data_9BFX
# 
_entry.id   9BFX 
# 
_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   9BFX         pdb_00009bfx 10.2210/pdb9bfx/pdb 
WWPDB D_1000283282 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-05 ? 
2 'Structure model' 1 1 2025-03-12 ? 
3 'Structure model' 1 2 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Structure summary'   
2 3 'Structure model' 'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' struct          
2 3 'Structure model' citation        
3 3 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_struct.title'                     
2 3 'Structure model' '_citation.journal_volume'          
3 3 'Structure model' '_citation.page_first'              
4 3 'Structure model' '_citation.page_last'               
5 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9BFX 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-18 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jyano@revmed.com 
_pdbx_contact_author.name_first         Jason 
_pdbx_contact_author.name_last          Yano 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9774-2611 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Tomlinson, A.C.A.'    1 0000-0002-9663-773X 
'Saldajeno-Concar, M.' 2 ?                   
'Knox, J.E.'           3 ?                   
'Yano, J.K.'           4 0000-0002-9774-2611 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            68 
_citation.language                  ? 
_citation.page_first                6041 
_citation.page_last                 6063 
_citation.title                     
;Discovery of Elironrasib (RMC-6291), a Potent and Orally Bioavailable, RAS(ON) G12C-Selective, Covalent Tricomplex Inhibitor for the Treatment of Patients with RAS G12C-Addicted Cancers.
;
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02313 
_citation.pdbx_database_id_PubMed   39993169 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Cregg, J.'         1  ? 
primary 'Pota, K.'          2  ? 
primary 'Tomlinson, A.C.A.' 3  ? 
primary 'Yano, J.'          4  ? 
primary 'Marquez, A.'       5  ? 
primary 'Liu, Y.'           6  ? 
primary 'Schulze, C.J.'     7  ? 
primary 'Seamon, K.J.'      8  ? 
primary 'Holderfield, M.'   9  ? 
primary 'Wei, X.'           10 ? 
primary 'Zhuang, Y.'        11 ? 
primary 'Yang, Y.C.'        12 ? 
primary 'Jiang, J.'         13 ? 
primary 'Huang, Y.'         14 ? 
primary 'Zhao, R.'          15 ? 
primary 'Ling, Y.'          16 ? 
primary 'Wang, Z.'          17 ? 
primary 'Flagella, M.'      18 ? 
primary 'Wang, Z.'          19 ? 
primary 'Singh, M.'         20 ? 
primary 'Knox, J.E.'        21 ? 
primary 'Nichols, R.'       22 ? 
primary 'Wildes, D.'        23 ? 
primary 'Smith, J.A.M.'     24 ? 
primary 'Koltun, E.S.'      25 ? 
primary 'Gill, A.L.'        26 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'GTPase KRas' 19382.811 2   3.6.5.2 ? ? ? 
2 polymer     man 'Peptidyl-prolyl cis-trans isomerase A' 18123.582 2   5.2.1.8 ? ? ? 
3 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' 522.196   2   ?       ? ? ? 
4 non-polymer syn 'MAGNESIUM ION' 24.305    2   ?       ? ? ? 
5 non-polymer syn 
;1-[(2E)-4-(dimethylamino)-4-methylpent-2-enoyl]-N-[(2R)-1-{[(2S,6S,8S,10R,14S,21M)-22-ethyl-21-{2-[(1S)-1-methoxyethyl]pyridin-3-yl}-18,18-dimethyl-9,15-dioxo-5,16-dioxa-2,10,22,28-tetraazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),20,23,26-tetraen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-4-fluoro-N-methylpiperidine-4-carboxamide (non-preferred name)
;
1014.278  2   ?       ? ? ? 
6 non-polymer syn 'CHLORIDE ION' 35.453    2   ?       ? ? ? 
7 water       nat water 18.015    763 ?       ? ? ? 
# 
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,B ? 
