   -6.65800  -17.43700 1.000 14.36696 ? 93  THR   D O     1 
ATOM   2204 C  CB    . THR   B 2 94  ? 0.89800   -8.91000  -17.80000 1.000 13.51703 ? 93  THR   D CB    1 
ATOM   2205 O  OG1   . THR   B 2 94  ? 0.73300   -9.11800  -19.20800 1.000 15.10473 ? 93  THR   D OG1   1 
ATOM   2206 C  CG2   . THR   B 2 94  ? -0.04500  -9.82400  -17.03200 1.000 15.27312 ? 93  THR   D CG2   1 
ATOM   2207 N  N     . GLY   B 2 95  ? 1.58400   -5.85100  -19.08700 1.000 11.45945 ? 94  GLY   D N     1 
ATOM   2208 C  CA    . GLY   B 2 95  ? 2.68100   -5.13300  -19.69700 1.000 11.72867 ? 94  GLY   D CA    1 
ATOM   2209 C  C     . GLY   B 2 95  ? 2.32500   -4.54400  -21.04300 1.000 11.18044 ? 94  GLY   D C     1 
ATOM   2210 O  O     . GLY   B 2 95  ? 1.17400   -4.60100  -21.48900 1.000 11.51338 ? 94  GLY   D O     1 
ATOM   2211 N  N     . PRO   B 2 96  ? 3.31800   -3.95600  -21.71500 1.000 11.81250 ? 95  PRO   D N     1 
ATOM   2212 C  CA    . PRO   B 2 96  ? 3.08200   -3.39100  -23.05000 1.000 11.54376 ? 95  PRO   D CA    1 
ATOM   2213 C  C     . PRO   B 2 96  ? 2.50100   -4.42000  -24.00800 1.000 10.95045 ? 95  PRO   D C     1 
ATOM   2214 O  O     . PRO   B 2 96  ? 2.85800   -5.60200  -23.97800 1.000 13.01659 ? 95  PRO   D O     1 
ATOM   2215 C  CB    . PRO   B 2 96  ? 4.48100   -2.95200  -23.50300 1.000 13.87471 ? 95  PRO   D CB    1 
ATOM   2216 C  CG    . PRO   B 2 96  ? 5.26500   -2.79900  -22.24100 1.000 14.62742 ? 95  PRO   D CG    1 
ATOM   2217 C  CD    . PRO   B 2 96  ? 4.72400   -3.83600  -21.29800 1.000 13.26352 ? 95  PRO   D CD    1 
ATOM   2218 N  N     . GLY   B 2 97  ? 1.60100   -3.95200  -24.86800 1.000 10.39930 ? 96  GLY   D N     1 
ATOM   2219 C  CA    . GLY   B 2 97  ? 1.02800   -4.76700  -25.91500 1.000 10.38038 ? 96  GLY   D CA    1 
ATOM   2220 C  C     . GLY   B 2 97  ? -0.30700  -5.39200  -25.57800 1.000 9.80179  ? 96  GLY   D C     1 
ATOM   2221 O  O     . GLY   B 2 97  ? -0.99300  -5.87200  -26.48900 1.000 9.86216  ? 96  GLY   D O     1 
ATOM   2222 N  N     . ILE   B 2 98  ? -0.70200  -5.39400  -24.30300 1.000 10.02543 ? 97  ILE   D N     1 
ATOM   2223 C  CA    . ILE   B 2 98  ? -1.98100  -5.98400  -23.91800 1.000 9.03226  ? 97  ILE   D CA    1 
ATOM   2224 C  C     . ILE   B 2 98  ? -3.13500  -5.24500  -24.58100 1.000 8.27649  ? 97  ILE   D C     1 
ATOM   2225 O  O     . ILE   B 2 98  ? -3.18300  -4.00600  -24.60300 1.000 9.46617  ? 97  ILE   D O     1 
ATOM   2226 C  CB    . ILE   B 2 98  ? -2.12400  -5.97700  -22.38700 1.000 10.72514 ? 97  ILE   D CB    1 
ATOM   2227 C  CG1   . ILE   B 2 98  ? -1.17400  -6.99700  -21.74500 1.000 12.52413 ? 97  ILE   D CG1   1 
ATOM   2228 C  CG2   . ILE   B 2 98  ? -3.58100  -6.21800  -21.96600 1.000 12.07464 ? 97  ILE   D CG2   1 
ATOM   2229 C  CD1   . ILE   B 2 98  ? -1.53400  -8.44300  -22.01900 1.000 14.61119 ? 97  ILE   D CD1   1 
ATOM   2230 N  N     . LEU   B 2 99  ? -4.08700  -6.01300  -25.10000 1.000 8.20833  ? 98  LEU   D N     1 
ATOM   2231 C  CA    . LEU   B 2 99  ? -5.29600  -5.51200  -25.73500 1.000 8.16841  ? 98  LEU   D CA    1 
ATOM   2232 C  C     . LEU   B 2 99  ? -6.48000  -5.80000  -24.81500 1.000 7.57748  ? 98  LEU   D C     1 
ATOM   2233 O  O     . LEU   B 2 99  ? -6.67900  -6.94600  -24.38600 1.000 8.61164  ? 98  LEU   D O     1 
ATOM   2234 C  CB    . LEU   B 2 99  ? -5.46500  -6.23100  -27.07000 1.000 10.46413 ? 98  LEU   D CB    1 
ATOM   2235 C  CG    . LEU   B 2 99  ? -6.60500  -5.84900  -27.99500 1.000 12.06305 ? 98  LEU   D CG    1 
ATOM   2236 C  CD1   . LEU   B 2 99  ? -6.49400  -4.39800  -28.44200 1.000 12.67930 ? 98  LEU   D CD1   1 
ATOM   2237 C  CD2   . LEU   B 2 99  ? -6.59400  -6.77200  -29.20700 1.000 12.01649 ? 98  LEU   D CD2   1 
ATOM   2238 N  N     . SER   B 2 100 ? -7.24600  -4.75600  -24.48800 1.000 7.47124  ? 99  SER   D N     1 
ATOM   2239 C  CA    . SER   B 2 100 ? -8.26700  -4.83600  -23.45200 1.000 8.02848  ? 99  SER   D CA    1 
ATOM   2240 C  C     . SER   B 2 100 ? -9.45800  -3.96100  -23.83200 1.000 7.16557  ? 99  SER   D C     1 
ATOM   2241 O  O     . SER   B 2 100 ? -9.34400  -3.03300  -24.63900 1.000 7.87248  ? 99  SER   D O     1 
ATOM   2242 C  CB    . SER   B 2 100 ? -7.65900  -4.42200  -22.11000 1.000 8.29589  ? 99  SER   D CB    1 
ATOM   2243 O  OG    . SER   B 2 100 ? -8.60000  -4.54000  -21.07000 1.000 8.97920  ? 99  SER   D OG    1 
ATOM   2244 N  N     . MET   B 2 101 ? -10.61400 -4.26500  -23.24600 1.000 8.06448  ? 100 MET   D N     1 
ATOM   2245 C  CA    . MET   B 2 101 ? -11.84600 -3.55400  -23.58500 1.000 7.66749  ? 100 MET   D CA    1 
ATOM   2246 C  C     . MET   B 2 101 ? -12.02100 -2.27600  -22.77400 1.000 7.29982  ? 100 MET   D C     1 
ATOM   2247 O  O     . MET   B 2 101 ? -11.90400 -2.28600  -21.54500 1.000 8.13382  ? 100 MET   D O     1 
ATOM   2248 C  CB    . MET   B 2 101 ? -13.07500 -4.43600  -23.37200 1.000 8.20734  ? 100 MET   D CB    1 
ATOM   2249 C  CG    . MET   B 2 101 ? -13.20600 -5.58900  -24.35300 1.000 9.05264  ? 100 MET   D CG    1 
ATOM   2250 S  SD    . MET   B 2 101 ? -13.24300 -5.08400  -26.08000 1.000 9.02562  ? 100 MET   D SD    1 
ATOM   2251 C  CE    . MET   B 2 101 ? -14.90800 -4.40100  -26.22400 1.000 10.77261 ? 100 MET   D CE    1 
ATOM   2252 N  N     . ALA   B 2 102 ? -12.33200 -1.18600  -23.46900 1.000 7.34220  ? 101 ALA   D N     1 
ATOM   2253 C  CA    . ALA   B 2 102 ? -12.82800 0.01200   -22.81500 1.000 7.82364  ? 101 ALA   D CA    1 
ATOM   2254 C  C     . ALA   B 2 102 ? -14.29800 -0.19600  -22.44900 1.000 7.52930  ? 101 ALA   D C     1 
ATOM   2255 O  O     . ALA   B 2 102 ? -14.98500 -1.03300  -23.04000 1.000 8.77065  ? 101 ALA   D O     1 
ATOM   2256 C  CB    . ALA   B 2 102 ? -12.67600 1.21600   -23.74300 1.000 8.78327  ? 101 ALA   D CB    1 
ATOM   2257 N  N     . ASN   B 2 103 ? -14.78300 0.55500   -21.45800 1.000 7.81158  ? 102 ASN   D N     1 
ATOM   2258 C  CA    . ASN   B 2 103 ? -16.17900 0.40000   -21.05900 1.000 8.20170  ? 102 ASN   D CA    1 
ATOM   2259 C  C     . ASN   B 2 103 ? -16.63100 1.61000   -20.25000 1.000 8.58952  ? 102 ASN   D C     1 
ATOM   2260 O  O     . ASN   B 2 103 ? -15.84200 2.50000   -19.91900 1.000 9.28828  ? 102 ASN   D O     1 
ATOM   2261 C  CB    . ASN   B 2 103 ? -16.40400 -0.92200  -20.30400 1.000 8.26780  ? 102 ASN   D CB    1 
ATOM   2262 C  CG    . ASN   B 2 103 ? -15.66900 -0.97500  -18.98200 1.000 8.94868  ? 102 ASN   D CG    1 
ATOM   2263 O  OD1   . ASN   B 2 103 ? -15.77500 -0.04900  -18.17800 1.000 9.69209  ? 102 ASN   D OD1   1 
ATOM   2264 N  ND2   . ASN   B 2 103 ? -14.92700 -2.05800  -18.74400 1.000 9.62648  ? 102 ASN   D ND2   1 
ATOM   2265 N  N     . ALA   B 2 104 ? -17.92900 1.62700   -19.94700 1.000 9.30124  ? 103 ALA   D N     1 
ATOM   2266 C  CA    . ALA   B 2 104 ? -18.55300 2.66600   -19.13900 1.000 10.64258 ? 103 ALA   D CA    1 
ATOM   2267 C  C     . ALA   B 2 104 ? -19.08900 2.08400   -17.83700 1.000 12.26622 ? 103 ALA   D C     1 
ATOM   2268 O  O     . ALA   B 2 104 ? -20.11700 2.53000   -17.32400 1.000 15.38516 ? 103 ALA   D O     1 
ATOM   2269 C  CB    . ALA   B 2 104 ? -19.66400 3.37500   -19.91800 1.000 11.95221 ? 103 ALA   D CB    1 
ATOM   2270 N  N     . GLY   B 2 105 ? -18.39700 1.08600   -17.29300 1.000 10.87025 ? 104 GLY   D N     1 
ATOM   2271 C  CA    . GLY   B 2 105 ? -18.85000 0.39600   -16.10800 1.000 11.95179 ? 104 GLY   D CA    1 
ATOM   2272 C  C     . GLY   B 2 105 ? -19.09600 -1.07100  -16.40400 1.000 11.13461 ? 104 GLY   D C     1 
ATOM   2273 O  O     . GLY   B 2 105 ? -18.86100 -1.54600  -17.51900 1.000 10.26957 ? 104 GLY   D O     1 
ATOM   2274 N  N     . PRO   B 2 106 ? -19.57800 -1.82100  -15.41200 1.000 12.42413 ? 105 PRO   D N     1 
ATOM   2275 C  CA    . PRO   B 2 106 ? -19.74400 -3.27000  -15.59800 1.000 12.83155 ? 105 PRO   D CA    1 
ATOM   2276 C  C     . PRO   B 2 106 ? -20.68100 -3.60200  -16.75400 1.000 11.76300 ? 105 PRO   D C     1 
ATOM   2277 O  O     . PRO   B 2 106 ? -21.73200 -2.98200  -16.92500 1.000 12.45902 ? 105 PRO   D O     1 
ATOM   2278 C  CB    . PRO   B 2 106 ? -20.32500 -3.73000  -14.25500 1.000 14.98655 ? 105 PRO   D CB    1 
ATOM   2279 C  CG    . PRO   B 2 106 ? -19.83300 -2.71300  -13.27200 1.000 16.98994 ? 105 PRO   D CG    1 
ATOM   2280 C  CD    . PRO   B 2 106 ? -19.84000 -1.40600  -14.02000 1.000 14.80315 ? 105 PRO   D CD    1 
ATOM   2281 N  N     . ASN   B 2 107 ? -20.28100 -4.59500  -17.55300 1.000 11.28929 ? 106 ASN   D N     1 
ATOM   2282 C  CA    . ASN   B 2 107 ? -21.14700 -5.18800  -18.57700 1.000 11.36515 ? 106 ASN   D CA    1 
ATOM   2283 C  C     . ASN   B 2 107 ? -21.60500 -4.16600  -19.61800 1.000 11.00332 ? 106 ASN   D C     1 
ATOM   2284 O  O     . ASN   B 2 107 ? -22.76900 -4.14400  -20.02200 1.000 12.60856 ? 106 ASN   D O     1 
ATOM   2285 C  CB    . ASN   B 2 107 ? -22.32200 -5.93500  -17.94700 1.000 13.33878 ? 106 ASN   D CB    1 
ATOM   2286 C  CG    . ASN   B 2 107 ? -21.86000 -6.96900  -16.95500 1.000 13.60145 ? 106 ASN   D CG    1 
ATOM   2287 O  OD1   . ASN   B 2 107 ? -20.96900 -7.76900  -17.24900 1.000 12.95388 ? 106 ASN   D OD1   1 
ATOM   2288 N  ND2   . ASN   B 2 107 ? -22.42400 -6.93400  -15.75900 1.000 17.51815 ? 106 ASN   D ND2   1 
ATOM   2289 N  N     . THR   B 2 108 ? -20.67100 -3.32700  -20.07800 1.000 10.61431 ? 107 THR   D N     1 
ATOM   2290 C  CA    . THR   B 2 108 ? -20.95800 -2.31300  -21.09000 1.000 10.39728 ? 107 THR   D CA    1 
ATOM   2291 C  C     . THR   B 2 108 ? -19.98200 -2.38300  -22.26000 1.000 10.19088 ? 107 THR   D C     1 
ATOM   2292 O  O     . THR   B 2 108 ? -19.67800 -1.36600  -22.88000 1.000 12.08732 ? 107 THR   D O     1 
ATOM   2293 C  CB    . THR   B 2 108 ? -21.00900 -0.89800  -20.50000 1.000 10.65755 ? 107 THR   D CB    1 
ATOM   2294 O  OG1   . THR   B 2 108 ? -19.73400 -0.56000  -19.93400 1.000 10.15821 ? 107 THR   D OG1   1 
ATOM   2295 C  CG2   . THR   B 2 108 ? -22.10500 -0.77300  -19.44100 1.000 11.99090 ? 107 THR   D CG2   1 
ATOM   2296 N  N     . ASN   B 2 109 ? -19.50300 -3.57400  -22.59700 1.000 9.75760  ? 108 ASN   D N     1 
ATOM   2297 C  CA    . ASN   B 2 109 ? -18.57100 -3.70600  -23.71100 1.000 9.64391  ? 108 ASN   D CA    1 
ATOM   2298 C  C     . ASN   B 2 109 ? -19.26600 -3.44300  -25.03900 1.000 9.67635  ? 108 ASN   D C     1 
ATOM   2299 O  O     . ASN   B 2 109 ? -20.35300 -3.96400  -25.29800 1.000 10.74834 ? 108 ASN   D O     1 
ATOM   2300 C  CB    . ASN   B 2 109 ? -17.95900 -5.10300  -23.70900 1.000 9.98126  ? 108 ASN   D CB    1 
ATOM   2301 C  CG    . ASN   B 2 109 ? -17.15700 -5.35900  -22.46700 1.000 9.05802  ? 108 ASN   D CG    1 
ATOM   2302 O  OD1   . ASN   B 2 109 ? -16.06000 -4.82600  -22.31400 1.000 10.04595 ? 108 ASN   D OD1   1 
ATOM   2303 N  ND2   . ASN   B 2 109 ? -17.71200 -6.14700  -21.54500 1.000 9.78590  ? 108 ASN   D ND2   1 
ATOM   2304 N  N     . GLY   B 2 110 ? -18.62500 -2.64400  -25.88800 1.000 8.78069  ? 109 GLY   D N     1 
ATOM   2305 C  CA    . GLY   B 2 110 ? -19.11500 -2.36400  -27.22200 1.000 9.15290  ? 109 GLY   D CA    1 
ATOM   2306 C  C     . GLY   B 2 110 ? -18.05700 -2.71000  -28.24100 1.000 8.41095  ? 109 GLY   D C     1 
ATOM   2307 O  O     . GLY   B 2 110 ? -17.78300 -3.88700  -28.49900 1.000 9.73756  ? 109 GLY   D O     1 
ATOM   2308 N  N     . SER   B 2 111 ? -17.44000 -1.68600  -28.81800 1.000 8.17961  ? 110 SER   D N     1 
ATOM   2309 C  CA    . SER   B 2 111 ? -16.32000 -1.87900  -29.72500 1.000 7.91253  ? 110 SER   D CA    1 
ATOM   2310 C  C     . SER   B 2 111 ? -15.03100 -1.22300  -29.25900 1.000 7.70843  ? 110 SER   D C     1 
ATOM   2311 O  O     . SER   B 2 111 ? -13.96300 -1.60100  -29.74400 1.000 8.50312  ? 110 SER   D O     1 
ATOM   2312 C  CB    . SER   B 2 111 ? -16.66600 -1.35500  -31.12400 1.000 8.93076  ? 110 SER   D CB    1 
ATOM   2313 O  OG    . SER   B 2 111 ? -17.00800 0.01800   -31.06300 1.000 9.40738  ? 110 SER   D OG    1 
ATOM   2314 N  N     . GLN   B 2 112 ? -15.09100 -0.25900  -28.34600 1.000 7.76256  ? 111 GLN   D N     1 
ATOM   2315 C  CA    . GLN   B 2 112 ? -13.87900 0.46000   -27.98100 1.000 7.68926  ? 111 GLN   D CA    1 
ATOM   2316 C  C     . GLN   B 2 112 ? -12.92300 -0.43000  -27.19500 1.000 6.89672  ? 111 GLN   D C     1 
ATOM   2317 O  O     . GLN   B 2 112 ? -13.33300 -1.26900  -26.38500 1.000 8.05966  ? 111 GLN   D O     1 
ATOM   2318 C  CB    . GLN   B 2 112 ? -14.21200 1.71600   -27.18700 1.000 8.37086  ? 111 GLN   D CB    1 
ATOM   2319 C  CG    . GLN   B 2 112 ? -14.80400 2.82100   -28.04300 1.000 9.02562  ? 111 GLN   D CG    1 
ATOM   2320 C  CD    . GLN   B 2 112 ? -14.90600 4.10900   -27.27400 1.000 9.18289  ? 111 GLN   D CD    1 
ATOM   2321 O  OE1   . GLN   B 2 112 ? -13.93400 4.55200   -26.65000 1.000 9.33235  ? 111 GLN   D OE1   1 
ATOM   2322 N  NE2   . GLN   B 2 112 ? -16.09100 4.71600   -27.28300 1.000 10.19694 ? 111 GLN   D NE2   1 
ATOM   2323 N  N     . PHE   B 2 113 ? -11.63400 -0.22600  -27.43600 1.000 7.51186  ? 112 PHE   D N     1 
ATOM   2324 C  CA    . PHE   B 2 113 ? -10.58200 -1.06700  -26.89400 1.000 7.33691  ? 112 PHE   D CA    1 
ATOM   2325 C  C     . PHE   B 2 113 ? -9.38800  -0.16800  -26.61300 1.000 6.99427  ? 112 PHE   D C     1 
ATOM   2326 O  O     . PHE   B 2 113 ? -9.32700  0.98100   -27.06900 1.000 7.87485  ? 112 PHE   D O     1 
ATOM   2327 C  CB    . PHE   B 2 113 ? -10.18300 -2.13800  -27.91900 1.000 8.51713  ? 112 PHE   D CB    1 
ATOM   2328 C  CG    . PHE   B 2 113 ? -9.63900  -1.54800  -29.18900 1.000 8.39417  ? 112 PHE   D CG    1 
ATOM   2329 C  CD1   . PHE   B 2 113 ? -8.28800  -1.25400  -29.31100 1.000 9.01873  ? 112 PHE   D CD1   1 
ATOM   2330 C  CD2   . PHE   B 2 113 ? -10.49000 -1.21700  -30.23700 1.000 9.00693  ? 112 PHE   D CD2   1 
ATOM   2331 C  CE1   . PHE   B 2 113 ? -7.79300  -0.65300  -30.45400 1.000 10.43878 ? 112 PHE   D CE1   1 
ATOM   2332 C  CE2   . PHE   B 2 113 ? -9.99700  -0.61600  -31.39100 1.000 10.04863 ? 112 PHE   D CE2   1 
ATOM   2333 C  CZ    . PHE   B 2 113 ? -8.64600  -0.33400  -31.49800 1.000 10.33641 ? 112 PHE   D CZ    1 
ATOM   2334 N  N     . PHE   B 2 114 ? -8.40800  -0.71100  -25.90200 1.000 7.40776  ? 113 PHE   D N     1 
ATOM   2335 C  CA    . PHE   B 2 114 ? -7.14600  -0.00800  -25.74800 1.000 7.36831  ? 113 PHE   D CA    1 
ATOM   2336 C  C     . PHE   B 2 114 ? -5.97900  -0.97700  -25.84600 1.000 7.69015  ? 113 PHE   D C     1 
ATOM   2337 O  O     . PHE   B 2 114 ? -6.10000  -2.16700  -25.53300 1.000 8.03605  ? 113 PHE   D O     1 
ATOM   2338 C  CB    . PHE   B 2 114 ? -7.08200  0.85500   -24.47200 1.000 7.97554  ? 113 PHE   D CB    1 
ATOM   2339 C  CG    . PHE   B 2 114 ? -7.27000  0.09200   -23.18300 1.000 7.55092  ? 113 PHE   D CG    1 
ATOM   2340 C  CD1   . PHE   B 2 114 ? -8.53300  -0.29700  -22.76100 1.000 8.49677  ? 113 PHE   D CD1   1 
ATOM   2341 C  CD2   . PHE   B 2 114 ? -6.18300  -0.18900  -22.36600 1.000 8.26460  ? 113 PHE   D CD2   1 
ATOM   2342 C  CE1   . PHE   B 2 114 ? -8.70900  -0.98700  -21.55800 1.000 8.37258  ? 113 PHE   D CE1   1 
ATOM   2343 C  CE2   . PHE   B 2 114 ? -6.34300  -0.87100  -21.16800 1.000 8.38194  ? 113 PHE   D CE2   1 
ATOM   2344 C  CZ    . PHE   B 2 114 ? -7.61400  -1.27400  -20.75800 1.000 8.56086  ? 113 PHE   D CZ    1 
ATOM   2345 N  N     . ILE   B 2 115 ? -4.85000  -0.43500  -26.30100 1.000 7.70821  ? 114 ILE   D N     1 
ATOM   2346 C  CA    . ILE   B 2 115 ? -3.57900  -1.14300  -26.39300 1.000 8.85792  ? 114 ILE   D CA    1 
ATOM   2347 C  C     . ILE   B 2 115 ? -2.66100  -0.53900  -25.34300 1.000 8.93671  ? 114 ILE   D C     1 
ATOM   2348 O  O     . ILE   B 2 115 ? -2.30700  0.64300   -25.42800 1.000 9.02027  ? 114 ILE   D O     1 
ATOM   2349 C  CB    . ILE   B 2 115 ? -2.94200  -1.00200  -27.78700 1.000 9.59258  ? 114 ILE   D CB    1 
ATOM   2350 C  CG1   . ILE   B 2 115 ? -3.92400  -1.35800  -28.90900 1.000 10.33511 ? 114 ILE   D CG1   1 
ATOM   2351 C  CG2   . ILE   B 2 115 ? -1.66000  -1.83500  -27.87400 1.000 10.03885 ? 114 ILE   D CG2   1 
ATOM   2352 C  CD1   . ILE   B 2 115 ? -3.46600  -0.89800  -30.28400 1.000 11.70846 ? 114 ILE   D CD1   1 
ATOM   2353 N  N     . CYS   B 2 116 ? -2.26700  -1.34200  -24.36100 1.000 9.29325  ? 115 CYS   D N     1 
ATOM   2354 C  CA    . CYS   B 2 116 ? -1.38300  -0.85800  -23.31200 1.000 9.63586  ? 115 CYS   D CA    1 
ATOM   2355 C  C     . CYS   B 2 116 ? 0.02700   -0.65600  -23.84300 1.000 10.12382 ? 115 CYS   D C     1 
ATOM   2356 O  O     . CYS   B 2 116 ? 0.51000   -1.41600  -24.68400 1.000 10.30244 ? 115 CYS   D O     1 
ATOM   2357 C  CB    . CYS   B 2 116 ? -1.33500  -1.87500  -22.17900 1.000 10.67687 ? 115 CYS   D CB    1 
ATOM   2358 S  SG    . CYS   B 2 116 ? -2.91800  -2.13700  -21.39100 1.000 11.88456 ? 115 CYS   D SG    1 
ATOM   2359 N  N     . THR   B 2 117 ? 0.70000   0.36700   -23.32700 1.000 10.90088 ? 116 THR   D N     1 
ATOM   2360 C  CA    . THR   B 2 117 ? 2.11600   0.56500   -23.59600 1.000 11.42154 ? 116 THR   D CA    1 
ATOM   2361 C  C     . THR   B 2 117 ? 2.95000   0.40200   -22.33500 1.000 12.55289 ? 116 THR   D C     1 
ATOM   2362 O  O     . THR   B 2 117 ? 4.15300   0.68200   -22.35000 1.000 15.66417 ? 116 THR   D O     1 
ATOM   2363 C  CB    . THR   B 2 117 ? 2.35500   1.92500   -24.25200 1.000 12.83146 ? 116 THR   D CB    1 
ATOM   2364 O  OG1   . THR   B 2 117 ? 1.81600   2.94900   -23.41200 1.000 13.87854 ? 116 THR   D OG1   1 
ATOM   2365 C  CG2   . THR   B 2 117 ? 1.68600   1.97700   -25.62200 1.000 13.72410 ? 116 THR   D CG2   1 
ATOM   2366 N  N     . ALA   B 2 118 ? 2.33400   -0.06800  -21.25600 1.000 12.24087 ? 117 ALA   D N     1 
ATOM   2367 C  CA    . ALA   B 2 118 ? 2.98000   -0.33100  -19.97900 1.000 12.65734 ? 117 ALA   D CA    1 
ATOM   2368 C  C     . ALA   B 2 118 ? 2.07700   -1.28800  -19.21200 1.000 11.52467 ? 117 ALA   D C     1 
ATOM   2369 O  O     . ALA   B 2 118 ? 0.94200   -1.55200  -19.61200 1.000 11.83269 ? 117 ALA   D O     1 
ATOM   2370 C  CB    . ALA   B 2 118 ? 3.19100   0.96500   -19.18900 1.000 15.05858 ? 117 ALA   D CB    1 
ATOM   2371 N  N     . LYS   B 2 119 ? 2.59100   -1.81100  -18.10600 1.000 12.07959 ? 118 LYS   D N     1 
ATOM   2372 C  CA    . LYS   B 2 119 ? 1.74300   -2.55600  -17.18300 1.000 12.25675 ? 118 LYS   D CA    1 
ATOM   2373 C  C     . LYS   B 2 119 ? 0.72200   -1.60200  -16.57200 1.000 12.08980 ? 118 LYS   D C     1 
ATOM   2374 O  O     . LYS   B 2 119 ? 1.08200   -0.52200  -16.10000 1.000 13.68911 ? 118 LYS   D O     1 
ATOM   2375 C  CB    . LYS   B 2 119 ? 2.61600   -3.17000  -16.08800 1.000 14.66729 ? 118 LYS   D CB    1 
ATOM   2376 C  CG    . LYS   B 2 119 ? 1.88000   -4.02600  -15.06200 1.000 15.24723 ? 118 LYS   D CG    1 
ATOM   2377 C  CD    . LYS   B 2 119 ? 2.85800   -4.61300  -14.04500 1.000 19.36094 ? 118 LYS   D CD    1 
ATOM   2378 C  CE    . LYS   B 2 119 ? 2.13900   -5.41700  -12.97500 1.000 22.83389 ? 118 LYS   D CE    1 
ATOM   2379 N  NZ    . LYS   B 2 119 ? 3.11200   -5.97300  -11.98900 1.000 26.05246 ? 118 LYS   D NZ    1 
ATOM   2380 N  N     . THR   B 2 120 ? -0.56200  -1.97900  -16.59500 1.000 11.45562 ? 119 THR   D N     1 
ATOM   2381 C  CA    . THR   B 2 120 ? -1.64000  -1.13600  -16.05400 1.000 12.18266 ? 119 THR   D CA    1 
ATOM   2382 C  C     . THR   B 2 120 ? -2.49200  -1.96600  -15.08800 1.000 11.24563 ? 119 THR   D C     1 
ATOM   2383 O  O     . THR   B 2 120 ? -3.68100  -2.20100  -15.32200 1.000 10.69998 ? 119 THR   D O     1 
ATOM   2384 C  CB    . THR   B 2 120 ? -2.48900  -0.50400  -17.16500 1.000 11.85470 ? 119 THR   D CB    1 
ATOM   2385 O  OG1   . THR   B 2 120 ? -3.10100  -1.53600  -17.95200 1.000 11.35850 ? 119 THR   D OG1   1 
ATOM   2386 C  CG2   . THR   B 2 120 ? -1.64300  0.37800   -18.06400 1.000 13.65461 ? 119 THR   D CG2   1 
ATOM   2387 N  N     . GLU   B 2 121 ? -1.87500  -2.37000  -13.97500 1.000 12.86238 ? 120 GLU   D N     1 
ATOM   2388 C  CA    . GLU   B 2 121 ? -2.49500  -3.33400  -13.07200 1.000 14.07075 ? 120 GLU   D CA    1 
ATOM   2389 C  C     . GLU   B 2 121 ? -3.78800  -2.81400  -12.45300 1.000 12.71023 ? 120 GLU   D C     1 
ATOM   2390 O  O     . GLU   B 2 121 ? -4.69100  -3.61000  -12.15900 1.000 12.63993 ? 120 GLU   D O     1 
ATOM   2391 C  CB    . GLU   B 2 121 ? -1.50200  -3.74100  -11.98200 1.000 16.34286 ? 120 GLU   D CB    1 
ATOM   2392 C  CG    . GLU   B 2 121 ? -2.08300  -4.72500  -10.97900 1.000 19.70383 ? 120 GLU   D CG    1 
ATOM   2393 C  CD    . GLU   B 2 121 ? -1.06000  -5.28100  -10.01000 1.000 24.94123 ? 120 GLU   D CD    1 
ATOM   2394 O  OE1   . GLU   B 2 121 ? 0.12400   -4.88600  -10.08600 1.000 26.59820 ? 120 GLU   D OE1   1 
ATOM   2395 O  OE2   . GLU   B 2 121 ? -1.44600  -6.12000  -9.17000  1.000 27.36171 ? 120 GLU   D OE2   1 
ATOM   2396 N  N     . TRP   B 2 122 ? -3.90700  -1.49400  -12.25300 1.000 12.98474 ? 121 TRP   D N     1 
ATOM   2397 C  CA    . TRP   B 2 122 ? -5.09500  -0.94900  -11.60200 1.000 13.38488 ? 121 TRP   D CA    1 
ATOM   2398 C  C     . TRP   B 2 122 ? -6.35900  -1.19000  -12.41200 1.000 11.21118 ? 121 TRP   D C     1 
ATOM   2399 O  O     . TRP   B 2 122 ? -7.46000  -1.05600  -11.87000 1.000 13.71389 ? 121 TRP   D O     1 
ATOM   2400 C  CB    . TRP   B 2 122 ? -4.91800  0.54800   -11.27600 1.000 14.37604 ? 121 TRP   D CB    1 
ATOM   2401 C  CG    . TRP   B 2 122 ? -5.44100  1.54100   -12.30800 1.000 15.02907 ? 121 TRP   D CG    1 
ATOM   2402 C  CD1   . TRP   B 2 122 ? -6.66200  2.16100   -12.30600 1.000 16.18097 ? 121 TRP   D CD1   1 
ATOM   2403 C  CD2   . TRP   B 2 122 ? -4.74300  2.04300   -13.45600 1.000 13.73606 ? 121 TRP   D CD2   1 
ATOM   2404 N  NE1   . TRP   B 2 122 ? -6.77000  3.00600   -13.38600 1.000 16.19893 ? 121 TRP   D NE1   1 
ATOM   2405 C  CE2   . TRP   B 2 122 ? -5.60500  2.95400   -14.10500 1.000 14.72225 ? 121 TRP   D CE2   1 
ATOM   2406 C  CE3   . TRP   B 2 122 ? -3.46800  1.82300   -13.99200 1.000 13.65807 ? 121 TRP   D CE3   1 
ATOM   2407 C  CZ2   . TRP   B 2 122 ? -5.24000  3.62500   -15.26500 1.000 13.83261 ? 121 TRP   D CZ2   1 
ATOM   2408 C  CZ3   . TRP   B 2 122 ? -3.11100  2.49200   -15.15300 1.000 14.44421 ? 121 TRP   D CZ3   1 
ATOM   2409 C  CH2   . TRP   B 2 122 ? -3.98900  3.38300   -15.77100 1.000 13.13770 ? 121 TRP   D CH2   1 
ATOM   2410 N  N     . LEU   B 2 123 ? -6.22900  -1.54000  -13.69100 1.000 10.22032 ? 122 LEU   D N     1 
ATOM   2411 C  CA    . LEU   B 2 123 ? -7.37900  -1.84900  -14.52900 1.000 9.61884  ? 122 LEU   D CA    1 
ATOM   2412 C  C     . LEU   B 2 123 ? -7.84200  -3.29900  -14.40600 1.000 9.39030  ? 122 LEU   D C     1 
ATOM   2413 O  O     . LEU   B 2 123 ? -8.92900  -3.62900  -14.90500 1.000 9.56546  ? 122 LEU   D O     1 
ATOM   2414 C  CB    . LEU   B 2 123 ? -7.06200  -1.50600  -15.99300 1.000 10.05044 ? 122 LEU   D CB    1 
ATOM   2415 C  CG    . LEU   B 2 123 ? -6.72300  -0.02800  -16.24700 1.000 10.39974 ? 122 LEU   D CG    1 
ATOM   2416 C  CD1   . LEU   B 2 123 ? -6.27700  0.20100   -17.68400 1.000 10.87099 ? 122 LEU   D CD1   1 
ATOM   2417 C  CD2   . LEU   B 2 123 ? -7.91400  0.85800   -15.92000 1.000 11.93314 ? 122 LEU   D CD2   1 
ATOM   2418 N  N     . ASP   B 2 124 ? -7.05100  -4.16600  -13.76300 1.000 9.39863  ? 123 ASP   D N     1 
ATOM   2419 C  CA    . ASP   B 2 124 ? -7.40600  -5.57800  -13.64300 1.000 10.13828 ? 123 ASP   D CA    1 
ATOM   2420 C  C     . ASP   B 2 124 ? -8.74800  -5.73200  -12.94000 1.000 9.53187  ? 123 ASP   D C     1 
ATOM   2421 O  O     . ASP   B 2 124 ? -9.01400  -5.08700  -11.92500 1.000 10.25430 ? 123 ASP   D O     1 
ATOM   2422 C  CB    . ASP   B 2 124 ? -6.35300  -6.32200  -12.81600 1.000 10.43101 ? 123 ASP   D CB    1 
ATOM   2423 C  CG    . ASP   B 2 124 ? -5.02800  -6.49600  -13.54000 1.000 10.71543 ? 123 ASP   D CG    1 
ATOM   2424 O  OD1   . ASP   B 2 124 ? -4.93000  -6.18600  -14.74600 1.000 10.64560 ? 123 ASP   D OD1   1 
ATOM   2425 O  OD2   . ASP   B 2 124 ? -4.06100  -6.95400  -12.89000 1.000 11.83933 ? 123 ASP   D OD2   1 
ATOM   2426 N  N     . GLY   B 2 125 ? -9.58900  -6.61500  -13.47200 1.000 9.33187  ? 124 GLY   D N     1 
ATOM   2427 C  CA    . GLY   B 2 125 ? -10.87100 -6.89100  -12.85900 1.000 9.59119  ? 124 GLY   D CA    1 
ATOM   2428 C  C     . GLY   B 2 125 ? -11.97400 -5.93300  -13.23700 1.000 8.60964  ? 124 GLY   D C     1 
ATOM   2429 O  O     . GLY   B 2 125 ? -13.12700 -6.15500  -12.84300 1.000 9.80942  ? 124 GLY   D O     1 
ATOM   2430 N  N     . LYS   B 2 126 ? -11.66700 -4.87100  -13.98400 1.000 9.18928  ? 125 LYS   D N     1 
ATOM   2431 C  CA    . LYS   B 2 126 ? -12.68800 -3.98300  -14.51900 1.000 10.23402 ? 125 LYS   D CA    1 
ATOM   2432 C  C     . LYS   B 2 126 ? -12.70400 -3.90900  -16.03500 1.000 8.82131  ? 125 LYS   D C     1 
ATOM   2433 O  O     . LYS   B 2 126 ? -13.73800 -3.54600  -16.60100 1.000 10.19395 ? 125 LYS   D O     1 
ATOM   2434 C  CB    . LYS   B 2 126 ? -12.57900 -2.56900  -13.92000 1.000 14.98815 ? 125 LYS   D CB    1 
ATOM   2435 C  CG    . LYS   B 2 126 ? -13.18700 -2.49100  -12.52000 1.000 20.01419 ? 125 LYS   D CG    1 
ATOM   2436 C  CD    . LYS   B 2 126 ? -13.38400 -1.06400  -12.03600 1.000 23.87550 ? 125 LYS   D CD    1 
ATOM   2437 C  CE    . LYS   B 2 126 ? -14.03700 -1.03000  -10.66200 1.000 28.17445 ? 125 LYS   D CE    1 
ATOM   2438 N  NZ    . LYS   B 2 126 ? -15.38500 -1.67200  -10.66400 1.000 31.55430 ? 125 LYS   D NZ    1 
ATOM   2439 N  N     . HIS   B 2 127 ? -11.61000 -4.26500  -16.70200 1.000 7.87055  ? 126 HIS   D N     1 
ATOM   2440 C  CA    . HIS   B 2 127 ? -11.53100 -4.28300  -18.15600 1.000 7.80812  ? 126 HIS   D CA    1 
ATOM   2441 C  C     . HIS   B 2 127 ? -11.11800 -5.67300  -18.60500 1.000 8.00939  ? 126 HIS   D C     1 
ATOM   2442 O  O     . HIS   B 2 127 ? -10.15900 -6.23600  -18.07200 1.000 8.58369  ? 126 HIS   D O     1 
ATOM   2443 C  CB    . HIS   B 2 127 ? -10.54600 -3.22300  -18.64900 1.000 8.89574  ? 126 HIS   D CB    1 
ATOM   2444 C  CG    . HIS   B 2 127 ? -10.94800 -1.85400  -18.22000 1.000 8.56878  ? 126 HIS   D CG    1 
ATOM   2445 N  ND1   . HIS   B 2 127 ? -11.68800 -1.01000  -19.01900 1.000 8.71275  ? 126 HIS   D ND1   1 
ATOM   2446 C  CD2   . HIS   B 2 127 ? -10.82200 -1.23000  -17.02500 1.000 10.15087 ? 126 HIS   D CD2   1 
ATOM   2447 C  CE1   . HIS   B 2 127 ? -11.96400 0.09500   -18.34800 1.000 9.85111  ? 126 HIS   D CE1   1 
ATOM   2448 N  NE2   . HIS   B 2 127 ? -11.45400 -0.01600  -17.13500 1.000 10.18586 ? 126 HIS   D NE2   1 
ATOM   2449 N  N     . VAL   B 2 128 ? -11.85000 -6.22800  -19.56800 1.000 7.99892  ? 127 VAL   D N     1 
ATOM   2450 C  CA    . VAL   B 2 128 ? -11.59400 -7.58500  -20.04500 1.000 7.98878  ? 127 VAL   D CA    1 
ATOM   2451 C  C     . VAL   B 2 128 ? -10.41700 -7.58200  -21.01500 1.000 8.03744  ? 127 VAL   D C     1 
ATOM   2452 O  O     . VAL   B 2 128 ? -10.48000 -6.98000  -22.09900 1.000 8.19644  ? 127 VAL   D O     1 
ATOM   2453 C  CB    . VAL   B 2 128 ? -12.84800 -8.18400  -20.69800 1.000 8.12082  ? 127 VAL   D CB    1 
ATOM   2454 C  CG1   . VAL   B 2 128 ? -12.53200 -9.54800  -21.31700 1.000 8.74989  ? 127 VAL   D CG1   1 
ATOM   2455 C  CG2   . VAL   B 2 128 ? -13.98900 -8.29000  -19.68600 1.000 9.18952  ? 127 VAL   D CG2   1 
ATOM   2456 N  N     . VAL   B 2 129 ? -9.34200  -8.25900  -20.61900 1.000 8.04533  ? 128 VAL   D N     1 
ATOM   2457 C  CA    . VAL   B 2 129 ? -8.17000  -8.47600  -21.46100 1.000 8.54301  ? 128 VAL   D CA    1 
ATOM   2458 C  C     . VAL   B 2 129 ? -8.44200  -9.63800  -22.40800 1.000 7.47417  ? 128 VAL   D C     1 
ATOM   2459 O  O     . VAL   B 2 129 ? -8.89400  -10.71200 -21.98700 1.000 8.54777  ? 128 VAL   D O     1 
ATOM   2460 C  CB    . VAL   B 2 129 ? -6.94200  -8.76100  -20.58400 1.000 8.29429  ? 128 VAL   D CB    1 
ATOM   2461 C  CG1   . VAL   B 2 129 ? -5.76100  -9.21200  -21.43400 1.000 9.26756  ? 128 VAL   D CG1   1 
ATOM   2462 C  CG2   . VAL   B 2 129 ? -6.59500  -7.54500  -19.73500 1.000 9.58749  ? 128 VAL   D CG2   1 
ATOM   2463 N  N     . PHE   B 2 130 ? -8.15000  -9.44000  -23.69600 1.000 8.13724  ? 129 PHE   D N     1 
ATOM   2464 C  CA    . PHE   B 2 130 ? -8.52400  -10.43200 -24.69700 1.000 9.05705  ? 129 PHE   D CA    1 
ATOM   2465 C  C     . PHE   B 2 130 ? -7.51100  -10.64200 -25.81600 1.000 8.50093  ? 129 PHE   D C     1 
ATOM   2466 O  O     . PHE   B 2 130 ? -7.78300  -11.44600 -26.71500 1.000 9.36901  ? 129 PHE   D O     1 
ATOM   2467 C  CB    . PHE   B 2 130 ? -9.90500  -10.11600 -25.30100 1.000 9.66152  ? 129 PHE   D CB    1 
ATOM   2468 C  CG    . PHE   B 2 130 ? -9.93100  -8.86100  -26.11300 1.000 8.96080  ? 129 PHE   D CG    1 
ATOM   2469 C  CD1   . PHE   B 2 130 ? -10.13600 -7.61900  -25.51300 1.000 9.31820  ? 129 PHE   D CD1   1 
ATOM   2470 C  CD2   . PHE   B 2 130 ? -9.75500  -8.91600  -27.48900 1.000 9.50231  ? 129 PHE   D CD2   1 
ATOM   2471 C  CE1   . PHE   B 2 130 ? -10.15400 -6.46600  -26.27100 1.000 9.39117  ? 129 PHE   D CE1   1 
ATOM   2472 C  CE2   . PHE   B 2 130 ? -9.76700  -7.76300  -28.25200 1.000 9.98569  ? 129 PHE   D CE2   1 
ATOM   2473 C  CZ    . PHE   B 2 130 ? -9.97800  -6.53800  -27.64300 1.000 10.39647 ? 129 PHE   D CZ    1 
ATOM   2474 N  N     . GLY   B 2 131 ? -6.36400  -9.97000  -25.80000 1.000 8.80772  ? 130 GLY   D N     1 
ATOM   2475 C  CA    . GLY   B 2 131 ? -5.39500  -10.17100 -26.86200 1.000 8.89065  ? 130 GLY   D CA    1 
ATOM   2476 C  C     . GLY   B 2 131 ? -4.10100  -9.46700  -26.53000 1.000 8.41259  ? 130 GLY   D C     1 
ATOM   2477 O  O     . GLY   B 2 131 ? -3.93800  -8.88900  -25.44900 1.000 9.20465  ? 130 GLY   D O     1 
ATOM   2478 N  N     A LYS   B 2 132 ? -3.17500  -9.50800  -27.48800 0.500 8.78098  ? 131 LYS   D N     1 
ATOM   2479 N  N     B LYS   B 2 132 ? -3.17800  -9.52200  -27.48300 0.500 9.13383  ? 131 LYS   D N     1 
ATOM   2480 C  CA    A LYS   B 2 132 ? -1.87600  -8.87800  -27.29300 0.500 9.50580  ? 131 LYS   D CA    1 
ATOM   2481 C  CA    B LYS   B 2 132 ? -1.91100  -8.83100  -27.32700 0.500 10.27549 ? 131 LYS   D CA    1 
ATOM   2482 C  C     A LYS   B 2 132 ? -1.22700  -8.61500  -28.64500 0.500 9.68832  ? 131 LYS   D C     1 
ATOM   2483 C  C     B LYS   B 2 132 ? -1.35700  -8.51100  -28.70400 0.500 10.30085 ? 131 LYS   D C     1 
ATOM   2484 O  O     A LYS   B 2 132 ? -1.36900  -9.42000  -29.57200 0.500 10.51993 ? 131 LYS   D O     1 
ATOM   2485 O  O     B LYS   B 2 132 ? -1.68300  -9.16500  -29.69900 0.500 12.58113 ? 131 LYS   D O     1 
ATOM   2486 C  CB    A LYS   B 2 132 ? -0.96600  -9.76700  -26.43900 0.500 11.13173 ? 131 LYS   D CB    1 
ATOM   2487 C  CB    B LYS   B 2 132 ? -0.89600  -9.67900  -26.55900 0.500 11.78975 ? 131 LYS   D CB    1 
ATOM   2488 C  CG    A LYS   B 2 132 ? 0.23500   -9.05500  -25.84900 0.500 12.46267 ? 131 LYS   D CG    1 
ATOM   2489 C  CG    B LYS   B 2 132 ? -0.46700  -10.90200 -27.33200 0.500 13.86575 ? 131 LYS   D CG    1 
ATOM   2490 C  CD    A LYS   B 2 132 ? 0.92700   -9.94000  -24.83200 0.500 14.81473 ? 131 LYS   D CD    1 
ATOM   2491 C  CD    B LYS   B 2 132 ? 0.57800   -11.70700 -26.60400 0.500 16.54086 ? 131 LYS   D CD    1 
ATOM   2492 C  CE    A LYS   B 2 132 ? 1.96500   -9.17400  -24.04100 0.500 17.22939 ? 131 LYS   D CE    1 
ATOM   2493 C  CE    B LYS   B 2 132 ? 0.74600   -13.04500 -27.30100 0.500 17.52191 ? 131 LYS   D CE    1 
ATOM   2494 N  NZ    A LYS   B 2 132 ? 2.46400   -9.99900  -22.91600 0.500 19.23313 ? 131 LYS   D NZ    1 
ATOM   2495 N  NZ    B LYS   B 2 132 ? 2.08900   -13.65300 -27.07900 0.500 21.05916 ? 131 LYS   D NZ    1 
ATOM   2496 N  N     . VAL   B 2 133 ? -0.50800  -7.48800  -28.74500 1.000 9.98896  ? 132 VAL   D N     1 
ATOM   2497 C  CA    . VAL   B 2 133 ? 0.23500   -7.18300  -29.96100 1.000 10.85232 ? 132 VAL   D CA    1 
ATOM   2498 C  C     . VAL   B 2 133 ? 1.18700   -8.32700  -30.26700 1.000 12.36579 ? 132 VAL   D C     1 
ATOM   2499 O  O     . VAL   B 2 133 ? 1.89600   -8.82500  -29.38100 1.000 12.70582 ? 132 VAL   D O     1 
ATOM   2500 C  CB    . VAL   B 2 133 ? 0.99200   -5.85600  -29.81300 1.000 10.91728 ? 132 VAL   D CB    1 
ATOM   2501 C  CG1   . VAL   B 2 133 ? 1.97300   -5.66000  -30.97900 1.000 11.93979 ? 132 VAL   D CG1   1 
ATOM   2502 C  CG2   . VAL   B 2 133 ? 0.00200   -4.70300  -29.75300 1.000 11.21914 ? 132 VAL   D CG2   1 
ATOM   2503 N  N     . LYS   B 2 134 ? 1.19100   -8.75700  -31.53000 1.000 12.88922 ? 133 LYS   D N     1 
ATOM   2504 C  CA    . LYS   B 2 134 ? 2.06700   -9.80900  -32.02900 1.000 15.89159 ? 133 LYS   D CA    1 
ATOM   2505 C  C     . LYS   B 2 134 ? 3.28500   -9.21300  -32.72100 1.000 17.41608 ? 133 LYS   D C     1 
ATOM   2506 O  O     . LYS   B 2 134 ? 4.42100   -9.50500  -32.34500 1.000 21.68077 ? 133 LYS   D O     1 
ATOM   2507 C  CB    . LYS   B 2 134 ? 1.27100   -10.71000 -32.98900 1.000 18.59468 ? 133 LYS   D CB    1 
ATOM   2508 C  CG    . LYS   B 2 134 ? 2.04500   -11.88600 -33.56100 1.000 22.17407 ? 133 LYS   D CG    1 
ATOM   2509 C  CD    . LYS   B 2 134 ? 1.14000   -12.81700 -34.37000 1.000 26.61969 ? 133 LYS   D CD    1 
ATOM   2510 C  CE    . LYS   B 2 134 ? 1.90900   -14.03000 -34.87400 1.000 31.36906 ? 133 LYS   D CE    1 
ATOM   2511 N  NZ    . LYS   B 2 134 ? 1.03000   -15.02000 -35.56100 1.000 34.50392 ? 133 LYS   D NZ    1 
ATOM   2512 N  N     . GLU   B 2 135 ? 3.05900   -8.38100  -33.73500 1.000 16.11481 ? 134 GLU   D N     1 
ATOM   2513 C  CA    . GLU   B 2 135 ? 4.11000   -7.65600  -34.42700 1.000 17.73650 ? 134 GLU   D CA    1 
ATOM   2514 C  C     . GLU   B 2 135 ? 3.72300   -6.18800  -34.51200 1.000 15.91820 ? 134 GLU   D C     1 
ATOM   2515 O  O     . GLU   B 2 135 ? 2.54200   -5.83500  -34.48300 1.000 15.34055 ? 134 GLU   D O     1 
ATOM   2516 C  CB    . GLU   B 2 135 ? 4.30600   -8.19100  -35.84700 1.000 23.96633 ? 134 GLU   D CB    1 
ATOM   2517 C  CG    . GLU   B 2 135 ? 4.54000   -9.67900  -35.91700 1.000 30.37288 ? 134 GLU   D CG    1 
ATOM   2518 C  CD    . GLU   B 2 135 ? 5.88800   -10.01300 -36.50800 1.000 36.47801 ? 134 GLU   D CD    1 
ATOM   2519 O  OE1   . GLU   B 2 135 ? 6.86000   -9.28200  -36.21900 1.000 39.64691 ? 134 GLU   D OE1   1 
ATOM   2520 O  OE2   . GLU   B 2 135 ? 5.97000   -10.99700 -37.26700 1.000 37.25164 ? 134 GLU   D OE2   1 
ATOM   2521 N  N     . GLY   B 2 136 ? 4.73300   -5.33200  -34.60800 1.000 16.78160 ? 135 GLY   D N     1 
ATOM   2522 C  CA    . GLY   B 2 136 ? 4.49100   -3.92100  -34.79300 1.000 16.80006 ? 135 GLY   D CA    1 
ATOM   2523 C  C     . GLY   B 2 136 ? 4.34300   -3.11800  -33.52600 1.000 16.33631 ? 135 GLY   D C     1 
ATOM   2524 O  O     . GLY   B 2 136 ? 3.77400   -2.02300  -33.56900 1.000 16.26690 ? 135 GLY   D O     1 
ATOM   2525 N  N     . MET   B 2 137 ? 4.84800   -3.61000  -32.39500 1.000 16.23764 ? 136 MET   D N     1 
ATOM   2526 C  CA    . MET   B 2 137 ? 4.86100   -2.78100  -31.19600 1.000 16.39487 ? 136 MET   D CA    1 
ATOM   2527 C  C     . MET   B 2 137 ? 5.63100   -1.47900  -31.41700 1.000 16.17899 ? 136 MET   D C     1 
ATOM   2528 O  O     . MET   B 2 137 ? 5.30400   -0.45800  -30.80300 1.000 17.18712 ? 136 MET   D O     1 
ATOM   2529 C  CB    . MET   B 2 137 ? 5.41000   -3.56000  -30.00100 1.000 17.61466 ? 136 MET   D CB    1 
ATOM   2530 C  CG    . MET   B 2 137 ? 5.08300   -2.90900  -28.67500 1.000 17.90863 ? 136 MET   D CG    1 
ATOM   2531 S  SD    . MET   B 2 137 ? 3.31200   -2.89300  -28.31100 1.000 16.69407 ? 136 MET   D SD    1 
ATOM   2532 C  CE    . MET   B 2 137 ? 3.24800   -1.54100  -27.13700 1.000 17.12936 ? 136 MET   D CE    1 
ATOM   2533 N  N     . ASN   B 2 138 ? 6.63200   -1.48000  -32.30600 1.000 16.59398 ? 137 ASN   D N     1 
ATOM   2534 C  CA    . ASN   B 2 138 ? 7.32700   -0.23200  -32.61900 1.000 16.28492 ? 137 ASN   D CA    1 
ATOM   2535 C  C     . ASN   B 2 138 ? 6.38400   0.79800   -33.23400 1.000 15.98933 ? 137 ASN   D C     1 
ATOM   2536 O  O     . ASN   B 2 138 ? 6.58100   2.00900   -33.06300 1.000 15.17112 ? 137 ASN   D O     1 
ATOM   2537 C  CB    . ASN   B 2 138 ? 8.52100   -0.49700  -33.54400 1.000 17.83718 ? 137 ASN   D CB    1 
ATOM   2538 C  CG    . ASN   B 2 138 ? 8.10300   -1.00800  -34.90600 1.000 19.31266 ? 137 ASN   D CG    1 
ATOM   2539 O  OD1   . ASN   B 2 138 ? 7.36300   -1.98600  -35.01400 1.000 18.94839 ? 137 ASN   D OD1   1 
ATOM   2540 N  ND2   . ASN   B 2 138 ? 8.57200   -0.34300  -35.95800 1.000 22.55230 ? 137 ASN   D ND2   1 
ATOM   2541 N  N     . ILE   B 2 139 ? 5.35800   0.34000   -33.95000 1.000 15.22077 ? 138 ILE   D N     1 
ATOM   2542 C  CA    . ILE   B 2 139 ? 4.36500   1.24900   -34.51000 1.000 14.24645 ? 138 ILE   D CA    1 
ATOM   2543 C  C     . ILE   B 2 139 ? 3.49700   1.84200   -33.40600 1.000 12.99221 ? 138 ILE   D C     1 
ATOM   2544 O  O     . ILE   B 2 139 ? 3.19100   3.04000   -33.41800 1.000 13.15964 ? 138 ILE   D O     1 
ATOM   2545 C  CB    . ILE   B 2 139 ? 3.53800   0.52100   -35.58800 1.000 15.39239 ? 138 ILE   D CB    1 
ATOM   2546 C  CG1   . ILE   B 2 139 ? 4.45600   -0.01400  -36.69900 1.000 16.88019 ? 138 ILE   D CG1   1 
ATOM   2547 C  CG2   . ILE   B 2 139 ? 2.45900   1.43200   -36.15400 1.000 16.06610 ? 138 ILE   D CG2   1 
ATOM   2548 C  CD1   . ILE   B 2 139 ? 5.34100   1.04000   -37.35100 1.000 18.90358 ? 138 ILE   D CD1   1 
ATOM   2549 N  N     . VAL   B 2 140 ? 3.09200   1.02200   -32.43200 1.000 12.88121 ? 139 VAL   D N     1 
ATOM   2550 C  CA    . VAL   B 2 140 ? 2.35100   1.54200   -31.28500 1.000 12.48629 ? 139 VAL   D CA    1 
ATOM   2551 C  C     . VAL   B 2 140 ? 3.18700   2.57100   -30.53400 1.000 12.78683 ? 139 VAL   D C     1 
ATOM   2552 O  O     . VAL   B 2 140 ? 2.68400   3.62400   -30.12500 1.000 12.82175 ? 139 VAL   D O     1 
ATOM   2553 C  CB    . VAL   B 2 140 ? 1.87200   0.39400   -30.37200 1.000 13.50250 ? 139 VAL   D CB    1 
ATOM   2554 C  CG1   . VAL   B 2 140 ? 1.10100   0.94500   -29.17600 1.000 14.43745 ? 139 VAL   D CG1   1 
ATOM   2555 C  CG2   . VAL   B 2 140 ? 1.01100   -0.59200  -31.15200 1.000 14.02581 ? 139 VAL   D CG2   1 
ATOM   2556 N  N     . GLU   B 2 141 ? 4.47900   2.29000   -30.35100 1.000 14.08858 ? 140 GLU   D N     1 
ATOM   2557 C  CA    . GLU   B 2 141 ? 5.36200   3.25100   -29.69700 1.000 14.38218 ? 140 GLU   D CA    1 
ATOM   2558 C  C     . GLU   B 2 141 ? 5.44400   4.55900   -30.47900 1.000 14.04375 ? 140 GLU   D C     1 
ATOM   2559 O  O     . GLU   B 2 141 ? 5.45100   5.64400   -29.88600 1.000 14.69845 ? 140 GLU   D O     1 
ATOM   2560 C  CB    . GLU   B 2 141 ? 6.75200   2.63900   -29.51500 1.000 16.88506 ? 140 GLU   D CB    1 
ATOM   2561 C  CG    . GLU   B 2 141 ? 6.75700   1.44400   -28.58000 1.000 21.05252 ? 140 GLU   D CG    1 
ATOM   2562 C  CD    . GLU   B 2 141 ? 7.88900   0.47500   -28.86300 1.000 25.97939 ? 140 GLU   D CD    1 
ATOM   2563 O  OE1   . GLU   B 2 141 ? 8.76600   0.79300   -29.69400 1.000 27.76327 ? 140 GLU   D OE1   1 
ATOM   2564 O  OE2   . GLU   B 2 141 ? 7.89200   -0.61900  -28.26100 1.000 28.03218 ? 140 GLU   D OE2   1 
ATOM   2565 N  N     . ALA   B 2 142 ? 5.48700   4.47500   -31.81100 1.000 13.48482 ? 141 ALA   D N     1 
ATOM   2566 C  CA    . ALA   B 2 142 ? 5.51600   5.68000   -32.63400 1.000 13.96857 ? 141 ALA   D CA    1 
ATOM   2567 C  C     . ALA   B 2 142 ? 4.22600   6.48000   -32.48200 1.000 13.77022 ? 141 ALA   D C     1 
ATOM   2568 O  O     . ALA   B 2 142 ? 4.24700   7.71700   -32.46900 1.000 13.84303 ? 141 ALA   D O     1 
ATOM   2569 C  CB    . ALA   B 2 142 ? 5.76400   5.30400   -34.09500 1.000 14.26378 ? 141 ALA   D CB    1 
ATOM   2570 N  N     . MET   B 2 143 ? 3.09400   5.78600   -32.34600 1.000 13.32209 ? 142 MET   D N     1 
ATOM   2571 C  CA    . MET   B 2 143 ? 1.81800   6.46000   -32.12600 1.000 13.73795 ? 142 MET   D CA    1 
ATOM   2572 C  C     . MET   B 2 143 ? 1.83300   7.29900   -30.85500 1.000 14.30909 ? 142 MET   D C     1 
ATOM   2573 O  O     . MET   B 2 143 ? 1.18800   8.35300   -30.80200 1.000 12.94371 ? 142 MET   D O     1 
ATOM   2574 C  CB    . MET   B 2 143 ? 0.69800   5.42000   -32.03700 1.000 13.99092 ? 142 MET   D CB    1 
ATOM   2575 C  CG    . MET   B 2 143 ? 0.37900   4.74000   -33.35900 1.000 14.87038 ? 142 MET   D CG    1 
ATOM   2576 S  SD    . MET   B 2 143 ? -0.61300  3.24100   -33.17700 1.000 14.94311 ? 142 MET   D SD    1 
ATOM   2577 C  CE    . MET   B 2 143 ? -2.01900  3.87000   -32.26000 1.000 15.54462 ? 142 MET   D CE    1 
ATOM   2578 N  N     . GLU   B 2 144 ? 2.55100   6.84700   -29.82000 1.000 16.97519 ? 143 GLU   D N     1 
ATOM   2579 C  CA    . GLU   B 2 144 ? 2.54200   7.54900   -28.53700 1.000 18.16555 ? 143 GLU   D CA    1 
ATOM   2580 C  C     . GLU   B 2 144 ? 3.06700   8.96600   -28.65700 1.000 19.44200 ? 143 GLU   D C     1 
ATOM   2581 O  O     . GLU   B 2 144 ? 2.67100   9.83900   -27.87800 1.000 20.47683 ? 143 GLU   D O     1 
ATOM   2582 C  CB    . GLU   B 2 144 ? 3.41300   6.82200   -27.51900 1.000 20.43339 ? 143 GLU   D CB    1 
ATOM   2583 C  CG    . GLU   B 2 144 ? 2.76600   5.64700   -26.86000 1.000 20.36562 ? 143 GLU   D CG    1 
ATOM   2584 C  CD    . GLU   B 2 144 ? 3.62100   5.07800   -25.74600 1.000 20.44419 ? 143 GLU   D CD    1 
ATOM   2585 O  OE1   . GLU   B 2 144 ? 4.71700   4.56100   -26.04400 1.000 21.86581 ? 143 GLU   D OE1   1 
ATOM   2586 O  OE2   . GLU   B 2 144 ? 3.19900   5.14000   -24.57300 1.000 20.95424 ? 143 GLU   D OE2   1 
ATOM   2587 N  N     . ARG   B 2 145 ? 3.97000   9.21300   -29.60400 1.000 18.85962 ? 144 ARG   D N     1 
ATOM   2588 C  CA    . ARG   B 2 145 ? 4.52700   10.54900  -29.75200 1.000 21.16727 ? 144 ARG   D CA    1 
ATOM   2589 C  C     . ARG   B 2 145 ? 3.46200   11.57300  -30.10300 1.000 17.74904 ? 144 ARG   D C     1 
ATOM   2590 O  O     . ARG   B 2 145 ? 3.69600   12.77400  -29.94100 1.000 19.89698 ? 144 ARG   D O     1 
ATOM   2591 C  CB    . ARG   B 2 145 ? 5.63000   10.53400  -30.81000 1.000 26.09162 ? 144 ARG   D CB    1 
ATOM   2592 C  CG    . ARG   B 2 145 ? 6.81900   9.65100   -30.44400 1.000 33.23442 ? 144 ARG   D CG    1 
ATOM   2593 C  CD    . ARG   B 2 145 ? 7.85300   9.58100   -31.56400 1.000 39.01566 ? 144 ARG   D CD    1 
ATOM   2594 N  NE    . ARG   B 2 145 ? 8.45700   10.87400  -31.87400 1.000 43.17379 ? 144 ARG   D NE    1 
ATOM   2595 C  CZ    . ARG   B 2 145 ? 8.07300   11.66900  -32.86500 1.000 45.69217 ? 144 ARG   D CZ    1 
ATOM   2596 N  NH1   . ARG   B 2 145 ? 7.06500   11.34900  -33.66000 1.000 44.64418 ? 144 ARG   D NH1   1 
ATOM   2597 N  NH2   . ARG   B 2 145 ? 8.71900   12.81500  -33.06200 1.000 47.61682 ? 144 ARG   D NH2   1 
ATOM   2598 N  N     . PHE   B 2 146 ? 2.29500   11.12900  -30.55700 1.000 13.36464 ? 145 PHE   D N     1 
ATOM   2599 C  CA    . PHE   B 2 146 ? 1.22300   12.03200  -30.94000 1.000 11.91632 ? 145 PHE   D CA    1 
ATOM   2600 C  C     . PHE   B 2 146 ? 0.16900   12.19600  -29.85800 1.000 11.15078 ? 145 PHE   D C     1 
ATOM   2601 O  O     . PHE   B 2 146 ? -0.82100  12.89400  -30.07900 1.000 12.66877 ? 145 PHE   D O     1 
ATOM   2602 C  CB    . PHE   B 2 146 ? 0.62200   11.58900  -32.27400 1.000 12.61089 ? 145 PHE   D CB    1 
ATOM   2603 C  CG    . PHE   B 2 146 ? 1.65200   11.46600  -33.35100 1.000 12.03889 ? 145 PHE   D CG    1 
ATOM   2604 C  CD1   . PHE   B 2 146 ? 2.30900   12.59400  -33.81300 1.000 14.05851 ? 145 PHE   D CD1   1 
ATOM   2605 C  CD2   . PHE   B 2 146 ? 2.01800   10.23000  -33.85600 1.000 13.76995 ? 145 PHE   D CD2   1 
ATOM   2606 C  CE1   . PHE   B 2 146 ? 3.28700   12.49500  -34.78300 1.000 15.95424 ? 145 PHE   D CE1   1 
ATOM   2607 C  CE2   . PHE   B 2 146 ? 2.99700   10.12700  -34.83300 1.000 15.09736 ? 145 PHE   D CE2   1 
ATOM   2608 C  CZ    . PHE   B 2 146 ? 3.62900   11.26100  -35.29300 1.000 16.02950 ? 145 PHE   D CZ    1 
ATOM   2609 N  N     . GLY   B 2 147 ? 0.36800   11.59100  -28.68800 1.000 10.52164 ? 146 GLY   D N     1 
ATOM   2610 C  CA    . GLY   B 2 147 ? -0.54200  11.73600  -27.57600 1.000 10.26797 ? 146 GLY   D CA    1 
ATOM   2611 C  C     . GLY   B 2 147 ? -0.09200  12.80500  -26.59700 1.000 10.00560 ? 146 GLY   D C     1 
ATOM   2612 O  O     . GLY   B 2 147 ? 0.81800   13.59600  -26.85500 1.000 11.98259 ? 146 GLY   D O     1 
ATOM   2613 N  N     . SER   B 2 148 ? -0.74400  12.81600  -25.43900 1.000 9.40061  ? 147 SER   D N     1 
ATOM   2614 C  CA    . SER   B 2 148 ? -0.47900  13.82800  -24.42500 1.000 10.32939 ? 147 SER   D CA    1 
ATOM   2615 C  C     . SER   B 2 148 ? -1.01300  13.33300  -23.08500 1.000 10.30493 ? 147 SER   D C     1 
ATOM   2616 O  O     . SER   B 2 148 ? -1.67200  12.29300  -22.99700 1.000 10.30535 ? 147 SER   D O     1 
ATOM   2617 C  CB    . SER   B 2 148 ? -1.11800  15.16600  -24.79700 1.000 10.81752 ? 147 SER   D CB    1 
ATOM   2618 O  OG    . SER   B 2 148 ? -2.52800  15.04500  -24.79600 1.000 11.32495 ? 147 SER   D OG    1 
ATOM   2619 N  N     . ARG   B 2 149 ? -0.75300  14.13100  -22.04300 1.000 11.18710 ? 148 ARG   D N     1 
ATOM   2620 C  CA    . ARG   B 2 149 ? -1.05800  13.75600  -20.66600 1.000 12.78439 ? 148 ARG   D CA    1 
ATOM   2621 C  C     . ARG   B 2 149 ? -2.53100  13.40900  -20.47400 1.000 11.35614 ? 148 ARG   D C     1 
ATOM   2622 O  O     . ARG   B 2 149 ? -2.85700  12.52700  -19.66700 1.000 12.29658 ? 148 ARG   D O     1 
ATOM   2623 C  CB    . ARG   B 2 149 ? -0.65500  14.91500  -19.74400 1.000 14.45079 ? 148 ARG   D CB    1 
ATOM   2624 C  CG    . ARG   B 2 149 ? -0.79900  14.67300  -18.24900 1.000 14.63842 ? 148 ARG   D CG    1 
ATOM   2625 C  CD    . ARG   B 2 149 ? 0.46200   14.06700  -17.63400 1.000 15.84451 ? 148 ARG   D CD    1 
ATOM   2626 N  NE    . ARG   B 2 149 ? 0.40400   14.15100  -16.17900 1.000 16.38821 ? 148 ARG   D NE    1 
ATOM   2627 C  CZ    . ARG   B 2 149 ? -0.21000  13.27200  -15.40000 1.000 17.88209 ? 148 ARG   D CZ    1 
ATOM   2628 N  NH1   . ARG   B 2 149 ? -0.75600  12.17400  -15.89700 1.000 19.01586 ? 148 ARG   D NH1   1 
ATOM   2629 N  NH2   . ARG   B 2 149 ? -0.28800  13.50300  -14.09200 1.000 19.20111 ? 148 ARG   D NH2   1 
ATOM   2630 N  N     . ASN   B 2 150 ? -3.43100  14.09000  -21.19000 1.000 11.04446 ? 149 ASN   D N     1 
ATOM   2631 C  CA    . ASN   B 2 150 ? -4.86900  13.87000  -21.07800 1.000 11.27308 ? 149 ASN   D CA    1 
ATOM   2632 C  C     . ASN   B 2 150 ? -5.44600  13.12400  -22.27800 1.000 10.84077 ? 149 ASN   D C     1 
ATOM   2633 O  O     . ASN   B 2 150 ? -6.66600  13.11300  -22.45800 1.000 12.18997 ? 149 ASN   D O     1 
ATOM   2634 C  CB    . ASN   B 2 150 ? -5.62300  15.18700  -20.84500 1.000 12.18519 ? 149 ASN   D CB    1 
ATOM   2635 C  CG    . ASN   B 2 150 ? -5.55600  16.10600  -22.04700 1.000 12.46887 ? 149 ASN   D CG    1 
ATOM   2636 O  OD1   . ASN   B 2 150 ? -4.91800  15.77900  -23.04900 1.000 12.65781 ? 149 ASN   D OD1   1 
ATOM   2637 N  ND2   . ASN   B 2 150 ? -6.22000  17.25700  -21.96300 1.000 13.66342 ? 149 ASN   D ND2   1 
ATOM   2638 N  N     . GLY   B 2 151 ? -4.60200  12.50800  -23.11000 1.000 10.10086 ? 150 GLY   D N     1 
ATOM   2639 C  CA    . GLY   B 2 151 ? -5.07300  11.70700  -24.22200 1.000 9.80496  ? 150 GLY   D CA    1 
ATOM   2640 C  C     . GLY   B 2 151 ? -5.30300  12.44300  -25.52300 1.000 9.48953  ? 150 GLY   D C     1 
ATOM   2641 O  O     . GLY   B 2 151 ? -5.44000  11.79300  -26.56700 1.000 9.73861  ? 150 GLY   D O     1 
ATOM   2642 N  N     . LYS   B 2 152 ? -5.35300  13.77000  -25.51500 1.000 10.85442 ? 151 LYS   D N     1 
ATOM   2643 C  CA    . LYS   B 2 152 ? -5.60600  14.48400  -26.76000 1.000 11.51706 ? 151 LYS   D CA    1 
ATOM   2644 C  C     . LYS   B 2 152 ? -4.44700  14.28600  -27.73400 1.000 10.36595 ? 151 LYS   D C     1 
ATOM   2645 O  O     . LYS   B 2 152 ? -3.27500  14.31700  -27.34500 1.000 11.45691 ? 151 LYS   D O     1 
ATOM   2646 C  CB    . LYS   B 2 152 ? -5.87600  15.96300  -26.47900 1.000 14.48380 ? 151 LYS   D CB    1 
ATOM   2647 C  CG    . LYS   B 2 152 ? -7.15000  16.13300  -25.64900 1.000 19.91170 ? 151 LYS   D CG    1 
ATOM   2648 C  CD    . LYS   B 2 152 ? -7.60600  17.56900  -25.46300 1.000 24.66470 ? 151 LYS   D CD    1 
ATOM   2649 C  CE    . LYS   B 2 152 ? -8.80000  17.60500  -24.50200 1.000 29.41600 ? 151 LYS   D CE    1 
ATOM   2650 N  NZ    . LYS   B 2 152 ? -9.40400  18.94900  -24.32400 1.000 32.55255 ? 151 LYS   D NZ    1 
ATOM   2651 N  N     . THR   B 2 153 ? -4.77800  14.06300  -29.00500 1.000 10.55958 ? 152 THR   D N     1 
ATOM   2652 C  CA    . THR   B 2 153 ? -3.77100  13.76700  -30.01500 1.000 10.89225 ? 152 THR   D CA    1 
ATOM   2653 C  C     . THR   B 2 153 ? -3.46200  15.00400  -30.85800 1.000 11.20364 ? 152 THR   D C     1 
ATOM   2654 O  O     . THR   B 2 153 ? -4.34300  15.82400  -31.13000 1.000 12.73969 ? 152 THR   D O     1 
ATOM   2655 C  CB    . THR   B 2 153 ? -4.16300  12.56500  -30.89500 1.000 10.95503 ? 152 THR   D CB    1 
ATOM   2656 O  OG1   . THR   B 2 153 ? -5.37200  12.83000  -31.62000 1.000 11.28308 ? 152 THR   D OG1   1 
ATOM   2657 C  CG2   . THR   B 2 153 ? -4.34500  11.29900  -30.04900 1.000 12.01799 ? 152 THR   D CG2   1 
ATOM   2658 N  N     . SER   B 2 154 ? -2.19400  15.13500  -31.25800 1.000 11.39086 ? 153 SER   D N     1 
ATOM   2659 C  CA    . SER   B 2 154 ? -1.72500  16.28300  -32.02600 1.000 12.15593 ? 153 SER   D CA    1 
ATOM   2660 C  C     . SER   B 2 154 ? -1.74600  16.04100  -33.52800 1.000 12.02859 ? 153 SER   D C     1 
ATOM   2661 O  O     . SER   B 2 154 ? -1.59600  16.99500  -34.30100 1.000 13.27803 ? 153 SER   D O     1 
ATOM   2662 C  CB    . SER   B 2 154 ? -0.31400  16.67300  -31.57600 1.000 14.22189 ? 153 SER   D CB    1 
ATOM   2663 O  OG    . SER   B 2 154 ? 0.56400   15.56700  -31.67500 1.000 15.18872 ? 153 SER   D OG    1 
ATOM   2664 N  N     . LYS   B 2 155 ? -1.90300  14.78900  -33.95000 1.000 11.19473 ? 154 LYS   D N     1 
ATOM   2665 C  CA    . LYS   B 2 155 ? -2.17400  14.43000  -35.33200 1.000 10.73735 ? 154 LYS   D CA    1 
ATOM   2666 C  C     . LYS   B 2 155 ? -3.25300  13.36000  -35.30200 1.000 11.04588 ? 154 LYS   D C     1 
ATOM   2667 O  O     . LYS   B 2 155 ? -3.46200  12.70100  -34.28200 1.000 11.74036 ? 154 LYS   D O     1 
ATOM   2668 C  CB    . LYS   B 2 155 ? -0.91400  13.92500  -36.05100 1.000 12.58685 ? 154 LYS   D CB    1 
ATOM   2669 C  CG    . LYS   B 2 155 ? 0.20200   14.96700  -36.15200 1.000 13.72985 ? 154 LYS   D CG    1 
ATOM   2670 C  CD    . LYS   B 2 155 ? 1.36600   14.47100  -37.00500 1.000 16.36598 ? 154 LYS   D CD    1 
ATOM   2671 C  CE    . LYS   B 2 155 ? 2.52700   15.45900  -37.01000 1.000 18.67639 ? 154 LYS   D CE    1 
ATOM   2672 N  NZ    . LYS   B 2 155 ? 2.11100   16.78100  -37.54300 1.000 21.72907 ? 154 LYS   D NZ    1 
ATOM   2673 N  N     . LYS   B 2 156 ? -3.96900  13.21400  -36.41200 1.000 10.41148 ? 155 LYS   D N     1 
ATOM   2674 C  CA    . LYS   B 2 156 ? -5.07800  12.27200  -36.46400 1.000 11.07276 ? 155 LYS   D CA    1 
ATOM   2675 C  C     . LYS   B 2 156 ? -4.55600  10.87900  -36.78900 1.000 9.77369  ? 155 LYS   D C     1 
ATOM   2676 O  O     . LYS   B 2 156 ? -4.00700  10.64500  -37.87100 1.000 10.45511 ? 155 LYS   D O     1 
ATOM   2677 C  CB    . LYS   B 2 156 ? -6.10700  12.72300  -37.49300 1.000 12.39274 ? 155 LYS   D CB    1 
ATOM   2678 C  CG    . LYS   B 2 156 ? -7.38100  11.91200  -37.41300 1.000 14.66112 ? 155 LYS   D CG    1 
ATOM   2679 C  CD    . LYS   B 2 156 ? -8.45400  12.44600  -38.31200 1.000 16.57015 ? 155 LYS   D CD    1 
ATOM   2680 C  CE    . LYS   B 2 156 ? -9.71800  11.62600  -38.16000 1.000 16.81574 ? 155 LYS   D CE    1 
ATOM   2681 N  NZ    . LYS   B 2 156 ? -10.78500 12.05700  -39.09500 1.000 18.42462 ? 155 LYS   D NZ    1 
ATOM   2682 N  N     . ILE   B 2 157 ? -4.73400  9.95600   -35.85400 1.000 9.94957  ? 156 ILE   D N     1 
ATOM   2683 C  CA    . ILE   B 2 157 ? -4.17800  8.61400   -35.95200 1.000 9.93045  ? 156 ILE   D CA    1 
ATOM   2684 C  C     . ILE   B 2 157 ? -5.33000  7.68700   -36.31000 1.000 9.97314  ? 156 ILE   D C     1 
ATOM   2685 O  O     . ILE   B 2 157 ? -6.25300  7.50100   -35.51100 1.000 10.81879 ? 156 ILE   D O     1 
ATOM   2686 C  CB    . ILE   B 2 157 ? -3.51500  8.20400   -34.62900 1.000 10.89968 ? 156 ILE   D CB    1 
ATOM   2687 C  CG1   . ILE   B 2 157 ? -2.55000  9.29400   -34.12100 1.000 11.94613 ? 156 ILE   D CG1   1 
ATOM   2688 C  CG2   . ILE   B 2 157 ? -2.82900  6.85100   -34.76300 1.000 12.45549 ? 156 ILE   D CG2   1 
ATOM   2689 C  CD1   . ILE   B 2 157 ? -1.47900  9.73600   -35.10200 1.000 13.40584 ? 156 ILE   D CD1   1 
ATOM   2690 N  N     . THR   B 2 158 ? -5.28600  7.08600   -37.49600 1.000 9.97841  ? 157 THR   D N     1 
ATOM   2691 C  CA    . THR   B 2 158 ? -6.41000  6.29900   -37.98300 1.000 10.22398 ? 157 THR   D CA    1 
ATOM   2692 C  C     . THR   B 2 158 ? -6.02000  4.85900   -38.30500 1.000 9.72935  ? 157 THR   D C     1 
ATOM   2693 O  O     . THR   B 2 158 ? -4.85700  4.54100   -38.58000 1.000 11.25855 ? 157 THR   D O     1 
ATOM   2694 C  CB    . THR   B 2 158 ? -7.03100  6.91800   -39.24000 1.000 12.70666 ? 157 THR   D CB    1 
ATOM   2695 O  OG1   . THR   B 2 158 ? -6.01200  7.09500   -40.22800 1.000 12.35211 ? 157 THR   D OG1   1 
ATOM   2696 C  CG2   . THR   B 2 158 ? -7.68600  8.25200   -38.92400 1.000 14.07788 ? 157 THR   D CG2   1 
ATOM   2697 N  N     . ILE   B 2 159 ? -7.03900  4.00000   -38.27900 1.000 9.63927  ? 158 ILE   D N     1 
ATOM   2698 C  CA    . ILE   B 2 159 ? -6.95400  2.63600   -38.80600 1.000 10.26361 ? 158 ILE   D CA    1 
ATOM   2699 C  C     . ILE   B 2 159 ? -7.32100  2.74900   -40.28500 1.000 11.18518 ? 158 ILE   D C     1 
ATOM   2700 O  O     . ILE   B 2 159 ? -8.49200  2.72300   -40.66500 1.000 12.77885 ? 158 ILE   D O     1 
ATOM   2701 C  CB    . ILE   B 2 159 ? -7.87400  1.68700   -38.04300 1.000 10.40086 ? 158 ILE   D CB    1 
ATOM   2702 C  CG1   . ILE   B 2 159 ? -7.51200  1.67100   -36.55400 1.000 11.04843 ? 158 ILE   D CG1   1 
ATOM   2703 C  CG2   . ILE   B 2 159 ? -7.81800  0.28600   -38.63800 1.000 11.76914 ? 158 ILE   D CG2   1 
ATOM   2704 C  CD1   . ILE   B 2 159 ? -8.50100  0.90900   -35.67600 1.000 10.42962 ? 158 ILE   D CD1   1 
ATOM   2705 N  N     . ALA   B 2 160 ? -6.30500  2.91500   -41.13300 1.000 11.84252 ? 159 ALA   D N     1 
ATOM   2706 C  CA    . ALA   B 2 160 ? -6.56700  3.07500   -42.56200 1.000 13.54971 ? 159 ALA   D CA    1 
ATOM   2707 C  C     . ALA   B 2 160 ? -7.12400  1.79800   -43.18100 1.000 14.03323 ? 159 ALA   D C     1 
ATOM   2708 O  O     . ALA   B 2 160 ? -7.93900  1.85900   -44.11100 1.000 14.41551 ? 159 ALA   D O     1 
ATOM   2709 C  CB    . ALA   B 2 160 ? -5.29300  3.50300   -43.28400 1.000 14.08249 ? 159 ALA   D CB    1 
ATOM   2710 N  N     . ASP   B 2 161 ? -6.68300  0.64300   -42.69500 1.000 12.90371 ? 160 ASP   D N     1 
ATOM   2711 C  CA    . ASP   B 2 161 ? -7.20400  -0.64100  -43.13000 1.000 14.26663 ? 160 ASP   D CA    1 
ATOM   2712 C  C     . ASP   B 2 161 ? -7.04000  -1.60600  -41.97200 1.000 13.07135 ? 160 ASP   D C     1 
ATOM   2713 O  O     . ASP   B 2 161 ? -6.22200  -1.39600  -41.07000 1.000 13.28144 ? 160 ASP   D O     1 
ATOM   2714 C  CB    . ASP   B 2 161 ? -6.46500  -1.17200  -44.36900 1.000 15.99956 ? 160 ASP   D CB    1 
ATOM   2715 C  CG    . ASP   B 2 161 ? -7.22200  -2.29800  -45.08300 1.000 16.88824 ? 160 ASP   D CG    1 
ATOM   2716 O  OD1   . ASP   B 2 161 ? -8.43400  -2.46600  -44.84800 1.000 16.15682 ? 160 ASP   D OD1   1 
ATOM   2717 O  OD2   . ASP   B 2 161 ? -6.60500  -3.02800  -45.88800 1.000 19.75207 ? 160 ASP   D OD2   1 
ATOM   2718 N  N     . CYS   B 2 162 ? -7.83900  -2.66300  -41.99800 1.000 12.01604 ? 161 CYS   D N     1 
ATOM   2719 C  CA    . CYS   B 2 162 ? -7.75500  -3.68700  -40.96900 1.000 11.48548 ? 161 CYS   D CA    1 
ATOM   2720 C  C     . CYS   B 2 162 ? -8.40200  -4.95400  -41.50100 1.000 11.31073 ? 161 CYS   D C     1 
ATOM   2721 O  O     . CYS   B 2 162 ? -9.18500  -4.92000  -42.45000 1.000 12.57735 ? 161 CYS   D O     1 
ATOM   2722 C  CB    . CYS   B 2 162 ? -8.38900  -3.22600  -39.64500 1.000 10.58892 ? 161 CYS   D CB    1 
ATOM   2723 S  SG    . CYS   B 2 162 ? -10.05500 -2.52900  -39.76900 1.000 10.98457 ? 161 CYS   D SG    1 
ATOM   2724 N  N     . GLY   B 2 163 ? -8.04900  -6.07600  -40.88800 1.000 11.64517 ? 162 GLY   D N     1 
ATOM   2725 C  CA    . GLY   B 2 163 ? -8.55600  -7.35300  -41.34300 1.000 12.56708 ? 162 GLY   D CA    1 
ATOM   2726 C  C     . GLY   B 2 163 ? -7.89600  -8.47400  -40.57300 1.000 11.98478 ? 162 GLY   D C     1 
ATOM   2727 O  O     . GLY   B 2 163 ? -7.28000  -8.25400  -39.53200 1.000 12.11767 ? 162 GLY   D O     1 
ATOM   2728 N  N     . GLN   B 2 164 ? -8.04500  -9.68000  -41.10400 1.000 11.88132 ? 163 GLN   D N     1 
ATOM   2729 C  CA    . GLN   B 2 164 ? -7.50800  -10.87500 -40.48000 1.000 12.23978 ? 163 GLN   D CA    1 
ATOM   2730 C  C     . GLN   B 2 164 ? -6.35700  -11.42100 -41.31800 1.000 12.90295 ? 163 GLN   D C     1 
ATOM   2731 O  O     . GLN   B 2 164 ? -6.35700  -11.30600 -42.54800 1.000 15.71150 ? 163 GLN   D O     1 
ATOM   2732 C  CB    . GLN   B 2 164 ? -8.61500  -11.92500 -40.34700 1.000 13.37670 ? 163 GLN   D CB    1 
ATOM   2733 C  CG    . GLN   B 2 164 ? -8.26100  -13.11800 -39.48400 1.000 13.69701 ? 163 GLN   D CG    1 
ATOM   2734 C  CD    . GLN   B 2 164 ? -9.47400  -13.92900 -39.06700 1.000 14.39137 ? 163 GLN   D CD    1 
ATOM   2735 O  OE1   . GLN   B 2 164 ? -10.61800 -13.56400 -39.34900 1.000 14.73003 ? 163 GLN   D OE1   1 
ATOM   2736 N  NE2   . GLN   B 2 164 ? -9.22500  -15.04400 -38.40900 1.000 14.87892 ? 163 GLN   D NE2   1 
ATOM   2737 N  N     . LEU   B 2 165 ? -5.36100  -11.99400 -40.64400 1.000 13.37924 ? 164 LEU   D N     1 
ATOM   2738 C  CA    . LEU   B 2 165 ? -4.23100  -12.64900 -41.29300 1.000 15.13949 ? 164 LEU   D CA    1 
ATOM   2739 C  C     . LEU   B 2 165 ? -4.27600  -14.15300 -41.05400 1.000 16.49885 ? 164 LEU   D C     1 
ATOM   2740 O  O     . LEU   B 2 165 ? -5.05300  -14.65700 -40.24000 1.000 17.37485 ? 164 LEU   D O     1 
ATOM   2741 C  CB    . LEU   B 2 165 ? -2.90500  -12.10600 -40.75600 1.000 16.71827 ? 164 LEU   D CB    1 
ATOM   2742 C  CG    . LEU   B 2 165 ? -2.63400  -10.61500 -40.96300 1.000 18.29712 ? 164 LEU   D CG    1 
ATOM   2743 C  CD1   . LEU   B 2 165 ? -1.32900  -10.21700 -40.29900 1.000 19.73878 ? 164 LEU   D CD1   1 
ATOM   2744 C  CD2   . LEU   B 2 165 ? -2.61900  -10.26400 -42.44500 1.000 19.57511 ? 164 LEU   D CD2   1 
ATOM   2745 N  N     . GLU   B 2 166 ? -3.41200  -14.86900 -41.77600 1.000 20.26251 ? 165 GLU   D N     1 
ATOM   2746 C  CA    . GLU   B 2 166 ? -3.16200  -16.29800 -41.55300 1.000 26.06718 ? 165 GLU   D CA    1 
ATOM   2747 C  C     . GLU   B 2 166 ? -4.42200  -17.15600 -41.59600 1.000 28.09947 ? 165 GLU   D C     1 
ATOM   2748 O  O     . GLU   B 2 166 ? -4.64700  -18.01600 -40.73800 1.000 28.88421 ? 165 GLU   D O     1 
ATOM   2749 C  CB    . GLU   B 2 166 ? -2.42600  -16.51800 -40.22600 1.000 30.70381 ? 165 GLU   D CB    1 
ATOM   2750 C  CG    . GLU   B 2 166 ? -1.11400  -15.75800 -40.10300 1.000 35.48471 ? 165 GLU   D CG    1 
ATOM   2751 C  CD    . GLU   B 2 166 ? -0.39200  -16.05600 -38.80100 1.000 39.81623 ? 165 GLU   D CD    1 