2 'polypeptide(L)' no no 
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
;SMVNPTVFFDIAVDGEPLGRVSFELFADKVPKTAENFRALSTGEKGFGYKGSCFHRIIPGFMCQGGDFTRHNGTGGKSIY
GEKFEDENFILKHTGPGILSMANAGPNTNGSQFFICTAKTEWLDGKHVVFGKVKEGMNIVEAMERFGSRNGKTSKKITIA
DCGQLE
;
D,C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER' GNP   
4 'MAGNESIUM ION' MG    
5 
;1-[(2E)-4-(dimethylamino)-4-methylpent-2-enoyl]-N-[(2R)-1-{[(2S,6S,8S,10R,14S,21M)-22-ethyl-21-{2-[(1S)-1-methoxyethyl]pyridin-3-yl}-18,18-dimethyl-9,15-dioxo-5,16-dioxa-2,10,22,28-tetraazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),20,23,26-tetraen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-4-fluoro-N-methylpiperidine-4-carboxamide (non-preferred name)
;
A1AOD 
6 'CHLORIDE ION' CL    
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  CYS n 
2 54  PHE n 
2 55  HIS n 
2 56  ARG n 
2 57  ILE n 
2 58  ILE n 
2 59  PRO n 
2 60  GLY n 
2 61  PHE n 
2 62  MET n 
2 63  CYS n 
2 64  GLN n 
2 65  GLY n 
2 66  GLY n 
2 67  ASP n 
2 68  PHE n 
2 69  THR n 
2 70  ARG n 
2 71  HIS n 
2 72  ASN n 
2 73  GLY n 
2 74  THR n 
2 75  GLY n 
2 76  GLY n 
2 77  LYS n 
2 78  SER n 
2 79  ILE n 
2 80  TYR n 
2 81  GLY n 
2 82  GLU n 
2 83  LYS n 
2 84  PHE n 
2 85  GLU n 
2 86  ASP n 
2 87  GLU n 
2 88  ASN n 
2 89  PHE n 
2 90  ILE n 
2 91  LEU n 
2 92  LYS n 
2 93  HIS n 
2 94  THR n 
2 95  GLY n 
2 96  PRO n 
2 97  GLY n 
2 98  ILE n 
2 99  LEU n 
2 100 SER n 
2 101 MET n 
2 102 ALA n 
2 103 ASN n 
2 104 ALA n 
2 105 GLY n 
2 106 PRO n 
2 107 ASN n 
2 108 THR n 
2 109 ASN n 
2 110 GLY n 
2 111 SER n 
2 112 GLN n 
2 113 PHE n 
2 114 PHE n 
2 115 ILE n 
2 116 CYS n 
2 117 THR n 
2 118 ALA n 
2 119 LYS n 
2 120 THR n 
2 121 GLU n 
2 122 TRP n 
2 123 LEU n 
2 124 ASP n 
2 125 GLY n 
2 126 LYS n 
2 127 HIS n 
2 128 VAL n 
2 129 VAL n 
2 130 PHE n 
2 131 GLY n 
2 132 LYS n 
2 133 VAL n 
2 134 LYS n 
2 135 GLU n 
2 136 GLY n 
2 137 MET n 
2 138 ASN n 
2 139 ILE n 
2 140 VAL n 
2 141 GLU n 
2 142 ALA n 
2 143 MET n 
2 144 GLU n 
2 145 ARG n 
2 146 PHE n 
2 147 GLY n 
2 148 SER n 
2 149 ARG n 
2 150 ASN n 
2 151 GLY n 
2 152 LYS n 
2 153 THR n 
2 154 SER n 
2 155 LYS n 
2 156 LYS n 
2 157 ILE n 
2 158 THR n 
2 159 ILE n 
2 160 ALA n 
2 161 ASP n 
2 162 CYS n 
2 163 GLY n 
2 164 GLN n 
2 165 LEU n 
2 166 GLU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_entity_src_gen.gene_src_tissue 
_entity_src_gen.gene_src_tissue_fraction 
_entity_src_gen.gene_src_details 
_entity_src_gen.pdbx_gene_src_fragment 
_entity_src_gen.pdbx_gene_src_scientific_name 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 170 human ? 'KRAS, KRAS2, RASK2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 166 human ? 'PPIA, CYPA'         ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1AOD non-polymer         . 
;1-[(2E)-4-(dimethylamino)-4-methylpent-2-enoyl]-N-[(2R)-1-{[(2S,6S,8S,10R,14S,21M)-22-ethyl-21-{2-[(1S)-1-methoxyethyl]pyridin-3-yl}-18,18-dimethyl-9,15-dioxo-5,16-dioxa-2,10,22,28-tetraazapentacyclo[18.5.2.1~2,6~.1~10,14~.0~23,27~]nonacosa-1(25),20,23,26-tetraen-8-yl]amino}-3-methyl-1-oxobutan-2-yl]-4-fluoro-N-methylpiperidine-4-carboxamide (non-preferred name)
;
? 'C55 H80 F N9 O8'   1014.278 
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  
CL    non-polymer         . 'CHLORIDE ION' ? 'Cl -1'             35.453   
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   ?   ?   ?   D . n 
B 2 2   MET 2   1   ?   ?   ?   D . n 
B 2 3   VAL 3   2   ?   ?   ?   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  CYS 53  52  52  CYS CYS 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 ?   ?   ?   D . n 
C 1 1   SER 1   0   0   SER SER B . n 
C 1 2   MET 2   1   1   MET MET B . n 
C 1 3   THR 3   2   2   THR THR B . n 
C 1 4   GLU 4   3   3   GLU GLU B . n 
C 1 5   TYR 5   4   4   TYR TYR B . n 
C 1 6   LYS 6   5   5   LYS LYS B . n 
C 1 7   LEU 7   6   6   LEU LEU B . n 
C 1 8   VAL 8   7   7   VAL VAL B . n 
C 1 9   VAL 9   8   8   VAL VAL B . n 
C 1 10  VAL 10  9   9   VAL VAL B . n 
C 1 11  GLY 11  10  10  GLY GLY B . n 
C 1 12  ALA 12  11  11  ALA ALA B . n 
C 1 13  CYS 13  12  12  CYS CYS B . n 
C 1 14  GLY 14  13  13  GLY GLY B . n 
C 1 15  VAL 15  14  14  VAL VAL B . n 
C 1 16  GLY 16  15  15  GLY GLY B . n 
C 1 17  LYS 17  16  16  LYS LYS B . n 
C 1 18  SER 18  17  17  SER SER B . n 
C 1 19  ALA 19  18  18  ALA ALA B . n 
C 1 20  LEU 20  19  19  LEU LEU B . n 
C 1 21  THR 21  20  20  THR THR B . n 
C 1 22  ILE 22  21  21  ILE ILE B . n 
C 1 23  GLN 23  22  22  GLN GLN B . n 
C 1 24  LEU 24  23  23  LEU LEU B . n 
C 1 25  ILE 25  24  24  ILE ILE B . n 
C 1 26  GLN 26  25  25  GLN GLN B . n 
C 1 27  ASN 27  26  26  ASN ASN B . n 
C 1 28  HIS 28  27  27  HIS HIS B . n 
C 1 29  PHE 29  28  28  PHE PHE B . n 
C 1 30  VAL 30  29  29  VAL VAL B . n 
C 1 31  ASP 31  30  30  ASP ASP B . n 
C 1 32  GLU 32  31  31  GLU GLU B . n 
C 1 33  TYR 33  32  32  TYR TYR B . n 
C 1 34  ASP 34  33  33  ASP ASP B . n 
C 1 35  PRO 35  34  34  PRO PRO B . n 
C 1 36  THR 36  35  35  THR THR B . n 
C 1 37  ILE 37  36  36  ILE ILE B . n 
C 1 38  GLU 38  37  37  GLU GLU B . n 
C 1 39  ASP 39  38  38  ASP ASP B . n 
C 1 40  SER 40  39  39  SER SER B . n 
C 1 41  TYR 41  40  40  TYR TYR B . n 
C 1 42  ARG 42  41  41  ARG ARG B . n 
C 1 43  LYS 43  42  42  LYS LYS B . n 
C 1 44  GLN 44  43  43  GLN GLN B . n 
C 1 45  VAL 45  44  44  VAL VAL B . n 
C 1 46  VAL 46  45  45  VAL VAL B . n 
C 1 47  ILE 47  46  46  ILE ILE B . n 
C 1 48  ASP 48  47  47  ASP ASP B . n 
C 1 49  GLY 49  48  48  GLY GLY B . n 
C 1 50  GLU 50  49  49  GLU GLU B . n 
C 1 51  THR 51  50  50  THR THR B . n 
C 1 52  SER 52  51  51  SER SER B . n 
C 1 53  LEU 53  52  52  LEU LEU B . n 
C 1 54  LEU 54  53  53  LEU LEU B . n 
C 1 55  ASP 55  54  54  ASP ASP B . n 
C 1 56  ILE 56  55  55  ILE ILE B . n 
C 1 57  LEU 57  56  56  LEU LEU B . n 
C 1 58  ASP 58  57  57  ASP ASP B . n 
C 1 59  THR 59  58  58  THR THR B . n 
C 1 60  ALA 60  59  59  ALA ALA B . n 
C 1 61  GLY 61  60  60  GLY GLY B . n 
C 1 62  GLN 62  61  61  GLN GLN B . n 