ATOM   2752 O  OE1   . GLU   B 2 166 ? -0.13400  -17.24700 -38.52100 1.000 41.47676 ? 165 GLU   D OE1   1 
ATOM   2753 O  OE2   . GLU   B 2 166 ? -0.09200  -15.09900 -38.05500 1.000 41.00586 ? 165 GLU   D OE2   1 
ATOM   2754 O  OXT   . GLU   B 2 166 ? -5.24200  -17.01800 -42.49900 1.000 29.75600 ? 165 GLU   D OXT   1 
HETATM 2755 P  PG    . GNP   C 3 .   ? -17.16400 14.23600  -16.87200 1.000 8.00084  ? 201 GNP   A PG    1 
HETATM 2756 O  O1G   . GNP   C 3 .   ? -16.07700 15.11000  -17.40200 1.000 9.87894  ? 201 GNP   A O1G   1 
HETATM 2757 O  O2G   . GNP   C 3 .   ? -17.00100 13.89700  -15.40500 1.000 11.30511 ? 201 GNP   A O2G   1 
HETATM 2758 O  O3G   . GNP   C 3 .   ? -17.30600 12.97600  -17.73200 1.000 9.77538  ? 201 GNP   A O3G   1 
HETATM 2759 N  N3B   . GNP   C 3 .   ? -18.64200 15.09600  -16.98500 1.000 8.25533  ? 201 GNP   A N3B   1 
HETATM 2760 P  PB    . GNP   C 3 .   ? -18.85900 16.63100  -16.42400 1.000 7.30446  ? 201 GNP   A PB    1 
HETATM 2761 O  O1B   . GNP   C 3 .   ? -19.10700 16.67300  -14.94300 1.000 7.56040  ? 201 GNP   A O1B   1 
HETATM 2762 O  O2B   . GNP   C 3 .   ? -17.76300 17.53400  -16.91000 1.000 7.41210  ? 201 GNP   A O2B   1 
HETATM 2763 O  O3A   . GNP   C 3 .   ? -20.25800 17.09000  -17.12800 1.000 7.87749  ? 201 GNP   A O3A   1 
HETATM 2764 P  PA    . GNP   C 3 .   ? -20.42900 17.97200  -18.44400 1.000 7.91044  ? 201 GNP   A PA    1 
HETATM 2765 O  O1A   . GNP   C 3 .   ? -20.11300 19.42100  -18.11100 1.000 8.79916  ? 201 GNP   A O1A   1 
HETATM 2766 O  O2A   . GNP   C 3 .   ? -19.72600 17.31200  -19.56200 1.000 8.67196  ? 201 GNP   A O2A   1 
HETATM 2767 O  "O5'" . GNP   C 3 .   ? -21.99000 17.88000  -18.64600 1.000 8.39109  ? 201 GNP   A "O5'" 1 
HETATM 2768 C  "C5'" . GNP   C 3 .   ? -22.64500 16.60600  -18.82500 1.000 9.21059  ? 201 GNP   A "C5'" 1 
HETATM 2769 C  "C4'" . GNP   C 3 .   ? -23.96800 16.83100  -19.51200 1.000 9.61631  ? 201 GNP   A "C4'" 1 
HETATM 2770 O  "O4'" . GNP   C 3 .   ? -24.83600 17.58800  -18.63700 1.000 8.63428  ? 201 GNP   A "O4'" 1 
HETATM 2771 C  "C3'" . GNP   C 3 .   ? -23.91600 17.60800  -20.82600 1.000 10.08286 ? 201 GNP   A "C3'" 1 
HETATM 2772 O  "O3'" . GNP   C 3 .   ? -24.89200 17.09900  -21.72500 1.000 11.05315 ? 201 GNP   A "O3'" 1 
HETATM 2773 C  "C2'" . GNP   C 3 .   ? -24.24000 19.03800  -20.39000 1.000 9.83465  ? 201 GNP   A "C2'" 1 
HETATM 2774 O  "O2'" . GNP   C 3 .   ? -24.87900 19.79400  -21.40700 1.000 10.76596 ? 201 GNP   A "O2'" 1 
HETATM 2775 C  "C1'" . GNP   C 3 .   ? -25.23400 18.78900  -19.25900 1.000 9.16752  ? 201 GNP   A "C1'" 1 
HETATM 2776 N  N9    . GNP   C 3 .   ? -25.23900 19.86000  -18.24800 1.000 8.39448  ? 201 GNP   A N9    1 
HETATM 2777 C  C8    . GNP   C 3 .   ? -24.15400 20.36600  -17.57500 1.000 8.30145  ? 201 GNP   A C8    1 
HETATM 2778 N  N7    . GNP   C 3 .   ? -24.47200 21.32000  -16.73200 1.000 7.89625  ? 201 GNP   A N7    1 
HETATM 2779 C  C5    . GNP   C 3 .   ? -25.84400 21.45400  -16.87100 1.000 7.94916  ? 201 GNP   A C5    1 
HETATM 2780 C  C6    . GNP   C 3 .   ? -26.77800 22.34000  -16.22000 1.000 8.07746  ? 201 GNP   A C6    1 
HETATM 2781 O  O6    . GNP   C 3 .   ? -26.53200 23.20000  -15.36900 1.000 8.73939  ? 201 GNP   A O6    1 
HETATM 2782 N  N1    . GNP   C 3 .   ? -28.07300 22.13000  -16.65100 1.000 8.38759  ? 201 GNP   A N1    1 
HETATM 2783 C  C2    . GNP   C 3 .   ? -28.45500 21.19700  -17.57700 1.000 8.96167  ? 201 GNP   A C2    1 
HETATM 2784 N  N2    . GNP   C 3 .   ? -29.75800 21.12700  -17.86200 1.000 9.95863  ? 201 GNP   A N2    1 
HETATM 2785 N  N3    . GNP   C 3 .   ? -27.60300 20.37600  -18.18500 1.000 8.83774  ? 201 GNP   A N3    1 
HETATM 2786 C  C4    . GNP   C 3 .   ? -26.32800 20.55800  -17.79300 1.000 8.71975  ? 201 GNP   A C4    1 
HETATM 2787 MG MG    . MG    D 4 .   ? -15.99100 17.06100  -17.83000 1.000 7.94739  ? 202 MG    A MG    1 
HETATM 2788 C  C1    . BTB   E 5 .   ? -33.65300 13.77900  2.91200   1.000 17.56521 ? 203 BTB   A C1    1 
HETATM 2789 O  O1    . BTB   E 5 .   ? -32.51200 13.12800  2.41800   1.000 17.07410 ? 203 BTB   A O1    1 
HETATM 2790 C  C2    . BTB   E 5 .   ? -34.91500 12.93500  2.64700   1.000 17.79401 ? 203 BTB   A C2    1 
HETATM 2791 C  C3    . BTB   E 5 .   ? -34.98800 11.92200  3.81900   1.000 18.31751 ? 203 BTB   A C3    1 
HETATM 2792 O  O3    . BTB   E 5 .   ? -33.91100 11.01900  3.84800   1.000 17.18973 ? 203 BTB   A O3    1 
HETATM 2793 C  C4    . BTB   E 5 .   ? -36.15400 13.83900  2.80100   1.000 20.98011 ? 203 BTB   A C4    1 
HETATM 2794 O  O4    . BTB   E 5 .   ? -37.39000 13.16000  2.70200   1.000 25.18602 ? 203 BTB   A O4    1 
HETATM 2795 N  N     . BTB   E 5 .   ? -34.89200 12.26000  1.33200   1.000 16.82195 ? 203 BTB   A N     1 
HETATM 2796 C  C5    . BTB   E 5 .   ? -35.79200 11.12300  1.14000   1.000 17.31106 ? 203 BTB   A C5    1 
HETATM 2797 C  C6    . BTB   E 5 .   ? -35.18500 9.72800   1.22900   1.000 17.89015 ? 203 BTB   A C6    1 
HETATM 2798 O  O6    . BTB   E 5 .   ? -33.90600 9.69600   0.61700   1.000 18.62674 ? 203 BTB   A O6    1 
HETATM 2799 C  C7    . BTB   E 5 .   ? -34.92800 13.17800  0.19800   1.000 16.18959 ? 203 BTB   A C7    1 
HETATM 2800 C  C8    . BTB   E 5 .   ? -34.22700 12.73500  -1.07600  1.000 16.05328 ? 203 BTB   A C8    1 
HETATM 2801 O  O8    . BTB   E 5 .   ? -32.85300 12.48800  -0.83500  1.000 15.73397 ? 203 BTB   A O8    1 
HETATM 2802 C  C1    . A1AOM F 6 .   ? -18.01600 4.79200   -23.85400 1.000 10.52217 ? 204 A1AOM A C1    1 
HETATM 2803 C  C10   . A1AOM F 6 .   ? -8.04800  3.73000   -19.94500 1.000 9.69383  ? 204 A1AOM A C10   1 
HETATM 2804 C  C11   . A1AOM F 6 .   ? -9.07100  4.85600   -19.81900 1.000 8.37931  ? 204 A1AOM A C11   1 
HETATM 2805 C  C12   . A1AOM F 6 .   ? -8.40000  6.17200   -20.00000 1.000 8.90473  ? 204 A1AOM A C12   1 
HETATM 2806 C  C13   . A1AOM F 6 .   ? -6.73300  7.69800   -19.08700 1.000 9.65466  ? 204 A1AOM A C13   1 
HETATM 2807 C  C14   . A1AOM F 6 .   ? -5.65200  7.70300   -18.02300 1.000 9.86421  ? 204 A1AOM A C14   1 
HETATM 2808 C  C15   . A1AOM F 6 .   ? -4.65500  6.59100   -18.34400 1.000 10.56671 ? 204 A1AOM A C15   1 
HETATM 2809 C  C16   . A1AOM F 6 .   ? -4.95800  9.06400   -18.11100 1.000 9.99775  ? 204 A1AOM A C16   1 
HETATM 2810 C  C17   . A1AOM F 6 .   ? -6.25000  7.44500   -16.62700 1.000 9.02809  ? 204 A1AOM A C17   1 
HETATM 2811 C  C18   . A1AOM F 6 .   ? -6.30900  9.46700   -15.18300 1.000 8.97491  ? 204 A1AOM A C18   1 
HETATM 2812 C  C19   . A1AOM F 6 .   ? -7.23300  10.42900  -14.84200 1.000 8.60534  ? 204 A1AOM A C19   1 
HETATM 2813 C  C2    . A1AOM F 6 .   ? -16.50600 4.79500   -23.61800 1.000 9.13659  ? 204 A1AOM A C2    1 
HETATM 2814 C  C20   . A1AOM F 6 .   ? -6.98700  11.46000  -14.00200 1.000 8.63511  ? 204 A1AOM A C20   1 
HETATM 2815 C  C21   . A1AOM F 6 .   ? -12.78400 5.07300   -19.00000 1.000 8.54246  ? 204 A1AOM A C21   1 
HETATM 2816 C  C22   . A1AOM F 6 .   ? -12.73500 6.57500   -18.79400 1.000 8.36433  ? 204 A1AOM A C22   1 
HETATM 2817 C  C23   . A1AOM F 6 .   ? -11.71500 7.11200   -18.01500 1.000 8.19480  ? 204 A1AOM A C23   1 
HETATM 2818 C  C24   . A1AOM F 6 .   ? -11.62500 8.49100   -17.79800 1.000 8.26319  ? 204 A1AOM A C24   1 
HETATM 2819 C  C25   . A1AOM F 6 .   ? -10.51600 9.06400   -16.96800 1.000 7.89905  ? 204 A1AOM A C25   1 
HETATM 2820 C  C26   . A1AOM F 6 .   ? -9.26300  8.44800   -16.96300 1.000 8.44901  ? 204 A1AOM A C26   1 
HETATM 2821 C  C27   . A1AOM F 6 .   ? -8.22100  8.99300   -16.21000 1.000 7.81040  ? 204 A1AOM A C27   1 
HETATM 2822 C  C28   . A1AOM F 6 .   ? -8.45100  10.15700  -15.46300 1.000 7.94012  ? 204 A1AOM A C28   1 
HETATM 2823 C  C29   . A1AOM F 6 .   ? -9.69400  10.79700  -15.46000 1.000 8.09792  ? 204 A1AOM A C29   1 
HETATM 2824 C  C3    . A1AOM F 6 .   ? -15.93700 3.39800   -23.87400 1.000 9.51004  ? 204 A1AOM A C3    1 
HETATM 2825 C  C30   . A1AOM F 6 .   ? -10.71800 10.23900  -16.23200 1.000 8.11938  ? 204 A1AOM A C30   1 
HETATM 2826 C  C31   . A1AOM F 6 .   ? -12.57400 9.33000   -18.38300 1.000 7.73300  ? 204 A1AOM A C31   1 
HETATM 2827 C  C32   . A1AOM F 6 .   ? -13.59300 8.79100   -19.16600 1.000 8.10314  ? 204 A1AOM A C32   1 
HETATM 2828 C  C33   . A1AOM F 6 .   ? -13.67700 7.41800   -19.36800 1.000 8.64894  ? 204 A1AOM A C33   1 
HETATM 2829 C  C34   . A1AOM F 6 .   ? -16.56300 7.67600   -22.78000 1.000 10.14075 ? 204 A1AOM A C34   1 
HETATM 2830 C  C35   . A1AOM F 6 .   ? -17.21600 6.69300   -20.62500 1.000 10.68853 ? 204 A1AOM A C35   1 
HETATM 2831 C  C36   . A1AOM F 6 .   ? -17.87100 8.00300   -20.27700 1.000 13.31367 ? 204 A1AOM A C36   1 
HETATM 2832 C  C37   . A1AOM F 6 .   ? -19.22900 7.79500   -19.60600 1.000 13.54260 ? 204 A1AOM A C37   1 
HETATM 2833 C  C38   . A1AOM F 6 .   ? -19.10000 8.82200   -17.31900 1.000 17.79062 ? 204 A1AOM A C38   1 
HETATM 2834 C  C39   . A1AOM F 6 .   ? -18.09200 9.54100   -16.47400 1.000 17.89754 ? 204 A1AOM A C39   1 
HETATM 2835 C  C4    . A1AOM F 6 .   ? -16.13400 5.23500   -22.19400 1.000 8.59913  ? 204 A1AOM A C4    1 
HETATM 2836 C  C40   . A1AOM F 6 .   ? -17.29300 8.64200   -19.02100 1.000 14.40737 ? 204 A1AOM A C40   1 
HETATM 2837 C  C5    . A1AOM F 6 .   ? -14.64300 5.28100   -21.98300 1.000 8.08736  ? 204 A1AOM A C5    1 
HETATM 2838 C  C6    . A1AOM F 6 .   ? -12.79900 4.67800   -20.48400 1.000 7.78454  ? 204 A1AOM A C6    1 
HETATM 2839 C  C7    . A1AOM F 6 .   ? -12.02400 3.39100   -20.65400 1.000 7.82818  ? 204 A1AOM A C7    1 
HETATM 2840 C  C8    . A1AOM F 6 .   ? -9.82500  2.33800   -20.99800 1.000 8.81260  ? 204 A1AOM A C8    1 
HETATM 2841 C  C9    . A1AOM F 6 .   ? -8.74600  2.37900   -19.92500 1.000 9.75507  ? 204 A1AOM A C9    1 
HETATM 2842 N  N1    . A1AOM F 6 .   ? -14.16700 4.56100   -20.96000 1.000 8.19689  ? 204 A1AOM A N1    1 
HETATM 2843 N  N2    . A1AOM F 6 .   ? -10.69700 3.49800   -20.80200 1.000 8.31987  ? 204 A1AOM A N2    1 
HETATM 2844 N  N3    . A1AOM F 6 .   ? -6.93000  8.60600   -16.02600 1.000 8.41948  ? 204 A1AOM A N3    1 
HETATM 2845 N  N4    . A1AOM F 6 .   ? -6.80100  12.33900  -13.25400 1.000 10.04740 ? 204 A1AOM A N4    1 
HETATM 2846 N  N5    . A1AOM F 6 .   ? -10.15000 4.73700   -20.81000 1.000 8.39372  ? 204 A1AOM A N5    1 
HETATM 2847 N  N6    . A1AOM F 6 .   ? -16.68400 6.55700   -21.84700 1.000 9.05049  ? 204 A1AOM A N6    1 
HETATM 2848 N  N7    . A1AOM F 6 .   ? -18.61600 8.44700   -18.48000 1.000 14.46694 ? 204 A1AOM A N7    1 
HETATM 2849 O  O1    . A1AOM F 6 .   ? -7.44700  6.47000   -18.99800 1.000 9.06625  ? 204 A1AOM A O1    1 
HETATM 2850 O  O2    . A1AOM F 6 .   ? -8.60600  6.97000   -20.89400 1.000 9.38614  ? 204 A1AOM A O2    1 
HETATM 2851 O  O3    . A1AOM F 6 .   ? -12.59600 2.30100   -20.64500 1.000 8.55160  ? 204 A1AOM A O3    1 
HETATM 2852 O  O4    . A1AOM F 6 .   ? -14.51500 9.61100   -19.74800 1.000 8.82901  ? 204 A1AOM A O4    1 
HETATM 2853 O  O5    . A1AOM F 6 .   ? -13.92100 5.98100   -22.69200 1.000 8.87452  ? 204 A1AOM A O5    1 
HETATM 2854 O  O6    . A1AOM F 6 .   ? -20.26000 8.60800   -16.99700 1.000 22.48836 ? 204 A1AOM A O6    1 
HETATM 2855 O  O7    . A1AOM F 6 .   ? -17.17700 5.78500   -19.80600 1.000 11.64960 ? 204 A1AOM A O7    1 
HETATM 2856 O  O     . HOH   G 7 .   ? -27.80300 19.45600  -21.89500 1.000 35.10708 ? 301 HOH   A O     1 
HETATM 2857 O  O     . HOH   G 7 .   ? -18.88500 19.61800  -27.34400 1.000 33.15570 ? 302 HOH   A O     1 
HETATM 2858 O  O     . HOH   G 7 .   ? -30.55500 21.44400  -22.42200 1.000 46.58006 ? 303 HOH   A O     1 
HETATM 2859 O  O     . HOH   G 7 .   ? -9.76300  27.23500  4.62000   1.000 34.93153 ? 304 HOH   A O     1 
HETATM 2860 O  O     . HOH   G 7 .   ? -27.83700 21.23300  9.88200   1.000 39.45561 ? 305 HOH   A O     1 
HETATM 2861 O  O     . HOH   G 7 .   ? 1.07900   33.64000  -11.70500 1.000 46.72561 ? 306 HOH   A O     1 
HETATM 2862 O  O     . HOH   G 7 .   ? -16.01000 13.73700  5.17100   1.000 46.76210 ? 307 HOH   A O     1 
HETATM 2863 O  O     . HOH   G 7 .   ? -15.12500 16.62500  6.19700   1.000 37.35092 ? 308 HOH   A O     1 
HETATM 2864 O  O     . HOH   G 7 .   ? -29.26900 29.25000  -2.76000  1.000 34.50848 ? 309 HOH   A O     1 
HETATM 2865 O  O     . HOH   G 7 .   ? -13.13000 20.92800  -20.08000 1.000 21.09082 ? 310 HOH   A O     1 
HETATM 2866 O  O     . HOH   G 7 .   ? -3.75000  26.19200  -16.47400 1.000 40.40895 ? 311 HOH   A O     1 
HETATM 2867 O  O     . HOH   G 7 .   ? 1.70600   18.56800  5.36900   1.000 47.50293 ? 312 HOH   A O     1 
HETATM 2868 O  O     . HOH   G 7 .   ? -19.17300 6.01200   1.36800   1.000 20.35673 ? 313 HOH   A O     1 
HETATM 2869 O  O     . HOH   G 7 .   ? -13.50900 12.20100  -24.10800 1.000 45.97953 ? 314 HOH   A O     1 
HETATM 2870 O  O     . HOH   G 7 .   ? -30.14400 18.50000  9.43000   1.000 54.23145 ? 315 HOH   A O     1 
HETATM 2871 O  O     . HOH   G 7 .   ? -17.78400 42.79200  -4.90000  1.000 27.50806 ? 316 HOH   A O     1 
HETATM 2872 O  O     . HOH   G 7 .   ? -0.16000  36.06700  -11.90200 1.000 33.44761 ? 317 HOH   A O     1 
HETATM 2873 O  O     . HOH   G 7 .   ? -21.42000 8.20700   -11.30900 1.000 18.55155 ? 318 HOH   A O     1 
HETATM 2874 O  O     . HOH   G 7 .   ? 0.17300   24.24100  -6.34100  1.000 21.21954 ? 319 HOH   A O     1 
HETATM 2875 O  O     . HOH   G 7 .   ? -1.09200  8.98200   -7.64500  1.000 33.60310 ? 320 HOH   A O     1 
HETATM 2876 O  O     . HOH   G 7 .   ? -2.84500  32.27900  -4.34300  1.000 22.37370 ? 321 HOH   A O     1 
HETATM 2877 O  O     . HOH   G 7 .   ? -15.87900 12.11800  -13.83400 1.000 9.75080  ? 322 HOH   A O     1 
HETATM 2878 O  O     . HOH   G 7 .   ? -0.12100  15.33800  -0.56600  1.000 23.06845 ? 323 HOH   A O     1 
HETATM 2879 O  O     . HOH   G 7 .   ? -26.30800 17.99700  -29.34000 1.000 42.73720 ? 324 HOH   A O     1 
HETATM 2880 O  O     . HOH   G 7 .   ? -32.96000 28.10100  -2.88400  1.000 42.99655 ? 325 HOH   A O     1 
HETATM 2881 O  O     . HOH   G 7 .   ? -25.44800 33.03100  -6.56900  1.000 16.32606 ? 326 HOH   A O     1 
HETATM 2882 O  O     . HOH   G 7 .   ? -14.84800 17.42800  -16.12500 1.000 8.39359  ? 327 HOH   A O     1 
HETATM 2883 O  O     . HOH   G 7 .   ? -4.35000  39.89700  -7.79700  1.000 24.75546 ? 328 HOH   A O     1 
HETATM 2884 O  O     . HOH   G 7 .   ? -19.17800 37.46400  -15.84600 1.000 36.47539 ? 329 HOH   A O     1 
HETATM 2885 O  O     . HOH   G 7 .   ? -13.27900 30.28400  4.84100   1.000 45.46966 ? 330 HOH   A O     1 
HETATM 2886 O  O     . HOH   G 7 .   ? -12.91300 2.57400   -16.68300 1.000 13.19263 ? 331 HOH   A O     1 
HETATM 2887 O  O     . HOH   G 7 .   ? -15.55500 36.74300  -20.30700 1.000 23.93967 ? 332 HOH   A O     1 
HETATM 2888 O  O     . HOH   G 7 .   ? -16.17800 35.72400  -14.53100 1.000 38.29133 ? 333 HOH   A O     1 
HETATM 2889 O  O     . HOH   G 7 .   ? -11.52100 21.74700  5.18500   1.000 38.58046 ? 334 HOH   A O     1 
HETATM 2890 O  O     . HOH   G 7 .   ? -15.37400 1.84900   -12.62400 1.000 52.34386 ? 335 HOH   A O     1 
HETATM 2891 O  O     . HOH   G 7 .   ? -16.62400 5.67200   -17.20400 1.000 23.47572 ? 336 HOH   A O     1 
HETATM 2892 O  O     . HOH   G 7 .   ? -4.91400  36.34600  2.78200   1.000 53.17716 ? 337 HOH   A O     1 
HETATM 2893 O  O     . HOH   G 7 .   ? -31.18800 28.31600  -13.65000 1.000 19.60679 ? 338 HOH   A O     1 
HETATM 2894 O  O     . HOH   G 7 .   ? -13.25700 18.17000  -20.94200 1.000 30.47253 ? 339 HOH   A O     1 
HETATM 2895 O  O     . HOH   G 7 .   ? -17.69600 9.83600   -8.19300  1.000 12.64027 ? 340 HOH   A O     1 
HETATM 2896 O  O     . HOH   G 7 .   ? -9.48200  35.05800  7.29600   1.000 45.42474 ? 341 HOH   A O     1 
HETATM 2897 O  O     . HOH   G 7 .   ? -32.28600 11.61400  -12.58000 1.000 31.41106 ? 342 HOH   A O     1 
HETATM 2898 O  O     . HOH   G 7 .   ? -3.10600  41.53200  -17.38200 1.000 30.61401 ? 343 HOH   A O     1 
HETATM 2899 O  O     . HOH   G 7 .   ? -15.04300 11.54900  -17.97600 1.000 8.39272  ? 344 HOH   A O     1 
HETATM 2900 O  O     . HOH   G 7 .   ? -22.72500 26.64100  4.77600   1.000 24.47492 ? 345 HOH   A O     1 
HETATM 2901 O  O     . HOH   G 7 .   ? -4.23200  12.72100  -17.06300 1.000 14.83579 ? 346 HOH   A O     1 
HETATM 2902 O  O     . HOH   G 7 .   ? -23.67200 32.93000  -2.55400  1.000 17.43440 ? 347 HOH   A O     1 
HETATM 2903 O  O     . HOH   G 7 .   ? -33.71500 25.26900  -8.88600  1.000 18.80004 ? 348 HOH   A O     1 
HETATM 2904 O  O     . HOH   G 7 .   ? -34.21600 17.48700  3.31700   1.000 27.11441 ? 349 HOH   A O     1 
HETATM 2905 O  O     . HOH   G 7 .   ? -17.08200 16.82900  -19.61100 1.000 9.77915  ? 350 HOH   A O     1 
HETATM 2906 O  O     . HOH   G 7 .   ? -16.04500 40.16200  -12.71000 1.000 45.46052 ? 351 HOH   A O     1 
HETATM 2907 O  O     . HOH   G 7 .   ? -9.72100  45.33300  -4.37100  1.000 12.78062 ? 352 HOH   A O     1 
HETATM 2908 O  O     . HOH   G 7 .   ? -11.92700 39.39700  -2.64200  1.000 14.07198 ? 353 HOH   A O     1 
HETATM 2909 O  O     . HOH   G 7 .   ? -16.10400 41.65100  -10.36700 1.000 18.05422 ? 354 HOH   A O     1 
HETATM 2910 O  O     . HOH   G 7 .   ? -3.71100  16.81600  -18.26900 1.000 15.88438 ? 355 HOH   A O     1 
HETATM 2911 O  O     . HOH   G 7 .   ? -28.31100 28.03600  -22.45000 1.000 33.12223 ? 356 HOH   A O     1 
HETATM 2912 O  O     . HOH   G 7 .   ? -20.47400 24.74600  10.65900  1.000 29.57848 ? 357 HOH   A O     1 
HETATM 2913 O  O     . HOH   G 7 .   ? -14.23000 27.07300  2.29600   1.000 12.33721 ? 358 HOH   A O     1 
HETATM 2914 O  O     . HOH   G 7 .   ? -30.50700 23.83800  -6.69300  1.000 16.79167 ? 359 HOH   A O     1 
HETATM 2915 O  O     . HOH   G 7 .   ? 2.55700   14.42400  -11.09200 1.000 19.15277 ? 360 HOH   A O     1 
HETATM 2916 O  O     . HOH   G 7 .   ? -20.88200 25.37700  -20.69100 1.000 13.81623 ? 361 HOH   A O     1 
HETATM 2917 O  O     . HOH   G 7 .   ? -26.97500 30.75400  -6.72300  1.000 14.64779 ? 362 HOH   A O     1 
HETATM 2918 O  O     . HOH   G 7 .   ? -2.56100  13.29400  4.12300   1.000 25.83046 ? 363 HOH   A O     1 
HETATM 2919 O  O     . HOH   G 7 .   ? -29.92000 22.50400  -4.33500  1.000 15.03121 ? 364 HOH   A O     1 
HETATM 2920 O  O     . HOH   G 7 .   ? -9.29600  32.29900  -21.00700 1.000 39.92604 ? 365 HOH   A O     1 
HETATM 2921 O  O     . HOH   G 7 .   ? -34.97600 21.28300  0.55600   1.000 29.04819 ? 366 HOH   A O     1 
HETATM 2922 O  O     . HOH   G 7 .   ? -27.39400 14.89400  -14.04100 1.000 11.81853 ? 367 HOH   A O     1 
HETATM 2923 O  O     . HOH   G 7 .   ? -6.77700  25.73200  -21.95400 1.000 35.50983 ? 368 HOH   A O     1 
HETATM 2924 O  O     . HOH   G 7 .   ? -8.87200  42.96000  -3.16700  1.000 13.75818 ? 369 HOH   A O     1 
HETATM 2925 O  O     . HOH   G 7 .   ? -19.33500 18.22800  -22.10400 1.000 12.59954 ? 370 HOH   A O     1 
HETATM 2926 O  O     . HOH   G 7 .   ? -22.19300 36.03200  -3.33800  1.000 32.78711 ? 371 HOH   A O     1 
HETATM 2927 O  O     . HOH   G 7 .   ? -3.38800  29.45500  -1.04800  1.000 27.81621 ? 372 HOH   A O     1 
HETATM 2928 O  O     . HOH   G 7 .   ? -32.08700 27.33800  -7.60400  1.000 21.81019 ? 373 HOH   A O     1 
HETATM 2929 O  O     . HOH   G 7 .   ? -4.91600  7.51000   -3.87500  1.000 22.43168 ? 374 HOH   A O     1 
HETATM 2930 O  O     . HOH   G 7 .   ? -35.51800 21.24800  -9.70900  1.000 18.37548 ? 375 HOH   A O     1 
HETATM 2931 O  O     . HOH   G 7 .   ? -16.72200 29.87700  4.77000   1.000 40.38802 ? 376 HOH   A O     1 
HETATM 2932 O  O     . HOH   G 7 .   ? -7.45100  6.88400   -4.40400  1.000 30.30323 ? 377 HOH   A O     1 
HETATM 2933 O  O     . HOH   G 7 .   ? -33.69500 22.97900  -18.47800 1.000 22.25040 ? 378 HOH   A O     1 
HETATM 2934 O  O     . HOH   G 7 .   ? -13.97700 9.71400   -6.21400  1.000 23.79941 ? 379 HOH   A O     1 
HETATM 2935 O  O     . HOH   G 7 .   ? -9.23700  12.33800  4.29000   1.000 19.68422 ? 380 HOH   A O     1 
HETATM 2936 O  O     . HOH   G 7 .   ? -20.48800 15.78100  7.42300   1.000 18.10139 ? 381 HOH   A O     1 
HETATM 2937 O  O     . HOH   G 7 .   ? -29.95700 16.79400  5.74600   1.000 15.32676 ? 382 HOH   A O     1 
HETATM 2938 O  O     . HOH   G 7 .   ? 0.36300   39.17500  -6.28800  1.000 39.24646 ? 383 HOH   A O     1 
HETATM 2939 O  O     . HOH   G 7 .   ? -3.19500  20.61500  -18.42200 1.000 26.38230 ? 384 HOH   A O     1 
HETATM 2940 O  O     . HOH   G 7 .   ? -22.83600 10.34700  -12.09600 1.000 14.74637 ? 385 HOH   A O     1 
HETATM 2941 O  O     . HOH   G 7 .   ? -32.76500 8.84100   -5.79400  1.000 36.90084 ? 386 HOH   A O     1 
HETATM 2942 O  O     . HOH   G 7 .   ? -22.97800 33.73100  -13.12400 1.000 13.99968 ? 387 HOH   A O     1 
HETATM 2943 O  O     . HOH   G 7 .   ? -1.48100  10.28700  -3.93200  1.000 25.36964 ? 388 HOH   A O     1 
HETATM 2944 O  O     . HOH   G 7 .   ? 2.09400   39.72900  -11.27200 1.000 45.82982 ? 389 HOH   A O     1 
HETATM 2945 O  O     . HOH   G 7 .   ? -9.67000  15.74900  -21.02700 1.000 11.51337 ? 390 HOH   A O     1 
HETATM 2946 O  O     . HOH   G 7 .   ? -0.80200  24.16100  -1.77300  1.000 42.24367 ? 391 HOH   A O     1 
HETATM 2947 O  O     . HOH   G 7 .   ? -11.75100 9.66000   -0.78500  1.000 22.52542 ? 392 HOH   A O     1 
HETATM 2948 O  O     . HOH   G 7 .   ? -11.86500 9.07800   -4.47100  1.000 35.75210 ? 393 HOH   A O     1 
HETATM 2949 O  O     . HOH   G 7 .   ? -20.27900 14.51700  -7.20000  1.000 8.85001  ? 394 HOH   A O     1 
HETATM 2950 O  O     . HOH   G 7 .   ? -10.29100 47.72000  -10.39700 1.000 24.32262 ? 395 HOH   A O     1 
HETATM 2951 O  O     . HOH   G 7 .   ? -8.77900  14.59000  -13.68500 1.000 8.99684  ? 396 HOH   A O     1 
HETATM 2952 O  O     . HOH   G 7 .   ? -17.09200 33.61700  0.90500   1.000 25.79408 ? 397 HOH   A O     1 
HETATM 2953 O  O     . HOH   G 7 .   ? -10.02100 37.56500  -19.34800 1.000 19.92136 ? 398 HOH   A O     1 
HETATM 2954 O  O     . HOH   G 7 .   ? -1.15300  45.10800  -8.64500  1.000 46.26319 ? 399 HOH   A O     1 
HETATM 2955 O  O     . HOH   G 7 .   ? -24.95800 14.01600  -13.18500 1.000 17.53415 ? 400 HOH   A O     1 
HETATM 2956 O  O     . HOH   G 7 .   ? -25.24500 25.66300  4.34800   1.000 17.83890 ? 401 HOH   A O     1 
HETATM 2957 O  O     . HOH   G 7 .   ? -15.72800 34.32800  -23.79300 1.000 41.00408 ? 402 HOH   A O     1 
HETATM 2958 O  O     . HOH   G 7 .   ? -31.26900 11.26200  -2.88900  1.000 18.82391 ? 403 HOH   A O     1 
HETATM 2959 O  O     . HOH   G 7 .   ? -15.97600 24.82500  -26.01200 1.000 32.04940 ? 404 HOH   A O     1 
HETATM 2960 O  O     . HOH   G 7 .   ? -20.81800 34.10500  -25.54100 1.000 44.73688 ? 405 HOH   A O     1 
HETATM 2961 O  O     . HOH   G 7 .   ? -2.12400  11.63900  -12.74600 1.000 14.17043 ? 406 HOH   A O     1 
HETATM 2962 O  O     . HOH   G 7 .   ? -28.06500 33.79700  -15.27700 1.000 32.08304 ? 407 HOH   A O     1 
HETATM 2963 O  O     . HOH   G 7 .   ? -33.64500 25.64200  -4.32400  1.000 30.29964 ? 408 HOH   A O     1 
HETATM 2964 O  O     . HOH   G 7 .   ? -11.21500 14.02900  -23.02500 1.000 42.21354 ? 409 HOH   A O     1 
HETATM 2965 O  O     . HOH   G 7 .   ? -2.23500  22.16700  2.10500   1.000 34.45223 ? 410 HOH   A O     1 
HETATM 2966 O  O     . HOH   G 7 .   ? 2.49900   12.15300  -13.43500 1.000 26.97993 ? 411 HOH   A O     1 
HETATM 2967 O  O     . HOH   G 7 .   ? -29.27600 27.37500  -0.68800  1.000 34.34213 ? 412 HOH   A O     1 
HETATM 2968 O  O     . HOH   G 7 .   ? -1.19600  30.24100  -7.08400  1.000 31.67218 ? 413 HOH   A O     1 
HETATM 2969 O  O     . HOH   G 7 .   ? -10.71000 29.57300  4.15600   1.000 33.01217 ? 414 HOH   A O     1 
HETATM 2970 O  O     . HOH   G 7 .   ? -29.14600 11.95500  -1.34800  1.000 16.36590 ? 415 HOH   A O     1 
HETATM 2971 O  O     . HOH   G 7 .   ? -8.88200  1.40900   -10.02500 1.000 32.48188 ? 416 HOH   A O     1 
HETATM 2972 O  O     . HOH   G 7 .   ? -12.99800 25.47000  4.11800   1.000 27.95718 ? 417 HOH   A O     1 
HETATM 2973 O  O     . HOH   G 7 .   ? -19.36800 36.18000  -5.70900  1.000 14.80268 ? 418 HOH   A O     1 
HETATM 2974 O  O     . HOH   G 7 .   ? -4.56200  36.40800  -2.15800  1.000 23.51068 ? 419 HOH   A O     1 
HETATM 2975 O  O     . HOH   G 7 .   ? -26.90300 28.34100  0.01100   1.000 35.17094 ? 420 HOH   A O     1 
HETATM 2976 O  O     . HOH   G 7 .   ? -14.73500 12.36200  -11.35000 1.000 8.43157  ? 421 HOH   A O     1 
HETATM 2977 O  O     . HOH   G 7 .   ? 0.36500   11.08500  -5.98400  1.000 22.18474 ? 422 HOH   A O     1 
HETATM 2978 O  O     . HOH   G 7 .   ? -25.55700 20.67900  9.28200   1.000 19.91605 ? 423 HOH   A O     1 
HETATM 2979 O  O     . HOH   G 7 .   ? -20.99900 33.28000  -1.47400  1.000 32.33088 ? 424 HOH   A O     1 
HETATM 2980 O  O     . HOH   G 7 .   ? -33.98000 24.56200  2.64300   1.000 39.79544 ? 425 HOH   A O     1 
HETATM 2981 O  O     . HOH   G 7 .   ? -34.59300 10.86900  -4.18800  1.000 18.98249 ? 426 HOH   A O     1 
HETATM 2982 O  O     . HOH   G 7 .   ? -36.15000 24.51500  -11.50500 1.000 31.84004 ? 427 HOH   A O     1 
HETATM 2983 O  O     . HOH   G 7 .   ? -30.51200 19.36800  -19.99700 1.000 28.38682 ? 428 HOH   A O     1 
HETATM 2984 O  O     . HOH   G 7 .   ? -3.06600  35.40700  -18.58200 1.000 46.28457 ? 429 HOH   A O     1 
HETATM 2985 O  O     . HOH   G 7 .   ? -9.19400  9.61200   0.78300   1.000 21.99515 ? 430 HOH   A O     1 
HETATM 2986 O  O     . HOH   G 7 .   ? -25.11900 31.15400  -21.57200 1.000 37.24065 ? 431 HOH   A O     1 
HETATM 2987 O  O     . HOH   G 7 .   ? -3.84000  42.81000  -9.91000  1.000 29.83704 ? 432 HOH   A O     1 
HETATM 2988 O  O     . HOH   G 7 .   ? -26.46900 34.16300  -11.06500 1.000 25.86340 ? 433 HOH   A O     1 
HETATM 2989 O  O     . HOH   G 7 .   ? -5.17000  20.54300  9.41700   1.000 42.33479 ? 434 HOH   A O     1 
HETATM 2990 O  O     . HOH   G 7 .   ? -13.59300 14.80100  -10.18700 1.000 8.18436  ? 435 HOH   A O     1 
HETATM 2991 O  O     . HOH   G 7 .   ? -25.39900 30.71000  -2.04000  1.000 22.06047 ? 436 HOH   A O     1 
HETATM 2992 O  O     . HOH   G 7 .   ? -14.04700 39.65900  -14.34600 1.000 31.93269 ? 437 HOH   A O     1 
HETATM 2993 O  O     . HOH   G 7 .   ? -27.37200 16.22200  -20.51200 1.000 23.92400 ? 438 HOH   A O     1 
HETATM 2994 O  O     . HOH   G 7 .   ? -24.92000 29.51900  -24.20500 1.000 29.12037 ? 439 HOH   A O     1 
HETATM 2995 O  O     . HOH   G 7 .   ? 0.26000   34.36100  -7.28000  1.000 23.46001 ? 440 HOH   A O     1 
HETATM 2996 O  O     . HOH   G 7 .   ? -30.71500 10.20900  -9.02100  1.000 17.13189 ? 441 HOH   A O     1 
HETATM 2997 O  O     . HOH   G 7 .   ? -33.59800 14.38200  -14.63900 1.000 22.69957 ? 442 HOH   A O     1 
HETATM 2998 O  O     . HOH   G 7 .   ? -26.26400 8.43900   -11.11100 1.000 31.82365 ? 443 HOH   A O     1 
HETATM 2999 O  O     . HOH   G 7 .   ? -5.20700  21.20000  -20.49600 1.000 24.77992 ? 444 HOH   A O     1 
HETATM 3000 O  O     . HOH   G 7 .   ? -35.22800 20.70600  -2.70600  1.000 22.11802 ? 445 HOH   A O     1 
HETATM 3001 O  O     . HOH   G 7 .   ? -14.63400 10.15400  -15.53500 1.000 9.57130  ? 446 HOH   A O     1 
HETATM 3002 O  O     . HOH   G 7 .   ? -28.10200 17.42500  -18.09000 1.000 12.05743 ? 447 HOH   A O     1 
HETATM 3003 O  O     . HOH   G 7 .   ? -7.22600  4.90400   -8.88100  1.000 18.07142 ? 448 HOH   A O     1 
HETATM 3004 O  O     . HOH   G 7 .   ? -23.68700 28.93700  1.87000   1.000 28.11459 ? 449 HOH   A O     1 
HETATM 3005 O  O     . HOH   G 7 .   ? -16.43300 40.91600  -7.81300  1.000 13.72623 ? 450 HOH   A O     1 
HETATM 3006 O  O     . HOH   G 7 .   ? -15.58800 41.82000  -0.48700  1.000 13.15590 ? 451 HOH   A O     1 
HETATM 3007 O  O     . HOH   G 7 .   ? -23.09400 34.07600  -10.35400 1.000 13.84851 ? 452 HOH   A O     1 
HETATM 3008 O  O     . HOH   G 7 .   ? -10.18800 40.57000  -4.28200  1.000 23.05242 ? 453 HOH   A O     1 
HETATM 3009 O  O     . HOH   G 7 .   ? -5.14200  25.40600  0.20200   1.000 31.27202 ? 454 HOH   A O     1 
HETATM 3010 O  O     . HOH   G 7 .   ? -37.57100 23.94700  -14.92900 1.000 43.46991 ? 455 HOH   A O     1 
HETATM 3011 O  O     . HOH   G 7 .   ? -27.09600 31.16000  -20.41600 1.000 42.41275 ? 456 HOH   A O     1 
HETATM 3012 O  O     . HOH   G 7 .   ? -35.12000 23.04500  -7.84300  1.000 15.13185 ? 457 HOH   A O     1 
HETATM 3013 O  O     . HOH   G 7 .   ? -21.67300 35.49900  -19.96500 1.000 39.64380 ? 458 HOH   A O     1 
HETATM 3014 O  O     . HOH   G 7 .   ? -7.02400  28.69900  -21.05800 1.000 25.37582 ? 459 HOH   A O     1 
HETATM 3015 O  O     . HOH   G 7 .   ? -20.16900 5.74700   -13.41500 1.000 34.01862 ? 460 HOH   A O     1 
HETATM 3016 O  O     . HOH   G 7 .   ? -0.13300  37.28400  -3.76600  1.000 48.78894 ? 461 HOH   A O     1 
HETATM 3017 O  O     . HOH   G 7 .   ? -10.52400 28.20700  -23.75600 1.000 30.50751 ? 462 HOH   A O     1 
HETATM 3018 O  O     . HOH   G 7 .   ? -26.94300 29.72400  -4.15000  1.000 14.35895 ? 463 HOH   A O     1 
HETATM 3019 O  O     . HOH   G 7 .   ? -6.20300  15.68300  6.69800   1.000 45.85250 ? 464 HOH   A O     1 
HETATM 3020 O  O     . HOH   G 7 .   ? -29.69000 15.60900  -16.67000 1.000 22.29522 ? 465 HOH   A O     1 
HETATM 3021 O  O     . HOH   G 7 .   ? -29.42200 31.54400  -7.35700  1.000 23.98424 ? 466 HOH   A O     1 
HETATM 3022 O  O     . HOH   G 7 .   ? -16.19000 36.22600  2.69100   1.000 30.88655 ? 467 HOH   A O     1 
HETATM 3023 O  O     . HOH   G 7 .   ? -14.94700 43.88900  -9.36300  1.000 12.06282 ? 468 HOH   A O     1 
HETATM 3024 O  O     . HOH   G 7 .   ? 2.99000   9.29200   -11.37900 1.000 45.55883 ? 469 HOH   A O     1 
HETATM 3025 O  O     . HOH   G 7 .   ? -2.23400  10.26000  0.22000   1.000 18.88840 ? 470 HOH   A O     1 
HETATM 3026 O  O     . HOH   G 7 .   ? -1.44700  12.86300  -0.15800  1.000 22.28289 ? 471 HOH   A O     1 
HETATM 3027 O  O     . HOH   G 7 .   ? -13.16100 37.88200  -16.64800 1.000 29.30087 ? 472 HOH   A O     1 
HETATM 3028 O  O     . HOH   G 7 .   ? -18.72300 39.15600  -7.13800  1.000 16.52049 ? 473 HOH   A O     1 
HETATM 3029 O  O     . HOH   G 7 .   ? -35.50400 17.01000  -15.45400 1.000 7.63167  ? 474 HOH   A O     1 
HETATM 3030 O  O     . HOH   G 7 .   ? -9.77000  9.23300   -2.56300  1.000 33.07631 ? 475 HOH   A O     1 
HETATM 3031 O  O     . HOH   G 7 .   ? -25.67500 13.98300  -17.38900 1.000 29.36849 ? 476 HOH   A O     1 
HETATM 3032 O  O     . HOH   G 7 .   ? -15.43600 4.03100   -13.56200 1.000 50.48395 ? 477 HOH   A O     1 
HETATM 3033 O  O     . HOH   G 7 .   ? -14.71700 6.18300   -13.50300 1.000 32.27480 ? 478 HOH   A O     1 
HETATM 3034 O  O     . HOH   G 7 .   ? -35.03500 26.89100  -12.25700 1.000 40.51015 ? 479 HOH   A O     1 
HETATM 3035 O  O     . HOH   G 7 .   ? -13.30200 23.16700  4.72000   1.000 37.76851 ? 480 HOH   A O     1 
HETATM 3036 O  O     . HOH   G 7 .   ? -18.56800 4.55100   -3.87200  1.000 43.41067 ? 481 HOH   A O     1 
HETATM 3037 O  O     . HOH   G 7 .   ? -0.50100  19.74800  -1.27300  1.000 39.04421 ? 482 HOH   A O     1 
HETATM 3038 O  O     . HOH   G 7 .   ? -24.18700 35.40900  -16.22600 1.000 43.38062 ? 483 HOH   A O     1 
HETATM 3039 O  O     . HOH   G 7 .   ? -11.65200 6.21000   -4.50500  1.000 45.58594 ? 484 HOH   A O     1 
HETATM 3040 O  O     . HOH   G 7 .   ? -15.53000 4.70200   -10.65700 1.000 11.73868 ? 485 HOH   A O     1 
HETATM 3041 O  O     . HOH   G 7 .   ? -5.78300  37.96300  1.20600   1.000 24.67690 ? 486 HOH   A O     1 
HETATM 3042 O  O     . HOH   G 7 .   ? -22.02100 11.22800  -17.72800 1.000 37.22377 ? 487 HOH   A O     1 
HETATM 3043 O  O     . HOH   G 7 .   ? -7.62000  35.85900  -20.00800 1.000 12.04888 ? 488 HOH   A O     1 
HETATM 3044 O  O     . HOH   G 7 .   ? -18.45600 37.99800  -19.86800 1.000 42.20829 ? 489 HOH   A O     1 
HETATM 3045 O  O     . HOH   G 7 .   ? -3.87200  26.22200  -19.14100 1.000 45.94714 ? 490 HOH   A O     1 
HETATM 3046 O  O     . HOH   G 7 .   ? -11.31000 8.54100   4.58300   1.000 50.60453 ? 491 HOH   A O     1 
HETATM 3047 O  O     . HOH   G 7 .   ? -13.23300 10.98300  -4.52700  1.000 57.27077 ? 492 HOH   A O     1 
HETATM 3048 O  O     . HOH   G 7 .   ? -19.14600 28.92200  4.97500   1.000 32.86383 ? 493 HOH   A O     1 
HETATM 3049 O  O     . HOH   G 7 .   ? -5.19400  6.75200   -1.07500  1.000 37.67745 ? 494 HOH   A O     1 
HETATM 3050 O  O     . HOH   G 7 .   ? -8.13400  6.79100   0.31800   1.000 48.59198 ? 495 HOH   A O     1 
HETATM 3051 O  O     . HOH   G 7 .   ? -11.34300 33.41300  7.90700   1.000 32.34552 ? 496 HOH   A O     1 
HETATM 3052 O  O     . HOH   G 7 .   ? -35.80200 23.04800  -4.13100  1.000 40.61723 ? 497 HOH   A O     1 
HETATM 3053 O  O     . HOH   G 7 .   ? -4.99400  34.08800  -19.18400 1.000 47.08772 ? 498 HOH   A O     1 
HETATM 3054 O  O     . HOH   G 7 .   ? -36.72100 19.95000  1.83800   1.000 40.09927 ? 499 HOH   A O     1 
HETATM 3055 O  O     . HOH   G 7 .   ? -0.09700  7.10700   -12.12100 1.000 31.43734 ? 500 HOH   A O     1 
HETATM 3056 O  O     . HOH   G 7 .   ? -22.61700 27.20300  7.49900   1.000 35.56212 ? 501 HOH   A O     1 
HETATM 3057 O  O     . HOH   G 7 .   ? -1.44300  6.88400   -9.88100  1.000 37.29594 ? 502 HOH   A O     1 
HETATM 3058 O  O     . HOH   G 7 .   ? -2.68000  25.52000  -0.72400  1.000 51.59473 ? 503 HOH   A O     1 
HETATM 3059 O  O     . HOH   G 7 .   ? -20.21000 37.17400  -8.48700  1.000 30.98972 ? 504 HOH   A O     1 
HETATM 3060 O  O     . HOH   G 7 .   ? -0.79100  40.53900  -16.70000 1.000 49.94436 ? 505 HOH   A O     1 
HETATM 3061 O  O     . HOH   G 7 .   ? -33.41700 26.42500  -18.85800 1.000 41.92426 ? 506 HOH   A O     1 
HETATM 3062 O  O     . HOH   G 7 .   ? -17.20000 23.77900  10.79600  1.000 43.52716 ? 507 HOH   A O     1 
HETATM 3063 O  O     . HOH   G 7 .   ? -7.01100  12.93900  5.88400   1.000 33.73461 ? 508 HOH   A O     1 
HETATM 3064 O  O     . HOH   G 7 .   ? -14.95600 20.48400  -21.99700 1.000 32.11528 ? 509 HOH   A O     1 
HETATM 3065 O  O     . HOH   G 7 .   ? -13.01300 1.38300   -8.24200  1.000 51.12703 ? 510 HOH   A O     1 
HETATM 3066 O  O     . HOH   G 7 .   ? -8.57100  29.71900  -22.50800 1.000 56.28031 ? 511 HOH   A O     1 
HETATM 3067 O  O     . HOH   G 7 .   ? -8.88200  9.60400   3.76600   1.000 30.10760 ? 512 HOH   A O     1 
HETATM 3068 O  O     . HOH   G 7 .   ? -18.11900 42.93600  -7.07700  1.000 49.45210 ? 513 HOH   A O     1 
HETATM 3069 O  O     . HOH   G 7 .   ? -4.97500  23.57000  2.07200   1.000 36.76246 ? 514 HOH   A O     1 
HETATM 3070 O  O     . HOH   G 7 .   ? -20.46100 7.69400   -22.52600 1.000 24.71729 ? 515 HOH   A O     1 
HETATM 3071 O  O     . HOH   G 7 .   ? -17.98700 16.16500  8.83100   1.000 45.97070 ? 516 HOH   A O     1 
HETATM 3072 O  O     . HOH   G 7 .   ? -28.12700 12.28600  -14.59400 1.000 32.75567 ? 517 HOH   A O     1 
HETATM 3073 O  O     . HOH   G 7 .   ? -26.82300 27.12200  2.57700   1.000 29.02459 ? 518 HOH   A O     1 
HETATM 3074 O  O     . HOH   G 7 .   ? -25.31300 34.80700  -8.63400  1.000 24.48713 ? 519 HOH   A O     1 
HETATM 3075 O  O     . HOH   G 7 .   ? -30.86300 11.31200  -15.19900 1.000 52.40902 ? 520 HOH   A O     1 
HETATM 3076 O  O     . HOH   G 7 .   ? 1.39600   36.57900  -6.39100  1.000 50.56767 ? 521 HOH   A O     1 
HETATM 3077 O  O     . HOH   G 7 .   ? -1.15600  22.58500  -18.18000 1.000 42.06082 ? 522 HOH   A O     1 
HETATM 3078 O  O     . HOH   G 7 .   ? -32.42300 16.18200  5.07800   1.000 22.87846 ? 523 HOH   A O     1 
HETATM 3079 O  O     . HOH   G 7 .   ? -38.56700 24.51200  -12.93500 1.000 44.20371 ? 524 HOH   A O     1 
HETATM 3080 O  O     . HOH   G 7 .   ? -34.63500 27.64400  -16.73000 1.000 44.09195 ? 525 HOH   A O     1 
HETATM 3081 O  O     . HOH   G 7 .   ? -12.57600 47.14700  -11.04600 1.000 21.85778 ? 526 HOH   A O     1 
HETATM 3082 O  O     . HOH   G 7 .   ? -0.55500  9.13200   -1.66800  1.000 32.25357 ? 527 HOH   A O     1 
HETATM 3083 O  O     . HOH   G 7 .   ? -17.36300 19.97800  -22.43300 1.000 40.80847 ? 528 HOH   A O     1 
HETATM 3084 O  O     . HOH   G 7 .   ? 0.26800   23.05800  0.75500   1.000 48.07186 ? 529 HOH   A O     1 
HETATM 3085 O  O     . HOH   G 7 .   ? -14.15500 38.71000  -19.00700 1.000 17.50406 ? 530 HOH   A O     1 
HETATM 3086 O  O     . HOH   G 7 .   ? -27.25200 34.46300  -4.91600  1.000 41.00380 ? 531 HOH   A O     1 
HETATM 3087 O  O     . HOH   G 7 .   ? -9.19600  6.27400   -2.27400  1.000 45.17161 ? 532 HOH   A O     1 
HETATM 3088 O  O     . HOH   G 7 .   ? -23.34200 13.33800  -19.08300 1.000 22.98073 ? 533 HOH   A O     1 
HETATM 3089 O  O     . HOH   G 7 .   ? -14.77200 7.34800   -15.72900 1.000 24.63834 ? 534 HOH   A O     1 
HETATM 3090 O  O     . HOH   G 7 .   ? -3.10700  43.69600  -13.10400 1.000 41.21707 ? 535 HOH   A O     1 
HETATM 3091 O  O     . HOH   G 7 .   ? -1.57600  18.44800  -19.18500 1.000 18.10810 ? 536 HOH   A O     1 
HETATM 3092 O  O     . HOH   G 7 .   ? -2.67900  5.94900   -4.15400  1.000 44.38080 ? 537 HOH   A O     1 
HETATM 3093 O  O     . HOH   G 7 .   ? -22.49300 6.10500   -19.94700 1.000 39.51877 ? 538 HOH   A O     1 
HETATM 3094 O  O     . HOH   G 7 .   ? -15.58100 25.37500  10.22200  1.000 36.32462 ? 539 HOH   A O     1 
HETATM 3095 O  O     . HOH   G 7 .   ? -5.20000  3.10600   -8.95000  1.000 41.63849 ? 540 HOH   A O     1 
HETATM 3096 O  O     . HOH   G 7 .   ? -33.24000 16.02400  7.40900   1.000 49.42421 ? 541 HOH   A O     1 
HETATM 3097 O  O     . HOH   G 7 .   ? -33.84200 28.39400  -14.57800 1.000 30.04234 ? 542 HOH   A O     1 
HETATM 3098 O  O     . HOH   G 7 .   ? -19.01800 27.02600  10.03200  1.000 52.89565 ? 543 HOH   A O     1 
HETATM 3099 O  O     . HOH   G 7 .   ? -1.82400  41.93500  -19.49800 1.000 51.70783 ? 544 HOH   A O     1 
HETATM 3100 O  O     . HOH   G 7 .   ? -29.31000 33.86500  -10.96700 1.000 48.45449 ? 545 HOH   A O     1 
HETATM 3101 O  O     . HOH   G 7 .   ? -6.51600  8.59200   4.44000   1.000 53.72258 ? 546 HOH   A O     1 
HETATM 3102 O  O     . HOH   G 7 .   ? -35.56900 21.11500  -18.81400 1.000 33.49879 ? 547 HOH   A O     1 
HETATM 3103 O  O     . HOH   G 7 .   ? -32.08300 28.54400  -20.76700 1.000 45.68786 ? 548 HOH   A O     1 
HETATM 3104 O  O     . HOH   G 7 .   ? 2.20900   9.41000   -1.96100  1.000 37.40766 ? 549 HOH   A O     1 
HETATM 3105 O  O     . HOH   G 7 .   ? -21.36600 5.50300   -21.87700 1.000 44.48735 ? 550 HOH   A O     1 
HETATM 3106 O  O     . HOH   G 7 .   ? -19.78900 33.75800  -27.85300 1.000 50.67863 ? 551 HOH   A O     1 
HETATM 3107 O  O     . HOH   G 7 .   ? -20.22200 32.48300  1.11200   1.000 37.27724 ? 552 HOH   A O     1 
HETATM 3108 O  O     . HOH   G 7 .   ? -14.61100 45.64800  -11.56100 1.000 18.00757 ? 553 HOH   A O     1 
HETATM 3109 O  O     . HOH   G 7 .   ? -24.75200 34.74400  -0.87000  1.000 43.74195 ? 554 HOH   A O     1 
HETATM 3110 O  O     . HOH   G 7 .   ? -36.19200 18.34900  -18.29800 1.000 19.55783 ? 555 HOH   A O     1 
HETATM 3111 O  O     . HOH   G 7 .   ? -6.45900  19.89600  12.29500  1.000 50.47627 ? 556 HOH   A O     1 
HETATM 3112 O  O     . HOH   G 7 .   ? -2.24200  9.35000   2.69200   1.000 43.75237 ? 557 HOH   A O     1 
HETATM 3113 O  O     . HOH   G 7 .   ? -9.05700  37.35100  8.73700   1.000 16.57327 ? 558 HOH   A O     1 
HETATM 3114 O  O     . HOH   G 7 .   ? 3.44600   8.15100   -14.48400 1.000 49.09930 ? 559 HOH   A O     1 
HETATM 3115 O  O     . HOH   G 7 .   ? -16.15900 48.09900  -11.69000 1.000 34.31520 ? 560 HOH   A O     1 
HETATM 3116 O  O     A HOH   H 7 .   ? -3.66300  -3.34500  -45.67100 0.500 23.30298 ? 201 HOH   D O     1 
HETATM 3117 O  O     B HOH   H 7 .   ? -4.05500  -1.74500  -46.25700 0.500 18.55722 ? 201 HOH   D O     1 
HETATM 3118 O  O     . HOH   H 7 .   ? 9.87000   2.70900   -30.41400 1.000 43.91041 ? 202 HOH   D O     1 
HETATM 3119 O  O     . HOH   H 7 .   ? 6.26200   2.95100   -24.94300 1.000 30.28187 ? 203 HOH   D O     1 
HETATM 3120 O  O     . HOH   H 7 .   ? 0.49000   16.65400  -40.16600 1.000 36.22328 ? 204 HOH   D O     1 
HETATM 3121 O  O     . HOH   H 7 .   ? -8.05700  -9.19300  -11.38700 1.000 32.85285 ? 205 HOH   D O     1 
HETATM 3122 O  O     . HOH   H 7 .   ? -16.62300 7.91700   -35.08100 1.000 24.14449 ? 206 HOH   D O     1 
HETATM 3123 O  O     . HOH   H 7 .   ? -21.14200 3.60900   -26.32400 1.000 38.27544 ? 207 HOH   D O     1 
HETATM 3124 O  O     . HOH   H 7 .   ? -26.62300 -5.18100  -22.82700 1.000 44.02905 ? 208 HOH   D O     1 
HETATM 3125 O  O     . HOH   H 7 .   ? -20.20400 -14.09600 -21.44600 1.000 28.82432 ? 209 HOH   D O     1 
HETATM 3126 O  O     . HOH   H 7 .   ? 6.23500   8.91000   -34.08600 1.000 17.80944 ? 210 HOH   D O     1 
HETATM 3127 O  O     . HOH   H 7 .   ? 2.97500   -8.90400  -20.55800 1.000 25.45395 ? 211 HOH   D O     1 
HETATM 3128 O  O     . HOH   H 7 .   ? -19.48400 -12.48900 -38.48700 1.000 27.05448 ? 212 HOH   D O     1 
HETATM 3129 O  O     . HOH   H 7 .   ? -16.97900 -17.48400 -22.56500 1.000 27.13402 ? 213 HOH   D O     1 
HETATM 3130 O  O     . HOH   H 7 .   ? 1.30600   -16.47200 -28.09600 1.000 45.67871 ? 214 HOH   D O     1 
HETATM 3131 O  O     . HOH   H 7 .   ? -15.21800 9.60700   -31.50500 1.000 39.79314 ? 215 HOH   D O     1 
HETATM 3132 O  O     . HOH   H 7 .   ? -19.36600 -11.77000 -22.86200 1.000 30.79290 ? 216 HOH   D O     1 
HETATM 3133 O  O     . HOH   H 7 .   ? 4.90400   -3.87800  -38.42100 1.000 32.67484 ? 217 HOH   D O     1 
HETATM 3134 O  O     . HOH   H 7 .   ? -19.85900 6.42000   -38.25700 1.000 33.59530 ? 218 HOH   D O     1 
HETATM 3135 O  O     . HOH   H 7 .   ? -6.37800  -15.48500 -38.08100 1.000 16.67332 ? 219 HOH   D O     1 
HETATM 3136 O  O     . HOH   H 7 .   ? -9.86800  -0.46300  -12.85100 1.000 38.54322 ? 220 HOH   D O     1 
HETATM 3137 O  O     . HOH   H 7 .   ? -16.12300 -1.20400  -25.45200 1.000 11.02449 ? 221 HOH   D O     1 
HETATM 3138 O  O     . HOH   H 7 .   ? -24.68800 -5.38300  -33.20400 1.000 22.04219 ? 222 HOH   D O     1 
HETATM 3139 O  O     . HOH   H 7 .   ? 7.34600   -3.70900  -37.06100 1.000 35.32724 ? 223 HOH   D O     1 
HETATM 3140 O  O     . HOH   H 7 .   ? -13.14600 7.15100   -34.76700 1.000 17.25824 ? 224 HOH   D O     1 
HETATM 3141 O  O     . HOH   H 7 .   ? -4.18400  -7.83600  -10.36300 1.000 33.27711 ? 225 HOH   D O     1 
HETATM 3142 O  O     . HOH   H 7 .   ? -24.43700 -3.94300  -41.17900 1.000 41.79774 ? 226 HOH   D O     1 
HETATM 3143 O  O     . HOH   H 7 .   ? 6.80500   6.13700   -27.62600 1.000 38.20403 ? 227 HOH   D O     1 
HETATM 3144 O  O     . HOH   H 7 .   ? 9.30100   -9.93000  -35.31400 1.000 50.62507 ? 228 HOH   D O     1 
HETATM 3145 O  O     . HOH   H 7 .   ? 1.30300   15.25500  -29.11000 1.000 25.51954 ? 229 HOH   D O     1 
HETATM 3146 O  O     . HOH   H 7 .   ? -12.76800 -15.60900 -32.94000 1.000 15.04642 ? 230 HOH   D O     1 
HETATM 3147 O  O     . HOH   H 7 .   ? -1.45200  -14.99600 -33.57900 1.000 36.75320 ? 231 HOH   D O     1 
HETATM 3148 O  O     . HOH   H 7 .   ? -6.90400  -18.08900 -39.26200 1.000 44.11833 ? 232 HOH   D O     1 
HETATM 3149 O  O     . HOH   H 7 .   ? -19.26200 -13.16400 -35.78400 1.000 21.74516 ? 233 HOH   D O     1 
HETATM 3150 O  O     . HOH   H 7 .   ? -17.11700 -0.08400  -11.99300 1.000 42.67187 ? 234 HOH   D O     1 
HETATM 3151 O  O     . HOH   H 7 .   ? 4.35400   9.31600   -46.93300 1.000 51.69025 ? 235 HOH   D O     1 
HETATM 3152 O  O     . HOH   H 7 .   ? -21.27900 5.48100   -24.31700 1.000 31.53618 ? 236 HOH   D O     1 
HETATM 3153 O  O     . HOH   H 7 .   ? -19.24600 -14.91700 -19.29400 1.000 30.95369 ? 237 HOH   D O     1 
HETATM 3154 O  O     . HOH   H 7 .   ? 4.26400   -7.18900  -22.28800 1.000 21.40905 ? 238 HOH   D O     1 
HETATM 3155 O  O     . HOH   H 7 .   ? -28.85400 -8.00100  -28.92000 1.000 44.51106 ? 239 HOH   D O     1 
HETATM 3156 O  O     . HOH   H 7 .   ? -19.10700 1.28500   -22.90700 1.000 13.81516 ? 240 HOH   D O     1 
HETATM 3157 O  O     . HOH   H 7 .   ? -6.92400  6.70500   -42.75300 1.000 30.90789 ? 241 HOH   D O     1 
HETATM 3158 O  O     . HOH   H 7 .   ? 1.76200   12.55300  -41.44100 1.000 31.61549 ? 242 HOH   D O     1 
HETATM 3159 O  O     . HOH   H 7 .   ? -23.70600 4.83700   -31.48100 1.000 33.13407 ? 243 HOH   D O     1 
HETATM 3160 O  O     . HOH   H 7 .   ? -4.67000  -21.73500 -28.03000 1.000 34.60624 ? 244 HOH   D O     1 
HETATM 3161 O  O     . HOH   H 7 .   ? -12.23600 5.96200   -31.66700 1.000 11.36266 ? 245 HOH   D O     1 
HETATM 3162 O  O     . HOH   H 7 .   ? -20.43200 -10.29200 -16.36800 1.000 33.48114 ? 246 HOH   D O     1 
HETATM 3163 O  O     . HOH   H 7 .   ? -23.05300 -0.92000  -15.72700 1.000 24.27371 ? 247 HOH   D O     1 
HETATM 3164 O  O     . HOH   H 7 .   ? 1.31400   10.54800  -19.97000 1.000 16.47968 ? 248 HOH   D O     1 
HETATM 3165 O  O     . HOH   H 7 .   ? 1.62600   -2.71100  -10.75600 1.000 40.71383 ? 249 HOH   D O     1 
HETATM 3166 O  O     . HOH   H 7 .   ? -10.48000 -3.10700  -46.53300 1.000 23.32857 ? 250 HOH   D O     1 
HETATM 3167 O  O     . HOH   H 7 .   ? 2.71600   3.66200   -16.72200 1.000 36.52402 ? 251 HOH   D O     1 
HETATM 3168 O  O     . HOH   H 7 .   ? -22.22700 6.97900   -36.97400 1.000 24.47659 ? 252 HOH   D O     1 
HETATM 3169 O  O     . HOH   H 7 .   ? -9.73300  -6.16400  -44.82000 1.000 29.40526 ? 253 HOH   D O     1 
HETATM 3170 O  O     . HOH   H 7 .   ? 2.59800   16.22000  -33.38000 1.000 27.20018 ? 254 HOH   D O     1 
HETATM 3171 O  O     . HOH   H 7 .   ? -10.07200 3.16500   -33.71800 1.000 11.72064 ? 255 HOH   D O     1 
HETATM 3172 O  O     . HOH   H 7 .   ? 6.75100   -1.44300  -25.91600 1.000 35.26901 ? 256 HOH   D O     1 
HETATM 3173 O  O     A HOH   H 7 .   ? 2.85900   -7.63900  -27.11200 0.500 13.41183 ? 257 HOH   D O     1 
HETATM 3174 O  O     B HOH   H 7 .   ? 4.46600   -6.62700  -27.40400 0.500 27.11787 ? 257 HOH   D O     1 
HETATM 3175 O  O     . HOH   H 7 .   ? -14.52700 -4.74800  -20.04900 1.000 10.13938 ? 258 HOH   D O     1 
HETATM 3176 O  O     . HOH   H 7 .   ? -4.85100  9.57400   -40.30500 1.000 11.75783 ? 259 HOH   D O     1 
HETATM 3177 O  O     . HOH   H 7 .   ? 3.45900   -8.20600  -15.25500 1.000 38.92741 ? 260 HOH   D O     1 
HETATM 3178 O  O     . HOH   H 7 .   ? -7.70600  -5.43800  -46.59600 1.000 20.84033 ? 261 HOH   D O     1 
HETATM 3179 O  O     . HOH   H 7 .   ? -3.87800  -16.91700 -36.25500 1.000 19.59478 ? 262 HOH   D O     1 
HETATM 3180 O  O     . HOH   H 7 .   ? -9.43300  12.73400  -26.62000 1.000 29.98313 ? 263 HOH   D O     1 
HETATM 3181 O  O     . HOH   H 7 .   ? -18.18000 -6.58300  -38.72900 1.000 13.04401 ? 264 HOH   D O     1 
HETATM 3182 O  O     . HOH   H 7 .   ? -14.68000 -0.12000  -15.66100 1.000 14.93601 ? 265 HOH   D O     1 
HETATM 3183 O  O     . HOH   H 7 .   ? 2.96900   -11.25300 -28.66300 1.000 43.35954 ? 266 HOH   D O     1 
HETATM 3184 O  O     . HOH   H 7 .   ? -12.08300 -19.37000 -20.69200 1.000 13.66338 ? 267 HOH   D O     1 
HETATM 3185 O  O     . HOH   H 7 .   ? -12.54400 -20.85000 -26.13900 1.000 24.82685 ? 268 HOH   D O     1 
HETATM 3186 O  O     . HOH   H 7 .   ? -26.30400 -2.79100  -35.32200 1.000 39.44689 ? 269 HOH   D O     1 
HETATM 3187 O  O     . HOH   H 7 .   ? -1.49300  -6.64000  -13.85300 1.000 16.27941 ? 270 HOH   D O     1 
HETATM 3188 O  O     . HOH   H 7 .   ? 8.94300   3.42700   -32.82400 1.000 22.22929 ? 271 HOH   D O     1 
HETATM 3189 O  O     . HOH   H 7 .   ? 0.54000   2.09500   -15.37700 1.000 28.14674 ? 272 HOH   D O     1 
HETATM 3190 O  O     . HOH   H 7 .   ? -15.47900 3.25100   -17.27900 1.000 15.74106 ? 273 HOH   D O     1 
HETATM 3191 O  O     . HOH   H 7 .   ? -16.59700 -15.49300 -40.20600 1.000 34.21683 ? 274 HOH   D O     1 
HETATM 3192 O  O     . HOH   H 7 .   ? -13.73200 -16.68100 -30.56600 1.000 19.96073 ? 275 HOH   D O     1 
HETATM 3193 O  O     . HOH   H 7 .   ? -11.63600 8.65800   -38.18900 1.000 18.30857 ? 276 HOH   D O     1 
HETATM 3194 O  O     . HOH   H 7 .   ? -8.26900  -18.66300 -36.31100 1.000 43.86219 ? 277 HOH   D O     1 
HETATM 3195 O  O     . HOH   H 7 .   ? -7.28700  -9.85800  -44.72100 1.000 32.11642 ? 278 HOH   D O     1 
HETATM 3196 O  O     . HOH   H 7 .   ? -13.70500 7.67300   -24.89000 1.000 10.84000 ? 279 HOH   D O     1 
HETATM 3197 O  O     . HOH   H 7 .   ? -16.23400 -4.10100  -15.52400 1.000 12.78841 ? 280 HOH   D O     1 
HETATM 3198 O  O     . HOH   H 7 .   ? -9.57200  -9.88400  -18.21400 1.000 9.04898  ? 281 HOH   D O     1 
HETATM 3199 O  O     . HOH   H 7 .   ? -14.18900 -7.24100  -28.23700 1.000 11.40534 ? 282 HOH   D O     1 
HETATM 3200 O  O     . HOH   H 7 .   ? -4.04800  -14.55100 -15.69500 1.000 24.03325 ? 283 HOH   D O     1 
HETATM 3201 O  O     . HOH   H 7 .   ? -17.92500 -3.53800  -19.26100 1.000 9.48282  ? 284 HOH   D O     1 
HETATM 3202 O  O     . HOH   H 7 .   ? -6.15000  10.64600  -33.38200 1.000 10.60287 ? 285 HOH   D O     1 
HETATM 3203 O  O     . HOH   H 7 .   ? 1.79200   -10.64600 -37.78000 1.000 27.54129 ? 286 HOH   D O     1 
HETATM 3204 O  O     A HOH   H 7 .   ? -8.96200  14.48300  -23.25500 0.500 17.27592 ? 287 HOH   D O     1 
HETATM 3205 O  O     B HOH   H 7 .   ? -9.11500  12.91700  -23.93700 0.500 29.28291 ? 287 HOH   D O     1 
HETATM 3206 O  O     . HOH   H 7 .   ? -8.35800  -20.68900 -30.11900 1.000 22.19788 ? 288 HOH   D O     1 
HETATM 3207 O  O     . HOH   H 7 .   ? -15.80900 -5.39700  -13.01600 1.000 15.19295 ? 289 HOH   D O     1 
HETATM 3208 O  O     . HOH   H 7 .   ? -19.56700 -15.13200 -30.28700 1.000 16.15464 ? 290 HOH   D O     1 
HETATM 3209 O  O     . HOH   H 7 .   ? -16.21300 -9.13600  -22.29800 1.000 9.32805  ? 291 HOH   D O     1 
HETATM 3210 O  O     . HOH   H 7 .   ? -10.37800 7.71000   -41.74500 1.000 24.22651 ? 292 HOH   D O     1 
HETATM 3211 O  O     . HOH   H 7 .   ? -13.79500 -8.14900  -11.00000 1.000 13.81268 ? 293 HOH   D O     1 
HETATM 3212 O  O     . HOH   H 7 .   ? 0.93000   18.15500  -35.41300 1.000 48.51785 ? 294 HOH   D O     1 
HETATM 3213 O  O     . HOH   H 7 .   ? -0.94700  10.85700  -18.36000 1.000 14.04984 ? 295 HOH   D O     1 
HETATM 3214 O  O     . HOH   H 7 .   ? -14.75400 10.32100  -24.70000 1.000 21.03377 ? 296 HOH   D O     1 
HETATM 3215 O  O     . HOH   H 7 .   ? -5.30700  15.37700  -40.76800 1.000 19.79951 ? 297 HOH   D O     1 
HETATM 3216 O  O     . HOH   H 7 .   ? -6.82100  -25.89300 -36.20400 1.000 23.57176 ? 298 HOH   D O     1 
HETATM 3217 O  O     . HOH   H 7 .   ? -18.35400 -7.24900  -14.38000 1.000 25.20678 ? 299 HOH   D O     1 
HETATM 3218 O  O     . HOH   H 7 .   ? -2.55100  -11.29900 -19.54700 1.000 23.98168 ? 300 HOH   D O     1 
HETATM 3219 O  O     . HOH   H 7 .   ? -24.66900 -10.56900 -25.61000 1.000 42.08686 ? 301 HOH   D O     1 
HETATM 3220 O  O     . HOH   H 7 .   ? -6.33100  14.23100  -33.86000 1.000 20.93689 ? 302 HOH   D O     1 
HETATM 3221 O  O     . HOH   H 7 .   ? -11.66200 11.47700  -25.24500 1.000 36.20114 ? 303 HOH   D O     1 
HETATM 3222 O  O     . HOH   H 7 .   ? -9.74600  3.97500   -44.53500 1.000 24.91931 ? 304 HOH   D O     1 
HETATM 3223 O  O     . HOH   H 7 .   ? -7.10600  16.15000  -30.69000 1.000 42.27106 ? 305 HOH   D O     1 
HETATM 3224 O  O     . HOH   H 7 .   ? -7.50600  13.05700  -29.78700 1.000 14.77340 ? 306 HOH   D O     1 
HETATM 3225 O  O     . HOH   H 7 .   ? -24.89600 -7.40800  -39.89500 1.000 24.61503 ? 307 HOH   D O     1 
HETATM 3226 O  O     . HOH   H 7 .   ? -2.39900  19.62700  -33.64600 1.000 30.40608 ? 308 HOH   D O     1 
HETATM 3227 O  O     . HOH   H 7 .   ? 5.23500   -1.11200  -17.37400 1.000 32.65916 ? 309 HOH   D O     1 
HETATM 3228 O  O     . HOH   H 7 .   ? -3.21700  17.88000  -23.90000 1.000 17.59572 ? 310 HOH   D O     1 
HETATM 3229 O  O     . HOH   H 7 .   ? 6.23900   0.78900   -41.18400 1.000 40.49745 ? 311 HOH   D O     1 
HETATM 3230 O  O     . HOH   H 7 .   ? -10.34200 -23.14300 -24.89200 1.000 40.57300 ? 312 HOH   D O     1 
HETATM 3231 O  O     . HOH   H 7 .   ? -26.96900 -2.32400  -25.16700 1.000 39.76369 ? 313 HOH   D O     1 
HETATM 3232 O  O     . HOH   H 7 .   ? -25.15700 -3.11200  -18.87800 1.000 38.76393 ? 314 HOH   D O     1 
HETATM 3233 O  O     . HOH   H 7 .   ? -4.58000  -17.48500 -24.06400 1.000 32.12209 ? 315 HOH   D O     1 
HETATM 3234 O  O     . HOH   H 7 .   ? -4.81700  17.84600  -33.07400 1.000 18.78338 ? 316 HOH   D O     1 
HETATM 3235 O  O     . HOH   H 7 .   ? 5.48900   -5.58900  -17.75900 1.000 39.10726 ? 317 HOH   D O     1 
HETATM 3236 O  O     . HOH   H 7 .   ? -19.53000 5.01300   -16.05700 1.000 46.65192 ? 318 HOH   D O     1 
HETATM 3237 O  O     . HOH   H 7 .   ? -2.33000  -17.54600 -32.98600 1.000 24.51088 ? 319 HOH   D O     1 
HETATM 3238 O  O     . HOH   H 7 .   ? -1.73200  16.54200  -28.23800 1.000 21.39456 ? 320 HOH   D O     1 
HETATM 3239 O  O     . HOH   H 7 .   ? -17.83100 0.99700   -27.86000 1.000 12.69399 ? 321 HOH   D O     1 
HETATM 3240 O  O     . HOH   H 7 .   ? -7.25100  1.75400   -46.87800 1.000 30.33812 ? 322 HOH   D O     1 
HETATM 3241 O  O     . HOH   H 7 .   ? -1.73700  -18.81000 -30.57200 1.000 31.87009 ? 323 HOH   D O     1 
HETATM 3242 O  O     . HOH   H 7 .   ? -19.94600 -10.13300 -45.30400 1.000 40.10268 ? 324 HOH   D O     1 
HETATM 3243 O  O     . HOH   H 7 .   ? 1.32600   -8.72700  -42.15700 1.000 24.87235 ? 325 HOH   D O     1 
HETATM 3244 O  O     . HOH   H 7 .   ? -23.25600 -11.79900 -33.55400 1.000 20.12321 ? 326 HOH   D O     1 
HETATM 3245 O  O     . HOH   H 7 .   ? 0.29700   4.80900   -24.96200 1.000 30.18209 ? 327 HOH   D O     1 
HETATM 3246 O  O     . HOH   H 7 .   ? -9.54100  1.50300   -48.27900 1.000 25.34287 ? 328 HOH   D O     1 
HETATM 3247 O  O     . HOH   H 7 .   ? -25.78300 1.75300   -35.09600 1.000 32.28939 ? 329 HOH   D O     1 
HETATM 3248 O  O     . HOH   H 7 .   ? -24.36900 -6.11200  -21.36300 1.000 26.11736 ? 330 HOH   D O     1 
HETATM 3249 O  O     . HOH   H 7 .   ? -0.58100  2.11000   -42.96200 1.000 22.25576 ? 331 HOH   D O     1 
HETATM 3250 O  O     . HOH   H 7 .   ? 1.18900   -14.20900 -24.40200 1.000 48.20167 ? 332 HOH   D O     1 
HETATM 3251 O  O     . HOH   H 7 .   ? -10.85000 -30.78600 -33.83500 1.000 15.77121 ? 333 HOH   D O     1 
HETATM 3252 O  O     . HOH   H 7 .   ? -9.68300  -12.32900 -19.61000 1.000 9.91529  ? 334 HOH   D O     1 
HETATM 3253 O  O     . HOH   H 7 .   ? -8.65800  -7.63300  -16.04500 1.000 10.87154 ? 335 HOH   D O     1 
HETATM 3254 O  O     . HOH   H 7 .   ? 5.17500   -7.34200  -13.46900 1.000 43.79146 ? 336 HOH   D O     1 
HETATM 3255 O  O     . HOH   H 7 .   ? -25.46900 -9.64900  -37.84000 1.000 51.07928 ? 337 HOH   D O     1 
HETATM 3256 O  O     . HOH   H 7 .   ? -8.90500  11.37100  -33.54600 1.000 21.24552 ? 338 HOH   D O     1 
HETATM 3257 O  O     . HOH   H 7 .   ? -21.84500 -12.63700 -39.88900 1.000 16.37304 ? 339 HOH   D O     1 
HETATM 3258 O  O     . HOH   H 7 .   ? 0.63100   -1.34900  -12.96300 1.000 19.29833 ? 340 HOH   D O     1 
HETATM 3259 O  O     . HOH   H 7 .   ? 5.09100   4.07400   -18.53300 1.000 42.00531 ? 341 HOH   D O     1 
HETATM 3260 O  O     . HOH   H 7 .   ? -10.93900 -17.11700 -37.34500 1.000 29.01981 ? 342 HOH   D O     1 
HETATM 3261 O  O     . HOH   H 7 .   ? -2.18600  -17.64700 -26.25700 1.000 46.01682 ? 343 HOH   D O     1 
HETATM 3262 O  O     . HOH   H 7 .   ? -28.93900 -3.97800  -32.45700 1.000 20.14407 ? 344 HOH   D O     1 
HETATM 3263 O  O     . HOH   H 7 .   ? -9.39400  -25.38900 -30.86600 1.000 46.88715 ? 345 HOH   D O     1 
HETATM 3264 O  O     . HOH   H 7 .   ? -23.26300 -15.39500 -25.01700 1.000 44.90936 ? 346 HOH   D O     1 
HETATM 3265 O  O     . HOH   H 7 .   ? -24.36000 -4.97600  -14.83800 1.000 27.77630 ? 347 HOH   D O     1 
HETATM 3266 O  O     . HOH   H 7 .   ? -3.86100  -20.67200 -30.45200 1.000 15.99333 ? 348 HOH   D O     1 
HETATM 3267 O  O     . HOH   H 7 .   ? 5.63900   0.42400   -24.83300 1.000 42.14473 ? 349 HOH   D O     1 
HETATM 3268 O  O     . HOH   H 7 .   ? -2.65600  -21.11600 -21.00600 1.000 36.77204 ? 350 HOH   D O     1 
HETATM 3269 O  O     . HOH   H 7 .   ? -17.71800 -3.07700  -42.82600 1.000 24.31889 ? 351 HOH   D O     1 
HETATM 3270 O  O     . HOH   H 7 .   ? -13.49900 -2.91500  -40.32100 1.000 10.81252 ? 352 HOH   D O     1 
HETATM 3271 O  O     . HOH   H 7 .   ? -10.09000 -19.33700 -33.03300 1.000 32.54640 ? 353 HOH   D O     1 
HETATM 3272 O  O     . HOH   H 7 .   ? -11.51700 -7.65500  -44.15300 1.000 36.97762 ? 354 HOH   D O     1 
HETATM 3273 O  O     . HOH   H 7 .   ? -15.65900 -17.13900 -19.43000 1.000 19.78027 ? 355 HOH   D O     1 
HETATM 3274 O  O     . HOH   H 7 .   ? -22.85200 2.92200   -18.27500 1.000 39.19757 ? 356 HOH   D O     1 
HETATM 3275 O  O     . HOH   H 7 .   ? 5.09300   3.80600   -22.77000 1.000 50.19747 ? 357 HOH   D O     1 
HETATM 3276 O  O     . HOH   H 7 .   ? -7.02200  -4.24400  -9.92700  1.000 40.25012 ? 358 HOH   D O     1 
HETATM 3277 O  O     . HOH   H 7 .   ? 4.87500   -1.86800  -40.65700 1.000 28.60271 ? 359 HOH   D O     1 
HETATM 3278 O  O     . HOH   H 7 .   ? 1.01000   16.47300  -22.33500 1.000 18.70936 ? 360 HOH   D O     1 
HETATM 3279 O  O     . HOH   H 7 .   ? -0.91000  -3.84000  -19.30100 1.000 13.33941 ? 361 HOH   D O     1 
HETATM 3280 O  O     . HOH   H 7 .   ? -7.07900  -1.74000  -9.00500  1.000 51.87743 ? 362 HOH   D O     1 
HETATM 3281 O  O     . HOH   H 7 .   ? -6.46000  -21.78100 -22.94700 1.000 31.54454 ? 363 HOH   D O     1 
HETATM 3282 O  O     . HOH   H 7 .   ? -14.27600 -13.52700 -14.13600 1.000 14.18821 ? 364 HOH   D O     1 
HETATM 3283 O  O     . HOH   H 7 .   ? 7.63100   -6.03900  -34.42000 1.000 30.69711 ? 365 HOH   D O     1 
HETATM 3284 O  O     . HOH   H 7 .   ? -2.62000  -12.58400 -17.06000 1.000 19.17445 ? 366 HOH   D O     1 
HETATM 3285 O  O     . HOH   H 7 .   ? -9.90100  -9.66400  -43.46300 1.000 19.47981 ? 367 HOH   D O     1 
HETATM 3286 O  O     . HOH   H 7 .   ? 6.04500   -6.29800  -31.78700 1.000 24.67626 ? 368 HOH   D O     1 
HETATM 3287 O  O     . HOH   H 7 .   ? 4.09700   8.73400   -18.86800 1.000 44.71619 ? 369 HOH   D O     1 
HETATM 3288 O  O     . HOH   H 7 .   ? -3.81500  -18.97900 -38.01000 1.000 46.84986 ? 370 HOH   D O     1 
HETATM 3289 O  O     . HOH   H 7 .   ? -1.44000  0.22400   -11.81600 1.000 29.46372 ? 371 HOH   D O     1 
HETATM 3290 O  O     . HOH   H 7 .   ? -3.43000  10.93600  -15.14000 1.000 15.93932 ? 372 HOH   D O     1 
HETATM 3291 O  O     . HOH   H 7 .   ? 3.51500   8.32600   -40.92400 1.000 34.64769 ? 373 HOH   D O     1 
HETATM 3292 O  O     . HOH   H 7 .   ? -24.03200 -0.06000  -39.06900 1.000 39.73995 ? 374 HOH   D O     1 
HETATM 3293 O  O     . HOH   H 7 .   ? -20.99900 -8.37600  -13.47400 1.000 51.92558 ? 375 HOH   D O     1 
HETATM 3294 O  O     . HOH   H 7 .   ? -24.76300 -7.30700  -35.34400 1.000 42.79600 ? 376 HOH   D O     1 
HETATM 3295 O  O     . HOH   H 7 .   ? -16.99400 -16.37600 -16.68200 1.000 34.90395 ? 377 HOH   D O     1 
HETATM 3296 O  O     . HOH   H 7 .   ? -12.09200 -3.93500  -42.49500 1.000 16.53895 ? 378 HOH   D O     1 
HETATM 3297 O  O     . HOH   H 7 .   ? -9.65000  10.44800  -41.47700 1.000 20.96981 ? 379 HOH   D O     1 
HETATM 3298 O  O     . HOH   H 7 .   ? -5.35700  19.49800  -23.93600 1.000 39.76262 ? 380 HOH   D O     1 
HETATM 3299 O  O     . HOH   H 7 .   ? -14.26700 15.05800  -33.39300 1.000 40.58808 ? 381 HOH   D O     1 
HETATM 3300 O  O     . HOH   H 7 .   ? 10.40000  9.99600   -34.24500 1.000 44.35043 ? 382 HOH   D O     1 