C 1 63  GLU 63  62  62  GLU GLU B . n 
C 1 64  GLU 64  63  63  GLU GLU B . n 
C 1 65  TYR 65  64  64  TYR TYR B . n 
C 1 66  SER 66  65  65  SER SER B . n 
C 1 67  ALA 67  66  66  ALA ALA B . n 
C 1 68  MET 68  67  67  MET MET B . n 
C 1 69  ARG 69  68  68  ARG ARG B . n 
C 1 70  ASP 70  69  69  ASP ASP B . n 
C 1 71  GLN 71  70  70  GLN GLN B . n 
C 1 72  TYR 72  71  71  TYR TYR B . n 
C 1 73  MET 73  72  72  MET MET B . n 
C 1 74  ARG 74  73  73  ARG ARG B . n 
C 1 75  THR 75  74  74  THR THR B . n 
C 1 76  GLY 76  75  75  GLY GLY B . n 
C 1 77  GLU 77  76  76  GLU GLU B . n 
C 1 78  GLY 78  77  77  GLY GLY B . n 
C 1 79  PHE 79  78  78  PHE PHE B . n 
C 1 80  LEU 80  79  79  LEU LEU B . n 
C 1 81  LEU 81  80  80  LEU LEU B . n 
C 1 82  VAL 82  81  81  VAL VAL B . n 
C 1 83  PHE 83  82  82  PHE PHE B . n 
C 1 84  ALA 84  83  83  ALA ALA B . n 
C 1 85  ILE 85  84  84  ILE ILE B . n 
C 1 86  ASN 86  85  85  ASN ASN B . n 
C 1 87  ASN 87  86  86  ASN ASN B . n 
C 1 88  THR 88  87  87  THR THR B . n 
C 1 89  LYS 89  88  88  LYS LYS B . n 
C 1 90  SER 90  89  89  SER SER B . n 
C 1 91  PHE 91  90  90  PHE PHE B . n 
C 1 92  GLU 92  91  91  GLU GLU B . n 
C 1 93  ASP 93  92  92  ASP ASP B . n 
C 1 94  ILE 94  93  93  ILE ILE B . n 
C 1 95  HIS 95  94  94  HIS HIS B . n 
C 1 96  HIS 96  95  95  HIS HIS B . n 
C 1 97  TYR 97  96  96  TYR TYR B . n 
C 1 98  ARG 98  97  97  ARG ARG B . n 
C 1 99  GLU 99  98  98  GLU GLU B . n 
C 1 100 GLN 100 99  99  GLN GLN B . n 
C 1 101 ILE 101 100 100 ILE ILE B . n 
C 1 102 LYS 102 101 101 LYS LYS B . n 
C 1 103 ARG 103 102 102 ARG ARG B . n 
C 1 104 VAL 104 103 103 VAL VAL B . n 
C 1 105 LYS 105 104 104 LYS LYS B . n 
C 1 106 ASP 106 105 105 ASP ASP B . n 
C 1 107 SER 107 106 106 SER SER B . n 
C 1 108 GLU 108 107 107 GLU GLU B . n 
C 1 109 ASP 109 108 108 ASP ASP B . n 
C 1 110 VAL 110 109 109 VAL VAL B . n 
C 1 111 PRO 111 110 110 PRO PRO B . n 
C 1 112 MET 112 111 111 MET MET B . n 
C 1 113 VAL 113 112 112 VAL VAL B . n 
C 1 114 LEU 114 113 113 LEU LEU B . n 
C 1 115 VAL 115 114 114 VAL VAL B . n 
C 1 116 GLY 116 115 115 GLY GLY B . n 
C 1 117 ASN 117 116 116 ASN ASN B . n 
C 1 118 LYS 118 117 117 LYS LYS B . n 
C 1 119 SER 119 118 118 SER SER B . n 
C 1 120 ASP 120 119 119 ASP ASP B . n 
C 1 121 LEU 121 120 120 LEU LEU B . n 
C 1 122 PRO 122 121 121 PRO PRO B . n 
C 1 123 SER 123 122 122 SER SER B . n 
C 1 124 ARG 124 123 123 ARG ARG B . n 
C 1 125 THR 125 124 124 THR THR B . n 
C 1 126 VAL 126 125 125 VAL VAL B . n 
C 1 127 ASP 127 126 126 ASP ASP B . n 
C 1 128 THR 128 127 127 THR THR B . n 
C 1 129 LYS 129 128 128 LYS LYS B . n 
C 1 130 GLN 130 129 129 GLN GLN B . n 
C 1 131 ALA 131 130 130 ALA ALA B . n 
C 1 132 GLN 132 131 131 GLN GLN B . n 
C 1 133 ASP 133 132 132 ASP ASP B . n 
C 1 134 LEU 134 133 133 LEU LEU B . n 
C 1 135 ALA 135 134 134 ALA ALA B . n 
C 1 136 ARG 136 135 135 ARG ARG B . n 
C 1 137 SER 137 136 136 SER SER B . n 
C 1 138 TYR 138 137 137 TYR TYR B . n 
C 1 139 GLY 139 138 138 GLY GLY B . n 
C 1 140 ILE 140 139 139 ILE ILE B . n 
C 1 141 PRO 141 140 140 PRO PRO B . n 
C 1 142 PHE 142 141 141 PHE PHE B . n 
C 1 143 ILE 143 142 142 ILE ILE B . n 
C 1 144 GLU 144 143 143 GLU GLU B . n 
C 1 145 THR 145 144 144 THR THR B . n 
C 1 146 SER 146 145 145 SER SER B . n 
C 1 147 ALA 147 146 146 ALA ALA B . n 
C 1 148 LYS 148 147 147 LYS LYS B . n 
C 1 149 THR 149 148 148 THR THR B . n 
C 1 150 ARG 150 149 149 ARG ARG B . n 
C 1 151 GLN 151 150 150 GLN GLN B . n 
C 1 152 GLY 152 151 151 GLY GLY B . n 
C 1 153 VAL 153 152 152 VAL VAL B . n 
C 1 154 ASP 154 153 153 ASP ASP B . n 
C 1 155 ASP 155 154 154 ASP ASP B . n 
C 1 156 ALA 156 155 155 ALA ALA B . n 
C 1 157 PHE 157 156 156 PHE PHE B . n 
C 1 158 TYR 158 157 157 TYR TYR B . n 
C 1 159 THR 159 158 158 THR THR B . n 
C 1 160 LEU 160 159 159 LEU LEU B . n 
C 1 161 VAL 161 160 160 VAL VAL B . n 
C 1 162 ARG 162 161 161 ARG ARG B . n 
C 1 163 GLU 163 162 162 GLU GLU B . n 
C 1 164 ILE 164 163 163 ILE ILE B . n 
C 1 165 ARG 165 164 164 ARG ARG B . n 
C 1 166 LYS 166 165 165 LYS LYS B . n 
C 1 167 HIS 167 166 166 HIS HIS B . n 
C 1 168 LYS 168 167 167 LYS LYS B . n 
C 1 169 GLU 169 168 168 GLU GLU B . n 
C 1 170 LYS 170 169 169 LYS LYS B . n 
D 2 1   SER 1   0   0   SER SER C . n 
D 2 2   MET 2   1   1   MET MET C . n 
D 2 3   VAL 3   2   2   VAL VAL C . n 
D 2 4   ASN 4   3   3   ASN ASN C . n 
D 2 5   PRO 5   4   4   PRO PRO C . n 
D 2 6   THR 6   5   5   THR THR C . n 
D 2 7   VAL 7   6   6   VAL VAL C . n 
D 2 8   PHE 8   7   7   PHE PHE C . n 
D 2 9   PHE 9   8   8   PHE PHE C . n 
D 2 10  ASP 10  9   9   ASP ASP C . n 
D 2 11  ILE 11  10  10  ILE ILE C . n 
D 2 12  ALA 12  11  11  ALA ALA C . n 
D 2 13  VAL 13  12  12  VAL VAL C . n 
D 2 14  ASP 14  13  13  ASP ASP C . n 
D 2 15  GLY 15  14  14  GLY GLY C . n 
D 2 16  GLU 16  15  15  GLU GLU C . n 
D 2 17  PRO 17  16  16  PRO PRO C . n 
D 2 18  LEU 18  17  17  LEU LEU C . n 
D 2 19  GLY 19  18  18  GLY GLY C . n 
D 2 20  ARG 20  19  19  ARG ARG C . n 
D 2 21  VAL 21  20  20  VAL VAL C . n 
D 2 22  SER 22  21  21  SER SER C . n 
D 2 23  PHE 23  22  22  PHE PHE C . n 
D 2 24  GLU 24  23  23  GLU GLU C . n 
D 2 25  LEU 25  24  24  LEU LEU C . n 
D 2 26  PHE 26  25  25  PHE PHE C . n 
D 2 27  ALA 27  26  26  ALA ALA C . n 
D 2 28  ASP 28  27  27  ASP ASP C . n 
D 2 29  LYS 29  28  28  LYS LYS C . n 
D 2 30  VAL 30  29  29  VAL VAL C . n 
D 2 31  PRO 31  30  30  PRO PRO C . n 
D 2 32  LYS 32  31  31  LYS LYS C . n 
D 2 33  THR 33  32  32  THR THR C . n 
D 2 34  ALA 34  33  33  ALA ALA C . n 
D 2 35  GLU 35  34  34  GLU GLU C . n 
D 2 36  ASN 36  35  35  ASN ASN C . n 
D 2 37  PHE 37  36  36  PHE PHE C . n 
D 2 38  ARG 38  37  37  ARG ARG C . n 
D 2 39  ALA 39  38  38  ALA ALA C . n 
D 2 40  LEU 40  39  39  LEU LEU C . n 
D 2 41  SER 41  40  40  SER SER C . n 
D 2 42  THR 42  41  41  THR THR C . n 
D 2 43  GLY 43  42  42  GLY GLY C . n 
D 2 44  GLU 44  43  43  GLU GLU C . n 
D 2 45  LYS 45  44  44  LYS LYS C . n 
D 2 46  GLY 46  45  45  GLY GLY C . n 