HETATM 3301 O  O     . HOH   H 7 .   ? 3.12500   -0.30000  -13.65400 1.000 44.21748 ? 383 HOH   D O     1 
HETATM 3302 O  O     . HOH   H 7 .   ? -17.36700 -11.77900 -15.27400 1.000 46.62585 ? 384 HOH   D O     1 
HETATM 3303 O  O     . HOH   H 7 .   ? 4.14200   -11.29300 -26.28500 1.000 52.07859 ? 385 HOH   D O     1 
HETATM 3304 O  O     . HOH   H 7 .   ? -16.52000 -1.55300  -14.35400 1.000 16.96877 ? 386 HOH   D O     1 
HETATM 3305 O  O     . HOH   H 7 .   ? -13.11100 -20.53800 -23.10200 1.000 21.76707 ? 387 HOH   D O     1 
HETATM 3306 O  O     . HOH   H 7 .   ? 5.78800   7.43000   -41.55100 1.000 42.38808 ? 388 HOH   D O     1 
HETATM 3307 O  O     . HOH   H 7 .   ? -11.16700 -28.90300 -31.24300 1.000 35.40122 ? 389 HOH   D O     1 
HETATM 3308 O  O     . HOH   H 7 .   ? 4.19400   13.09100  -26.66100 1.000 52.57546 ? 390 HOH   D O     1 
HETATM 3309 O  O     . HOH   H 7 .   ? -16.82600 2.79900   -14.86100 1.000 34.81741 ? 391 HOH   D O     1 
HETATM 3310 O  O     . HOH   H 7 .   ? -2.01400  9.06800   -16.38500 1.000 22.88282 ? 392 HOH   D O     1 
HETATM 3311 O  O     . HOH   H 7 .   ? -3.08100  18.64000  -29.71600 1.000 37.80833 ? 393 HOH   D O     1 
HETATM 3312 O  O     . HOH   H 7 .   ? -13.19900 8.63900   -32.44100 1.000 29.77287 ? 394 HOH   D O     1 
HETATM 3313 O  O     . HOH   H 7 .   ? -21.55300 1.83300   -14.22800 1.000 51.85999 ? 395 HOH   D O     1 
HETATM 3314 O  O     . HOH   H 7 .   ? 2.41000   12.79000  -21.40800 1.000 18.68179 ? 396 HOH   D O     1 
HETATM 3315 O  O     . HOH   H 7 .   ? -4.92900  6.69800   -45.11300 1.000 40.57322 ? 397 HOH   D O     1 
HETATM 3316 O  O     . HOH   H 7 .   ? -15.26800 10.10600  -35.67000 1.000 46.92312 ? 398 HOH   D O     1 
HETATM 3317 O  O     . HOH   H 7 .   ? -17.76300 -16.86600 -29.29300 1.000 25.26197 ? 399 HOH   D O     1 
HETATM 3318 O  O     . HOH   H 7 .   ? 1.81100   9.93200   -14.87700 1.000 23.88799 ? 400 HOH   D O     1 
HETATM 3319 O  O     . HOH   H 7 .   ? 5.51600   10.95400  -26.05500 1.000 45.71309 ? 401 HOH   D O     1 
HETATM 3320 O  O     . HOH   H 7 .   ? -25.43300 -12.14700 -27.48200 1.000 56.43937 ? 402 HOH   D O     1 
HETATM 3321 O  O     . HOH   H 7 .   ? 6.20500   7.25300   -23.56600 1.000 52.16162 ? 403 HOH   D O     1 
HETATM 3322 O  O     . HOH   H 7 .   ? -0.58600  9.34200   -13.59200 1.000 17.57461 ? 404 HOH   D O     1 
HETATM 3323 O  O     . HOH   H 7 .   ? 1.67000   0.54700   -43.42600 1.000 35.41833 ? 405 HOH   D O     1 
HETATM 3324 O  O     . HOH   H 7 .   ? -6.83900  10.92700  -41.63300 1.000 17.61797 ? 406 HOH   D O     1 
HETATM 3325 O  O     . HOH   H 7 .   ? 3.98400   1.72300   -15.78400 1.000 43.83588 ? 407 HOH   D O     1 
HETATM 3326 O  O     . HOH   H 7 .   ? -12.97500 -4.00600  -45.02600 1.000 30.20724 ? 408 HOH   D O     1 
HETATM 3327 O  O     . HOH   H 7 .   ? -1.69500  18.35600  -26.21400 1.000 24.29111 ? 409 HOH   D O     1 
HETATM 3328 O  O     . HOH   H 7 .   ? -18.22400 1.00500   -25.42700 1.000 33.16167 ? 410 HOH   D O     1 
HETATM 3329 O  O     . HOH   H 7 .   ? -10.80600 -21.48200 -29.16400 1.000 43.65030 ? 411 HOH   D O     1 
HETATM 3330 O  O     . HOH   H 7 .   ? -6.06100  13.42800  -42.41600 1.000 18.58773 ? 412 HOH   D O     1 
HETATM 3331 O  O     . HOH   H 7 .   ? -18.58200 -2.40300  -44.95000 1.000 43.71891 ? 413 HOH   D O     1 
HETATM 3332 O  O     . HOH   H 7 .   ? 1.73200   -8.26700  -39.52500 1.000 29.32526 ? 414 HOH   D O     1 
HETATM 3333 O  O     . HOH   H 7 .   ? -26.01800 -2.97800  -38.90300 1.000 47.23506 ? 415 HOH   D O     1 
HETATM 3334 O  O     . HOH   H 7 .   ? -2.06100  -0.86600  -8.92100  1.000 48.28479 ? 416 HOH   D O     1 
HETATM 3335 O  O     . HOH   H 7 .   ? -15.31300 1.93800   -9.29500  1.000 42.08715 ? 417 HOH   D O     1 
HETATM 3336 O  O     . HOH   H 7 .   ? -22.17600 1.80700   -37.64500 1.000 27.62482 ? 418 HOH   D O     1 
HETATM 3337 O  O     . HOH   H 7 .   ? 8.66500   7.71500   -34.09600 1.000 32.46556 ? 419 HOH   D O     1 
HETATM 3338 O  O     . HOH   H 7 .   ? -25.37100 -7.59400  -19.29400 1.000 47.73009 ? 420 HOH   D O     1 
HETATM 3339 O  O     . HOH   H 7 .   ? -13.55800 -19.41800 -30.16200 1.000 26.58507 ? 421 HOH   D O     1 
HETATM 3340 O  O     . HOH   H 7 .   ? 0.16800   -8.42700  -13.11600 1.000 42.42656 ? 422 HOH   D O     1 
HETATM 3341 O  O     . HOH   H 7 .   ? -3.10400  5.06600   -45.78700 1.000 33.47907 ? 423 HOH   D O     1 
HETATM 3342 O  O     . HOH   H 7 .   ? 4.11900   12.90000  -17.01500 1.000 34.34057 ? 424 HOH   D O     1 
HETATM 3343 O  O     . HOH   H 7 .   ? 2.68800   10.73700  -17.39600 1.000 27.29346 ? 425 HOH   D O     1 
HETATM 3344 O  O     . HOH   H 7 .   ? -26.41600 -3.14500  -33.02200 1.000 28.37428 ? 426 HOH   D O     1 
HETATM 3345 O  O     . HOH   H 7 .   ? -4.81800  -26.43800 -33.88600 1.000 40.72576 ? 427 HOH   D O     1 
HETATM 3346 O  O     . HOH   H 7 .   ? -4.65700  1.00100   -46.35800 1.000 40.01319 ? 428 HOH   D O     1 
HETATM 3347 O  O     A HOH   H 7 .   ? -5.86100  -13.29500 -9.63900  0.500 11.44528 ? 429 HOH   D O     1 
HETATM 3348 O  O     B HOH   H 7 .   ? -7.32000  -12.66500 -10.13000 0.500 21.99874 ? 429 HOH   D O     1 
HETATM 3349 O  O     . HOH   H 7 .   ? -3.19800  -15.77900 -22.72000 1.000 37.09815 ? 430 HOH   D O     1 
HETATM 3350 O  O     . HOH   H 7 .   ? 6.10600   8.98100   -36.84800 1.000 28.10429 ? 431 HOH   D O     1 
HETATM 3351 O  O     . HOH   H 7 .   ? 11.68400  1.97300   -32.30300 1.000 42.16524 ? 432 HOH   D O     1 
HETATM 3352 O  O     . HOH   H 7 .   ? -23.73100 5.77300   -24.41200 1.000 54.15883 ? 433 HOH   D O     1 
HETATM 3353 O  O     . HOH   H 7 .   ? -17.77200 -17.49400 -20.38200 1.000 45.77754 ? 434 HOH   D O     1 
HETATM 3354 O  O     . HOH   H 7 .   ? 4.06800   12.32500  -38.80400 1.000 34.04247 ? 435 HOH   D O     1 
HETATM 3355 O  O     . HOH   H 7 .   ? 2.49000   16.74400  -24.79200 1.000 40.55635 ? 436 HOH   D O     1 
HETATM 3356 O  O     . HOH   H 7 .   ? -14.01200 -18.67600 -35.13500 1.000 41.10480 ? 437 HOH   D O     1 
HETATM 3357 O  O     . HOH   H 7 .   ? 6.32400   8.36600   -26.18200 1.000 44.20547 ? 438 HOH   D O     1 
HETATM 3358 O  O     . HOH   H 7 .   ? -9.49500  13.51600  -31.35500 1.000 46.38696 ? 439 HOH   D O     1 
HETATM 3359 O  O     . HOH   H 7 .   ? -1.08500  18.32600  -21.90200 1.000 27.66127 ? 440 HOH   D O     1 
HETATM 3360 O  O     . HOH   H 7 .   ? -7.00700  9.57800   -43.93500 1.000 35.58412 ? 441 HOH   D O     1 
HETATM 3361 O  O     . HOH   H 7 .   ? -22.46800 9.45000   -23.47900 1.000 36.65470 ? 442 HOH   D O     1 
HETATM 3362 O  O     . HOH   H 7 .   ? -14.45500 -21.34900 -27.57700 1.000 38.28377 ? 443 HOH   D O     1 
HETATM 3363 O  O     . HOH   H 7 .   ? -25.44600 -12.42200 -31.76000 1.000 42.05552 ? 444 HOH   D O     1 
HETATM 3364 O  O     . HOH   H 7 .   ? -16.33500 -18.05100 -31.23200 1.000 32.74929 ? 445 HOH   D O     1 
HETATM 3365 O  O     . HOH   H 7 .   ? 4.44900   -6.33600  -39.54000 1.000 39.84938 ? 446 HOH   D O     1 
HETATM 3366 O  O     . HOH   H 7 .   ? -8.19900  -20.44900 -37.99900 1.000 49.14185 ? 447 HOH   D O     1 
HETATM 3367 O  O     . HOH   H 7 .   ? -11.87100 -17.72600 -34.45800 1.000 29.58085 ? 448 HOH   D O     1 
HETATM 3368 O  O     . HOH   H 7 .   ? -9.18500  6.33100   -43.26500 1.000 37.18312 ? 449 HOH   D O     1 
HETATM 3369 O  O     . HOH   H 7 .   ? 6.63700   -4.67900  -25.86100 1.000 41.09198 ? 450 HOH   D O     1 
HETATM 3370 O  O     . HOH   H 7 .   ? 4.17900   9.66600   -38.59500 1.000 27.39002 ? 451 HOH   D O     1 
HETATM 3371 O  O     . HOH   H 7 .   ? -2.57500  -0.94100  -48.06500 1.000 48.15672 ? 452 HOH   D O     1 
HETATM 3372 O  O     . HOH   H 7 .   ? -11.23700 -23.15800 -27.25600 1.000 41.56721 ? 453 HOH   D O     1 
HETATM 3373 O  O     . HOH   H 7 .   ? 4.01400   1.50300   -44.68400 1.000 46.20365 ? 454 HOH   D O     1 
HETATM 3374 O  O     . HOH   H 7 .   ? -21.31500 2.94100   -23.03800 1.000 20.36295 ? 455 HOH   D O     1 
HETATM 3375 O  O     . HOH   H 7 .   ? -18.12600 -10.08700 -13.90600 1.000 44.82987 ? 456 HOH   D O     1 
HETATM 3376 O  O     . HOH   H 7 .   ? -12.73100 -22.93600 -31.59400 1.000 44.96431 ? 457 HOH   D O     1 
HETATM 3377 O  O     . HOH   H 7 .   ? 6.10700   -7.18800  -28.96800 1.000 50.38608 ? 458 HOH   D O     1 
HETATM 3378 O  O     . HOH   H 7 .   ? -18.46500 -18.55900 -27.31900 1.000 46.29321 ? 459 HOH   D O     1 
HETATM 3379 O  O     . HOH   H 7 .   ? -13.10800 -23.38200 -22.82400 1.000 58.85721 ? 460 HOH   D O     1 
HETATM 3380 O  O     . HOH   H 7 .   ? -24.51600 15.29800  -31.13300 1.000 54.53979 ? 461 HOH   D O     1 
HETATM 3381 O  O     . HOH   H 7 .   ? -12.16500 -27.10400 -30.20600 1.000 38.98635 ? 462 HOH   D O     1 
HETATM 3382 O  O     . HOH   H 7 .   ? -2.93100  20.19900  -31.43400 1.000 44.92198 ? 463 HOH   D O     1 
HETATM 3383 O  O     . HOH   H 7 .   ? -9.74600  15.08800  -27.75800 1.000 45.91060 ? 464 HOH   D O     1 
HETATM 3384 O  O     . HOH   H 7 .   ? -21.77100 -15.79100 -28.66900 1.000 39.30855 ? 465 HOH   D O     1 
HETATM 3385 O  O     . HOH   H 7 .   ? 0.42700   2.94400   -13.21000 1.000 49.27594 ? 466 HOH   D O     1 
HETATM 3386 O  O     . HOH   H 7 .   ? -11.02400 3.68200   -49.11500 1.000 44.43106 ? 467 HOH   D O     1 
HETATM 3387 O  O     . HOH   H 7 .   ? -23.64200 4.43600   -36.83600 1.000 32.20640 ? 468 HOH   D O     1 
HETATM 3388 O  O     . HOH   H 7 .   ? 3.57100   14.48800  -19.57900 1.000 46.00234 ? 469 HOH   D O     1 
HETATM 3389 O  O     . HOH   H 7 .   ? -15.72400 -19.97200 -22.74700 1.000 27.26159 ? 470 HOH   D O     1 
HETATM 3390 O  O     . HOH   H 7 .   ? 3.45600   5.31600   -14.95700 1.000 46.53692 ? 471 HOH   D O     1 
HETATM 3391 O  O     . HOH   H 7 .   ? -15.24600 -16.02100 -14.54800 1.000 20.87229 ? 472 HOH   D O     1 
HETATM 3392 O  O     . HOH   H 7 .   ? -15.10200 -2.46800  -44.62900 1.000 44.30653 ? 473 HOH   D O     1 
HETATM 3393 O  O     . HOH   H 7 .   ? -11.64200 -11.76500 -43.72500 1.000 43.96908 ? 474 HOH   D O     1 
HETATM 3394 O  O     . HOH   H 7 .   ? -6.30900  -7.91600  -46.26500 1.000 20.87929 ? 475 HOH   D O     1 
HETATM 3395 O  O     . HOH   H 7 .   ? -2.11400  2.56700   -45.15000 1.000 31.87499 ? 476 HOH   D O     1 
HETATM 3396 O  O     . HOH   H 7 .   ? 2.67100   17.15200  -20.14900 1.000 31.08711 ? 477 HOH   D O     1 
HETATM 3397 O  O     . HOH   H 7 .   ? -0.73100  -12.48100 -14.99400 1.000 29.43968 ? 478 HOH   D O     1 
HETATM 3398 O  O     . HOH   H 7 .   ? -2.37200  -22.92800 -31.21700 1.000 41.57164 ? 479 HOH   D O     1 
HETATM 3399 O  O     . HOH   H 7 .   ? -1.65300  2.87800   -10.90400 1.000 51.86315 ? 480 HOH   D O     1 
HETATM 3400 O  O     . HOH   H 7 .   ? -0.20200  -10.88800 -13.11000 1.000 44.47330 ? 481 HOH   D O     1 
HETATM 3401 O  O     . HOH   H 7 .   ? -0.12300  1.79000   -47.10000 1.000 43.62957 ? 482 HOH   D O     1 
HETATM 3402 O  O     . HOH   H 7 .   ? -13.73600 -20.86800 -32.54300 1.000 39.19404 ? 483 HOH   D O     1 
HETATM 3403 O  O     . HOH   H 7 .   ? -14.32900 -25.10600 -30.50800 1.000 26.86548 ? 484 HOH   D O     1 
HETATM 3404 O  O     . HOH   H 7 .   ? -16.94200 -20.83800 -27.68300 1.000 41.15562 ? 485 HOH   D O     1 
HETATM 3405 O  O     . HOH   H 7 .   ? -14.32400 -19.35700 -39.19300 1.000 31.72247 ? 486 HOH   D O     1 
HETATM 3406 O  O     . HOH   H 7 .   ? -16.81200 -21.69800 -24.73000 1.000 40.78781 ? 487 HOH   D O     1 
HETATM 3407 O  O     . HOH   H 7 .   ? 5.29800   17.26500  -23.61700 1.000 50.21936 ? 488 HOH   D O     1 
HETATM 3408 O  O     . HOH   H 7 .   ? -4.02400  -17.28900 -49.26500 1.000 38.36777 ? 489 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   ? 0.54472 0.35193 0.38091 -0.11607 -0.05095 -0.02840 0   SER   A N     
2    C  CA    . SER   A 1   ? 0.53142 0.33850 0.37016 -0.12841 -0.04304 -0.02914 0   SER   A CA    
3    C  C     . SER   A 1   ? 0.45937 0.28883 0.33547 -0.10151 -0.01109 -0.02549 0   SER   A C     
4    O  O     . SER   A 1   ? 0.51207 0.33612 0.35819 -0.07553 -0.02647 -0.04357 0   SER   A O     
5    C  CB    . SER   A 1   ? 0.60937 0.37888 0.39590 -0.12097 -0.02783 -0.01436 0   SER   A CB    
6    O  OG    . SER   A 1   ? 0.66094 0.40529 0.41317 -0.10965 -0.01570 -0.00674 0   SER   A OG    
7    N  N     A MET   A 2   ? 0.39377 0.23480 0.30127 -0.09950 -0.00387 -0.00642 1   MET   A N     
8    N  N     B MET   A 2   ? 0.38519 0.23405 0.30398 -0.09548 0.00731  0.00015  1   MET   A N     
9    C  CA    A MET   A 2   ? 0.31713 0.18206 0.26452 -0.06928 0.00417  0.00440  1   MET   A CA    
10   C  CA    B MET   A 2   ? 0.29911 0.18069 0.27097 -0.05950 0.02611  0.01803  1   MET   A CA    
11   C  C     A MET   A 2   ? 0.24429 0.15769 0.22626 -0.03763 0.01965  0.00870  1   MET   A C     
12   C  C     B MET   A 2   ? 0.23215 0.15499 0.22764 -0.02996 0.03116  0.01515  1   MET   A C     
13   O  O     A MET   A 2   ? 0.24596 0.18046 0.23643 -0.02489 0.04403  0.01641  1   MET   A O     
14   O  O     B MET   A 2   ? 0.22883 0.17686 0.23548 -0.01344 0.05497  0.02214  1   MET   A O     
15   C  CB    A MET   A 2   ? 0.31132 0.16956 0.26928 -0.07892 -0.01477 0.00496  1   MET   A CB    
16   C  CB    B MET   A 2   ? 0.27864 0.17203 0.28435 -0.05591 0.02529  0.03340  1   MET   A CB    
17   C  CG    A MET   A 2   ? 0.28769 0.15639 0.27399 -0.04824 -0.02763 0.00350  1   MET   A CG    
18   C  CG    B MET   A 2   ? 0.23206 0.16389 0.29585 -0.02060 0.02550  0.04794  1   MET   A CG    
19   S  SD    A MET   A 2   ? 0.27026 0.14483 0.26972 -0.01917 -0.04012 0.00434  1   MET   A SD    
20   S  SD    B MET   A 2   ? 0.19954 0.15071 0.30118 0.01464  0.02539  0.05712  1   MET   A SD    
21   C  CE    A MET   A 2   ? 0.26732 0.14820 0.26556 -0.02774 -0.04408 0.00653  1   MET   A CE    
22   C  CE    B MET   A 2   ? 0.17877 0.16785 0.29932 0.00665  0.01707  0.06391  1   MET   A CE    
23   N  N     . THR   A 3   ? 0.22757 0.13628 0.18772 -0.01942 0.01881  -0.00279 2   THR   A N     
24   C  CA    . THR   A 3   ? 0.20279 0.13661 0.16755 -0.04872 0.02689  -0.00161 2   THR   A CA    
25   C  C     . THR   A 3   ? 0.14060 0.13470 0.17793 -0.02139 0.03027  0.00516  2   THR   A C     
26   O  O     . THR   A 3   ? 0.16760 0.13012 0.16733 -0.00029 0.02289  0.00757  2   THR   A O     
27   C  CB    . THR   A 3   ? 0.22327 0.17119 0.16429 -0.03564 0.03325  -0.00927 2   THR   A CB    
28   O  OG1   . THR   A 3   ? 0.23254 0.19225 0.16834 -0.03045 0.02971  -0.02114 2   THR   A OG1   
29   C  CG2   . THR   A 3   ? 0.22253 0.19244 0.16715 -0.04544 0.02778  0.01929  2   THR   A CG2   
30   N  N     A GLU   A 4   ? 0.15192 0.14212 0.18726 -0.02003 0.02750  -0.00161 3   GLU   A N     
31   N  N     B GLU   A 4   ? 0.13969 0.12482 0.18453 -0.03710 0.02902  -0.01263 3   GLU   A N     
32   C  CA    A GLU   A 4   ? 0.17278 0.14220 0.18940 -0.00856 0.02951  0.00514  3   GLU   A CA    
33   C  CA    B GLU   A 4   ? 0.15150 0.11088 0.18585 -0.03689 0.03451  -0.01434 3   GLU   A CA    
34   C  C     A GLU   A 4   ? 0.15740 0.13333 0.17880 -0.01228 0.01029  0.01785  3   GLU   A C     
35   C  C     B GLU   A 4   ? 0.14812 0.11701 0.17698 -0.02676 0.01374  0.00837  3   GLU   A C     
36   O  O     A GLU   A 4   ? 0.18089 0.16209 0.18655 -0.01867 -0.00972 0.02595  3   GLU   A O     
37   O  O     B GLU   A 4   ? 0.17503 0.14095 0.18573 -0.03916 -0.00297 0.01303  3   GLU   A O     
38   C  CB    A GLU   A 4   ? 0.23339 0.18687 0.20757 0.02541  0.04205  -0.00421 3   GLU   A CB    
39   C  CB    B GLU   A 4   ? 0.19121 0.13832 0.20231 -0.01354 0.04833  -0.04147 3   GLU   A CB    
40   C  CG    A GLU   A 4   ? 0.32403 0.24139 0.23518 0.07868  0.06255  -0.00409 3   GLU   A CG    
41   C  CG    B GLU   A 4   ? 0.27525 0.18800 0.23109 0.04222  0.07612  -0.05792 3   GLU   A CG    
42   C  CD    A GLU   A 4   ? 0.41203 0.29589 0.25604 0.08848  0.08630  -0.00710 3   GLU   A CD    
43   C  CD    B GLU   A 4   ? 0.34565 0.24280 0.25506 0.05829  0.09358  -0.07202 3   GLU   A CD    
44   O  OE1   A GLU   A 4   ? 0.44401 0.32400 0.27484 0.09906  0.07091  -0.00384 3   GLU   A OE1   
45   O  OE1   B GLU   A 4   ? 0.31762 0.27590 0.26517 0.07271  0.11307  -0.06685 3   GLU   A OE1   
46   O  OE2   A GLU   A 4   ? 0.42327 0.30697 0.24996 0.09056  0.11726  -0.01545 3   GLU   A OE2   
47   O  OE2   B GLU   A 4   ? 0.39577 0.24948 0.26394 0.08338  0.08398  -0.09504 3   GLU   A OE2   
48   N  N     . TYR   A 5   ? 0.14545 0.09143 0.17158 -0.01723 0.01084  0.00201  4   TYR   A N     
49   C  CA    . TYR   A 5   ? 0.15524 0.10092 0.15929 -0.02566 0.01743  0.00339  4   TYR   A CA    
50   C  C     . TYR   A 5   ? 0.15452 0.09383 0.15928 -0.02853 0.01172  0.01320  4   TYR   A C     
51   O  O     . TYR   A 5   ? 0.20607 0.10934 0.16172 -0.01244 -0.00625 0.01110  4   TYR   A O     
52   C  CB    . TYR   A 5   ? 0.15534 0.12849 0.16302 -0.01793 0.03739  -0.01825 4   TYR   A CB    
53   C  CG    . TYR   A 5   ? 0.14758 0.12270 0.16341 -0.01095 0.03917  -0.02004 4   TYR   A CG    
54   C  CD1   . TYR   A 5   ? 0.17120 0.16501 0.18287 -0.02399 0.05101  -0.02395 4   TYR   A CD1   
55   C  CD2   . TYR   A 5   ? 0.15908 0.12869 0.17944 0.00081  0.03167  -0.02014 4   TYR   A CD2   
56   C  CE1   . TYR   A 5   ? 0.16796 0.16303 0.19546 -0.03410 0.04324  -0.03405 4   TYR   A CE1   
57   C  CE2   . TYR   A 5   ? 0.17380 0.14878 0.18217 -0.01091 0.03404  -0.03746 4   TYR   A CE2   
58   C  CZ    . TYR   A 5   ? 0.16779 0.15505 0.19798 -0.03553 0.06706  -0.05053 4   TYR   A CZ    
59   O  OH    . TYR   A 5   ? 0.22094 0.18788 0.22169 -0.04663 0.08113  -0.07617 4   TYR   A OH    
60   N  N     . LYS   A 6   ? 0.13351 0.08799 0.16626 -0.01586 0.02264  0.02354  5   LYS   A N     
61   C  CA    . LYS   A 6   ? 0.12296 0.09838 0.17987 -0.01041 0.02590  0.01456  5   LYS   A CA    
62   C  C     . LYS   A 6   ? 0.14045 0.08873 0.13636 -0.00696 0.02137  0.01115  5   LYS   A C     
63   O  O     . LYS   A 6   ? 0.14614 0.10892 0.12262 0.00247  0.00863  0.01243  5   LYS   A O     
64   C  CB    . LYS   A 6   ? 0.11332 0.13591 0.22960 0.02348  0.02238  0.02373  5   LYS   A CB    
65   C  CG    . LYS   A 6   ? 0.13259 0.18794 0.27785 0.01773  0.03105  0.03864  5   LYS   A CG    
66   C  CD    . LYS   A 6   ? 0.14477 0.24094 0.32377 0.00965  0.02889  0.02559  5   LYS   A CD    
67   C  CE    . LYS   A 6   ? 0.16144 0.30147 0.35821 0.03921  0.02664  0.02437  5   LYS   A CE    
68   N  NZ    . LYS   A 6   ? 0.24754 0.32881 0.37817 0.04355  0.03959  0.02157  5   LYS   A NZ    
69   N  N     . LEU   A 7   ? 0.13859 0.09617 0.10960 -0.00157 0.02261  0.00217  6   LEU   A N     
70   C  CA    . LEU   A 7   ? 0.13025 0.08625 0.10548 -0.00863 0.02459  -0.00576 6   LEU   A CA    
71   C  C     . LEU   A 7   ? 0.15544 0.08294 0.09746 -0.00624 0.03171  0.01040  6   LEU   A C     
72   O  O     . LEU   A 7   ? 0.26286 0.09967 0.09635 -0.02786 0.05808  -0.01135 6   LEU   A O     
73   C  CB    . LEU   A 7   ? 0.13678 0.08735 0.11510 -0.00034 0.00386  -0.01524 6   LEU   A CB    
74   C  CG    . LEU   A 7   ? 0.13723 0.09600 0.12494 0.01138  0.00826  -0.02290 6   LEU   A CG    
75   C  CD1   . LEU   A 7   ? 0.13836 0.11336 0.14415 0.00222  0.00896  -0.01443 6   LEU   A CD1   
76   C  CD2   . LEU   A 7   ? 0.15796 0.10591 0.12981 -0.00553 0.02483  -0.02908 6   LEU   A CD2   
77   N  N     . VAL   A 8   ? 0.12804 0.08504 0.09671 -0.01802 0.02856  -0.00522 7   VAL   A N     
78   C  CA    . VAL   A 8   ? 0.11583 0.08535 0.09626 -0.00660 0.01478  -0.00730 7   VAL   A CA    
79   C  C     . VAL   A 8   ? 0.11324 0.09042 0.07777 0.00854  0.02381  -0.00713 7   VAL   A C     
80   O  O     . VAL   A 8   ? 0.12655 0.11555 0.08867 -0.00513 0.02570  -0.01076 7   VAL   A O     
81   C  CB    . VAL   A 8   ? 0.10808 0.09371 0.10461 0.00460  0.00598  0.00230  7   VAL   A CB    
82   C  CG1   . VAL   A 8   ? 0.13443 0.09295 0.11401 0.00665  0.00638  -0.00228 7   VAL   A CG1   
83   C  CG2   . VAL   A 8   ? 0.13168 0.11675 0.12880 -0.00838 -0.00566 -0.00780 7   VAL   A CG2   
84   N  N     . VAL   A 9   ? 0.10805 0.08805 0.08576 -0.00377 0.01903  -0.00617 8   VAL   A N     
85   C  CA    . VAL   A 9   ? 0.11146 0.08516 0.09076 -0.00690 0.01314  -0.00242 8   VAL   A CA    
86   C  C     . VAL   A 9   ? 0.09859 0.08350 0.07620 0.00994  0.02352  0.00272  8   VAL   A C     
87   O  O     . VAL   A 9   ? 0.11621 0.08543 0.08907 0.00259  0.03608  -0.00883 8   VAL   A O     
88   C  CB    . VAL   A 9   ? 0.10817 0.08877 0.09404 -0.00290 0.01269  -0.00067 8   VAL   A CB    
89   C  CG1   . VAL   A 9   ? 0.11387 0.09661 0.10056 0.00336  0.01413  -0.00506 8   VAL   A CG1   
90   C  CG2   . VAL   A 9   ? 0.13968 0.09151 0.10503 0.00140  0.01677  0.00467  8   VAL   A CG2   
91   N  N     . VAL   A 10  ? 0.09945 0.08779 0.08070 -0.00198 0.02794  -0.00321 9   VAL   A N     
92   C  CA    . VAL   A 10  ? 0.09354 0.09062 0.08689 -0.00123 0.02293  0.00250  9   VAL   A CA    
93   C  C     . VAL   A 10  ? 0.10706 0.08474 0.07645 0.00657  0.02580  -0.01230 9   VAL   A C     
94   O  O     . VAL   A 10  ? 0.10601 0.09865 0.08792 0.00438  0.03110  -0.00613 9   VAL   A O     
95   C  CB    . VAL   A 10  ? 0.08865 0.10796 0.08305 0.00723  0.03454  0.00136  9   VAL   A CB    
96   C  CG1   . VAL   A 10  ? 0.11699 0.11846 0.10359 0.01197  0.02027  -0.00231 9   VAL   A CG1   
97   C  CG2   . VAL   A 10  ? 0.13557 0.12352 0.07841 -0.00070 0.01569  0.00137  9   VAL   A CG2   
98   N  N     . GLY   A 11  ? 0.09686 0.08848 0.08403 -0.00635 0.02136  -0.00153 10  GLY   A N     
99   C  CA    . GLY   A 11  ? 0.10447 0.09324 0.09263 -0.01032 0.02463  -0.00750 10  GLY   A CA    
100  C  C     . GLY   A 11  ? 0.10767 0.07602 0.09455 0.00524  0.03009  0.00004  10  GLY   A C     
101  O  O     . GLY   A 11  ? 0.09585 0.09318 0.09507 -0.00303 0.03322  -0.00867 10  GLY   A O     
102  N  N     . ALA   A 12  ? 0.10637 0.09531 0.09285 0.00196  0.01540  -0.00644 11  ALA   A N     
103  C  CA    . ALA   A 12  ? 0.10885 0.09836 0.10313 -0.01221 0.02022  -0.00796 11  ALA   A CA    
104  C  C     . ALA   A 12  ? 0.09171 0.08767 0.11792 0.00616  0.02609  -0.02499 11  ALA   A C     
105  O  O     . ALA   A 12  ? 0.11810 0.09080 0.10597 -0.00062 0.02506  -0.01048 11  ALA   A O     
106  C  CB    . ALA   A 12  ? 0.12007 0.11533 0.12082 -0.01510 0.02193  -0.00268 11  ALA   A CB    
107  N  N     . CYS   A 13  ? 0.11443 0.08852 0.11227 0.01651  0.00410  -0.02021 12  CYS   A N     
108  C  CA    . CYS   A 13  ? 0.14140 0.09221 0.11263 0.03277  0.00364  -0.03500 12  CYS   A CA    
109  C  C     . CYS   A 13  ? 0.11886 0.09008 0.11043 0.00171  0.01407  -0.01443 12  CYS   A C     
110  O  O     . CYS   A 13  ? 0.11825 0.09882 0.11927 -0.01734 0.01095  0.00446  12  CYS   A O     
111  C  CB    . CYS   A 13  ? 0.18680 0.13698 0.16488 0.06480  0.01482  -0.03082 12  CYS   A CB    
112  S  SG    . CYS   A 13  ? 0.21743 0.16043 0.19708 0.06481  -0.01332 -0.06606 12  CYS   A SG    
113  N  N     . GLY   A 14  ? 0.11869 0.09206 0.09416 -0.00579 0.02264  -0.01777 13  GLY   A N     
114  C  CA    . GLY   A 14  ? 0.11691 0.09824 0.10334 0.01208  0.01399  -0.01414 13  GLY   A CA    
115  C  C     . GLY   A 14  ? 0.10562 0.11215 0.09832 0.00541  0.02975  -0.00683 13  GLY   A C     
116  O  O     . GLY   A 14  ? 0.11128 0.12478 0.11477 0.01791  0.00872  -0.02117 13  GLY   A O     
117  N  N     . VAL   A 15  ? 0.11111 0.10287 0.07526 -0.00332 0.02017  -0.01323 14  VAL   A N     
118  C  CA    . VAL   A 15  ? 0.10055 0.09690 0.08027 0.00366  0.02864  -0.01305 14  VAL   A CA    
119  C  C     . VAL   A 15  ? 0.10187 0.08568 0.07942 0.00841  0.02730  -0.00829 14  VAL   A C     
120  O  O     . VAL   A 15  ? 0.11848 0.08757 0.08872 0.00614  0.02292  -0.00771 14  VAL   A O     
121  C  CB    . VAL   A 15  ? 0.12167 0.09566 0.08666 -0.00338 0.03059  -0.00601 14  VAL   A CB    
122  C  CG1   . VAL   A 15  ? 0.11751 0.09275 0.11058 -0.00006 0.03589  0.00255  14  VAL   A CG1   
123  C  CG2   . VAL   A 15  ? 0.12247 0.11395 0.09246 0.00011  0.01112  -0.00905 14  VAL   A CG2   
124  N  N     . GLY   A 16  ? 0.11428 0.08699 0.08199 -0.01082 0.02603  0.00538  15  GLY   A N     
125  C  CA    . GLY   A 16  ? 0.10902 0.09581 0.08418 -0.00270 0.02384  0.01007  15  GLY   A CA    
126  C  C     . GLY   A 16  ? 0.10885 0.09207 0.08218 0.00915  0.02392  0.00442  15  GLY   A C     
127  O  O     . GLY   A 16  ? 0.12668 0.08588 0.09928 0.00394  0.03220  0.00322  15  GLY   A O     
128  N  N     . LYS   A 17  ? 0.09772 0.09772 0.08118 0.00470  0.03199  -0.00806 16  LYS   A N     
129  C  CA    . LYS   A 17  ? 0.09605 0.10579 0.07982 -0.00885 0.02212  -0.00009 16  LYS   A CA    
130  C  C     . LYS   A 17  ? 0.10906 0.08395 0.08664 0.00522  0.02803  0.00028  16  LYS   A C     
131  O  O     . LYS   A 17  ? 0.10466 0.09060 0.10112 -0.00322 0.02719  0.00041  16  LYS   A O     
132  C  CB    . LYS   A 17  ? 0.11654 0.10482 0.08330 0.00045  0.00640  0.00148  16  LYS   A CB    
133  C  CG    . LYS   A 17  ? 0.13906 0.10792 0.08722 -0.00281 0.02338  0.01109  16  LYS   A CG    
134  C  CD    . LYS   A 17  ? 0.13171 0.13470 0.11159 -0.00678 0.00207  0.02311  16  LYS   A CD    
135  C  CE    . LYS   A 17  ? 0.10460 0.13219 0.13612 0.00858  0.02745  0.02689  16  LYS   A CE    
136  N  NZ    . LYS   A 17  ? 0.09975 0.11179 0.10828 0.00916  0.02294  -0.01395 16  LYS   A NZ    
137  N  N     . SER   A 18  ? 0.10298 0.11156 0.07801 0.00567  0.02512  0.00750  17  SER   A N     
138  C  CA    . SER   A 18  ? 0.13290 0.10048 0.07136 0.01275  0.03051  0.00809  17  SER   A CA    
139  C  C     . SER   A 18  ? 0.12328 0.09940 0.07781 0.00225  0.02443  -0.01101 17  SER   A C     
140  O  O     . SER   A 18  ? 0.13190 0.09578 0.09910 -0.00138 0.03025  0.00724  17  SER   A O     
141  C  CB    . SER   A 18  ? 0.12820 0.10330 0.08091 0.02128  0.03617  -0.00143 17  SER   A CB    
142  O  OG    . SER   A 18  ? 0.12016 0.09805 0.08776 0.01053  0.03078  0.00027  17  SER   A OG    
143  N  N     . ALA   A 19  ? 0.12130 0.09773 0.08608 0.01791  0.02512  0.00273  18  ALA   A N     
144  C  CA    . ALA   A 19  ? 0.13248 0.10353 0.10171 0.01921  0.01693  0.00201  18  ALA   A CA    
145  C  C     . ALA   A 19  ? 0.10164 0.10047 0.09359 0.00302  0.01848  0.00572  18  ALA   A C     
146  O  O     . ALA   A 19  ? 0.13816 0.08006 0.09940 0.01242  0.02487  0.01277  18  ALA   A O     
147  C  CB    . ALA   A 19  ? 0.12021 0.12171 0.12375 -0.00340 0.01571  0.00061  18  ALA   A CB    
148  N  N     . LEU   A 20  ? 0.11898 0.09222 0.09191 0.00634  0.01662  -0.00078 19  LEU   A N     
149  C  CA    . LEU   A 20  ? 0.13543 0.10105 0.08500 -0.00645 0.03340  0.00318  19  LEU   A CA    
150  C  C     . LEU   A 20  ? 0.13521 0.09065 0.09653 0.00069  0.04866  0.00307  19  LEU   A C     
151  O  O     . LEU   A 20  ? 0.14737 0.08750 0.11400 -0.01014 0.03513  0.01224  19  LEU   A O     
152  C  CB    . LEU   A 20  ? 0.14956 0.11369 0.09514 -0.00478 0.04904  -0.00105 19  LEU   A CB    
153  C  CG    . LEU   A 20  ? 0.12148 0.10464 0.11238 0.00520  0.04046  0.00745  19  LEU   A CG    
154  C  CD1   . LEU   A 20  ? 0.16011 0.13109 0.09830 -0.01824 0.03710  0.02440  19  LEU   A CD1   
155  C  CD2   . LEU   A 20  ? 0.15227 0.10277 0.13878 0.01975  0.05614  -0.01379 19  LEU   A CD2   
156  N  N     . THR   A 21  ? 0.11605 0.11094 0.09321 -0.00771 0.04743  0.00934  20  THR   A N     
157  C  CA    . THR   A 21  ? 0.12412 0.10853 0.10293 -0.00251 0.04350  0.00825  20  THR   A CA    
158  C  C     . THR   A 21  ? 0.13952 0.10849 0.09896 -0.01058 0.04139  0.02175  20  THR   A C     
159  O  O     . THR   A 21  ? 0.15117 0.10786 0.12925 -0.00899 0.03609  0.01919  20  THR   A O     
160  C  CB    . THR   A 21  ? 0.11589 0.13655 0.11540 0.00628  0.03683  0.02767  20  THR   A CB    
161  O  OG1   . THR   A 21  ? 0.13713 0.14515 0.11039 -0.00639 0.02419  0.02243  20  THR   A OG1   
162  C  CG2   . THR   A 21  ? 0.12919 0.15575 0.14469 -0.00625 0.03779  0.03758  20  THR   A CG2   
163  N  N     . ILE   A 22  ? 0.14901 0.12280 0.08390 -0.00302 0.03388  0.01742  21  ILE   A N     
164  C  CA    . ILE   A 22  ? 0.17271 0.13020 0.09470 0.01057  0.04569  0.02034  21  ILE   A CA    
165  C  C     . ILE   A 22  ? 0.17497 0.13124 0.10871 0.00576  0.03931  0.02787  21  ILE   A C     
166  O  O     . ILE   A 22  ? 0.17143 0.12751 0.12373 -0.00284 0.03617  0.04224  21  ILE   A O     
167  C  CB    . ILE   A 22  ? 0.19453 0.15291 0.09963 0.01571  0.03960  0.01419  21  ILE   A CB    
168  C  CG1   . ILE   A 22  ? 0.19212 0.16695 0.13978 0.01162  0.05982  0.00850  21  ILE   A CG1   
169  C  CG2   . ILE   A 22  ? 0.25968 0.16358 0.10709 -0.00513 0.02487  0.02804  21  ILE   A CG2   
170  C  CD1   . ILE   A 22  ? 0.27252 0.21691 0.18562 0.03694  0.06300  0.00302  21  ILE   A CD1   
171  N  N     . GLN   A 23  ? 0.13844 0.11733 0.11464 0.00899  0.03081  0.01464  22  GLN   A N     
172  C  CA    . GLN   A 23  ? 0.17611 0.12996 0.13567 0.01916  0.02366  0.01648  22  GLN   A CA    
173  C  C     . GLN   A 23  ? 0.20653 0.11556 0.14633 -0.00188 -0.00284 0.00194  22  GLN   A C     
174  O  O     . GLN   A 23  ? 0.21864 0.12534 0.18688 0.00358  0.00436  0.02438  22  GLN   A O     
175  C  CB    . GLN   A 23  ? 0.17231 0.15610 0.14076 0.01794  0.05759  0.01457  22  GLN   A CB    
176  C  CG    . GLN   A 23  ? 0.18558 0.15366 0.14902 0.00478  0.03861  0.02833  22  GLN   A CG    
177  C  CD    . GLN   A 23  ? 0.18432 0.16924 0.15174 -0.00244 0.05678  0.05768  22  GLN   A CD    
178  O  OE1   . GLN   A 23  ? 0.20107 0.20756 0.17856 -0.00668 0.02370  0.05753  22  GLN   A OE1   
179  N  NE2   . GLN   A 23  ? 0.18020 0.17255 0.13743 -0.01100 0.03629  0.02211  22  GLN   A NE2   
180  N  N     . LEU   A 24  ? 0.19197 0.11384 0.13211 -0.00523 0.00520  -0.00938 23  LEU   A N     
181  C  CA    . LEU   A 24  ? 0.21902 0.13899 0.13694 0.00126  -0.01009 0.00104  23  LEU   A CA    
182  C  C     . LEU   A 24  ? 0.22381 0.13177 0.15920 -0.03889 0.00531  0.03755  23  LEU   A C     
183  O  O     . LEU   A 24  ? 0.26062 0.12562 0.19808 -0.03507 -0.00973 0.03444  23  LEU   A O     
184  C  CB    . LEU   A 24  ? 0.23069 0.15582 0.13122 -0.00501 -0.00790 -0.00563 23  LEU   A CB    
185  C  CG    . LEU   A 24  ? 0.30237 0.19210 0.15922 -0.04743 -0.00682 -0.00949 23  LEU   A CG    
186  C  CD1   . LEU   A 24  ? 0.37126 0.19196 0.16954 -0.01996 -0.01109 -0.03461 23  LEU   A CD1   
187  C  CD2   . LEU   A 24  ? 0.31923 0.24184 0.16136 -0.07444 0.00196  0.00363  23  LEU   A CD2   
188  N  N     . ILE   A 25  ? 0.21775 0.16507 0.15204 -0.05322 -0.00038 0.04410  24  ILE   A N     
189  C  CA    . ILE   A 25  ? 0.20765 0.18141 0.15971 -0.05338 0.01376  0.06749  24  ILE   A CA    
190  C  C     . ILE   A 25  ? 0.23349 0.19877 0.15990 -0.05953 0.00524  0.08744  24  ILE   A C     
191  O  O     . ILE   A 25  ? 0.25865 0.21641 0.17999 -0.06414 0.02364  0.09598  24  ILE   A O     
192  C  CB    . ILE   A 25  ? 0.19662 0.20205 0.17679 -0.02432 0.02637  0.05135  24  ILE   A CB    
193  C  CG1   . ILE   A 25  ? 0.21013 0.20852 0.18351 -0.04869 0.02096  0.04179  24  ILE   A CG1   
194  C  CG2   . ILE   A 25  ? 0.21957 0.22808 0.19641 -0.04488 0.04012  0.04565  24  ILE   A CG2   
195  C  CD1   . ILE   A 25  ? 0.25009 0.18183 0.18408 -0.03831 0.02837  0.02151  24  ILE   A CD1   
196  N  N     . GLN   A 26  ? 0.21179 0.23287 0.15888 -0.06895 -0.01678 0.06553  25  GLN   A N     
197  C  CA    . GLN   A 26  ? 0.20950 0.23540 0.15762 -0.02794 -0.00414 0.06658  25  GLN   A CA    
198  C  C     . GLN   A 26  ? 0.24538 0.20570 0.16625 -0.02717 0.01283  0.07545  25  GLN   A C     
199  O  O     . GLN   A 26  ? 0.27943 0.24962 0.17072 -0.01529 -0.00808 0.08682  25  GLN   A O     
200  C  CB    . GLN   A 26  ? 0.22095 0.25902 0.15612 -0.02627 0.01322  0.06082  25  GLN   A CB    
201  C  CG    . GLN   A 26  ? 0.24257 0.28921 0.16742 -0.01387 0.02518  0.05256  25  GLN   A CG    
202  C  CD    . GLN   A 26  ? 0.22424 0.33907 0.16836 0.01768  0.02536  0.04139  25  GLN   A CD    
203  O  OE1   . GLN   A 26  ? 0.24106 0.35047 0.17522 0.00685  0.03539  0.02798  25  GLN   A OE1   
204  N  NE2   . GLN   A 26  ? 0.24002 0.36802 0.17877 0.03783  0.02876  0.04398  25  GLN   A NE2   
205  N  N     . ASN   A 27  ? 0.21850 0.20547 0.18769 -0.01448 0.00545  0.05824  26  ASN   A N     
206  C  CA    . ASN   A 27  ? 0.25588 0.16755 0.19539 -0.03834 -0.01423 0.05863  26  ASN   A CA    
207  C  C     . ASN   A 27  ? 0.26655 0.15251 0.17173 -0.01919 -0.00909 0.05444  26  ASN   A C     
208  O  O     . ASN   A 27  ? 0.31092 0.14786 0.19913 -0.00319 -0.03426 0.04404  26  ASN   A O     
209  C  CB    . ASN   A 27  ? 0.36028 0.18445 0.22296 -0.05964 -0.01459 0.05052  26  ASN   A CB    
210  C  CG    . ASN   A 27  ? 0.45083 0.21945 0.25040 -0.10716 -0.00580 0.04006  26  ASN   A CG    
211  O  OD1   . ASN   A 27  ? 0.52093 0.23274 0.27037 -0.07310 0.00185  0.05169  26  ASN   A OD1   
212  N  ND2   . ASN   A 27  ? 0.46086 0.29698 0.27681 -0.11416 -0.01432 -0.00011 26  ASN   A ND2   
213  N  N     . HIS   A 28  ? 0.24391 0.14699 0.14880 -0.00163 0.02170  0.04554  27  HIS   A N     
214  C  CA    . HIS   A 28  ? 0.25161 0.15235 0.12687 -0.00323 0.04099  0.03649  27  HIS   A CA    
215  C  C     . HIS   A 28  ? 0.22990 0.14141 0.12069 0.01538  0.04101  0.02842  27  HIS   A C     
216  O  O     . HIS   A 28  ? 0.22302 0.13566 0.12503 0.00218  0.02654  0.02603  27  HIS   A O     
217  C  CB    . HIS   A 28  ? 0.31570 0.20167 0.14709 -0.03605 0.05501  0.04144  27  HIS   A CB    
218  C  CG    . HIS   A 28  ? 0.36649 0.23761 0.16541 -0.05761 0.09378  0.01404  27  HIS   A CG    
219  N  ND1   . HIS   A 28  ? 0.38832 0.28272 0.18079 -0.07160 0.09281  -0.02384 27  HIS   A ND1   
220  C  CD2   . HIS   A 28  ? 0.34154 0.25643 0.16580 -0.08568 0.07840  -0.00165 27  HIS   A CD2   
221  C  CE1   . HIS   A 28  ? 0.35727 0.26341 0.16612 -0.08056 0.09912  -0.03027 27  HIS   A CE1   
222  N  NE2   . HIS   A 28  ? 0.39719 0.27481 0.16881 -0.04763 0.08354  -0.00885 27  HIS   A NE2   
223  N  N     A PHE   A 29  ? 0.24047 0.13254 0.11553 -0.01917 0.04363  0.02570  28  PHE   A N     
224  N  N     B PHE   A 29  ? 0.22593 0.16311 0.12038 0.00406  0.04411  0.00644  28  PHE   A N     
225  C  CA    A PHE   A 29  ? 0.23339 0.12203 0.09675 -0.01629 0.03587  0.02619  28  PHE   A CA    
226  C  CA    B PHE   A 29  ? 0.21323 0.18824 0.10854 0.00073  0.03015  -0.00549 28  PHE   A CA    
227  C  C     A PHE   A 29  ? 0.26446 0.12070 0.08830 -0.00312 0.05850  0.00142  28  PHE   A C     
228  C  C     B PHE   A 29  ? 0.25993 0.22761 0.12303 -0.00164 0.02800  -0.03318 28  PHE   A C     
229  O  O     A PHE   A 29  ? 0.32085 0.15190 0.10131 -0.01301 0.06226  -0.00783 28  PHE   A O     
230  O  O     B PHE   A 29  ? 0.26904 0.24823 0.11474 0.00833  0.01089  -0.05368 28  PHE   A O     
231  C  CB    A PHE   A 29  ? 0.20959 0.12450 0.10243 -0.01952 0.03333  0.01633  28  PHE   A CB    
232  C  CB    B PHE   A 29  ? 0.17460 0.18357 0.08592 -0.00355 0.02113  -0.01520 28  PHE   A CB    
233  C  CG    A PHE   A 29  ? 0.17584 0.12035 0.11118 -0.00658 0.02535  0.02022  28  PHE   A CG    
234  C  CG    B PHE   A 29  ? 0.19601 0.17423 0.08378 0.01499  0.02216  -0.02829 28  PHE   A CG    
235  C  CD1   A PHE   A 29  ? 0.15868 0.12260 0.11250 0.01337  0.01941  0.03527  28  PHE   A CD1   
236  C  CD1   B PHE   A 29  ? 0.21300 0.17387 0.08955 0.02800  0.03185  -0.02034 28  PHE   A CD1   
237  C  CD2   A PHE   A 29  ? 0.21135 0.13125 0.13025 -0.00385 0.02047  0.01689  28  PHE   A CD2   
238  C  CD2   B PHE   A 29  ? 0.22319 0.19233 0.09854 0.01209  0.03537  -0.03623 28  PHE   A CD2   
239  C  CE1   A PHE   A 29  ? 0.15090 0.13245 0.12136 0.00330  0.01187  0.03426  28  PHE   A CE1   
240  C  CE1   B PHE   A 29  ? 0.20064 0.19025 0.09431 0.01021  0.03972  -0.02272 28  PHE   A CE1   
241  C  CE2   A PHE   A 29  ? 0.20562 0.13238 0.12924 0.01362  0.02179  0.02365  28  PHE   A CE2   
242  C  CE2   B PHE   A 29  ? 0.22866 0.19684 0.09686 0.01748  0.03986  -0.02984 28  PHE   A CE2   
243  C  CZ    A PHE   A 29  ? 0.17493 0.13671 0.12566 0.00299  0.01739  0.03033  28  PHE   A CZ    
244  C  CZ    B PHE   A 29  ? 0.20670 0.20059 0.09527 0.00517  0.03732  -0.02278 28  PHE   A CZ    
245  N  N     A VAL   A 30  ? 0.24409 0.12663 0.10007 -0.01006 0.06920  -0.01977 29  VAL   A N     
246  N  N     B VAL   A 30  ? 0.28328 0.24953 0.13331 0.00987  0.03612  -0.04881 29  VAL   A N     
247  C  CA    A VAL   A 30  ? 0.29688 0.14252 0.12538 -0.02623 0.07800  -0.02033 29  VAL   A CA    
248  C  CA    B VAL   A 30  ? 0.31282 0.27036 0.15550 0.03067  0.02414  -0.05960 29  VAL   A CA    
249  C  C     A VAL   A 30  ? 0.27141 0.12627 0.12092 -0.00454 0.05120  -0.02122 29  VAL   A C     
250  C  C     B VAL   A 30  ? 0.32232 0.25598 0.17194 0.05345  0.01388  -0.05893 29  VAL   A C     
251  O  O     A VAL   A 30  ? 0.27379 0.14079 0.10793 -0.02199 0.05059  -0.02013 29  VAL   A O     
252  O  O     B VAL   A 30  ? 0.34378 0.24969 0.16915 0.03643  0.01375  -0.05873 29  VAL   A O     
253  C  CB    A VAL   A 30  ? 0.34635 0.16535 0.15746 -0.03905 0.10851  -0.02849 29  VAL   A CB    
254  C  CB    B VAL   A 30  ? 0.34202 0.30351 0.17056 -0.01862 0.04618  -0.07732 29  VAL   A CB    
255  C  CG1   A VAL   A 30  ? 0.37706 0.17367 0.17448 -0.04470 0.12586  -0.02099 29  VAL   A CG1   
256  C  CG1   B VAL   A 30  ? 0.33215 0.31461 0.16799 -0.04013 0.05209  -0.09103 29  VAL   A CG1   
257  C  CG2   A VAL   A 30  ? 0.34238 0.18430 0.16993 -0.02761 0.11672  -0.04243 29  VAL   A CG2   
258  C  CG2   B VAL   A 30  ? 0.36946 0.33484 0.18333 -0.04482 0.03782  -0.06552 29  VAL   A CG2   
259  N  N     A ASP   A 31  ? 0.22116 0.12259 0.14308 -0.03452 0.04679  -0.01398 30  ASP   A N     
260  N  N     B ASP   A 31  ? 0.33468 0.26130 0.19479 0.07136  -0.00664 -0.04705 30  ASP   A N     
261  C  CA    A ASP   A 31  ? 0.19801 0.15233 0.15472 0.02390  -0.00248 0.00357  30  ASP   A CA    
262  C  CA    B ASP   A 31  ? 0.32854 0.27306 0.21449 0.04898  -0.02843 -0.04190 30  ASP   A CA    
263  C  C     A ASP   A 31  ? 0.20114 0.16030 0.15636 0.03064  -0.00046 0.00552  30  ASP   A C     
264  C  C     B ASP   A 31  ? 0.30069 0.24356 0.20891 0.05636  -0.01566 -0.03564 30  ASP   A C     
265  O  O     A ASP   A 31  ? 0.20133 0.17375 0.09896 -0.02151 -0.03011 -0.00101 30  ASP   A O     
266  O  O     B ASP   A 31  ? 0.31107 0.27013 0.20961 0.01577  -0.02803 -0.05040 30  ASP   A O     
267  C  CB    A ASP   A 31  ? 0.20256 0.17676 0.18057 0.00992  -0.03713 0.00816  30  ASP   A CB    
268  C  CB    B ASP   A 31  ? 0.37445 0.31147 0.24450 0.03256  -0.03073 -0.04020 30  ASP   A CB    
269  C  CG    A ASP   A 31  ? 0.25193 0.22921 0.20775 0.01930  -0.04324 0.00964  30  ASP   A CG    
270  C  CG    B ASP   A 31  ? 0.42310 0.35001 0.27074 0.00108  -0.03699 -0.04649 30  ASP   A CG    
271  O  OD1   A ASP   A 31  ? 0.23288 0.23446 0.22647 0.01915  -0.03489 -0.01406 30  ASP   A OD1   
272  O  OD1   B ASP   A 31  ? 0.48125 0.36429 0.29319 -0.00381 -0.01487 -0.04630 30  ASP   A OD1   
273  O  OD2   A ASP   A 31  ? 0.29189 0.27486 0.22819 0.04539  -0.04383 0.03597  30  ASP   A OD2   
274  O  OD2   B ASP   A 31  ? 0.39349 0.35514 0.26620 -0.01886 -0.05764 -0.04810 30  ASP   A OD2   
275  N  N     . GLU   A 32  ? 0.28230 0.20591 0.22714 0.06800  0.01794  -0.01810 31  GLU   A N     
276  C  CA    . GLU   A 32  ? 0.24372 0.23211 0.27953 0.06854  -0.00784 -0.05396 31  GLU   A CA    
277  C  C     . GLU   A 32  ? 0.22070 0.21885 0.29780 0.04178  -0.03447 -0.10201 31  GLU   A C     
278  O  O     . GLU   A 32  ? 0.21786 0.25400 0.31784 0.01013  -0.03424 -0.10621 31  GLU   A O     
279  C  CB    . GLU   A 32  ? 0.30504 0.28640 0.31028 0.06685  0.02422  -0.05308 31  GLU   A CB    
280  C  CG    . GLU   A 32  ? 0.36231 0.34504 0.34415 0.06563  0.05528  -0.04075 31  GLU   A CG    
281  C  CD    . GLU   A 32  ? 0.40844 0.40680 0.37258 0.04228  0.08204  -0.02543 31  GLU   A CD    
282  O  OE1   . GLU   A 32  ? 0.43592 0.41266 0.39048 0.03629  0.10164  -0.02846 31  GLU   A OE1   
283  O  OE2   . GLU   A 32  ? 0.43837 0.43308 0.37707 0.04179  0.09965  -0.01066 31  GLU   A OE2   
284  N  N     . TYR   A 33  ? 0.18367 0.22234 0.30597 0.07595  -0.08358 -0.09288 32  TYR   A N     
285  C  CA    . TYR   A 33  ? 0.22730 0.21943 0.29994 0.07508  -0.07504 -0.10405 32  TYR   A CA    
286  C  C     . TYR   A 33  ? 0.21613 0.25876 0.26338 0.09361  -0.08306 -0.12944 32  TYR   A C     
287  O  O     . TYR   A 33  ? 0.28100 0.33119 0.31483 0.11402  -0.08143 -0.17430 32  TYR   A O     
288  C  CB    . TYR   A 33  ? 0.26136 0.20675 0.32221 0.05191  -0.09167 -0.08003 32  TYR   A CB    
289  C  CG    . TYR   A 33  ? 0.25173 0.19619 0.31416 0.03990  -0.10267 -0.08155 32  TYR   A CG    
290  C  CD1   . TYR   A 33  ? 0.17304 0.19591 0.28947 0.05512  -0.05653 -0.10319 32  TYR   A CD1   
291  C  CD2   . TYR   A 33  ? 0.26384 0.20785 0.33140 0.03944  -0.11463 -0.05245 32  TYR   A CD2   
292  C  CE1   . TYR   A 33  ? 0.16797 0.17968 0.29298 0.03215  -0.01406 -0.11098 32  TYR   A CE1   
293  C  CE2   . TYR   A 33  ? 0.23102 0.19510 0.32850 0.01695  -0.10274 -0.05682 32  TYR   A CE2   
294  C  CZ    . TYR   A 33  ? 0.16709 0.18451 0.31727 0.01039  -0.06680 -0.05634 32  TYR   A CZ    
295  O  OH    . TYR   A 33  ? 0.20998 0.16473 0.31901 -0.00463 -0.07771 -0.04363 32  TYR   A OH    
296  N  N     . ASP   A 34  ? 0.18999 0.22361 0.18639 0.09476  -0.03854 -0.08379 33  ASP   A N     
297  C  CA    . ASP   A 34  ? 0.24073 0.22769 0.16408 0.09900  -0.03274 -0.03378 33  ASP   A CA    
298  C  C     . ASP   A 34  ? 0.19270 0.17474 0.11424 0.04258  0.00679  -0.04436 33  ASP   A C     
299  O  O     . ASP   A 34  ? 0.17065 0.14208 0.11479 0.03514  0.03917  -0.00661 33  ASP   A O     
300  C  CB    . ASP   A 34  ? 0.37742 0.24346 0.21053 0.09226  -0.05397 0.01332  33  ASP   A CB    
301  C  CG    . ASP   A 34  ? 0.56905 0.26976 0.24762 0.05350  -0.01596 0.01605  33  ASP   A CG    
302  O  OD1   . ASP   A 34  ? 0.62214 0.25740 0.25007 0.06102  -0.02436 0.03184  33  ASP   A OD1   
303  O  OD2   . ASP   A 34  ? 0.64102 0.29743 0.26871 0.03793  -0.00511 0.03202  33  ASP   A OD2   
304  N  N     . PRO   A 35  ? 0.17920 0.17008 0.12013 0.04435  -0.00756 -0.06946 34  PRO   A N     
305  C  CA    . PRO   A 35  ? 0.14375 0.14395 0.13692 0.01956  -0.02338 -0.04467 34  PRO   A CA    
306  C  C     . PRO   A 35  ? 0.13424 0.13529 0.11394 0.00568  0.01450  -0.02985 34  PRO   A C     
307  O  O     . PRO   A 35  ? 0.15817 0.20890 0.10912 0.00876  0.02695  -0.04180 34  PRO   A O     
308  C  CB    . PRO   A 35  ? 0.16978 0.14736 0.18473 0.01326  -0.04590 -0.05777 34  PRO   A CB    
309  C  CG    . PRO   A 35  ? 0.22805 0.17096 0.19131 0.03392  -0.05316 -0.06143 34  PRO   A CG    
310  C  CD    . PRO   A 35  ? 0.20119 0.19565 0.15940 0.05352  -0.06038 -0.06197 34  PRO   A CD    
311  N  N     . THR   A 36  ? 0.11751 0.10004 0.09932 0.00360  0.01854  -0.01360 35  THR   A N     
312  C  CA    . THR   A 36  ? 0.10846 0.09947 0.10071 0.01423  0.02632  -0.01272 35  THR   A CA    
313  C  C     . THR   A 36  ? 0.10712 0.09709 0.10076 -0.01003 0.03236  -0.01782 35  THR   A C     
314  O  O     . THR   A 36  ? 0.10488 0.09736 0.09460 -0.00198 0.02987  -0.01833 35  THR   A O     
315  C  CB    . THR   A 36  ? 0.10549 0.09239 0.10728 0.00436  0.02590  -0.02265 35  THR   A CB    
316  O  OG1   . THR   A 36  ? 0.11989 0.10878 0.10458 0.01559  0.03507  -0.00801 35  THR   A OG1   
317  C  CG2   . THR   A 36  ? 0.11016 0.13372 0.13093 -0.00425 0.03157  -0.03541 35  THR   A CG2   
318  N  N     . ILE   A 37  ? 0.10988 0.08863 0.10397 0.00390  0.02931  -0.01696 36  ILE   A N     
319  C  CA    . ILE   A 37  ? 0.10254 0.10540 0.10528 0.01341  0.03213  -0.02114 36  ILE   A CA    
320  C  C     . ILE   A 37  ? 0.11421 0.09217 0.09928 0.00248  0.03854  -0.00637 36  ILE   A C     
321  O  O     . ILE   A 37  ? 0.12564 0.10007 0.09970 -0.00162 0.02841  -0.00720 36  ILE   A O     
322  C  CB    . ILE   A 37  ? 0.11568 0.10519 0.12085 0.00486  0.03195  -0.01728 36  ILE   A CB    
323  C  CG1   . ILE   A 37  ? 0.14339 0.11045 0.12964 0.00783  0.04173  -0.04078 36  ILE   A CG1   
324  C  CG2   . ILE   A 37  ? 0.12342 0.11848 0.11707 0.01827  0.03247  -0.00162 36  ILE   A CG2   
325  C  CD1   . ILE   A 37  ? 0.16169 0.11738 0.15066 -0.00711 0.05882  -0.03266 36  ILE   A CD1   
326  N  N     . GLU   A 38  ? 0.11222 0.09083 0.10867 0.01007  0.03787  -0.01083 37  GLU   A N     
327  C  CA    . GLU   A 38  ? 0.11594 0.09194 0.10368 -0.00859 0.02874  -0.00325 37  GLU   A CA    
328  C  C     . GLU   A 38  ? 0.11546 0.08988 0.11118 -0.00069 0.04237  -0.01928 37  GLU   A C     
329  O  O     . GLU   A 38  ? 0.14681 0.10486 0.11663 0.01622  0.05826  -0.00585 37  GLU   A O     
330  C  CB    . GLU   A 38  ? 0.11902 0.10208 0.11834 -0.00927 0.02014  -0.00725 37  GLU   A CB    
331  C  CG    . GLU   A 38  ? 0.14781 0.12561 0.14879 -0.01393 0.01155  -0.01322 37  GLU   A CG    
332  C  CD    . GLU   A 38  ? 0.14861 0.11803 0.17137 0.00529  0.02785  -0.02757 37  GLU   A CD    
333  O  OE1   . GLU   A 38  ? 0.16248 0.13403 0.17057 -0.02868 0.04161  -0.00822 37  GLU   A OE1   
334  O  OE2   . GLU   A 38  ? 0.19356 0.12506 0.19887 0.00215  0.02544  -0.01855 37  GLU   A OE2   
335  N  N     . ASP   A 39  ? 0.14716 0.09120 0.11285 -0.00301 0.04503  -0.00251 38  ASP   A N     
336  C  CA    . ASP   A 39  ? 0.16430 0.09866 0.11637 -0.00498 0.04467  0.01014  38  ASP   A CA    
337  C  C     . ASP   A 39  ? 0.18359 0.08709 0.12446 -0.00066 0.06553  -0.00029 38  ASP   A C     
338  O  O     . ASP   A 39  ? 0.20523 0.11067 0.12935 -0.01860 0.08861  -0.01827 38  ASP   A O     
339  C  CB    . ASP   A 39  ? 0.20546 0.12767 0.12669 0.02191  0.04347  0.01334  38  ASP   A CB    
340  C  CG    . ASP   A 39  ? 0.21311 0.17916 0.14488 0.00425  0.03488  0.01225  38  ASP   A CG    
341  O  OD1   . ASP   A 39  ? 0.22997 0.20458 0.14453 0.02295  0.01973  0.00537  38  ASP   A OD1   
342  O  OD2   . ASP   A 39  ? 0.22257 0.21600 0.17322 -0.00608 0.00909  -0.00271 38  ASP   A OD2   
343  N  N     . SER   A 40  ? 0.17614 0.09192 0.13568 -0.01191 0.07421  -0.00102 39  SER   A N     
344  C  CA    . SER   A 40  ? 0.19492 0.09913 0.14885 -0.00385 0.05500  -0.00023 39  SER   A CA    
345  C  C     . SER   A 40  ? 0.19148 0.09403 0.13422 -0.01551 0.06552  0.00356  39  SER   A C     
346  O  O     . SER   A 40  ? 0.26955 0.10249 0.13745 0.01031  0.07849  0.00582  39  SER   A O     
347  C  CB    . SER   A 40  ? 0.19638 0.14952 0.19403 -0.01773 0.01892  0.03502  39  SER   A CB    
348  O  OG    . SER   A 40  ? 0.20577 0.20604 0.24468 -0.02596 -0.00007 0.07449  39  SER   A OG    
349  N  N     . TYR   A 41  ? 0.18416 0.09635 0.13859 -0.00015 0.05308  -0.00421 40  TYR   A N     
350  C  CA    . TYR   A 41  ? 0.21305 0.09726 0.14353 0.00813  0.05338  0.00292  40  TYR   A CA    
351  C  C     . TYR   A 41  ? 0.21798 0.10488 0.13187 -0.01077 0.07524  0.00437  40  TYR   A C     
352  O  O     . TYR   A 41  ? 0.26934 0.13412 0.13098 -0.03530 0.07013  0.01050  40  TYR   A O     
353  C  CB    . TYR   A 41  ? 0.20417 0.11957 0.15092 0.00843  0.02416  -0.00367 40  TYR   A CB    
354  C  CG    . TYR   A 41  ? 0.18411 0.14254 0.14699 0.00062  0.03661  -0.00235 40  TYR   A CG    
355  C  CD1   . TYR   A 41  ? 0.13677 0.14744 0.14607 0.00320  0.04147  -0.00925 40  TYR   A CD1   
356  C  CD2   . TYR   A 41  ? 0.25231 0.17412 0.15107 -0.02232 0.02395  0.00871  40  TYR   A CD2   
357  C  CE1   . TYR   A 41  ? 0.17446 0.15603 0.13125 -0.00406 0.03695  -0.01158 40  TYR   A CE1   
358  C  CE2   . TYR   A 41  ? 0.26776 0.17940 0.15277 -0.04558 0.02018  0.01219  40  TYR   A CE2   
359  C  CZ    . TYR   A 41  ? 0.23206 0.17325 0.14249 -0.03314 0.02718  -0.00436 40  TYR   A CZ    
360  O  OH    . TYR   A 41  ? 0.26698 0.20762 0.15700 -0.05400 0.01024  -0.00620 40  TYR   A OH    
361  N  N     . ARG   A 42  ? 0.23357 0.07289 0.14004 -0.00145 0.06468  -0.01168 41  ARG   A N     
362  C  CA    . ARG   A 42  ? 0.23021 0.09830 0.17146 0.00436  0.06956  0.00137  41  ARG   A CA    
363  C  C     . ARG   A 42  ? 0.24136 0.09236 0.14806 0.01516  0.03918  -0.00325 41  ARG   A C     
364  O  O     . ARG   A 42  ? 0.32454 0.12817 0.14641 0.02038  0.02482  -0.01216 41  ARG   A O     
365  C  CB    . ARG   A 42  ? 0.21422 0.18057 0.22805 -0.00363 0.03090  0.03637  41  ARG   A CB    
366  C  CG    . ARG   A 42  ? 0.26755 0.29444 0.29593 -0.00301 0.04352  0.04291  41  ARG   A CG    
367  C  CD    . ARG   A 42  ? 0.38232 0.39706 0.34486 0.00408  0.06284  0.03387  41  ARG   A CD    
368  N  NE    . ARG   A 42  ? 0.50114 0.48035 0.37890 0.00005  0.10389  0.01468  41  ARG   A NE    
369  C  CZ    . ARG   A 42  ? 0.62181 0.54113 0.40314 0.00023  0.15523  0.01638  41  ARG   A CZ    
370  N  NH1   . ARG   A 42  ? 0.67720 0.56359 0.40950 0.00454  0.17509  0.01678  41  ARG   A NH1   
371  N  NH2   . ARG   A 42  ? 0.64903 0.55893 0.40778 0.00512  0.16812  0.01328  41  ARG   A NH2   
372  N  N     . LYS   A 43  ? 0.20358 0.08534 0.15934 -0.01348 0.04029  -0.00945 42  LYS   A N     
373  C  CA    . LYS   A 43  ? 0.19159 0.10126 0.18593 0.00818  0.01931  -0.02234 42  LYS   A CA    
374  C  C     . LYS   A 43  ? 0.17577 0.09938 0.14597 0.00613  0.03680  -0.01137 42  LYS   A C     
375  O  O     . LYS   A 43  ? 0.16794 0.11670 0.14555 0.00023  0.04050  0.01101  42  LYS   A O     
376  C  CB    . LYS   A 43  ? 0.24075 0.14912 0.25596 0.01150  -0.01893 -0.03618 42  LYS   A CB    
377  C  CG    . LYS   A 43  ? 0.26856 0.16141 0.30371 0.05428  -0.03549 -0.03711 42  LYS   A CG    
378  C  CD    . LYS   A 43  ? 0.31013 0.17259 0.32914 0.01703  -0.03716 -0.02953 42  LYS   A CD    
379  C  CE    . LYS   A 43  ? 0.29212 0.18637 0.34838 -0.00258 -0.04866 -0.02662 42  LYS   A CE    
380  N  NZ    . LYS   A 43  ? 0.33060 0.22396 0.36337 -0.01326 -0.02348 -0.00182 42  LYS   A NZ    
381  N  N     . GLN   A 44  ? 0.17592 0.08878 0.14035 0.00575  0.03351  0.00322  43  GLN   A N     
382  C  CA    . GLN   A 44  ? 0.18607 0.07884 0.14825 0.01135  0.04137  -0.00040 43  GLN   A CA    
383  C  C     . GLN   A 44  ? 0.19844 0.09047 0.13580 0.01343  0.01743  -0.01427 43  GLN   A C     
384  O  O     . GLN   A 44  ? 0.18580 0.13906 0.13405 0.01959  0.01216  -0.00721 43  GLN   A O     
385  C  CB    . GLN   A 44  ? 0.16227 0.12222 0.16102 -0.00162 0.02546  0.02096  43  GLN   A CB    
386  C  CG    . GLN   A 44  ? 0.16767 0.16866 0.20153 0.01137  0.04384  0.03599  43  GLN   A CG    
387  C  CD    . GLN   A 44  ? 0.19289 0.22528 0.25351 0.02027  0.04027  0.05516  43  GLN   A CD    
388  O  OE1   . GLN   A 44  ? 0.21431 0.22955 0.30899 0.01693  0.03241  0.08037  43  GLN   A OE1   
389  N  NE2   . GLN   A 44  ? 0.19408 0.28856 0.24721 0.00192  0.03932  0.05295  43  GLN   A NE2   
390  N  N     . VAL   A 45  ? 0.17483 0.10480 0.13952 0.00189  0.02781  -0.01804 44  VAL   A N     
391  C  CA    . VAL   A 45  ? 0.15654 0.12624 0.14997 -0.00817 0.02352  -0.02347 44  VAL   A CA    
392  C  C     . VAL   A 45  ? 0.14783 0.12643 0.14628 0.02704  0.02479  -0.02147 44  VAL   A C     
393  O  O     . VAL   A 45  ? 0.16651 0.17976 0.19285 0.04328  -0.01460 -0.04491 44  VAL   A O     
394  C  CB    . VAL   A 45  ? 0.22940 0.13754 0.18157 -0.03522 0.05066  -0.03353 44  VAL   A CB    
395  C  CG1   . VAL   A 45  ? 0.25874 0.16190 0.20148 -0.06348 0.04519  -0.03152 44  VAL   A CG1   
396  C  CG2   . VAL   A 45  ? 0.29557 0.12643 0.18241 -0.01293 0.09695  -0.00621 44  VAL   A CG2   
397  N  N     . VAL   A 46  ? 0.15190 0.11839 0.12213 -0.00338 0.02569  -0.00683 45  VAL   A N     
398  C  CA    . VAL   A 46  ? 0.17266 0.10427 0.12021 0.00055  0.03588  0.00473  45  VAL   A CA    
399  C  C     . VAL   A 46  ? 0.14407 0.10021 0.12791 0.01276  0.01435  0.00691  45  VAL   A C     
400  O  O     . VAL   A 46  ? 0.14178 0.14645 0.14937 -0.00245 0.00709  0.01281  45  VAL   A O     
401  C  CB    . VAL   A 46  ? 0.18068 0.11164 0.11995 0.00675  0.03501  0.01599  45  VAL   A CB    
402  C  CG1   . VAL   A 46  ? 0.22604 0.11946 0.13377 0.01037  0.04592  0.01391  45  VAL   A CG1   
403  C  CG2   . VAL   A 46  ? 0.20060 0.13746 0.11592 0.00902  0.03685  0.01857  45  VAL   A CG2   
404  N  N     . ILE   A 47  ? 0.16004 0.08966 0.12338 0.00691  0.02424  0.00609  46  ILE   A N     
405  C  CA    . ILE   A 47  ? 0.17071 0.09632 0.12997 -0.00440 0.04116  0.01455  46  ILE   A CA    
406  C  C     . ILE   A 47  ? 0.13389 0.10205 0.13428 0.00170  0.02618  0.00537  46  ILE   A C     
407  O  O     . ILE   A 47  ? 0.12793 0.11213 0.14341 0.00344  0.01714  0.00571  46  ILE   A O     
408  C  CB    . ILE   A 47  ? 0.18123 0.10034 0.14710 0.00109  0.03565  0.00878  46  ILE   A CB    
409  C  CG1   . ILE   A 47  ? 0.18906 0.10995 0.17306 0.00774  0.03480  -0.00201 46  ILE   A CG1   
410  C  CG2   . ILE   A 47  ? 0.19412 0.11212 0.15725 -0.01331 0.04656  0.00428  46  ILE   A CG2   
411  C  CD1   . ILE   A 47  ? 0.23730 0.10648 0.18332 0.03056  0.04331  0.01588  46  ILE   A CD1   
412  N  N     . ASP   A 48  ? 0.13569 0.11585 0.11277 -0.00207 0.02036  0.00674  47  ASP   A N     
413  C  CA    . ASP   A 48  ? 0.16936 0.11822 0.11304 -0.01114 0.01864  -0.00347 47  ASP   A CA    
414  C  C     . ASP   A 48  ? 0.13865 0.11404 0.11639 0.00477  0.02694  -0.01613 47  ASP   A C     
415  O  O     . ASP   A 48  ? 0.14931 0.12745 0.13352 -0.00868 0.01888  -0.02655 47  ASP   A O     
416  C  CB    . ASP   A 48  ? 0.16668 0.13457 0.11058 -0.01251 0.01426  0.01500  47  ASP   A CB    
417  C  CG    . ASP   A 48  ? 0.17152 0.13403 0.11531 0.01126  -0.00548 0.01457  47  ASP   A CG    
418  O  OD1   . ASP   A 48  ? 0.15573 0.13675 0.13677 0.01419  0.02013  0.01395  47  ASP   A OD1   
419  O  OD2   . ASP   A 48  ? 0.16038 0.14086 0.13332 0.00658  0.00464  0.00963  47  ASP   A OD2   
420  N  N     . GLY   A 49  ? 0.13926 0.10004 0.11922 -0.00164 0.04065  -0.00284 48  GLY   A N     
421  C  CA    . GLY   A 49  ? 0.14481 0.11343 0.13600 0.00661  0.01863  -0.01741 48  GLY   A CA    
422  C  C     . GLY   A 49  ? 0.14634 0.10699 0.13172 0.00052  0.01097  -0.01257 48  GLY   A C     
423  O  O     . GLY   A 49  ? 0.16838 0.12282 0.14879 -0.01302 0.01324  0.01764  48  GLY   A O     
424  N  N     . GLU   A 50  ? 0.15220 0.10970 0.13493 0.01954  0.01730  -0.02416 49  GLU   A N     
425  C  CA    . GLU   A 50  ? 0.13185 0.13459 0.14230 0.01000  0.02166  -0.01178 49  GLU   A CA    
426  C  C     . GLU   A 50  ? 0.12502 0.12276 0.13847 0.00376  0.02614  -0.00335 49  GLU   A C     
427  O  O     . GLU   A 50  ? 0.15121 0.12226 0.14586 -0.01654 0.03489  -0.00160 49  GLU   A O     
428  C  CB    . GLU   A 50  ? 0.12068 0.16458 0.14768 0.02188  0.00230  0.00560  49  GLU   A CB    
429  C  CG    . GLU   A 50  ? 0.17952 0.19204 0.13970 0.02826  -0.00012 -0.00609 49  GLU   A CG    
430  C  CD    . GLU   A 50  ? 0.18343 0.22068 0.13801 0.03347  0.01433  -0.02553 49  GLU   A CD    
431  O  OE1   . GLU   A 50  ? 0.20296 0.23507 0.14539 0.03030  0.00863  -0.01817 49  GLU   A OE1   
432  O  OE2   . GLU   A 50  ? 0.20892 0.25360 0.14244 0.06065  0.01236  -0.01316 49  GLU   A OE2   
433  N  N     . THR   A 51  ? 0.13239 0.11667 0.12894 0.00938  0.02232  -0.00704 50  THR   A N     
434  C  CA    . THR   A 51  ? 0.15562 0.10836 0.12244 0.01354  0.04023  0.01548  50  THR   A CA    
435  C  C     . THR   A 51  ? 0.17888 0.11213 0.11544 0.00515  0.01600  0.01059  50  THR   A C     
436  O  O     . THR   A 51  ? 0.16732 0.13302 0.13630 0.01951  0.01019  0.00868  50  THR   A O     
437  C  CB    . THR   A 51  ? 0.16024 0.11990 0.13191 0.01835  0.03317  0.01884  50  THR   A CB    
438  O  OG1   . THR   A 51  ? 0.17719 0.11557 0.16121 0.01477  0.02117  0.03096  50  THR   A OG1   
439  C  CG2   . THR   A 51  ? 0.18449 0.13962 0.13010 0.01993  0.03195  0.02151  50  THR   A CG2   
440  N  N     . SER   A 52  ? 0.15889 0.09813 0.12522 0.01033  0.03180  0.00211  51  SER   A N     
441  C  CA    . SER   A 52  ? 0.23455 0.11044 0.12879 0.00979  0.03382  0.00618  51  SER   A CA    
442  C  C     . SER   A 52  ? 0.18669 0.10494 0.13116 0.03131  0.01313  0.01218  51  SER   A C     
443  O  O     . SER   A 52  ? 0.20018 0.12875 0.14304 0.04685  0.00738  0.00236  51  SER   A O     
444  C  CB    . SER   A 52  ? 0.40691 0.15448 0.12001 -0.01290 0.06530  -0.00713 51  SER   A CB    
445  O  OG    . SER   A 52  ? 0.49963 0.18217 0.15835 -0.06055 0.09468  -0.01389 51  SER   A OG    
446  N  N     . LEU   A 53  ? 0.15929 0.09795 0.15025 -0.00510 0.01764  0.00463  52  LEU   A N     
447  C  CA    . LEU   A 53  ? 0.15356 0.09258 0.16586 -0.00339 0.03902  0.00644  52  LEU   A CA    
448  C  C     . LEU   A 53  ? 0.16452 0.08792 0.15350 -0.00470 0.03314  0.00545  52  LEU   A C     
449  O  O     . LEU   A 53  ? 0.18020 0.10471 0.16474 -0.00516 0.02011  0.02431  52  LEU   A O     
450  C  CB    . LEU   A 53  ? 0.13871 0.11367 0.17708 0.01219  0.04711  0.00583  52  LEU   A CB    
451  C  CG    . LEU   A 53  ? 0.16707 0.15024 0.19250 0.02528  0.04539  0.01449  52  LEU   A CG    
452  C  CD1   . LEU   A 53  ? 0.23143 0.17717 0.19119 0.02197  0.04442  0.00880  52  LEU   A CD1   
453  C  CD2   . LEU   A 53  ? 0.17835 0.20693 0.22082 0.04160  0.05169  0.01101  52  LEU   A CD2   
454  N  N     . LEU   A 54  ? 0.16589 0.08307 0.14892 -0.00523 0.04252  -0.01404 53  LEU   A N     
455  C  CA    . LEU   A 54  ? 0.17370 0.08431 0.15605 -0.01031 0.04297  -0.01410 53  LEU   A CA    
456  C  C     . LEU   A 54  ? 0.16953 0.08746 0.13564 -0.01262 0.04582  0.00636  53  LEU   A C     
457  O  O     . LEU   A 54  ? 0.23364 0.10979 0.12498 0.01846  0.04960  0.01160  53  LEU   A O     
458  C  CB    . LEU   A 54  ? 0.16231 0.09711 0.15879 -0.00102 0.04105  -0.01513 53  LEU   A CB    
459  C  CG    . LEU   A 54  ? 0.16279 0.12163 0.15413 0.00035  0.03705  -0.01435 53  LEU   A CG    
460  C  CD1   . LEU   A 54  ? 0.16961 0.12970 0.18961 0.00707  0.05133  0.00920  53  LEU   A CD1   
461  C  CD2   . LEU   A 54  ? 0.21011 0.14340 0.14389 0.01282  0.05806  -0.00202 53  LEU   A CD2   
462  N  N     A ASP   A 55  ? 0.16436 0.09251 0.14619 -0.01099 0.03266  0.00553  54  ASP   A N     
463  N  N     B ASP   A 55  ? 0.15566 0.07570 0.13505 -0.01319 0.04871  0.00243  54  ASP   A N     
464  C  CA    A ASP   A 55  ? 0.16516 0.10981 0.16462 -0.00678 0.02906  0.01367  54  ASP   A CA    
465  C  CA    B ASP   A 55  ? 0.14980 0.07237 0.14261 0.00009  0.05741  0.00803  54  ASP   A CA    
466  C  C     A ASP   A 55  ? 0.15856 0.09279 0.14018 -0.00300 0.03799  0.00119  54  ASP   A C     
467  C  C     B ASP   A 55  ? 0.15046 0.07182 0.13012 -0.01400 0.07113  -0.00951 54  ASP   A C     
468  O  O     A ASP   A 55  ? 0.17076 0.11493 0.12051 -0.01153 0.04225  0.00152  54  ASP   A O     
469  O  O     B ASP   A 55  ? 0.13152 0.10424 0.12669 -0.00019 0.06646  -0.00016 54  ASP   A O     
470  C  CB    A ASP   A 55  ? 0.17888 0.17308 0.21563 -0.03106 0.02350  0.02777  54  ASP   A CB    
471  C  CB    B ASP   A 55  ? 0.14701 0.12548 0.17563 0.00581  0.05075  0.01364  54  ASP   A CB    
472  C  CG    A ASP   A 55  ? 0.24612 0.22593 0.25966 -0.02622 0.01225  0.03782  54  ASP   A CG    