D 2 47  PHE 47  46  46  PHE PHE C . n 
D 2 48  GLY 48  47  47  GLY GLY C . n 
D 2 49  TYR 49  48  48  TYR TYR C . n 
D 2 50  LYS 50  49  49  LYS LYS C . n 
D 2 51  GLY 51  50  50  GLY GLY C . n 
D 2 52  SER 52  51  51  SER SER C . n 
D 2 53  CYS 53  52  52  CYS CYS C . n 
D 2 54  PHE 54  53  53  PHE PHE C . n 
D 2 55  HIS 55  54  54  HIS HIS C . n 
D 2 56  ARG 56  55  55  ARG ARG C . n 
D 2 57  ILE 57  56  56  ILE ILE C . n 
D 2 58  ILE 58  57  57  ILE ILE C . n 
D 2 59  PRO 59  58  58  PRO PRO C . n 
D 2 60  GLY 60  59  59  GLY GLY C . n 
D 2 61  PHE 61  60  60  PHE PHE C . n 
D 2 62  MET 62  61  61  MET MET C . n 
D 2 63  CYS 63  62  62  CYS CYS C . n 
D 2 64  GLN 64  63  63  GLN GLN C . n 
D 2 65  GLY 65  64  64  GLY GLY C . n 
D 2 66  GLY 66  65  65  GLY GLY C . n 
D 2 67  ASP 67  66  66  ASP ASP C . n 
D 2 68  PHE 68  67  67  PHE PHE C . n 
D 2 69  THR 69  68  68  THR THR C . n 
D 2 70  ARG 70  69  69  ARG ARG C . n 
D 2 71  HIS 71  70  70  HIS HIS C . n 
D 2 72  ASN 72  71  71  ASN ASN C . n 
D 2 73  GLY 73  72  72  GLY GLY C . n 
D 2 74  THR 74  73  73  THR THR C . n 
D 2 75  GLY 75  74  74  GLY GLY C . n 
D 2 76  GLY 76  75  75  GLY GLY C . n 
D 2 77  LYS 77  76  76  LYS LYS C . n 
D 2 78  SER 78  77  77  SER SER C . n 
D 2 79  ILE 79  78  78  ILE ILE C . n 
D 2 80  TYR 80  79  79  TYR TYR C . n 
D 2 81  GLY 81  80  80  GLY GLY C . n 
D 2 82  GLU 82  81  81  GLU GLU C . n 
D 2 83  LYS 83  82  82  LYS LYS C . n 
D 2 84  PHE 84  83  83  PHE PHE C . n 
D 2 85  GLU 85  84  84  GLU GLU C . n 
D 2 86  ASP 86  85  85  ASP ASP C . n 
D 2 87  GLU 87  86  86  GLU GLU C . n 
D 2 88  ASN 88  87  87  ASN ASN C . n 
D 2 89  PHE 89  88  88  PHE PHE C . n 
D 2 90  ILE 90  89  89  ILE ILE C . n 
D 2 91  LEU 91  90  90  LEU LEU C . n 
D 2 92  LYS 92  91  91  LYS LYS C . n 
D 2 93  HIS 93  92  92  HIS HIS C . n 
D 2 94  THR 94  93  93  THR THR C . n 
D 2 95  GLY 95  94  94  GLY GLY C . n 
D 2 96  PRO 96  95  95  PRO PRO C . n 
D 2 97  GLY 97  96  96  GLY GLY C . n 
D 2 98  ILE 98  97  97  ILE ILE C . n 
D 2 99  LEU 99  98  98  LEU LEU C . n 
D 2 100 SER 100 99  99  SER SER C . n 
D 2 101 MET 101 100 100 MET MET C . n 
D 2 102 ALA 102 101 101 ALA ALA C . n 
D 2 103 ASN 103 102 102 ASN ASN C . n 
D 2 104 ALA 104 103 103 ALA ALA C . n 
D 2 105 GLY 105 104 104 GLY GLY C . n 
D 2 106 PRO 106 105 105 PRO PRO C . n 
D 2 107 ASN 107 106 106 ASN ASN C . n 
D 2 108 THR 108 107 107 THR THR C . n 
D 2 109 ASN 109 108 108 ASN ASN C . n 
D 2 110 GLY 110 109 109 GLY GLY C . n 
D 2 111 SER 111 110 110 SER SER C . n 
D 2 112 GLN 112 111 111 GLN GLN C . n 
D 2 113 PHE 113 112 112 PHE PHE C . n 
D 2 114 PHE 114 113 113 PHE PHE C . n 
D 2 115 ILE 115 114 114 ILE ILE C . n 
D 2 116 CYS 116 115 115 CYS CYS C . n 
D 2 117 THR 117 116 116 THR THR C . n 
D 2 118 ALA 118 117 117 ALA ALA C . n 
D 2 119 LYS 119 118 118 LYS LYS C . n 
D 2 120 THR 120 119 119 THR THR C . n 
D 2 121 GLU 121 120 120 GLU GLU C . n 
D 2 122 TRP 122 121 121 TRP TRP C . n 
D 2 123 LEU 123 122 122 LEU LEU C . n 
D 2 124 ASP 124 123 123 ASP ASP C . n 