473  C  CG    B ASP   A 55  ? 0.17600 0.17977 0.20404 0.04623  0.02886  0.00050  54  ASP   A CG    
474  O  OD1   A ASP   A 55  ? 0.30133 0.25459 0.28073 -0.03690 0.02291  0.03278  54  ASP   A OD1   
475  O  OD1   B ASP   A 55  ? 0.19237 0.19393 0.21609 0.05705  0.04557  -0.01600 54  ASP   A OD1   
476  O  OD2   A ASP   A 55  ? 0.28526 0.25621 0.27906 -0.04252 0.00234  0.04076  54  ASP   A OD2   
477  O  OD2   B ASP   A 55  ? 0.22731 0.22034 0.22690 0.04284  0.00972  -0.01047 54  ASP   A OD2   
478  N  N     A ILE   A 56  ? 0.16519 0.08536 0.13448 -0.00331 0.02918  0.00219  55  ILE   A N     
479  N  N     B ILE   A 56  ? 0.15482 0.07523 0.12000 -0.01113 0.04632  -0.00208 55  ILE   A N     
480  C  CA    A ILE   A 56  ? 0.15393 0.08765 0.13042 -0.00969 0.03159  -0.00697 55  ILE   A CA    
481  C  CA    B ILE   A 56  ? 0.14862 0.07877 0.11490 -0.00892 0.03110  -0.00322 55  ILE   A CA    
482  C  C     A ILE   A 56  ? 0.15885 0.09430 0.11453 -0.00453 0.03554  -0.00312 55  ILE   A C     
483  C  C     B ILE   A 56  ? 0.13376 0.08505 0.10265 -0.00163 0.03362  -0.00144 55  ILE   A C     
484  O  O     A ILE   A 56  ? 0.20996 0.10999 0.10269 -0.00117 0.04718  0.00376  55  ILE   A O     
485  O  O     B ILE   A 56  ? 0.17431 0.09018 0.08576 0.01319  0.05317  0.00483  55  ILE   A O     
486  C  CB    A ILE   A 56  ? 0.16533 0.11876 0.14935 0.00755  0.02905  -0.00434 55  ILE   A CB    
487  C  CB    B ILE   A 56  ? 0.15683 0.09490 0.12468 0.00802  0.02796  0.00605  55  ILE   A CB    
488  C  CG1   A ILE   A 56  ? 0.14423 0.11838 0.13948 0.04785  0.03789  -0.00317 55  ILE   A CG1   
489  C  CG1   B ILE   A 56  ? 0.18003 0.09358 0.11964 0.00574  0.04762  0.01775  55  ILE   A CG1   
490  C  CG2   A ILE   A 56  ? 0.17691 0.13253 0.16800 -0.01073 0.02417  0.00228  55  ILE   A CG2   
491  C  CG2   B ILE   A 56  ? 0.14143 0.11837 0.14828 0.02094  0.01069  0.01794  55  ILE   A CG2   
492  C  CD1   A ILE   A 56  ? 0.16845 0.12530 0.14361 0.02318  0.03324  -0.01225 55  ILE   A CD1   
493  C  CD1   B ILE   A 56  ? 0.18600 0.11007 0.13233 -0.00696 0.02404  0.01179  55  ILE   A CD1   
494  N  N     . LEU   A 57  ? 0.13073 0.07961 0.10733 -0.01015 0.02205  -0.00436 56  LEU   A N     
495  C  CA    . LEU   A 57  ? 0.12568 0.08270 0.10644 -0.01075 0.02804  -0.00170 56  LEU   A CA    
496  C  C     . LEU   A 57  ? 0.12074 0.08601 0.09588 0.00214  0.04065  -0.00600 56  LEU   A C     
497  O  O     . LEU   A 57  ? 0.13677 0.11234 0.10761 -0.01739 0.05159  -0.01341 56  LEU   A O     
498  C  CB    . LEU   A 57  ? 0.12415 0.12280 0.12839 0.01177  0.01102  0.01539  56  LEU   A CB    
499  C  CG    . LEU   A 57  ? 0.14074 0.17606 0.18241 0.02456  0.02144  0.01542  56  LEU   A CG    
500  C  CD1   . LEU   A 57  ? 0.16214 0.23431 0.21201 0.04676  -0.00404 0.03449  56  LEU   A CD1   
501  C  CD2   . LEU   A 57  ? 0.25216 0.23193 0.19936 0.00295  0.00884  0.00854  56  LEU   A CD2   
502  N  N     . ASP   A 58  ? 0.12272 0.08125 0.09909 -0.00101 0.03240  -0.00680 57  ASP   A N     
503  C  CA    . ASP   A 58  ? 0.12101 0.08553 0.09787 -0.00804 0.01718  -0.00517 57  ASP   A CA    
504  C  C     . ASP   A 58  ? 0.11010 0.08524 0.09252 -0.00327 0.02969  -0.01527 57  ASP   A C     
505  O  O     . ASP   A 58  ? 0.15711 0.09274 0.10925 -0.00074 0.04838  -0.00866 57  ASP   A O     
506  C  CB    . ASP   A 58  ? 0.12522 0.11365 0.09893 -0.01241 0.01197  -0.00513 57  ASP   A CB    
507  C  CG    . ASP   A 58  ? 0.12928 0.10823 0.09758 0.00036  0.01178  -0.01882 57  ASP   A CG    
508  O  OD1   . ASP   A 58  ? 0.13324 0.12247 0.11483 -0.00875 0.03902  -0.00902 57  ASP   A OD1   
509  O  OD2   . ASP   A 58  ? 0.13713 0.13709 0.11837 -0.01093 0.01471  -0.00247 57  ASP   A OD2   
510  N  N     . THR   A 59  ? 0.11888 0.08693 0.10210 -0.00515 0.03019  -0.00178 58  THR   A N     
511  C  CA    . THR   A 59  ? 0.12387 0.07968 0.09585 -0.00517 0.01979  -0.01109 58  THR   A CA    
512  C  C     . THR   A 59  ? 0.11004 0.08279 0.07966 0.00315  0.02903  -0.01553 58  THR   A C     
513  O  O     . THR   A 59  ? 0.11699 0.09608 0.09148 0.00092  0.02361  -0.00370 58  THR   A O     
514  C  CB    . THR   A 59  ? 0.08746 0.10852 0.10065 -0.00766 0.02391  -0.00489 58  THR   A CB    
515  O  OG1   . THR   A 59  ? 0.11685 0.09778 0.08774 -0.00531 0.03523  0.00043  58  THR   A OG1   
516  C  CG2   . THR   A 59  ? 0.11416 0.11304 0.12482 -0.02161 0.00865  -0.01369 58  THR   A CG2   
517  N  N     . ALA   A 60  ? 0.11796 0.08018 0.08993 -0.00471 0.03357  -0.01268 59  ALA   A N     
518  C  CA    . ALA   A 60  ? 0.11147 0.07967 0.09487 -0.00611 0.02165  -0.01312 59  ALA   A CA    
519  C  C     . ALA   A 60  ? 0.11870 0.08504 0.10908 0.00119  0.03770  -0.01078 59  ALA   A C     
520  O  O     . ALA   A 60  ? 0.11533 0.10374 0.11100 0.00506  0.01723  -0.00421 59  ALA   A O     
521  C  CB    . ALA   A 60  ? 0.13507 0.10143 0.09052 -0.00673 0.01994  -0.01772 59  ALA   A CB    
522  N  N     . GLY   A 61  ? 0.11962 0.07093 0.11847 0.00268  0.02454  -0.01562 60  GLY   A N     
523  C  CA    . GLY   A 61  ? 0.12810 0.08910 0.11990 0.00512  0.02756  -0.00480 60  GLY   A CA    
524  C  C     . GLY   A 61  ? 0.10815 0.08812 0.11908 0.01635  0.01301  0.00006  60  GLY   A C     
525  O  O     . GLY   A 61  ? 0.13060 0.09317 0.13050 0.00784  0.02543  -0.00850 60  GLY   A O     
526  N  N     . GLN   A 62  ? 0.10935 0.10280 0.10689 -0.01078 0.03155  0.00377  61  GLN   A N     
527  C  CA    . GLN   A 62  ? 0.12308 0.10758 0.13690 -0.01836 0.02760  0.01085  61  GLN   A CA    
528  C  C     . GLN   A 62  ? 0.13855 0.10557 0.12520 -0.00998 0.03615  0.01740  61  GLN   A C     
529  O  O     . GLN   A 62  ? 0.13977 0.11185 0.13258 -0.01214 0.02011  0.02049  61  GLN   A O     
530  C  CB    . GLN   A 62  ? 0.11513 0.11921 0.16312 0.01172  0.02280  0.01441  61  GLN   A CB    
531  C  CG    . GLN   A 62  ? 0.13349 0.11098 0.20047 -0.00439 -0.00603 -0.01156 61  GLN   A CG    
532  C  CD    . GLN   A 62  ? 0.16368 0.09475 0.22031 0.01609  -0.00135 -0.00684 61  GLN   A CD    
533  O  OE1   . GLN   A 62  ? 0.15304 0.09359 0.20556 0.01224  0.00500  0.00096  61  GLN   A OE1   
534  N  NE2   . GLN   A 62  ? 0.19283 0.12582 0.27640 0.01584  -0.00767 -0.03533 61  GLN   A NE2   
535  N  N     . GLU   A 63  ? 0.15340 0.11121 0.12294 -0.00324 0.02038  0.02377  62  GLU   A N     
536  C  CA    . GLU   A 63  ? 0.18902 0.11817 0.13937 -0.01714 0.03560  0.02659  62  GLU   A CA    
537  C  C     . GLU   A 63  ? 0.16980 0.10100 0.11915 -0.00063 0.00531  0.01102  62  GLU   A C     
538  O  O     . GLU   A 63  ? 0.18424 0.14286 0.14233 0.00133  0.00772  0.02562  62  GLU   A O     
539  C  CB    . GLU   A 63  ? 0.25228 0.11957 0.17428 0.00573  0.07117  0.02883  62  GLU   A CB    
540  C  CG    . GLU   A 63  ? 0.35276 0.17119 0.22653 0.04461  0.07292  0.03224  62  GLU   A CG    
541  C  CD    . GLU   A 63  ? 0.41100 0.21133 0.28678 0.04446  0.11417  0.02063  62  GLU   A CD    
542  O  OE1   . GLU   A 63  ? 0.46692 0.26492 0.33212 0.00290  0.13561  0.00838  62  GLU   A OE1   
543  O  OE2   . GLU   A 63  ? 0.35157 0.21968 0.26952 0.05044  0.11591  0.03081  62  GLU   A OE2   
544  N  N     . GLU   A 64  ? 0.18178 0.11099 0.13505 -0.00982 0.03468  0.00238  63  GLU   A N     
545  C  CA    . GLU   A 64  ? 0.17773 0.13179 0.14323 -0.00214 0.00590  -0.00583 63  GLU   A CA    
546  C  C     . GLU   A 64  ? 0.16557 0.11061 0.16272 0.00271  0.01208  -0.00260 63  GLU   A C     
547  O  O     . GLU   A 64  ? 0.18123 0.11287 0.20703 0.00954  0.01656  -0.00457 63  GLU   A O     
548  C  CB    . GLU   A 64  ? 0.18722 0.13613 0.14535 -0.03292 0.00876  -0.01811 63  GLU   A CB    
549  C  CG    . GLU   A 64  ? 0.21564 0.14801 0.14927 -0.00462 0.01480  -0.00574 63  GLU   A CG    
550  C  CD    . GLU   A 64  ? 0.19755 0.16747 0.14615 0.00633  0.00846  -0.00326 63  GLU   A CD    
551  O  OE1   . GLU   A 64  ? 0.21575 0.19286 0.13363 0.00904  0.00948  0.00253  63  GLU   A OE1   
552  O  OE2   . GLU   A 64  ? 0.22150 0.16309 0.14620 0.00003  -0.00730 -0.02663 63  GLU   A OE2   
553  N  N     . TYR   A 65  ? 0.16290 0.10594 0.15183 -0.00596 0.00819  0.00289  64  TYR   A N     
554  C  CA    . TYR   A 65  ? 0.14187 0.12146 0.14390 -0.00234 0.01864  -0.00604 64  TYR   A CA    
555  C  C     . TYR   A 65  ? 0.13226 0.11685 0.13948 0.01195  0.01775  -0.00832 64  TYR   A C     
556  O  O     . TYR   A 65  ? 0.14452 0.11943 0.15125 0.00166  0.02499  -0.00423 64  TYR   A O     
557  C  CB    . TYR   A 65  ? 0.15073 0.11367 0.13465 0.00598  0.02522  0.00128  64  TYR   A CB    
558  C  CG    . TYR   A 65  ? 0.12955 0.10750 0.13466 0.02076  0.01526  0.00205  64  TYR   A CG    
559  C  CD1   . TYR   A 65  ? 0.16067 0.11411 0.13848 0.01700  0.03615  -0.00445 64  TYR   A CD1   
560  C  CD2   . TYR   A 65  ? 0.14859 0.10758 0.12471 0.01316  0.02460  0.01148  64  TYR   A CD2   
561  C  CE1   . TYR   A 65  ? 0.15217 0.11694 0.13727 0.00904  0.03799  -0.00327 64  TYR   A CE1   
562  C  CE2   . TYR   A 65  ? 0.16968 0.10084 0.11179 0.02358  0.04255  -0.00221 64  TYR   A CE2   
563  C  CZ    . TYR   A 65  ? 0.18511 0.11948 0.10486 0.00420  0.03810  0.00635  64  TYR   A CZ    
564  O  OH    . TYR   A 65  ? 0.18514 0.12474 0.11198 0.02499  0.04010  -0.02359 64  TYR   A OH    
565  N  N     . SER   A 66  ? 0.16477 0.11611 0.12262 0.00546  0.01500  -0.01125 65  SER   A N     
566  C  CA    A SER   A 66  ? 0.15723 0.12903 0.11462 -0.00052 0.01555  -0.00627 65  SER   A CA    
567  C  CA    B SER   A 66  ? 0.17524 0.14494 0.12773 -0.00284 0.02296  -0.01074 65  SER   A CA    
568  C  C     . SER   A 66  ? 0.15323 0.12674 0.14013 0.01633  0.02614  0.00693  65  SER   A C     
569  O  O     . SER   A 66  ? 0.15563 0.11519 0.14827 0.00603  0.02553  0.00543  65  SER   A O     
570  C  CB    A SER   A 66  ? 0.18458 0.12585 0.10904 -0.00465 0.02874  0.00022  65  SER   A CB    
571  C  CB    B SER   A 66  ? 0.23411 0.18764 0.14620 -0.01070 0.04104  -0.01530 65  SER   A CB    
572  O  OG    A SER   A 66  ? 0.16439 0.09551 0.09282 -0.01532 0.02786  0.01593  65  SER   A OG    
573  O  OG    B SER   A 66  ? 0.26671 0.21258 0.15901 -0.02183 0.04167  -0.00793 65  SER   A OG    
574  N  N     . ALA   A 67  ? 0.15639 0.12466 0.17099 0.01048  0.00891  0.00512  66  ALA   A N     
575  C  CA    . ALA   A 67  ? 0.16971 0.11795 0.19209 0.01647  -0.01648 0.00444  66  ALA   A CA    
576  C  C     . ALA   A 67  ? 0.13471 0.12250 0.18608 0.02825  -0.00177 -0.02258 66  ALA   A C     
577  O  O     . ALA   A 67  ? 0.16379 0.13948 0.18859 0.01082  -0.02328 -0.02171 66  ALA   A O     
578  C  CB    . ALA   A 67  ? 0.21639 0.14588 0.22728 0.02028  0.01002  0.01919  66  ALA   A CB    
579  N  N     A MET   A 68  ? 0.11795 0.10963 0.16320 0.01893  0.01872  -0.02770 67  MET   A N     
580  N  N     B MET   A 68  ? 0.13681 0.13194 0.16323 0.01833  0.01330  -0.02960 67  MET   A N     
581  C  CA    A MET   A 68  ? 0.11237 0.11908 0.15525 0.00755  0.02284  -0.04022 67  MET   A CA    
582  C  CA    B MET   A 68  ? 0.15666 0.15879 0.15527 0.01228  0.01654  -0.04217 67  MET   A CA    
583  C  C     A MET   A 68  ? 0.10282 0.11430 0.12714 0.00083  0.02216  -0.02931 67  MET   A C     
584  C  C     B MET   A 68  ? 0.12174 0.14036 0.13186 -0.00859 0.02239  -0.02879 67  MET   A C     
585  O  O     A MET   A 68  ? 0.11382 0.12414 0.11590 0.00196  0.01996  -0.02756 67  MET   A O     
586  O  O     B MET   A 68  ? 0.11720 0.15537 0.12604 -0.02852 0.02320  -0.01929 67  MET   A O     
587  C  CB    A MET   A 68  ? 0.09667 0.12599 0.17472 0.01127  0.01622  -0.06860 67  MET   A CB    
588  C  CB    B MET   A 68  ? 0.18467 0.19364 0.16695 0.03496  -0.00053 -0.07193 67  MET   A CB    
589  C  CG    A MET   A 68  ? 0.11601 0.12605 0.19220 0.00665  0.02302  -0.05884 67  MET   A CG    
590  C  CG    B MET   A 68  ? 0.20715 0.22428 0.17472 0.05697  -0.00894 -0.07503 67  MET   A CG    
591  S  SD    A MET   A 68  ? 0.17123 0.12132 0.19011 0.01230  0.00400  -0.03592 67  MET   A SD    
592  S  SD    B MET   A 68  ? 0.21585 0.23597 0.16721 0.09506  -0.03304 -0.07493 67  MET   A SD    
593  C  CE    A MET   A 68  ? 0.18696 0.12849 0.19875 0.01841  -0.00060 -0.02500 67  MET   A CE    
594  C  CE    B MET   A 68  ? 0.24680 0.24957 0.17511 0.08330  -0.01475 -0.07108 67  MET   A CE    
595  N  N     . ARG   A 69  ? 0.09776 0.12155 0.13445 -0.00247 0.02012  -0.02833 68  ARG   A N     
596  C  CA    . ARG   A 69  ? 0.10270 0.10246 0.12618 -0.01444 0.02975  -0.02388 68  ARG   A CA    
597  C  C     . ARG   A 69  ? 0.09895 0.11210 0.11721 -0.00999 0.01781  -0.02274 68  ARG   A C     
598  O  O     . ARG   A 69  ? 0.10460 0.10358 0.13526 -0.01503 0.01137  -0.01110 68  ARG   A O     
599  C  CB    . ARG   A 69  ? 0.10986 0.10529 0.12175 0.00354  0.03164  -0.00765 68  ARG   A CB    
600  C  CG    . ARG   A 69  ? 0.10265 0.10755 0.11823 -0.00379 0.01768  -0.01171 68  ARG   A CG    
601  C  CD    . ARG   A 69  ? 0.10939 0.09669 0.11812 0.00062  0.03021  0.01220  68  ARG   A CD    
602  N  NE    . ARG   A 69  ? 0.10267 0.09696 0.11622 0.00432  0.01327  0.00458  68  ARG   A NE    
603  C  CZ    . ARG   A 69  ? 0.09766 0.10268 0.10927 -0.00774 0.00961  0.00781  68  ARG   A CZ    
604  N  NH1   . ARG   A 69  ? 0.11111 0.11162 0.12725 -0.00616 0.01043  -0.00782 68  ARG   A NH1   
605  N  NH2   . ARG   A 69  ? 0.10626 0.12404 0.12784 -0.01117 0.02506  0.02616  68  ARG   A NH2   
606  N  N     . ASP   A 70  ? 0.12342 0.11633 0.11196 0.00554  0.01852  -0.00849 69  ASP   A N     
607  C  CA    . ASP   A 70  ? 0.11290 0.11140 0.10760 -0.00153 0.01298  0.00477  69  ASP   A CA    
608  C  C     . ASP   A 70  ? 0.11363 0.10170 0.11210 0.01395  0.01509  -0.00064 69  ASP   A C     
609  O  O     . ASP   A 70  ? 0.11040 0.10526 0.12510 0.00776  0.01034  -0.00326 69  ASP   A O     
610  C  CB    . ASP   A 70  ? 0.13545 0.11162 0.13443 0.00871  0.01386  0.02141  69  ASP   A CB    
611  C  CG    . ASP   A 70  ? 0.13902 0.10304 0.14723 0.02555  0.00168  0.01867  69  ASP   A CG    
612  O  OD1   . ASP   A 70  ? 0.14348 0.13613 0.14943 0.00351  -0.00101 0.01266  69  ASP   A OD1   
613  O  OD2   . ASP   A 70  ? 0.16560 0.14323 0.17090 0.01340  0.02367  0.03650  69  ASP   A OD2   
614  N  N     . GLN   A 71  ? 0.10125 0.11153 0.12922 -0.00220 0.02054  -0.00580 70  GLN   A N     
615  C  CA    . GLN   A 71  ? 0.09991 0.11060 0.13406 -0.00088 0.01560  -0.01425 70  GLN   A CA    
616  C  C     . GLN   A 71  ? 0.10644 0.10362 0.11823 0.00912  0.02627  -0.01660 70  GLN   A C     
617  O  O     . GLN   A 71  ? 0.11441 0.10865 0.12576 0.00191  0.02195  -0.01175 70  GLN   A O     
618  C  CB    . GLN   A 71  ? 0.12619 0.12909 0.15990 0.01581  0.04032  -0.02371 70  GLN   A CB    
619  C  CG    . GLN   A 71  ? 0.14516 0.15547 0.19013 0.02421  0.04487  -0.02409 70  GLN   A CG    
620  C  CD    . GLN   A 71  ? 0.15363 0.18941 0.20483 0.00079  0.00118  -0.04735 70  GLN   A CD    
621  O  OE1   . GLN   A 71  ? 0.16314 0.20950 0.20600 0.00792  0.03705  -0.05715 70  GLN   A OE1   
622  N  NE2   . GLN   A 71  ? 0.21843 0.20252 0.23552 0.02350  0.00232  -0.06041 70  GLN   A NE2   
623  N  N     . TYR   A 72  ? 0.11281 0.12578 0.10684 -0.00287 0.01277  -0.00721 71  TYR   A N     
624  C  CA    . TYR   A 72  ? 0.11312 0.12776 0.10534 -0.00035 0.01159  -0.00373 71  TYR   A CA    
625  C  C     . TYR   A 72  ? 0.09828 0.12036 0.10919 -0.01749 0.00897  -0.00644 71  TYR   A C     
626  O  O     . TYR   A 72  ? 0.14251 0.10862 0.11481 -0.01506 0.00483  0.00416  71  TYR   A O     
627  C  CB    . TYR   A 72  ? 0.12311 0.14000 0.10747 -0.00198 0.00972  -0.00653 71  TYR   A CB    
628  C  CG    . TYR   A 72  ? 0.11699 0.14736 0.11227 -0.02333 0.02446  -0.01160 71  TYR   A CG    
629  C  CD1   . TYR   A 72  ? 0.11240 0.16056 0.11903 -0.01937 0.02961  -0.00818 71  TYR   A CD1   
630  C  CD2   . TYR   A 72  ? 0.15840 0.14397 0.12755 -0.01782 0.02390  -0.01695 71  TYR   A CD2   
631  C  CE1   . TYR   A 72  ? 0.10876 0.16001 0.12801 -0.00321 0.01804  -0.01012 71  TYR   A CE1   
632  C  CE2   . TYR   A 72  ? 0.17811 0.14402 0.12559 -0.01289 0.04489  -0.02201 71  TYR   A CE2   
633  C  CZ    . TYR   A 72  ? 0.15054 0.16551 0.11668 -0.02330 0.03131  -0.02691 71  TYR   A CZ    
634  O  OH    . TYR   A 72  ? 0.19896 0.18967 0.12653 -0.03000 0.03954  -0.03244 71  TYR   A OH    
635  N  N     . MET   A 73  ? 0.09786 0.10560 0.09872 -0.00514 0.01773  0.00089  72  MET   A N     
636  C  CA    . MET   A 73  ? 0.10888 0.11152 0.10082 0.00434  0.02608  0.00437  72  MET   A CA    
637  C  C     . MET   A 73  ? 0.09582 0.10372 0.10317 0.00008  0.01843  0.00045  72  MET   A C     
638  O  O     . MET   A 73  ? 0.11602 0.10966 0.11096 0.00519  0.01730  -0.00342 72  MET   A O     
639  C  CB    . MET   A 73  ? 0.11489 0.11102 0.11037 0.00507  0.00941  0.00872  72  MET   A CB    
640  C  CG    . MET   A 73  ? 0.11722 0.11355 0.11273 -0.00895 0.00096  -0.00054 72  MET   A CG    
641  S  SD    . MET   A 73  ? 0.12046 0.10838 0.11064 -0.00501 0.01936  -0.00570 72  MET   A SD    
642  C  CE    . MET   A 73  ? 0.12234 0.12609 0.12490 0.01929  0.03045  0.00502  72  MET   A CE    
643  N  N     . ARG   A 74  ? 0.09310 0.12165 0.11452 -0.00612 0.00886  0.00641  73  ARG   A N     
644  C  CA    . ARG   A 74  ? 0.10402 0.13072 0.12481 0.01434  0.00293  0.00158  73  ARG   A CA    
645  C  C     . ARG   A 74  ? 0.12466 0.11901 0.12799 0.00469  -0.00159 -0.00162 73  ARG   A C     
646  O  O     . ARG   A 74  ? 0.15951 0.15290 0.14021 -0.03209 -0.01026 -0.02045 73  ARG   A O     
647  C  CB    . ARG   A 74  ? 0.09615 0.14657 0.12828 0.02375  -0.00268 -0.00573 73  ARG   A CB    
648  C  CG    . ARG   A 74  ? 0.13510 0.16809 0.14431 0.02972  0.00539  -0.00109 73  ARG   A CG    
649  C  CD    . ARG   A 74  ? 0.16469 0.18997 0.15873 0.02255  0.01516  0.00891  73  ARG   A CD    
650  N  NE    . ARG   A 74  ? 0.16793 0.21213 0.17172 0.03482  0.01477  0.02043  73  ARG   A NE    
651  C  CZ    . ARG   A 74  ? 0.11686 0.20807 0.17831 0.00989  0.01730  0.03350  73  ARG   A CZ    
652  N  NH1   . ARG   A 74  ? 0.11215 0.20919 0.21148 0.01942  0.02212  0.02001  73  ARG   A NH1   
653  N  NH2   . ARG   A 74  ? 0.16896 0.25401 0.20090 0.02351  0.01391  0.05122  73  ARG   A NH2   
654  N  N     A THR   A 75  ? 0.10927 0.09252 0.11878 0.00353  0.00841  -0.00258 74  THR   A N     
655  N  N     B THR   A 75  ? 0.12555 0.10585 0.13687 -0.00359 0.00691  0.00127  74  THR   A N     
656  C  CA    A THR   A 75  ? 0.12444 0.09817 0.11025 0.00419  0.01649  0.00317  74  THR   A CA    
657  C  CA    B THR   A 75  ? 0.14234 0.12358 0.14619 0.00227  0.01517  0.00849  74  THR   A CA    
658  C  C     A THR   A 75  ? 0.12383 0.10431 0.11040 -0.00978 0.00892  -0.00378 74  THR   A C     
659  C  C     B THR   A 75  ? 0.12287 0.11131 0.13324 -0.00489 0.00265  0.00039  74  THR   A C     
660  O  O     A THR   A 75  ? 0.14042 0.11213 0.10314 -0.01488 0.00313  -0.00925 74  THR   A O     
661  O  O     B THR   A 75  ? 0.11241 0.10297 0.12578 0.00480  -0.01916 0.00512  74  THR   A O     
662  C  CB    A THR   A 75  ? 0.16632 0.08631 0.11677 0.02141  0.01998  0.02287  74  THR   A CB    
663  C  CB    B THR   A 75  ? 0.18914 0.15047 0.17080 0.02818  0.01931  0.02614  74  THR   A CB    
664  O  OG1   A THR   A 75  ? 0.20058 0.07045 0.11234 0.03826  0.02632  0.01519  74  THR   A OG1   
665  O  OG1   B THR   A 75  ? 0.15279 0.15811 0.17564 0.04465  0.00484  0.02073  74  THR   A OG1   
666  C  CG2   A THR   A 75  ? 0.14646 0.07841 0.11607 -0.02404 0.02326  0.00185  74  THR   A CG2   
667  C  CG2   B THR   A 75  ? 0.22018 0.15015 0.17465 0.04366  0.02155  0.02138  74  THR   A CG2   
668  N  N     . GLY   A 76  ? 0.11100 0.10582 0.12773 -0.00693 0.00939  -0.00847 75  GLY   A N     
669  C  CA    . GLY   A 76  ? 0.11588 0.12249 0.12425 0.01548  -0.00587 -0.00795 75  GLY   A CA    
670  C  C     . GLY   A 76  ? 0.09847 0.11926 0.12208 0.00433  0.00087  0.01758  75  GLY   A C     
671  O  O     . GLY   A 76  ? 0.14878 0.11435 0.13139 0.00414  0.00031  0.00135  75  GLY   A O     
672  N  N     . GLU   A 77  ? 0.12045 0.09772 0.13090 0.00443  0.02087  0.00610  76  GLU   A N     
673  C  CA    . GLU   A 77  ? 0.11803 0.11633 0.15054 -0.02356 0.00070  -0.01297 76  GLU   A CA    
674  C  C     . GLU   A 77  ? 0.11247 0.14379 0.14000 -0.01864 0.02269  -0.03166 76  GLU   A C     
675  O  O     . GLU   A 77  ? 0.13166 0.23242 0.14449 -0.01432 0.00541  -0.06713 76  GLU   A O     
676  C  CB    . GLU   A 77  ? 0.11302 0.14081 0.19126 -0.02075 -0.00517 0.00441  76  GLU   A CB    
677  C  CG    . GLU   A 77  ? 0.19188 0.19569 0.22503 -0.05633 -0.03293 0.04764  76  GLU   A CG    
678  C  CD    . GLU   A 77  ? 0.32974 0.22808 0.25087 -0.12321 -0.08525 0.05539  76  GLU   A CD    
679  O  OE1   . GLU   A 77  ? 0.31053 0.21860 0.24192 -0.13615 -0.10949 0.06636  76  GLU   A OE1   
680  O  OE2   . GLU   A 77  ? 0.46669 0.26646 0.27244 -0.13056 -0.10190 0.04755  76  GLU   A OE2   
681  N  N     . GLY   A 78  ? 0.10273 0.11966 0.12901 -0.00958 0.01088  -0.02470 77  GLY   A N     
682  C  CA    . GLY   A 78  ? 0.10723 0.12319 0.12537 0.00047  0.00703  -0.03719 77  GLY   A CA    
683  C  C     . GLY   A 78  ? 0.10915 0.10488 0.09792 -0.00414 0.01043  -0.02628 77  GLY   A C     
684  O  O     . GLY   A 78  ? 0.11370 0.10117 0.10136 -0.00445 0.01940  -0.01700 77  GLY   A O     
685  N  N     . PHE   A 79  ? 0.10461 0.08870 0.09031 -0.00310 0.01092  -0.00932 78  PHE   A N     
686  C  CA    . PHE   A 79  ? 0.09990 0.08699 0.08700 -0.00511 0.01578  -0.01074 78  PHE   A CA    
687  C  C     . PHE   A 79  ? 0.10305 0.09166 0.07507 -0.01130 0.01460  -0.01464 78  PHE   A C     
688  O  O     . PHE   A 79  ? 0.10196 0.10501 0.08511 0.00791  0.01712  -0.01848 78  PHE   A O     
689  C  CB    . PHE   A 79  ? 0.11835 0.09272 0.09587 -0.01395 0.01159  0.00449  78  PHE   A CB    
690  C  CG    . PHE   A 79  ? 0.09751 0.09675 0.10215 0.01330  0.01044  0.01054  78  PHE   A CG    
691  C  CD1   . PHE   A 79  ? 0.10700 0.12651 0.10059 0.00347  0.00153  0.02042  78  PHE   A CD1   
692  C  CD2   . PHE   A 79  ? 0.12719 0.10023 0.10769 0.02032  0.02116  0.00792  78  PHE   A CD2   
693  C  CE1   . PHE   A 79  ? 0.11920 0.12753 0.11298 0.01199  0.00295  0.01237  78  PHE   A CE1   
694  C  CE2   . PHE   A 79  ? 0.12799 0.11780 0.10814 0.01364  0.02218  0.02339  78  PHE   A CE2   
695  C  CZ    . PHE   A 79  ? 0.12601 0.13187 0.10699 0.01861  0.01361  0.01739  78  PHE   A CZ    
696  N  N     . LEU   A 80  ? 0.10018 0.08673 0.07641 0.00327  0.01071  -0.00452 79  LEU   A N     
697  C  CA    . LEU   A 80  ? 0.09896 0.09124 0.08165 0.00236  0.00295  -0.00049 79  LEU   A CA    
698  C  C     . LEU   A 80  ? 0.10953 0.07971 0.07837 0.00441  0.01059  -0.01203 79  LEU   A C     
699  O  O     . LEU   A 80  ? 0.12454 0.09041 0.09159 0.00141  0.02023  -0.01595 79  LEU   A O     
700  C  CB    . LEU   A 80  ? 0.12319 0.09933 0.07683 0.00646  0.01157  -0.00879 79  LEU   A CB    
701  C  CG    . LEU   A 80  ? 0.13611 0.09748 0.09531 -0.00373 0.02220  -0.00161 79  LEU   A CG    
702  C  CD1   . LEU   A 80  ? 0.15805 0.10871 0.09695 0.00214  -0.00341 0.01779  79  LEU   A CD1   
703  C  CD2   . LEU   A 80  ? 0.13268 0.09019 0.10795 0.01056  0.02616  -0.01628 79  LEU   A CD2   
704  N  N     . LEU   A 81  ? 0.11106 0.09082 0.08146 -0.00974 0.00872  -0.00527 80  LEU   A N     
705  C  CA    . LEU   A 81  ? 0.11500 0.09697 0.09124 -0.00259 -0.00293 0.00877  80  LEU   A CA    
706  C  C     . LEU   A 81  ? 0.10191 0.07592 0.07775 -0.00085 0.00254  -0.00662 80  LEU   A C     
707  O  O     . LEU   A 81  ? 0.12424 0.09709 0.08222 0.02171  0.01755  -0.00744 80  LEU   A O     
708  C  CB    . LEU   A 81  ? 0.15422 0.13142 0.11474 -0.03386 -0.03430 0.02200  80  LEU   A CB    
709  C  CG    . LEU   A 81  ? 0.18846 0.15984 0.14277 -0.04972 -0.03766 0.03284  80  LEU   A CG    
710  C  CD1   . LEU   A 81  ? 0.20406 0.18591 0.16247 -0.02822 -0.01297 0.03272  80  LEU   A CD1   
711  C  CD2   . LEU   A 81  ? 0.19259 0.18269 0.19115 -0.02050 -0.01084 0.05101  80  LEU   A CD2   
712  N  N     . VAL   A 82  ? 0.10776 0.09496 0.08211 -0.00294 0.01865  -0.00630 81  VAL   A N     
713  C  CA    . VAL   A 82  ? 0.07915 0.09857 0.07558 -0.01020 -0.00201 -0.00243 81  VAL   A CA    
714  C  C     . VAL   A 82  ? 0.09289 0.09042 0.07176 -0.00156 0.01656  -0.00336 81  VAL   A C     
715  O  O     . VAL   A 82  ? 0.09934 0.08546 0.09512 0.00459  0.01777  -0.00418 81  VAL   A O     
716  C  CB    . VAL   A 82  ? 0.09915 0.09342 0.08045 -0.01192 0.01481  0.00143  81  VAL   A CB    
717  C  CG1   . VAL   A 82  ? 0.12194 0.11061 0.08353 0.01362  -0.00165 -0.00798 81  VAL   A CG1   
718  C  CG2   . VAL   A 82  ? 0.11282 0.09945 0.08873 -0.01143 0.03246  -0.00011 81  VAL   A CG2   
719  N  N     . PHE   A 83  ? 0.09204 0.09818 0.07685 -0.00606 0.01999  0.00221  82  PHE   A N     
720  C  CA    . PHE   A 83  ? 0.09269 0.08436 0.09567 -0.01134 0.01269  0.00302  82  PHE   A CA    
721  C  C     . PHE   A 83  ? 0.08950 0.09243 0.08857 0.00633  0.01147  0.00042  82  PHE   A C     
722  O  O     . PHE   A 83  ? 0.11048 0.08922 0.09350 0.00461  0.00751  0.00626  82  PHE   A O     
723  C  CB    . PHE   A 83  ? 0.10883 0.09288 0.08525 -0.00648 0.02106  0.00326  82  PHE   A CB    
724  C  CG    . PHE   A 83  ? 0.11067 0.10254 0.07428 -0.00775 0.01522  0.00733  82  PHE   A CG    
725  C  CD1   . PHE   A 83  ? 0.13890 0.09573 0.05810 -0.01603 0.01655  -0.00475 82  PHE   A CD1   
726  C  CD2   . PHE   A 83  ? 0.11698 0.12621 0.07591 0.00092  0.01821  0.00589  82  PHE   A CD2   
727  C  CE1   . PHE   A 83  ? 0.13753 0.10986 0.06953 -0.00727 0.02842  0.00256  82  PHE   A CE1   
728  C  CE2   . PHE   A 83  ? 0.13498 0.12492 0.07391 -0.00161 0.01878  -0.00709 82  PHE   A CE2   
729  C  CZ    . PHE   A 83  ? 0.13951 0.12241 0.06751 0.00346  0.02397  0.01872  82  PHE   A CZ    
730  N  N     . ALA   A 84  ? 0.08915 0.09836 0.08838 -0.00267 0.00631  0.00283  83  ALA   A N     
731  C  CA    . ALA   A 84  ? 0.08682 0.11507 0.08355 -0.00315 0.01178  0.01274  83  ALA   A CA    
732  C  C     . ALA   A 84  ? 0.10398 0.09223 0.09003 -0.00573 0.00440  -0.00463 83  ALA   A C     
733  O  O     . ALA   A 84  ? 0.10477 0.08710 0.09742 0.00174  0.01456  0.00885  83  ALA   A O     
734  C  CB    . ALA   A 84  ? 0.10267 0.12616 0.08762 -0.00731 0.01881  -0.00743 83  ALA   A CB    
735  N  N     . ILE   A 85  ? 0.10389 0.09152 0.08950 0.00981  0.01641  -0.00839 84  ILE   A N     
736  C  CA    . ILE   A 85  ? 0.09399 0.09269 0.10362 -0.00303 0.03304  -0.00166 84  ILE   A CA    
737  C  C     . ILE   A 85  ? 0.08567 0.09708 0.10174 -0.00585 0.01850  0.00478  84  ILE   A C     
738  O  O     . ILE   A 85  ? 0.09742 0.11081 0.11361 -0.01442 0.01209  0.00322  84  ILE   A O     
739  C  CB    . ILE   A 85  ? 0.11872 0.10398 0.10485 0.01154  0.02836  -0.00309 84  ILE   A CB    
740  C  CG1   . ILE   A 85  ? 0.12894 0.11880 0.11437 0.03552  0.02961  0.01143  84  ILE   A CG1   
741  C  CG2   . ILE   A 85  ? 0.12187 0.12567 0.12365 -0.02572 0.03134  -0.01794 84  ILE   A CG2   
742  C  CD1   . ILE   A 85  ? 0.15510 0.14408 0.13064 0.03000  0.03369  0.01103  84  ILE   A CD1   
743  N  N     . ASN   A 86  ? 0.10494 0.09951 0.09358 0.00162  0.00602  -0.01270 85  ASN   A N     
744  C  CA    . ASN   A 86  ? 0.11419 0.11200 0.10487 -0.00671 0.00519  -0.00741 85  ASN   A CA    
745  C  C     . ASN   A 86  ? 0.12110 0.10763 0.10050 -0.01027 0.00130  -0.00200 85  ASN   A C     
746  O  O     . ASN   A 86  ? 0.14711 0.10782 0.12946 -0.00463 -0.01821 -0.01252 85  ASN   A O     
747  C  CB    . ASN   A 86  ? 0.11694 0.13317 0.08770 -0.01232 0.00080  -0.00023 85  ASN   A CB    
748  C  CG    . ASN   A 86  ? 0.12205 0.12088 0.08605 -0.00144 -0.00648 0.00379  85  ASN   A CG    
749  O  OD1   . ASN   A 86  ? 0.11606 0.14428 0.09635 -0.02031 0.00534  0.00244  85  ASN   A OD1   
750  N  ND2   . ASN   A 86  ? 0.14157 0.13760 0.10835 -0.00138 -0.00535 -0.00029 85  ASN   A ND2   
751  N  N     . ASN   A 87  ? 0.11956 0.10442 0.09268 0.00420  0.00180  0.00526  86  ASN   A N     
752  C  CA    . ASN   A 87  ? 0.12033 0.10832 0.09333 0.00621  0.00785  0.00812  86  ASN   A CA    
753  C  C     . ASN   A 87  ? 0.11227 0.09502 0.09371 -0.00004 0.02782  0.00090  86  ASN   A C     
754  O  O     . ASN   A 87  ? 0.10768 0.09768 0.10080 -0.00973 0.01842  0.00384  86  ASN   A O     
755  C  CB    . ASN   A 87  ? 0.13503 0.12882 0.09416 0.00853  0.02461  0.01310  86  ASN   A CB    
756  C  CG    . ASN   A 87  ? 0.14054 0.13671 0.09334 -0.00900 0.01796  -0.00083 86  ASN   A CG    
757  O  OD1   . ASN   A 87  ? 0.15531 0.12254 0.11140 0.01529  0.02021  0.00852  86  ASN   A OD1   
758  N  ND2   . ASN   A 87  ? 0.14106 0.16354 0.11027 0.00172  0.03500  -0.01034 86  ASN   A ND2   
759  N  N     . THR   A 88  ? 0.12480 0.10373 0.09627 -0.00805 0.03094  0.01473  87  THR   A N     
760  C  CA    . THR   A 88  ? 0.11276 0.11790 0.10654 -0.01112 0.03487  0.02105  87  THR   A CA    
761  C  C     . THR   A 88  ? 0.11275 0.08170 0.11386 -0.00773 0.03044  0.01510  87  THR   A C     
762  O  O     . THR   A 88  ? 0.10924 0.10610 0.10245 -0.00608 0.01628  0.00528  87  THR   A O     
763  C  CB    . THR   A 88  ? 0.12448 0.14689 0.13258 -0.02126 0.01902  0.04572  87  THR   A CB    
764  O  OG1   . THR   A 88  ? 0.13215 0.18107 0.15389 -0.00590 0.01388  0.03199  87  THR   A OG1   
765  C  CG2   . THR   A 88  ? 0.16573 0.16080 0.15016 -0.02629 0.02655  0.03807  87  THR   A CG2   
766  N  N     . LYS   A 89  ? 0.12364 0.08749 0.11615 -0.00329 0.01530  0.00689  88  LYS   A N     
767  C  CA    . LYS   A 89  ? 0.12791 0.09463 0.11114 0.01006  0.02967  -0.00119 88  LYS   A CA    
768  C  C     . LYS   A 89  ? 0.11874 0.09168 0.09087 0.01080  0.02736  0.00216  88  LYS   A C     
769  O  O     . LYS   A 89  ? 0.12590 0.09766 0.09782 0.01114  0.02369  0.01220  88  LYS   A O     
770  C  CB    . LYS   A 89  ? 0.15906 0.10269 0.16335 0.00567  0.03076  0.00336  88  LYS   A CB    
771  C  CG    . LYS   A 89  ? 0.18559 0.13327 0.21009 0.02958  0.06034  -0.01149 88  LYS   A CG    
772  C  CD    . LYS   A 89  ? 0.23447 0.16745 0.25253 0.02381  0.07450  -0.04016 88  LYS   A CD    
773  C  CE    . LYS   A 89  ? 0.25563 0.20991 0.28460 0.00463  0.06568  -0.03090 88  LYS   A CE    
774  N  NZ    . LYS   A 89  ? 0.21402 0.22225 0.29203 -0.00858 0.08425  -0.06079 88  LYS   A NZ    
775  N  N     . SER   A 90  ? 0.12218 0.09092 0.08258 0.00729  0.02645  0.02143  89  SER   A N     
776  C  CA    . SER   A 90  ? 0.11065 0.10302 0.07842 -0.00224 0.03544  0.01109  89  SER   A CA    
777  C  C     . SER   A 90  ? 0.10289 0.09168 0.09432 0.00354  0.03126  0.02103  89  SER   A C     
778  O  O     . SER   A 90  ? 0.10895 0.11014 0.10581 -0.00470 0.01407  0.01564  89  SER   A O     
779  C  CB    . SER   A 90  ? 0.10845 0.11023 0.08481 0.01614  0.02354  0.01549  89  SER   A CB    
780  O  OG    . SER   A 90  ? 0.11215 0.09745 0.09617 0.00606  0.01741  0.00865  89  SER   A OG    
781  N  N     . PHE   A 91  ? 0.10804 0.09410 0.09823 0.00848  0.02282  0.00589  90  PHE   A N     
782  C  CA    . PHE   A 91  ? 0.09650 0.10507 0.09046 0.00777  0.02904  -0.00080 90  PHE   A CA    
783  C  C     . PHE   A 91  ? 0.09778 0.10853 0.08943 -0.00560 0.02487  0.00273  90  PHE   A C     
784  O  O     . PHE   A 91  ? 0.10998 0.11281 0.09761 0.00403  0.02876  -0.00140 90  PHE   A O     
785  C  CB    . PHE   A 91  ? 0.11035 0.12445 0.09982 0.00927  0.03493  -0.00496 90  PHE   A CB    
786  C  CG    . PHE   A 91  ? 0.11234 0.13347 0.12669 0.00492  0.04100  -0.02315 90  PHE   A CG    
787  C  CD1   . PHE   A 91  ? 0.12509 0.12429 0.15048 0.02301  -0.00030 -0.03698 90  PHE   A CD1   
788  C  CD2   . PHE   A 91  ? 0.15403 0.19523 0.14439 0.00741  0.06968  -0.03641 90  PHE   A CD2   
789  C  CE1   . PHE   A 91  ? 0.15597 0.18633 0.17313 0.03086  0.01380  -0.06023 90  PHE   A CE1   
790  C  CE2   . PHE   A 91  ? 0.18989 0.23944 0.16913 -0.00949 0.07589  -0.05523 90  PHE   A CE2   
791  C  CZ    . PHE   A 91  ? 0.19033 0.23053 0.16790 0.02192  0.04032  -0.07645 90  PHE   A CZ    
792  N  N     . GLU   A 92  ? 0.12249 0.08479 0.09140 -0.00682 0.02661  0.01092  91  GLU   A N     
793  C  CA    . GLU   A 92  ? 0.12676 0.10838 0.09187 0.00225  0.01570  0.02894  91  GLU   A CA    
794  C  C     . GLU   A 92  ? 0.14937 0.12198 0.09556 0.01672  0.01815  0.02950  91  GLU   A C     
795  O  O     . GLU   A 92  ? 0.15645 0.18579 0.11025 0.01732  0.01814  0.04034  91  GLU   A O     
796  C  CB    . GLU   A 92  ? 0.13687 0.11154 0.10298 -0.00897 0.01442  0.01668  91  GLU   A CB    
797  C  CG    . GLU   A 92  ? 0.15070 0.12845 0.10975 -0.01110 0.01813  0.00517  91  GLU   A CG    
798  C  CD    . GLU   A 92  ? 0.13622 0.13161 0.11589 -0.01682 0.02223  0.02181  91  GLU   A CD    
799  O  OE1   . GLU   A 92  ? 0.15435 0.15463 0.10357 -0.00525 0.01447  0.03589  91  GLU   A OE1   
800  O  OE2   . GLU   A 92  ? 0.16456 0.15401 0.14204 0.01647  0.02592  0.02254  91  GLU   A OE2   
801  N  N     . ASP   A 93  ? 0.12456 0.09805 0.10529 0.01579  0.02599  0.01340  92  ASP   A N     
802  C  CA    . ASP   A 93  ? 0.12871 0.11186 0.12416 0.00243  0.02781  0.00788  92  ASP   A CA    
803  C  C     . ASP   A 93  ? 0.12949 0.09955 0.11637 0.00996  0.02723  0.02518  92  ASP   A C     
804  O  O     . ASP   A 93  ? 0.10450 0.12027 0.13586 0.00234  0.01967  0.01966  92  ASP   A O     
805  C  CB    . ASP   A 93  ? 0.13932 0.13970 0.13846 -0.00462 0.03349  -0.00451 92  ASP   A CB    
806  C  CG    . ASP   A 93  ? 0.15332 0.16855 0.16222 0.02274  0.04474  -0.00197 92  ASP   A CG    
807  O  OD1   . ASP   A 93  ? 0.18618 0.14373 0.20030 0.01971  0.04070  -0.01929 92  ASP   A OD1   
808  O  OD2   . ASP   A 93  ? 0.19248 0.20758 0.16271 -0.01729 0.05349  -0.03170 92  ASP   A OD2   
809  N  N     . ILE   A 94  ? 0.13615 0.08631 0.11919 0.00310  0.02249  0.01053  93  ILE   A N     
810  C  CA    . ILE   A 94  ? 0.11490 0.11137 0.10915 0.00037  0.00454  0.01504  93  ILE   A CA    
811  C  C     . ILE   A 94  ? 0.12324 0.11058 0.12355 0.00608  0.02055  0.04051  93  ILE   A C     
812  O  O     . ILE   A 94  ? 0.10948 0.12682 0.12908 -0.00311 0.01664  0.03090  93  ILE   A O     
813  C  CB    . ILE   A 94  ? 0.10693 0.11155 0.09573 0.00567  0.00823  0.00366  93  ILE   A CB    
814  C  CG1   . ILE   A 94  ? 0.11314 0.12583 0.09975 -0.01723 0.01402  0.01583  93  ILE   A CG1   
815  C  CG2   . ILE   A 94  ? 0.13776 0.11263 0.09699 -0.00019 0.00678  0.00452  93  ILE   A CG2   
816  C  CD1   . ILE   A 94  ? 0.14170 0.11655 0.10215 -0.00250 0.01218  0.01178  93  ILE   A CD1   
817  N  N     A HIS   A 95  ? 0.10888 0.13677 0.12309 0.00087  0.01052  0.05451  94  HIS   A N     
818  N  N     B HIS   A 95  ? 0.12615 0.14235 0.14632 0.00380  0.01780  0.06195  94  HIS   A N     
819  C  CA    A HIS   A 95  ? 0.12961 0.18158 0.14072 0.00553  0.02375  0.07782  94  HIS   A CA    
820  C  CA    B HIS   A 95  ? 0.14063 0.19238 0.18215 0.01743  0.02846  0.08771  94  HIS   A CA    
821  C  C     A HIS   A 95  ? 0.11489 0.16422 0.16155 0.01067  0.02320  0.08723  94  HIS   A C     
822  C  C     B HIS   A 95  ? 0.11723 0.17214 0.18660 0.01325  0.02086  0.08360  94  HIS   A C     
823  O  O     A HIS   A 95  ? 0.11369 0.17906 0.15663 0.00115  0.02704  0.09296  94  HIS   A O     
824  O  O     B HIS   A 95  ? 0.10773 0.19122 0.18893 -0.00122 0.01279  0.07798  94  HIS   A O     
825  C  CB    A HIS   A 95  ? 0.13378 0.20782 0.15835 -0.00390 0.02752  0.09390  94  HIS   A CB    
826  C  CB    B HIS   A 95  ? 0.15527 0.23716 0.23039 0.03037  0.02886  0.11577  94  HIS   A CB    
827  C  CG    A HIS   A 95  ? 0.13229 0.18771 0.17079 -0.01437 0.03440  0.09139  94  HIS   A CG    
828  C  CG    B HIS   A 95  ? 0.16508 0.24688 0.28000 0.01346  0.02758  0.11978  94  HIS   A CG    
829  N  ND1   A HIS   A 95  ? 0.13782 0.19074 0.15889 -0.00446 0.03045  0.09516  94  HIS   A ND1   
830  N  ND1   B HIS   A 95  ? 0.15053 0.25129 0.30837 0.00024  0.00316  0.11931  94  HIS   A ND1   
831  C  CD2   A HIS   A 95  ? 0.11881 0.17673 0.17052 -0.03844 0.02606  0.07452  94  HIS   A CD2   
832  C  CD2   B HIS   A 95  ? 0.17640 0.25900 0.29366 0.03379  0.00153  0.11848  94  HIS   A CD2   
833  C  CE1   A HIS   A 95  ? 0.12328 0.17648 0.16925 0.01767  0.01441  0.10142  94  HIS   A CE1   
834  C  CE1   B HIS   A 95  ? 0.15901 0.24965 0.32488 0.02320  0.01283  0.11005  94  HIS   A CE1   
835  N  NE2   A HIS   A 95  ? 0.11373 0.18337 0.16782 -0.01091 0.01374  0.09959  94  HIS   A NE2   
836  N  NE2   B HIS   A 95  ? 0.22031 0.26558 0.31707 0.02576  0.02605  0.10618  94  HIS   A NE2   
837  N  N     . HIS   A 96  ? 0.11669 0.14652 0.19192 0.00246  0.02066  0.06248  95  HIS   A N     
838  C  CA    . HIS   A 96  ? 0.14680 0.12425 0.21179 0.00044  0.01943  0.02950  95  HIS   A CA    
839  C  C     . HIS   A 96  ? 0.12470 0.12018 0.14601 -0.00966 0.01596  0.02033  95  HIS   A C     
840  O  O     . HIS   A 96  ? 0.11744 0.11915 0.14688 -0.00015 0.00575  0.02424  95  HIS   A O     
841  C  CB    . HIS   A 96  ? 0.20444 0.13285 0.30871 -0.00899 0.02238  0.01146  95  HIS   A CB    
842  C  CG    . HIS   A 96  ? 0.23097 0.16564 0.40372 -0.00155 0.06915  0.03309  95  HIS   A CG    
843  N  ND1   . HIS   A 96  ? 0.30238 0.15592 0.43629 -0.01290 0.08142  0.06045  95  HIS   A ND1   
844  C  CD2   . HIS   A 96  ? 0.27341 0.18095 0.44826 0.00402  0.09184  0.00812  95  HIS   A CD2   
845  C  CE1   . HIS   A 96  ? 0.33592 0.18484 0.45784 -0.00370 0.08296  0.02603  95  HIS   A CE1   
846  N  NE2   . HIS   A 96  ? 0.30327 0.17297 0.46116 -0.01771 0.08012  0.01211  95  HIS   A NE2   
847  N  N     . TYR   A 97  ? 0.13807 0.11651 0.10320 0.01148  0.01075  0.00771  96  TYR   A N     
848  C  CA    . TYR   A 97  ? 0.12097 0.12027 0.09653 0.01231  0.01783  0.02136  96  TYR   A CA    
849  C  C     . TYR   A 97  ? 0.11667 0.11538 0.09535 0.01445  0.01140  0.02178  96  TYR   A C     
850  O  O     . TYR   A 97  ? 0.11827 0.12655 0.11834 -0.00503 0.00945  0.02195  96  TYR   A O     
851  C  CB    . TYR   A 97  ? 0.13668 0.12951 0.08615 0.02143  0.02074  0.01667  96  TYR   A CB    
852  C  CG    . TYR   A 97  ? 0.12625 0.11973 0.08363 0.02267  0.01731  0.01498  96  TYR   A CG    
853  C  CD1   . TYR   A 97  ? 0.13900 0.11894 0.09434 0.02987  0.02646  0.02399  96  TYR   A CD1   
854  C  CD2   . TYR   A 97  ? 0.11496 0.12224 0.10278 0.01711  0.02957  0.01697  96  TYR   A CD2   
855  C  CE1   . TYR   A 97  ? 0.11500 0.11884 0.09657 0.02025  0.02786  0.01431  96  TYR   A CE1   
856  C  CE2   . TYR   A 97  ? 0.12733 0.11928 0.11324 0.01703  0.03840  0.00392  96  TYR   A CE2   
857  C  CZ    . TYR   A 97  ? 0.12769 0.12565 0.09352 0.02196  0.03086  0.00911  96  TYR   A CZ    
858  O  OH    . TYR   A 97  ? 0.13464 0.13669 0.11044 0.02309  0.02418  0.01252  96  TYR   A OH    
859  N  N     . ARG   A 98  ? 0.12261 0.12166 0.09471 0.02018  0.01285  0.00620  97  ARG   A N     
860  C  CA    . ARG   A 98  ? 0.14317 0.14636 0.10943 0.03060  0.01298  0.00847  97  ARG   A CA    
861  C  C     . ARG   A 98  ? 0.11242 0.14316 0.10673 0.00385  0.02335  0.01241  97  ARG   A C     
862  O  O     . ARG   A 98  ? 0.14152 0.14696 0.11228 -0.00423 0.01389  0.01080  97  ARG   A O     
863  C  CB    . ARG   A 98  ? 0.17766 0.20775 0.12553 0.04932  0.00537  -0.03043 97  ARG   A CB    
864  C  CG    . ARG   A 98  ? 0.24066 0.23530 0.17669 0.05371  0.00837  -0.04467 97  ARG   A CG    
865  C  CD    . ARG   A 98  ? 0.27003 0.23110 0.19212 -0.01556 -0.02385 -0.03457 97  ARG   A CD    
866  N  NE    . ARG   A 98  ? 0.24058 0.26235 0.21728 -0.02208 0.01594  -0.07071 97  ARG   A NE    
867  C  CZ    . ARG   A 98  ? 0.30675 0.32080 0.22440 -0.02873 0.02833  -0.09507 97  ARG   A CZ    
868  N  NH1   . ARG   A 98  ? 0.35676 0.33061 0.24203 -0.03613 0.03813  -0.09456 97  ARG   A NH1   
869  N  NH2   . ARG   A 98  ? 0.31914 0.35417 0.22970 -0.01162 0.01819  -0.11736 97  ARG   A NH2   
870  N  N     . GLU   A 99  ? 0.13448 0.12775 0.10720 0.01000  0.01961  0.03933  98  GLU   A N     
871  C  CA    . GLU   A 99  ? 0.14940 0.13122 0.12029 0.01199  0.01751  0.04090  98  GLU   A CA    
872  C  C     . GLU   A 99  ? 0.12296 0.12187 0.11050 0.01466  0.00558  0.02930  98  GLU   A C     
873  O  O     . GLU   A 99  ? 0.14213 0.14485 0.11186 0.01798  -0.00791 0.02243  98  GLU   A O     
874  C  CB    . GLU   A 99  ? 0.15702 0.18090 0.13848 0.00657  0.01084  0.05562  98  GLU   A CB    
875  C  CG    . GLU   A 99  ? 0.19849 0.26772 0.15779 0.03244  0.01382  0.07423  98  GLU   A CG    
876  C  CD    . GLU   A 99  ? 0.32589 0.35572 0.21850 0.08461  0.02549  0.08581  98  GLU   A CD    
877  O  OE1   . GLU   A 99  ? 0.37787 0.40074 0.25270 0.08378  0.03121  0.08657  98  GLU   A OE1   
878  O  OE2   . GLU   A 99  ? 0.41515 0.40310 0.24260 0.07120  0.04601  0.06379  98  GLU   A OE2   
879  N  N     . GLN   A 100 ? 0.13254 0.13109 0.09838 0.01339  0.02095  0.02407  99  GLN   A N     
880  C  CA    . GLN   A 100 ? 0.11811 0.13014 0.10211 -0.00304 0.02236  0.00682  99  GLN   A CA    
881  C  C     . GLN   A 100 ? 0.11073 0.12400 0.10611 0.00871  0.00843  -0.00261 99  GLN   A C     
882  O  O     . GLN   A 100 ? 0.12339 0.12727 0.11691 0.00571  0.00010  0.00030  99  GLN   A O     
883  C  CB    . GLN   A 100 ? 0.12542 0.13473 0.09883 0.00285  0.01007  -0.00226 99  GLN   A CB    
884  C  CG    . GLN   A 100 ? 0.12300 0.12217 0.11443 0.01339  0.00785  -0.00610 99  GLN   A CG    
885  C  CD    . GLN   A 100 ? 0.11723 0.11316 0.12368 0.00305  0.01699  -0.00394 99  GLN   A CD    
886  O  OE1   . GLN   A 100 ? 0.11235 0.12515 0.12628 -0.00380 0.01926  -0.00324 99  GLN   A OE1   
887  N  NE2   . GLN   A 100 ? 0.12640 0.11015 0.12975 0.00814  0.03133  -0.01019 99  GLN   A NE2   
888  N  N     . ILE   A 101 ? 0.14270 0.10707 0.09329 0.00590  0.00325  0.00122  100 ILE   A N     
889  C  CA    . ILE   A 101 ? 0.15402 0.11364 0.11179 -0.00051 0.00324  0.00561  100 ILE   A CA    
890  C  C     . ILE   A 101 ? 0.14829 0.12034 0.12508 -0.00029 0.00216  0.00432  100 ILE   A C     
891  O  O     . ILE   A 101 ? 0.13603 0.13313 0.16232 0.00398  -0.00329 -0.00318 100 ILE   A O     
892  C  CB    . ILE   A 101 ? 0.14034 0.10741 0.11366 0.02260  -0.00150 0.00336  100 ILE   A CB    
893  C  CG1   . ILE   A 101 ? 0.13533 0.11751 0.11027 0.01186  0.00613  0.00834  100 ILE   A CG1   
894  C  CG2   . ILE   A 101 ? 0.17992 0.12059 0.13791 0.01847  -0.00638 0.00156  100 ILE   A CG2   
895  C  CD1   . ILE   A 101 ? 0.14149 0.11765 0.12987 0.00952  0.00275  0.00332  100 ILE   A CD1   
896  N  N     . LYS   A 102 ? 0.16820 0.15328 0.10466 0.01629  -0.01647 0.00658  101 LYS   A N     
897  C  CA    . LYS   A 102 ? 0.18445 0.19918 0.12567 0.02407  -0.01896 0.00109  101 LYS   A CA    
898  C  C     . LYS   A 102 ? 0.17758 0.18667 0.14512 0.01780  -0.03377 -0.00124 101 LYS   A C     
899  O  O     . LYS   A 102 ? 0.19877 0.19613 0.15849 0.01362  -0.05356 -0.00368 101 LYS   A O     
900  C  CB    . LYS   A 102 ? 0.21457 0.25702 0.13849 0.05067  -0.00611 0.00589  101 LYS   A CB    
901  C  CG    . LYS   A 102 ? 0.25033 0.30856 0.18516 0.06208  0.02033  -0.00117 101 LYS   A CG    
902  C  CD    . LYS   A 102 ? 0.31869 0.37314 0.24241 0.06570  0.06624  0.00225  101 LYS   A CD    
903  C  CE    . LYS   A 102 ? 0.34729 0.42265 0.27174 0.04203  0.09028  0.01584  101 LYS   A CE    
904  N  NZ    . LYS   A 102 ? 0.36634 0.44797 0.27958 0.03832  0.09723  0.03128  101 LYS   A NZ    
905  N  N     . ARG   A 103 ? 0.16804 0.17071 0.16114 0.03292  -0.02712 0.01129  102 ARG   A N     
906  C  CA    . ARG   A 103 ? 0.16721 0.16954 0.17685 0.01914  -0.01664 0.00984  102 ARG   A CA    
907  C  C     . ARG   A 103 ? 0.15623 0.17367 0.17478 0.03333  -0.02308 0.00954  102 ARG   A C     
908  O  O     . ARG   A 103 ? 0.14986 0.20818 0.17852 0.02112  -0.04014 0.02871  102 ARG   A O     
909  C  CB    . ARG   A 103 ? 0.19727 0.17554 0.18501 0.03388  -0.01245 0.01140  102 ARG   A CB    
910  C  CG    . ARG   A 103 ? 0.19655 0.18557 0.18718 0.04007  -0.00846 0.01181  102 ARG   A CG    
911  C  CD    . ARG   A 103 ? 0.21170 0.16217 0.16333 0.01543  -0.00063 0.03152  102 ARG   A CD    
912  N  NE    . ARG   A 103 ? 0.19904 0.15508 0.15611 0.01021  0.01631  0.03780  102 ARG   A NE    
913  C  CZ    . ARG   A 103 ? 0.18166 0.15229 0.16555 0.01362  0.02289  0.04745  102 ARG   A CZ    
914  N  NH1   . ARG   A 103 ? 0.15930 0.17065 0.18316 0.00975  0.02331  0.04124  102 ARG   A NH1   
915  N  NH2   . ARG   A 103 ? 0.19968 0.14889 0.17447 0.01103  0.02129  0.04166  102 ARG   A NH2   
916  N  N     . VAL   A 104 ? 0.16127 0.17236 0.17573 0.04107  -0.03520 0.00738  103 VAL   A N     
917  C  CA    . VAL   A 104 ? 0.14904 0.18439 0.19250 0.02615  -0.04338 0.00020  103 VAL   A CA    
918  C  C     . VAL   A 104 ? 0.16408 0.20873 0.19848 0.01048  -0.04130 -0.01645 103 VAL   A C     
919  O  O     . VAL   A 104 ? 0.14548 0.26630 0.24062 0.00244  -0.04025 -0.04635 103 VAL   A O     
920  C  CB    . VAL   A 104 ? 0.22423 0.17976 0.19476 0.04190  -0.05213 -0.02087 103 VAL   A CB    
921  C  CG1   . VAL   A 104 ? 0.23052 0.16781 0.19728 0.03580  -0.03166 -0.04561 103 VAL   A CG1   
922  C  CG2   . VAL   A 104 ? 0.22804 0.20558 0.21433 0.03890  -0.04564 -0.00944 103 VAL   A CG2   
923  N  N     . LYS   A 105 ? 0.16513 0.14654 0.18501 0.00059  -0.02590 -0.00760 104 LYS   A N     
924  C  CA    . LYS   A 105 ? 0.17848 0.18072 0.17850 0.00071  -0.05934 0.01017  104 LYS   A CA    
925  C  C     . LYS   A 105 ? 0.23220 0.19008 0.19504 -0.00901 -0.06974 0.02110  104 LYS   A C     
926  O  O     . LYS   A 105 ? 0.26699 0.20278 0.20361 -0.02248 -0.09099 0.02865  104 LYS   A O     
927  C  CB    . LYS   A 105 ? 0.17995 0.16339 0.17112 0.00001  -0.03303 0.02816  104 LYS   A CB    
928  C  CG    . LYS   A 105 ? 0.16008 0.17533 0.17325 -0.01354 -0.03549 0.02948  104 LYS   A CG    
929  C  CD    . LYS   A 105 ? 0.17135 0.18286 0.17605 -0.03542 -0.04178 0.02723  104 LYS   A CD    
930  C  CE    . LYS   A 105 ? 0.19911 0.20062 0.18998 -0.02657 -0.03438 0.04188  104 LYS   A CE    
931  N  NZ    . LYS   A 105 ? 0.20258 0.19692 0.20415 -0.01289 -0.02869 0.04572  104 LYS   A NZ    
932  N  N     . ASP   A 106 ? 0.22684 0.18301 0.19434 0.01825  -0.06751 0.03337  105 ASP   A N     
933  C  CA    . ASP   A 106 ? 0.23513 0.21194 0.20396 0.02482  -0.10599 0.02697  105 ASP   A CA    
934  C  C     . ASP   A 106 ? 0.27018 0.21353 0.19735 0.04154  -0.11348 0.00772  105 ASP   A C     
935  O  O     . ASP   A 106 ? 0.29830 0.24407 0.22125 0.02368  -0.12426 -0.00095 105 ASP   A O     
936  C  CB    . ASP   A 106 ? 0.27326 0.25742 0.24788 0.03359  -0.10588 0.05404  105 ASP   A CB    
937  C  CG    . ASP   A 106 ? 0.30495 0.29500 0.27521 0.02437  -0.10478 0.07069  105 ASP   A CG    
938  O  OD1   . ASP   A 106 ? 0.32304 0.30474 0.27498 0.04411  -0.09357 0.09327  105 ASP   A OD1   
939  O  OD2   . ASP   A 106 ? 0.30566 0.32903 0.29744 0.01115  -0.12203 0.06939  105 ASP   A OD2   
940  N  N     . SER   A 107 ? 0.27087 0.20116 0.18303 0.06047  -0.10613 -0.01524 106 SER   A N     
941  C  CA    . SER   A 107 ? 0.28337 0.21056 0.18931 0.04897  -0.09331 -0.01550 106 SER   A CA    
942  C  C     . SER   A 107 ? 0.29022 0.23449 0.17483 0.04907  -0.08066 -0.00211 106 SER   A C     
943  O  O     . SER   A 107 ? 0.27248 0.22837 0.18937 0.02416  -0.06725 -0.00121 106 SER   A O     
944  C  CB    . SER   A 107 ? 0.31761 0.20142 0.23221 0.03844  -0.07557 -0.00409 106 SER   A CB    
945  O  OG    . SER   A 107 ? 0.35220 0.22012 0.26265 0.03246  -0.03857 -0.01969 106 SER   A OG    
946  N  N     . GLU   A 108 ? 0.32062 0.26411 0.16365 0.06519  -0.07636 -0.02081 107 GLU   A N     
947  C  CA    . GLU   A 108 ? 0.38019 0.31890 0.16991 0.07513  -0.05999 -0.00858 107 GLU   A CA    
948  C  C     . GLU   A 108 ? 0.43160 0.34750 0.16358 0.08457  -0.05000 -0.00811 107 GLU   A C     
949  O  O     . GLU   A 108 ? 0.45216 0.38000 0.18757 0.08665  -0.02464 0.01893  107 GLU   A O     
950  C  CB    . GLU   A 108 ? 0.39380 0.35581 0.19948 0.06715  -0.04379 0.01687  107 GLU   A CB    
951  C  CG    . GLU   A 108 ? 0.43799 0.40886 0.26408 0.06987  -0.00847 0.00832  107 GLU   A CG    
952  C  CD    . GLU   A 108 ? 0.50000 0.46022 0.32692 0.06242  0.03486  -0.00004 107 GLU   A CD    
953  O  OE1   . GLU   A 108 ? 0.53114 0.48263 0.34620 0.04677  0.05186  -0.01112 107 GLU   A OE1   
954  O  OE2   . GLU   A 108 ? 0.52996 0.47940 0.35343 0.04712  0.05329  0.00424  107 GLU   A OE2   
955  N  N     . ASP   A 109 ? 0.45272 0.32393 0.13328 0.08848  -0.03617 -0.02987 108 ASP   A N     
956  C  CA    . ASP   A 109 ? 0.49050 0.32191 0.14100 0.08446  -0.02754 -0.03953 108 ASP   A CA    
957  C  C     . ASP   A 109 ? 0.43550 0.27710 0.14113 0.04199  -0.02911 -0.02855 108 ASP   A C     
958  O  O     . ASP   A 109 ? 0.50618 0.29747 0.18031 0.01457  -0.06528 -0.03663 108 ASP   A O     
959  C  CB    . ASP   A 109 ? 0.58610 0.36786 0.18757 0.11042  -0.00944 -0.07417 108 ASP   A CB    
960  C  CG    . ASP   A 109 ? 0.70146 0.43324 0.23454 0.11527  0.01246  -0.10015 108 ASP   A CG    
961  O  OD1   . ASP   A 109 ? 0.74549 0.45664 0.25690 0.13095  0.03475  -0.10390 108 ASP   A OD1   
962  O  OD2   . ASP   A 109 ? 0.74547 0.45089 0.25003 0.12377  0.00370  -0.10708 108 ASP   A OD2   
963  N  N     . VAL   A 110 ? 0.26285 0.22471 0.10989 0.04447  -0.04095 -0.00844 109 VAL   A N     
964  C  CA    . VAL   A 110 ? 0.19764 0.18546 0.10838 0.02709  -0.03238 -0.01346 109 VAL   A CA    
965  C  C     . VAL   A 110 ? 0.16079 0.16625 0.10994 0.01334  -0.01829 -0.01671 109 VAL   A C     
966  O  O     . VAL   A 110 ? 0.16365 0.15877 0.11759 -0.00094 0.00346  -0.01405 109 VAL   A O     
967  C  CB    . VAL   A 110 ? 0.19550 0.14835 0.12089 0.02613  -0.03452 -0.00951 109 VAL   A CB    
968  C  CG1   . VAL   A 110 ? 0.19653 0.13574 0.12702 0.00991  -0.01633 -0.01815 109 VAL   A CG1   
969  C  CG2   . VAL   A 110 ? 0.22098 0.18075 0.14362 0.04994  -0.03966 -0.00932 109 VAL   A CG2   
970  N  N     . PRO   A 111 ? 0.13203 0.13684 0.11794 0.00917  -0.00270 -0.02423 110 PRO   A N     
971  C  CA    . PRO   A 111 ? 0.15250 0.12702 0.10950 -0.00086 0.00036  -0.02460 110 PRO   A CA    
972  C  C     . PRO   A 111 ? 0.12491 0.11882 0.08834 0.01423  0.00828  -0.02012 110 PRO   A C     
973  O  O     . PRO   A 111 ? 0.12974 0.13157 0.10106 0.00470  0.01009  -0.02520 110 PRO   A O     
974  C  CB    . PRO   A 111 ? 0.14068 0.13339 0.13264 -0.02396 0.01439  -0.02105 110 PRO   A CB    
975  C  CG    . PRO   A 111 ? 0.15941 0.15306 0.14169 -0.00902 0.00036  -0.01914 110 PRO   A CG    
976  C  CD    . PRO   A 111 ? 0.15256 0.14855 0.14410 0.00010  -0.00183 -0.02038 110 PRO   A CD    
977  N  N     . MET   A 112 ? 0.12572 0.11594 0.09444 0.00294  -0.00069 -0.01912 111 MET   A N     
978  C  CA    . MET   A 112 ? 0.13364 0.11732 0.11989 0.00987  -0.01574 -0.02150 111 MET   A CA    
979  C  C     . MET   A 112 ? 0.11795 0.09713 0.09156 0.00321  0.01220  -0.02231 111 MET   A C     
980  O  O     . MET   A 112 ? 0.14259 0.11732 0.08898 -0.00621 0.00692  -0.02957 111 MET   A O     
981  C  CB    . MET   A 112 ? 0.17900 0.12774 0.18784 0.01407  -0.03944 -0.03826 111 MET   A CB    
982  C  CG    . MET   A 112 ? 0.20389 0.14886 0.17016 0.00116  -0.00366 -0.00420 111 MET   A CG    
983  S  SD    . MET   A 112 ? 0.29119 0.15231 0.14663 -0.05290 0.02103  0.02068  111 MET   A SD    
984  C  CE    . MET   A 112 ? 0.29092 0.24312 0.20266 -0.03076 -0.00220 0.00430  111 MET   A CE    
985  N  N     . VAL   A 113 ? 0.11241 0.10399 0.08577 0.00495  0.01277  -0.01782 112 VAL   A N     
986  C  CA    . VAL   A 113 ? 0.11324 0.09153 0.09131 -0.00396 0.00972  -0.01410 112 VAL   A CA    
987  C  C     . VAL   A 113 ? 0.11684 0.08482 0.07539 0.00563  0.02739  -0.00477 112 VAL   A C     
988  O  O     . VAL   A 113 ? 0.11247 0.10349 0.09772 0.00079  0.02661  -0.02354 112 VAL   A O     
989  C  CB    . VAL   A 113 ? 0.11758 0.09521 0.10422 0.00562  0.01278  -0.00298 112 VAL   A CB    
990  C  CG1   . VAL   A 113 ? 0.15311 0.10566 0.10990 0.00653  0.00939  0.00880  112 VAL   A CG1   
991  C  CG2   . VAL   A 113 ? 0.14178 0.08752 0.12104 -0.02851 0.03425  -0.01400 112 VAL   A CG2   
992  N  N     . LEU   A 114 ? 0.11345 0.09870 0.07070 0.00477  0.01420  -0.00142 113 LEU   A N     
993  C  CA    . LEU   A 114 ? 0.12420 0.08850 0.06708 -0.01044 0.00338  0.00161  113 LEU   A CA    
994  C  C     . LEU   A 114 ? 0.11425 0.10053 0.07218 -0.00305 0.03031  -0.00333 113 LEU   A C     
995  O  O     . LEU   A 114 ? 0.12026 0.10769 0.08014 0.01598  0.01657  -0.00754 113 LEU   A O     
996  C  CB    . LEU   A 114 ? 0.13496 0.09066 0.07741 -0.00670 0.01157  -0.01776 113 LEU   A CB    
997  C  CG    . LEU   A 114 ? 0.13652 0.10446 0.08893 -0.01030 0.03315  -0.00703 113 LEU   A CG    
998  C  CD1   . LEU   A 114 ? 0.14586 0.09538 0.10675 0.00431  0.02811  -0.00293 113 LEU   A CD1   
999  C  CD2   . LEU   A 114 ? 0.13841 0.13571 0.08219 -0.00566 0.02933  0.00085  113 LEU   A CD2   
1000 N  N     . VAL   A 115 ? 0.11095 0.09781 0.06739 -0.01036 0.00981  -0.00030 114 VAL   A N     
1001 C  CA    . VAL   A 115 ? 0.09802 0.09434 0.06939 0.00526  0.01856  -0.00290 114 VAL   A CA    
1002 C  C     . VAL   A 115 ? 0.08969 0.08781 0.08760 0.00311  0.01604  -0.00475 114 VAL   A C     
1003 O  O     . VAL   A 115 ? 0.11201 0.08811 0.09752 0.00250  0.01471  -0.01336 114 VAL   A O     
1004 C  CB    . VAL   A 115 ? 0.10290 0.10591 0.07129 -0.00312 0.03970  -0.00493 114 VAL   A CB    
1005 C  CG1   . VAL   A 115 ? 0.14796 0.12831 0.07335 0.01375  0.01134  0.00861  114 VAL   A CG1   
1006 C  CG2   . VAL   A 115 ? 0.11262 0.11748 0.09280 -0.02354 0.02627  -0.00077 114 VAL   A CG2   
1007 N  N     . GLY   A 116 ? 0.09024 0.10482 0.07819 0.00161  0.00562  0.00065  115 GLY   A N     
1008 C  CA    . GLY   A 116 ? 0.11459 0.10093 0.07708 -0.00483 0.00458  0.00559  115 GLY   A CA    
1009 C  C     . GLY   A 116 ? 0.10199 0.09566 0.07650 -0.00017 0.02585  0.00523  115 GLY   A C     
1010 O  O     . GLY   A 116 ? 0.11711 0.10165 0.08534 0.01724  0.02449  0.00199  115 GLY   A O     
1011 N  N     . ASN   A 117 ? 0.09764 0.10041 0.07433 0.00008  0.02186  0.00477  116 ASN   A N     
1012 C  CA    . ASN   A 117 ? 0.11148 0.09628 0.07549 0.00804  0.02798  0.00352  116 ASN   A CA    
1013 C  C     . ASN   A 117 ? 0.09588 0.08783 0.07064 -0.00227 0.02855  0.01273  116 ASN   A C     
1014 O  O     . ASN   A 117 ? 0.11250 0.10617 0.07454 0.00028  0.01682  0.00396  116 ASN   A O     
1015 C  CB    . ASN   A 117 ? 0.10126 0.09963 0.07795 0.01580  0.03753  0.00043  116 ASN   A CB    
1016 C  CG    . ASN   A 117 ? 0.09782 0.09759 0.08699 0.00962  0.02758  0.00409  116 ASN   A CG    
1017 O  OD1   . ASN   A 117 ? 0.11556 0.09170 0.08780 -0.00369 0.02006  0.00318  116 ASN   A OD1   
1018 N  ND2   . ASN   A 117 ? 0.09441 0.10720 0.08622 0.00155  0.01914  -0.00989 116 ASN   A ND2   
1019 N  N     . LYS   A 118 ? 0.10677 0.09144 0.07425 -0.00287 0.01699  0.00334  117 LYS   A N     
1020 C  CA    . LYS   A 118 ? 0.10017 0.09570 0.09145 0.00939  0.01107  -0.00263 117 LYS   A CA    
1021 C  C     . LYS   A 118 ? 0.08802 0.09857 0.09761 0.00628  0.01476  0.00533  117 LYS   A C     
1022 O  O     . LYS   A 118 ? 0.09691 0.11429 0.10500 -0.00336 0.00941  0.00206  117 LYS   A O     
1023 C  CB    . LYS   A 118 ? 0.10424 0.10102 0.10619 0.01306  0.01782  -0.00967 117 LYS   A CB    
1024 C  CG    . LYS   A 118 ? 0.11820 0.10147 0.09632 0.00107  0.01992  -0.00294 117 LYS   A CG    
1025 C  CD    . LYS   A 118 ? 0.10447 0.10890 0.10752 0.01679  0.02299  -0.02598 117 LYS   A CD    
1026 C  CE    . LYS   A 118 ? 0.12157 0.11367 0.10344 -0.00028 0.01949  -0.02915 117 LYS   A CE    
1027 N  NZ    . LYS   A 118 ? 0.12763 0.11730 0.09596 0.00623  0.01632  -0.03042 117 LYS   A NZ    
1028 N  N     . SER   A 119 ? 0.12389 0.08373 0.08985 0.01047  0.01940  -0.01137 118 SER   A N     
1029 C  CA    . SER   A 119 ? 0.12011 0.10834 0.10614 0.02004  0.02943  -0.02011 118 SER   A CA    
1030 C  C     . SER   A 119 ? 0.11476 0.11499 0.11851 0.01613  0.02628  -0.01815 118 SER   A C     
1031 O  O     . SER   A 119 ? 0.12506 0.13489 0.14211 0.02361  0.03315  -0.01872 118 SER   A O     
1032 C  CB    . SER   A 119 ? 0.13800 0.11488 0.11557 0.01122  0.00661  -0.01114 118 SER   A CB    
1033 O  OG    . SER   A 119 ? 0.14720 0.16838 0.13718 0.01073  0.01584  -0.01633 118 SER   A OG    
1034 N  N     . ASP   A 120 ? 0.12896 0.11105 0.10848 0.01009  0.01557  -0.00233 119 ASP   A N     
1035 C  CA    . ASP   A 120 ? 0.12697 0.12700 0.12115 0.00021  0.00666  0.00708  119 ASP   A CA    
1036 C  C     . ASP   A 120 ? 0.12432 0.12486 0.13710 -0.01708 0.00808  0.00381  119 ASP   A C     
1037 O  O     . ASP   A 120 ? 0.12137 0.15759 0.15591 0.00290  -0.00256 0.00177  119 ASP   A O     
1038 C  CB    . ASP   A 120 ? 0.12991 0.12772 0.12730 -0.00131 0.01543  0.00919  119 ASP   A CB    
1039 C  CG    . ASP   A 120 ? 0.12913 0.12145 0.11598 0.00369  0.00067  0.00396  119 ASP   A CG    
1040 O  OD1   . ASP   A 120 ? 0.11494 0.11373 0.11270 0.01302  0.00319  0.00229  119 ASP   A OD1   
1041 O  OD2   . ASP   A 120 ? 0.10705 0.14781 0.13269 0.01416  -0.00235 -0.00318 119 ASP   A OD2   
1042 N  N     . LEU   A 121 ? 0.12262 0.11918 0.11704 -0.01659 0.02394  -0.00556 120 LEU   A N     
1043 C  CA    . LEU   A 121 ? 0.12598 0.12319 0.11657 -0.00210 0.01703  -0.01306 120 LEU   A CA    
1044 C  C     . LEU   A 121 ? 0.13345 0.14639 0.09918 -0.01574 0.00377  -0.01456 120 LEU   A C     
1045 O  O     . LEU   A 121 ? 0.13082 0.15411 0.12611 -0.02224 0.01299  -0.01538 120 LEU   A O     
1046 C  CB    . LEU   A 121 ? 0.13802 0.11672 0.14358 -0.00535 0.02033  -0.00899 120 LEU   A CB    
1047 C  CG    . LEU   A 121 ? 0.14336 0.11587 0.15913 -0.00634 0.01666  -0.02155 120 LEU   A CG    
1048 C  CD1   . LEU   A 121 ? 0.15991 0.10502 0.20169 0.00924  -0.00028 -0.01502 120 LEU   A CD1   
1049 C  CD2   . LEU   A 121 ? 0.16521 0.14967 0.15782 -0.01103 0.01618  -0.01568 120 LEU   A CD2   
1050 N  N     . PRO   A 122 ? 0.11172 0.15682 0.11696 -0.02339 0.00512  -0.00403 121 PRO   A N     
1051 C  CA    . PRO   A 122 ? 0.10945 0.16901 0.13552 -0.01555 0.00427  -0.00240 121 PRO   A CA    
1052 C  C     . PRO   A 122 ? 0.12618 0.16732 0.14068 -0.00999 0.00990  -0.01193 121 PRO   A C     
1053 O  O     . PRO   A 122 ? 0.12900 0.19025 0.15580 -0.00226 0.02224  -0.00554 121 PRO   A O     
1054 C  CB    . PRO   A 122 ? 0.13154 0.19430 0.13651 -0.02513 0.01059  0.00982  121 PRO   A CB    
1055 C  CG    . PRO   A 122 ? 0.13232 0.20533 0.13450 -0.03643 -0.00257 0.00065  121 PRO   A CG    
1056 C  CD    . PRO   A 122 ? 0.14086 0.18527 0.11736 -0.02599 -0.01282 0.00137  121 PRO   A CD    
1057 N  N     . SER   A 123 ? 0.14117 0.15207 0.13914 -0.00010 0.02019  0.00889  122 SER   A N     
1058 C  CA    . SER   A 123 ? 0.13853 0.14879 0.14276 -0.00354 0.00191  0.00907  122 SER   A CA    
1059 C  C     . SER   A 123 ? 0.11323 0.16370 0.13444 -0.00493 0.01775  0.01356  122 SER   A C     