D 2 125 GLY 125 124 124 GLY GLY C . n 
D 2 126 LYS 126 125 125 LYS LYS C . n 
D 2 127 HIS 127 126 126 HIS HIS C . n 
D 2 128 VAL 128 127 127 VAL VAL C . n 
D 2 129 VAL 129 128 128 VAL VAL C . n 
D 2 130 PHE 130 129 129 PHE PHE C . n 
D 2 131 GLY 131 130 130 GLY GLY C . n 
D 2 132 LYS 132 131 131 LYS LYS C . n 
D 2 133 VAL 133 132 132 VAL VAL C . n 
D 2 134 LYS 134 133 133 LYS LYS C . n 
D 2 135 GLU 135 134 134 GLU GLU C . n 
D 2 136 GLY 136 135 135 GLY GLY C . n 
D 2 137 MET 137 136 136 MET MET C . n 
D 2 138 ASN 138 137 137 ASN ASN C . n 
D 2 139 ILE 139 138 138 ILE ILE C . n 
D 2 140 VAL 140 139 139 VAL VAL C . n 
D 2 141 GLU 141 140 140 GLU GLU C . n 
D 2 142 ALA 142 141 141 ALA ALA C . n 
D 2 143 MET 143 142 142 MET MET C . n 
D 2 144 GLU 144 143 143 GLU GLU C . n 
D 2 145 ARG 145 144 144 ARG ARG C . n 
D 2 146 PHE 146 145 145 PHE PHE C . n 
D 2 147 GLY 147 146 146 GLY GLY C . n 
D 2 148 SER 148 147 147 SER SER C . n 
D 2 149 ARG 149 148 148 ARG ARG C . n 
D 2 150 ASN 150 149 149 ASN ASN C . n 
D 2 151 GLY 151 150 150 GLY GLY C . n 
D 2 152 LYS 152 151 151 LYS LYS C . n 
D 2 153 THR 153 152 152 THR THR C . n 
D 2 154 SER 154 153 153 SER SER C . n 
D 2 155 LYS 155 154 154 LYS LYS C . n 
D 2 156 LYS 156 155 155 LYS LYS C . n 
D 2 157 ILE 157 156 156 ILE ILE C . n 
D 2 158 THR 158 157 157 THR THR C . n 
D 2 159 ILE 159 158 158 ILE ILE C . n 
D 2 160 ALA 160 159 159 ALA ALA C . n 
D 2 161 ASP 161 160 160 ASP ASP C . n 
D 2 162 CYS 162 161 161 CYS CYS C . n 
D 2 163 GLY 163 162 162 GLY GLY C . n 
D 2 164 GLN 164 163 163 GLN GLN C . n 
D 2 165 LEU 165 164 164 LEU LEU C . n 
D 2 166 GLU 166 165 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AOD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AOD 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E 3 GNP   1   201 201  GNP   GNP A . 
F 4 MG    1   202 301  MG    MG  A . 
G 5 A1AOD 1   203 6291 A1AOD RMC A . 
H 6 CL    1   204 1    CL    CL  A . 
I 3 GNP   1   201 201  GNP   GNP B . 
J 4 MG    1   202 301  MG    MG  B . 
K 5 A1AOD 1   203 6291 A1AOD RMC B . 
L 6 CL    1   204 2    CL    CL  B . 
M 7 HOH   1   301 738  HOH   HOH A . 
M 7 HOH   2   302 97   HOH   HOH A . 
M 7 HOH   3   303 318  HOH   HOH A . 
M 7 HOH   4   304 553  HOH   HOH A . 
M 7 HOH   5   305 762  HOH   HOH A . 
M 7 HOH   6   306 277  HOH   HOH A . 
M 7 HOH   7   307 807  HOH   HOH A . 
M 7 HOH   8   308 780  HOH   HOH A . 
M 7 HOH   9   309 513  HOH   HOH A . 
M 7 HOH   10  310 426  HOH   HOH A . 
M 7 HOH   11  311 369  HOH   HOH A . 
M 7 HOH   12  312 353  HOH   HOH A . 
M 7 HOH   13  313 216  HOH   HOH A . 
M 7 HOH   14  314 26   HOH   HOH A . 
M 7 HOH   15  315 352  HOH   HOH A . 
M 7 HOH   16  316 209  HOH   HOH A . 
M 7 HOH   17  317 800  HOH   HOH A . 
M 7 HOH   18  318 65   HOH   HOH A . 
M 7 HOH   19  319 166  HOH   HOH A . 
M 7 HOH   20  320 740  HOH   HOH A . 
M 7 HOH   21  321 42   HOH   HOH A . 
M 7 HOH   22  322 168  HOH   HOH A . 
M 7 HOH   23  323 535  HOH   HOH A . 
M 7 HOH   24  324 528  HOH   HOH A . 