1060 O  O     . SER   A 123 ? 0.13243 0.19431 0.15138 -0.01402 0.02854  0.01087  122 SER   A O     
1061 C  CB    . SER   A 123 ? 0.15267 0.15546 0.16129 -0.00492 0.03649  -0.01093 122 SER   A CB    
1062 O  OG    . SER   A 123 ? 0.17545 0.16785 0.16226 0.00852  0.03462  -0.01810 122 SER   A OG    
1063 N  N     . ARG   A 124 ? 0.10878 0.13623 0.11943 -0.00016 0.00521  0.00134  123 ARG   A N     
1064 C  CA    . ARG   A 124 ? 0.10670 0.12751 0.13115 -0.01809 0.00350  0.00395  123 ARG   A CA    
1065 C  C     . ARG   A 124 ? 0.09306 0.12904 0.12694 -0.03008 0.01463  -0.00572 123 ARG   A C     
1066 O  O     . ARG   A 124 ? 0.09731 0.14238 0.14844 -0.01621 0.00857  0.01369  123 ARG   A O     
1067 C  CB    . ARG   A 124 ? 0.15146 0.13978 0.15545 -0.01883 0.02031  -0.01592 123 ARG   A CB    
1068 C  CG    . ARG   A 124 ? 0.13359 0.13874 0.17012 0.00049  0.03378  -0.02542 123 ARG   A CG    
1069 C  CD    . ARG   A 124 ? 0.13630 0.18105 0.18357 0.01766  0.01813  -0.03110 123 ARG   A CD    
1070 N  NE    . ARG   A 124 ? 0.16938 0.18848 0.16955 -0.01298 0.01537  -0.01937 123 ARG   A NE    
1071 C  CZ    . ARG   A 124 ? 0.15839 0.17520 0.14649 -0.03597 0.03195  -0.02021 123 ARG   A CZ    
1072 N  NH1   . ARG   A 124 ? 0.13842 0.19960 0.14442 -0.01625 0.02452  -0.03197 123 ARG   A NH1   
1073 N  NH2   . ARG   A 124 ? 0.15658 0.18420 0.14034 -0.01831 0.03051  -0.00473 123 ARG   A NH2   
1074 N  N     . THR   A 125 ? 0.08909 0.13112 0.12034 -0.00118 0.00421  0.00196  124 THR   A N     
1075 C  CA    . THR   A 125 ? 0.11714 0.12939 0.11364 0.00461  0.00597  -0.00916 124 THR   A CA    
1076 C  C     . THR   A 125 ? 0.12514 0.14574 0.12021 0.00297  0.01805  0.00454  124 THR   A C     
1077 O  O     . THR   A 125 ? 0.15866 0.17921 0.12175 -0.02880 0.01367  0.01062  124 THR   A O     
1078 C  CB    . THR   A 125 ? 0.10128 0.13764 0.12373 0.00239  0.01375  -0.01439 124 THR   A CB    
1079 O  OG1   . THR   A 125 ? 0.11699 0.15311 0.13849 -0.00014 0.02832  -0.00943 124 THR   A OG1   
1080 C  CG2   . THR   A 125 ? 0.17427 0.13693 0.13148 -0.02317 0.01716  -0.01648 124 THR   A CG2   
1081 N  N     . VAL   A 126 ? 0.11760 0.13916 0.10584 0.00437  0.01453  -0.01707 125 VAL   A N     
1082 C  CA    . VAL   A 126 ? 0.12532 0.15375 0.11845 -0.00307 0.00624  -0.02128 125 VAL   A CA    
1083 C  C     . VAL   A 126 ? 0.14663 0.13965 0.11628 0.00658  -0.00108 -0.01769 125 VAL   A C     
1084 O  O     . VAL   A 126 ? 0.18693 0.13720 0.13177 0.01959  -0.01059 0.00594  125 VAL   A O     
1085 C  CB    . VAL   A 126 ? 0.12357 0.18402 0.13672 0.01054  -0.00002 -0.02655 125 VAL   A CB    
1086 C  CG1   . VAL   A 126 ? 0.15246 0.19811 0.12777 -0.01989 -0.01271 -0.01774 125 VAL   A CG1   
1087 C  CG2   . VAL   A 126 ? 0.13428 0.21309 0.16617 0.02016  -0.01019 -0.04275 125 VAL   A CG2   
1088 N  N     . ASP   A 127 ? 0.20381 0.17909 0.12329 0.05168  0.01580  -0.01752 126 ASP   A N     
1089 C  CA    . ASP   A 127 ? 0.24417 0.22173 0.13859 0.08138  0.03107  -0.02174 126 ASP   A CA    
1090 C  C     . ASP   A 127 ? 0.24092 0.18810 0.11104 0.07363  0.01729  -0.02827 126 ASP   A C     
1091 O  O     . ASP   A 127 ? 0.21604 0.19867 0.13294 0.07832  -0.01011 -0.03040 126 ASP   A O     
1092 C  CB    . ASP   A 127 ? 0.29708 0.32498 0.16227 0.09783  0.03491  -0.01632 126 ASP   A CB    
1093 C  CG    . ASP   A 127 ? 0.33293 0.41121 0.17206 0.08936  0.00690  -0.00990 126 ASP   A CG    
1094 O  OD1   . ASP   A 127 ? 0.38078 0.47519 0.18286 0.05317  0.01456  -0.02264 126 ASP   A OD1   
1095 O  OD2   . ASP   A 127 ? 0.34182 0.45986 0.19031 0.07121  -0.01189 -0.00125 126 ASP   A OD2   
1096 N  N     . THR   A 128 ? 0.22877 0.19874 0.10630 0.06304  0.01133  -0.01362 127 THR   A N     
1097 C  CA    A THR   A 128 ? 0.22364 0.19129 0.10248 0.05533  -0.00765 0.00508  127 THR   A CA    
1098 C  CA    B THR   A 128 ? 0.26367 0.21479 0.11546 0.06517  0.00137  0.00050  127 THR   A CA    
1099 C  C     . THR   A 128 ? 0.22295 0.18829 0.09960 0.06624  0.00673  0.00783  127 THR   A C     
1100 O  O     . THR   A 128 ? 0.21043 0.15334 0.11289 0.04386  0.00687  0.01647  127 THR   A O     
1101 C  CB    A THR   A 128 ? 0.19998 0.18513 0.10538 0.06428  -0.02846 0.02222  127 THR   A CB    
1102 C  CB    B THR   A 128 ? 0.32457 0.25728 0.14238 0.08393  -0.00459 0.00687  127 THR   A CB    
1103 O  OG1   A THR   A 128 ? 0.19498 0.17867 0.12245 0.02913  0.00290  0.02274  127 THR   A OG1   
1104 O  OG1   B THR   A 128 ? 0.36145 0.27545 0.17396 0.08531  0.00458  0.00631  127 THR   A OG1   
1105 C  CG2   A THR   A 128 ? 0.20038 0.17503 0.12063 0.06300  -0.00443 0.03123  127 THR   A CG2   
1106 C  CG2   B THR   A 128 ? 0.35995 0.27395 0.15162 0.07603  0.02091  0.00821  127 THR   A CG2   
1107 N  N     . LYS   A 129 ? 0.18705 0.18339 0.08643 0.04632  0.02310  -0.01008 128 LYS   A N     
1108 C  CA    . LYS   A 129 ? 0.17102 0.17937 0.09743 0.02338  0.03069  -0.00187 128 LYS   A CA    
1109 C  C     . LYS   A 129 ? 0.16448 0.13883 0.07313 0.01601  0.01500  0.00303  128 LYS   A C     
1110 O  O     . LYS   A 129 ? 0.16484 0.14350 0.08776 -0.01154 0.01305  0.00390  128 LYS   A O     
1111 C  CB    . LYS   A 129 ? 0.18898 0.23771 0.11623 0.04001  0.02553  -0.01883 128 LYS   A CB    
1112 C  CG    . LYS   A 129 ? 0.31235 0.29627 0.16144 0.07636  0.06196  -0.01967 128 LYS   A CG    
1113 C  CD    . LYS   A 129 ? 0.47507 0.36877 0.20048 0.10041  0.09866  -0.01076 128 LYS   A CD    
1114 C  CE    . LYS   A 129 ? 0.59060 0.41846 0.22384 0.10836  0.10758  0.00021  128 LYS   A CE    
1115 N  NZ    . LYS   A 129 ? 0.65901 0.45341 0.23465 0.11527  0.11768  0.00810  128 LYS   A NZ    
1116 N  N     . GLN   A 130 ? 0.15288 0.12852 0.09083 0.01042  0.01179  -0.00398 129 GLN   A N     
1117 C  CA    . GLN   A 130 ? 0.17555 0.12448 0.11265 0.01033  0.00540  0.00047  129 GLN   A CA    
1118 C  C     . GLN   A 130 ? 0.16513 0.10651 0.09371 0.00803  0.00530  -0.00257 129 GLN   A C     
1119 O  O     . GLN   A 130 ? 0.17530 0.12718 0.08965 0.01238  0.02940  0.00501  129 GLN   A O     
1120 C  CB    . GLN   A 130 ? 0.19378 0.15143 0.14457 -0.00379 -0.01185 -0.00915 129 GLN   A CB    
1121 C  CG    . GLN   A 130 ? 0.20181 0.15128 0.15541 -0.00127 -0.00128 -0.01564 129 GLN   A CG    
1122 C  CD    . GLN   A 130 ? 0.18948 0.15325 0.14998 -0.00225 -0.00888 -0.00307 129 GLN   A CD    
1123 O  OE1   . GLN   A 130 ? 0.17890 0.16858 0.14443 0.00643  -0.00461 0.01205  129 GLN   A OE1   
1124 N  NE2   . GLN   A 130 ? 0.19708 0.15437 0.15658 0.00724  0.00482  0.00779  129 GLN   A NE2   
1125 N  N     . ALA   A 131 ? 0.19585 0.11760 0.07161 0.00519  0.01056  0.00584  130 ALA   A N     
1126 C  CA    . ALA   A 131 ? 0.19406 0.13319 0.07176 0.01509  0.03516  0.00068  130 ALA   A CA    
1127 C  C     . ALA   A 131 ? 0.18341 0.12691 0.07936 0.02545  0.03483  0.00452  130 ALA   A C     
1128 O  O     . ALA   A 131 ? 0.18114 0.13642 0.09107 0.01272  0.03266  0.01026  130 ALA   A O     
1129 C  CB    . ALA   A 131 ? 0.23700 0.15325 0.07606 0.01893  0.03781  -0.00293 130 ALA   A CB    
1130 N  N     . GLN   A 132 ? 0.19305 0.13460 0.07519 0.02114  0.04185  -0.00072 131 GLN   A N     
1131 C  CA    . GLN   A 132 ? 0.17844 0.13305 0.08633 0.02778  0.03710  -0.01557 131 GLN   A CA    
1132 C  C     . GLN   A 132 ? 0.16572 0.13215 0.08319 0.01872  0.02916  -0.00725 131 GLN   A C     
1133 O  O     . GLN   A 132 ? 0.17137 0.15609 0.09073 0.00598  0.03526  -0.00399 131 GLN   A O     
1134 C  CB    . GLN   A 132 ? 0.20374 0.14953 0.11618 0.03230  0.02923  -0.01075 131 GLN   A CB    
1135 C  CG    . GLN   A 132 ? 0.23079 0.16751 0.15328 0.06825  0.03514  0.00514  131 GLN   A CG    
1136 C  CD    . GLN   A 132 ? 0.27234 0.21679 0.19718 0.06646  0.05211  0.00904  131 GLN   A CD    
1137 O  OE1   . GLN   A 132 ? 0.25814 0.25306 0.23438 0.07110  0.05253  0.00777  131 GLN   A OE1   
1138 N  NE2   . GLN   A 132 ? 0.29715 0.22595 0.21440 0.09325  0.03287  0.01410  131 GLN   A NE2   
1139 N  N     . ASP   A 133 ? 0.17412 0.12009 0.08113 0.01244  0.04547  0.00589  132 ASP   A N     
1140 C  CA    . ASP   A 133 ? 0.14692 0.14594 0.08488 0.00463  0.03445  0.01162  132 ASP   A CA    
1141 C  C     . ASP   A 133 ? 0.16254 0.13848 0.07706 -0.00325 0.03176  0.00676  132 ASP   A C     
1142 O  O     . ASP   A 133 ? 0.16606 0.15197 0.08297 -0.00501 0.02749  0.00467  132 ASP   A O     
1143 C  CB    . ASP   A 133 ? 0.14059 0.17643 0.12067 -0.00457 0.03239  0.01865  132 ASP   A CB    
1144 C  CG    . ASP   A 133 ? 0.19565 0.18870 0.14103 0.00293  0.04208  0.00776  132 ASP   A CG    
1145 O  OD1   . ASP   A 133 ? 0.21008 0.22776 0.16481 0.03196  0.05918  -0.01620 132 ASP   A OD1   
1146 O  OD2   . ASP   A 133 ? 0.17836 0.21484 0.15625 -0.00731 0.03941  0.03523  132 ASP   A OD2   
1147 N  N     . LEU   A 134 ? 0.13735 0.14090 0.08116 0.01012  0.03887  -0.00126 133 LEU   A N     
1148 C  CA    . LEU   A 134 ? 0.14994 0.12875 0.07803 0.00465  0.03731  0.00950  133 LEU   A CA    
1149 C  C     . LEU   A 134 ? 0.16188 0.13676 0.08139 0.01222  0.02683  0.01462  133 LEU   A C     
1150 O  O     . LEU   A 134 ? 0.17046 0.13320 0.09105 0.01441  0.02189  0.00961  133 LEU   A O     
1151 C  CB    . LEU   A 134 ? 0.14864 0.12548 0.08403 0.01220  0.02853  0.01179  133 LEU   A CB    
1152 C  CG    . LEU   A 134 ? 0.14531 0.12298 0.09921 0.01421  0.03911  0.00846  133 LEU   A CG    
1153 C  CD1   . LEU   A 134 ? 0.17978 0.13124 0.12047 0.02973  0.04104  0.02181  133 LEU   A CD1   
1154 C  CD2   . LEU   A 134 ? 0.16873 0.14087 0.11072 0.01199  0.04312  -0.01364 133 LEU   A CD2   
1155 N  N     . ALA   A 135 ? 0.16195 0.13304 0.07659 0.00018  0.02159  0.01177  134 ALA   A N     
1156 C  CA    . ALA   A 135 ? 0.17917 0.11947 0.07718 -0.01684 0.02349  0.00911  134 ALA   A CA    
1157 C  C     . ALA   A 135 ? 0.14989 0.12318 0.07587 -0.01130 0.03097  0.00974  134 ALA   A C     
1158 O  O     . ALA   A 135 ? 0.15438 0.15283 0.08054 -0.01939 0.02031  0.00797  134 ALA   A O     
1159 C  CB    . ALA   A 135 ? 0.17578 0.12945 0.08964 0.00162  0.03926  0.02074  134 ALA   A CB    
1160 N  N     A ARG   A 136 ? 0.17213 0.12422 0.06828 0.00377  0.02852  -0.00887 135 ARG   A N     
1161 N  N     B ARG   A 136 ? 0.16231 0.13903 0.07817 -0.00229 0.04268  -0.00583 135 ARG   A N     
1162 C  CA    A ARG   A 136 ? 0.19145 0.14268 0.07187 0.01686  0.02118  -0.01335 135 ARG   A CA    
1163 C  CA    B ARG   A 136 ? 0.16807 0.17106 0.08907 0.00289  0.04655  -0.00493 135 ARG   A CA    
1164 C  C     A ARG   A 136 ? 0.19909 0.14940 0.06968 0.00930  0.00821  -0.00687 135 ARG   A C     
1165 C  C     B ARG   A 136 ? 0.18748 0.16241 0.08131 -0.00030 0.02670  -0.00064 135 ARG   A C     
1166 O  O     A ARG   A 136 ? 0.21496 0.15939 0.08593 0.00814  0.00426  -0.00834 135 ARG   A O     
1167 O  O     B ARG   A 136 ? 0.20034 0.16906 0.09754 -0.00582 0.02806  -0.00024 135 ARG   A O     
1168 C  CB    A ARG   A 136 ? 0.21132 0.14314 0.08102 0.01205  0.03093  -0.02669 135 ARG   A CB    
1169 C  CB    B ARG   A 136 ? 0.15652 0.20666 0.10654 -0.00592 0.06621  -0.01729 135 ARG   A CB    
1170 C  CG    A ARG   A 136 ? 0.23079 0.12583 0.09940 0.03803  0.02633  -0.02023 135 ARG   A CG    
1171 C  CG    B ARG   A 136 ? 0.14372 0.22531 0.13186 -0.01111 0.06295  -0.01545 135 ARG   A CG    
1172 C  CD    A ARG   A 136 ? 0.25455 0.13487 0.11213 0.05181  0.02828  -0.01633 135 ARG   A CD    
1173 C  CD    B ARG   A 136 ? 0.18774 0.26443 0.15523 0.00634  0.06909  -0.00803 135 ARG   A CD    
1174 N  NE    A ARG   A 136 ? 0.28039 0.13111 0.11809 0.05794  0.02348  -0.00016 135 ARG   A NE    
1175 N  NE    B ARG   A 136 ? 0.21726 0.30102 0.17905 0.03788  0.06718  0.00028  135 ARG   A NE    
1176 C  CZ    A ARG   A 136 ? 0.27275 0.13628 0.13293 0.05027  0.04537  0.00600  135 ARG   A CZ    
1177 C  CZ    B ARG   A 136 ? 0.24681 0.33237 0.19676 0.04625  0.06623  0.01100  135 ARG   A CZ    
1178 N  NH1   A ARG   A 136 ? 0.27042 0.13864 0.17745 0.03073  0.07014  0.00394  135 ARG   A NH1   
1179 N  NH1   B ARG   A 136 ? 0.25836 0.34085 0.20747 0.03481  0.07596  0.00988  135 ARG   A NH1   
1180 N  NH2   A ARG   A 136 ? 0.27202 0.13759 0.12317 0.07770  0.05518  0.00469  135 ARG   A NH2   
1181 N  NH2   B ARG   A 136 ? 0.26593 0.35659 0.19705 0.03902  0.05654  0.02994  135 ARG   A NH2   
1182 N  N     . SER   A 137 ? 0.19188 0.14622 0.07650 0.00492  0.02641  0.01083  136 SER   A N     
1183 C  CA    . SER   A 137 ? 0.19327 0.16330 0.09893 -0.00580 0.01967  0.02802  136 SER   A CA    
1184 C  C     . SER   A 137 ? 0.20684 0.19037 0.09827 0.00119  0.00536  0.01793  136 SER   A C     
1185 O  O     . SER   A 137 ? 0.21336 0.23274 0.12178 0.01118  0.00302  0.02360  136 SER   A O     
1186 C  CB    . SER   A 137 ? 0.20871 0.15732 0.09057 0.00178  0.02006  0.01401  136 SER   A CB    
1187 O  OG    . SER   A 137 ? 0.21770 0.15604 0.11237 -0.00236 0.02508  0.02477  136 SER   A OG    
1188 N  N     . TYR   A 138 ? 0.18175 0.16752 0.09684 -0.01158 0.02019  0.01149  137 TYR   A N     
1189 C  CA    . TYR   A 138 ? 0.18007 0.16456 0.10247 -0.00245 0.00028  0.00384  137 TYR   A CA    
1190 C  C     . TYR   A 138 ? 0.17396 0.16888 0.10804 0.00187  -0.00732 -0.00265 137 TYR   A C     
1191 O  O     . TYR   A 138 ? 0.20257 0.19484 0.13017 -0.00588 -0.02156 -0.00492 137 TYR   A O     
1192 C  CB    . TYR   A 138 ? 0.19617 0.16590 0.10845 0.00425  0.02297  0.00141  137 TYR   A CB    
1193 C  CG    . TYR   A 138 ? 0.17089 0.13806 0.13333 0.00820  0.02865  0.00354  137 TYR   A CG    
1194 C  CD1   . TYR   A 138 ? 0.18661 0.14624 0.14887 -0.00274 0.03569  0.01366  137 TYR   A CD1   
1195 C  CD2   . TYR   A 138 ? 0.18927 0.13753 0.14534 -0.00482 0.03124  -0.00150 137 TYR   A CD2   
1196 C  CE1   . TYR   A 138 ? 0.19128 0.14843 0.16303 -0.00050 0.03360  0.01171  137 TYR   A CE1   
1197 C  CE2   . TYR   A 138 ? 0.18538 0.13146 0.16326 -0.00317 0.01862  0.00053  137 TYR   A CE2   
1198 C  CZ    . TYR   A 138 ? 0.17397 0.13220 0.17102 -0.00270 0.02974  -0.00647 137 TYR   A CZ    
1199 O  OH    . TYR   A 138 ? 0.19892 0.14079 0.20405 -0.00984 0.02643  -0.01214 137 TYR   A OH    
1200 N  N     . GLY   A 139 ? 0.19644 0.14588 0.09837 -0.00114 -0.00118 0.00149  138 GLY   A N     
1201 C  CA    . GLY   A 139 ? 0.23689 0.14636 0.10443 0.00103  -0.00109 0.00557  138 GLY   A CA    
1202 C  C     . GLY   A 139 ? 0.20445 0.14680 0.10158 -0.02645 0.00434  -0.01054 138 GLY   A C     
1203 O  O     . GLY   A 139 ? 0.21898 0.17740 0.11880 -0.05818 -0.00639 -0.01721 138 GLY   A O     
1204 N  N     . ILE   A 140 ? 0.17502 0.14751 0.07956 -0.01074 0.00583  -0.01386 139 ILE   A N     
1205 C  CA    . ILE   A 140 ? 0.15996 0.15087 0.07800 -0.01851 0.01416  -0.01079 139 ILE   A CA    
1206 C  C     . ILE   A 140 ? 0.12935 0.13621 0.08429 -0.00665 0.02599  -0.01432 139 ILE   A C     
1207 O  O     . ILE   A 140 ? 0.15780 0.14715 0.08980 0.00490  0.02775  -0.01465 139 ILE   A O     
1208 C  CB    . ILE   A 140 ? 0.13806 0.14615 0.09363 -0.02104 0.02216  -0.02337 139 ILE   A CB    
1209 C  CG1   . ILE   A 140 ? 0.15389 0.15076 0.08906 -0.00026 0.01746  -0.02385 139 ILE   A CG1   
1210 C  CG2   . ILE   A 140 ? 0.12516 0.17875 0.10764 -0.00590 0.00427  -0.01411 139 ILE   A CG2   
1211 C  CD1   . ILE   A 140 ? 0.14553 0.13335 0.10150 0.00611  0.01813  -0.00574 139 ILE   A CD1   
1212 N  N     . PRO   A 141 ? 0.14929 0.11964 0.08011 0.00574  0.01760  -0.02424 140 PRO   A N     
1213 C  CA    . PRO   A 141 ? 0.15490 0.12461 0.09224 0.00201  0.00815  -0.01298 140 PRO   A CA    
1214 C  C     . PRO   A 141 ? 0.15416 0.11429 0.08165 0.00722  0.02293  -0.00398 140 PRO   A C     
1215 O  O     . PRO   A 141 ? 0.14194 0.11869 0.09226 0.00761  0.02834  -0.01441 140 PRO   A O     
1216 C  CB    . PRO   A 141 ? 0.17071 0.12307 0.10872 -0.00997 0.01421  -0.01470 140 PRO   A CB    
1217 C  CG    . PRO   A 141 ? 0.17948 0.13835 0.12030 0.00628  0.00581  -0.01168 140 PRO   A CG    
1218 C  CD    . PRO   A 141 ? 0.15248 0.13181 0.10956 -0.01414 0.01733  -0.00042 140 PRO   A CD    
1219 N  N     . PHE   A 142 ? 0.13636 0.11341 0.09149 0.01642  0.01345  -0.02661 141 PHE   A N     
1220 C  CA    . PHE   A 142 ? 0.15144 0.11157 0.08558 0.00711  0.01738  -0.00682 141 PHE   A CA    
1221 C  C     . PHE   A 142 ? 0.15840 0.08725 0.08505 0.00471  0.02048  -0.01292 141 PHE   A C     
1222 O  O     . PHE   A 142 ? 0.17169 0.10585 0.10253 0.02549  0.02671  -0.01295 141 PHE   A O     
1223 C  CB    . PHE   A 142 ? 0.14152 0.13552 0.10355 0.00260  0.02551  -0.00680 141 PHE   A CB    
1224 C  CG    . PHE   A 142 ? 0.13201 0.12168 0.10401 -0.00518 0.00956  0.00158  141 PHE   A CG    
1225 C  CD1   . PHE   A 142 ? 0.14796 0.11654 0.08919 -0.00415 0.00050  0.00267  141 PHE   A CD1   
1226 C  CD2   . PHE   A 142 ? 0.13711 0.17062 0.13835 0.00483  0.01298  -0.00532 141 PHE   A CD2   
1227 C  CE1   . PHE   A 142 ? 0.12396 0.13866 0.09333 0.00085  0.02259  0.01660  141 PHE   A CE1   
1228 C  CE2   . PHE   A 142 ? 0.13875 0.18887 0.15231 0.02150  0.01917  -0.00874 141 PHE   A CE2   
1229 C  CZ    . PHE   A 142 ? 0.13846 0.16453 0.12643 -0.00692 0.02827  -0.00082 141 PHE   A CZ    
1230 N  N     . ILE   A 143 ? 0.13293 0.09649 0.07550 0.00805  0.01086  -0.00598 142 ILE   A N     
1231 C  CA    . ILE   A 143 ? 0.15488 0.10764 0.08599 0.00851  0.01544  -0.00199 142 ILE   A CA    
1232 C  C     . ILE   A 143 ? 0.13340 0.09764 0.07227 0.00818  0.02040  0.00092  142 ILE   A C     
1233 O  O     . ILE   A 143 ? 0.14329 0.08547 0.09245 0.01561  0.01058  -0.01489 142 ILE   A O     
1234 C  CB    . ILE   A 143 ? 0.15518 0.11031 0.11670 -0.00631 0.01067  0.00551  142 ILE   A CB    
1235 C  CG1   . ILE   A 143 ? 0.22021 0.16549 0.14411 -0.03248 -0.00422 0.01931  142 ILE   A CG1   
1236 C  CG2   . ILE   A 143 ? 0.19699 0.10674 0.11856 -0.00456 0.01604  0.01437  142 ILE   A CG2   
1237 C  CD1   . ILE   A 143 ? 0.23416 0.20037 0.18200 -0.02852 0.03297  0.01216  142 ILE   A CD1   
1238 N  N     . GLU   A 144 ? 0.13333 0.11110 0.07604 0.01891  0.02215  -0.00176 143 GLU   A N     
1239 C  CA    . GLU   A 144 ? 0.11333 0.13078 0.08783 0.00136  0.01085  -0.01457 143 GLU   A CA    
1240 C  C     . GLU   A 144 ? 0.12215 0.10752 0.08271 0.00833  0.01833  -0.00326 143 GLU   A C     
1241 O  O     . GLU   A 144 ? 0.18500 0.10736 0.10293 0.03290  0.02273  -0.00317 143 GLU   A O     
1242 C  CB    . GLU   A 144 ? 0.12211 0.14791 0.11618 0.01261  0.03425  -0.01074 143 GLU   A CB    
1243 C  CG    . GLU   A 144 ? 0.14785 0.16262 0.13499 0.01660  0.04046  -0.00746 143 GLU   A CG    
1244 C  CD    . GLU   A 144 ? 0.19187 0.21035 0.17988 0.00846  0.05690  -0.02644 143 GLU   A CD    
1245 O  OE1   . GLU   A 144 ? 0.18816 0.21465 0.19067 0.00605  0.01532  -0.00445 143 GLU   A OE1   
1246 O  OE2   . GLU   A 144 ? 0.22556 0.27147 0.23393 0.01396  0.07467  -0.05362 143 GLU   A OE2   
1247 N  N     . THR   A 145 ? 0.11868 0.10184 0.07420 0.00769  0.01758  -0.00030 144 THR   A N     
1248 C  CA    . THR   A 145 ? 0.12325 0.10443 0.06846 -0.00274 0.01390  0.00167  144 THR   A CA    
1249 C  C     . THR   A 145 ? 0.12252 0.08412 0.08643 0.00919  0.02201  0.00801  144 THR   A C     
1250 O  O     . THR   A 145 ? 0.10108 0.09142 0.09710 0.00734  0.02154  0.00732  144 THR   A O     
1251 C  CB    . THR   A 145 ? 0.11497 0.09570 0.08472 0.01067  0.01801  0.00376  144 THR   A CB    
1252 O  OG1   . THR   A 145 ? 0.10055 0.09005 0.10050 0.00322  0.01929  0.00342  144 THR   A OG1   
1253 C  CG2   . THR   A 145 ? 0.13143 0.10577 0.09570 0.00191  -0.00546 -0.00661 144 THR   A CG2   
1254 N  N     . SER   A 146 ? 0.12404 0.11166 0.08512 0.02045  0.01438  0.00556  145 SER   A N     
1255 C  CA    . SER   A 146 ? 0.12373 0.11090 0.08077 -0.00347 0.01313  0.00104  145 SER   A CA    
1256 C  C     . SER   A 146 ? 0.11785 0.10612 0.09448 0.00449  0.01615  0.00779  145 SER   A C     
1257 O  O     . SER   A 146 ? 0.14253 0.09286 0.09145 0.00341  0.02038  0.00808  145 SER   A O     
1258 C  CB    . SER   A 146 ? 0.11820 0.11553 0.08159 -0.00050 0.00431  -0.00400 145 SER   A CB    
1259 O  OG    . SER   A 146 ? 0.11386 0.12319 0.09872 0.00170  0.01280  0.00833  145 SER   A OG    
1260 N  N     . ALA   A 147 ? 0.10635 0.10366 0.09795 0.01587  0.02598  0.01546  146 ALA   A N     
1261 C  CA    . ALA   A 147 ? 0.13495 0.11586 0.09277 0.01430  0.03556  -0.00009 146 ALA   A CA    
1262 C  C     . ALA   A 147 ? 0.14479 0.12328 0.08819 0.01375  0.03600  0.00470  146 ALA   A C     
1263 O  O     . ALA   A 147 ? 0.16994 0.14678 0.11173 0.00570  0.04430  0.03097  146 ALA   A O     
1264 C  CB    . ALA   A 147 ? 0.14017 0.11558 0.12500 0.02315  0.04334  0.00603  146 ALA   A CB    
1265 N  N     . LYS   A 148 ? 0.13901 0.12333 0.09077 0.00469  0.02246  -0.00279 147 LYS   A N     
1266 C  CA    . LYS   A 148 ? 0.17027 0.14673 0.10214 0.01048  0.01201  0.00966  147 LYS   A CA    
1267 C  C     . LYS   A 148 ? 0.16187 0.15215 0.10963 0.00697  0.00174  0.02530  147 LYS   A C     
1268 O  O     . LYS   A 148 ? 0.21628 0.18614 0.12209 0.01508  0.00624  0.03998  147 LYS   A O     
1269 C  CB    . LYS   A 148 ? 0.18271 0.16727 0.12070 -0.00097 -0.01181 0.00869  147 LYS   A CB    
1270 C  CG    . LYS   A 148 ? 0.21570 0.21906 0.13454 -0.00536 -0.02644 0.01626  147 LYS   A CG    
1271 C  CD    . LYS   A 148 ? 0.23091 0.25593 0.15570 -0.02493 -0.04813 0.00550  147 LYS   A CD    
1272 C  CE    . LYS   A 148 ? 0.29695 0.28353 0.19715 -0.05726 -0.05369 0.00935  147 LYS   A CE    
1273 N  NZ    . LYS   A 148 ? 0.35451 0.30594 0.22452 -0.07251 -0.05965 0.01435  147 LYS   A NZ    
1274 N  N     . THR   A 149 ? 0.14521 0.13061 0.12075 0.01700  0.00259  0.01438  148 THR   A N     
1275 C  CA    . THR   A 149 ? 0.16440 0.12425 0.13746 0.01882  0.00027  0.02002  148 THR   A CA    
1276 C  C     . THR   A 149 ? 0.18031 0.11386 0.14332 0.01119  0.00057  0.03293  148 THR   A C     
1277 O  O     . THR   A 149 ? 0.21513 0.13138 0.16850 0.01959  -0.01362 0.03836  148 THR   A O     
1278 C  CB    . THR   A 149 ? 0.15737 0.15338 0.14040 0.02232  -0.01162 0.01664  148 THR   A CB    
1279 O  OG1   . THR   A 149 ? 0.14861 0.14492 0.13839 0.03124  0.00209  -0.00061 148 THR   A OG1   
1280 C  CG2   . THR   A 149 ? 0.17147 0.17139 0.14080 -0.00143 -0.02838 0.00183  148 THR   A CG2   
1281 N  N     . ARG   A 150 ? 0.13877 0.12930 0.13332 0.00658  0.00058  0.03299  149 ARG   A N     
1282 C  CA    . ARG   A 150 ? 0.14218 0.13165 0.15439 -0.00437 -0.00201 0.04454  149 ARG   A CA    
1283 C  C     . ARG   A 150 ? 0.14562 0.09837 0.15543 0.00894  0.00224  0.02176  149 ARG   A C     
1284 O  O     . ARG   A 150 ? 0.16653 0.12691 0.16863 -0.00864 -0.01117 0.02088  149 ARG   A O     
1285 C  CB    . ARG   A 150 ? 0.16534 0.15465 0.18794 -0.01353 0.00225  0.05404  149 ARG   A CB    
1286 C  CG    . ARG   A 150 ? 0.19332 0.17983 0.23030 -0.00491 0.02758  0.07230  149 ARG   A CG    
1287 C  CD    . ARG   A 150 ? 0.22474 0.21914 0.25553 -0.00818 0.04860  0.07006  149 ARG   A CD    
1288 N  NE    . ARG   A 150 ? 0.26617 0.22281 0.25862 0.00511  0.04124  0.05714  149 ARG   A NE    
1289 C  CZ    . ARG   A 150 ? 0.23171 0.23710 0.26358 0.02691  0.03415  0.05952  149 ARG   A CZ    
1290 N  NH1   . ARG   A 150 ? 0.23640 0.24222 0.28030 0.06020  0.07072  0.05530  149 ARG   A NH1   
1291 N  NH2   . ARG   A 150 ? 0.24009 0.25785 0.26775 0.02796  0.04564  0.06330  149 ARG   A NH2   
1292 N  N     . GLN   A 151 ? 0.14779 0.11716 0.14562 0.01539  0.01187  0.00232  150 GLN   A N     
1293 C  CA    . GLN   A 151 ? 0.15429 0.13919 0.13758 0.00816  0.01743  -0.00740 150 GLN   A CA    
1294 C  C     . GLN   A 151 ? 0.14449 0.11191 0.11700 0.00706  0.00225  0.00355  150 GLN   A C     
1295 O  O     . GLN   A 151 ? 0.14095 0.09812 0.12371 -0.00902 0.00567  0.00284  150 GLN   A O     
1296 C  CB    . GLN   A 151 ? 0.15624 0.20949 0.15284 0.00894  0.03142  -0.01332 150 GLN   A CB    
1297 C  CG    . GLN   A 151 ? 0.19052 0.22973 0.15840 0.01701  0.02323  -0.00107 150 GLN   A CG    
1298 C  CD    . GLN   A 151 ? 0.24051 0.28826 0.15574 -0.00077 0.02514  0.00129  150 GLN   A CD    
1299 O  OE1   . GLN   A 151 ? 0.27667 0.35356 0.17744 -0.01994 0.00451  0.01612  150 GLN   A OE1   
1300 N  NE2   . GLN   A 151 ? 0.30863 0.31565 0.16083 -0.05903 0.02273  0.01305  150 GLN   A NE2   
1301 N  N     . GLY   A 152 ? 0.13956 0.11257 0.13380 0.00951  0.00220  -0.01036 151 GLY   A N     
1302 C  CA    . GLY   A 152 ? 0.13217 0.10594 0.12142 0.00604  -0.00144 -0.01564 151 GLY   A CA    
1303 C  C     . GLY   A 152 ? 0.13864 0.09295 0.11379 -0.00931 0.00458  -0.01304 151 GLY   A C     
1304 O  O     . GLY   A 152 ? 0.14229 0.11094 0.10916 -0.00728 -0.00503 0.00577  151 GLY   A O     
1305 N  N     . VAL   A 153 ? 0.13687 0.09664 0.11156 -0.00093 0.01319  -0.00833 152 VAL   A N     
1306 C  CA    . VAL   A 153 ? 0.15189 0.11242 0.11681 0.01685  0.01836  -0.01410 152 VAL   A CA    
1307 C  C     . VAL   A 153 ? 0.14856 0.10334 0.11804 0.01762  0.02023  -0.00238 152 VAL   A C     
1308 O  O     . VAL   A 153 ? 0.14120 0.11691 0.12120 0.01240  0.01118  0.00099  152 VAL   A O     
1309 C  CB    . VAL   A 153 ? 0.15361 0.12986 0.11811 0.03074  0.00770  -0.02655 152 VAL   A CB    
1310 C  CG1   . VAL   A 153 ? 0.16810 0.19423 0.12881 0.03018  0.00738  -0.02171 152 VAL   A CG1   
1311 C  CG2   . VAL   A 153 ? 0.18967 0.13319 0.12719 0.02680  -0.03388 -0.02117 152 VAL   A CG2   
1312 N  N     . ASP   A 154 ? 0.13556 0.10705 0.11630 -0.00156 0.00770  0.01224  153 ASP   A N     
1313 C  CA    . ASP   A 154 ? 0.17673 0.11386 0.12499 -0.01283 0.00261  0.01612  153 ASP   A CA    
1314 C  C     . ASP   A 154 ? 0.14787 0.09915 0.12542 -0.00511 0.01235  0.01205  153 ASP   A C     
1315 O  O     . ASP   A 154 ? 0.15365 0.11343 0.13807 -0.01179 -0.00193 0.01785  153 ASP   A O     
1316 C  CB    . ASP   A 154 ? 0.21219 0.13516 0.15700 -0.00461 -0.02291 0.03091  153 ASP   A CB    
1317 C  CG    . ASP   A 154 ? 0.26237 0.17997 0.19681 -0.01310 -0.02304 0.05190  153 ASP   A CG    
1318 O  OD1   . ASP   A 154 ? 0.32663 0.22009 0.19763 -0.01727 0.01576  0.06110  153 ASP   A OD1   
1319 O  OD2   . ASP   A 154 ? 0.33964 0.22870 0.22896 0.02357  -0.01786 0.10051  153 ASP   A OD2   
1320 N  N     . ASP   A 155 ? 0.13834 0.09044 0.13114 0.00501  0.01644  -0.00045 154 ASP   A N     
1321 C  CA    . ASP   A 155 ? 0.12574 0.10114 0.13495 0.00882  0.02879  -0.00967 154 ASP   A CA    
1322 C  C     . ASP   A 155 ? 0.12340 0.10315 0.12526 -0.00069 0.01562  -0.01667 154 ASP   A C     
1323 O  O     . ASP   A 155 ? 0.12816 0.10790 0.11137 0.00551  0.01547  -0.02853 154 ASP   A O     
1324 C  CB    . ASP   A 155 ? 0.14271 0.12391 0.15096 0.02309  0.03412  -0.00670 154 ASP   A CB    
1325 C  CG    . ASP   A 155 ? 0.14985 0.13095 0.16858 -0.00008 0.02840  -0.02133 154 ASP   A CG    
1326 O  OD1   . ASP   A 155 ? 0.18085 0.14738 0.15492 -0.00042 0.03125  -0.03283 154 ASP   A OD1   
1327 O  OD2   . ASP   A 155 ? 0.19266 0.16543 0.18405 -0.00512 0.03713  -0.03426 154 ASP   A OD2   
1328 N  N     . ALA   A 156 ? 0.12766 0.08790 0.12327 0.00334  0.02509  -0.00427 155 ALA   A N     
1329 C  CA    . ALA   A 156 ? 0.12964 0.08899 0.11181 0.00635  0.01525  -0.00101 155 ALA   A CA    
1330 C  C     . ALA   A 156 ? 0.13156 0.08446 0.08865 0.00948  0.01480  -0.00657 155 ALA   A C     
1331 O  O     . ALA   A 156 ? 0.13174 0.09747 0.09372 0.01065  0.02068  0.00146  155 ALA   A O     
1332 C  CB    . ALA   A 156 ? 0.13280 0.09658 0.12055 -0.00050 -0.00128 -0.00867 155 ALA   A CB    
1333 N  N     . PHE   A 157 ? 0.12513 0.09760 0.09069 -0.00333 0.02806  -0.00603 156 PHE   A N     
1334 C  CA    . PHE   A 157 ? 0.11749 0.10394 0.08716 -0.00382 0.02899  -0.02277 156 PHE   A CA    
1335 C  C     . PHE   A 157 ? 0.13706 0.09562 0.08787 -0.00225 0.02572  -0.01200 156 PHE   A C     
1336 O  O     . PHE   A 157 ? 0.14861 0.09403 0.09379 -0.00293 0.01319  -0.01544 156 PHE   A O     
1337 C  CB    . PHE   A 157 ? 0.13579 0.10829 0.08025 -0.00204 0.01996  -0.02538 156 PHE   A CB    
1338 C  CG    . PHE   A 157 ? 0.14837 0.10204 0.08614 -0.00599 0.01988  -0.02170 156 PHE   A CG    
1339 C  CD1   . PHE   A 157 ? 0.17435 0.10613 0.09316 0.00338  0.03876  -0.01401 156 PHE   A CD1   
1340 C  CD2   . PHE   A 157 ? 0.17114 0.11237 0.08896 -0.01600 0.02390  -0.02081 156 PHE   A CD2   
1341 C  CE1   . PHE   A 157 ? 0.17217 0.12228 0.09544 -0.00236 0.04661  -0.01584 156 PHE   A CE1   
1342 C  CE2   . PHE   A 157 ? 0.16814 0.12369 0.09463 0.00171  0.02600  -0.01582 156 PHE   A CE2   
1343 C  CZ    . PHE   A 157 ? 0.16760 0.12085 0.09291 0.00435  0.03734  -0.00502 156 PHE   A CZ    
1344 N  N     . TYR   A 158 ? 0.12971 0.08670 0.09623 -0.00624 0.02806  -0.01007 157 TYR   A N     
1345 C  CA    . TYR   A 158 ? 0.14761 0.07959 0.10399 -0.00863 0.01660  -0.01363 157 TYR   A CA    
1346 C  C     . TYR   A 158 ? 0.12964 0.07420 0.09907 -0.00141 0.01956  -0.01591 157 TYR   A C     
1347 O  O     . TYR   A 158 ? 0.14126 0.08301 0.10679 -0.00785 0.01528  -0.02114 157 TYR   A O     
1348 C  CB    . TYR   A 158 ? 0.16750 0.10155 0.11871 0.00625  0.01975  0.00733  157 TYR   A CB    
1349 C  CG    . TYR   A 158 ? 0.17258 0.11818 0.13001 -0.03246 0.02598  0.00653  157 TYR   A CG    
1350 C  CD1   . TYR   A 158 ? 0.21060 0.14809 0.11926 -0.04885 0.03186  0.01173  157 TYR   A CD1   
1351 C  CD2   . TYR   A 158 ? 0.22836 0.15359 0.15447 -0.01002 0.02751  0.03965  157 TYR   A CD2   
1352 C  CE1   . TYR   A 158 ? 0.22916 0.16326 0.12257 -0.05237 0.03749  0.00618  157 TYR   A CE1   
1353 C  CE2   . TYR   A 158 ? 0.28244 0.18525 0.16198 -0.01695 0.01498  0.04993  157 TYR   A CE2   
1354 C  CZ    . TYR   A 158 ? 0.27608 0.19315 0.12990 -0.04761 0.01207  0.03316  157 TYR   A CZ    
1355 O  OH    . TYR   A 158 ? 0.32449 0.22545 0.15215 -0.07448 0.02769  0.04936  157 TYR   A OH    
1356 N  N     . THR   A 159 ? 0.13262 0.08993 0.09969 -0.00919 0.03425  -0.00346 158 THR   A N     
1357 C  CA    . THR   A 159 ? 0.12757 0.10747 0.10135 -0.00897 0.03284  -0.00830 158 THR   A CA    
1358 C  C     . THR   A 159 ? 0.13367 0.09496 0.09087 -0.00268 0.02719  -0.01707 158 THR   A C     
1359 O  O     . THR   A 159 ? 0.13499 0.10731 0.09922 0.00473  0.01886  -0.02336 158 THR   A O     
1360 C  CB    . THR   A 159 ? 0.12036 0.12079 0.10738 0.00059  0.02664  -0.01122 158 THR   A CB    
1361 O  OG1   . THR   A 159 ? 0.12918 0.11689 0.12052 0.00916  0.04573  -0.01590 158 THR   A OG1   
1362 C  CG2   . THR   A 159 ? 0.13442 0.14317 0.09974 -0.00553 0.02981  -0.00077 158 THR   A CG2   
1363 N  N     . LEU   A 160 ? 0.13251 0.08557 0.09400 -0.00221 0.02541  -0.01245 159 LEU   A N     
1364 C  CA    . LEU   A 160 ? 0.10750 0.09849 0.10129 -0.00754 0.02183  -0.00728 159 LEU   A CA    
1365 C  C     . LEU   A 160 ? 0.13325 0.09233 0.10197 -0.00547 0.03013  -0.01017 159 LEU   A C     
1366 O  O     . LEU   A 160 ? 0.13768 0.11022 0.10143 0.00109  0.01635  -0.02255 159 LEU   A O     
1367 C  CB    . LEU   A 160 ? 0.12690 0.10316 0.09573 0.00103  0.02304  -0.01239 159 LEU   A CB    
1368 C  CG    . LEU   A 160 ? 0.11955 0.10963 0.08988 -0.00822 0.02272  -0.01464 159 LEU   A CG    
1369 C  CD1   . LEU   A 160 ? 0.13647 0.12019 0.08906 -0.00463 0.01501  -0.00137 159 LEU   A CD1   
1370 C  CD2   . LEU   A 160 ? 0.15099 0.11043 0.08829 -0.00498 0.02848  -0.03092 159 LEU   A CD2   
1371 N  N     . VAL   A 161 ? 0.12391 0.09189 0.11008 -0.00528 0.02729  -0.01999 160 VAL   A N     
1372 C  CA    . VAL   A 161 ? 0.13076 0.08741 0.10945 -0.00489 0.03037  -0.01589 160 VAL   A CA    
1373 C  C     . VAL   A 161 ? 0.14458 0.10073 0.10873 -0.00414 0.03376  -0.03572 160 VAL   A C     
1374 O  O     . VAL   A 161 ? 0.13912 0.11956 0.13835 -0.00622 -0.00311 -0.02580 160 VAL   A O     
1375 C  CB    . VAL   A 161 ? 0.14092 0.08888 0.12243 -0.01534 0.03225  -0.01232 160 VAL   A CB    
1376 C  CG1   . VAL   A 161 ? 0.18109 0.12168 0.15411 -0.03013 0.03734  -0.01611 160 VAL   A CG1   
1377 C  CG2   . VAL   A 161 ? 0.17228 0.10606 0.12512 0.00164  0.04128  -0.00832 160 VAL   A CG2   
1378 N  N     . ARG   A 162 ? 0.15232 0.10460 0.10230 -0.01839 0.04432  -0.03600 161 ARG   A N     
1379 C  CA    . ARG   A 162 ? 0.14920 0.12241 0.11240 0.01078  0.02253  -0.03225 161 ARG   A CA    
1380 C  C     . ARG   A 162 ? 0.13943 0.10870 0.11150 0.01800  0.00238  -0.02870 161 ARG   A C     
1381 O  O     . ARG   A 162 ? 0.15394 0.13995 0.12465 0.00679  -0.00505 -0.04172 161 ARG   A O     
1382 C  CB    . ARG   A 162 ? 0.13957 0.12281 0.11579 0.01192  0.01522  -0.02177 161 ARG   A CB    
1383 C  CG    . ARG   A 162 ? 0.15010 0.11545 0.10827 0.00556  -0.00522 -0.02559 161 ARG   A CG    
1384 C  CD    . ARG   A 162 ? 0.15965 0.11795 0.12480 0.04227  0.03087  -0.01796 161 ARG   A CD    
1385 N  NE    . ARG   A 162 ? 0.16198 0.12099 0.12761 0.01642  0.02236  -0.02786 161 ARG   A NE    
1386 C  CZ    . ARG   A 162 ? 0.14972 0.10662 0.13950 0.01536  0.01781  -0.02519 161 ARG   A CZ    
1387 N  NH1   . ARG   A 162 ? 0.17363 0.11069 0.16222 0.00159  0.01437  -0.03352 161 ARG   A NH1   
1388 N  NH2   . ARG   A 162 ? 0.15783 0.13196 0.14338 0.01709  0.02177  -0.01368 161 ARG   A NH2   
1389 N  N     . GLU   A 163 ? 0.15590 0.10659 0.12431 0.00981  0.01057  -0.01851 162 GLU   A N     
1390 C  CA    . GLU   A 163 ? 0.14669 0.11576 0.12710 0.00852  -0.00416 -0.01625 162 GLU   A CA    
1391 C  C     . GLU   A 163 ? 0.17332 0.11408 0.12351 0.01775  0.00494  -0.02973 162 GLU   A C     
1392 O  O     . GLU   A 163 ? 0.18863 0.15403 0.11818 0.02292  -0.01721 -0.02037 162 GLU   A O     
1393 C  CB    . GLU   A 163 ? 0.14977 0.11838 0.13154 0.01063  0.02168  -0.01713 162 GLU   A CB    
1394 C  CG    . GLU   A 163 ? 0.17097 0.12986 0.13050 0.01192  0.00815  -0.02696 162 GLU   A CG    
1395 C  CD    . GLU   A 163 ? 0.20403 0.12888 0.15611 0.00873  0.01270  -0.02527 162 GLU   A CD    
1396 O  OE1   . GLU   A 163 ? 0.25197 0.14257 0.13301 0.00905  0.02612  -0.02811 162 GLU   A OE1   
1397 O  OE2   . GLU   A 163 ? 0.25732 0.15197 0.18349 0.03167  0.03271  -0.04995 162 GLU   A OE2   
1398 N  N     . ILE   A 164 ? 0.15097 0.12697 0.14183 0.01849  0.01576  -0.04477 163 ILE   A N     
1399 C  CA    . ILE   A 164 ? 0.14979 0.14351 0.16885 0.01148  0.00299  -0.05823 163 ILE   A CA    
1400 C  C     . ILE   A 164 ? 0.16890 0.16411 0.20700 0.01933  -0.02554 -0.06972 163 ILE   A C     
1401 O  O     . ILE   A 164 ? 0.19695 0.18940 0.24004 0.02248  -0.05746 -0.08528 163 ILE   A O     
1402 C  CB    . ILE   A 164 ? 0.14051 0.13058 0.16049 0.00353  0.01395  -0.03743 163 ILE   A CB    
1403 C  CG1   . ILE   A 164 ? 0.16845 0.11798 0.14047 0.00471  0.01640  -0.04576 163 ILE   A CG1   
1404 C  CG2   . ILE   A 164 ? 0.14371 0.16683 0.17592 -0.00231 0.01852  -0.02951 163 ILE   A CG2   
1405 C  CD1   . ILE   A 164 ? 0.17823 0.13689 0.12578 0.00560  0.01666  -0.02589 163 ILE   A CD1   
1406 N  N     . ARG   A 165 ? 0.15838 0.14374 0.21880 0.00226  -0.01084 -0.08470 164 ARG   A N     
1407 C  CA    . ARG   A 165 ? 0.16937 0.16048 0.24011 0.00545  -0.03049 -0.10086 164 ARG   A CA    
1408 C  C     . ARG   A 165 ? 0.21553 0.19660 0.24630 0.00885  -0.06473 -0.11774 164 ARG   A C     
1409 O  O     . ARG   A 165 ? 0.26396 0.25885 0.26688 -0.01719 -0.07730 -0.13216 164 ARG   A O     
1410 C  CB    . ARG   A 165 ? 0.16089 0.15493 0.25458 -0.01583 0.00603  -0.09117 164 ARG   A CB    
1411 C  CG    . ARG   A 165 ? 0.16682 0.17476 0.26122 -0.04317 0.05182  -0.08534 164 ARG   A CG    
1412 C  CD    . ARG   A 165 ? 0.23770 0.17968 0.26890 -0.06145 0.08343  -0.07447 164 ARG   A CD    
1413 N  NE    . ARG   A 165 ? 0.35672 0.18776 0.27149 -0.08439 0.12272  -0.08461 164 ARG   A NE    
1414 C  CZ    . ARG   A 165 ? 0.41659 0.21308 0.27638 -0.12165 0.09186  -0.07171 164 ARG   A CZ    
1415 N  NH1   . ARG   A 165 ? 0.48400 0.26374 0.28210 -0.11091 0.07202  -0.03929 164 ARG   A NH1   
1416 N  NH2   . ARG   A 165 ? 0.47455 0.21007 0.29002 -0.12821 0.04691  -0.05762 164 ARG   A NH2   
1417 N  N     . LYS   A 166 ? 0.25616 0.19573 0.22336 0.05797  -0.08145 -0.10957 165 LYS   A N     
1418 C  CA    . LYS   A 166 ? 0.33042 0.22508 0.21635 0.07532  -0.10536 -0.10272 165 LYS   A CA    
1419 C  C     . LYS   A 166 ? 0.40399 0.27944 0.25647 0.10298  -0.15541 -0.10569 165 LYS   A C     
1420 O  O     . LYS   A 166 ? 0.46445 0.30970 0.25854 0.10918  -0.16734 -0.09646 165 LYS   A O     
1421 C  CB    . LYS   A 166 ? 0.32632 0.21727 0.19854 0.09185  -0.05747 -0.09301 165 LYS   A CB    
1422 C  CG    . LYS   A 166 ? 0.34353 0.20932 0.21088 0.08995  -0.01981 -0.07905 165 LYS   A CG    
1423 C  CD    . LYS   A 166 ? 0.36582 0.20833 0.23272 0.04978  0.00852  -0.05558 165 LYS   A CD    
1424 C  CE    . LYS   A 166 ? 0.33277 0.21349 0.23935 0.04481  0.02451  -0.04610 165 LYS   A CE    
1425 N  NZ    . LYS   A 166 ? 0.32655 0.22980 0.24415 0.05340  0.05021  -0.04523 165 LYS   A NZ    
1426 N  N     . HIS   A 167 ? 0.40885 0.29124 0.31736 0.16202  -0.17853 -0.09041 166 HIS   A N     
1427 C  CA    . HIS   A 167 ? 0.46842 0.39531 0.40419 0.17597  -0.17613 -0.04748 166 HIS   A CA    
1428 C  C     . HIS   A 167 ? 0.54094 0.48386 0.45133 0.12523  -0.17287 -0.03550 166 HIS   A C     
1429 O  O     . HIS   A 167 ? 0.56646 0.51189 0.46898 0.10107  -0.16763 -0.04284 166 HIS   A O     
1430 C  CB    . HIS   A 167 ? 0.50398 0.42836 0.44834 0.22177  -0.15203 -0.00328 166 HIS   A CB    
1431 C  CG    . HIS   A 167 ? 0.52732 0.47778 0.49973 0.24635  -0.11298 0.03885  166 HIS   A CG    
1432 N  ND1   . HIS   A 167 ? 0.52759 0.49454 0.51736 0.26528  -0.10146 0.05438  166 HIS   A ND1   
1433 C  CD2   . HIS   A 167 ? 0.55989 0.50329 0.52374 0.24221  -0.08411 0.05494  166 HIS   A CD2   
1434 C  CE1   . HIS   A 167 ? 0.53839 0.50082 0.52994 0.27219  -0.08782 0.06451  166 HIS   A CE1   
1435 N  NE2   . HIS   A 167 ? 0.56393 0.50725 0.53192 0.26295  -0.07493 0.05999  166 HIS   A NE2   
1436 N  N     . LYS   A 168 ? 0.59473 0.54127 0.48239 0.07718  -0.15504 -0.02942 167 LYS   A N     
1437 C  CA    . LYS   A 168 ? 0.65952 0.59791 0.49825 0.02786  -0.14985 -0.02564 167 LYS   A CA    
1438 C  C     . LYS   A 168 ? 0.69990 0.62384 0.51630 0.00618  -0.13681 -0.03163 167 LYS   A C     
1439 O  O     . LYS   A 168 ? 0.72638 0.64116 0.53079 -0.00828 -0.12150 -0.03350 167 LYS   A O     
1440 C  CB    . LYS   A 168 ? 0.68129 0.61874 0.49646 0.01448  -0.14701 -0.01366 167 LYS   A CB    
1441 C  CG    . LYS   A 168 ? 0.69474 0.62877 0.49230 0.01645  -0.14519 0.00075  167 LYS   A CG    
1442 C  CD    . LYS   A 168 ? 0.69982 0.63203 0.48737 0.01789  -0.14813 0.00984  167 LYS   A CD    
1443 C  CE    . LYS   A 168 ? 0.69196 0.62963 0.47782 0.02069  -0.15937 0.01783  167 LYS   A CE    
1444 N  NZ    . LYS   A 168 ? 0.67530 0.61995 0.46511 0.03324  -0.17356 0.03099  167 LYS   A NZ    
1445 N  N     . SER   B 1   ? 0.21892 0.15100 0.15443 -0.03099 -0.02336 -0.00961 0   SER   D N     
1446 C  CA    . SER   B 1   ? 0.22988 0.16052 0.15996 -0.02235 -0.01313 0.00245  0   SER   D CA    
1447 C  C     . SER   B 1   ? 0.29990 0.16982 0.15020 -0.02364 -0.00864 0.00293  0   SER   D C     
1448 O  O     . SER   B 1   ? 0.37193 0.18205 0.14936 -0.01710 -0.02015 0.01361  0   SER   D O     
1449 C  CB    . SER   B 1   ? 0.24611 0.17135 0.16593 -0.00451 0.02943  0.01393  0   SER   D CB    
1450 O  OG    . SER   B 1   ? 0.25587 0.13946 0.15566 -0.01039 0.03036  -0.00662 0   SER   D OG    
1451 N  N     . MET   B 2   ? 0.27411 0.16331 0.17009 -0.03636 -0.00544 -0.01019 1   MET   D N     
1452 C  CA    . MET   B 2   ? 0.27502 0.15961 0.18980 -0.04356 0.02229  -0.03437 1   MET   D CA    
1453 C  C     . MET   B 2   ? 0.25600 0.16560 0.17167 -0.03592 0.04353  -0.03909 1   MET   D C     
1454 O  O     . MET   B 2   ? 0.30429 0.20574 0.17162 -0.02131 0.04337  -0.01835 1   MET   D O     
1455 C  CB    . MET   B 2   ? 0.28313 0.19598 0.20150 -0.01970 0.00037  -0.02952 1   MET   D CB    
1456 C  CG    . MET   B 2   ? 0.26658 0.20434 0.21086 -0.01731 -0.00053 -0.01483 1   MET   D CG    
1457 S  SD    . MET   B 2   ? 0.24759 0.22064 0.20797 -0.00096 -0.00031 -0.01243 1   MET   D SD    
1458 C  CE    . MET   B 2   ? 0.29945 0.21940 0.24323 0.01651  0.00699  0.00531  1   MET   D CE    
1459 N  N     . VAL   B 3   ? 0.25948 0.14314 0.19234 -0.03051 0.03041  -0.04852 2   VAL   D N     
1460 C  CA    . VAL   B 3   ? 0.22770 0.13383 0.20259 -0.02620 0.02109  -0.04209 2   VAL   D CA    
1461 C  C     . VAL   B 3   ? 0.20522 0.11496 0.16391 -0.00665 0.00812  -0.02348 2   VAL   D C     
1462 O  O     . VAL   B 3   ? 0.20478 0.13299 0.17128 -0.00771 0.00015  -0.03357 2   VAL   D O     
1463 C  CB    . VAL   B 3   ? 0.22390 0.17842 0.23566 0.00854  0.03196  -0.06666 2   VAL   D CB    
1464 C  CG1   . VAL   B 3   ? 0.28833 0.22560 0.24251 -0.02471 0.02824  -0.05606 2   VAL   D CG1   
1465 C  CG2   . VAL   B 3   ? 0.25982 0.19429 0.24907 0.01409  0.06034  -0.08110 2   VAL   D CG2   
1466 N  N     . ASN   B 4   ? 0.17302 0.11068 0.14126 0.00876  0.02023  -0.00321 3   ASN   D N     
1467 C  CA    . ASN   B 4   ? 0.18425 0.10879 0.11106 0.02314  0.01207  0.00234  3   ASN   D CA    
1468 C  C     . ASN   B 4   ? 0.16770 0.11523 0.11641 0.00879  0.00991  -0.00956 3   ASN   D C     
1469 O  O     . ASN   B 4   ? 0.18901 0.12812 0.14010 -0.00322 0.03670  -0.00633 3   ASN   D O     
1470 C  CB    . ASN   B 4   ? 0.18667 0.10951 0.12148 0.01536  0.00625  0.00167  3   ASN   D CB    
1471 C  CG    . ASN   B 4   ? 0.18064 0.10553 0.13736 0.03595  0.00685  0.01056  3   ASN   D CG    
1472 O  OD1   . ASN   B 4   ? 0.18758 0.11488 0.15774 0.02493  0.03134  0.00286  3   ASN   D OD1   
1473 N  ND2   . ASN   B 4   ? 0.20809 0.12135 0.13716 0.03331  0.01580  -0.01430 3   ASN   D ND2   
1474 N  N     . PRO   B 5   ? 0.18073 0.12101 0.11067 0.00409  0.01762  -0.00161 4   PRO   D N     
1475 C  CA    . PRO   B 5   ? 0.18312 0.14023 0.12076 -0.00005 0.01040  0.01048  4   PRO   D CA    
1476 C  C     . PRO   B 5   ? 0.20140 0.10016 0.11442 0.00453  0.03302  -0.01161 4   PRO   D C     
1477 O  O     . PRO   B 5   ? 0.20812 0.09932 0.12109 0.00273  0.02363  -0.01595 4   PRO   D O     
1478 C  CB    . PRO   B 5   ? 0.22261 0.20733 0.13449 0.00734  -0.00090 0.03424  4   PRO   D CB    
1479 C  CG    . PRO   B 5   ? 0.22860 0.19737 0.13128 0.05933  0.00930  0.02626  4   PRO   D CG    
1480 C  CD    . PRO   B 5   ? 0.17158 0.13242 0.12260 0.02224  0.01718  -0.00175 4   PRO   D CD    
1481 N  N     . THR   B 6   ? 0.20689 0.10045 0.11999 0.00466  0.03152  -0.00474 5   THR   D N     
1482 C  CA    . THR   B 6   ? 0.19378 0.11037 0.14335 0.01020  0.03751  0.01223  5   THR   D CA    
1483 C  C     . THR   B 6   ? 0.21412 0.10993 0.10498 0.02248  0.03160  -0.00301 5   THR   D C     
1484 O  O     . THR   B 6   ? 0.25437 0.14334 0.10026 0.02161  0.01887  -0.00794 5   THR   D O     
1485 C  CB    . THR   B 6   ? 0.22883 0.13941 0.19596 0.02416  0.05428  0.01201  5   THR   D CB    
1486 O  OG1   . THR   B 6   ? 0.24068 0.17077 0.22880 0.03822  0.05723  0.01073  5   THR   D OG1   
1487 C  CG2   . THR   B 6   ? 0.23368 0.16155 0.20569 0.01217  0.05462  0.01338  5   THR   D CG2   
1488 N  N     . VAL   B 7   ? 0.18697 0.11569 0.11876 0.01725  0.03717  -0.00688 6   VAL   D N     
1489 C  CA    . VAL   B 7   ? 0.18263 0.11481 0.14508 0.01870  0.04196  0.00251  6   VAL   D CA    
1490 C  C     . VAL   B 7   ? 0.20399 0.09162 0.13632 0.02559  0.04323  -0.00855 6   VAL   D C     
1491 O  O     . VAL   B 7   ? 0.19508 0.12520 0.13732 0.01999  0.04936  -0.00342 6   VAL   D O     
1492 C  CB    . VAL   B 7   ? 0.23028 0.15003 0.17865 0.01514  0.03600  0.02778  6   VAL   D CB    
1493 C  CG1   . VAL   B 7   ? 0.22977 0.21907 0.17666 -0.00602 0.04421  0.03876  6   VAL   D CG1   
1494 C  CG2   . VAL   B 7   ? 0.23014 0.14657 0.19259 0.01551  0.00675  0.01790  6   VAL   D CG2   
1495 N  N     . PHE   B 8   ? 0.21661 0.10595 0.15049 0.00662  0.03619  0.01618  7   PHE   D N     
1496 C  CA    . PHE   B 8   ? 0.22251 0.11236 0.15979 -0.00004 0.04655  0.00602  7   PHE   D CA    
1497 C  C     . PHE   B 8   ? 0.20709 0.10687 0.13041 0.01954  0.05481  0.00660  7   PHE   D C     
1498 O  O     . PHE   B 8   ? 0.20836 0.11182 0.10830 0.01606  0.05340  0.00514  7   PHE   D O     
1499 C  CB    . PHE   B 8   ? 0.25484 0.12484 0.17016 0.00455  0.05907  -0.01159 7   PHE   D CB    
1500 C  CG    . PHE   B 8   ? 0.27029 0.12264 0.15110 0.02277  0.09909  -0.00796 7   PHE   D CG    
1501 C  CD1   . PHE   B 8   ? 0.29977 0.14827 0.15124 0.03622  0.09211  -0.01942 7   PHE   D CD1   
1502 C  CD2   . PHE   B 8   ? 0.29796 0.14968 0.15570 0.02883  0.11286  0.00222  7   PHE   D CD2   
1503 C  CE1   . PHE   B 8   ? 0.32919 0.15936 0.15182 0.01534  0.09958  -0.01714 7   PHE   D CE1   
1504 C  CE2   . PHE   B 8   ? 0.32777 0.15988 0.16685 0.02002  0.12221  -0.00258 7   PHE   D CE2   
1505 C  CZ    . PHE   B 8   ? 0.36022 0.17130 0.15554 0.01150  0.11059  -0.01533 7   PHE   D CZ    
1506 N  N     . PHE   B 9   ? 0.22129 0.10390 0.12269 0.00531  0.06072  -0.00206 8   PHE   D N     
1507 C  CA    . PHE   B 9   ? 0.22298 0.10803 0.11791 0.00746  0.07978  0.00061  8   PHE   D CA    
1508 C  C     . PHE   B 9   ? 0.21692 0.11470 0.12312 0.02690  0.06934  -0.00840 8   PHE   D C     
1509 O  O     . PHE   B 9   ? 0.22928 0.12982 0.14193 0.01720  0.06016  0.00986  8   PHE   D O     
1510 C  CB    . PHE   B 9   ? 0.20314 0.10707 0.10955 -0.00646 0.07902  -0.01382 8   PHE   D CB    
1511 C  CG    . PHE   B 9   ? 0.18170 0.10800 0.11018 0.01186  0.05356  0.00700  8   PHE   D CG    
1512 C  CD1   . PHE   B 9   ? 0.18880 0.12443 0.10889 0.00953  0.05371  0.02405  8   PHE   D CD1   
1513 C  CD2   . PHE   B 9   ? 0.17312 0.11603 0.10016 0.02566  0.04998  -0.00237 8   PHE   D CD2   
1514 C  CE1   . PHE   B 9   ? 0.16509 0.11312 0.10674 0.01724  0.01985  0.00495  8   PHE   D CE1   
1515 C  CE2   . PHE   B 9   ? 0.15694 0.10903 0.11254 0.03426  0.03973  0.00689  8   PHE   D CE2   
1516 C  CZ    . PHE   B 9   ? 0.16746 0.09876 0.12155 0.00454  0.01556  0.00886  8   PHE   D CZ    
1517 N  N     . ASP   B 10  ? 0.22212 0.10781 0.13008 0.01809  0.08451  0.00520  9   ASP   D N     
1518 C  CA    . ASP   B 10  ? 0.26163 0.11940 0.14311 0.02347  0.09917  0.00905  9   ASP   D CA    
1519 C  C     . ASP   B 10  ? 0.22500 0.10893 0.14819 0.03035  0.09851  0.01811  9   ASP   D C     
1520 O  O     . ASP   B 10  ? 0.23006 0.12792 0.15530 0.02403  0.07322  0.00843  9   ASP   D O     
1521 C  CB    . ASP   B 10  ? 0.31840 0.14231 0.14832 0.04237  0.09803  0.00524  9   ASP   D CB    
1522 C  CG    . ASP   B 10  ? 0.34972 0.18037 0.16300 0.04397  0.06689  0.00167  9   ASP   D CG    
1523 O  OD1   . ASP   B 10  ? 0.31375 0.18826 0.19357 0.06196  0.07065  -0.03469 9   ASP   D OD1   
1524 O  OD2   . ASP   B 10  ? 0.43062 0.21240 0.16437 0.05282  0.04312  0.01061  9   ASP   D OD2   
1525 N  N     . ILE   B 11  ? 0.24320 0.11624 0.15944 0.02342  0.10166  0.00304  10  ILE   D N     
1526 C  CA    . ILE   B 11  ? 0.23517 0.10454 0.15377 0.01369  0.10238  0.00389  10  ILE   D CA    
1527 C  C     . ILE   B 11  ? 0.21187 0.12390 0.15081 0.00558  0.10372  0.01144  10  ILE   D C     
1528 O  O     . ILE   B 11  ? 0.22306 0.12811 0.17871 0.00715  0.11835  0.00723  10  ILE   D O     
1529 C  CB    . ILE   B 11  ? 0.24269 0.12729 0.16293 -0.00335 0.10531  0.00585  10  ILE   D CB    
1530 C  CG1   . ILE   B 11  ? 0.25247 0.12404 0.16912 0.00578  0.11578  0.01936  10  ILE   D CG1   
1531 C  CG2   . ILE   B 11  ? 0.23279 0.11946 0.16850 0.00996  0.07995  -0.00600 10  ILE   D CG2   
1532 C  CD1   . ILE   B 11  ? 0.26081 0.13501 0.17026 -0.01871 0.10698  0.01807  10  ILE   D CD1   
1533 N  N     . ALA   B 12  ? 0.21915 0.12081 0.12650 0.00718  0.07829  0.01008  11  ALA   D N     
1534 C  CA    . ALA   B 12  ? 0.23499 0.12562 0.11982 0.00807  0.06809  0.02352  11  ALA   D CA    
1535 C  C     . ALA   B 12  ? 0.20032 0.11681 0.12862 0.00324  0.08292  0.02881  11  ALA   D C     
1536 O  O     . ALA   B 12  ? 0.16726 0.11898 0.13413 0.00789  0.05707  0.02530  11  ALA   D O     
1537 C  CB    . ALA   B 12  ? 0.29099 0.13777 0.12872 0.00887  0.06631  0.03059  11  ALA   D CB    
1538 N  N     . VAL   B 13  ? 0.19304 0.12796 0.13207 0.00453  0.06558  0.03281  12  VAL   D N     
1539 C  CA    . VAL   B 13  ? 0.18944 0.13454 0.13927 0.00493  0.06525  0.03110  12  VAL   D CA    
1540 C  C     . VAL   B 13  ? 0.19274 0.11955 0.14658 0.00112  0.06513  0.03164  12  VAL   D C     
1541 O  O     . VAL   B 13  ? 0.19937 0.13854 0.16569 -0.00506 0.07654  0.04115  12  VAL   D O     
1542 C  CB    . VAL   B 13  ? 0.20351 0.14870 0.15925 0.01303  0.04528  0.02519  12  VAL   D CB    
1543 C  CG1   . VAL   B 13  ? 0.24094 0.16113 0.16699 0.02818  0.03977  0.01446  12  VAL   D CG1   
1544 C  CG2   . VAL   B 13  ? 0.24536 0.16715 0.17661 0.02617  0.05463  0.03334  12  VAL   D CG2   
1545 N  N     . ASP   B 14  ? 0.18811 0.12950 0.15177 -0.00465 0.03938  0.04885  13  ASP   D N     
1546 C  CA    . ASP   B 14  ? 0.22818 0.12963 0.14092 -0.01867 0.04970  0.05165  13  ASP   D CA    
1547 C  C     . ASP   B 14  ? 0.25546 0.15216 0.13741 -0.00922 0.06559  0.03852  13  ASP   D C     
1548 O  O     . ASP   B 14  ? 0.29368 0.17791 0.16023 0.00035  0.06259  0.05519  13  ASP   D O     
1549 C  CB    . ASP   B 14  ? 0.21426 0.14832 0.15852 -0.02672 0.01846  0.05188  13  ASP   D CB    
1550 C  CG    . ASP   B 14  ? 0.19990 0.15652 0.16488 -0.04670 -0.00399 0.05775  13  ASP   D CG    
1551 O  OD1   . ASP   B 14  ? 0.21469 0.15438 0.14890 -0.03244 -0.01555 0.05556  13  ASP   D OD1   
1552 O  OD2   . ASP   B 14  ? 0.22743 0.20083 0.20433 -0.05966 -0.01348 0.05306  13  ASP   D OD2   
1553 N  N     . GLY   B 15  ? 0.26152 0.16493 0.13927 -0.01647 0.04852  0.01763  14  GLY   D N     
1554 C  CA    . GLY   B 15  ? 0.31810 0.18228 0.15978 -0.04394 0.05652  -0.02329 14  GLY   D CA    
1555 C  C     . GLY   B 15  ? 0.37111 0.21129 0.17155 -0.05349 0.10573  -0.02155 14  GLY   D C     
1556 O  O     . GLY   B 15  ? 0.43975 0.28408 0.20332 -0.06254 0.10770  -0.05887 14  GLY   D O     
1557 N  N     . GLU   B 16  ? 0.34490 0.18627 0.17632 -0.01928 0.11419  0.01192  15  GLU   D N     
1558 C  CA    . GLU   B 16  ? 0.36566 0.21998 0.21630 -0.01774 0.14291  0.02462  15  GLU   D CA    
1559 C  C     . GLU   B 16  ? 0.33908 0.20492 0.21055 -0.00418 0.14745  0.02329  15  GLU   D C     
1560 O  O     . GLU   B 16  ? 0.34161 0.18919 0.20680 0.00708  0.14731  0.02229  15  GLU   D O     
1561 C  CB    . GLU   B 16  ? 0.38761 0.26088 0.26903 -0.03732 0.17358  0.02218  15  GLU   D CB    
1562 C  CG    . GLU   B 16  ? 0.48559 0.36039 0.31977 -0.04889 0.17754  -0.00078 15  GLU   D CG    
1563 C  CD    . GLU   B 16  ? 0.57138 0.43933 0.35842 -0.04722 0.20489  -0.01282 15  GLU   D CD    
1564 O  OE1   . GLU   B 16  ? 0.59347 0.45669 0.36905 -0.04821 0.19748  -0.02729 15  GLU   D OE1   
1565 O  OE2   . GLU   B 16  ? 0.61027 0.47594 0.38153 -0.04557 0.20244  -0.00608 15  GLU   D OE2   
1566 N  N     . PRO   B 17  ? 0.34485 0.18682 0.21747 0.00822  0.15227  0.02636  16  PRO   D N     
1567 C  CA    . PRO   B 17  ? 0.31999 0.17568 0.23180 0.01286  0.15825  0.02026  16  PRO   D CA    
1568 C  C     . PRO   B 17  ? 0.29356 0.18026 0.24846 0.00631  0.15773  0.02657  16  PRO   D C     
1569 O  O     . PRO   B 17  ? 0.29179 0.23382 0.25580 -0.00438 0.14791  0.05791  16  PRO   D O     
1570 C  CB    . PRO   B 17  ? 0.38617 0.19359 0.23192 0.02082  0.16605  0.02082  16  PRO   D CB    
1571 C  CG    . PRO   B 17  ? 0.45177 0.21768 0.23211 0.03433  0.15207  0.02200  16  PRO   D CG    
1572 C  CD    . PRO   B 17  ? 0.41154 0.20340 0.22006 0.02399  0.16239  0.02014  16  PRO   D CD    
1573 N  N     . LEU   B 18  ? 0.26485 0.14489 0.24923 0.01173  0.14208  0.02407  17  LEU   D N     
1574 C  CA    . LEU   B 18  ? 0.25677 0.14887 0.25484 0.00775  0.14209  0.02280  17  LEU   D CA    
1575 C  C     . LEU   B 18  ? 0.24488 0.16142 0.27098 0.00147  0.14488  0.02271  17  LEU   D C     
1576 O  O     . LEU   B 18  ? 0.25588 0.19535 0.31189 -0.00575 0.16011  0.01832  17  LEU   D O     
1577 C  CB    . LEU   B 18  ? 0.24874 0.15152 0.24954 0.00213  0.13163  0.02107  17  LEU   D CB    
1578 C  CG    . LEU   B 18  ? 0.25405 0.16491 0.24574 -0.01428 0.10372  0.03231  17  LEU   D CG    
1579 C  CD1   . LEU   B 18  ? 0.28453 0.22660 0.25991 -0.02218 0.09712  0.03999  17  LEU   D CD1   
1580 C  CD2   . LEU   B 18  ? 0.25149 0.18373 0.24138 -0.00318 0.09268  0.02418  17  LEU   D CD2   
1581 N  N     . GLY   B 19  ? 0.24249 0.14167 0.24908 -0.00349 0.13635  0.02670  18  GLY   D N     
1582 C  CA    . GLY   B 19  ? 0.24594 0.14012 0.24951 0.01444  0.14826  0.01139  18  GLY   D CA    
1583 C  C     . GLY   B 19  ? 0.24159 0.13198 0.24412 0.01808  0.14453  0.00965  18  GLY   D C     
1584 O  O     . GLY   B 19  ? 0.24759 0.14455 0.24067 0.03335  0.14138  0.01435  18  GLY   D O     
1585 N  N     . ARG   B 20  ? 0.26189 0.13891 0.24988 0.03333  0.15101  0.02239  19  ARG   D N     
1586 C  CA    . ARG   B 20  ? 0.24189 0.13650 0.25208 0.03178  0.14541  0.02126  19  ARG   D CA    
1587 C  C     . ARG   B 20  ? 0.20715 0.14072 0.24905 0.04518  0.12460  0.02962  19  ARG   D C     
1588 O  O     . ARG   B 20  ? 0.20205 0.18583 0.28187 0.04781  0.11037  0.06389  19  ARG   D O     
1589 C  CB    . ARG   B 20  ? 0.28555 0.15213 0.26037 0.02034  0.16157  0.00696  19  ARG   D CB    
1590 C  CG    . ARG   B 20  ? 0.32702 0.15591 0.25516 0.02325  0.16892  0.00754  19  ARG   D CG    
1591 C  CD    . ARG   B 20  ? 0.35131 0.15975 0.25289 0.02961  0.17356  0.02284  19  ARG   D CD    
1592 N  NE    . ARG   B 20  ? 0.36577 0.16348 0.25675 0.04275  0.17223  0.01310  19  ARG   D NE    
1593 C  CZ    . ARG   B 20  ? 0.40645 0.17737 0.25222 0.04602  0.17229  0.00562  19  ARG   D CZ    
1594 N  NH1   . ARG   B 20  ? 0.42196 0.17109 0.25707 0.00600  0.18003  -0.01536 19  ARG   D NH1   
1595 N  NH2   . ARG   B 20  ? 0.45543 0.21247 0.25389 0.04782  0.18000  0.00332  19  ARG   D NH2   
1596 N  N     . VAL   B 21  ? 0.20482 0.12570 0.21010 0.01861  0.10756  0.01755  20  VAL   D N     
1597 C  CA    . VAL   B 21  ? 0.18671 0.12326 0.19246 0.01616  0.08771  0.02197  20  VAL   D CA    
1598 C  C     . VAL   B 21  ? 0.17983 0.12048 0.19330 0.02749  0.07653  0.01681  20  VAL   D C     
1599 O  O     . VAL   B 21  ? 0.18355 0.13235 0.20095 0.01366  0.05688  0.00556  20  VAL   D O     
1600 C  CB    . VAL   B 21  ? 0.20027 0.14148 0.18340 0.00036  0.06666  0.01148  20  VAL   D CB    
1601 C  CG1   . VAL   B 21  ? 0.20592 0.14892 0.17608 0.00414  0.05374  0.01513  20  VAL   D CG1   
1602 C  CG2   . VAL   B 21  ? 0.21312 0.14715 0.19169 0.01245  0.05768  0.00781  20  VAL   D CG2   
1603 N  N     . SER   B 22  ? 0.17806 0.10437 0.17894 0.01499  0.08182  0.02003  21  SER   D N     
1604 C  CA    . SER   B 22  ? 0.20178 0.11071 0.17040 -0.00084 0.07665  0.00480  21  SER   D CA    
1605 C  C     . SER   B 22  ? 0.18588 0.10989 0.16115 0.01902  0.06038  0.01304  21  SER   D C     
1606 O  O     . SER   B 22  ? 0.18073 0.14041 0.15152 0.00457  0.05309  0.01372  21  SER   D O     
1607 C  CB    . SER   B 22  ? 0.21834 0.14533 0.18354 0.02697  0.08432  -0.01492 21  SER   D CB    
1608 O  OG    . SER   B 22  ? 0.20295 0.17615 0.22313 0.02448  0.07045  -0.02062 21  SER   D OG    
1609 N  N     . PHE   B 23  ? 0.16972 0.10620 0.15107 0.01222  0.06782  -0.00097 22  PHE   D N     
1610 C  CA    . PHE   B 23  ? 0.16461 0.10196 0.14011 0.00179  0.05344  0.00355  22  PHE   D CA    
1611 C  C     . PHE   B 23  ? 0.18380 0.10984 0.12858 -0.00065 0.04632  -0.01055 22  PHE   D C     
1612 O  O     . PHE   B 23  ? 0.21200 0.11240 0.12511 0.00372  0.02099  0.00109  22  PHE   D O     
1613 C  CB    . PHE   B 23  ? 0.15932 0.09524 0.15825 0.02073  0.04928  0.00201  22  PHE   D CB    
1614 C  CG    . PHE   B 23  ? 0.14699 0.11540 0.15355 0.01414  0.04523  -0.00852 22  PHE   D CG    
1615 C  CD1   . PHE   B 23  ? 0.15248 0.11737 0.14856 0.02039  0.03860  -0.02262 22  PHE   D CD1   
1616 C  CD2   . PHE   B 23  ? 0.17257 0.11400 0.13552 0.01582  0.02418  -0.01290 22  PHE   D CD2   
1617 C  CE1   . PHE   B 23  ? 0.15969 0.11938 0.14672 0.03633  0.02513  -0.01602 22  PHE   D CE1   
1618 C  CE2   . PHE   B 23  ? 0.18514 0.11722 0.14205 0.02670  0.03466  -0.02216 22  PHE   D CE2   
1619 C  CZ    . PHE   B 23  ? 0.16716 0.11969 0.14121 0.02583  0.02108  -0.01930 22  PHE   D CZ    
1620 N  N     . GLU   B 24  ? 0.14365 0.10670 0.12793 0.00745  0.05303  -0.00293 23  GLU   D N     
1621 C  CA    . GLU   B 24  ? 0.15954 0.09461 0.13598 0.01941  0.04033  0.00072  23  GLU   D CA    
1622 C  C     . GLU   B 24  ? 0.13800 0.09459 0.11128 0.02147  0.03453  -0.01248 23  GLU   D C     
1623 O  O     . GLU   B 24  ? 0.15529 0.11101 0.11841 -0.00327 0.02942  -0.02803 23  GLU   D O     
1624 C  CB    . GLU   B 24  ? 0.15584 0.10933 0.16770 0.01051  0.01825  -0.00074 23  GLU   D CB    
1625 C  CG    . GLU   B 24  ? 0.16932 0.09743 0.18856 0.02623  0.02082  0.00761  23  GLU   D CG    
1626 C  CD    . GLU   B 24  ? 0.19868 0.12208 0.22689 0.01143  0.01523  -0.00302 23  GLU   D CD    
1627 O  OE1   . GLU   B 24  ? 0.24556 0.15385 0.25585 0.03088  -0.00679 0.02643  23  GLU   D OE1   
1628 O  OE2   . GLU   B 24  ? 0.20783 0.12794 0.21864 0.02399  -0.01636 0.00205  23  GLU   D OE2   
1629 N  N     . LEU   B 25  ? 0.13289 0.09482 0.11229 0.01414  0.02561  -0.00383 24  LEU   D N     
1630 C  CA    . LEU   B 25  ? 0.14492 0.09242 0.12674 0.01958  0.02969  0.00070  24  LEU   D CA    
1631 C  C     . LEU   B 25  ? 0.14057 0.09851 0.10632 0.00535  0.02607  -0.00317 24  LEU   D C     
1632 O  O     . LEU   B 25  ? 0.17837 0.08649 0.11520 0.01496  0.03680  -0.01169 24  LEU   D O     
1633 C  CB    . LEU   B 25  ? 0.14436 0.08509 0.12607 -0.00120 0.01867  -0.00469 24  LEU   D CB    
1634 C  CG    . LEU   B 25  ? 0.14798 0.09476 0.12142 0.00765  0.01098  -0.00699 24  LEU   D CG    
1635 C  CD1   . LEU   B 25  ? 0.17035 0.11521 0.12639 0.01600  0.00135  -0.00871 24  LEU   D CD1   
1636 C  CD2   . LEU   B 25  ? 0.19356 0.09497 0.13230 0.00523  0.00611  -0.01148 24  LEU   D CD2   
1637 N  N     . PHE   B 26  ? 0.16237 0.10127 0.11055 0.00792  0.01629  0.00282  25  PHE   D N     
1638 C  CA    . PHE   B 26  ? 0.17738 0.10858 0.10747 -0.00677 0.02985  0.00937  25  PHE   D CA    
1639 C  C     . PHE   B 26  ? 0.17862 0.09685 0.09783 0.00981  0.03526  0.00472  25  PHE   D C     
1640 O  O     . PHE   B 26  ? 0.19915 0.10993 0.12015 0.00851  0.03772  0.00448  25  PHE   D O     
1641 C  CB    . PHE   B 26  ? 0.17419 0.12177 0.11071 -0.01049 0.02825  -0.01198 25  PHE   D CB    
1642 C  CG    . PHE   B 26  ? 0.18820 0.12124 0.12339 0.00977  0.01159  -0.00785 25  PHE   D CG    
1643 C  CD1   . PHE   B 26  ? 0.20744 0.15690 0.14033 -0.01465 0.02588  -0.01704 25  PHE   D CD1   
1644 C  CD2   . PHE   B 26  ? 0.21544 0.10807 0.13439 -0.00355 -0.02686 0.01209  25  PHE   D CD2   
1645 C  CE1   . PHE   B 26  ? 0.20553 0.16966 0.14641 -0.00942 0.01066  -0.00834 25  PHE   D CE1   
1646 C  CE2   . PHE   B 26  ? 0.24268 0.11573 0.14193 -0.00815 -0.02739 0.01581  25  PHE   D CE2   
1647 C  CZ    . PHE   B 26  ? 0.22999 0.15831 0.14468 -0.02433 0.00397  0.00618  25  PHE   D CZ    
1648 N  N     . ALA   B 27  ? 0.16934 0.09025 0.11979 0.00038  0.02780  0.01400  26  ALA   D N     
1649 C  CA    . ALA   B 27  ? 0.18474 0.10987 0.11937 -0.00711 0.02249  0.01983  26  ALA   D CA    
1650 C  C     . ALA   B 27  ? 0.19142 0.10066 0.12315 0.00570  0.04022  0.00677  26  ALA   D C     
1651 O  O     . ALA   B 27  ? 0.21349 0.10444 0.13374 0.00005  0.03615  0.01039  26  ALA   D O     
1652 C  CB    . ALA   B 27  ? 0.20591 0.16245 0.11964 0.00402  0.00932  0.01367  26  ALA   D CB    
1653 N  N     . ASP   B 28  ? 0.19767 0.09736 0.11810 0.00873  0.02944  0.00839  27  ASP   D N     
1654 C  CA    . ASP   B 28  ? 0.20305 0.12174 0.13533 0.03348  0.03682  0.01969  27  ASP   D CA    
1655 C  C     . ASP   B 28  ? 0.22676 0.12956 0.14329 0.03424  0.02388  0.02793  27  ASP   D C     
1656 O  O     . ASP   B 28  ? 0.32217 0.13276 0.16091 0.00795  0.07205  0.03497  27  ASP   D O     
1657 C  CB    . ASP   B 28  ? 0.22248 0.16306 0.16085 0.04736  0.01984  0.01697  27  ASP   D CB    
1658 C  CG    . ASP   B 28  ? 0.20856 0.22050 0.18860 0.08070  0.00210  0.03718  27  ASP   D CG    
1659 O  OD1   . ASP   B 28  ? 0.21780 0.20837 0.19046 0.04518  0.01074  0.02922  27  ASP   D OD1   
1660 O  OD2   . ASP   B 28  ? 0.24740 0.29727 0.23360 0.09112  0.01572  0.04006  27  ASP   D OD2   
1661 N  N     . LYS   B 29  ? 0.17677 0.12686 0.12566 0.01592  0.01247  0.00543  28  LYS   D N     
1662 C  CA    . LYS   B 29  ? 0.18541 0.15192 0.12772 0.01122  0.00911  -0.00036 28  LYS   D CA    
1663 C  C     . LYS   B 29  ? 0.16364 0.10245 0.10698 0.00953  0.01595  0.00670  28  LYS   D C     
1664 O  O     . LYS   B 29  ? 0.19168 0.10265 0.10699 0.00197  0.01869  0.00878  28  LYS   D O     
1665 C  CB    . LYS   B 29  ? 0.20817 0.22089 0.15655 0.03012  0.00459  -0.00886 28  LYS   D CB    
1666 C  CG    . LYS   B 29  ? 0.22458 0.25524 0.18840 0.04339  -0.01056 0.00407  28  LYS   D CG    
1667 C  CD    . LYS   B 29  ? 0.25032 0.27467 0.20950 0.06364  -0.04178 0.02682  28  LYS   D CD    
1668 C  CE    . LYS   B 29  ? 0.27827 0.27095 0.22871 0.04812  -0.03003 0.01974  28  LYS   D CE    
1669 N  NZ    . LYS   B 29  ? 0.31502 0.26052 0.24052 0.04105  -0.01138 0.01591  28  LYS   D NZ    
1670 N  N     . VAL   B 30  ? 0.14973 0.11515 0.10588 0.00768  -0.00496 0.02214  29  VAL   D N     
1671 C  CA    . VAL   B 30  ? 0.17242 0.09281 0.11011 0.00972  -0.00947 0.00444  29  VAL   D CA    
1672 C  C     . VAL   B 30  ? 0.16211 0.09750 0.10591 0.00944  0.01307  0.01103  29  VAL   D C     
1673 O  O     . VAL   B 30  ? 0.16499 0.09058 0.10798 0.01308  0.00999  0.00990  29  VAL   D O     
1674 C  CB    . VAL   B 30  ? 0.22756 0.13171 0.12194 -0.03433 0.00009  0.00696  29  VAL   D CB    
1675 C  CG1   . VAL   B 30  ? 0.26146 0.18119 0.14962 -0.03444 0.03173  -0.02598 29  VAL   D CG1   
1676 C  CG2   . VAL   B 30  ? 0.25403 0.16063 0.14470 0.00749  -0.01987 -0.00916 29  VAL   D CG2   
1677 N  N     . PRO   B 31  ? 0.17219 0.08239 0.12666 -0.00367 -0.00242 -0.00068 30  PRO   D N     
1678 C  CA    . PRO   B 31  ? 0.17356 0.09086 0.11406 0.00910  -0.01354 0.00023  30  PRO   D CA    
1679 C  C     . PRO   B 31  ? 0.15233 0.09756 0.11164 0.00111  -0.00187 0.00253  30  PRO   D C     
1680 O  O     . PRO   B 31  ? 0.17134 0.09805 0.09043 0.00612  0.00760  0.00411  30  PRO   D O     
1681 C  CB    . PRO   B 31  ? 0.18916 0.09029 0.12872 -0.00503 -0.00608 0.00839  30  PRO   D CB    
1682 C  CG    . PRO   B 31  ? 0.20301 0.10401 0.13067 -0.01346 -0.01101 0.00612  30  PRO   D CG    
1683 C  CD    . PRO   B 31  ? 0.17709 0.09150 0.13101 -0.00977 -0.00640 0.02012  30  PRO   D CD    
1684 N  N     . LYS   B 32  ? 0.14740 0.10403 0.11502 -0.00169 -0.00430 -0.00717 31  LYS   D N     
1685 C  CA    A LYS   B 32  ? 0.17482 0.10197 0.12407 -0.00684 0.01578  0.00132  31  LYS   D CA    
1686 C  CA    B LYS   B 32  ? 0.15211 0.08709 0.10742 0.00112  0.00570  0.00306  31  LYS   D CA    
1687 C  C     . LYS   B 32  ? 0.16037 0.09339 0.09264 0.00471  0.00643  0.00861  31  LYS   D C     
1688 O  O     . LYS   B 32  ? 0.14158 0.09993 0.10000 0.00043  0.00515  -0.00704 31  LYS   D O     
1689 C  CB    A LYS   B 32  ? 0.18873 0.14483 0.16529 -0.02376 0.04486  0.00472  31  LYS   D CB    
1690 C  CB    B LYS   B 32  ? 0.11640 0.10317 0.11863 -0.00145 0.01663  0.00751  31  LYS   D CB    
1691 C  CG    A LYS   B 32  ? 0.22842 0.17700 0.20088 -0.02309 0.07309  0.01371  31  LYS   D CG    
1692 C  CG    B LYS   B 32  ? 0.12688 0.10340 0.11598 -0.01036 0.01627  0.00514  31  LYS   D CG    
1693 C  CD    A LYS   B 32  ? 0.30040 0.21018 0.22833 -0.02288 0.09382  0.02088  31  LYS   D CD    
1694 C  CD    B LYS   B 32  ? 0.14804 0.13200 0.13707 0.00771  0.03678  0.02518  31  LYS   D CD    
1695 C  CE    A LYS   B 32  ? 0.35214 0.22481 0.25146 -0.01544 0.10085  0.03258  31  LYS   D CE    
1696 C  CE    B LYS   B 32  ? 0.16895 0.16065 0.16442 0.02571  0.06599  0.04717  31  LYS   D CE    
1697 N  NZ    A LYS   B 32  ? 0.36050 0.22660 0.25936 -0.00502 0.10896  0.05031  31  LYS   D NZ    
1698 N  NZ    B LYS   B 32  ? 0.20143 0.20257 0.19128 0.04749  0.08309  0.04908  31  LYS   D NZ    
1699 N  N     . THR   B 33  ? 0.14041 0.08805 0.08172 -0.00260 0.01167  -0.00624 32  THR   D N     
1700 C  CA    . THR   B 33  ? 0.14789 0.09506 0.08551 -0.00762 0.01594  -0.00824 32  THR   D CA    
1701 C  C     . THR   B 33  ? 0.13074 0.07786 0.07613 0.00295  0.01375  -0.00872 32  THR   D C     
1702 O  O     . THR   B 33  ? 0.14668 0.09009 0.08366 0.00071  0.01926  0.00119  32  THR   D O     
1703 C  CB    . THR   B 33  ? 0.13696 0.09737 0.09511 0.00138  0.02828  -0.01011 32  THR   D CB    
1704 O  OG1   . THR   B 33  ? 0.14347 0.10554 0.08769 0.00098  0.02505  -0.01273 32  THR   D OG1   
1705 C  CG2   . THR   B 33  ? 0.15515 0.09014 0.10202 -0.00982 0.00792  -0.00435 32  THR   D CG2   
1706 N  N     . ALA   B 34  ? 0.13388 0.09684 0.09288 0.00040  0.00923  -0.01634 33  ALA   D N     
1707 C  CA    . ALA   B 34  ? 0.13770 0.09993 0.08820 0.01300  0.01265  -0.00854 33  ALA   D CA    
1708 C  C     . ALA   B 34  ? 0.13450 0.09792 0.08802 0.01787  0.02706  -0.00023 33  ALA   D C     
1709 O  O     . ALA   B 34  ? 0.16047 0.09508 0.09225 0.01616  0.02387  0.00793  33  ALA   D O     
1710 C  CB    . ALA   B 34  ? 0.16147 0.10328 0.11440 0.03226  0.01523  0.00204  33  ALA   D CB    
1711 N  N     . GLU   B 35  ? 0.13301 0.10150 0.09618 0.00057  0.00224  -0.00679 34  GLU   D N     
1712 C  CA    . GLU   B 35  ? 0.16841 0.08423 0.09927 0.00762  -0.00110 -0.00398 34  GLU   D CA    
1713 C  C     . GLU   B 35  ? 0.14367 0.09303 0.08911 0.00441  0.00836  -0.00944 34  GLU   D C     
1714 O  O     . GLU   B 35  ? 0.14580 0.10241 0.08679 0.00895  0.01520  -0.00453 34  GLU   D O     
1715 C  CB    . GLU   B 35  ? 0.15748 0.09145 0.11543 -0.00636 -0.01165 -0.02033 34  GLU   D CB    
1716 C  CG    . GLU   B 35  ? 0.17948 0.11144 0.12443 -0.01773 0.00254  -0.01692 34  GLU   D CG    
1717 C  CD    . GLU   B 35  ? 0.17829 0.14239 0.12830 -0.01208 -0.01991 -0.01527 34  GLU   D CD    
1718 O  OE1   . GLU   B 35  ? 0.20550 0.13717 0.12925 -0.01056 0.01115  -0.01446 34  GLU   D OE1   
1719 O  OE2   . GLU   B 35  ? 0.22422 0.21879 0.14558 -0.03071 -0.00700 -0.02349 34  GLU   D OE2   
1720 N  N     . ASN   B 36  ? 0.14524 0.08211 0.08766 0.00684  0.01437  -0.00959 35  ASN   D N     
1721 C  CA    . ASN   B 36  ? 0.14361 0.09173 0.09167 0.00341  0.01949  -0.01442 35  ASN   D CA    
1722 C  C     . ASN   B 36  ? 0.13856 0.10085 0.08062 0.01180  0.01013  -0.01813 35  ASN   D C     
1723 O  O     . ASN   B 36  ? 0.15616 0.09915 0.08291 0.00886  0.00430  -0.01135 35  ASN   D O     
1724 C  CB    . ASN   B 36  ? 0.14537 0.10790 0.09322 0.00620  0.01779  -0.01661 35  ASN   D CB    
1725 C  CG    . ASN   B 36  ? 0.13097 0.10503 0.09166 0.01017  0.00005  -0.00944 35  ASN   D CG    
1726 O  OD1   . ASN   B 36  ? 0.14447 0.09628 0.12203 0.01336  0.00136  -0.01362 35  ASN   D OD1   
1727 N  ND2   . ASN   B 36  ? 0.14676 0.10553 0.10080 -0.00198 0.00949  -0.00722 35  ASN   D ND2   
1728 N  N     . PHE   B 37  ? 0.13604 0.09872 0.08762 0.00473  0.01230  -0.01998 36  PHE   D N     
1729 C  CA    . PHE   B 37  ? 0.14470 0.09847 0.08324 -0.00998 0.01140  -0.01776 36  PHE   D CA    
1730 C  C     . PHE   B 37  ? 0.13055 0.09255 0.07621 0.00467  0.01058  -0.01138 36  PHE   D C     
1731 O  O     . PHE   B 37  ? 0.14136 0.09877 0.08022 0.00629  0.01766  -0.00336 36  PHE   D O     
1732 C  CB    . PHE   B 37  ? 0.14145 0.11475 0.08299 -0.01180 0.00593  -0.00935 36  PHE   D CB    
1733 C  CG    . PHE   B 37  ? 0.14545 0.09167 0.07253 0.01309  0.01401  -0.00519 36  PHE   D CG    
1734 C  CD1   . PHE   B 37  ? 0.14647 0.10889 0.08992 0.00575  -0.00434 -0.00022 36  PHE   D CD1   
1735 C  CD2   . PHE   B 37  ? 0.15542 0.12305 0.08649 0.00382  0.01420  0.00168  36  PHE   D CD2   
1736 C  CE1   . PHE   B 37  ? 0.16722 0.11918 0.10086 0.01042  -0.01426 0.01961  36  PHE   D CE1   
1737 C  CE2   . PHE   B 37  ? 0.18357 0.13602 0.10708 0.01087  0.00936  0.02343  36  PHE   D CE2   
1738 C  CZ    . PHE   B 37  ? 0.16739 0.12981 0.11101 0.00443  -0.01439 0.03207  36  PHE   D CZ    
1739 N  N     . ARG   B 38  ? 0.13904 0.09461 0.08788 0.01104  0.00781  -0.02447 37  ARG   D N     
1740 C  CA    . ARG   B 38  ? 0.16799 0.08975 0.08342 0.01149  0.00692  -0.01965 37  ARG   D CA    
1741 C  C     . ARG   B 38  ? 0.16613 0.07843 0.09106 0.01626  0.00929  -0.01667 37  ARG   D C     
1742 O  O     . ARG   B 38  ? 0.17211 0.10542 0.08432 0.00888  0.00774  -0.00983 37  ARG   D O     
1743 C  CB    . ARG   B 38  ? 0.18426 0.09224 0.08718 0.01062  0.02127  -0.02192 37  ARG   D CB    
1744 C  CG    . ARG   B 38  ? 0.18627 0.09199 0.09570 0.00395  0.02005  -0.01554 37  ARG   D CG    
1745 C  CD    . ARG   B 38  ? 0.19832 0.11550 0.10494 0.00222  0.00099  -0.02741 37  ARG   D CD    
1746 N  NE    . ARG   B 38  ? 0.21945 0.12048 0.10995 0.01015  -0.01853 -0.02214 37  ARG   D NE    
1747 C  CZ    . ARG   B 38  ? 0.21955 0.13173 0.11669 -0.00194 -0.02173 -0.01200 37  ARG   D CZ    
1748 N  NH1   . ARG   B 38  ? 0.25490 0.13228 0.12453 -0.00051 -0.00187 -0.00405 37  ARG   D NH1   
1749 N  NH2   . ARG   B 38  ? 0.22387 0.13422 0.14445 0.00332  -0.02058 -0.00905 37  ARG   D NH2   
1750 N  N     . ALA   B 39  ? 0.15118 0.09599 0.09197 0.00724  -0.00913 -0.02123 38  ALA   D N     
1751 C  CA    . ALA   B 39  ? 0.16068 0.10474 0.08890 0.00177  0.00177  -0.01477 38  ALA   D CA    
1752 C  C     . ALA   B 39  ? 0.17249 0.10578 0.08167 0.01406  0.01191  -0.01405 38  ALA   D C     
1753 O  O     . ALA   B 39  ? 0.17179 0.10883 0.08730 0.01656  0.00798  0.00201  38  ALA   D O     
1754 C  CB    . ALA   B 39  ? 0.15096 0.12290 0.10193 -0.01437 0.01378  -0.01806 38  ALA   D CB    
1755 N  N     . LEU   B 40  ? 0.16834 0.09660 0.08514 0.00487  0.00857  -0.00458 39  LEU   D N     
1756 C  CA    . LEU   B 40  ? 0.16585 0.09694 0.07916 0.00036  0.01755  -0.01472 39  LEU   D CA    
1757 C  C     . LEU   B 40  ? 0.17001 0.08054 0.07400 -0.00086 0.01236  -0.00978 39  LEU   D C     
1758 O  O     . LEU   B 40  ? 0.18720 0.10023 0.08870 0.01537  0.01393  -0.00299 39  LEU   D O     
1759 C  CB    . LEU   B 40  ? 0.13988 0.11766 0.08317 -0.00453 0.02709  -0.01814 39  LEU   D CB    
1760 C  CG    . LEU   B 40  ? 0.13717 0.10272 0.09034 0.01368  0.00898  -0.01399 39  LEU   D CG    
1761 C  CD1   . LEU   B 40  ? 0.16094 0.11937 0.09918 -0.00771 0.01343  -0.01383 39  LEU   D CD1   
1762 C  CD2   . LEU   B 40  ? 0.16241 0.13390 0.12180 0.02360  0.00326  0.01517  39  LEU   D CD2   
1763 N  N     . SER   B 41  ? 0.15284 0.10180 0.09247 0.01578  0.01768  -0.01491 40  SER   D N     
1764 C  CA    . SER   B 41  ? 0.16529 0.11242 0.07987 0.00621  0.02100  -0.01170 40  SER   D CA    
1765 C  C     . SER   B 41  ? 0.17580 0.11427 0.08112 0.01148  0.01958  -0.01300 40  SER   D C     
1766 O  O     . SER   B 41  ? 0.22990 0.13253 0.09003 -0.01826 0.03298  -0.01013 40  SER   D O     
1767 C  CB    . SER   B 41  ? 0.18540 0.12563 0.08488 0.01784  0.00258  -0.01791 40  SER   D CB    
1768 O  OG    . SER   B 41  ? 0.17514 0.12628 0.09092 -0.00722 0.01592  -0.00653 40  SER   D OG    
1769 N  N     . THR   B 42  ? 0.20202 0.11271 0.08374 0.00549  0.01807  -0.03329 41  THR   D N     
1770 C  CA    . THR   B 42  ? 0.21138 0.11312 0.09791 0.00642  0.00659  -0.01891 41  THR   D CA    
1771 C  C     . THR   B 42  ? 0.21396 0.12135 0.10061 0.00188  -0.00126 -0.01639 41  THR   D C     
1772 O  O     . THR   B 42  ? 0.23748 0.16404 0.09356 0.02047  0.00305  0.00602  41  THR   D O     
1773 C  CB    . THR   B 42  ? 0.21363 0.14023 0.11427 0.01593  0.01600  -0.01756 41  THR   D CB    
1774 O  OG1   . THR   B 42  ? 0.20683 0.13456 0.10745 0.00104  0.01423  -0.02396 41  THR   D OG1   
1775 C  CG2   . THR   B 42  ? 0.22191 0.13720 0.12368 0.02288  0.01904  -0.01146 41  THR   D CG2   
1776 N  N     . GLY   B 43  ? 0.19962 0.10535 0.11965 0.00273  0.01005  -0.01351 42  GLY   D N     
1777 C  CA    . GLY   B 43  ? 0.19825 0.12359 0.12653 -0.02196 -0.01101 0.00577  42  GLY   D CA    
1778 C  C     . GLY   B 43  ? 0.22621 0.12988 0.12524 -0.01084 -0.01110 0.00709  42  GLY   D C     
1779 O  O     . GLY   B 43  ? 0.21712 0.13982 0.14715 -0.00661 -0.01771 0.02259  42  GLY   D O     
1780 N  N     . GLU   B 44  ? 0.21633 0.14361 0.12728 -0.00609 -0.02463 -0.01018 43  GLU   D N     
1781 C  CA    . GLU   B 44  ? 0.22778 0.12588 0.14355 0.00841  -0.01556 -0.00927 43  GLU   D CA    
1782 C  C     . GLU   B 44  ? 0.23569 0.13284 0.15748 -0.00014 -0.03972 -0.00355 43  GLU   D C     
1783 O  O     . GLU   B 44  ? 0.23864 0.16902 0.18181 -0.03025 -0.05009 -0.01643 43  GLU   D O     
1784 C  CB    . GLU   B 44  ? 0.26550 0.14458 0.13658 0.01571  -0.01505 0.00005  43  GLU   D CB    
1785 C  CG    . GLU   B 44  ? 0.25565 0.14818 0.14663 0.00305  -0.01497 0.01702  43  GLU   D CG    
1786 C  CD    . GLU   B 44  ? 0.22967 0.13116 0.15215 -0.01304 -0.01219 0.00324  43  GLU   D CD    
1787 O  OE1   . GLU   B 44  ? 0.26272 0.14435 0.15990 -0.01624 -0.01515 0.00634  43  GLU   D OE1   
1788 O  OE2   . GLU   B 44  ? 0.26907 0.13934 0.15982 -0.03859 -0.02905 0.00633  43  GLU   D OE2   
1789 N  N     . LYS   B 45  ? 0.18871 0.14091 0.17675 -0.00682 -0.02307 0.00510  44  LYS   D N     
1790 C  CA    . LYS   B 45  ? 0.21097 0.14319 0.19948 -0.01934 -0.01838 0.00374  44  LYS   D CA    
1791 C  C     . LYS   B 45  ? 0.20948 0.14218 0.18989 -0.01174 -0.03712 -0.01842 44  LYS   D C     
1792 O  O     . LYS   B 45  ? 0.22154 0.15549 0.19761 -0.00658 -0.03679 -0.01107 44  LYS   D O     
1793 C  CB    . LYS   B 45  ? 0.24806 0.18930 0.21856 -0.01276 -0.00177 0.01635  44  LYS   D CB    
1794 C  CG    . LYS   B 45  ? 0.33654 0.21306 0.22460 -0.01615 -0.00699 -0.01342 44  LYS   D CG    
1795 C  CD    . LYS   B 45  ? 0.41669 0.23025 0.22987 -0.03261 -0.01223 -0.00810 44  LYS   D CD    
1796 C  CE    . LYS   B 45  ? 0.47369 0.19560 0.21051 -0.04729 -0.02117 -0.02348 44  LYS   D CE    
1797 N  NZ    . LYS   B 45  ? 0.50595 0.19250 0.20389 -0.05881 -0.00424 -0.03383 44  LYS   D NZ    
1798 N  N     . GLY   B 46  ? 0.23764 0.12493 0.16617 -0.01652 -0.05674 -0.01014 45  GLY   D N     
1799 C  CA    . GLY   B 46  ? 0.25749 0.13879 0.16229 -0.00067 -0.05381 -0.00128 45  GLY   D CA    
1800 C  C     . GLY   B 46  ? 0.25401 0.13298 0.15472 0.01773  -0.04099 0.00241  45  GLY   D C     
1801 O  O     . GLY   B 46  ? 0.28838 0.12875 0.16002 0.02355  -0.04917 0.01393  45  GLY   D O     
1802 N  N     . PHE   B 47  ? 0.20788 0.12177 0.13967 0.00885  -0.02481 -0.01348 46  PHE   D N     
1803 C  CA    . PHE   B 47  ? 0.20496 0.11839 0.13574 -0.00036 -0.02176 -0.01892 46  PHE   D CA    
1804 C  C     . PHE   B 47  ? 0.18542 0.11740 0.11097 0.00355  -0.01321 -0.00370 46  PHE   D C     
1805 O  O     . PHE   B 47  ? 0.20910 0.12104 0.11367 0.01092  -0.01204 0.00233  46  PHE   D O     
1806 C  CB    . PHE   B 47  ? 0.18959 0.14754 0.16454 0.00844  -0.02890 -0.01016 46  PHE   D CB    
1807 C  CG    . PHE   B 47  ? 0.18766 0.14747 0.15316 0.02157  -0.01044 -0.01365 46  PHE   D CG    
1808 C  CD1   . PHE   B 47  ? 0.19305 0.14631 0.14746 0.02246  -0.00109 -0.01879 46  PHE   D CD1   
1809 C  CD2   . PHE   B 47  ? 0.20264 0.18309 0.16426 0.00661  -0.00411 0.00242  46  PHE   D CD2   
1810 C  CE1   . PHE   B 47  ? 0.18337 0.18959 0.15885 0.02333  -0.01103 -0.01335 46  PHE   D CE1   
1811 C  CE2   . PHE   B 47  ? 0.21274 0.20169 0.17344 -0.00380 -0.01497 0.01007  46  PHE   D CE2   
1812 C  CZ    . PHE   B 47  ? 0.18616 0.20522 0.17319 -0.00062 -0.01010 0.00257  46  PHE   D CZ    
1813 N  N     . GLY   B 48  ? 0.17603 0.11908 0.11207 0.01497  -0.00406 -0.00705 47  GLY   D N     
1814 C  CA    . GLY   B 48  ? 0.18348 0.12712 0.10341 0.00774  0.00188  0.00918  47  GLY   D CA    
1815 C  C     . GLY   B 48  ? 0.17790 0.10638 0.08135 0.01393  0.00438  -0.00645 47  GLY   D C     
1816 O  O     . GLY   B 48  ? 0.22832 0.09969 0.08245 0.01080  0.00581  -0.00366 47  GLY   D O     
1817 N  N     . TYR   B 49  ? 0.17338 0.10862 0.08152 0.00754  -0.00114 -0.00768 48  TYR   D N     
1818 C  CA    . TYR   B 49  ? 0.16404 0.10908 0.07742 0.00142  0.00350  0.00310  48  TYR   D CA    
1819 C  C     . TYR   B 49  ? 0.17638 0.10002 0.07237 0.00235  0.01032  -0.00131 48  TYR   D C     
1820 O  O     . TYR   B 49  ? 0.21551 0.10539 0.07711 -0.01059 0.00210  -0.00848 48  TYR   D O     
1821 C  CB    . TYR   B 49  ? 0.16243 0.11463 0.07864 0.01633  0.00449  0.00675  48  TYR   D CB    
1822 C  CG    . TYR   B 49  ? 0.15707 0.09277 0.07101 -0.00468 0.00733  -0.00086 48  TYR   D CG    
1823 C  CD1   . TYR   B 49  ? 0.15847 0.09874 0.07534 0.00908  0.01527  -0.00889 48  TYR   D CD1   
1824 C  CD2   . TYR   B 49  ? 0.15746 0.09299 0.06895 -0.00353 0.00027  0.00463  48  TYR   D CD2   
1825 C  CE1   . TYR   B 49  ? 0.15730 0.10740 0.06614 -0.00118 0.01037  -0.00447 48  TYR   D CE1   
1826 C  CE2   . TYR   B 49  ? 0.16267 0.10775 0.05728 0.01449  0.02034  0.00427  48  TYR   D CE2   
1827 C  CZ    . TYR   B 49  ? 0.14831 0.10035 0.06001 -0.00118 0.00926  0.00230  48  TYR   D CZ    
1828 O  OH    . TYR   B 49  ? 0.14361 0.10889 0.06635 0.00781  0.01609  0.00510  48  TYR   D OH    
1829 N  N     . LYS   B 50  ? 0.19214 0.12383 0.06430 0.01502  0.01533  0.00214  49  LYS   D N     
1830 C  CA    . LYS   B 50  ? 0.20977 0.13122 0.05754 -0.00643 0.00716  -0.00137 49  LYS   D CA    
1831 C  C     . LYS   B 50  ? 0.23178 0.12505 0.07369 0.01391  0.00488  -0.00112 49  LYS   D C     
1832 O  O     . LYS   B 50  ? 0.23741 0.13230 0.10012 0.00996  0.00301  0.00826  49  LYS   D O     
1833 C  CB    . LYS   B 50  ? 0.23416 0.15484 0.05966 -0.00893 0.01000  -0.00423 49  LYS   D CB    
1834 C  CG    . LYS   B 50  ? 0.26975 0.17896 0.07637 -0.01163 0.03053  -0.01854 49  LYS   D CG    
1835 C  CD    . LYS   B 50  ? 0.30690 0.19508 0.09224 -0.02811 0.04251  -0.02481 49  LYS   D CD    
1836 C  CE    . LYS   B 50  ? 0.30950 0.24597 0.09674 -0.01741 0.03112  -0.04661 49  LYS   D CE    
1837 N  NZ    . LYS   B 50  ? 0.33330 0.26912 0.09514 -0.00058 0.03142  -0.03533 49  LYS   D NZ    
1838 N  N     . GLY   B 51  ? 0.24158 0.10270 0.08204 -0.00556 -0.00034 0.00593  50  GLY   D N     
1839 C  CA    . GLY   B 51  ? 0.23090 0.12113 0.09622 -0.00778 0.02261  0.00596  50  GLY   D CA    
1840 C  C     . GLY   B 51  ? 0.22403 0.11390 0.09851 -0.00685 0.01119  0.01171  50  GLY   D C     
1841 O  O     . GLY   B 51  ? 0.26192 0.10712 0.10426 0.00126  0.01333  0.00706  50  GLY   D O     
1842 N  N     . SER   B 52  ? 0.19884 0.11639 0.08303 -0.00048 0.00196  0.00946  51  SER   D N     
1843 C  CA    . SER   B 52  ? 0.17182 0.11372 0.08870 -0.01064 0.00953  0.00737  51  SER   D CA    
1844 C  C     . SER   B 52  ? 0.16332 0.11187 0.09293 0.00449  0.01644  0.00131  51  SER   D C     
1845 O  O     . SER   B 52  ? 0.18910 0.11122 0.13138 0.00122  0.04063  0.00253  51  SER   D O     
1846 C  CB    . SER   B 52  ? 0.17612 0.11367 0.09712 -0.00501 0.01739  0.00617  51  SER   D CB    
1847 O  OG    . SER   B 52  ? 0.19894 0.10964 0.08686 -0.00594 0.01213  0.00107  51  SER   D OG    
1848 N  N     . SER   B 53  ? 0.15990 0.11062 0.09997 0.00567  0.00584  0.00457  52  SER   D N     
1849 C  CA    . SER   B 53  ? 0.16296 0.10827 0.11888 -0.01915 -0.00440 0.00020  52  SER   D CA    
1850 C  C     . SER   B 53  ? 0.11991 0.10668 0.10611 0.00087  0.02005  0.00032  52  SER   D C     
1851 O  O     . SER   B 53  ? 0.14565 0.14444 0.10798 -0.03099 0.02290  -0.01051 52  SER   D O     
1852 C  CB    . SER   B 53  ? 0.24396 0.14815 0.17523 -0.01418 -0.00180 -0.01399 52  SER   D CB    
1853 O  OG    . SER   B 53  ? 0.26672 0.17102 0.22293 -0.01444 0.00996  0.01070  52  SER   D OG    
1854 N  N     . PHE   B 54  ? 0.12933 0.10598 0.08319 0.00217  0.01786  0.00530  53  PHE   D N     
1855 C  CA    . PHE   B 54  ? 0.15017 0.11336 0.07862 -0.00436 0.01533  0.00590  53  PHE   D CA    
1856 C  C     . PHE   B 54  ? 0.14390 0.11003 0.09030 -0.00958 0.02145  0.00285  53  PHE   D C     
1857 O  O     . PHE   B 54  ? 0.16967 0.12442 0.10564 -0.01635 0.02456  0.01061  53  PHE   D O     
1858 C  CB    . PHE   B 54  ? 0.14056 0.12897 0.11106 -0.00634 0.02008  0.00918  53  PHE   D CB    
1859 C  CG    . PHE   B 54  ? 0.12867 0.12568 0.10748 -0.01091 0.02276  -0.00449 53  PHE   D CG    
1860 C  CD1   . PHE   B 54  ? 0.13188 0.15878 0.11309 0.00270  0.00507  -0.00580 53  PHE   D CD1   
1861 C  CD2   . PHE   B 54  ? 0.14143 0.11393 0.11641 0.00081  0.02309  0.01343  53  PHE   D CD2   
1862 C  CE1   . PHE   B 54  ? 0.15003 0.17186 0.11228 0.00687  0.02212  -0.01489 53  PHE   D CE1   
1863 C  CE2   . PHE   B 54  ? 0.12913 0.13445 0.14146 0.00904  0.02839  0.00224  53  PHE   D CE2   
1864 C  CZ    . PHE   B 54  ? 0.15315 0.16295 0.12857 0.00701  0.02882  -0.00781 53  PHE   D CZ    
1865 N  N     . HIS   B 55  ? 0.14073 0.11117 0.10403 0.01352  0.02157  0.00277  54  HIS   D N     
1866 C  CA    . HIS   B 55  ? 0.12605 0.10991 0.12022 0.01766  0.00487  -0.01085 54  HIS   D CA    
1867 C  C     . HIS   B 55  ? 0.12543 0.09996 0.11380 0.01534  0.01886  0.00701  54  HIS   D C     
1868 O  O     . HIS   B 55  ? 0.16219 0.08936 0.13847 0.01340  0.00866  -0.00685 54  HIS   D O     
1869 C  CB    . HIS   B 55  ? 0.12912 0.12997 0.13326 0.02073  0.00490  0.00724  54  HIS   D CB    
1870 C  CG    . HIS   B 55  ? 0.12399 0.13124 0.11713 0.02795  -0.00122 -0.00357 54  HIS   D CG    
1871 N  ND1   . HIS   B 55  ? 0.15248 0.13483 0.10772 0.01065  0.00716  0.01123  54  HIS   D ND1   
1872 C  CD2   . HIS   B 55  ? 0.14356 0.17286 0.12184 0.01885  0.00270  0.00802  54  HIS   D CD2   
1873 C  CE1   . HIS   B 55  ? 0.13997 0.17359 0.09222 0.01054  0.01806  0.02671  54  HIS   D CE1   
1874 N  NE2   . HIS   B 55  ? 0.15003 0.18958 0.12206 0.02041  0.01397  0.02481  54  HIS   D NE2   
1875 N  N     . ARG   B 56  ? 0.11419 0.10433 0.09982 0.01027  0.01282  -0.00127 55  ARG   D N     
1876 C  CA    . ARG   B 56  ? 0.11780 0.10711 0.10057 0.00626  0.00640  -0.00400 55  ARG   D CA    
1877 C  C     . ARG   B 56  ? 0.12389 0.09400 0.12035 0.01129  0.00192  -0.00735 55  ARG   D C     
1878 O  O     . ARG   B 56  ? 0.14482 0.09138 0.17165 0.00183  0.00014  -0.01188 55  ARG   D O     
1879 C  CB    . ARG   B 56  ? 0.15170 0.11959 0.10399 0.00819  0.02437  -0.00560 55  ARG   D CB    
1880 C  CG    . ARG   B 56  ? 0.12274 0.13185 0.11825 0.02021  0.01645  -0.00073 55  ARG   D CG    
1881 C  CD    . ARG   B 56  ? 0.14728 0.14033 0.11783 0.00865  0.04919  -0.00220 55  ARG   D CD    
1882 N  NE    . ARG   B 56  ? 0.17525 0.14386 0.12628 0.02175  0.04594  -0.00525 55  ARG   D NE    
1883 C  CZ    . ARG   B 56  ? 0.14389 0.14514 0.12848 0.00008  0.02905  -0.01167 55  ARG   D CZ    
1884 N  NH1   . ARG   B 56  ? 0.16121 0.12716 0.13951 -0.00970 0.04077  -0.01767 55  ARG   D NH1   
1885 N  NH2   . ARG   B 56  ? 0.15732 0.18917 0.15400 0.04610  0.03053  0.00129  55  ARG   D NH2   
1886 N  N     . ILE   B 57  ? 0.11698 0.09240 0.09722 0.00343  0.01014  -0.01128 56  ILE   D N     
1887 C  CA    . ILE   B 57  ? 0.11927 0.11156 0.09303 0.01180  0.01637  -0.00225 56  ILE   D CA    
1888 C  C     . ILE   B 57  ? 0.11559 0.10209 0.10102 -0.00034 0.02723  -0.00624 56  ILE   D C     
1889 O  O     . ILE   B 57  ? 0.14167 0.09441 0.10302 -0.00089 0.02534  -0.00616 56  ILE   D O     
1890 C  CB    . ILE   B 57  ? 0.13469 0.12847 0.09126 0.01352  0.02063  -0.01055 56  ILE   D CB    
1891 C  CG1   . ILE   B 57  ? 0.15350 0.15095 0.08521 0.01359  0.02235  -0.01086 56  ILE   D CG1   
1892 C  CG2   . ILE   B 57  ? 0.12127 0.13594 0.11994 0.01658  0.01561  -0.01283 56  ILE   D CG2   
1893 C  CD1   . ILE   B 57  ? 0.15404 0.18858 0.09932 0.01998  0.03404  -0.03026 56  ILE   D CD1   
1894 N  N     . ILE   B 58  ? 0.12426 0.10667 0.08899 -0.00514 0.01709  0.00088  57  ILE   D N     
1895 C  CA    . ILE   B 58  ? 0.11658 0.10907 0.09370 -0.00195 0.01072  0.00215  57  ILE   D CA    
1896 C  C     . ILE   B 58  ? 0.13050 0.09745 0.11969 -0.00745 0.01805  -0.00833 57  ILE   D C     
1897 O  O     . ILE   B 58  ? 0.13380 0.11533 0.12213 0.01150  0.00950  -0.00513 57  ILE   D O     
1898 C  CB    . ILE   B 58  ? 0.12071 0.14013 0.10239 -0.00383 0.01092  -0.00636 57  ILE   D CB    
1899 C  CG1   . ILE   B 58  ? 0.13445 0.16940 0.12641 -0.00459 0.01767  -0.01212 57  ILE   D CG1   
1900 C  CG2   . ILE   B 58  ? 0.15406 0.14265 0.10934 -0.01026 0.01133  -0.01842 57  ILE   D CG2   
1901 C  CD1   . ILE   B 58  ? 0.14828 0.18632 0.13161 0.00911  0.00310  0.00349  57  ILE   D CD1   
1902 N  N     . PRO   B 59  ? 0.11939 0.11605 0.13479 -0.00446 0.02198  -0.00848 58  PRO   D N     
1903 C  CA    . PRO   B 59  ? 0.11564 0.15840 0.15038 -0.01512 0.01482  0.00921  58  PRO   D CA    
1904 C  C     . PRO   B 59  ? 0.12261 0.15376 0.16318 -0.01814 0.00960  -0.00363 58  PRO   D C     
1905 O  O     . PRO   B 59  ? 0.15004 0.16659 0.16427 -0.01544 -0.00832 0.00260  58  PRO   D O     
1906 C  CB    . PRO   B 59  ? 0.13490 0.16462 0.17001 -0.02459 0.01703  0.00989  58  PRO   D CB    
1907 C  CG    . PRO   B 59  ? 0.16050 0.14764 0.17403 -0.02130 0.04105  0.01681  58  PRO   D CG    
1908 C  CD    . PRO   B 59  ? 0.14407 0.11856 0.15639 -0.01183 0.03564  0.01057  58  PRO   D CD    
1909 N  N     . GLY   B 60  ? 0.12899 0.13490 0.19273 0.00544  0.00298  0.00998  59  GLY   D N     
1910 C  CA    . GLY   B 60  ? 0.17089 0.15277 0.19511 -0.00582 -0.01203 0.02085  59  GLY   D CA    
1911 C  C     . GLY   B 60  ? 0.16848 0.13025 0.16342 -0.00603 -0.00908 0.01312  59  GLY   D C     
1912 O  O     . GLY   B 60  ? 0.17434 0.15070 0.18845 -0.00497 -0.04802 0.01368  59  GLY   D O     
1913 N  N     . PHE   B 61  ? 0.11063 0.12647 0.13317 0.00398  -0.01008 -0.01249 60  PHE   D N     
1914 C  CA    . PHE   B 61  ? 0.13505 0.12878 0.12121 0.00446  -0.00078 -0.01171 60  PHE   D CA    
1915 C  C     . PHE   B 61  ? 0.13221 0.09999 0.11339 0.00500  0.00804  -0.00516 60  PHE   D C     
1916 O  O     . PHE   B 61  ? 0.15100 0.10039 0.13047 0.01251  0.00377  0.00323  60  PHE   D O     
1917 C  CB    . PHE   B 61  ? 0.17170 0.12462 0.10499 0.00870  0.00914  -0.01981 60  PHE   D CB    
1918 C  CG    . PHE   B 61  ? 0.20289 0.12298 0.11138 0.00328  -0.01011 -0.01371 60  PHE   D CG    
1919 C  CD1   . PHE   B 61  ? 0.22228 0.14973 0.13877 -0.00135 -0.03868 -0.02746 60  PHE   D CD1   
1920 C  CD2   . PHE   B 61  ? 0.26419 0.16070 0.11457 0.00928  -0.00850 -0.00603 60  PHE   D CD2   
1921 C  CE1   . PHE   B 61  ? 0.26610 0.17681 0.14887 0.01003  -0.04356 -0.01638 60  PHE   D CE1   
1922 C  CE2   . PHE   B 61  ? 0.35200 0.17895 0.14429 -0.01005 -0.00630 -0.00882 60  PHE   D CE2   
1923 C  CZ    . PHE   B 61  ? 0.32869 0.18179 0.15465 0.00214  -0.02805 -0.01865 60  PHE   D CZ    
1924 N  N     . MET   B 62  ? 0.12762 0.10445 0.10971 0.00342  0.00323  0.00091  61  MET   D N     
1925 C  CA    . MET   B 62  ? 0.13639 0.09659 0.10481 -0.00221 0.00819  -0.00178 61  MET   D CA    
1926 C  C     . MET   B 62  ? 0.11827 0.09165 0.10724 -0.00072 0.02361  0.00126  61  MET   D C     
1927 O  O     . MET   B 62  ? 0.12870 0.09464 0.12261 0.00715  0.01630  0.00608  61  MET   D O     
1928 C  CB    . MET   B 62  ? 0.13514 0.10138 0.11806 -0.01082 0.02876  -0.01448 61  MET   D CB    
1929 C  CG    . MET   B 62  ? 0.13574 0.11967 0.13423 0.02403  0.03847  -0.03431 61  MET   D CG    
1930 S  SD    . MET   B 62  ? 0.14648 0.13916 0.13256 -0.00118 0.03027  -0.02384 61  MET   D SD    
1931 C  CE    . MET   B 62  ? 0.18445 0.14026 0.11590 0.02121  0.01153  0.01568  61  MET   D CE    
1932 N  N     . CYS   B 63  ? 0.12797 0.10690 0.09406 0.00181  0.00538  -0.00343 62  CYS   D N     
1933 C  CA    A CYS   B 63  ? 0.08499 0.09859 0.08918 0.00631  0.00503  0.01271  62  CYS   D CA    
1934 C  CA    B CYS   B 63  ? 0.18594 0.14608 0.12767 -0.00667 0.00705  0.01167  62  CYS   D CA    
1935 C  C     . CYS   B 63  ? 0.11209 0.08993 0.11064 -0.00952 0.01530  0.01688  62  CYS   D C     
1936 O  O     . CYS   B 63  ? 0.12920 0.09011 0.15068 -0.00526 0.00333  0.02512  62  CYS   D O     
1937 C  CB    A CYS   B 63  ? 0.07151 0.10432 0.08542 -0.02861 0.02869  0.00871  62  CYS   D CB    
1938 C  CB    B CYS   B 63  ? 0.30971 0.21872 0.18339 -0.03303 0.01338  0.00639  62  CYS   D CB    
1939 S  SG    A CYS   B 63  ? 0.08265 0.07416 0.09233 0.00285  0.03202  0.00109  62  CYS   D SG    
1940 S  SG    B CYS   B 63  ? 0.39164 0.26797 0.23830 -0.04128 0.01348  0.01112  62  CYS   D SG    
1941 N  N     . GLN   B 64  ? 0.11322 0.09601 0.08439 -0.00289 0.01394  0.00059  63  GLN   D N     
1942 C  CA    . GLN   B 64  ? 0.12698 0.10037 0.08005 0.00228  0.00894  -0.00186 63  GLN   D CA    
1943 C  C     . GLN   B 64  ? 0.13070 0.09784 0.06975 0.00179  0.02048  0.00175  63  GLN   D C     
1944 O  O     . GLN   B 64  ? 0.14669 0.10258 0.08715 0.01086  0.01927  0.01160  63  GLN   D O     
1945 C  CB    . GLN   B 64  ? 0.12384 0.10092 0.08891 0.00732  0.01770  -0.00191 63  GLN   D CB    
1946 C  CG    . GLN   B 64  ? 0.13008 0.11112 0.08174 0.01391  0.02234  -0.01858 63  GLN   D CG    
1947 C  CD    . GLN   B 64  ? 0.13386 0.11831 0.08131 0.00627  0.00848  -0.01938 63  GLN   D CD    
1948 O  OE1   . GLN   B 64  ? 0.14408 0.18054 0.08457 -0.00353 0.01965  -0.02535 63  GLN   D OE1   
1949 N  NE2   . GLN   B 64  ? 0.12740 0.10283 0.10450 0.01012  0.01303  -0.01170 63  GLN   D NE2   
1950 N  N     . GLY   B 65  ? 0.12158 0.10811 0.07960 0.00609  0.00951  -0.01040 64  GLY   D N     
1951 C  CA    . GLY   B 65  ? 0.13502 0.11551 0.08689 -0.00563 0.00838  0.00362  64  GLY   D CA    
1952 C  C     . GLY   B 65  ? 0.12452 0.11148 0.07738 0.01639  0.00883  0.01254  64  GLY   D C     
1953 O  O     . GLY   B 65  ? 0.13137 0.10769 0.09287 0.00574  0.00004  -0.00423 64  GLY   D O     
1954 N  N     . GLY   B 66  ? 0.13373 0.13370 0.08090 0.01207  -0.00303 -0.00589 65  GLY   D N     
1955 C  CA    . GLY   B 66  ? 0.12406 0.14371 0.10456 0.00706  -0.02333 -0.02044 65  GLY   D CA    
1956 C  C     . GLY   B 66  ? 0.15264 0.13299 0.10490 0.00197  -0.00376 -0.02258 65  GLY   D C     
1957 O  O     . GLY   B 66  ? 0.14300 0.14222 0.12865 -0.02153 -0.00679 -0.00397 65  GLY   D O     
1958 N  N     . ASP   B 67  ? 0.13393 0.13090 0.10576 0.02539  -0.00112 -0.02109 66  ASP   D N     
1959 C  CA    . ASP   B 67  ? 0.14199 0.12842 0.11357 0.01044  0.00234  -0.02064 66  ASP   D CA    
1960 C  C     . ASP   B 67  ? 0.13179 0.12177 0.12627 0.01259  0.00663  0.00304  66  ASP   D C     
1961 O  O     . ASP   B 67  ? 0.17445 0.13454 0.13740 -0.00632 -0.00674 0.00172  66  ASP   D O     
1962 C  CB    . ASP   B 67  ? 0.16343 0.15084 0.13035 0.03157  0.00976  -0.03746 66  ASP   D CB    
1963 C  CG    . ASP   B 67  ? 0.18036 0.14688 0.13432 0.02555  -0.01944 -0.03676 66  ASP   D CG    
1964 O  OD1   . ASP   B 67  ? 0.17537 0.17220 0.14835 0.01689  -0.00690 -0.04812 66  ASP   D OD1   
1965 O  OD2   . ASP   B 67  ? 0.18721 0.14471 0.13191 0.02061  -0.00144 -0.04173 66  ASP   D OD2   
1966 N  N     . PHE   B 68  ? 0.16618 0.13595 0.10928 -0.00497 -0.01000 -0.01451 67  PHE   D N     
1967 C  CA    . PHE   B 68  ? 0.19518 0.13609 0.10129 0.00587  -0.00302 -0.00760 67  PHE   D CA    
1968 C  C     . PHE   B 68  ? 0.22575 0.13200 0.09792 0.01683  -0.01706 -0.00453 67  PHE   D C     
1969 O  O     . PHE   B 68  ? 0.27582 0.14906 0.11436 0.07026  -0.01481 -0.00155 67  PHE   D O     
1970 C  CB    . PHE   B 68  ? 0.19695 0.13137 0.09771 0.01279  0.01484  -0.00881 67  PHE   D CB    
1971 C  CG    . PHE   B 68  ? 0.18101 0.12944 0.09379 0.02440  0.00031  -0.01666 67  PHE   D CG    
1972 C  CD1   . PHE   B 68  ? 0.17956 0.13075 0.11637 0.02140  -0.01052 -0.02446 67  PHE   D CD1   
1973 C  CD2   . PHE   B 68  ? 0.20215 0.12632 0.09821 0.01416  -0.02297 -0.01154 67  PHE   D CD2   
1974 C  CE1   . PHE   B 68  ? 0.21088 0.13986 0.13591 0.01295  0.00052  -0.02868 67  PHE   D CE1   
1975 C  CE2   . PHE   B 68  ? 0.23539 0.14678 0.10227 0.00575  -0.01629 -0.01209 67  PHE   D CE2   
1976 C  CZ    . PHE   B 68  ? 0.24836 0.16347 0.12385 0.01751  0.00606  -0.03360 67  PHE   D CZ    
1977 N  N     . THR   B 69  ? 0.18499 0.12891 0.11832 0.02800  -0.01506 -0.00606 68  THR   D N     
1978 C  CA    . THR   B 69  ? 0.19353 0.14719 0.14284 0.02623  -0.02296 -0.00975 68  THR   D CA    
1979 C  C     . THR   B 69  ? 0.25478 0.13741 0.15067 0.02348  -0.02220 0.00146  68  THR   D C     
1980 O  O     . THR   B 69  ? 0.25126 0.14898 0.17201 0.06635  -0.03645 -0.00696 68  THR   D O     
1981 C  CB    . THR   B 69  ? 0.21286 0.15169 0.15682 0.01353  -0.02518 -0.02341 68  THR   D CB    
1982 O  OG1   . THR   B 69  ? 0.20984 0.14605 0.15731 0.02653  -0.02782 -0.01736 68  THR   D OG1   
1983 C  CG2   . THR   B 69  ? 0.23809 0.15567 0.18356 0.01553  -0.00056 -0.03778 68  THR   D CG2   
1984 N  N     A ARG   B 70  ? 0.30617 0.13642 0.15717 0.01303  -0.02832 -0.00436 69  ARG   D N     
1985 N  N     B ARG   B 70  ? 0.30827 0.14601 0.14949 0.00654  -0.00784 -0.00922 69  ARG   D N     
1986 C  CA    A ARG   B 70  ? 0.38490 0.13814 0.17128 0.00280  -0.02845 0.00259  69  ARG   D CA    
1987 C  CA    B ARG   B 70  ? 0.38942 0.15862 0.15728 -0.00986 0.00821  -0.00752 69  ARG   D CA    
1988 C  C     A ARG   B 70  ? 0.44139 0.17832 0.16828 -0.05433 -0.03574 0.00996  69  ARG   D C     
1989 C  C     B ARG   B 70  ? 0.44420 0.18697 0.16043 -0.06017 -0.01268 0.00741  69  ARG   D C     
1990 O  O     A ARG   B 70  ? 0.43473 0.21522 0.16684 -0.08744 -0.04471 0.00506  69  ARG   D O     
1991 O  O     B ARG   B 70  ? 0.43876 0.22108 0.15869 -0.09409 -0.01189 0.00836  69  ARG   D O     
1992 C  CB    A ARG   B 70  ? 0.41453 0.12888 0.19864 0.03058  -0.03236 0.00453  69  ARG   D CB    
1993 C  CB    B ARG   B 70  ? 0.42350 0.16983 0.17550 0.00797  0.02977  -0.01550 69  ARG   D CB    
1994 C  CG    A ARG   B 70  ? 0.44523 0.16718 0.24525 0.02945  -0.03002 0.00884  69  ARG   D CG    
1995 C  CG    B ARG   B 70  ? 0.45619 0.21911 0.21128 0.00528  0.04360  -0.01250 69  ARG   D CG    
1996 C  CD    A ARG   B 70  ? 0.49217 0.22224 0.28918 0.00418  -0.02742 0.00153  69  ARG   D CD    
1997 C  CD    B ARG   B 70  ? 0.51518 0.28277 0.24673 -0.02520 0.04552  -0.01857 69  ARG   D CD    
1998 N  NE    A ARG   B 70  ? 0.50228 0.24721 0.30863 0.00384  -0.04763 -0.00574 69  ARG   D NE    
1999 N  NE    B ARG   B 70  ? 0.54110 0.32765 0.26509 -0.05035 0.04537  -0.03032 69  ARG   D NE    
2000 C  CZ    A ARG   B 70  ? 0.49507 0.26061 0.31758 0.00832  -0.06803 -0.00040 69  ARG   D CZ    
2001 C  CZ    B ARG   B 70  ? 0.54227 0.35254 0.28516 -0.07552 0.04320  -0.03748 69  ARG   D CZ    
2002 N  NH1   A ARG   B 70  ? 0.48555 0.27337 0.31547 0.02900  -0.07398 0.01207  69  ARG   D NH1   
2003 N  NH1   B ARG   B 70  ? 0.53419 0.35664 0.28937 -0.08745 0.03808  -0.03456 69  ARG   D NH1   
2004 N  NH2   A ARG   B 70  ? 0.51552 0.26418 0.32582 -0.00642 -0.06450 -0.00082 69  ARG   D NH2   
2005 N  NH2   B ARG   B 70  ? 0.56962 0.37133 0.29336 -0.08450 0.04038  -0.04386 69  ARG   D NH2   
2006 N  N     . HIS   B 71  ? 0.49287 0.18778 0.17239 -0.09691 -0.02667 0.02244  70  HIS   D N     
2007 C  CA    . HIS   B 71  ? 0.53122 0.22056 0.19777 -0.13696 -0.05336 0.04461  70  HIS   D CA    
2008 C  C     . HIS   B 71  ? 0.54485 0.23584 0.20921 -0.15137 -0.04923 0.04181  70  HIS   D C     
2009 O  O     . HIS   B 71  ? 0.57168 0.26943 0.25095 -0.16818 -0.02702 0.02700  70  HIS   D O     
2010 C  CB    . HIS   B 71  ? 0.56337 0.23049 0.22192 -0.10251 -0.08294 0.07133  70  HIS   D CB    
2011 C  CG    . HIS   B 71  ? 0.57434 0.22044 0.23774 -0.09211 -0.14957 0.05937  70  HIS   D CG    
2012 N  ND1   . HIS   B 71  ? 0.59368 0.21996 0.24823 -0.08211 -0.16320 0.05480  70  HIS   D ND1   
2013 C  CD2   . HIS   B 71  ? 0.59386 0.22467 0.25858 -0.04323 -0.17349 0.04890  70  HIS   D CD2   
2014 C  CE1   . HIS   B 71  ? 0.61547 0.22969 0.27307 -0.06595 -0.19063 0.05047  70  HIS   D CE1   
2015 N  NE2   . HIS   B 71  ? 0.64619 0.24368 0.27689 -0.02984 -0.17367 0.05573  70  HIS   D NE2   
2016 N  N     . ASN   B 72  ? 0.51140 0.19271 0.17564 -0.10665 -0.07625 0.04225  71  ASN   D N     
2017 C  CA    . ASN   B 72  ? 0.47028 0.17258 0.17514 -0.06808 -0.07852 0.03560  71  ASN   D CA    
2018 C  C     . ASN   B 72  ? 0.39190 0.16034 0.16780 -0.06570 -0.04722 0.03390  71  ASN   D C     
2019 O  O     . ASN   B 72  ? 0.41802 0.14541 0.17803 -0.04658 -0.08095 0.00984  71  ASN   D O     
2020 C  CB    . ASN   B 72  ? 0.49491 0.16824 0.18809 -0.00020 -0.10736 0.02949  71  ASN   D CB    
2021 C  CG    . ASN   B 72  ? 0.47584 0.18823 0.19672 0.04905  -0.11998 -0.03037 71  ASN   D CG    
2022 O  OD1   . ASN   B 72  ? 0.46872 0.16120 0.20160 0.06122  -0.10246 -0.04749 71  ASN   D OD1   
2023 N  ND2   . ASN   B 72  ? 0.48275 0.20705 0.20873 0.07821  -0.13675 -0.05166 71  ASN   D ND2   
2024 N  N     . GLY   B 73  ? 0.27428 0.16641 0.15311 -0.05947 -0.02343 0.02206  72  GLY   D N     
2025 C  CA    . GLY   B 73  ? 0.19811 0.16849 0.15650 -0.03332 0.00133  0.02637  72  GLY   D CA    
2026 C  C     . GLY   B 73  ? 0.15546 0.11238 0.12719 0.00248  0.01021  -0.00816 72  GLY   D C     
2027 O  O     . GLY   B 73  ? 0.15450 0.11777 0.12956 0.02155  0.00780  -0.00304 72  GLY   D O     
2028 N  N     . THR   B 74  ? 0.15389 0.09762 0.12702 0.00363  -0.00382 -0.01018 73  THR   D N     
2029 C  CA    . THR   B 74  ? 0.15436 0.13583 0.13976 0.02594  0.01449  -0.02384 73  THR   D CA    
2030 C  C     . THR   B 74  ? 0.14212 0.13079 0.14648 0.00281  -0.01576 0.00091  73  THR   D C     
2031 O  O     . THR   B 74  ? 0.18494 0.19380 0.18721 -0.03517 0.00222  0.01865  73  THR   D O     
2032 C  CB    . THR   B 74  ? 0.20205 0.18116 0.16261 0.07755  -0.01971 -0.06144 73  THR   D CB    
2033 O  OG1   . THR   B 74  ? 0.23462 0.21349 0.21152 0.09878  -0.03727 -0.06981 73  THR   D OG1   
2034 C  CG2   . THR   B 74  ? 0.23888 0.17952 0.16939 0.07762  -0.01694 -0.07313 73  THR   D CG2   
2035 N  N     . GLY   B 75  ? 0.16620 0.11898 0.14567 0.02343  -0.02462 -0.01673 74  GLY   D N     
2036 C  CA    . GLY   B 75  ? 0.16936 0.09753 0.16727 0.01152  -0.02783 -0.02946 74  GLY   D CA    
2037 C  C     . GLY   B 75  ? 0.15027 0.11880 0.19419 0.01761  -0.04577 -0.01367 74  GLY   D C     
2038 O  O     . GLY   B 75  ? 0.16371 0.09901 0.20024 0.01937  -0.03368 -0.00818 74  GLY   D O     
2039 N  N     . GLY   B 76  ? 0.17993 0.11257 0.19426 0.01965  -0.02912 -0.03182 75  GLY   D N     
2040 C  CA    . GLY   B 76  ? 0.17358 0.09937 0.19668 0.01108  -0.03283 -0.03136 75  GLY   D CA    
2041 C  C     . GLY   B 76  ? 0.17398 0.09904 0.18110 0.01693  -0.02862 -0.03104 75  GLY   D C     
2042 O  O     . GLY   B 76  ? 0.24642 0.11742 0.20949 0.02183  0.01707  -0.04446 75  GLY   D O     
2043 N  N     . LYS   B 77  ? 0.15373 0.09426 0.16789 0.00686  -0.01937 -0.01287 76  LYS   D N     
2044 C  CA    . LYS   B 77  ? 0.14359 0.11241 0.16882 0.01899  0.00414  -0.01665 76  LYS   D CA    
2045 C  C     . LYS   B 77  ? 0.11823 0.11481 0.14699 0.01159  0.00813  -0.01560 76  LYS   D C     
2046 O  O     . LYS   B 77  ? 0.13108 0.10938 0.14986 0.00808  0.00820  -0.00265 76  LYS   D O     
2047 C  CB    . LYS   B 77  ? 0.17986 0.15009 0.16520 0.03936  -0.01094 -0.00813 76  LYS   D CB    
2048 C  CG    . LYS   B 77  ? 0.18491 0.19046 0.15143 0.05400  -0.01206 -0.00080 76  LYS   D CG    
2049 C  CD    . LYS   B 77  ? 0.21656 0.23670 0.15710 0.06517  -0.03626 -0.02675 76  LYS   D CD    
2050 C  CE    . LYS   B 77  ? 0.22193 0.29627 0.16965 0.08991  -0.04324 -0.01506 76  LYS   D CE    
2051 N  NZ    . LYS   B 77  ? 0.22748 0.33892 0.19358 0.07709  -0.06454 -0.01196 76  LYS   D NZ    
2052 N  N     . SER   B 78  ? 0.13243 0.10916 0.12890 0.00764  0.02162  -0.02055 77  SER   D N     
2053 C  CA    . SER   B 78  ? 0.13477 0.09554 0.12838 0.00441  0.00315  -0.01130 77  SER   D CA    
2054 C  C     . SER   B 78  ? 0.14016 0.09871 0.13601 0.01191  0.00270  -0.00960 77  SER   D C     
2055 O  O     . SER   B 78  ? 0.15658 0.13159 0.15944 0.02943  -0.01621 -0.03279 77  SER   D O     
2056 C  CB    . SER   B 78  ? 0.15808 0.11979 0.12089 -0.01811 0.02531  -0.01247 77  SER   D CB    
2057 O  OG    . SER   B 78  ? 0.18410 0.14856 0.13767 -0.04290 0.04685  -0.02519 77  SER   D OG    
2058 N  N     . ILE   B 79  ? 0.15879 0.09436 0.10795 0.00853  -0.00058 -0.01534 78  ILE   D N     
2059 C  CA    . ILE   B 79  ? 0.16290 0.10663 0.12350 0.01070  0.00675  -0.03498 78  ILE   D CA    
2060 C  C     . ILE   B 79  ? 0.15747 0.12066 0.14994 0.00752  0.02023  -0.03354 78  ILE   D C     
2061 O  O     . ILE   B 79  ? 0.15702 0.15376 0.17011 -0.00028 -0.01042 -0.04624 78  ILE   D O     
2062 C  CB    . ILE   B 79  ? 0.16943 0.10905 0.12438 0.01303  -0.00310 -0.02207 78  ILE   D CB    
2063 C  CG1   . ILE   B 79  ? 0.17122 0.10800 0.12697 0.00811  0.00544  -0.01570 78  ILE   D CG1   
2064 C  CG2   . ILE   B 79  ? 0.17261 0.14073 0.12375 0.00802  0.01970  -0.01686 78  ILE   D CG2   
2065 C  CD1   . ILE   B 79  ? 0.18500 0.10784 0.15072 0.00436  0.00717  -0.03679 78  ILE   D CD1   
2066 N  N     . TYR   B 80  ? 0.16147 0.10677 0.17318 0.00973  0.03615  -0.00532 79  TYR   D N     
2067 C  CA    . TYR   B 80  ? 0.15265 0.14178 0.19361 0.02345  0.04585  0.01128  79  TYR   D CA    
2068 C  C     . TYR   B 80  ? 0.22828 0.18197 0.26029 0.04223  0.08421  0.03403  79  TYR   D C     
2069 O  O     . TYR   B 80  ? 0.23346 0.22272 0.31354 0.04442  0.08082  0.04646  79  TYR   D O     
2070 C  CB    . TYR   B 80  ? 0.15635 0.13270 0.17418 0.00664  0.03478  -0.01091 79  TYR   D CB    
2071 C  CG    . TYR   B 80  ? 0.14349 0.12710 0.15266 0.00541  0.00888  -0.01554 79  TYR   D CG    
2072 C  CD1   . TYR   B 80  ? 0.15371 0.12292 0.15984 0.00795  0.01038  -0.02373 79  TYR   D CD1   
2073 C  CD2   . TYR   B 80  ? 0.14151 0.12586 0.12037 -0.00315 0.00655  -0.00538 79  TYR   D CD2   
2074 C  CE1   . TYR   B 80  ? 0.15395 0.13023 0.14951 -0.00024 -0.00365 -0.01150 79  TYR   D CE1   
2075 C  CE2   . TYR   B 80  ? 0.15312 0.12199 0.11856 -0.00387 0.01389  -0.00222 79  TYR   D CE2   
2076 C  CZ    . TYR   B 80  ? 0.15204 0.12037 0.13651 0.00817  0.00584  -0.01757 79  TYR   D CZ    
2077 O  OH    . TYR   B 80  ? 0.16069 0.12460 0.13247 0.00556  -0.00656 -0.01726 79  TYR   D OH    
2078 N  N     . GLY   B 81  ? 0.19652 0.19948 0.26484 0.05655  0.00413  -0.00452 80  GLY   D N     
2079 C  CA    . GLY   B 81  ? 0.22226 0.23419 0.28710 0.07001  -0.00122 -0.03624 80  GLY   D CA    
2080 C  C     . GLY   B 81  ? 0.17914 0.25082 0.31675 0.08338  -0.03004 -0.04186 80  GLY   D C     
2081 O  O     . GLY   B 81  ? 0.24445 0.28346 0.30630 0.06533  -0.05395 -0.08663 80  GLY   D O     
2082 N  N     . GLU   B 82  ? 0.18509 0.24068 0.32537 0.02618  -0.07745 -0.03771 81  GLU   D N     
2083 C  CA    . GLU   B 82  ? 0.22329 0.28142 0.33619 0.01721  -0.02962 -0.02493 81  GLU   D CA    
2084 C  C     . GLU   B 82  ? 0.16893 0.24337 0.29039 0.02421  -0.02646 -0.03398 81  GLU   D C     
2085 O  O     . GLU   B 82  ? 0.17956 0.22023 0.32169 0.03107  -0.00010 -0.01237 81  GLU   D O     
2086 C  CB    . GLU   B 82  ? 0.37511 0.36956 0.40509 0.00591  0.02752  0.01000  81  GLU   D CB    
2087 C  CG    . GLU   B 82  ? 0.51225 0.44545 0.46554 -0.00906 0.07862  0.04255  81  GLU   D CG    
2088 C  CD    . GLU   B 82  ? 0.63095 0.50331 0.52113 -0.01698 0.10876  0.06219  81  GLU   D CD    
2089 O  OE1   . GLU   B 82  ? 0.66855 0.53262 0.54648 -0.02014 0.12134  0.06728  81  GLU   D OE1   
2090 O  OE2   . GLU   B 82  ? 0.66922 0.51243 0.53608 -0.02683 0.11948  0.07068  81  GLU   D OE2   
2091 N  N     . LYS   B 83  ? 0.20306 0.23648 0.24852 0.09898  -0.03780 -0.04761 82  LYS   D N     
2092 C  CA    . LYS   B 83  ? 0.15995 0.21502 0.23331 0.02442  -0.04817 -0.02494 82  LYS   D CA    
2093 C  C     . LYS   B 83  ? 0.15705 0.19333 0.25487 0.01060  -0.00520 -0.00577 82  LYS   D C     
2094 O  O     . LYS   B 83  ? 0.18073 0.22966 0.34005 -0.01004 -0.01717 0.01508  82  LYS   D O     
2095 C  CB    . LYS   B 83  ? 0.20017 0.24357 0.25995 -0.00297 -0.07855 0.00098  82  LYS   D CB    
2096 C  CG    . LYS   B 83  ? 0.27177 0.30600 0.31324 -0.02121 -0.04138 0.03785  82  LYS   D CG    
2097 C  CD    . LYS   B 83  ? 0.35443 0.37881 0.35461 -0.03222 -0.00798 0.05354  82  LYS   D CD    
2098 C  CE    . LYS   B 83  ? 0.40423 0.42983 0.38352 -0.09016 0.00498  0.05272  82  LYS   D CE    
2099 N  NZ    . LYS   B 83  ? 0.44073 0.46310 0.40358 -0.09138 0.01401  0.06639  82  LYS   D NZ    
2100 N  N     . PHE   B 84  ? 0.14362 0.15190 0.17676 0.02445  0.00247  -0.00114 83  PHE   D N     
2101 C  CA    . PHE   B 84  ? 0.13653 0.15441 0.15558 -0.00428 0.00046  -0.01368 83  PHE   D CA    
2102 C  C     . PHE   B 84  ? 0.12503 0.13724 0.13801 -0.00835 0.01157  -0.01236 83  PHE   D C     
2103 O  O     . PHE   B 84  ? 0.12367 0.14849 0.14093 -0.01504 0.01643  -0.01632 83  PHE   D O     
2104 C  CB    . PHE   B 84  ? 0.13685 0.14783 0.14168 -0.01506 0.01133  -0.02609 83  PHE   D CB    
2105 C  CG    . PHE   B 84  ? 0.14122 0.12836 0.12957 -0.00422 0.00249  -0.00829 83  PHE   D CG    
2106 C  CD1   . PHE   B 84  ? 0.15945 0.13811 0.10916 -0.01148 0.00339  -0.00706 83  PHE   D CD1   
2107 C  CD2   . PHE   B 84  ? 0.15987 0.13061 0.12898 0.00642  0.02123  -0.01909 83  PHE   D CD2   
2108 C  CE1   . PHE   B 84  ? 0.16873 0.11184 0.11703 -0.00424 0.00530  -0.01603 83  PHE   D CE1   
2109 C  CE2   . PHE   B 84  ? 0.16827 0.13467 0.11823 0.02089  -0.00416 -0.02098 83  PHE   D CE2   
2110 C  CZ    . PHE   B 84  ? 0.18428 0.12562 0.11150 0.00251  0.01329  -0.02399 83  PHE   D CZ    
2111 N  N     A GLU   B 85  ? 0.14015 0.13059 0.13588 -0.01889 0.00592  -0.00187 84  GLU   D N     
2112 N  N     B GLU   B 85  ? 0.15980 0.14066 0.13893 -0.01595 0.01313  0.00523  84  GLU   D N     
2113 C  CA    A GLU   B 85  ? 0.13512 0.13982 0.14208 -0.02669 0.01866  -0.00548 84  GLU   D CA    
2114 C  CA    B GLU   B 85  ? 0.17419 0.16072 0.14952 -0.02261 0.02570  0.00657  84  GLU   D CA    
2115 C  C     A GLU   B 85  ? 0.14113 0.12124 0.12100 -0.01184 0.01581  -0.00748 84  GLU   D C     
2116 C  C     B GLU   B 85  ? 0.16115 0.13812 0.12369 -0.01614 0.01534  0.00086  84  GLU   D C     
2117 O  O     A GLU   B 85  ? 0.14696 0.12973 0.13126 0.00878  0.00956  -0.01193 84  GLU   D O     
2118 O  O     B GLU   B 85  ? 0.17550 0.16239 0.12688 -0.00237 -0.00085 -0.00077 84  GLU   D O     
2119 C  CB    A GLU   B 85  ? 0.15359 0.15983 0.17867 -0.04866 0.00887  -0.00726 84  GLU   D CB    
2120 C  CB    B GLU   B 85  ? 0.22838 0.19906 0.19575 -0.03092 0.03022  0.01334  84  GLU   D CB    
2121 C  CG    A GLU   B 85  ? 0.21122 0.17831 0.20791 -0.05992 0.01896  -0.02000 84  GLU   D CG    
2122 C  CG    B GLU   B 85  ? 0.30808 0.24529 0.23829 -0.04110 0.04970  0.01382  84  GLU   D CG    
2123 C  CD    A GLU   B 85  ? 0.27739 0.17764 0.23264 -0.07572 0.04371  -0.04913 84  GLU   D CD    
2124 C  CD    B GLU   B 85  ? 0.37925 0.28136 0.27839 -0.04126 0.06572  0.01302  84  GLU   D CD    
2125 O  OE1   A GLU   B 85  ? 0.32022 0.17769 0.24144 -0.12058 0.06833  -0.05441 84  GLU   D OE1   
2126 O  OE1   B GLU   B 85  ? 0.41604 0.28710 0.29241 -0.04398 0.07054  0.01435  84  GLU   D OE1   
2127 O  OE2   A GLU   B 85  ? 0.27383 0.19713 0.23947 -0.07006 0.03172  -0.04675 84  GLU   D OE2   
2128 O  OE2   B GLU   B 85  ? 0.41721 0.30264 0.29721 -0.04612 0.06419  0.02130  84  GLU   D OE2   
2129 N  N     . ASP   B 86  ? 0.14131 0.11609 0.11455 -0.00140 0.00893  0.00017  85  ASP   D N     
2130 C  CA    . ASP   B 86  ? 0.15285 0.12009 0.11418 0.00013  0.01646  0.00020  85  ASP   D CA    
2131 C  C     . ASP   B 86  ? 0.14707 0.11516 0.11045 -0.01249 0.02879  0.00677  85  ASP   D C     
2132 O  O     . ASP   B 86  ? 0.20732 0.12895 0.10810 -0.00915 0.04140  0.00193  85  ASP   D O     
2133 C  CB    . ASP   B 86  ? 0.16171 0.11663 0.09909 -0.00825 0.02717  0.00535  85  ASP   D CB    
2134 C  CG    . ASP   B 86  ? 0.16107 0.12170 0.09521 0.00454  0.03565  0.00920  85  ASP   D CG    
2135 O  OD1   . ASP   B 86  ? 0.13873 0.12347 0.10160 0.00156  0.02021  0.00155  85  ASP   D OD1   
2136 O  OD2   . ASP   B 86  ? 0.14883 0.14233 0.12017 -0.01157 0.03811  0.00316  85  ASP   D OD2   
2137 N  N     . GLU   B 87  ? 0.13226 0.10892 0.11707 -0.01708 0.01979  0.00462  86  GLU   D N     
2138 C  CA    . GLU   B 87  ? 0.15565 0.10194 0.10349 -0.00031 0.01074  0.00204  86  GLU   D CA    
2139 C  C     . GLU   B 87  ? 0.16073 0.10749 0.10594 -0.01450 0.01623  0.00560  86  GLU   D C     
2140 O  O     . GLU   B 87  ? 0.15690 0.13398 0.11980 -0.01283 0.02356  0.01184  86  GLU   D O     
2141 C  CB    . GLU   B 87  ? 0.15844 0.10583 0.09226 -0.00254 0.01387  0.00314  86  GLU   D CB    
2142 C  CG    . GLU   B 87  ? 0.18308 0.11313 0.09646 -0.00949 0.01794  0.00032  86  GLU   D CG    
2143 C  CD    . GLU   B 87  ? 0.18476 0.10410 0.09974 0.00616  0.00863  0.00187  86  GLU   D CD    
2144 O  OE1   . GLU   B 87  ? 0.18750 0.10435 0.08492 -0.01109 0.00856  0.00520  86  GLU   D OE1   
2145 O  OE2   . GLU   B 87  ? 0.21371 0.09819 0.10821 -0.01109 0.02583  -0.00567 86  GLU   D OE2   
2146 N  N     . ASN   B 88  ? 0.15226 0.11122 0.09292 -0.01224 0.01079  0.00732  87  ASN   D N     
2147 C  CA    . ASN   B 88  ? 0.16330 0.10563 0.10417 -0.01583 0.01179  -0.00431 87  ASN   D CA    
2148 C  C     . ASN   B 88  ? 0.15630 0.10359 0.09273 -0.00785 0.02069  -0.00106 87  ASN   D C     
2149 O  O     . ASN   B 88  ? 0.15917 0.10736 0.10398 -0.01573 0.01623  0.00294  87  ASN   D O     
2150 C  CB    . ASN   B 88  ? 0.16141 0.09326 0.11685 0.00466  0.02192  -0.00684 87  ASN   D CB    
2151 C  CG    . ASN   B 88  ? 0.16059 0.10497 0.11266 -0.00630 0.01294  -0.00617 87  ASN   D CG    
2152 O  OD1   . ASN   B 88  ? 0.15720 0.10515 0.10602 -0.00481 0.01028  -0.00042 87  ASN   D OD1   
2153 N  ND2   . ASN   B 88  ? 0.18055 0.10704 0.11571 0.00958  0.00578  -0.01261 87  ASN   D ND2   
2154 N  N     . PHE   B 89  ? 0.16697 0.10525 0.09010 -0.01373 0.00917  -0.00557 88  PHE   D N     
2155 C  CA    . PHE   B 89  ? 0.16275 0.10087 0.08083 -0.00674 0.00678  0.00758  88  PHE   D CA    
2156 C  C     . PHE   B 89  ? 0.18074 0.09253 0.08061 -0.00311 0.01399  0.01256  88  PHE   D C     
2157 O  O     . PHE   B 89  ? 0.17458 0.11121 0.09187 0.00492  0.00325  0.00090  88  PHE   D O     
2158 C  CB    . PHE   B 89  ? 0.18380 0.11629 0.08949 0.01297  0.01944  -0.01435 88  PHE   D CB    
2159 C  CG    . PHE   B 89  ? 0.17411 0.10203 0.09517 -0.00437 0.00557  -0.00974 88  PHE   D CG    
2160 C  CD1   . PHE   B 89  ? 0.17997 0.10257 0.09969 -0.00832 0.00339  0.00231  88  PHE   D CD1   
2161 C  CD2   . PHE   B 89  ? 0.17438 0.12070 0.10456 0.00672  0.00098  -0.00871 88  PHE   D CD2   
2162 C  CE1   . PHE   B 89  ? 0.17986 0.11914 0.09522 -0.00430 0.00450  -0.00998 88  PHE   D CE1   
2163 C  CE2   . PHE   B 89  ? 0.17208 0.13084 0.11438 0.00524  0.01856  -0.00931 88  PHE   D CE2   
2164 C  CZ    . PHE   B 89  ? 0.18523 0.11896 0.09955 -0.00339 0.00399  -0.01499 88  PHE   D CZ    
2165 N  N     . ILE   B 90  ? 0.16183 0.09159 0.09932 0.00677  0.01236  0.00589  89  ILE   D N     
2166 C  CA    . ILE   B 90  ? 0.17082 0.08947 0.11072 0.00662  0.01051  -0.00020 89  ILE   D CA    
2167 C  C     . ILE   B 90  ? 0.14483 0.10259 0.10056 0.01930  0.00890  0.01713  89  ILE   D C     
2168 O  O     . ILE   B 90  ? 0.16155 0.10965 0.11384 0.00493  -0.00874 0.01153  89  ILE   D O     
2169 C  CB    . ILE   B 90  ? 0.17187 0.10914 0.12057 0.00205  0.02516  -0.01035 89  ILE   D CB    
2170 C  CG1   . ILE   B 90  ? 0.18049 0.09932 0.12329 -0.03129 0.00888  -0.00133 89  ILE   D CG1   
2171 C  CG2   . ILE   B 90  ? 0.19026 0.12577 0.13018 0.03559  0.00843  -0.01417 89  ILE   D CG2   
2172 C  CD1   . ILE   B 90  ? 0.21619 0.13146 0.12912 -0.02237 -0.00367 -0.00748 89  ILE   D CD1   
2173 N  N     . LEU   B 91  ? 0.14330 0.10681 0.10768 -0.00168 0.01582  0.01300  90  LEU   D N     
2174 C  CA    . LEU   B 91  ? 0.16269 0.09734 0.10324 0.00753  0.01696  0.01872  90  LEU   D CA    
2175 C  C     . LEU   B 91  ? 0.15762 0.10188 0.11926 0.02267  0.00956  0.01558  90  LEU   D C     
2176 O  O     . LEU   B 91  ? 0.16583 0.11945 0.12110 -0.00127 -0.00846 0.00377  90  LEU   D O     
2177 C  CB    . LEU   B 91  ? 0.16322 0.11694 0.11607 0.00615  0.02101  0.00318  90  LEU   D CB    
2178 C  CG    . LEU   B 91  ? 0.18319 0.11968 0.12546 0.02560  0.02274  -0.00850 90  LEU   D CG    
2179 C  CD1   . LEU   B 91  ? 0.20277 0.14323 0.13066 0.00987  0.01934  -0.01198 90  LEU   D CD1   
2180 C  CD2   . LEU   B 91  ? 0.23498 0.13334 0.14567 0.02814  0.02129  -0.01054 90  LEU   D CD2   
2181 N  N     . LYS   B 92  ? 0.14740 0.11514 0.13562 -0.01486 0.01051  0.00845  91  LYS   D N     
2182 C  CA    . LYS   B 92  ? 0.15051 0.12859 0.12932 -0.00851 0.00338  0.01120  91  LYS   D CA    
2183 C  C     . LYS   B 92  ? 0.12561 0.12876 0.11409 -0.00511 0.01259  0.00309  91  LYS   D C     
2184 O  O     . LYS   B 92  ? 0.15479 0.11204 0.12539 0.00196  0.01063  0.00577  91  LYS   D O     
2185 C  CB    . LYS   B 92  ? 0.20241 0.16206 0.13431 -0.04297 0.00494  0.03594  91  LYS   D CB    
2186 C  CG    . LYS   B 92  ? 0.26390 0.23144 0.15997 -0.05457 0.03128  0.04478  91  LYS   D CG    
2187 C  CD    . LYS   B 92  ? 0.35741 0.27556 0.19271 -0.03561 0.04605  0.02587  91  LYS   D CD    
2188 C  CE    . LYS   B 92  ? 0.36280 0.31306 0.22116 -0.05249 0.09612  0.01080  91  LYS   D CE    
2189 N  NZ    . LYS   B 92  ? 0.31786 0.30323 0.21833 -0.05578 0.08018  0.01926  91  LYS   D NZ    
2190 N  N     . HIS   B 93  ? 0.13338 0.12523 0.12024 0.00182  0.00656  0.01259  92  HIS   D N     
2191 C  CA    . HIS   B 93  ? 0.12654 0.11934 0.13304 -0.00431 0.01337  0.01689  92  HIS   D CA    
2192 C  C     . HIS   B 93  ? 0.13224 0.12969 0.14680 0.00487  0.00229  0.00052  92  HIS   D C     
2193 O  O     . HIS   B 93  ? 0.16092 0.16965 0.17660 0.00440  -0.02086 -0.03485 92  HIS   D O     
2194 C  CB    . HIS   B 93  ? 0.13467 0.13356 0.12761 0.00619  0.00706  -0.00267 92  HIS   D CB    
2195 C  CG    . HIS   B 93  ? 0.11430 0.12422 0.09709 0.01377  0.01056  -0.00478 92  HIS   D CG    
2196 N  ND1   . HIS   B 93  ? 0.12342 0.11721 0.08929 0.00008  0.01129  -0.01187 92  HIS   D ND1   
2197 C  CD2   . HIS   B 93  ? 0.12378 0.11557 0.10221 -0.00045 0.00737  -0.00259 92  HIS   D CD2   
2198 C  CE1   . HIS   B 93  ? 0.14151 0.09528 0.08651 0.00201  0.00400  0.01297  92  HIS   D CE1   
2199 N  NE2   . HIS   B 93  ? 0.13658 0.09249 0.08905 0.00061  0.01486  0.00615  92  HIS   D NE2   
2200 N  N     . THR   B 94  ? 0.13269 0.12826 0.15800 0.01937  -0.00262 0.01664  93  THR   D N     
2201 C  CA    . THR   B 94  ? 0.15115 0.13347 0.18066 0.01651  -0.00449 0.01646  93  THR   D CA    
2202 C  C     . THR   B 94  ? 0.12829 0.13785 0.18372 0.01725  -0.00632 0.01653  93  THR   D C     
2203 O  O     . THR   B 94  ? 0.14247 0.19064 0.21277 -0.00101 -0.02054 0.02672  93  THR   D O     
2204 C  CB    . THR   B 94  ? 0.16437 0.14654 0.20268 0.01823  0.00124  0.01313  93  THR   D CB    
2205 O  OG1   . THR   B 94  ? 0.21927 0.14452 0.21012 0.03544  0.00616  -0.00256 93  THR   D OG1   
2206 C  CG2   . THR   B 94  ? 0.20674 0.15044 0.22312 0.00882  0.01796  0.03103  93  THR   D CG2   
2207 N  N     . GLY   B 95  ? 0.13380 0.12022 0.18138 0.01040  0.00654  0.00878  94  GLY   D N     
2208 C  CA    . GLY   B 95  ? 0.14580 0.13361 0.16622 -0.00291 0.00181  0.00541  94  GLY   D CA    
2209 C  C     . GLY   B 95  ? 0.12465 0.12504 0.17511 0.02316  0.02584  0.00489  94  GLY   D C     
2210 O  O     . GLY   B 95  ? 0.12856 0.12213 0.18677 0.02319  0.02424  -0.00223 94  GLY   D O     
2211 N  N     . PRO   B 96  ? 0.12971 0.14408 0.17504 0.00308  0.02305  -0.00712 95  PRO   D N     
2212 C  CA    . PRO   B 96  ? 0.12484 0.14551 0.16826 -0.00488 0.02467  -0.00917 95  PRO   D CA    
2213 C  C     . PRO   B 96  ? 0.11266 0.13378 0.16963 0.02866  0.02302  -0.00802 95  PRO   D C     
2214 O  O     . PRO   B 96  ? 0.13863 0.15206 0.20388 0.02217  0.00934  -0.02284 95  PRO   D O     
2215 C  CB    . PRO   B 96  ? 0.14722 0.19624 0.18372 -0.01724 0.01858  0.00775  95  PRO   D CB    
2216 C  CG    . PRO   B 96  ? 0.15687 0.21051 0.18840 -0.02535 0.01317  0.00656  95  PRO   D CG    
2217 C  CD    . PRO   B 96  ? 0.12909 0.18696 0.18790 -0.02444 0.01457  -0.00623 95  PRO   D CD    
2218 N  N     . GLY   B 97  ? 0.11199 0.13289 0.15024 0.00604  0.02992  -0.01177 96  GLY   D N     
2219 C  CA    . GLY   B 97  ? 0.11803 0.13678 0.13959 0.00907  0.02537  -0.02251 96  GLY   D CA    
2220 C  C     . GLY   B 97  ? 0.13023 0.10670 0.13550 0.01635  0.02492  -0.00148 96  GLY   D C     
2221 O  O     . GLY   B 97  ? 0.12617 0.11895 0.12960 0.00507  0.02775  -0.01074 96  GLY   D O     
2222 N  N     . ILE   B 98  ? 0.14095 0.11041 0.12956 0.02289  0.02937  0.00184  97  ILE   D N     
2223 C  CA    . ILE   B 98  ? 0.09978 0.12059 0.12281 0.00571  0.01031  0.00072  97  ILE   D CA    
2224 C  C     . ILE   B 98  ? 0.10121 0.10543 0.10783 -0.00336 0.01486  -0.00748 97  ILE   D C     
2225 O  O     . ILE   B 98  ? 0.13982 0.09804 0.12181 -0.00207 0.02428  0.00027  97  ILE   D O     
2226 C  CB    . ILE   B 98  ? 0.13982 0.14220 0.12549 -0.00433 0.00489  0.01063  97  ILE   D CB    
2227 C  CG1   . ILE   B 98  ? 0.17913 0.14226 0.15447 -0.00353 -0.02011 0.03227  97  ILE   D CG1   
2228 C  CG2   . ILE   B 98  ? 0.14841 0.18283 0.12754 -0.00720 0.02116  0.01060  97  ILE   D CG2   
2229 C  CD1   . ILE   B 98  ? 0.21410 0.16706 0.17400 0.00952  -0.03357 0.03373  97  ILE   D CD1   
2230 N  N     . LEU   B 99  ? 0.11296 0.09539 0.10353 0.01752  0.02073  0.00192  98  LEU   D N     
2231 C  CA    . LEU   B 99  ? 0.12898 0.09025 0.09114 0.01109  0.01003  -0.01107 98  LEU   D CA    
2232 C  C     . LEU   B 99  ? 0.11302 0.07671 0.09818 0.00032  0.00622  0.00204  98  LEU   D C     
2233 O  O     . LEU   B 99  ? 0.12328 0.09011 0.11381 0.00886  0.01632  0.00559  98  LEU   D O     
2234 C  CB    . LEU   B 99  ? 0.18910 0.10240 0.10609 0.01388  0.01259  -0.00134 98  LEU   D CB    
2235 C  CG    . LEU   B 99  ? 0.21609 0.10824 0.13401 0.01199  -0.01702 0.00437  98  LEU   D CG    
2236 C  CD1   . LEU   B 99  ? 0.24549 0.09918 0.13709 0.00236  -0.04405 0.01378  98  LEU   D CD1   
2237 C  CD2   . LEU   B 99  ? 0.22894 0.10727 0.12036 0.00948  -0.01943 -0.02341 98  LEU   D CD2   
2238 N  N     . SER   B 100 ? 0.10688 0.09014 0.08685 0.00945  0.01854  -0.00521 99  SER   D N     
2239 C  CA    . SER   B 100 ? 0.12762 0.10077 0.07665 0.01135  0.02434  -0.00081 99  SER   D CA    
2240 C  C     . SER   B 100 ? 0.10493 0.09645 0.07088 0.01597  0.02174  0.00723  99  SER   D C     
2241 O  O     . SER   B 100 ? 0.11658 0.09611 0.08642 0.00578  0.01390  0.01421  99  SER   D O     
2242 C  CB    . SER   B 100 ? 0.12281 0.11566 0.07674 0.00805  0.01243  -0.00215 99  SER   D CB    
2243 O  OG    . SER   B 100 ? 0.12883 0.13527 0.07706 0.00652  0.02387  0.00155  99  SER   D OG    
2244 N  N     . MET   B 101 ? 0.11360 0.10499 0.08782 0.01617  0.01201  0.00038  100 MET   D N     
2245 C  CA    . MET   B 101 ? 0.11182 0.09314 0.08636 0.00932  0.01509  -0.00508 100 MET   D CA    
2246 C  C     . MET   B 101 ? 0.10540 0.09630 0.07566 -0.00167 0.01505  -0.00556 100 MET   D C     
2247 O  O     . MET   B 101 ? 0.12408 0.10850 0.07647 0.00811  0.01751  0.00166  100 MET   D O     
2248 C  CB    . MET   B 101 ? 0.11650 0.10092 0.09443 -0.00755 0.02521  -0.01019 100 MET   D CB    
2249 C  CG    . MET   B 101 ? 0.13785 0.10122 0.10489 0.00423  0.02411  -0.01116 100 MET   D CG    
2250 S  SD    . MET   B 101 ? 0.13161 0.10499 0.10633 0.00691  0.00576  -0.01286 100 MET   D SD    
2251 C  CE    . MET   B 101 ? 0.13260 0.13949 0.13721 0.02173  0.01118  -0.00828 100 MET   D CE    
2252 N  N     . ALA   B 102 ? 0.11652 0.07455 0.08790 0.00576  0.02460  0.00395  101 ALA   D N     
2253 C  CA    . ALA   B 102 ? 0.11702 0.09005 0.09019 0.01840  0.02551  -0.00274 101 ALA   D CA    
2254 C  C     . ALA   B 102 ? 0.11100 0.10055 0.07452 0.02788  0.02660  0.00379  101 ALA   D C     
2255 O  O     . ALA   B 102 ? 0.12410 0.11622 0.09292 -0.00685 0.00037  -0.01745 101 ALA   D O     
2256 C  CB    . ALA   B 102 ? 0.13419 0.09684 0.10269 0.01074  0.01941  0.00860  101 ALA   D CB    
2257 N  N     . ASN   B 103 ? 0.10334 0.10551 0.08796 0.01522  0.03316  0.00012  102 ASN   D N     
2258 C  CA    . ASN   B 103 ? 0.11931 0.10204 0.09027 0.00534  0.02993  -0.00811 102 ASN   D CA    
2259 C  C     . ASN   B 103 ? 0.12800 0.09834 0.10002 0.00355  0.03744  -0.00493 102 ASN   D C     
2260 O  O     . ASN   B 103 ? 0.14317 0.09717 0.11257 -0.00176 0.03934  -0.00464 102 ASN   D O     
2261 C  CB    . ASN   B 103 ? 0.11243 0.10655 0.09516 0.00486  0.02207  0.00679  102 ASN   D CB    
2262 C  CG    . ASN   B 103 ? 0.11862 0.12100 0.10040 0.00673  0.02603  0.00267  102 ASN   D CG    
2263 O  OD1   . ASN   B 103 ? 0.14670 0.13269 0.08886 0.00917  0.01262  -0.00633 102 ASN   D OD1   
2264 N  ND2   . ASN   B 103 ? 0.12708 0.12528 0.11340 0.00950  0.02113  0.00721  102 ASN   D ND2   
2265 N  N     . ALA   B 104 ? 0.13194 0.11260 0.10886 0.02101  0.03582  -0.00848 103 ALA   D N     
2266 C  CA    . ALA   B 104 ? 0.14341 0.13310 0.12786 0.02758  0.04911  -0.02052 103 ALA   D CA    
2267 C  C     . ALA   B 104 ? 0.16918 0.16336 0.13352 0.00987  0.05707  -0.01726 103 ALA   D C     
2268 O  O     . ALA   B 104 ? 0.21435 0.20412 0.16609 0.04066  0.09879  -0.01049 103 ALA   D O     
2269 C  CB    . ALA   B 104 ? 0.15326 0.14288 0.15798 0.03548  0.04556  -0.00144 103 ALA   D CB    
2270 N  N     . GLY   B 105 ? 0.16332 0.14784 0.10186 -0.00614 0.04102  -0.03445 104 GLY   D N     
2271 C  CA    . GLY   B 105 ? 0.21462 0.14148 0.09801 -0.01334 0.04911  -0.03278 104 GLY   D CA    
2272 C  C     . GLY   B 105 ? 0.16833 0.14799 0.10675 -0.00011 0.03042  -0.02490 104 GLY   D C     
2273 O  O     . GLY   B 105 ? 0.15755 0.12880 0.10384 0.00118  0.03626  -0.01216 104 GLY   D O     
2274 N  N     . PRO   B 106 ? 0.20409 0.15671 0.11126 -0.01550 0.05430  -0.02238 105 PRO   D N     
2275 C  CA    . PRO   B 106 ? 0.20419 0.16604 0.11731 -0.02545 0.05776  -0.00024 105 PRO   D CA    
2276 C  C     . PRO   B 106 ? 0.15906 0.15147 0.13640 -0.00878 0.06884  -0.00804 105 PRO   D C     
2277 O  O     . PRO   B 106 ? 0.14309 0.16598 0.16432 -0.00225 0.06718  -0.02366 105 PRO   D O     
2278 C  CB    . PRO   B 106 ? 0.25022 0.19836 0.12085 -0.03658 0.06214  -0.00442 105 PRO   D CB    
2279 C  CG    . PRO   B 106 ? 0.31157 0.20392 0.13005 -0.04767 0.07057  -0.01412 105 PRO   D CG    
2280 C  CD    . PRO   B 106 ? 0.26710 0.18242 0.11293 -0.02517 0.07822  -0.00950 105 PRO   D CD    
2281 N  N     . ASN   B 107 ? 0.16219 0.14233 0.12441 0.00000  0.06624  0.00217  106 ASN   D N     
2282 C  CA    . ASN   B 107 ? 0.14603 0.13764 0.14815 -0.01319 0.04268  -0.00248 106 ASN   D CA    
2283 C  C     . ASN   B 107 ? 0.13928 0.12793 0.15087 0.00408  0.02598  -0.00992 106 ASN   D C     
2284 O  O     . ASN   B 107 ? 0.13919 0.16040 0.17947 -0.00771 0.02588  -0.01562 106 ASN   D O     
2285 C  CB    . ASN   B 107 ? 0.16435 0.17203 0.17043 -0.02384 0.04563  0.00116  106 ASN   D CB    
2286 C  CG    . ASN   B 107 ? 0.16601 0.17500 0.17579 -0.02162 0.06374  0.00694  106 ASN   D CG    
2287 O  OD1   . ASN   B 107 ? 0.16949 0.16297 0.15973 -0.01415 0.06071  0.01060  106 ASN   D OD1   
2288 N  ND2   . ASN   B 107 ? 0.25453 0.20913 0.20195 0.00347  0.11729  0.01187  106 ASN   D ND2   
2289 N  N     . THR   B 108 ? 0.15379 0.11949 0.13001 -0.00614 0.03308  -0.01709 107 THR   D N     
2290 C  CA    . THR   B 108 ? 0.14840 0.11995 0.12670 0.01098  0.02894  -0.01431 107 THR   D CA    
2291 C  C     . THR   B 108 ? 0.15253 0.11876 0.11592 0.01152  0.02047  -0.02358 107 THR   D C     
2292 O  O     . THR   B 108 ? 0.19664 0.11982 0.14280 0.01296  0.04609  -0.01107 107 THR   D O     
2293 C  CB    . THR   B 108 ? 0.12246 0.13376 0.14872 0.00212  0.03259  -0.02728 107 THR   D CB    
2294 O  OG1   . THR   B 108 ? 0.12194 0.13164 0.13238 -0.00190 0.01541  -0.02292 107 THR   D OG1   
2295 C  CG2   . THR   B 108 ? 0.14341 0.14212 0.17007 0.00105  0.05596  -0.03483 107 THR   D CG2   
2296 N  N     . ASN   B 109 ? 0.14696 0.12255 0.10123 0.02199  0.02082  -0.01292 108 ASN   D N     
2297 C  CA    . ASN   B 109 ? 0.15151 0.12735 0.08756 0.03426  0.02176  -0.01141 108 ASN   D CA    
2298 C  C     . ASN   B 109 ? 0.14539 0.12954 0.09273 0.01836  0.02310  -0.00235 108 ASN   D C     
2299 O  O     . ASN   B 109 ? 0.13110 0.15225 0.12503 0.00259  0.01013  0.00374  108 ASN   D O     
2300 C  CB    . ASN   B 109 ? 0.14472 0.13362 0.10090 0.02432  0.00073  0.00499  108 ASN   D CB    
2301 C  CG    . ASN   B 109 ? 0.13357 0.11910 0.09150 0.00721  0.01815  -0.00120 108 ASN   D CG    
2302 O  OD1   . ASN   B 109 ? 0.12716 0.15028 0.10426 -0.00922 0.01069  0.00986  108 ASN   D OD1   
2303 N  ND2   . ASN   B 109 ? 0.15722 0.10732 0.10728 0.00594  0.03254  0.01412  108 ASN   D ND2   
2304 N  N     . GLY   B 110 ? 0.13286 0.11739 0.08337 0.01882  0.01164  -0.00277 109 GLY   D N     
2305 C  CA    . GLY   B 110 ? 0.14167 0.11641 0.08968 0.02154  0.01707  -0.01647 109 GLY   D CA    
2306 C  C     . GLY   B 110 ? 0.12687 0.10121 0.09150 0.01440  0.00676  -0.00975 109 GLY   D C     
2307 O  O     . GLY   B 110 ? 0.16026 0.09703 0.11269 0.00726  0.02183  -0.01177 109 GLY   D O     
2308 N  N     . SER   B 111 ? 0.12355 0.09674 0.09050 -0.00081 0.00844  -0.00489 110 SER   D N     
2309 C  CA    . SER   B 111 ? 0.11681 0.09255 0.09128 0.01112  0.02454  -0.00642 110 SER   D CA    
2310 C  C     . SER   B 111 ? 0.13149 0.08593 0.07547 0.01431  0.01350  -0.00089 110 SER   D C     
2311 O  O     . SER   B 111 ? 0.12788 0.10530 0.08990 0.02153  0.01937  -0.02127 110 SER   D O     
2312 C  CB    . SER   B 111 ? 0.14192 0.10322 0.09418 0.01728  0.00730  -0.00913 110 SER   D CB    
2313 O  OG    . SER   B 111 ? 0.14568 0.11439 0.09737 0.01254  -0.00616 -0.00074 110 SER   D OG    
2314 N  N     . GLN   B 112 ? 0.11468 0.09536 0.08490 0.01099  0.01237  -0.01204 111 GLN   D N     
2315 C  CA    . GLN   B 112 ? 0.10581 0.09729 0.08905 0.01088  -0.00046 -0.00663 111 GLN   D CA    
2316 C  C     . GLN   B 112 ? 0.10541 0.08515 0.07148 0.00386  0.01433  -0.00275 111 GLN   D C     
2317 O  O     . GLN   B 112 ? 0.12114 0.09611 0.08898 0.01122  0.02553  -0.00193 111 GLN   D O     
2318 C  CB    . GLN   B 112 ? 0.14440 0.08097 0.09269 0.02409  0.00897  -0.00876 111 GLN   D CB    
2319 C  CG    . GLN   B 112 ? 0.14980 0.08601 0.10713 0.03080  -0.00784 -0.01157 111 GLN   D CG    
2320 C  CD    . GLN   B 112 ? 0.14948 0.09131 0.10812 0.00840  0.01554  -0.01028 111 GLN   D CD    
2321 O  OE1   . GLN   B 112 ? 0.13740 0.09452 0.12267 0.00670  -0.00227 -0.01478 111 GLN   D OE1   
2322 N  NE2   . GLN   B 112 ? 0.16263 0.11426 0.11055 0.04386  0.01405  -0.00878 111 GLN   D NE2   
2323 N  N     . PHE   B 113 ? 0.10585 0.10273 0.07684 0.00489  0.02052  -0.01091 112 PHE   D N     
2324 C  CA    . PHE   B 113 ? 0.10153 0.09312 0.08412 0.02153  0.01370  -0.01337 112 PHE   D CA    
2325 C  C     . PHE   B 113 ? 0.10877 0.08523 0.07176 0.01045  0.01709  -0.00195 112 PHE   D C     
2326 O  O     . PHE   B 113 ? 0.12069 0.09345 0.08507 0.00557  0.01564  0.00643  112 PHE   D O     
2327 C  CB    . PHE   B 113 ? 0.13246 0.10327 0.08789 0.01688  0.01604  -0.01181 112 PHE   D CB    
2328 C  CG    . PHE   B 113 ? 0.12980 0.11019 0.07895 0.02427  0.01673  -0.01437 112 PHE   D CG    
2329 C  CD1   . PHE   B 113 ? 0.12984 0.11992 0.09291 0.01792  0.02715  -0.00334 112 PHE   D CD1   
2330 C  CD2   . PHE   B 113 ? 0.15136 0.11516 0.07570 0.01832  0.01010  -0.01100 112 PHE   D CD2   
2331 C  CE1   . PHE   B 113 ? 0.16940 0.14352 0.08371 0.04316  0.04005  0.00640  112 PHE   D CE1   
2332 C  CE2   . PHE   B 113 ? 0.14989 0.14472 0.08719 0.03124  0.01936  0.00201  112 PHE   D CE2   
2333 C  CZ    . PHE   B 113 ? 0.14931 0.16124 0.08219 0.03373  0.03381  0.00568  112 PHE   D CZ    
2334 N  N     . PHE   B 114 ? 0.10915 0.10094 0.07137 0.01194  0.01375  -0.00420 113 PHE   D N     
2335 C  CA    . PHE   B 114 ? 0.10851 0.09147 0.07999 0.01972  0.02501  -0.00948 113 PHE   D CA    
2336 C  C     . PHE   B 114 ? 0.13616 0.07616 0.07986 -0.00322 0.02270  -0.00032 113 PHE   D C     
2337 O  O     . PHE   B 114 ? 0.13143 0.08211 0.09179 0.00535  0.01713  0.00707  113 PHE   D O     
2338 C  CB    . PHE   B 114 ? 0.12672 0.08933 0.08698 0.01863  0.02045  0.00414  113 PHE   D CB    
2339 C  CG    . PHE   B 114 ? 0.11999 0.08174 0.08517 0.01728  0.01919  -0.00794 113 PHE   D CG    
2340 C  CD1   . PHE   B 114 ? 0.13457 0.09734 0.09093 0.01307  0.02603  -0.01702 113 PHE   D CD1   
2341 C  CD2   . PHE   B 114 ? 0.13477 0.09442 0.08483 0.01722  0.00505  -0.00779 113 PHE   D CD2   
2342 C  CE1   . PHE   B 114 ? 0.13455 0.10450 0.07907 0.01654  0.00797  -0.00502 113 PHE   D CE1   
2343 C  CE2   . PHE   B 114 ? 0.12109 0.09520 0.10218 0.01920  0.01583  -0.01474 113 PHE   D CE2   
2344 C  CZ    . PHE   B 114 ? 0.13787 0.08728 0.10013 0.00584  0.01169  -0.01775 113 PHE   D CZ    
2345 N  N     . ILE   B 115 ? 0.09709 0.08766 0.10812 0.00609  0.03772  -0.00460 114 ILE   D N     
2346 C  CA    . ILE   B 115 ? 0.12397 0.10036 0.11223 0.00768  0.01836  -0.00643 114 ILE   D CA    
2347 C  C     . ILE   B 115 ? 0.13166 0.09075 0.11714 0.01660  0.03640  0.00078  114 ILE   D C     
2348 O  O     . ILE   B 115 ? 0.12873 0.08712 0.12688 0.00974  0.01172  -0.00843 114 ILE   D O     
2349 C  CB    . ILE   B 115 ? 0.14284 0.10916 0.11247 0.01612  0.02693  -0.00694 114 ILE   D CB    
2350 C  CG1   . ILE   B 115 ? 0.16172 0.11735 0.11363 0.01165  0.01912  -0.00298 114 ILE   D CG1   
2351 C  CG2   . ILE   B 115 ? 0.13244 0.11852 0.13047 0.01687  0.03295  -0.00155 114 ILE   D CG2   
2352 C  CD1   . ILE   B 115 ? 0.18097 0.14498 0.11891 0.01629  0.03239  -0.01999 114 ILE   D CD1   
2353 N  N     . CYS   B 116 ? 0.13373 0.11396 0.10542 0.00319  0.00831  0.00084  115 CYS   D N     
2354 C  CA    . CYS   B 116 ? 0.12271 0.12100 0.12241 0.00121  0.00969  0.00258  115 CYS   D CA    
2355 C  C     . CYS   B 116 ? 0.13701 0.11625 0.13140 0.01883  0.01242  -0.00101 115 CYS   D C     
2356 O  O     . CYS   B 116 ? 0.13176 0.11903 0.14066 0.02814  0.02019  -0.00795 115 CYS   D O     
2357 C  CB    . CYS   B 116 ? 0.13680 0.14405 0.12482 0.01508  0.01345  0.00243  115 CYS   D CB    
2358 S  SG    . CYS   B 116 ? 0.14238 0.18287 0.12631 -0.00489 0.01754  -0.01138 115 CYS   D SG    
2359 N  N     . THR   B 117 ? 0.13311 0.13446 0.14662 -0.00152 0.01075  -0.00062 116 THR   D N     
2360 C  CA    . THR   B 117 ? 0.13180 0.14839 0.15378 -0.02310 0.01094  -0.00080 116 THR   D CA    
2361 C  C     . THR   B 117 ? 0.12567 0.17497 0.17631 -0.01988 0.00561  -0.00902 116 THR   D C     
2362 O  O     . THR   B 117 ? 0.12722 0.25160 0.21635 -0.01354 0.00700  0.00064  116 THR   D O     
2363 C  CB    . THR   B 117 ? 0.19323 0.14927 0.14503 -0.02813 0.02857  -0.00835 116 THR   D CB    
2364 O  OG1   . THR   B 117 ? 0.23154 0.13823 0.15755 -0.02945 0.02762  -0.00496 116 THR   D OG1   
2365 C  CG2   . THR   B 117 ? 0.21894 0.15872 0.14379 -0.02716 0.03880  -0.00355 116 THR   D CG2   
2366 N  N     . ALA   B 118 ? 0.14871 0.15586 0.16053 0.00759  0.00362  -0.00398 117 ALA   D N     
2367 C  CA    . ALA   B 118 ? 0.16839 0.14516 0.16737 -0.00629 -0.00458 0.00360  117 ALA   D CA    
2368 C  C     . ALA   B 118 ? 0.13416 0.14468 0.15904 0.01506  -0.00415 0.01344  117 ALA   D C     
2369 O  O     . ALA   B 118 ? 0.12934 0.14981 0.17044 -0.00365 -0.00814 0.00702  117 ALA   D O     
2370 C  CB    . ALA   B 118 ? 0.23431 0.14577 0.19208 -0.00885 -0.01419 -0.00421 117 ALA   D CB    
2371 N  N     . LYS   B 119 ? 0.14313 0.16385 0.15199 0.00495  -0.00475 0.00640  118 LYS   D N     
2372 C  CA    . LYS   B 119 ? 0.14811 0.16726 0.15033 0.01368  -0.00124 0.01260  118 LYS   D CA    
2373 C  C     . LYS   B 119 ? 0.13928 0.15403 0.16605 0.00945  -0.00058 -0.00539 118 LYS   D C     
2374 O  O     . LYS   B 119 ? 0.15611 0.15499 0.20903 -0.01209 -0.00151 -0.02387 118 LYS   D O     
2375 C  CB    . LYS   B 119 ? 0.19167 0.20316 0.16246 -0.00325 -0.01713 0.02767  118 LYS   D CB    
2376 C  CG    . LYS   B 119 ? 0.18324 0.21303 0.18306 0.01556  -0.03254 0.04464  118 LYS   D CG    
2377 C  CD    . LYS   B 119 ? 0.24894 0.26376 0.22292 0.04599  -0.02615 0.06715  118 LYS   D CD    
2378 C  CE    . LYS   B 119 ? 0.29968 0.31694 0.25096 0.11257  -0.02920 0.08231  118 LYS   D CE    
2379 N  NZ    . LYS   B 119 ? 0.35347 0.37103 0.26537 0.12155  -0.03184 0.08821  118 LYS   D NZ    
2380 N  N     . THR   B 120 ? 0.14334 0.14339 0.14852 0.00559  -0.00249 -0.00654 119 THR   D N     
2381 C  CA    . THR   B 120 ? 0.15885 0.15807 0.14597 0.00323  0.00943  -0.01011 119 THR   D CA    
2382 C  C     . THR   B 120 ? 0.14002 0.14735 0.13992 0.00685  -0.01313 -0.00816 119 THR   D C     
2383 O  O     . THR   B 120 ? 0.14586 0.13822 0.12248 0.00421  -0.00037 -0.01063 119 THR   D O     
2384 C  CB    . THR   B 120 ? 0.16342 0.13431 0.15270 0.00323  0.00247  0.00313  119 THR   D CB    
2385 O  OG1   . THR   B 120 ? 0.16542 0.12340 0.14275 0.00908  -0.00589 -0.00892 119 THR   D OG1   
2386 C  CG2   . THR   B 120 ? 0.19723 0.14270 0.17889 0.00266  0.00777  0.00984  119 THR   D CG2   
2387 N  N     . GLU   B 121 ? 0.17139 0.17717 0.14015 -0.00411 -0.03813 0.01552  120 GLU   D N     
2388 C  CA    . GLU   B 121 ? 0.19514 0.19295 0.14653 0.01517  -0.03761 0.01820  120 GLU   D CA    
2389 C  C     . GLU   B 121 ? 0.17502 0.17562 0.13229 0.00628  -0.02469 0.00944  120 GLU   D C     
2390 O  O     . GLU   B 121 ? 0.17650 0.17743 0.12634 -0.00691 -0.02807 0.01448  120 GLU   D O     
2391 C  CB    . GLU   B 121 ? 0.22974 0.21696 0.17426 0.00677  -0.04356 0.03003  120 GLU   D CB    
2392 C  CG    . GLU   B 121 ? 0.27992 0.26592 0.20281 0.02045  -0.05435 0.07316  120 GLU   D CG    
2393 C  CD    . GLU   B 121 ? 0.36208 0.34866 0.23692 0.01971  -0.03651 0.09055  120 GLU   D CD    
2394 O  OE1   . GLU   B 121 ? 0.37187 0.38534 0.25340 0.00728  -0.04414 0.07512  120 GLU   D OE1   
2395 O  OE2   . GLU   B 121 ? 0.39668 0.37787 0.26506 0.04489  -0.02191 0.11356  120 GLU   D OE2   
2396 N  N     . TRP   B 122 ? 0.19355 0.16696 0.13285 0.01911  -0.03149 -0.00017 121 TRP   D N     
2397 C  CA    . TRP   B 122 ? 0.21605 0.16415 0.12836 -0.00762 -0.01689 -0.00973 121 TRP   D CA    
2398 C  C     . TRP   B 122 ? 0.17328 0.15342 0.09927 -0.01329 -0.00349 -0.00627 121 TRP   D C     
2399 O  O     . TRP   B 122 ? 0.21778 0.18829 0.11499 -0.02128 0.03264  -0.01972 121 TRP   D O     
2400 C  CB    . TRP   B 122 ? 0.23788 0.15480 0.15355 -0.00196 -0.01759 -0.01193 121 TRP   D CB    
2401 C  CG    . TRP   B 122 ? 0.21400 0.17067 0.18637 0.01831  0.01423  -0.02035 121 TRP   D CG    
2402 C  CD1   . TRP   B 122 ? 0.24186 0.17455 0.19839 0.03941  0.00863  0.00342  121 TRP   D CD1   
2403 C  CD2   . TRP   B 122 ? 0.20851 0.14589 0.16750 0.00060  -0.00839 -0.01905 121 TRP   D CD2   
2404 N  NE1   . TRP   B 122 ? 0.21276 0.18243 0.22030 0.00878  0.00329  0.00662  121 TRP   D NE1   
2405 C  CE2   . TRP   B 122 ? 0.19531 0.17257 0.19149 0.00945  0.01655  -0.00371 121 TRP   D CE2   
2406 C  CE3   . TRP   B 122 ? 0.22613 0.15281 0.14000 0.00135  -0.02676 -0.01163 121 TRP   D CE3   
2407 C  CZ2   . TRP   B 122 ? 0.16968 0.18138 0.17452 0.00069  -0.00746 -0.00073 121 TRP   D CZ2   
2408 C  CZ3   . TRP   B 122 ? 0.22821 0.16863 0.15197 0.01396  -0.01340 -0.00199 121 TRP   D CZ3   
2409 C  CH2   . TRP   B 122 ? 0.17743 0.15481 0.16693 0.02218  -0.01829 -0.01134 121 TRP   D CH2   
2410 N  N     . LEU   B 123 ? 0.16356 0.14358 0.08119 -0.00499 -0.00136 -0.00326 122 LEU   D N     
2411 C  CA    . LEU   B 123 ? 0.15943 0.12227 0.08377 -0.00241 -0.00065 -0.00533 122 LEU   D CA    
2412 C  C     . LEU   B 123 ? 0.14937 0.12918 0.07824 -0.01195 0.01280  0.00845  122 LEU   D C     
2413 O  O     . LEU   B 123 ? 0.14429 0.13151 0.08764 0.00734  0.00924  0.00572  122 LEU   D O     
2414 C  CB    . LEU   B 123 ? 0.16347 0.12154 0.09685 -0.00520 0.00939  0.00664  122 LEU   D CB    
2415 C  CG    . LEU   B 123 ? 0.17382 0.11437 0.10695 -0.00090 0.01694  -0.00682 122 LEU   D CG    
2416 C  CD1   . LEU   B 123 ? 0.19387 0.11643 0.10275 -0.00240 0.03219  0.00815  122 LEU   D CD1   
2417 C  CD2   . LEU   B 123 ? 0.18239 0.13648 0.13454 0.02651  0.03376  -0.00705 122 LEU   D CD2   
2418 N  N     . ASP   B 124 ? 0.15482 0.11173 0.09056 0.00181  0.02074  0.01449  123 ASP   D N     
2419 C  CA    . ASP   B 124 ? 0.14899 0.12779 0.10843 0.00130  0.01270  0.01398  123 ASP   D CA    
2420 C  C     . ASP   B 124 ? 0.13746 0.12546 0.09925 0.00790  0.01894  0.00585  123 ASP   D C     
2421 O  O     . ASP   B 124 ? 0.14609 0.14281 0.10071 -0.00368 0.01799  -0.00994 123 ASP   D O     
2422 C  CB    . ASP   B 124 ? 0.15297 0.14798 0.09539 0.02820  0.01299  0.02512  123 ASP   D CB    
2423 C  CG    . ASP   B 124 ? 0.17101 0.14683 0.08929 0.02702  -0.00645 0.01696  123 ASP   D CG    
2424 O  OD1   . ASP   B 124 ? 0.15987 0.15131 0.09330 0.02062  0.00453  0.00272  123 ASP   D OD1   
2425 O  OD2   . ASP   B 124 ? 0.17136 0.17568 0.10280 0.02579  0.00430  0.02322  123 ASP   D OD2   
2426 N  N     . GLY   B 125 ? 0.14312 0.11888 0.09257 -0.00735 0.01416  0.00348  124 GLY   D N     
2427 C  CA    . GLY   B 125 ? 0.15693 0.12111 0.08638 -0.00343 0.01321  0.00737  124 GLY   D CA    
2428 C  C     . GLY   B 125 ? 0.13561 0.12495 0.06656 -0.00587 0.01757  0.00629  124 GLY   D C     
2429 O  O     . GLY   B 125 ? 0.15635 0.14182 0.07454 -0.00973 0.01042  0.00424  124 GLY   D O     
2430 N  N     . LYS   B 126 ? 0.15720 0.12965 0.06230 0.01123  0.00857  0.00716  125 LYS   D N     
2431 C  CA    . LYS   B 126 ? 0.17878 0.13869 0.07137 0.03199  0.00672  -0.01212 125 LYS   D CA    
2432 C  C     . LYS   B 126 ? 0.14961 0.11453 0.07103 0.03378  0.01923  0.01056  125 LYS   D C     
2433 O  O     . LYS   B 126 ? 0.13972 0.15521 0.09240 0.03169  0.01759  -0.00174 125 LYS   D O     
2434 C  CB    . LYS   B 126 ? 0.29555 0.17692 0.09701 0.05866  -0.00572 -0.03802 125 LYS   D CB    
2435 C  CG    . LYS   B 126 ? 0.40173 0.22774 0.13098 0.06618  0.01415  -0.04779 125 LYS   D CG    
2436 C  CD    . LYS   B 126 ? 0.45839 0.27922 0.16956 0.02736  0.05422  -0.06129 125 LYS   D CD    
2437 C  CE    . LYS   B 126 ? 0.52116 0.33158 0.21776 -0.00181 0.06967  -0.06222 125 LYS   D CE    
2438 N  NZ    . LYS   B 126 ? 0.57553 0.37384 0.24955 0.00401  0.07700  -0.06346 125 LYS   D NZ    
2439 N  N     . HIS   B 127 ? 0.13532 0.09967 0.06405 0.00815  0.01490  -0.00290 126 HIS   D N     
2440 C  CA    . HIS   B 127 ? 0.13802 0.09109 0.06756 0.00262  0.01898  -0.00467 126 HIS   D CA    
2441 C  C     . HIS   B 127 ? 0.14075 0.09362 0.06995 0.00554  0.02493  0.00088  126 HIS   D C     
2442 O  O     . HIS   B 127 ? 0.14097 0.09785 0.08732 0.02019  0.00172  -0.00375 126 HIS   D O     
2443 C  CB    . HIS   B 127 ? 0.13905 0.10259 0.09636 0.00497  0.01420  -0.00311 126 HIS   D CB    
2444 C  CG    . HIS   B 127 ? 0.13252 0.09023 0.10282 -0.00385 0.02237  -0.00528 126 HIS   D CG    
2445 N  ND1   . HIS   B 127 ? 0.12640 0.08749 0.11715 0.01172  0.02177  0.01217  126 HIS   D ND1   
2446 C  CD2   . HIS   B 127 ? 0.16492 0.10750 0.11327 -0.00089 0.02712  -0.02746 126 HIS   D CD2   
2447 C  CE1   . HIS   B 127 ? 0.14785 0.09255 0.13390 0.00773  0.01983  -0.01068 126 HIS   D CE1   
2448 N  NE2   . HIS   B 127 ? 0.14933 0.10465 0.13303 0.00369  0.02283  -0.01986 126 HIS   D NE2   
2449 N  N     . VAL   B 128 ? 0.14177 0.09491 0.06724 0.00095  0.02445  -0.01002 127 VAL   D N     
2450 C  CA    . VAL   B 128 ? 0.12650 0.09208 0.08495 -0.00154 0.02042  0.00162  127 VAL   D CA    
2451 C  C     . VAL   B 128 ? 0.13533 0.08163 0.08842 -0.00044 0.02201  0.01070  127 VAL   D C     
2452 O  O     . VAL   B 128 ? 0.12742 0.08789 0.09612 0.00356  0.02122  0.00716  127 VAL   D O     
2453 C  CB    . VAL   B 128 ? 0.12191 0.09991 0.08673 0.00020  0.01064  -0.00277 127 VAL   D CB    
2454 C  CG1   . VAL   B 128 ? 0.15734 0.08623 0.08888 -0.00080 0.01770  -0.00110 127 VAL   D CG1   
2455 C  CG2   . VAL   B 128 ? 0.12222 0.13295 0.09398 -0.01892 0.04469  -0.01466 127 VAL   D CG2   
2456 N  N     . VAL   B 129 ? 0.12560 0.08762 0.09246 0.00653  0.01913  -0.00508 128 VAL   D N     
2457 C  CA    . VAL   B 129 ? 0.14347 0.10179 0.07934 0.01627  0.01714  -0.00393 128 VAL   D CA    
2458 C  C     . VAL   B 129 ? 0.10980 0.09704 0.07714 0.02115  0.02246  0.00996  128 VAL   D C     
2459 O  O     . VAL   B 129 ? 0.13486 0.09985 0.09006 0.00927  0.01764  0.00976  128 VAL   D O     
2460 C  CB    . VAL   B 129 ? 0.13148 0.09517 0.08850 0.01396  0.00074  -0.00817 128 VAL   D CB    
2461 C  CG1   . VAL   B 129 ? 0.14236 0.09363 0.11613 0.01178  0.02038  0.00886  128 VAL   D CG1   
2462 C  CG2   . VAL   B 129 ? 0.14890 0.10920 0.10618 0.00269  0.00268  -0.00750 128 VAL   D CG2   
2463 N  N     . PHE   B 130 ? 0.13431 0.09878 0.07609 0.01601  0.01927  -0.00661 129 PHE   D N     
2464 C  CA    . PHE   B 130 ? 0.14563 0.11440 0.08410 0.00783  0.01719  -0.00771 129 PHE   D CA    
2465 C  C     . PHE   B 130 ? 0.12841 0.10689 0.08769 0.00974  0.01261  -0.00087 129 PHE   D C     
2466 O  O     . PHE   B 130 ? 0.15515 0.10952 0.09131 0.01909  0.01229  -0.01718 129 PHE   D O     
2467 C  CB    . PHE   B 130 ? 0.12440 0.13058 0.11211 0.00967  0.01802  -0.00302 129 PHE   D CB    
2468 C  CG    . PHE   B 130 ? 0.12137 0.12396 0.09514 0.01941  -0.00130 -0.01422 129 PHE   D CG    
2469 C  CD1   . PHE   B 130 ? 0.13523 0.12408 0.09474 0.03214  0.01476  -0.00798 129 PHE   D CD1   
2470 C  CD2   . PHE   B 130 ? 0.13485 0.13379 0.09240 0.01800  -0.00162 -0.01496 129 PHE   D CD2   
2471 C  CE1   . PHE   B 130 ? 0.12443 0.14404 0.08836 0.01548  0.01487  0.00368  129 PHE   D CE1   
2472 C  CE2   . PHE   B 130 ? 0.15094 0.13091 0.09756 0.01942  0.00068  -0.01060 129 PHE   D CE2   
2473 C  CZ    . PHE   B 130 ? 0.15652 0.14091 0.09759 0.02554  0.01022  -0.01690 129 PHE   D CZ    
2474 N  N     . GLY   B 131 ? 0.12344 0.10714 0.10407 0.01151  0.02561  0.00172  130 GLY   D N     
2475 C  CA    . GLY   B 131 ? 0.12419 0.10167 0.11194 0.00276  0.03321  -0.01567 130 GLY   D CA    
2476 C  C     . GLY   B 131 ? 0.12297 0.09478 0.10189 0.02380  0.03778  0.00173  130 GLY   D C     
2477 O  O     . GLY   B 131 ? 0.15573 0.09895 0.09506 0.01946  0.02646  -0.00448 130 GLY   D O     
2478 N  N     A LYS   B 132 ? 0.11887 0.10044 0.11433 0.01939  0.02357  0.00353  131 LYS   D N     
2479 N  N     B LYS   B 132 ? 0.12708 0.10305 0.11691 0.02215  0.04258  0.01597  131 LYS   D N     
2480 C  CA    A LYS   B 132 ? 0.12410 0.10612 0.13096 -0.00467 0.00195  -0.01524 131 LYS   D CA    
2481 C  CA    B LYS   B 132 ? 0.13721 0.11564 0.13757 0.00445  0.03193  0.00848  131 LYS   D CA    
2482 C  C     A LYS   B 132 ? 0.12708 0.10118 0.13985 0.01266  0.03350  -0.02855 131 LYS   D C     
2483 C  C     B LYS   B 132 ? 0.13360 0.11857 0.13922 0.00992  0.04388  -0.00560 131 LYS   D C     
2484 O  O     A LYS   B 132 ? 0.15248 0.10609 0.14114 0.01427  0.04083  -0.04638 131 LYS   D O     
2485 O  O     B LYS   B 132 ? 0.19936 0.14020 0.13846 -0.00205 0.05487  0.00241  131 LYS   D O     
2486 C  CB    A LYS   B 132 ? 0.14548 0.11694 0.16053 0.00212  -0.00618 -0.00953 131 LYS   D CB    
2487 C  CB    B LYS   B 132 ? 0.15214 0.12409 0.17172 0.01430  0.03425  0.01484  131 LYS   D CB    
2488 C  CG    A LYS   B 132 ? 0.14960 0.14515 0.17878 0.00226  -0.01240 -0.00199 131 LYS   D CG    
2489 C  CG    B LYS   B 132 ? 0.17604 0.15146 0.19934 0.03054  0.03184  0.01735  131 LYS   D CG    
2490 C  CD    A LYS   B 132 ? 0.18208 0.18278 0.19803 0.00312  -0.01614 -0.00804 131 LYS   D CD    
2491 C  CD    B LYS   B 132 ? 0.23959 0.16598 0.22291 0.04967  0.04374  0.01367  131 LYS   D CD    
2492 C  CE    A LYS   B 132 ? 0.23343 0.20549 0.21572 0.00567  0.01084  -0.00131 131 LYS   D CE    
2493 C  CE    B LYS   B 132 ? 0.26735 0.15477 0.24363 0.06340  0.05736  0.00672  131 LYS   D CE    
2494 N  NZ    A LYS   B 132 ? 0.28550 0.21304 0.23224 0.04157  0.03375  0.01606  131 LYS   D NZ    
2495 N  NZ    B LYS   B 132 ? 0.32563 0.20638 0.26814 0.03465  0.06518  0.00626  131 LYS   D NZ    
2496 N  N     . VAL   B 133 ? 0.12467 0.10756 0.14730 0.00653  0.03778  0.00138  132 VAL   D N     
2497 C  CA    . VAL   B 133 ? 0.13842 0.11034 0.16358 0.01472  0.03861  0.00148  132 VAL   D CA    
2498 C  C     . VAL   B 133 ? 0.15962 0.13216 0.17806 0.02873  0.04127  -0.00667 132 VAL   D C     
2499 O  O     . VAL   B 133 ? 0.16135 0.13206 0.18936 0.02249  0.04572  -0.01448 132 VAL   D O     
2500 C  CB    . VAL   B 133 ? 0.12926 0.10936 0.17619 0.00645  0.06188  0.00037  132 VAL   D CB    
2501 C  CG1   . VAL   B 133 ? 0.16225 0.11659 0.17482 0.01058  0.06606  -0.00327 132 VAL   D CG1   
2502 C  CG2   . VAL   B 133 ? 0.14321 0.10709 0.17597 0.02155  0.04337  0.00274  132 VAL   D CG2   
2503 N  N     . LYS   B 134 ? 0.17522 0.12148 0.19304 0.03026  0.07080  -0.03072 133 LYS   D N     
2504 C  CA    . LYS   B 134 ? 0.21250 0.14440 0.24691 0.05179  0.09095  -0.02487 133 LYS   D CA    
2505 C  C     . LYS   B 134 ? 0.20857 0.17783 0.27533 0.08671  0.08271  -0.00429 133 LYS   D C     
2506 O  O     . LYS   B 134 ? 0.21436 0.29581 0.31361 0.06002  0.04644  0.04105  133 LYS   D O     
2507 C  CB    . LYS   B 134 ? 0.26147 0.16417 0.28087 0.04777  0.08555  -0.05458 133 LYS   D CB    
2508 C  CG    . LYS   B 134 ? 0.31668 0.20315 0.32269 0.08359  0.05723  -0.06903 133 LYS   D CG    
2509 C  CD    . LYS   B 134 ? 0.40031 0.24849 0.36262 0.06617  0.04481  -0.10015 133 LYS   D CD    
2510 C  CE    . LYS   B 134 ? 0.49035 0.29875 0.40279 0.04585  0.03016  -0.10825 133 LYS   D CE    
2511 N  NZ    . LYS   B 134 ? 0.54935 0.33601 0.42563 0.03527  0.02556  -0.10018 133 LYS   D NZ    
2512 N  N     . GLU   B 135 ? 0.19117 0.13676 0.28436 0.04427  0.08525  -0.00561 134 GLU   D N     
2513 C  CA    . GLU   B 135 ? 0.21381 0.15948 0.30061 0.02925  0.09485  -0.00460 134 GLU   D CA    
2514 C  C     . GLU   B 135 ? 0.16682 0.15086 0.28713 0.03408  0.08939  0.01880  134 GLU   D C     
2515 O  O     . GLU   B 135 ? 0.17049 0.14660 0.26578 0.02415  0.06602  0.02311  134 GLU   D O     
2516 C  CB    . GLU   B 135 ? 0.33547 0.22197 0.35317 0.02319  0.10740  -0.03278 134 GLU   D CB    
2517 C  CG    . GLU   B 135 ? 0.44657 0.30298 0.40449 0.05181  0.13941  -0.05676 134 GLU   D CG    
2518 C  CD    . GLU   B 135 ? 0.56335 0.37386 0.44879 0.04896  0.13363  -0.05390 134 GLU   D CD    
2519 O  OE1   . GLU   B 135 ? 0.64052 0.39191 0.47397 0.04779  0.14454  -0.04741 134 GLU   D OE1   
2520 O  OE2   . GLU   B 135 ? 0.57878 0.38451 0.45210 0.07482  0.12146  -0.06917 134 GLU   D OE2   
2521 N  N     . GLY   B 136 ? 0.16433 0.17228 0.30101 0.04012  0.08728  0.03177  135 GLY   D N     
2522 C  CA    . GLY   B 136 ? 0.16938 0.16072 0.30823 0.03936  0.09157  0.04517  135 GLY   D CA    
2523 C  C     . GLY   B 136 ? 0.15586 0.15813 0.30671 0.03182  0.09760  0.04608  135 GLY   D C     
2524 O  O     . GLY   B 136 ? 0.15380 0.14783 0.31644 0.02924  0.10466  0.04214  135 GLY   D O     
2525 N  N     . MET   B 137 ? 0.15240 0.17052 0.29404 0.04246  0.09827  0.04623  136 MET   D N     
2526 C  CA    . MET   B 137 ? 0.15093 0.18798 0.28402 0.06156  0.08656  0.05818  136 MET   D CA    
2527 C  C     . MET   B 137 ? 0.15657 0.17977 0.27839 0.06193  0.09737  0.06183  136 MET   D C     
2528 O  O     . MET   B 137 ? 0.18099 0.17993 0.29212 0.07230  0.09591  0.05012  136 MET   D O     
2529 C  CB    . MET   B 137 ? 0.19323 0.20275 0.27330 0.05671  0.09076  0.04720  136 MET   D CB    
2530 C  CG    . MET   B 137 ? 0.19706 0.21743 0.26596 0.03400  0.08702  0.02342  136 MET   D CG    
2531 S  SD    . MET   B 137 ? 0.19901 0.17408 0.26120 0.01042  0.08902  0.00250  136 MET   D SD    
2532 C  CE    . MET   B 137 ? 0.23416 0.16728 0.24940 0.05236  0.06969  0.02528  136 MET   D CE    
2533 N  N     . ASN   B 138 ? 0.17140 0.18213 0.27697 0.07178  0.09777  0.04944  137 ASN   D N     
2534 C  CA    . ASN   B 138 ? 0.18009 0.16639 0.27228 0.05376  0.10241  0.03810  137 ASN   D CA    
2535 C  C     . ASN   B 138 ? 0.18875 0.15557 0.26319 0.04149  0.10376  0.03107  137 ASN   D C     
2536 O  O     . ASN   B 138 ? 0.16165 0.14936 0.26542 0.03650  0.09075  0.02387  137 ASN   D O     
2537 C  CB    . ASN   B 138 ? 0.20735 0.18454 0.28585 0.05722  0.12796  0.03691  137 ASN   D CB    
2538 C  CG    . ASN   B 138 ? 0.22531 0.22404 0.28444 0.05323  0.14402  0.04910  137 ASN   D CG    
2539 O  OD1   . ASN   B 138 ? 0.20374 0.24636 0.26984 0.06724  0.11354  0.04079  137 ASN   D OD1   
2540 N  ND2   . ASN   B 138 ? 0.30089 0.25412 0.30188 0.06666  0.17429  0.06064  137 ASN   D ND2   
2541 N  N     . ILE   B 139 ? 0.18259 0.14689 0.24884 0.04483  0.10826  0.03126  138 ILE   D N     
2542 C  CA    . ILE   B 139 ? 0.16886 0.14985 0.22259 0.04149  0.10510  0.01331  138 ILE   D CA    
2543 C  C     . ILE   B 139 ? 0.14624 0.13837 0.20904 0.02338  0.07607  0.01404  138 ILE   D C     
2544 O  O     . ILE   B 139 ? 0.15739 0.12341 0.21922 0.01715  0.06592  0.00843  138 ILE   D O     
2545 C  CB    . ILE   B 139 ? 0.20412 0.16102 0.21969 0.03784  0.11029  0.01825  138 ILE   D CB    
2546 C  CG1   . ILE   B 139 ? 0.23627 0.17759 0.22751 0.02415  0.12708  0.01549  138 ILE   D CG1   
2547 C  CG2   . ILE   B 139 ? 0.23086 0.16647 0.21310 0.05274  0.08408  0.04193  138 ILE   D CG2   
2548 C  CD1   . ILE   B 139 ? 0.27730 0.20771 0.23324 0.03670  0.13661  0.01012  138 ILE   D CD1   
2549 N  N     . VAL   B 140 ? 0.16489 0.13663 0.18791 0.02739  0.08319  0.01425  139 VAL   D N     
2550 C  CA    . VAL   B 140 ? 0.15710 0.13764 0.17968 0.01316  0.07584  0.00916  139 VAL   D CA    
2551 C  C     . VAL   B 140 ? 0.13709 0.15054 0.19821 0.01219  0.05506  0.01008  139 VAL   D C     
2552 O  O     . VAL   B 140 ? 0.15702 0.14801 0.18214 0.03234  0.04912  -0.00819 139 VAL   D O     
2553 C  CB    . VAL   B 140 ? 0.17567 0.16035 0.17702 0.02197  0.06777  0.00115  139 VAL   D CB    
2554 C  CG1   . VAL   B 140 ? 0.20255 0.18017 0.16584 0.01713  0.06081  -0.00547 139 VAL   D CG1   
2555 C  CG2   . VAL   B 140 ? 0.18644 0.15785 0.18863 0.01593  0.05881  -0.00051 139 VAL   D CG2   
2556 N  N     . GLU   B 141 ? 0.12705 0.18971 0.21854 0.01631  0.05198  0.01109  140 GLU   D N     
2557 C  CA    . GLU   B 141 ? 0.12068 0.19904 0.22673 0.03049  0.04219  0.01155  140 GLU   D CA    
2558 C  C     . GLU   B 141 ? 0.12183 0.19030 0.22147 0.02872  0.05328  -0.00442 140 GLU   D C     
2559 O  O     . GLU   B 141 ? 0.15280 0.18380 0.22188 0.02542  0.05143  -0.01496 140 GLU   D O     
2560 C  CB    . GLU   B 141 ? 0.13959 0.24522 0.25674 0.05130  0.04933  0.04224  140 GLU   D CB    
2561 C  CG    . GLU   B 141 ? 0.18681 0.31046 0.30263 0.08620  0.05650  0.08197  140 GLU   D CG    
2562 C  CD    . GLU   B 141 ? 0.25566 0.38639 0.34505 0.11370  0.10621  0.11188  140 GLU   D CD    
2563 O  OE1   . GLU   B 141 ? 0.24468 0.43553 0.37466 0.11627  0.10742  0.10377  140 GLU   D OE1   
2564 O  OE2   . GLU   B 141 ? 0.30616 0.39925 0.35969 0.14423  0.12144  0.13386  140 GLU   D OE2   
2565 N  N     . ALA   B 142 ? 0.13095 0.17325 0.20816 0.03180  0.07068  0.00411  141 ALA   D N     
2566 C  CA    . ALA   B 142 ? 0.15964 0.17228 0.19883 0.01859  0.07733  -0.00123 141 ALA   D CA    
2567 C  C     . ALA   B 142 ? 0.17137 0.15436 0.19747 0.02134  0.08212  0.00466  141 ALA   D C     
2568 O  O     . ALA   B 142 ? 0.18204 0.14866 0.19527 0.01728  0.05729  0.00352  141 ALA   D O     
2569 C  CB    . ALA   B 142 ? 0.16475 0.17425 0.20295 0.01725  0.06865  0.00432  141 ALA   D CB    
2570 N  N     . MET   B 143 ? 0.13827 0.16758 0.20033 0.02245  0.08092  -0.00029 142 MET   D N     
2571 C  CA    . MET   B 143 ? 0.15562 0.17122 0.19514 0.02975  0.08037  0.02196  142 MET   D CA    
2572 C  C     . MET   B 143 ? 0.16826 0.18642 0.18900 0.05677  0.07874  0.01499  142 MET   D C     
2573 O  O     . MET   B 143 ? 0.13140 0.16565 0.19475 0.04077  0.05812  0.00475  142 MET   D O     
2574 C  CB    . MET   B 143 ? 0.15040 0.18517 0.19603 0.04368  0.07232  0.03280  142 MET   D CB    
2575 C  CG    . MET   B 143 ? 0.17781 0.18032 0.20688 0.02177  0.05874  0.02695  142 MET   D CG    
2576 S  SD    . MET   B 143 ? 0.17879 0.18206 0.20692 0.00059  0.04588  0.03251  142 MET   D SD    
2577 C  CE    . MET   B 143 ? 0.14869 0.23394 0.20799 0.04736  0.03452  0.04876  142 MET   D CE    
2578 N  N     . GLU   B 144 ? 0.21111 0.24380 0.19006 0.10357  0.07513  0.02801  143 GLU   D N     
2579 C  CA    . GLU   B 144 ? 0.20810 0.28705 0.19506 0.12908  0.06110  0.02825  143 GLU   D CA    
2580 C  C     . GLU   B 144 ? 0.21973 0.32714 0.19184 0.13300  0.02113  0.01976  143 GLU   D C     
2581 O  O     . GLU   B 144 ? 0.26329 0.33402 0.18072 0.14341  0.02776  0.00648  143 GLU   D O     
2582 C  CB    . GLU   B 144 ? 0.23801 0.31369 0.22468 0.11656  0.05010  0.05043  143 GLU   D CB    
2583 C  CG    . GLU   B 144 ? 0.25602 0.27114 0.24664 0.07937  0.05695  0.06091  143 GLU   D CG    
2584 C  CD    . GLU   B 144 ? 0.28826 0.24144 0.24708 0.08871  0.09166  0.05124  143 GLU   D CD    
2585 O  OE1   . GLU   B 144 ? 0.29451 0.27193 0.26436 0.07452  0.08678  0.04398  143 GLU   D OE1   
2586 O  OE2   . GLU   B 144 ? 0.35262 0.20294 0.24061 0.04441  0.10396  0.01047  143 GLU   D OE2   
2587 N  N     . ARG   B 145 ? 0.17448 0.32816 0.21394 0.10368  0.02394  -0.00907 144 ARG   D N     
2588 C  CA    . ARG   B 145 ? 0.21807 0.32976 0.25642 0.05785  0.03915  -0.04591 144 ARG   D CA    
2589 C  C     . ARG   B 145 ? 0.17430 0.27293 0.22715 0.01956  0.03253  -0.05809 144 ARG   D C     
2590 O  O     . ARG   B 145 ? 0.20237 0.29579 0.25784 -0.01222 0.00746  -0.09070 144 ARG   D O     
2591 C  CB    . ARG   B 145 ? 0.29382 0.36543 0.33211 0.05570  0.05870  -0.05040 144 ARG   D CB    
2592 C  CG    . ARG   B 145 ? 0.47525 0.39724 0.39027 0.01288  0.08689  -0.03149 144 ARG   D CG    
2593 C  CD    . ARG   B 145 ? 0.63196 0.41518 0.43528 -0.03161 0.10529  -0.00361 144 ARG   D CD    
2594 N  NE    . ARG   B 145 ? 0.75067 0.42122 0.46853 -0.07028 0.11794  0.01815  144 ARG   D NE    
2595 C  CZ    . ARG   B 145 ? 0.82843 0.41850 0.48917 -0.10374 0.12246  0.02748  144 ARG   D CZ    
2596 N  NH1   . ARG   B 145 ? 0.80613 0.40481 0.48533 -0.12308 0.10015  0.02555  144 ARG   D NH1   
2597 N  NH2   . ARG   B 145 ? 0.87154 0.43425 0.50343 -0.10243 0.12620  0.02958  144 ARG   D NH2   
2598 N  N     . PHE   B 146 ? 0.13269 0.21341 0.16169 0.01686  0.04837  -0.03206 145 PHE   D N     
2599 C  CA    . PHE   B 146 ? 0.14180 0.17602 0.13494 0.00680  0.04856  -0.01616 145 PHE   D CA    
2600 C  C     . PHE   B 146 ? 0.14472 0.14141 0.13755 0.00962  0.06139  -0.00375 145 PHE   D C     
2601 O  O     . PHE   B 146 ? 0.17029 0.15791 0.15315 0.03932  0.06907  0.02033  145 PHE   D O     
2602 C  CB    . PHE   B 146 ? 0.16467 0.19211 0.12237 0.02879  0.04918  -0.01103 145 PHE   D CB    
2603 C  CG    . PHE   B 146 ? 0.14098 0.19359 0.12286 0.01944  0.04468  -0.01565 145 PHE   D CG    
2604 C  CD1   . PHE   B 146 ? 0.18650 0.21259 0.13507 0.01718  0.04995  0.01529  145 PHE   D CD1   
2605 C  CD2   . PHE   B 146 ? 0.17284 0.21236 0.13799 0.04977  0.04152  -0.01487 145 PHE   D CD2   
2606 C  CE1   . PHE   B 146 ? 0.23890 0.23155 0.13573 0.03312  0.06704  0.01775  145 PHE   D CE1   
2607 C  CE2   . PHE   B 146 ? 0.20987 0.22374 0.14002 0.05298  0.05010  0.00094  145 PHE   D CE2   
2608 C  CZ    . PHE   B 146 ? 0.23028 0.23981 0.13896 0.05248  0.04398  0.01074  145 PHE   D CZ    
2609 N  N     . GLY   B 147 ? 0.14414 0.14377 0.11187 0.00427  0.03992  -0.02420 146 GLY   D N     
2610 C  CA    . GLY   B 147 ? 0.16128 0.13361 0.09525 -0.01088 0.04318  -0.02859 146 GLY   D CA    
2611 C  C     . GLY   B 147 ? 0.14671 0.12075 0.11271 0.00989  0.04139  -0.00468 146 GLY   D C     
2612 O  O     . GLY   B 147 ? 0.17630 0.14127 0.13772 -0.03024 0.06955  -0.01940 146 GLY   D O     
2613 N  N     . SER   B 148 ? 0.14124 0.10537 0.11057 0.00012  0.03773  -0.01107 147 SER   D N     
2614 C  CA    . SER   B 148 ? 0.16794 0.11177 0.11276 -0.00384 0.04535  -0.02398 147 SER   D CA    
2615 C  C     . SER   B 148 ? 0.16373 0.11787 0.10994 -0.00184 0.03727  -0.01437 147 SER   D C     
2616 O  O     . SER   B 148 ? 0.15718 0.10970 0.12468 0.00462  0.04374  -0.01361 147 SER   D O     
2617 C  CB    . SER   B 148 ? 0.15750 0.11293 0.14059 0.00118  0.04404  -0.01633 147 SER   D CB    
2618 O  OG    . SER   B 148 ? 0.17375 0.11976 0.13678 -0.00171 0.04208  -0.00095 147 SER   D OG    
2619 N  N     . ARG   B 149 ? 0.17401 0.13548 0.11558 0.01134  0.02825  -0.01680 148 ARG   D N     
2620 C  CA    . ARG   B 149 ? 0.21228 0.15110 0.12237 -0.00976 0.03911  -0.02650 148 ARG   D CA    
2621 C  C     . ARG   B 149 ? 0.18977 0.12545 0.11626 -0.00602 0.03922  -0.02111 148 ARG   D C     
2622 O  O     . ARG   B 149 ? 0.20847 0.13151 0.12724 -0.00194 0.03370  -0.02067 148 ARG   D O     
2623 C  CB    . ARG   B 149 ? 0.22892 0.18906 0.13108 -0.03752 0.00549  -0.02197 148 ARG   D CB    
2624 C  CG    . ARG   B 149 ? 0.21598 0.19094 0.14927 -0.00249 -0.00311 0.00253  148 ARG   D CG    
2625 C  CD    . ARG   B 149 ? 0.21972 0.22380 0.15850 -0.02797 -0.00146 0.00164  148 ARG   D CD    
2626 N  NE    . ARG   B 149 ? 0.23231 0.23002 0.16034 -0.04968 0.01190  -0.00630 148 ARG   D NE    
2627 C  CZ    . ARG   B 149 ? 0.30349 0.22524 0.15071 -0.09698 0.00178  -0.02381 148 ARG   D CZ    
2628 N  NH1   . ARG   B 149 ? 0.32360 0.24221 0.15671 -0.11992 -0.00774 -0.03769 148 ARG   D NH1   
2629 N  NH2   . ARG   B 149 ? 0.32987 0.24461 0.15508 -0.10396 0.01763  -0.03901 148 ARG   D NH2   
2630 N  N     . ASN   B 150 ? 0.16090 0.13159 0.12715 0.01845  0.05470  -0.02115 149 ASN   D N     
2631 C  CA    . ASN   B 150 ? 0.18241 0.12148 0.12443 0.02531  0.05586  -0.00666 149 ASN   D CA    
2632 C  C     . ASN   B 150 ? 0.16675 0.11441 0.13074 0.00347  0.05060  0.00611  149 ASN   D C     
2633 O  O     . ASN   B 150 ? 0.16413 0.14754 0.15149 0.00879  0.04913  -0.00234 149 ASN   D O     
2634 C  CB    . ASN   B 150 ? 0.20710 0.11370 0.14219 0.02818  0.07045  -0.00022 149 ASN   D CB    
2635 C  CG    . ASN   B 150 ? 0.21486 0.10834 0.15057 0.01280  0.08042  -0.00428 149 ASN   D CG    
2636 O  OD1   . ASN   B 150 ? 0.20859 0.11464 0.15771 0.01152  0.09963  -0.00225 149 ASN   D OD1   
2637 N  ND2   . ASN   B 150 ? 0.22726 0.12411 0.16778 0.02551  0.09701  0.00329  149 ASN   D ND2   
2638 N  N     . GLY   B 151 ? 0.17547 0.09847 0.10985 0.00905  0.05130  -0.00861 150 GLY   D N     
2639 C  CA    . GLY   B 151 ? 0.16774 0.08770 0.11710 0.00774  0.04706  0.00921  150 GLY   D CA    
2640 C  C     . GLY   B 151 ? 0.12732 0.09761 0.13562 0.00564  0.03551  0.00970  150 GLY   D C     
2641 O  O     . GLY   B 151 ? 0.14552 0.09824 0.12626 0.00199  0.02516  0.01360  150 GLY   D O     
2642 N  N     . LYS   B 152 ? 0.16788 0.10330 0.14123 0.00811  0.05928  0.01612  151 LYS   D N     
2643 C  CA    . LYS   B 152 ? 0.18097 0.10262 0.15401 0.02592  0.05914  0.00857  151 LYS   D CA    
2644 C  C     . LYS   B 152 ? 0.16255 0.09892 0.13239 0.01085  0.03330  0.00159  151 LYS   D C     
2645 O  O     . LYS   B 152 ? 0.14999 0.14806 0.13726 0.00018  0.03718  -0.00468 151 LYS   D O     
2646 C  CB    . LYS   B 152 ? 0.25184 0.12969 0.16879 0.04159  0.06660  -0.00369 151 LYS   D CB    
2647 C  CG    . LYS   B 152 ? 0.34190 0.20087 0.21378 0.07680  0.05757  -0.03058 151 LYS   D CG    
2648 C  CD    . LYS   B 152 ? 0.43019 0.25790 0.24906 0.11557  0.07952  -0.06322 151 LYS   D CD    
2649 C  CE    . LYS   B 152 ? 0.51091 0.31137 0.29539 0.14777  0.08071  -0.08227 151 LYS   D CE    
2650 N  NZ    . LYS   B 152 ? 0.57904 0.34854 0.30926 0.14098  0.07655  -0.09429 151 LYS   D NZ    
2651 N  N     . THR   B 153 ? 0.15645 0.11629 0.12847 0.01406  0.03671  -0.00252 152 THR   D N     
2652 C  CA    . THR   B 153 ? 0.16413 0.11637 0.13335 0.00471  0.02409  0.00130  152 THR   D CA    
2653 C  C     . THR   B 153 ? 0.15370 0.13279 0.13919 0.00743  0.01322  0.01050  152 THR   D C     
2654 O  O     . THR   B 153 ? 0.19895 0.13000 0.15510 0.01508  0.03025  0.03133  152 THR   D O     
2655 C  CB    . THR   B 153 ? 0.16502 0.11708 0.13414 -0.00252 0.00145  0.01316  152 THR   D CB    
2656 O  OG1   . THR   B 153 ? 0.18095 0.11171 0.13605 0.01127  0.00923  0.00925  152 THR   D OG1   
2657 C  CG2   . THR   B 153 ? 0.19485 0.12430 0.13748 0.00888  0.01619  0.01363  152 THR   D CG2   
2658 N  N     . SER   B 154 ? 0.17591 0.13855 0.11834 -0.00995 0.03524  0.00845  153 SER   D N     
2659 C  CA    . SER   B 154 ? 0.18529 0.13873 0.13785 -0.02230 0.02779  0.00819  153 SER   D CA    
2660 C  C     . SER   B 154 ? 0.19343 0.13009 0.13351 -0.02443 0.03179  0.02010  153 SER   D C     
2661 O  O     . SER   B 154 ? 0.21297 0.14286 0.14868 -0.02560 0.03620  0.02159  153 SER   D O     
2662 C  CB    . SER   B 154 ? 0.20817 0.15887 0.17333 -0.03386 0.02832  -0.00441 153 SER   D CB    
2663 O  OG    . SER   B 154 ? 0.20059 0.18246 0.19405 -0.03623 0.02468  0.01104  153 SER   D OG    
2664 N  N     . LYS   B 155 ? 0.17557 0.12588 0.12390 -0.00397 0.02627  -0.00210 154 LYS   D N     
2665 C  CA    . LYS   B 155 ? 0.16053 0.12347 0.12397 -0.01904 0.03745  0.01366  154 LYS   D CA    
2666 C  C     . LYS   B 155 ? 0.18351 0.11565 0.12053 -0.00899 0.04125  0.01166  154 LYS   D C     
2667 O  O     . LYS   B 155 ? 0.20011 0.12810 0.11787 -0.02528 0.04005  0.02405  154 LYS   D O     
2668 C  CB    . LYS   B 155 ? 0.16614 0.14833 0.16378 -0.01658 0.03580  0.00999  154 LYS   D CB    
2669 C  CG    . LYS   B 155 ? 0.16201 0.16091 0.19876 -0.02196 0.05002  0.01611  154 LYS   D CG    
2670 C  CD    . LYS   B 155 ? 0.18154 0.20581 0.23448 -0.02952 0.06607  0.00934  154 LYS   D CD    
2671 C  CE    . LYS   B 155 ? 0.17545 0.26356 0.27060 -0.00987 0.06996  0.00251  154 LYS   D CE    
2672 N  NZ    . LYS   B 155 ? 0.23137 0.30742 0.28682 -0.02647 0.08643  0.01137  154 LYS   D NZ    
2673 N  N     . LYS   B 156 ? 0.14499 0.11213 0.13847 0.00403  0.04033  0.01045  155 LYS   D N     
2674 C  CA    . LYS   B 156 ? 0.14496 0.12161 0.15415 -0.00670 0.02996  0.00366  155 LYS   D CA    
2675 C  C     . LYS   B 156 ? 0.13883 0.11753 0.11500 -0.00866 0.04159  0.01380  155 LYS   D C     
2676 O  O     . LYS   B 156 ? 0.16375 0.11921 0.11429 0.00185  0.03209  0.02879  155 LYS   D O     
2677 C  CB    . LYS   B 156 ? 0.16063 0.12068 0.18955 -0.01873 0.00312  0.02067  155 LYS   D CB    
2678 C  CG    . LYS   B 156 ? 0.20284 0.13553 0.21869 -0.01342 -0.01164 0.02720  155 LYS   D CG    
2679 C  CD    . LYS   B 156 ? 0.22098 0.17484 0.23377 -0.02187 -0.00867 0.04205  155 LYS   D CD    
2680 C  CE    . LYS   B 156 ? 0.22307 0.16596 0.24989 -0.03420 -0.03058 0.05508  155 LYS   D CE    
2681 N  NZ    . LYS   B 156 ? 0.27082 0.17685 0.25238 -0.03510 -0.02999 0.09548  155 LYS   D NZ    
2682 N  N     . ILE   B 157 ? 0.13640 0.11329 0.12835 0.00065  0.03928  0.01282  156 ILE   D N     
2683 C  CA    . ILE   B 157 ? 0.13344 0.11762 0.12625 -0.00073 0.03496  0.00377  156 ILE   D CA    
2684 C  C     . ILE   B 157 ? 0.14868 0.11919 0.11106 0.00819  0.04151  0.01040  156 ILE   D C     
2685 O  O     . ILE   B 157 ? 0.16035 0.15013 0.10058 -0.02355 0.04352  0.00584  156 ILE   D O     
2686 C  CB    . ILE   B 157 ? 0.14916 0.13809 0.12690 0.00173  0.02677  0.02880  156 ILE   D CB    
2687 C  CG1   . ILE   B 157 ? 0.15056 0.17468 0.12866 -0.02275 0.01958  0.00658  156 ILE   D CG1   
2688 C  CG2   . ILE   B 157 ? 0.18402 0.15264 0.13658 0.04262  0.04090  0.03449  156 ILE   D CG2   
2689 C  CD1   . ILE   B 157 ? 0.17202 0.20092 0.13642 -0.02105 0.04308  0.00323  156 ILE   D CD1   
2690 N  N     . THR   B 158 ? 0.16192 0.09938 0.11783 -0.00579 0.03583  0.00132  157 THR   D N     
2691 C  CA    . THR   B 158 ? 0.16505 0.10152 0.12189 0.00728  0.03491  0.00311  157 THR   D CA    
2692 C  C     . THR   B 158 ? 0.16068 0.10231 0.10668 0.00196  0.05471  0.01023  157 THR   D C     
2693 O  O     . THR   B 158 ? 0.19745 0.10680 0.12353 0.00623  0.05946  0.01561  157 THR   D O     
2694 C  CB    . THR   B 158 ? 0.21079 0.12883 0.14318 0.01139  0.04105  0.02335  157 THR   D CB    
2695 O  OG1   . THR   B 158 ? 0.20275 0.12274 0.14383 -0.00166 0.03409  0.02374  157 THR   D OG1   
2696 C  CG2   . THR   B 158 ? 0.23077 0.13746 0.16666 0.03184  0.03589  0.02325  157 THR   D CG2   
2697 N  N     . ILE   B 159 ? 0.18722 0.09321 0.08582 -0.00683 0.03238  0.00136  158 ILE   D N     
2698 C  CA    . ILE   B 159 ? 0.21393 0.09749 0.07855 -0.00594 0.03988  0.00460  158 ILE   D CA    
2699 C  C     . ILE   B 159 ? 0.21900 0.10972 0.09627 0.00167  0.03408  0.00333  158 ILE   D C     
2700 O  O     . ILE   B 159 ? 0.22239 0.16378 0.09936 0.00876  0.01666  0.00099  158 ILE   D O     
2701 C  CB    . ILE   B 159 ? 0.20733 0.10683 0.08103 -0.01594 0.02965  -0.00279 158 ILE   D CB    
2702 C  CG1   . ILE   B 159 ? 0.19948 0.11855 0.10176 0.00610  0.03879  -0.00252 158 ILE   D CG1   
2703 C  CG2   . ILE   B 159 ? 0.22350 0.12447 0.09920 0.00272  0.02854  -0.02703 158 ILE   D CG2   
2704 C  CD1   . ILE   B 159 ? 0.16923 0.11030 0.11675 -0.00208 0.02701  0.00915  158 ILE   D CD1   
2705 N  N     . ALA   B 160 ? 0.24250 0.11459 0.09287 -0.00730 0.05163  0.00496  159 ALA   D N     
2706 C  CA    . ALA   B 160 ? 0.29835 0.12364 0.09284 -0.01748 0.04933  0.00964  159 ALA   D CA    
2707 C  C     . ALA   B 160 ? 0.30612 0.13806 0.08902 -0.00626 0.04086  0.01283  159 ALA   D C     
2708 O  O     . ALA   B 160 ? 0.30381 0.14411 0.09980 0.00215  0.03447  0.00975  159 ALA   D O     
2709 C  CB    . ALA   B 160 ? 0.29780 0.13607 0.10120 -0.03750 0.06031  0.00380  159 ALA   D CB    
2710 N  N     . ASP   B 161 ? 0.28951 0.10755 0.09323 -0.01419 0.04088  -0.00092 160 ASP   D N     
2711 C  CA    . ASP   B 161 ? 0.31909 0.12884 0.09413 -0.00479 0.04578  -0.01316 160 ASP   D CA    
2712 C  C     . ASP   B 161 ? 0.29736 0.11053 0.08877 0.00581  0.04555  -0.00820 160 ASP   D C     
2713 O  O     . ASP   B 161 ? 0.29816 0.11486 0.09161 0.00548  0.04740  -0.00577 160 ASP   D O     
2714 C  CB    . ASP   B 161 ? 0.34065 0.15415 0.11311 -0.00324 0.06494  -0.02171 160 ASP   D CB    
2715 C  CG    . ASP   B 161 ? 0.32833 0.17229 0.14105 0.03038  0.08879  -0.02408 160 ASP   D CG    
2716 O  OD1   . ASP   B 161 ? 0.30524 0.18848 0.12017 0.02611  0.04401  -0.01040 160 ASP   D OD1   
2717 O  OD2   . ASP   B 161 ? 0.35510 0.20430 0.19110 -0.01066 0.11275  -0.05281 160 ASP   D OD2   
2718 N  N     . CYS   B 162 ? 0.25408 0.11973 0.08275 -0.00125 0.04767  -0.01113 161 CYS   D N     
2719 C  CA    . CYS   B 162 ? 0.23573 0.11689 0.08378 -0.00594 0.04636  -0.00731 161 CYS   D CA    
2720 C  C     . CYS   B 162 ? 0.22515 0.10716 0.09744 0.00500  0.03242  -0.01254 161 CYS   D C     
2721 O  O     . CYS   B 162 ? 0.25179 0.12585 0.10024 0.00326  0.01772  -0.01554 161 CYS   D O     
2722 C  CB    . CYS   B 162 ? 0.19867 0.11990 0.08376 0.02976  0.03524  -0.00357 161 CYS   D CB    
2723 S  SG    . CYS   B 162 ? 0.20319 0.11644 0.09773 0.00921  0.02920  -0.00368 161 CYS   D SG    
2724 N  N     . GLY   B 163 ? 0.23259 0.09653 0.11334 0.01768  0.03813  -0.01673 162 GLY   D N     
2725 C  CA    . GLY   B 163 ? 0.26543 0.10242 0.10965 0.00603  0.02373  -0.00901 162 GLY   D CA    
2726 C  C     . GLY   B 163 ? 0.21757 0.11443 0.12337 0.00152  0.03848  -0.01057 162 GLY   D C     
2727 O  O     . GLY   B 163 ? 0.21854 0.11876 0.12312 0.01550  0.02005  -0.01869 162 GLY   D O     
2728 N  N     . GLN   B 164 ? 0.21865 0.10399 0.12880 0.00270  0.02846  -0.01488 163 GLN   D N     
2729 C  CA    . GLN   B 164 ? 0.23288 0.10813 0.12405 0.01389  0.02282  -0.00674 163 GLN   D CA    
2730 C  C     . GLN   B 164 ? 0.25071 0.12154 0.11801 0.01538  0.04088  -0.01209 163 GLN   D C     
2731 O  O     . GLN   B 164 ? 0.32850 0.15212 0.11634 0.05791  0.04471  -0.02103 163 GLN   D O     
2732 C  CB    . GLN   B 164 ? 0.25292 0.13298 0.12235 -0.02403 0.01312  -0.00386 163 GLN   D CB    
2733 C  CG    . GLN   B 164 ? 0.24591 0.14344 0.13108 -0.01289 0.01002  -0.01548 163 GLN   D CG    
2734 C  CD    . GLN   B 164 ? 0.24586 0.17466 0.12629 -0.01821 0.03277  -0.02337 163 GLN   D CD    
2735 O  OE1   . GLN   B 164 ? 0.28086 0.15619 0.12262 -0.02342 0.04357  -0.00755 163 GLN   D OE1   
2736 N  NE2   . GLN   B 164 ? 0.25870 0.20118 0.10545 -0.02114 0.03258  -0.03483 163 GLN   D NE2   
2737 N  N     . LEU   B 165 ? 0.23190 0.13515 0.14130 0.03834  0.05083  -0.00395 164 LEU   D N     
2738 C  CA    . LEU   B 165 ? 0.26647 0.13515 0.17361 0.02957  0.05848  -0.02805 164 LEU   D CA    
2739 C  C     . LEU   B 165 ? 0.29125 0.13334 0.20228 0.03660  0.03677  -0.06223 164 LEU   D C     
2740 O  O     . LEU   B 165 ? 0.30513 0.13259 0.22245 0.01279  0.05407  -0.04367 164 LEU   D O     
2741 C  CB    . LEU   B 165 ? 0.28575 0.13139 0.21808 0.02723  0.07242  -0.01793 164 LEU   D CB    
2742 C  CG    . LEU   B 165 ? 0.30237 0.14087 0.25197 0.04276  0.09582  0.00075  164 LEU   D CG    
2743 C  CD1   . LEU   B 165 ? 0.32478 0.14812 0.27708 0.01713  0.08171  -0.01326 164 LEU   D CD1   
2744 C  CD2   . LEU   B 165 ? 0.32236 0.16327 0.25813 0.02813  0.12080  0.03839  164 LEU   D CD2   
2745 N  N     . GLU   B 166 ? 0.38547 0.13543 0.24898 0.02142  0.01300  -0.07381 165 GLU   D N     
2746 C  CA    . GLU   B 166 ? 0.52573 0.16868 0.29602 -0.00656 -0.01662 -0.07040 165 GLU   D CA    
2747 C  C     . GLU   B 166 ? 0.59650 0.18271 0.28843 -0.05633 -0.03139 -0.05302 165 GLU   D C     
2748 O  O     . GLU   B 166 ? 0.61902 0.19660 0.28185 -0.07208 -0.04474 -0.04924 165 GLU   D O     
2749 C  CB    . GLU   B 166 ? 0.58514 0.22056 0.36090 -0.00082 -0.04576 -0.05055 165 GLU   D CB    
2750 C  CG    . GLU   B 166 ? 0.65304 0.28214 0.41308 -0.00915 -0.06273 -0.03699 165 GLU   D CG    
2751 C  CD    . GLU   B 166 ? 0.71292 0.34255 0.45737 -0.01397 -0.05536 -0.03451 165 GLU   D CD    
2752 O  OE1   . GLU   B 166 ? 0.72761 0.37395 0.47437 0.00028  -0.05559 -0.01951 165 GLU   D OE1   
2753 O  OE2   . GLU   B 166 ? 0.72558 0.35897 0.47349 -0.02441 -0.04871 -0.04320 165 GLU   D OE2   
2754 O  OXT   . GLU   B 166 ? 0.65019 0.19175 0.28865 -0.06828 -0.03927 -0.03869 165 GLU   D OXT   
2755 P  PG    . GNP   C .   ? 0.11265 0.09945 0.09190 0.00494  0.02812  -0.01735 201 GNP   A PG    
2756 O  O1G   . GNP   C .   ? 0.11210 0.10515 0.15811 -0.00099 0.03995  -0.00428 201 GNP   A O1G   
2757 O  O2G   . GNP   C .   ? 0.20349 0.13072 0.09533 0.06984  0.03733  -0.00904 201 GNP   A O2G   
2758 O  O3G   . GNP   C .   ? 0.13153 0.10949 0.13040 0.00436  0.02648  -0.05593 201 GNP   A O3G   
2759 N  N3B   . GNP   C .   ? 0.10594 0.10036 0.10736 -0.00573 0.03848  -0.02635 201 GNP   A N3B   
2760 P  PB    . GNP   C .   ? 0.10355 0.09282 0.08117 0.00410  0.02322  -0.01226 201 GNP   A PB    
2761 O  O1B   . GNP   C .   ? 0.10093 0.10146 0.08487 0.00850  0.01704  -0.00865 201 GNP   A O1B   
2762 O  O2B   . GNP   C .   ? 0.10692 0.09292 0.08178 0.01027  0.02821  -0.00807 201 GNP   A O2B   
2763 O  O3A   . GNP   C .   ? 0.10239 0.11195 0.08497 0.00391  0.01855  -0.00646 201 GNP   A O3A   
2764 P  PA    . GNP   C .   ? 0.10976 0.11139 0.07940 0.00696  0.01847  -0.01202 201 GNP   A PA    
2765 O  O1A   . GNP   C .   ? 0.12746 0.10061 0.10626 0.00663  0.00747  -0.01245 201 GNP   A O1A   
2766 O  O2A   . GNP   C .   ? 0.11962 0.13462 0.07525 0.01022  0.01975  -0.01703 201 GNP   A O2A   
2767 O  "O5'" . GNP   C .   ? 0.11772 0.10019 0.10091 0.00237  0.01666  -0.01764 201 GNP   A "O5'" 
2768 C  "C5'" . GNP   C .   ? 0.12229 0.11591 0.11176 0.01087  0.00668  -0.01191 201 GNP   A "C5'" 
2769 C  "C4'" . GNP   C .   ? 0.12239 0.14699 0.09600 0.00617  0.00671  -0.00977 201 GNP   A "C4'" 
2770 O  "O4'" . GNP   C .   ? 0.11306 0.11426 0.10074 0.00596  0.01664  -0.01023 201 GNP   A "O4'" 
2771 C  "C3'" . GNP   C .   ? 0.13727 0.14196 0.10388 0.00063  -0.00421 -0.00842 201 GNP   A "C3'" 
2772 O  "O3'" . GNP   C .   ? 0.16699 0.14450 0.10848 0.00086  -0.01630 -0.02197 201 GNP   A "O3'" 
2773 C  "C2'" . GNP   C .   ? 0.13601 0.12808 0.10958 0.01415  0.00430  0.00117  201 GNP   A "C2'" 
2774 O  "O2'" . GNP   C .   ? 0.15203 0.15441 0.10261 0.01243  -0.00320 -0.00362 201 GNP   A "O2'" 
2775 C  "C1'" . GNP   C .   ? 0.13129 0.11444 0.10260 -0.00244 0.00722  -0.00882 201 GNP   A "C1'" 
2776 N  N9    . GNP   C .   ? 0.11412 0.11058 0.09425 0.00624  0.00435  -0.00298 201 GNP   A N9    
2777 C  C8    . GNP   C .   ? 0.11896 0.10872 0.08774 0.00701  0.00295  -0.01012 201 GNP   A C8    
2778 N  N7    . GNP   C .   ? 0.10572 0.10922 0.08508 -0.00523 0.01373  -0.00043 201 GNP   A N7    
2779 C  C5    . GNP   C .   ? 0.11528 0.11430 0.07245 -0.00595 0.00731  -0.00007 201 GNP   A C5    
2780 C  C6    . GNP   C .   ? 0.11716 0.09846 0.09129 -0.00427 0.01354  0.00641  201 GNP   A C6    
2781 O  O6    . GNP   C .   ? 0.12276 0.10078 0.10852 -0.01444 0.00394  0.00331  201 GNP   A O6    
2782 N  N1    . GNP   C .   ? 0.11576 0.10643 0.09650 -0.00019 0.00435  0.00063  201 GNP   A N1    
2783 C  C2    . GNP   C .   ? 0.11246 0.12114 0.10690 0.00740  0.01527  0.00742  201 GNP   A C2    
2784 N  N2    . GNP   C .   ? 0.10495 0.15619 0.11724 0.00510  0.00174  -0.01300 201 GNP   A N2    
2785 N  N3    . GNP   C .   ? 0.11911 0.11215 0.10454 -0.00147 0.00602  0.00287  201 GNP   A N3    
2786 C  C4    . GNP   C .   ? 0.11345 0.12393 0.09392 -0.00888 0.00761  0.00759  201 GNP   A C4    
2787 MG MG    . MG    D .   ? 0.11014 0.09675 0.09507 0.00307  0.02354  -0.01080 202 MG    A MG    
2788 C  C1    . BTB   E .   ? 0.19803 0.24718 0.22218 -0.01497 0.01789  0.00717  203 BTB   A C1    
2789 O  O1    . BTB   E .   ? 0.19862 0.24499 0.20513 -0.01782 0.02987  0.03128  203 BTB   A O1    
2790 C  C2    . BTB   E .   ? 0.19253 0.24706 0.23650 0.01484  0.02074  0.01827  203 BTB   A C2    
2791 C  C3    . BTB   E .   ? 0.21078 0.23931 0.24589 0.02256  0.04117  0.02977  203 BTB   A C3    
2792 O  O3    . BTB   E .   ? 0.18853 0.23054 0.23406 -0.01058 0.02820  0.02747  203 BTB   A O3    
2793 C  C4    . BTB   E .   ? 0.19063 0.31045 0.29607 0.04084  0.01917  0.02044  203 BTB   A C4    
2794 O  O4    . BTB   E .   ? 0.25088 0.35168 0.35440 0.06907  0.04017  0.03286  203 BTB   A O4    
2795 N  N     . BTB   E .   ? 0.21781 0.19314 0.22821 0.00313  -0.01828 0.03017  203 BTB   A N     
2796 C  C5    . BTB   E .   ? 0.20520 0.19968 0.25286 -0.01706 -0.02918 0.02430  203 BTB   A C5    
2797 C  C6    . BTB   E .   ? 0.21775 0.20420 0.25780 -0.00441 -0.02296 0.01748  203 BTB   A C6    
2798 O  O6    . BTB   E .   ? 0.23061 0.20521 0.27191 -0.00811 -0.00906 0.00720  203 BTB   A O6    
2799 C  C7    . BTB   E .   ? 0.17871 0.20899 0.22743 0.00545  -0.00641 0.01970  203 BTB   A C7    
2800 C  C8    . BTB   E .   ? 0.17595 0.21846 0.21554 0.02852  -0.00361 -0.01798 203 BTB   A C8    
2801 O  O8    . BTB   E .   ? 0.18007 0.19914 0.21862 0.02046  0.00683  -0.00034 203 BTB   A O8    
2802 C  C1    . A1AOM F .   ? 0.10160 0.15560 0.14259 0.00236  0.00391  -0.00660 204 A1AOM A C1    
2803 C  C10   . A1AOM F .   ? 0.14347 0.11022 0.11463 0.00915  0.01731  -0.01638 204 A1AOM A C10   
2804 C  C11   . A1AOM F .   ? 0.11972 0.08915 0.10951 0.01744  0.02098  -0.01477 204 A1AOM A C11   
2805 C  C12   . A1AOM F .   ? 0.12714 0.10716 0.10404 0.01744  0.02810  -0.00436 204 A1AOM A C12   
2806 C  C13   . A1AOM F .   ? 0.11905 0.11287 0.13492 -0.01709 0.02974  -0.03763 204 A1AOM A C13   
2807 C  C14   . A1AOM F .   ? 0.11347 0.13274 0.12859 0.00543  0.02058  -0.02951 204 A1AOM A C14   
2808 C  C15   . A1AOM F .   ? 0.12215 0.12966 0.14967 0.00404  0.02516  -0.03358 204 A1AOM A C15   
2809 C  C16   . A1AOM F .   ? 0.12144 0.13282 0.12560 -0.01923 0.02864  -0.03461 204 A1AOM A C16   
2810 C  C17   . A1AOM F .   ? 0.11400 0.12127 0.10776 0.00340  0.02454  -0.02027 204 A1AOM A C17   
2811 C  C18   . A1AOM F .   ? 0.14266 0.09406 0.10428 0.00174  0.02836  -0.04225 204 A1AOM A C18   
2812 C  C19   . A1AOM F .   ? 0.14340 0.08882 0.09474 -0.00363 0.02035  -0.03547 204 A1AOM A C19   
2813 C  C2    . A1AOM F .   ? 0.11128 0.12087 0.11500 0.01426  0.01449  -0.01482 204 A1AOM A C2    
2814 C  C20   . A1AOM F .   ? 0.11165 0.10856 0.10788 0.00155  0.01626  -0.03608 204 A1AOM A C20   
2815 C  C21   . A1AOM F .   ? 0.13242 0.09245 0.09970 0.00230  0.01762  -0.02080 204 A1AOM A C21   
2816 C  C22   . A1AOM F .   ? 0.12788 0.09261 0.09732 0.00490  0.02520  -0.02756 204 A1AOM A C22   
2817 C  C23   . A1AOM F .   ? 0.11306 0.09457 0.10373 -0.00187 0.03389  -0.03639 204 A1AOM A C23   
2818 C  C24   . A1AOM F .   ? 0.10898 0.09578 0.10920 -0.00682 0.02833  -0.03017 204 A1AOM A C24   
2819 C  C25   . A1AOM F .   ? 0.10330 0.10678 0.09005 -0.00008 0.02922  -0.02542 204 A1AOM A C25   
2820 C  C26   . A1AOM F .   ? 0.11542 0.10182 0.10378 -0.01638 0.02244  -0.02141 204 A1AOM A C26   
2821 C  C27   . A1AOM F .   ? 0.10195 0.09379 0.10102 -0.00293 0.01486  -0.02978 204 A1AOM A C27   
2822 C  C28   . A1AOM F .   ? 0.10850 0.09138 0.10180 -0.01077 0.01107  -0.02503 204 A1AOM A C28   
2823 C  C29   . A1AOM F .   ? 0.11583 0.09432 0.09753 -0.00160 0.03066  -0.02508 204 A1AOM A C29   
2824 C  C3    . A1AOM F .   ? 0.14486 0.10915 0.10733 0.01132  0.01356  -0.01951 204 A1AOM A C3    
2825 C  C30   . A1AOM F .   ? 0.13361 0.08991 0.08498 -0.01206 0.03331  -0.02278 204 A1AOM A C30   
2826 C  C31   . A1AOM F .   ? 0.07745 0.11007 0.10630 0.00983  0.02433  -0.02301 204 A1AOM A C31   
2827 C  C32   . A1AOM F .   ? 0.09320 0.10438 0.11030 0.00900  0.01869  -0.02196 204 A1AOM A C32   
2828 C  C33   . A1AOM F .   ? 0.12536 0.09497 0.10829 0.01240  0.03461  -0.03950 204 A1AOM A C33   
2829 C  C34   . A1AOM F .   ? 0.15069 0.10313 0.13148 0.02017  0.02212  -0.00598 204 A1AOM A C34   
2830 C  C35   . A1AOM F .   ? 0.15266 0.11265 0.14080 0.01106  0.04838  -0.02653 204 A1AOM A C35   
2831 C  C36   . A1AOM F .   ? 0.18256 0.14383 0.17947 0.02713  0.06318  -0.03600 204 A1AOM A C36   
2832 C  C37   . A1AOM F .   ? 0.15319 0.19714 0.16422 0.03079  0.03856  -0.06464 204 A1AOM A C37   
2833 C  C38   . A1AOM F .   ? 0.16263 0.29838 0.21495 -0.00227 0.03890  -0.08993 204 A1AOM A C38   
2834 C  C39   . A1AOM F .   ? 0.22562 0.25251 0.20189 0.00160  0.03194  -0.07447 204 A1AOM A C39   
2835 C  C4    . A1AOM F .   ? 0.10407 0.11395 0.10871 0.01188  0.02167  -0.03035 204 A1AOM A C4    
2836 C  C40   . A1AOM F .   ? 0.16203 0.17507 0.21031 0.00351  0.07434  -0.05421 204 A1AOM A C40   
2837 C  C5    . A1AOM F .   ? 0.10722 0.10862 0.09144 0.00240  0.02693  -0.01718 204 A1AOM A C5    
2838 C  C6    . A1AOM F .   ? 0.11409 0.09222 0.08946 0.00335  0.00573  -0.02169 204 A1AOM A C6    
2839 C  C7    . A1AOM F .   ? 0.12771 0.07788 0.09185 -0.01522 0.00842  -0.02814 204 A1AOM A C7    
2840 C  C8    . A1AOM F .   ? 0.11055 0.11125 0.11304 0.02275  0.00910  -0.03155 204 A1AOM A C8    
2841 C  C9    . A1AOM F .   ? 0.14494 0.10970 0.11601 0.01026  0.00133  -0.02199 204 A1AOM A C9    
2842 N  N1    . A1AOM F .   ? 0.12496 0.09331 0.09317 0.00421  0.01544  -0.01709 204 A1AOM A N1    
2843 N  N2    . A1AOM F .   ? 0.12381 0.08635 0.10596 -0.00517 0.01877  -0.01960 204 A1AOM A N2    
2844 N  N3    . A1AOM F .   ? 0.10548 0.10004 0.11438 0.02307  0.02460  -0.03695 204 A1AOM A N3    
2845 N  N4    . A1AOM F .   ? 0.11265 0.14597 0.12314 0.01075  0.01773  -0.01283 204 A1AOM A N4    
2846 N  N5    . A1AOM F .   ? 0.11306 0.10117 0.10470 0.00240  0.00718  -0.01782 204 A1AOM A N5    
2847 N  N6    . A1AOM F .   ? 0.11038 0.11568 0.11781 0.02725  0.01707  -0.01978 204 A1AOM A N6    
2848 N  N7    . A1AOM F .   ? 0.16054 0.19980 0.18934 0.01769  0.06572  -0.06960 204 A1AOM A N7    
2849 O  O1    . A1AOM F .   ? 0.11251 0.12536 0.10660 0.01503  0.01907  -0.02738 204 A1AOM A O1    
2850 O  O2    . A1AOM F .   ? 0.13736 0.10790 0.11137 -0.00559 0.01975  -0.01409 204 A1AOM A O2    
2851 O  O3    . A1AOM F .   ? 0.11573 0.10069 0.10850 0.00935  -0.00294 -0.02129 204 A1AOM A O3    
2852 O  O4    . A1AOM F .   ? 0.11061 0.10438 0.12047 0.01798  0.00643  -0.02090 204 A1AOM A O4    
2853 O  O5    . A1AOM F .   ? 0.11811 0.12590 0.09318 0.00936  0.01690  -0.00802 204 A1AOM A O5    
2854 O  O6    . A1AOM F .   ? 0.21916 0.39111 0.24419 -0.04086 0.09008  -0.10338 204 A1AOM A O6    
2855 O  O7    . A1AOM F .   ? 0.20745 0.11357 0.12162 0.01983  0.06131  -0.01906 204 A1AOM A O7    
2856 O  O     . HOH   G .   ? 0.45690 0.55339 0.32361 -0.11823 -0.19755 0.09079  301 HOH   A O     
2857 O  O     . HOH   G .   ? 0.39573 0.47774 0.38630 0.04877  0.07835  -0.02952 302 HOH   A O     
2858 O  O     . HOH   G .   ? 0.64585 0.45303 0.67095 -0.10502 -0.04973 -0.24476 303 HOH   A O     
2859 O  O     . HOH   G .   ? 0.62203 0.40439 0.30082 0.05790  0.02934  0.00434  304 HOH   A O     
2860 O  O     . HOH   G .   ? 0.53279 0.55564 0.41070 0.30077  -0.16732 -0.19217 305 HOH   A O     
2861 O  O     . HOH   G .   ? 0.37261 0.65907 0.74368 0.23852  0.12565  0.09390  306 HOH   A O     
2862 O  O     . HOH   G .   ? 0.44977 0.52604 0.80093 0.10672  -0.07129 -0.30527 307 HOH   A O     
2863 O  O     . HOH   G .   ? 0.22015 0.74530 0.45371 0.02873  0.00711  0.03124  308 HOH   A O     
2864 O  O     . HOH   G .   ? 0.34514 0.40492 0.56110 -0.02123 0.18184  -0.20508 309 HOH   A O     
2865 O  O     . HOH   G .   ? 0.36538 0.28323 0.15274 -0.17345 0.04324  -0.00787 310 HOH   A O     
2866 O  O     . HOH   G .   ? 0.68570 0.27117 0.57848 -0.12880 -0.26783 0.06539  311 HOH   A O     
2867 O  O     . HOH   G .   ? 0.58782 0.66101 0.55606 -0.23878 0.23892  -0.17145 312 HOH   A O     
2868 O  O     . HOH   G .   ? 0.25515 0.18148 0.33683 0.01930  0.05682  -0.04743 313 HOH   A O     
2869 O  O     . HOH   G .   ? 0.69311 0.70399 0.34991 0.28430  0.18464  0.11058  314 HOH   A O     
2870 O  O     . HOH   G .   ? 0.66523 1.10227 0.29305 -0.16418 -0.02842 0.03966  315 HOH   A O     
2871 O  O     . HOH   G .   ? 0.32104 0.30869 0.41545 0.14426  -0.16617 -0.17070 316 HOH   A O     
2872 O  O     . HOH   G .   ? 0.46488 0.39172 0.41426 0.17109  -0.02666 -0.06880 317 HOH   A O     
2873 O  O     . HOH   G .   ? 0.21148 0.20512 0.28827 0.01734  0.03462  0.01983  318 HOH   A O     
2874 O  O     . HOH   G .   ? 0.20855 0.23879 0.35891 -0.03818 0.00948  -0.06494 319 HOH   A O     
2875 O  O     . HOH   G .   ? 0.21899 0.35104 0.70673 0.04186  -0.03684 0.15546  320 HOH   A O     
2876 O  O     . HOH   G .   ? 0.42581 0.17339 0.25089 -0.02110 -0.05492 0.03166  321 HOH   A O     
2877 O  O     . HOH   G .   ? 0.12674 0.13451 0.10924 0.00458  0.01131  -0.00402 322 HOH   A O     
2878 O  O     . HOH   G .   ? 0.20424 0.36346 0.30880 0.06851  0.03575  0.07241  323 HOH   A O     
2879 O  O     . HOH   G .   ? 0.45249 0.71834 0.45299 -0.21747 -0.07310 0.13414  324 HOH   A O     
2880 O  O     . HOH   G .   ? 0.38813 0.60559 0.63995 0.23310  0.16157  0.07631  325 HOH   A O     
2881 O  O     . HOH   G .   ? 0.18692 0.17007 0.26333 -0.00778 0.01876  -0.01096 326 HOH   A O     
2882 O  O     . HOH   G .   ? 0.10126 0.12755 0.09010 0.00005  0.02714  -0.00651 327 HOH   A O     
2883 O  O     . HOH   G .   ? 0.35271 0.43492 0.15297 0.18347  -0.01674 -0.04025 328 HOH   A O     
2884 O  O     . HOH   G .   ? 0.69297 0.38792 0.30501 -0.06379 0.07549  0.14369  329 HOH   A O     
2885 O  O     . HOH   G .   ? 0.54933 0.25720 0.92110 0.09182  0.00058  -0.01635 330 HOH   A O     
2886 O  O     . HOH   G .   ? 0.22471 0.13226 0.14429 -0.01371 0.05398  -0.03640 331 HOH   A O     
2887 O  O     . HOH   G .   ? 0.35829 0.23960 0.31171 -0.12637 -0.03619 0.01916  332 HOH   A O     
2888 O  O     . HOH   G .   ? 0.73962 0.23428 0.48100 -0.08469 0.16668  0.02878  333 HOH   A O     
2889 O  O     . HOH   G .   ? 0.30732 0.80148 0.35708 -0.13775 -0.04439 0.25184  334 HOH   A O     
2890 O  O     . HOH   G .   ? 0.94526 0.65260 0.39097 -0.21952 0.20700  -0.06595 335 HOH   A O     
2891 O  O     . HOH   G .   ? 0.47527 0.23895 0.17775 -0.07836 0.02216  -0.02397 336 HOH   A O     
2892 O  O     . HOH   G .   ? 0.29050 0.81454 0.91545 0.05597  -0.14086 0.01389  337 HOH   A O     
2893 O  O     . HOH   G .   ? 0.20345 0.30346 0.23805 -0.02388 0.03166  0.02558  338 HOH   A O     
2894 O  O     . HOH   G .   ? 0.44747 0.32119 0.38916 0.18079  0.22283  0.15830  339 HOH   A O     
2895 O  O     . HOH   G .   ? 0.15403 0.14855 0.17770 -0.01391 0.04729  -0.02272 340 HOH   A O     
2896 O  O     . HOH   G .   ? 0.78477 0.44582 0.49534 0.13617  0.17313  -0.16710 341 HOH   A O     
2897 O  O     . HOH   G .   ? 0.46736 0.25941 0.46671 -0.04712 -0.24212 -0.04130 342 HOH   A O     
2898 O  O     . HOH   G .   ? 0.34231 0.19682 0.62407 -0.04717 -0.05931 0.10554  343 HOH   A O     
2899 O  O     . HOH   G .   ? 0.11928 0.09627 0.10334 0.00004  0.01766  -0.02346 344 HOH   A O     
2900 O  O     . HOH   G .   ? 0.28564 0.22190 0.42240 -0.04573 0.18178  -0.10836 345 HOH   A O     
2901 O  O     . HOH   G .   ? 0.19157 0.22829 0.14383 -0.01505 0.04723  -0.05968 346 HOH   A O     
2902 O  O     . HOH   G .   ? 0.23168 0.21737 0.21338 -0.01341 0.05396  -0.04231 347 HOH   A O     
2903 O  O     . HOH   G .   ? 0.21961 0.29172 0.20299 -0.04203 0.06063  -0.01976 348 HOH   A O     
2904 O  O     . HOH   G .   ? 0.53333 0.29202 0.20487 0.00580  -0.03251 -0.04153 349 HOH   A O     
2905 O  O     . HOH   G .   ? 0.12130 0.15116 0.09910 0.01499  0.02608  -0.03206 350 HOH   A O     
2906 O  O     . HOH   G .   ? 0.55775 0.80280 0.36675 0.04034  0.07239  0.26423  351 HOH   A O     
2907 O  O     . HOH   G .   ? 0.16168 0.19041 0.13352 0.01073  0.01633  -0.02843 352 HOH   A O     
2908 O  O     . HOH   G .   ? 0.19277 0.20935 0.13256 0.01440  0.01995  0.01272  353 HOH   A O     
2909 O  O     . HOH   G .   ? 0.25412 0.20709 0.22476 -0.00872 0.02332  -0.04215 354 HOH   A O     
2910 O  O     . HOH   G .   ? 0.25084 0.15709 0.19560 -0.03819 0.08441  -0.02528 355 HOH   A O     
2911 O  O     . HOH   G .   ? 0.63653 0.40680 0.21516 0.10751  -0.09700 0.04563  356 HOH   A O     
2912 O  O     . HOH   G .   ? 0.46743 0.43261 0.22382 -0.23023 0.10406  -0.10218 357 HOH   A O     
2913 O  O     . HOH   G .   ? 0.19792 0.15813 0.11270 -0.00096 0.02856  -0.01602 358 HOH   A O     
2914 O  O     . HOH   G .   ? 0.28145 0.20589 0.15066 -0.03310 0.02660  -0.00988 359 HOH   A O     
2915 O  O     . HOH   G .   ? 0.19279 0.25693 0.27800 0.05024  0.07419  0.03767  360 HOH   A O     
2916 O  O     . HOH   G .   ? 0.25530 0.13411 0.13555 0.01596  -0.01571 0.01708  361 HOH   A O     
2917 O  O     . HOH   G .   ? 0.20392 0.14733 0.20530 0.02219  0.04490  -0.03971 362 HOH   A O     
2918 O  O     . HOH   G .   ? 0.37419 0.40648 0.20077 0.11012  -0.04816 0.07310  363 HOH   A O     
2919 O  O     . HOH   G .   ? 0.18380 0.23559 0.15173 -0.08852 -0.02041 0.01482  364 HOH   A O     
2920 O  O     . HOH   G .   ? 0.53066 0.69045 0.29590 -0.24580 -0.03671 0.01172  365 HOH   A O     
2921 O  O     . HOH   G .   ? 0.25989 0.65024 0.19357 0.09506  -0.04491 -0.05790 366 HOH   A O     
2922 O  O     . HOH   G .   ? 0.19504 0.12989 0.12412 0.00907  0.02790  -0.00957 367 HOH   A O     
2923 O  O     . HOH   G .   ? 0.40151 0.64209 0.30561 0.08244  0.08706  0.06226  368 HOH   A O     
2924 O  O     . HOH   G .   ? 0.19970 0.18901 0.13404 0.02288  0.00809  -0.03737 369 HOH   A O     
2925 O  O     . HOH   G .   ? 0.18341 0.17359 0.12173 0.01208  0.01522  -0.00065 370 HOH   A O     
2926 O  O     . HOH   G .   ? 0.42693 0.34348 0.47535 -0.13375 0.22467  -0.19190 371 HOH   A O     
2927 O  O     . HOH   G .   ? 0.30103 0.28650 0.46936 -0.03163 -0.01924 0.00649  372 HOH   A O     
2928 O  O     . HOH   G .   ? 0.25102 0.31688 0.26078 -0.00451 0.06110  -0.02004 373 HOH   A O     
2929 O  O     . HOH   G .   ? 0.42140 0.17080 0.26011 0.01456  0.04700  0.02658  374 HOH   A O     
2930 O  O     . HOH   G .   ? 0.21771 0.25132 0.22915 0.01866  0.00349  0.00134  375 HOH   A O     
2931 O  O     . HOH   G .   ? 0.50271 0.76881 0.26304 -0.06559 0.11956  -0.10490 376 HOH   A O     
2932 O  O     . HOH   G .   ? 0.38529 0.46089 0.30521 -0.07339 -0.05805 0.12288  377 HOH   A O     
2933 O  O     . HOH   G .   ? 0.27063 0.32116 0.25363 0.05414  -0.11460 -0.03642 378 HOH   A O     
2934 O  O     . HOH   G .   ? 0.25093 0.36500 0.28834 -0.06286 0.03480  0.07743  379 HOH   A O     
2935 O  O     . HOH   G .   ? 0.24179 0.33730 0.16882 0.01196  -0.00274 0.07602  380 HOH   A O     
2936 O  O     . HOH   G .   ? 0.24409 0.21029 0.23339 0.04208  0.06800  0.08557  381 HOH   A O     
2937 O  O     . HOH   G .   ? 0.22821 0.19323 0.16091 -0.01863 0.02436  0.02603  382 HOH   A O     
2938 O  O     . HOH   G .   ? 0.47882 0.61703 0.39534 -0.23045 -0.07132 -0.13164 383 HOH   A O     
2939 O  O     . HOH   G .   ? 0.26703 0.24216 0.49322 0.10022  -0.09469 -0.11847 384 HOH   A O     
2940 O  O     . HOH   G .   ? 0.16855 0.15613 0.23561 -0.00383 0.05355  0.03867  385 HOH   A O     
2941 O  O     . HOH   G .   ? 0.25012 0.37368 0.77826 -0.07977 -0.03880 0.15118  386 HOH   A O     
2942 O  O     . HOH   G .   ? 0.19782 0.12439 0.20972 -0.00122 -0.02267 0.03741  387 HOH   A O     
2943 O  O     . HOH   G .   ? 0.15749 0.35777 0.44867 -0.01217 -0.00437 0.21436  388 HOH   A O     
2944 O  O     . HOH   G .   ? 0.53108 0.76106 0.44918 -0.19770 0.01755  -0.09721 389 HOH   A O     
2945 O  O     . HOH   G .   ? 0.17627 0.15131 0.10987 -0.00991 0.05491  -0.00472 390 HOH   A O     
2946 O  O     . HOH   G .   ? 0.64095 0.39515 0.56896 -0.25897 -0.04173 -0.09754 391 HOH   A O     
2947 O  O     . HOH   G .   ? 0.21230 0.21844 0.42513 0.01627  0.01042  0.09090  392 HOH   A O     
2948 O  O     . HOH   G .   ? 0.54907 0.38871 0.42064 0.23866  0.14811  0.02247  393 HOH   A O     
2949 O  O     . HOH   G .   ? 0.13656 0.08906 0.11064 0.00508  0.04903  -0.00568 394 HOH   A O     
2950 O  O     . HOH   G .   ? 0.30974 0.31714 0.29727 0.06045  0.09834  0.05393  395 HOH   A O     
2951 O  O     . HOH   G .   ? 0.11831 0.11784 0.10569 0.00217  0.02813  -0.01763 396 HOH   A O     
2952 O  O     . HOH   G .   ? 0.51074 0.24126 0.22806 0.11654  -0.09057 -0.05421 397 HOH   A O     
2953 O  O     . HOH   G .   ? 0.39893 0.20203 0.15597 0.11005  0.01132  0.01364  398 HOH   A O     
2954 O  O     . HOH   G .   ? 0.73583 0.48768 0.53428 -0.08844 -0.04500 -0.14721 399 HOH   A O     
2955 O  O     . HOH   G .   ? 0.20652 0.28626 0.17344 -0.08868 0.00477  0.04639  400 HOH   A O     
2956 O  O     . HOH   G .   ? 0.26053 0.17460 0.24266 -0.00823 0.05880  -0.00590 401 HOH   A O     
2957 O  O     . HOH   G .   ? 0.53494 0.26149 0.76153 -0.13899 -0.04181 -0.04838 402 HOH   A O     
2958 O  O     . HOH   G .   ? 0.19064 0.29494 0.22964 0.04110  0.01303  -0.08833 403 HOH   A O     
2959 O  O     . HOH   G .   ? 0.57730 0.39763 0.24279 -0.02061 0.16036  0.04225  404 HOH   A O     
2960 O  O     . HOH   G .   ? 0.70597 0.72261 0.27122 -0.11285 0.04946  0.15414  405 HOH   A O     
2961 O  O     . HOH   G .   ? 0.15893 0.21136 0.16812 -0.01295 0.03707  -0.03876 406 HOH   A O     
2962 O  O     . HOH   G .   ? 0.51872 0.23683 0.46345 0.11425  0.03668  0.03710  407 HOH   A O     
2963 O  O     . HOH   G .   ? 0.25730 0.52204 0.37191 -0.11746 0.10184  -0.11317 408 HOH   A O     
2964 O  O     . HOH   G .   ? 0.34166 0.94175 0.32052 0.05939  0.07204  -0.09762 409 HOH   A O     
2965 O  O     . HOH   G .   ? 0.55929 0.30145 0.44829 -0.12394 -0.25386 0.09849  410 HOH   A O     
2966 O  O     . HOH   G .   ? 0.43612 0.36073 0.22826 0.15680  -0.02037 -0.07334 411 HOH   A O     
2967 O  O     . HOH   G .   ? 0.49583 0.45314 0.35588 0.24553  0.19113  0.13748  412 HOH   A O     
2968 O  O     . HOH   G .   ? 0.23232 0.42129 0.54979 -0.04337 0.03270  0.20911  413 HOH   A O     
2969 O  O     . HOH   G .   ? 0.46505 0.59945 0.18981 -0.09634 0.06120  -0.00958 414 HOH   A O     
2970 O  O     . HOH   G .   ? 0.24574 0.20731 0.16878 0.05874  -0.01107 -0.01139 415 HOH   A O     
2971 O  O     . HOH   G .   ? 0.32599 0.23297 0.67521 0.02543  0.07791  0.10435  416 HOH   A O     
2972 O  O     . HOH   G .   ? 0.25955 0.48076 0.32193 0.00720  -0.02645 0.14800  417 HOH   A O     
2973 O  O     . HOH   G .   ? 0.20138 0.15270 0.20835 -0.01855 0.00099  -0.03771 418 HOH   A O     
2974 O  O     . HOH   G .   ? 0.22935 0.33837 0.32558 0.03905  0.04331  -0.02251 419 HOH   A O     
2975 O  O     . HOH   G .   ? 0.46056 0.30257 0.57320 0.07662  0.27911  0.00878  420 HOH   A O     
2976 O  O     . HOH   G .   ? 0.11514 0.08423 0.12100 -0.00127 0.03153  -0.00678 421 HOH   A O     
2977 O  O     . HOH   G .   ? 0.24534 0.33503 0.26255 -0.09188 -0.03170 0.03608  422 HOH   A O     
2978 O  O     . HOH   G .   ? 0.30836 0.31153 0.13683 -0.13260 0.06024  -0.05643 423 HOH   A O     
2979 O  O     . HOH   G .   ? 0.31545 0.63442 0.27855 0.11966  0.05150  -0.12908 424 HOH   A O     
2980 O  O     . HOH   G .   ? 0.56275 0.45375 0.49555 0.13776  0.19293  0.07045  425 HOH   A O     
2981 O  O     . HOH   G .   ? 0.24604 0.24901 0.22621 -0.08939 0.01305  0.02627  426 HOH   A O     
2982 O  O     . HOH   G .   ? 0.47835 0.24943 0.48200 0.00400  0.14694  -0.14459 427 HOH   A O     
2983 O  O     . HOH   G .   ? 0.42318 0.39133 0.26406 0.05296  -0.11523 -0.15266 428 HOH   A O     
2984 O  O     . HOH   G .   ? 0.65855 0.68979 0.41026 0.00714  0.27997  0.09664  429 HOH   A O     
2985 O  O     . HOH   G .   ? 0.18027 0.21400 0.44145 -0.02505 0.05385  0.02520  430 HOH   A O     
2986 O  O     . HOH   G .   ? 0.39252 0.60328 0.41918 0.14927  -0.09358 0.17928  431 HOH   A O     
2987 O  O     . HOH   G .   ? 0.38176 0.18418 0.56773 -0.07552 -0.11387 0.00847  432 HOH   A O     
2988 O  O     . HOH   G .   ? 0.38409 0.17943 0.41917 0.08060  -0.14895 -0.08318 433 HOH   A O     
2989 O  O     . HOH   G .   ? 0.48523 0.75857 0.36474 -0.08827 -0.10475 -0.20623 434 HOH   A O     
2990 O  O     . HOH   G .   ? 0.11304 0.10284 0.09509 0.00946  0.02972  -0.00863 435 HOH   A O     
2991 O  O     . HOH   G .   ? 0.24019 0.21133 0.38668 0.02273  0.10350  -0.01433 436 HOH   A O     
2992 O  O     . HOH   G .   ? 0.26831 0.58869 0.35630 0.12517  -0.11541 -0.19263 437 HOH   A O     
2993 O  O     . HOH   G .   ? 0.25890 0.39539 0.25472 -0.08897 0.02540  -0.11205 438 HOH   A O     
2994 O  O     . HOH   G .   ? 0.28577 0.32749 0.49318 0.01948  -0.04565 0.21061  439 HOH   A O     
2995 O  O     . HOH   G .   ? 0.19032 0.26880 0.43226 -0.01429 -0.09981 0.03492  440 HOH   A O     
2996 O  O     . HOH   G .   ? 0.19855 0.25494 0.19745 -0.06603 -0.03251 -0.00819 441 HOH   A O     
2997 O  O     . HOH   G .   ? 0.16752 0.38893 0.30603 0.01265  -0.05585 -0.16844 442 HOH   A O     
2998 O  O     . HOH   G .   ? 0.58474 0.32268 0.30174 -0.14358 0.11794  -0.11459 443 HOH   A O     
2999 O  O     . HOH   G .   ? 0.42494 0.24042 0.27617 0.03278  0.19265  -0.00243 444 HOH   A O     
3000 O  O     . HOH   G .   ? 0.19874 0.40215 0.23949 0.08374  0.05527  0.07473  445 HOH   A O     
3001 O  O     . HOH   G .   ? 0.13371 0.11537 0.11459 -0.00739 0.02652  -0.01183 446 HOH   A O     
3002 O  O     . HOH   G .   ? 0.14624 0.18388 0.12801 -0.02306 0.00997  -0.01577 447 HOH   A O     
3003 O  O     . HOH   G .   ? 0.24395 0.13908 0.30360 0.02790  -0.04731 -0.02560 448 HOH   A O     
3004 O  O     . HOH   G .   ? 0.35684 0.38624 0.32515 0.14582  -0.04615 -0.17661 449 HOH   A O     
3005 O  O     . HOH   G .   ? 0.18563 0.16346 0.17244 -0.00595 0.00251  -0.02421 450 HOH   A O     
3006 O  O     . HOH   G .   ? 0.15230 0.22322 0.12435 0.00972  -0.00579 -0.01891 451 HOH   A O     
3007 O  O     . HOH   G .   ? 0.16977 0.15494 0.20147 0.01044  -0.01409 0.01148  452 HOH   A O     
3008 O  O     . HOH   G .   ? 0.16668 0.41116 0.29805 -0.03189 0.02482  0.16744  453 HOH   A O     
3009 O  O     . HOH   G .   ? 0.21097 0.69548 0.28174 0.00104  -0.05402 -0.08694 454 HOH   A O     
3010 O  O     . HOH   G .   ? 0.48100 0.28446 0.88620 0.01445  0.25258  0.08096  455 HOH   A O     
3011 O  O     . HOH   G .   ? 0.65074 0.62147 0.33928 -0.15852 0.11101  0.10080  456 HOH   A O     
3012 O  O     . HOH   G .   ? 0.19679 0.18710 0.19105 0.02508  -0.04164 -0.01031 457 HOH   A O     
3013 O  O     . HOH   G .   ? 0.46395 0.45711 0.58523 -0.11612 -0.07721 0.29030  458 HOH   A O     
3014 O  O     . HOH   G .   ? 0.59522 0.20401 0.16494 -0.03839 0.07011  0.00207  459 HOH   A O     
3015 O  O     . HOH   G .   ? 0.31477 0.41254 0.56524 -0.12564 -0.01284 -0.17994 460 HOH   A O     
3016 O  O     . HOH   G .   ? 0.48640 0.52706 0.84030 -0.08083 -0.27669 -0.11765 461 HOH   A O     
3017 O  O     . HOH   G .   ? 0.31071 0.51040 0.33804 -0.07694 0.07366  0.02570  462 HOH   A O     
3018 O  O     . HOH   G .   ? 0.22525 0.14724 0.17308 0.05775  0.02237  -0.02822 463 HOH   A O     
3019 O  O     . HOH   G .   ? 0.54197 0.65084 0.54938 -0.04014 -0.06565 0.34331  464 HOH   A O     
3020 O  O     . HOH   G .   ? 0.40926 0.27220 0.16565 -0.15951 0.07833  -0.03649 465 HOH   A O     
3021 O  O     . HOH   G .   ? 0.22415 0.39860 0.28854 0.07064  -0.01382 -0.02583 466 HOH   A O     
3022 O  O     . HOH   G .   ? 0.34658 0.21084 0.61613 -0.00996 0.14863  -0.11146 467 HOH   A O     
3023 O  O     . HOH   G .   ? 0.16244 0.15643 0.13947 -0.01413 0.01133  -0.01291 468 HOH   A O     
3024 O  O     . HOH   G .   ? 0.59441 0.70530 0.43131 0.23908  0.02546  -0.22591 469 HOH   A O     
3025 O  O     . HOH   G .   ? 0.17553 0.25972 0.28243 0.02253  0.00397  0.02493  470 HOH   A O     
3026 O  O     . HOH   G .   ? 0.20500 0.24761 0.39404 0.00018  0.06300  0.11367  471 HOH   A O     
3027 O  O     . HOH   G .   ? 0.52779 0.26864 0.31687 -0.10952 -0.09553 -0.03198 472 HOH   A O     
3028 O  O     . HOH   G .   ? 0.21770 0.25468 0.15533 0.02552  0.03059  0.02522  473 HOH   A O     
3029 O  O     . HOH   G .   ? 0.11638 0.07963 0.09396 -0.02562 -0.00291 -0.00333 474 HOH   A O     
3030 O  O     . HOH   G .   ? 0.25977 0.24788 0.74910 0.00833  0.09866  0.03690  475 HOH   A O     
3031 O  O     . HOH   G .   ? 0.46281 0.27231 0.38075 -0.07670 0.07025  -0.16956 476 HOH   A O     
3032 O  O     . HOH   G .   ? 0.68562 0.71147 0.52107 -0.26459 0.20740  -0.27295 477 HOH   A O     
3033 O  O     . HOH   G .   ? 0.53289 0.29690 0.39650 0.09112  0.10955  0.04990  478 HOH   A O     
3034 O  O     . HOH   G .   ? 0.25078 0.54936 0.73906 0.05941  0.04230  0.05635  479 HOH   A O     
3035 O  O     . HOH   G .   ? 0.47328 0.31686 0.64489 0.06203  -0.29037 -0.00733 480 HOH   A O     
3036 O  O     . HOH   G .   ? 0.46178 0.78620 0.40142 0.04574  0.02920  -0.04642 481 HOH   A O     
3037 O  O     . HOH   G .   ? 0.25067 0.62099 0.61185 -0.00724 -0.00880 -0.35613 482 HOH   A O     
3038 O  O     . HOH   G .   ? 0.57710 0.42381 0.64735 -0.12277 0.31123  -0.13133 483 HOH   A O     
3039 O  O     . HOH   G .   ? 0.60680 0.58615 0.53911 -0.22066 0.22435  -0.25696 484 HOH   A O     
3040 O  O     . HOH   G .   ? 0.15650 0.10991 0.17961 -0.01680 0.01551  -0.01401 485 HOH   A O     
3041 O  O     . HOH   G .   ? 0.25634 0.33888 0.34239 -0.04620 0.00566  -0.07586 486 HOH   A O     
3042 O  O     . HOH   G .   ? 0.55255 0.44660 0.41518 0.24228  -0.11951 -0.17696 487 HOH   A O     
3043 O  O     . HOH   G .   ? 0.24165 0.10883 0.10732 0.04074  0.02143  0.01557  488 HOH   A O     
3044 O  O     . HOH   G .   ? 0.60894 0.33414 0.66064 -0.10209 0.12081  -0.11446 489 HOH   A O     
3045 O  O     . HOH   G .   ? 0.63764 0.50197 0.60617 -0.18248 0.21756  0.15292  490 HOH   A O     
3046 O  O     . HOH   G .   ? 0.88770 0.52832 0.50672 -0.13448 -0.12125 0.26162  491 HOH   A O     
3047 O  O     . HOH   G .   ? 0.53342 0.73787 0.90473 0.26362  0.12511  -0.03048 492 HOH   A O     
3048 O  O     . HOH   G .   ? 0.57729 0.36798 0.30340 -0.03255 0.06034  -0.17244 493 HOH   A O     
3049 O  O     . HOH   G .   ? 0.75496 0.24622 0.43040 -0.00911 -0.14742 0.01036  494 HOH   A O     
3050 O  O     . HOH   G .   ? 0.85050 0.34471 0.65106 -0.19867 0.20939  0.01373  495 HOH   A O     
3051 O  O     . HOH   G .   ? 0.51466 0.43254 0.28178 0.03641  0.07029  -0.05044 496 HOH   A O     
3052 O  O     . HOH   G .   ? 0.62041 0.63212 0.29074 0.36976  -0.04183 -0.06169 497 HOH   A O     
3053 O  O     . HOH   G .   ? 0.62405 0.41312 0.75195 -0.00217 0.16653  0.21169  498 HOH   A O     
3054 O  O     . HOH   G .   ? 0.35152 0.48435 0.68772 -0.18953 0.01281  -0.02038 499 HOH   A O     
3055 O  O     . HOH   G .   ? 0.38412 0.44929 0.36106 0.09070  0.03674  0.08429  500 HOH   A O     
3056 O  O     . HOH   G .   ? 0.88764 0.23249 0.23106 -0.04826 0.05578  -0.00057 501 HOH   A O     
3057 O  O     . HOH   G .   ? 0.40211 0.59192 0.42304 0.09128  -0.04239 -0.00590 502 HOH   A O     
3058 O  O     . HOH   G .   ? 0.58957 0.91072 0.46007 0.04234  -0.23422 0.16707  503 HOH   A O     
3059 O  O     . HOH   G .   ? 0.52098 0.30766 0.34883 -0.05423 -0.07121 0.03148  504 HOH   A O     
3060 O  O     . HOH   G .   ? 0.41266 0.65017 0.83482 -0.00663 0.17157  -0.16956 505 HOH   A O     
3061 O  O     . HOH   G .   ? 0.67673 0.59125 0.32495 0.31903  -0.07910 0.03427  506 HOH   A O     
3062 O  O     . HOH   G .   ? 0.48988 0.84047 0.32348 -0.04892 0.03213  -0.23182 507 HOH   A O     
3063 O  O     . HOH   G .   ? 0.33403 0.52992 0.41780 -0.03518 -0.15224 0.10849  508 HOH   A O     
3064 O  O     . HOH   G .   ? 0.29040 0.65930 0.27053 -0.16133 0.08515  -0.15154 509 HOH   A O     
3065 O  O     . HOH   G .   ? 0.44570 0.90879 0.58810 0.05430  0.23325  0.20386  510 HOH   A O     
3066 O  O     . HOH   G .   ? 0.62303 1.13647 0.37889 -0.28629 -0.00056 0.17419  511 HOH   A O     
3067 O  O     . HOH   G .   ? 0.44698 0.39739 0.29959 0.03768  0.05397  0.08152  512 HOH   A O     
3068 O  O     . HOH   G .   ? 0.86423 0.45148 0.56325 0.12424  0.24940  0.16221  513 HOH   A O     
3069 O  O     . HOH   G .   ? 0.41038 0.27714 0.70929 -0.07389 -0.19601 0.09386  514 HOH   A O     
3070 O  O     . HOH   G .   ? 0.36106 0.38095 0.19713 0.04931  -0.02287 -0.07268 515 HOH   A O     
3071 O  O     . HOH   G .   ? 0.55939 0.63577 0.55152 -0.22425 -0.23434 0.25414  516 HOH   A O     
3072 O  O     . HOH   G .   ? 0.41980 0.22149 0.60328 -0.03778 0.04318  -0.15140 517 HOH   A O     
3073 O  O     . HOH   G .   ? 0.47905 0.35799 0.26575 0.10698  0.02985  0.04338  518 HOH   A O     
3074 O  O     . HOH   G .   ? 0.28453 0.33025 0.31562 0.03167  -0.01351 -0.06599 519 HOH   A O     
3075 O  O     . HOH   G .   ? 0.47145 0.91053 0.60932 0.09057  -0.01977 -0.28763 520 HOH   A O     
3076 O  O     . HOH   G .   ? 0.38118 0.51778 1.02239 0.04288  -0.07576 -0.26221 521 HOH   A O     
3077 O  O     . HOH   G .   ? 0.74519 0.33314 0.51979 0.04378  0.16177  0.16656  522 HOH   A O     
3078 O  O     . HOH   G .   ? 0.27056 0.32954 0.26917 -0.06356 -0.03975 0.02938  523 HOH   A O     
3079 O  O     . HOH   G .   ? 0.50933 0.35713 0.81307 0.04388  0.23760  -0.15852 524 HOH   A O     
3080 O  O     . HOH   G .   ? 0.39967 0.50657 0.76906 0.10443  -0.05482 -0.07269 525 HOH   A O     
3081 O  O     . HOH   G .   ? 0.50519 0.15984 0.16547 -0.07755 0.08358  -0.00762 526 HOH   A O     
3082 O  O     . HOH   G .   ? 0.34110 0.50489 0.37949 0.08987  -0.03549 -0.02967 527 HOH   A O     
3083 O  O     . HOH   G .   ? 0.53643 0.61240 0.40171 -0.32130 -0.15814 0.18925  528 HOH   A O     
3084 O  O     . HOH   G .   ? 0.74291 0.76186 0.32175 0.03319  -0.02185 0.10686  529 HOH   A O     
3085 O  O     . HOH   G .   ? 0.23248 0.21324 0.21935 -0.01117 0.00167  0.01186  530 HOH   A O     
3086 O  O     . HOH   G .   ? 0.45949 0.45763 0.64084 0.18164  0.02747  -0.21732 531 HOH   A O     
3087 O  O     . HOH   G .   ? 0.50324 0.71761 0.49546 0.01048  0.01317  0.12215  532 HOH   A O     
3088 O  O     . HOH   G .   ? 0.37024 0.19497 0.30795 -0.01138 -0.03221 0.00643  533 HOH   A O     
3089 O  O     . HOH   G .   ? 0.50491 0.13630 0.29493 -0.00830 0.02950  -0.03099 534 HOH   A O     
3090 O  O     . HOH   G .   ? 0.56133 0.29940 0.70534 -0.15591 -0.19390 0.10533  535 HOH   A O     
3091 O  O     . HOH   G .   ? 0.32754 0.17941 0.18108 -0.01000 0.03297  0.00807  536 HOH   A O     
3092 O  O     . HOH   G .   ? 0.62702 0.49178 0.56747 0.29909  -0.19378 -0.09378 537 HOH   A O     
3093 O  O     . HOH   G .   ? 0.29638 0.56690 0.63824 0.09289  0.05771  -0.12557 538 HOH   A O     
3094 O  O     . HOH   G .   ? 0.43147 0.70188 0.24682 -0.05017 0.06333  -0.09683 539 HOH   A O     
3095 O  O     . HOH   G .   ? 0.71986 0.31953 0.54268 0.21607  -0.15114 -0.08240 540 HOH   A O     
3096 O  O     . HOH   G .   ? 0.43023 1.00193 0.44574 0.13382  0.16371  -0.01559 541 HOH   A O     
3097 O  O     . HOH   G .   ? 0.17985 0.40972 0.55190 -0.00677 0.01274  -0.18605 542 HOH   A O     
3098 O  O     . HOH   G .   ? 0.94459 0.64679 0.41841 0.31443  0.13467  0.03292  543 HOH   A O     
3099 O  O     . HOH   G .   ? 0.32008 0.84031 0.80428 0.07466  0.18242  -0.03192 544 HOH   A O     
3100 O  O     . HOH   G .   ? 0.54954 0.34149 0.95002 0.16619  -0.11908 -0.04948 545 HOH   A O     
3101 O  O     . HOH   G .   ? 0.80384 0.81544 0.42193 0.14935  0.14357  0.27443  546 HOH   A O     
3102 O  O     . HOH   G .   ? 0.72753 0.30376 0.24151 -0.19391 -0.04225 0.04846  547 HOH   A O     
3103 O  O     . HOH   G .   ? 0.88133 0.46410 0.39050 0.29804  -0.23419 -0.09017 548 HOH   A O     
3104 O  O     . HOH   G .   ? 0.76622 0.28771 0.36738 -0.17963 -0.09760 0.07800  549 HOH   A O     
3105 O  O     . HOH   G .   ? 0.60416 0.61607 0.47008 0.29641  -0.06979 0.12568  550 HOH   A O     
3106 O  O     . HOH   G .   ? 0.89350 0.46169 0.57036 0.01375  0.03730  -0.27906 551 HOH   A O     
3107 O  O     . HOH   G .   ? 0.71311 0.27822 0.42504 0.14361  0.29248  0.08453  552 HOH   A O     
3108 O  O     . HOH   G .   ? 0.31966 0.23136 0.13318 0.06420  0.04018  0.03431  553 HOH   A O     
3109 O  O     . HOH   G .   ? 0.58845 0.59654 0.47701 -0.00343 0.27422  -0.10189 554 HOH   A O     
3110 O  O     . HOH   G .   ? 0.23784 0.23112 0.27415 -0.03829 0.04554  -0.05328 555 HOH   A O     
3111 O  O     . HOH   G .   ? 0.90923 0.59806 0.41058 -0.26902 -0.20392 -0.02496 556 HOH   A O     
3112 O  O     . HOH   G .   ? 0.68927 0.55620 0.41692 0.25988  0.11075  0.18647  557 HOH   A O     
3113 O  O     . HOH   G .   ? 0.23273 0.19443 0.20256 0.02121  -0.01242 0.05949  558 HOH   A O     
3114 O  O     . HOH   G .   ? 0.42813 0.43177 1.00565 0.02945  -0.30217 -0.14599 559 HOH   A O     
3115 O  O     . HOH   G .   ? 0.57530 0.50926 0.21926 0.09843  0.00737  0.00147  560 HOH   A O     
3116 O  O     A HOH   H .   ? 0.37767 0.25454 0.25320 0.03067  0.10297  -0.06170 201 HOH   D O     
3117 O  O     B HOH   H .   ? 0.38189 0.16413 0.15906 0.00401  0.10960  -0.02075 201 HOH   D O     
3118 O  O     . HOH   H .   ? 0.33948 0.43646 0.89245 0.08783  0.16517  -0.08191 202 HOH   D O     
3119 O  O     . HOH   H .   ? 0.29464 0.35067 0.50526 -0.03117 -0.01335 0.13648  203 HOH   D O     
3120 O  O     . HOH   H .   ? 0.37995 0.55532 0.44105 -0.25582 0.06817  -0.00439 204 HOH   D O     
3121 O  O     . HOH   H .   ? 0.68249 0.26127 0.30449 0.05544  0.17387  -0.03125 205 HOH   D O     
3122 O  O     . HOH   H .   ? 0.31284 0.23928 0.36526 0.02583  -0.01643 0.13383  206 HOH   D O     
3123 O  O     . HOH   H .   ? 0.35084 0.45528 0.64817 -0.08092 0.10336  0.22644  207 HOH   D O     
3124 O  O     . HOH   H .   ? 0.27057 0.80561 0.59672 -0.00899 0.12504  0.14621  208 HOH   D O     
3125 O  O     . HOH   H .   ? 0.32824 0.31327 0.45369 -0.13328 -0.15160 0.12577  209 HOH   D O     
3126 O  O     . HOH   H .   ? 0.18888 0.21204 0.27575 -0.02543 0.05366  0.01669  210 HOH   D O     
3127 O  O     . HOH   H .   ? 0.32264 0.36476 0.27973 0.14092  0.10449  0.04532  211 HOH   D O     
3128 O  O     . HOH   H .   ? 0.37114 0.38214 0.27467 -0.11505 -0.10104 0.14035  212 HOH   D O     
3129 O  O     . HOH   H .   ? 0.44760 0.18342 0.39995 -0.05222 0.16365  0.03783  213 HOH   D O     
3130 O  O     . HOH   H .   ? 0.49471 0.53424 0.70664 0.06384  -0.24555 0.19841  214 HOH   D O     
3131 O  O     . HOH   H .   ? 0.47115 0.67159 0.36922 -0.31609 0.10651  -0.14736 215 HOH   D O     
3132 O  O     . HOH   H .   ? 0.71870 0.21154 0.23975 -0.01961 -0.09558 -0.02833 216 HOH   D O     
3133 O  O     . HOH   H .   ? 0.28319 0.57646 0.38185 0.16259  0.08214  -0.06648 217 HOH   D O     
3134 O  O     . HOH   H .   ? 0.30301 0.69996 0.27350 0.17260  0.05726  0.17965  218 HOH   D O     
3135 O  O     . HOH   H .   ? 0.29011 0.19658 0.14682 0.01257  0.03299  -0.06264 219 HOH   D O     
3136 O  O     . HOH   H .   ? 0.49151 0.53625 0.43671 0.12537  0.00151  -0.26184 220 HOH   D O     
3137 O  O     . HOH   H .   ? 0.16067 0.14700 0.11121 -0.03366 0.00615  -0.01039 221 HOH   D O     
3138 O  O     . HOH   H .   ? 0.18156 0.34107 0.31488 -0.00703 -0.01175 0.12039  222 HOH   D O     
3139 O  O     . HOH   H .   ? 0.28095 0.62101 0.44031 -0.06674 0.10511  -0.10987 223 HOH   D O     
3140 O  O     . HOH   H .   ? 0.20959 0.15509 0.29106 0.01803  0.03522  -0.00985 224 HOH   D O     
3141 O  O     . HOH   H .   ? 0.46493 0.54686 0.25258 0.14504  0.06743  0.16320  225 HOH   D O     
3142 O  O     . HOH   H .   ? 0.41610 0.52854 0.64349 0.01143  -0.11637 -0.09980 226 HOH   D O     
3143 O  O     . HOH   H .   ? 0.35967 0.61321 0.47871 0.14921  -0.09361 -0.20804 227 HOH   D O     
3144 O  O     . HOH   H .   ? 0.41053 0.54177 0.97122 0.17330  -0.07522 -0.24991 228 HOH   D O     
3145 O  O     . HOH   H .   ? 0.40955 0.34515 0.21493 -0.18998 -0.06486 0.09594  229 HOH   D O     
3146 O  O     . HOH   H .   ? 0.21556 0.16789 0.18825 0.03815  -0.00007 -0.05743 230 HOH   D O     
3147 O  O     . HOH   H .   ? 0.70647 0.30918 0.38081 0.11510  -0.09156 -0.13176 231 HOH   D O     
3148 O  O     . HOH   H .   ? 0.70685 0.42454 0.54490 0.09616  0.18016  0.00871  232 HOH   D O     
3149 O  O     . HOH   H .   ? 0.30642 0.25783 0.26196 0.11317  -0.10552 -0.11459 233 HOH   D O     
3150 O  O     . HOH   H .   ? 0.60781 0.73210 0.28142 -0.12495 0.00201  -0.06741 234 HOH   D O     
3151 O  O     . HOH   H .   ? 0.85409 0.38847 0.72144 -0.10786 -0.14433 -0.01989 235 HOH   D O     
3152 O  O     . HOH   H .   ? 0.19662 0.63874 0.36287 0.05727  -0.03055 -0.20617 236 HOH   D O     
3153 O  O     . HOH   H .   ? 0.33649 0.45222 0.38739 -0.19133 -0.13294 0.19753  237 HOH   D O     
3154 O  O     . HOH   H .   ? 0.29815 0.21628 0.29901 0.03834  0.00297  0.07975  238 HOH   D O     
3155 O  O     . HOH   H .   ? 0.36013 0.58780 0.74329 0.17404  -0.01410 -0.02774 239 HOH   D O     
3156 O  O     . HOH   H .   ? 0.20180 0.15812 0.16499 -0.01420 0.00957  -0.00729 240 HOH   D O     
3157 O  O     . HOH   H .   ? 0.50737 0.34847 0.31852 0.14738  -0.11846 -0.15978 241 HOH   D O     
3158 O  O     . HOH   H .   ? 0.31365 0.35340 0.53419 -0.09260 0.18234  0.00873  242 HOH   D O     
3159 O  O     . HOH   H .   ? 0.22079 0.45558 0.58257 0.05926  0.02294  -0.07458 243 HOH   D O     
3160 O  O     . HOH   H .   ? 0.50093 0.45519 0.35876 0.28445  0.01874  0.02166  244 HOH   D O     
3161 O  O     . HOH   H .   ? 0.15321 0.13885 0.13967 0.00278  0.01675  -0.00782 245 HOH   D O     
3162 O  O     . HOH   H .   ? 0.71122 0.22198 0.33893 0.03020  0.15308  0.00615  246 HOH   D O     
3163 O  O     . HOH   H .   ? 0.36043 0.27329 0.28857 0.11369  0.14121  -0.01170 247 HOH   D O     
3164 O  O     . HOH   H .   ? 0.20457 0.18051 0.24107 -0.03136 0.04220  -0.05047 248 HOH   D O     
3165 O  O     . HOH   H .   ? 0.38960 0.60167 0.55567 -0.17035 -0.11038 0.05822  249 HOH   D O     
3166 O  O     . HOH   H .   ? 0.48280 0.25144 0.15213 0.05280  0.01535  -0.05379 250 HOH   D O     
3167 O  O     . HOH   H .   ? 0.72394 0.31745 0.34635 0.19064  -0.23994 -0.09605 251 HOH   D O     
3168 O  O     . HOH   H .   ? 0.28443 0.45608 0.18949 0.04782  -0.01479 0.01998  252 HOH   D O     
3169 O  O     . HOH   H .   ? 0.41349 0.41390 0.28988 -0.02749 -0.01305 -0.17662 253 HOH   D O     
3170 O  O     . HOH   H .   ? 0.30511 0.37400 0.35437 -0.03781 0.11213  -0.00397 254 HOH   D O     
3171 O  O     . HOH   H .   ? 0.20153 0.14180 0.10200 -0.01161 0.02108  0.00713  255 HOH   D O     
3172 O  O     . HOH   H .   ? 0.31832 0.73594 0.28580 -0.21270 0.07213  -0.09626 256 HOH   D O     
3173 O  O     A HOH   H .   ? 0.19047 0.17980 0.13932 0.08656  -0.01852 -0.03758 257 HOH   D O     
3174 O  O     B HOH   H .   ? 0.37305 0.27844 0.37887 0.10036  0.20010  0.07412  257 HOH   D O     
3175 O  O     . HOH   H .   ? 0.14005 0.12902 0.11618 0.00639  0.01537  0.00121  258 HOH   D O     
3176 O  O     . HOH   H .   ? 0.19434 0.13307 0.11933 -0.00049 0.02512  0.03017  259 HOH   D O     
3177 O  O     . HOH   H .   ? 0.66544 0.37750 0.43613 0.13434  -0.21992 0.06725  260 HOH   D O     
3178 O  O     . HOH   H .   ? 0.28173 0.25694 0.25317 0.00592  0.02327  -0.07837 261 HOH   D O     
3179 O  O     . HOH   H .   ? 0.35203 0.18844 0.20404 0.05804  0.10008  0.01895  262 HOH   D O     
3180 O  O     . HOH   H .   ? 0.52925 0.22835 0.38162 0.09174  0.18858  -0.01893 263 HOH   D O     
3181 O  O     . HOH   H .   ? 0.20985 0.12393 0.16183 0.00053  -0.01778 -0.00658 264 HOH   D O     
3182 O  O     . HOH   H .   ? 0.23433 0.18004 0.15313 -0.03553 -0.00608 0.01307  265 HOH   D O     
3183 O  O     . HOH   H .   ? 0.73253 0.29673 0.61821 0.18603  -0.13202 0.02857  266 HOH   D O     
3184 O  O     . HOH   H .   ? 0.23083 0.13320 0.15512 -0.00598 -0.00371 0.02072  267 HOH   D O     
3185 O  O     . HOH   H .   ? 0.25503 0.16769 0.52059 0.00293  0.04364  0.10382  268 HOH   D O     
3186 O  O     . HOH   H .   ? 0.36878 0.50937 0.62066 0.14825  -0.08846 -0.02258 269 HOH   D O     
3187 O  O     . HOH   H .   ? 0.20521 0.24984 0.16349 0.03127  -0.01819 -0.01130 270 HOH   D O     
3188 O  O     . HOH   H .   ? 0.18312 0.28861 0.37288 0.01932  0.06979  0.04419  271 HOH   D O     
3189 O  O     . HOH   H .   ? 0.26172 0.21210 0.59563 0.03021  -0.06636 -0.09049 272 HOH   D O     
3190 O  O     . HOH   H .   ? 0.21764 0.25567 0.12477 -0.03873 0.04608  -0.02437 273 HOH   D O     
3191 O  O     . HOH   H .   ? 0.72393 0.22225 0.35390 -0.02649 0.06479  -0.07991 274 HOH   D O     
3192 O  O     . HOH   H .   ? 0.37240 0.25103 0.13498 0.17200  -0.00894 -0.01575 275 HOH   D O     
3193 O  O     . HOH   H .   ? 0.29430 0.17152 0.22982 0.05152  -0.06150 -0.01743 276 HOH   D O     
3194 O  O     . HOH   H .   ? 0.78666 0.51642 0.36348 0.02648  -0.22785 -0.01241 277 HOH   D O     
3195 O  O     . HOH   H .   ? 0.63115 0.40293 0.18620 -0.06915 0.09244  0.00191  278 HOH   D O     
3196 O  O     . HOH   H .   ? 0.16171 0.11640 0.13376 0.01179  0.03242  -0.00644 279 HOH   D O     
3197 O  O     . HOH   H .   ? 0.17286 0.17736 0.13568 -0.00353 0.02680  -0.02189 280 HOH   D O     
3198 O  O     . HOH   H .   ? 0.15344 0.10509 0.08528 0.00356  0.02460  0.01850  281 HOH   D O     
3199 O  O     . HOH   H .   ? 0.19695 0.10553 0.13087 0.03114  -0.03412 -0.01596 282 HOH   D O     
3200 O  O     . HOH   H .   ? 0.19377 0.31483 0.40455 0.01131  0.02415  0.19290  283 HOH   D O     
3201 O  O     . HOH   H .   ? 0.12349 0.13096 0.10585 -0.01068 0.03778  0.00880  284 HOH   D O     
3202 O  O     . HOH   H .   ? 0.15833 0.13051 0.11402 0.00469  0.03964  0.01062  285 HOH   D O     
3203 O  O     . HOH   H .   ? 0.26286 0.34061 0.44297 0.05670  0.05553  -0.18549 286 HOH   D O     
3204 O  O     A HOH   H .   ? 0.18249 0.32967 0.14424 0.04470  0.01857  -0.09105 287 HOH   D O     
3205 O  O     B HOH   H .   ? 0.34104 0.59083 0.18074 0.11745  0.02147  -0.04450 287 HOH   D O     
3206 O  O     . HOH   H .   ? 0.37413 0.25049 0.21879 -0.12243 0.11641  -0.06448 288 HOH   D O     
3207 O  O     . HOH   H .   ? 0.20254 0.24914 0.12558 0.02816  0.02787  -0.00939 289 HOH   D O     
3208 O  O     . HOH   H .   ? 0.26800 0.14341 0.20239 -0.01099 -0.03258 -0.03149 290 HOH   D O     
3209 O  O     . HOH   H .   ? 0.14236 0.10851 0.10356 -0.00093 0.01987  -0.00227 291 HOH   D O     
3210 O  O     . HOH   H .   ? 0.45954 0.24331 0.21764 -0.04790 0.05106  0.09679  292 HOH   D O     
3211 O  O     . HOH   H .   ? 0.26883 0.13570 0.12029 -0.02673 0.08624  -0.00484 293 HOH   D O     
3212 O  O     . HOH   H .   ? 0.59610 0.49542 0.75194 -0.17697 0.23004  0.15017  294 HOH   D O     
3213 O  O     . HOH   H .   ? 0.22454 0.15284 0.15646 -0.00931 -0.00767 -0.02242 295 HOH   D O     
3214 O  O     . HOH   H .   ? 0.37288 0.18364 0.24267 0.10467  -0.02392 -0.07591 296 HOH   D O     
3215 O  O     . HOH   H .   ? 0.25660 0.17478 0.32091 -0.02935 -0.07750 0.05820  297 HOH   D O     
3216 O  O     . HOH   H .   ? 0.46475 0.24158 0.18929 -0.15893 0.03243  -0.01766 298 HOH   D O     
3217 O  O     . HOH   H .   ? 0.47803 0.28697 0.19274 0.10914  0.12768  0.04553  299 HOH   D O     
3218 O  O     . HOH   H .   ? 0.34610 0.20148 0.36362 0.04370  0.10112  -0.03337 300 HOH   D O     
3219 O  O     . HOH   H .   ? 0.42201 0.69527 0.48183 -0.28784 -0.03978 0.09376  301 HOH   D O     
3220 O  O     . HOH   H .   ? 0.39768 0.22884 0.16899 0.08342  0.00377  0.01572  302 HOH   D O     
3221 O  O     . HOH   H .   ? 0.52013 0.43230 0.42304 0.24044  0.19572  0.19376  303 HOH   D O     
3222 O  O     . HOH   H .   ? 0.47087 0.18922 0.28673 0.05141  -0.10058 -0.00517 304 HOH   D O     
3223 O  O     . HOH   H .   ? 0.37333 0.36355 0.86923 0.09492  0.21629  0.24523  305 HOH   D O     
3224 O  O     . HOH   H .   ? 0.18177 0.19217 0.18738 -0.00473 0.03573  0.03121  306 HOH   D O     
3225 O  O     . HOH   H .   ? 0.32112 0.28201 0.33214 0.01307  0.04504  -0.04463 307 HOH   D O     
3226 O  O     . HOH   H .   ? 0.45473 0.27321 0.42736 0.09030  0.10850  0.09228  308 HOH   D O     
3227 O  O     . HOH   H .   ? 0.24825 0.51883 0.47382 -0.09437 -0.13410 0.19345  309 HOH   D O     
3228 O  O     . HOH   H .   ? 0.25814 0.13993 0.27049 -0.02328 0.07702  -0.03083 310 HOH   D O     
3229 O  O     . HOH   H .   ? 0.64171 0.37170 0.52531 -0.04994 0.33477  -0.01848 311 HOH   D O     
3230 O  O     . HOH   H .   ? 0.75887 0.20713 0.57559 0.05593  -0.08546 -0.03308 312 HOH   D O     
3231 O  O     . HOH   H .   ? 0.26992 0.64232 0.59860 0.09756  -0.08922 -0.20653 313 HOH   D O     
3232 O  O     . HOH   H .   ? 0.25858 0.59412 0.62016 0.03290  0.04469  0.21573  314 HOH   D O     
3233 O  O     . HOH   H .   ? 0.51834 0.28631 0.41585 0.01974  -0.18530 0.03762  315 HOH   D O     
3234 O  O     . HOH   H .   ? 0.33955 0.20200 0.17214 0.05144  0.01562  0.02679  316 HOH   D O     
3235 O  O     . HOH   H .   ? 0.24393 0.90070 0.34128 -0.03256 -0.02364 -0.12465 317 HOH   D O     
3236 O  O     . HOH   H .   ? 0.75180 0.35173 0.66904 -0.09505 0.29970  -0.17964 318 HOH   D O     
3237 O  O     . HOH   H .   ? 0.27936 0.39167 0.26028 0.02467  0.02772  -0.00135 319 HOH   D O     
3238 O  O     . HOH   H .   ? 0.36959 0.24388 0.19943 -0.13460 0.08120  -0.00317 320 HOH   D O     
3239 O  O     . HOH   H .   ? 0.19745 0.11122 0.17364 0.02244  0.01578  -0.02060 321 HOH   D O     
3240 O  O     . HOH   H .   ? 0.48611 0.51315 0.15345 0.02934  0.07377  -0.03730 322 HOH   D O     
3241 O  O     . HOH   H .   ? 0.31012 0.20602 0.69477 0.03615  0.02327  0.02268  323 HOH   D O     
3242 O  O     . HOH   H .   ? 0.59438 0.52770 0.40165 -0.14439 0.02180  -0.22121 324 HOH   D O     
3243 O  O     . HOH   H .   ? 0.35669 0.21534 0.37301 -0.02114 0.14504  -0.05605 325 HOH   D O     
3244 O  O     . HOH   H .   ? 0.25821 0.18631 0.32007 0.01927  -0.04077 -0.09117 326 HOH   D O     
3245 O  O     . HOH   H .   ? 0.37071 0.29242 0.48365 -0.01221 -0.09739 -0.13762 327 HOH   D O     
3246 O  O     . HOH   H .   ? 0.46210 0.36647 0.13435 -0.08008 0.04265  0.00633  328 HOH   D O     
3247 O  O     . HOH   H .   ? 0.36266 0.47934 0.38485 0.14327  0.07714  0.07364  329 HOH   D O     
3248 O  O     . HOH   H .   ? 0.20812 0.37680 0.40743 -0.02703 0.00208  -0.17144 330 HOH   D O     
3249 O  O     . HOH   H .   ? 0.45317 0.18204 0.21041 -0.05212 0.15390  -0.03281 331 HOH   D O     
3250 O  O     . HOH   H .   ? 0.57012 0.41476 0.84656 0.16184  -0.14248 0.03007  332 HOH   D O     
3251 O  O     . HOH   H .   ? 0.24707 0.14207 0.21009 -0.01199 -0.00893 -0.00770 333 HOH   D O     
3252 O  O     . HOH   H .   ? 0.16345 0.10511 0.10818 -0.00431 0.01220  0.00339  334 HOH   D O     
3253 O  O     . HOH   H .   ? 0.18422 0.13150 0.09734 0.00199  0.01335  -0.00400 335 HOH   D O     
3254 O  O     . HOH   H .   ? 0.39653 0.74473 0.52262 0.03453  -0.03588 -0.01568 336 HOH   D O     
3255 O  O     . HOH   H .   ? 0.41959 0.73285 0.78834 0.03747  -0.14752 0.24619  337 HOH   D O     
3256 O  O     . HOH   H .   ? 0.23780 0.22462 0.34481 0.04059  -0.04131 -0.04333 338 HOH   D O     
3257 O  O     . HOH   H .   ? 0.22834 0.18931 0.20445 -0.02057 0.01404  -0.02144 339 HOH   D O     
3258 O  O     . HOH   H .   ? 0.20316 0.28701 0.24308 0.00004  -0.03329 -0.05432 340 HOH   D O     
3259 O  O     . HOH   H .   ? 0.49787 0.37551 0.72263 -0.06345 -0.32186 0.16121  341 HOH   D O     
3260 O  O     . HOH   H .   ? 0.41634 0.23930 0.44698 -0.12201 0.21776  -0.11226 342 HOH   D O     
3261 O  O     . HOH   H .   ? 0.75622 0.33939 0.65283 0.08692  -0.34802 0.02994  343 HOH   D O     
3262 O  O     . HOH   H .   ? 0.16595 0.21271 0.38672 0.03127  0.07125  -0.06739 344 HOH   D O     
3263 O  O     . HOH   H .   ? 0.80811 0.62993 0.34346 -0.27476 -0.15592 -0.02262 345 HOH   D O     
3264 O  O     . HOH   H .   ? 0.52818 0.50724 0.67093 -0.27411 -0.05709 0.16992  346 HOH   D O     
3265 O  O     . HOH   H .   ? 0.33693 0.36830 0.35015 0.04499  0.16833  -0.01975 347 HOH   D O     
3266 O  O     . HOH   H .   ? 0.25827 0.16490 0.18450 0.05307  -0.01789 -0.00276 348 HOH   D O     
3267 O  O     . HOH   H .   ? 0.68872 0.30467 0.60792 0.03782  0.37858  0.00527  349 HOH   D O     
3268 O  O     . HOH   H .   ? 0.40124 0.62761 0.36832 0.28049  0.03743  0.08927  350 HOH   D O     
3269 O  O     . HOH   H .   ? 0.34794 0.22663 0.34944 -0.03449 -0.12056 0.07979  351 HOH   D O     
3270 O  O     . HOH   H .   ? 0.21831 0.10438 0.08814 -0.01014 -0.00190 -0.00536 352 HOH   D O     
3271 O  O     . HOH   H .   ? 0.43922 0.22467 0.57273 -0.02525 0.04166  -0.16058 353 HOH   D O     
3272 O  O     . HOH   H .   ? 0.55062 0.51967 0.33469 -0.02843 0.21182  0.06860  354 HOH   D O     
3273 O  O     . HOH   H .   ? 0.23161 0.15098 0.36896 -0.02221 0.00426  -0.00925 355 HOH   D O     
3274 O  O     . HOH   H .   ? 0.30396 0.31731 0.86806 0.03758  0.16666  -0.03907 356 HOH   D O     
3275 O  O     . HOH   H .   ? 0.73966 0.62221 0.54541 0.09786  0.25016  -0.16613 357 HOH   D O     
3276 O  O     . HOH   H .   ? 0.72195 0.54529 0.26208 0.05935  0.11420  -0.11843 358 HOH   D O     
3277 O  O     . HOH   H .   ? 0.29984 0.31743 0.46950 0.08838  0.18933  0.02084  359 HOH   D O     
3278 O  O     . HOH   H .   ? 0.27003 0.24112 0.19971 -0.10015 0.02441  -0.03010 360 HOH   D O     
3279 O  O     . HOH   H .   ? 0.17020 0.15389 0.18275 0.02676  0.02355  0.02885  361 HOH   D O     
3280 O  O     . HOH   H .   ? 0.77880 0.83913 0.35318 -0.22854 0.14143  0.09935  362 HOH   D O     
3281 O  O     . HOH   H .   ? 0.43070 0.51979 0.24806 -0.01559 -0.05578 0.00910  363 HOH   D O     
3282 O  O     . HOH   H .   ? 0.19288 0.21585 0.13036 -0.00570 0.03261  0.04897  364 HOH   D O     
3283 O  O     . HOH   H .   ? 0.21857 0.37874 0.56905 0.05056  0.14206  -0.02103 365 HOH   D O     
3284 O  O     . HOH   H .   ? 0.18483 0.18761 0.35610 0.01916  0.06247  0.02931  366 HOH   D O     
3285 O  O     . HOH   H .   ? 0.34468 0.23618 0.15928 -0.02283 0.01272  -0.01945 367 HOH   D O     
3286 O  O     . HOH   H .   ? 0.27178 0.21329 0.45252 0.11524  0.06365  0.01794  368 HOH   D O     
3287 O  O     . HOH   H .   ? 0.59504 0.36021 0.74376 -0.01720 -0.19110 -0.09271 369 HOH   D O     
3288 O  O     . HOH   H .   ? 0.89049 0.56442 0.32518 -0.27529 -0.04508 -0.08484 370 HOH   D O     
3289 O  O     . HOH   H .   ? 0.22628 0.33612 0.55709 -0.03667 0.00730  -0.23058 371 HOH   D O     
3290 O  O     . HOH   H .   ? 0.19455 0.23765 0.17342 -0.06135 0.02334  -0.01884 372 HOH   D O     
3291 O  O     . HOH   H .   ? 0.71370 0.25995 0.34280 -0.05672 -0.05027 -0.05061 373 HOH   D O     
3292 O  O     . HOH   H .   ? 0.59026 0.56818 0.35151 0.22562  -0.07285 0.13596  374 HOH   D O     
3293 O  O     . HOH   H .   ? 0.82665 0.66545 0.48083 0.07839  -0.01696 0.32045  375 HOH   D O     
3294 O  O     . HOH   H .   ? 0.70861 0.65918 0.25826 -0.31781 -0.04665 0.01197  376 HOH   D O     
3295 O  O     . HOH   H .   ? 0.39678 0.53130 0.39811 -0.03643 0.01678  0.26559  377 HOH   D O     
3296 O  O     . HOH   H .   ? 0.32475 0.18919 0.11447 0.01507  0.03970  -0.03221 378 HOH   D O     
3297 O  O     . HOH   H .   ? 0.27236 0.28106 0.24333 0.00971  0.00751  0.07534  379 HOH   D O     
3298 O  O     . HOH   H .   ? 0.57894 0.36998 0.56188 0.18329  0.29854  0.19707  380 HOH   D O     
3299 O  O     . HOH   H .   ? 0.86669 0.43935 0.23612 0.00141  -0.05069 0.05653  381 HOH   D O     
3300 O  O     . HOH   H .   ? 0.59479 0.57366 0.51666 -0.10896 -0.09875 0.02859  382 HOH   D O     
3301 O  O     . HOH   H .   ? 0.40049 0.56206 0.71751 -0.09717 -0.11798 -0.24056 383 HOH   D O     
3302 O  O     . HOH   H .   ? 0.88226 0.36643 0.52288 -0.08113 0.02716  0.11956  384 HOH   D O     
3303 O  O     . HOH   H .   ? 0.44446 0.76981 0.76448 0.06230  -0.18427 0.30837  385 HOH   D O     
3304 O  O     . HOH   H .   ? 0.23799 0.20762 0.19913 -0.01764 0.04066  -0.03215 386 HOH   D O     
3305 O  O     . HOH   H .   ? 0.32899 0.19443 0.30363 -0.02332 -0.02968 0.02480  387 HOH   D O     
3306 O  O     . HOH   H .   ? 0.61936 0.56788 0.42331 0.08882  0.19094  -0.10013 388 HOH   D O     
3307 O  O     . HOH   H .   ? 0.50408 0.52717 0.31383 -0.02298 -0.12956 0.01222  389 HOH   D O     
3308 O  O     . HOH   H .   ? 0.69958 0.71171 0.58634 -0.31781 -0.30847 0.27195  390 HOH   D O     
3309 O  O     . HOH   H .   ? 0.54847 0.52885 0.24559 -0.10463 0.04350  -0.05463 391 HOH   D O     
3310 O  O     . HOH   H .   ? 0.26441 0.28722 0.31781 -0.04787 -0.08494 0.08500  392 HOH   D O     
3311 O  O     . HOH   H .   ? 0.75219 0.38396 0.30039 0.12427  -0.06934 -0.01000 393 HOH   D O     
3312 O  O     . HOH   H .   ? 0.39953 0.28573 0.44597 0.07317  -0.19668 -0.04320 394 HOH   D O     
3313 O  O     . HOH   H .   ? 0.60364 0.51811 0.84869 0.20120  0.33810  0.06138  395 HOH   D O     
3314 O  O     . HOH   H .   ? 0.18594 0.17032 0.35357 -0.00935 -0.01016 0.01638  396 HOH   D O     
3315 O  O     . HOH   H .   ? 0.85673 0.33428 0.35058 0.10611  0.08249  0.11693  397 HOH   D O     
3316 O  O     . HOH   H .   ? 0.86704 0.44560 0.47022 -0.08082 0.29257  0.01331  398 HOH   D O     
3317 O  O     . HOH   H .   ? 0.30730 0.24676 0.40578 0.02975  -0.10719 -0.00460 399 HOH   D O     
3318 O  O     . HOH   H .   ? 0.27757 0.31788 0.31218 -0.03207 -0.02243 -0.14247 400 HOH   D O     
3319 O  O     . HOH   H .   ? 0.42513 0.93056 0.38119 -0.18654 0.03086  0.15716  401 HOH   D O     
3320 O  O     . HOH   H .   ? 0.66949 0.54942 0.92553 -0.26488 0.12765  0.04471  402 HOH   D O     
3321 O  O     . HOH   H .   ? 0.37927 0.57941 1.02323 0.08866  0.24435  0.02484  403 HOH   D O     
3322 O  O     . HOH   H .   ? 0.23538 0.18883 0.24354 0.01950  0.00037  -0.06463 404 HOH   D O     
3323 O  O     . HOH   H .   ? 0.48431 0.46889 0.39253 0.16354  0.05951  -0.06963 405 HOH   D O     
3324 O  O     . HOH   H .   ? 0.24317 0.20047 0.22576 -0.02813 -0.01726 0.06790  406 HOH   D O     
3325 O  O     . HOH   H .   ? 0.59307 0.74730 0.32519 0.09443  -0.13159 -0.06136 407 HOH   D O     
3326 O  O     . HOH   H .   ? 0.64420 0.28705 0.21649 0.01695  -0.14274 -0.01678 408 HOH   D O     
3327 O  O     . HOH   H .   ? 0.40109 0.20554 0.31632 -0.05029 0.11135  -0.00476 409 HOH   D O     
3328 O  O     . HOH   H .   ? 0.71362 0.29985 0.24653 -0.20041 0.13476  -0.05919 410 HOH   D O     
3329 O  O     . HOH   H .   ? 0.44121 0.60471 0.61259 -0.20448 0.10705  -0.20583 411 HOH   D O     
3330 O  O     . HOH   H .   ? 0.28559 0.15698 0.26368 -0.01712 -0.06460 0.06195  412 HOH   D O     
3331 O  O     . HOH   H .   ? 0.58740 0.71273 0.36099 0.03130  0.10870  0.07309  413 HOH   D O     
3332 O  O     . HOH   H .   ? 0.44781 0.36532 0.30110 -0.06439 0.10332  -0.03939 414 HOH   D O     
3333 O  O     . HOH   H .   ? 0.36215 0.66310 0.76947 0.11303  -0.15981 -0.18322 415 HOH   D O     
3334 O  O     . HOH   H .   ? 0.70347 0.73387 0.39726 0.09528  -0.21796 0.00892  416 HOH   D O     
3335 O  O     . HOH   H .   ? 0.54298 0.36158 0.69456 -0.08018 -0.17824 0.10486  417 HOH   D O     
3336 O  O     . HOH   H .   ? 0.29847 0.52379 0.22736 0.01736  -0.01693 -0.03263 418 HOH   D O     
3337 O  O     . HOH   H .   ? 0.22307 0.25398 0.75650 0.02007  0.08102  0.05445  419 HOH   D O     
3338 O  O     . HOH   H .   ? 0.55701 0.65757 0.59895 -0.29634 -0.04311 0.13336  420 HOH   D O     
3339 O  O     . HOH   H .   ? 0.37737 0.33877 0.29398 -0.03679 0.02265  -0.15263 421 HOH   D O     
3340 O  O     . HOH   H .   ? 0.31002 0.56203 0.73996 0.12451  -0.18110 0.01401  422 HOH   D O     
3341 O  O     . HOH   H .   ? 0.37540 0.60689 0.28976 0.02874  0.10964  0.16096  423 HOH   D O     
3342 O  O     . HOH   H .   ? 0.32337 0.52943 0.45198 -0.05206 0.03957  -0.28989 424 HOH   D O     
3343 O  O     . HOH   H .   ? 0.33273 0.36452 0.33978 -0.02772 -0.13756 -0.06476 425 HOH   D O     
3344 O  O     . HOH   H .   ? 0.17478 0.30182 0.60150 -0.01249 -0.01816 0.18960  426 HOH   D O     
3345 O  O     . HOH   H .   ? 0.57230 0.63775 0.33734 -0.05877 -0.03366 0.03380  427 HOH   D O     
3346 O  O     . HOH   H .   ? 0.63090 0.26389 0.62553 -0.06306 0.24140  0.06243  428 HOH   D O     
3347 O  O     A HOH   H .   ? 0.12611 0.13950 0.16926 -0.04021 0.02729  -0.00553 429 HOH   D O     
3348 O  O     B HOH   H .   ? 0.44233 0.16034 0.23317 -0.01741 0.12857  0.03589  429 HOH   D O     
3349 O  O     . HOH   H .   ? 0.64330 0.48151 0.28475 0.22717  -0.03793 -0.04721 430 HOH   D O     
3350 O  O     . HOH   H .   ? 0.33174 0.47479 0.26130 -0.05899 0.10441  -0.05663 431 HOH   D O     
3351 O  O     . HOH   H .   ? 0.42793 0.55449 0.61967 0.09501  0.06698  -0.25725 432 HOH   D O     
3352 O  O     . HOH   H .   ? 0.55424 0.90730 0.59625 0.29544  -0.14380 -0.26668 433 HOH   D O     
3353 O  O     . HOH   H .   ? 0.82327 0.39844 0.51763 0.01161  0.10798  -0.00149 434 HOH   D O     
3354 O  O     . HOH   H .   ? 0.52194 0.36869 0.40282 0.04971  0.02052  0.05845  435 HOH   D O     
3355 O  O     . HOH   H .   ? 0.43097 0.65582 0.45416 -0.20051 0.12967  -0.06930 436 HOH   D O     
3356 O  O     . HOH   H .   ? 0.53103 0.38364 0.64712 0.11407  -0.20615 -0.24869 437 HOH   D O     
3357 O  O     . HOH   H .   ? 0.63494 0.46729 0.57737 -0.03726 -0.19669 0.13673  438 HOH   D O     
3358 O  O     . HOH   H .   ? 0.56072 0.83407 0.36771 0.32608  -0.08077 -0.05859 439 HOH   D O     
3359 O  O     . HOH   H .   ? 0.60063 0.26568 0.18470 0.05907  0.07951  0.00883  440 HOH   D O     
3360 O  O     . HOH   H .   ? 0.58571 0.35007 0.41625 -0.12557 0.08564  0.03391  441 HOH   D O     
3361 O  O     . HOH   H .   ? 0.41805 0.39642 0.57824 -0.15881 0.22148  -0.24357 442 HOH   D O     
3362 O  O     . HOH   H .   ? 0.49770 0.27342 0.68349 0.10599  -0.10914 -0.13789 443 HOH   D O     
3363 O  O     . HOH   H .   ? 0.48564 0.53826 0.57402 -0.22126 0.08698  -0.18516 444 HOH   D O     
3364 O  O     . HOH   H .   ? 0.34947 0.42333 0.47153 -0.10245 -0.04705 0.08254  445 HOH   D O     
3365 O  O     . HOH   H .   ? 0.40615 0.45211 0.65583 0.11990  0.11642  -0.04074 446 HOH   D O     
3366 O  O     . HOH   H .   ? 0.46463 0.95484 0.44770 0.20701  -0.04258 -0.15250 447 HOH   D O     
3367 O  O     . HOH   H .   ? 0.33154 0.35435 0.43804 0.07727  -0.01661 -0.21955 448 HOH   D O     
3368 O  O     . HOH   H .   ? 0.65933 0.38508 0.36838 -0.04708 0.22284  -0.12539 449 HOH   D O     
3369 O  O     . HOH   H .   ? 0.52498 0.58227 0.45406 0.28200  0.15848  0.01878  450 HOH   D O     
3370 O  O     . HOH   H .   ? 0.29526 0.34115 0.40428 0.02105  0.09712  -0.07383 451 HOH   D O     
3371 O  O     . HOH   H .   ? 1.11528 0.42659 0.28787 0.15102  0.00171  0.01155  452 HOH   D O     
3372 O  O     . HOH   H .   ? 0.71170 0.23151 0.63616 -0.09175 0.07948  -0.07032 453 HOH   D O     
3373 O  O     . HOH   H .   ? 0.47796 0.47081 0.80676 -0.00639 0.13052  -0.15756 454 HOH   D O     
3374 O  O     . HOH   H .   ? 0.24402 0.23929 0.29038 0.03288  -0.01241 0.01012  455 HOH   D O     
3375 O  O     . HOH   H .   ? 0.50839 0.78198 0.41296 0.02556  0.24301  0.03096  456 HOH   D O     
3376 O  O     . HOH   H .   ? 0.82768 0.35661 0.52415 -0.18232 0.25339  -0.15377 457 HOH   D O     
3377 O  O     . HOH   H .   ? 0.60865 0.49069 0.81510 0.15023  -0.27384 0.13432  458 HOH   D O     
3378 O  O     . HOH   H .   ? 0.32301 0.61705 0.81887 0.03062  -0.12736 0.15041  459 HOH   D O     
3379 O  O     . HOH   H .   ? 0.58309 0.79684 0.85637 -0.18828 0.19434  0.30023  460 HOH   D O     
3380 O  O     . HOH   H .   ? 0.83455 0.55742 0.68030 0.06703  0.29913  0.27962  461 HOH   D O     
3381 O  O     . HOH   H .   ? 0.66960 0.46134 0.35036 0.02353  -0.08480 -0.05875 462 HOH   D O     
3382 O  O     . HOH   H .   ? 0.81006 0.53901 0.35775 -0.19609 0.12852  -0.04099 463 HOH   D O     
3383 O  O     . HOH   H .   ? 0.48737 0.34206 0.91496 0.04314  0.05769  0.05860  464 HOH   D O     
3384 O  O     . HOH   H .   ? 0.62111 0.42973 0.44270 -0.17823 0.23943  -0.01637 465 HOH   D O     
3385 O  O     . HOH   H .   ? 0.62960 0.78283 0.45983 0.04045  -0.27710 0.04256  466 HOH   D O     
3386 O  O     . HOH   H .   ? 0.71550 0.53958 0.43309 0.08575  0.10517  -0.25843 467 HOH   D O     
3387 O  O     . HOH   H .   ? 0.23718 0.55995 0.42657 0.04998  -0.03874 -0.02633 468 HOH   D O     
3388 O  O     . HOH   H .   ? 0.59632 0.63390 0.51765 0.01893  0.02251  -0.28194 469 HOH   D O     
3389 O  O     . HOH   H .   ? 0.63743 0.22163 0.17676 0.01117  -0.03572 -0.00247 470 HOH   D O     
3390 O  O     . HOH   H .   ? 0.41430 0.50484 0.84905 0.01790  -0.19913 0.04847  471 HOH   D O     
3391 O  O     . HOH   H .   ? 0.33287 0.23982 0.22036 -0.05201 -0.01357 0.03085  472 HOH   D O     
3392 O  O     . HOH   H .   ? 0.56490 0.78732 0.33122 0.11627  0.10627  0.14901  473 HOH   D O     
3393 O  O     . HOH   H .   ? 0.52040 0.82383 0.32639 -0.21130 0.06357  -0.20797 474 HOH   D O     
3394 O  O     . HOH   H .   ? 0.30176 0.19054 0.30102 0.00483  0.07694  -0.01909 475 HOH   D O     
3395 O  O     . HOH   H .   ? 0.64421 0.30713 0.25977 -0.01130 0.15295  0.03020  476 HOH   D O     
3396 O  O     . HOH   H .   ? 0.30403 0.40424 0.47290 -0.06432 -0.04379 0.10583  477 HOH   D O     
3397 O  O     . HOH   H .   ? 0.40509 0.33189 0.38160 0.00101  0.01446  0.15282  478 HOH   D O     
3398 O  O     . HOH   H .   ? 0.72125 0.39951 0.45877 0.27168  -0.19734 -0.11793 479 HOH   D O     
3399 O  O     . HOH   H .   ? 0.66099 0.68893 0.62065 -0.20357 -0.12181 0.25380  480 HOH   D O     
3400 O  O     . HOH   H .   ? 0.54742 0.53482 0.60754 0.00838  0.14361  0.16696  481 HOH   D O     
3401 O  O     . HOH   H .   ? 0.96565 0.39108 0.30100 -0.07761 0.15106  -0.06228 482 HOH   D O     
3402 O  O     . HOH   H .   ? 0.66244 0.43425 0.39250 0.14723  0.06775  0.06780  483 HOH   D O     
3403 O  O     . HOH   H .   ? 0.44911 0.26917 0.30249 -0.06043 -0.05255 -0.00220 484 HOH   D O     
3404 O  O     . HOH   H .   ? 0.56338 0.39750 0.60284 -0.13112 -0.18338 0.01473  485 HOH   D O     
3405 O  O     . HOH   H .   ? 0.42339 0.42211 0.35981 -0.14732 -0.01669 -0.10237 486 HOH   D O     
3406 O  O     . HOH   H .   ? 0.82971 0.32094 0.39910 0.05185  0.10422  0.05355  487 HOH   D O     
3407 O  O     . HOH   H .   ? 0.76609 0.77870 0.36332 -0.05062 0.08933  -0.00682 488 HOH   D O     
3408 O  O     . HOH   H .   ? 0.44112 0.33452 0.68216 -0.14495 0.04539  0.15513  489 HOH   D O     
# 