M 7 HOH   25  325 635  HOH   HOH A . 
M 7 HOH   26  326 648  HOH   HOH A . 
M 7 HOH   27  327 224  HOH   HOH A . 
M 7 HOH   28  328 508  HOH   HOH A . 
M 7 HOH   29  329 604  HOH   HOH A . 
M 7 HOH   30  330 4    HOH   HOH A . 
M 7 HOH   31  331 362  HOH   HOH A . 
M 7 HOH   32  332 507  HOH   HOH A . 
M 7 HOH   33  333 289  HOH   HOH A . 
M 7 HOH   34  334 240  HOH   HOH A . 
M 7 HOH   35  335 490  HOH   HOH A . 
M 7 HOH   36  336 156  HOH   HOH A . 
M 7 HOH   37  337 444  HOH   HOH A . 
M 7 HOH   38  338 105  HOH   HOH A . 
M 7 HOH   39  339 243  HOH   HOH A . 
M 7 HOH   40  340 550  HOH   HOH A . 
M 7 HOH   41  341 186  HOH   HOH A . 
M 7 HOH   42  342 15   HOH   HOH A . 
M 7 HOH   43  343 57   HOH   HOH A . 
M 7 HOH   44  344 218  HOH   HOH A . 
M 7 HOH   45  345 195  HOH   HOH A . 
M 7 HOH   46  346 292  HOH   HOH A . 
M 7 HOH   47  347 61   HOH   HOH A . 
M 7 HOH   48  348 136  HOH   HOH A . 
M 7 HOH   49  349 727  HOH   HOH A . 
M 7 HOH   50  350 123  HOH   HOH A . 
M 7 HOH   51  351 31   HOH   HOH A . 
M 7 HOH   52  352 461  HOH   HOH A . 
M 7 HOH   53  353 521  HOH   HOH A . 
M 7 HOH   54  354 155  HOH   HOH A . 
M 7 HOH   55  355 374  HOH   HOH A . 
M 7 HOH   56  356 757  HOH   HOH A . 
M 7 HOH   57  357 39   HOH   HOH A . 
M 7 HOH   58  358 165  HOH   HOH A . 
M 7 HOH   59  359 706  HOH   HOH A . 
M 7 HOH   60  360 548  HOH   HOH A . 
M 7 HOH   61  361 256  HOH   HOH A . 
M 7 HOH   62  362 475  HOH   HOH A . 
M 7 HOH   63  363 48   HOH   HOH A . 
M 7 HOH   64  364 785  HOH   HOH A . 
M 7 HOH   65  365 69   HOH   HOH A . 
M 7 HOH   66  366 305  HOH   HOH A . 
M 7 HOH   67  367 223  HOH   HOH A . 
M 7 HOH   68  368 101  HOH   HOH A . 
M 7 HOH   69  369 126  HOH   HOH A . 
M 7 HOH   70  370 33   HOH   HOH A . 
M 7 HOH   71  371 158  HOH   HOH A . 
M 7 HOH   72  372 415  HOH   HOH A . 
M 7 HOH   73  373 544  HOH   HOH A . 
M 7 HOH   74  374 575  HOH   HOH A . 
M 7 HOH   75  375 531  HOH   HOH A . 
M 7 HOH   76  376 44   HOH   HOH A . 
M 7 HOH   77  377 84   HOH   HOH A . 
M 7 HOH   78  378 321  HOH   HOH A . 
M 7 HOH   79  379 714  HOH   HOH A . 
M 7 HOH   80  380 13   HOH   HOH A . 
M 7 HOH   81  381 52   HOH   HOH A . 
M 7 HOH   82  382 500  HOH   HOH A . 
M 7 HOH   83  383 596  HOH   HOH A . 
M 7 HOH   84  384 385  HOH   HOH A . 
M 7 HOH   85  385 75   HOH   HOH A . 
M 7 HOH   86  386 664  HOH   HOH A . 
M 7 HOH   87  387 111  HOH   HOH A . 
M 7 HOH   88  388 64   HOH   HOH A . 
M 7 HOH   89  389 797  HOH   HOH A . 
M 7 HOH   90  390 259  HOH   HOH A . 
M 7 HOH   91  391 7    HOH   HOH A . 
M 7 HOH   92  392 278  HOH   HOH A . 
M 7 HOH   93  393 244  HOH   HOH A . 
M 7 HOH   94  394 71   HOH   HOH A . 
M 7 HOH   95  395 306  HOH   HOH A . 
M 7 HOH   96  396 448  HOH   HOH A . 
M 7 HOH   97  397 389  HOH   HOH A . 
M 7 HOH   98  398 154  HOH   HOH A . 
M 7 HOH   99  399 620  HOH   HOH A . 
M 7 HOH   100 400 164  HOH   HOH A . 
M 7 HOH   101 401 280  HOH   HOH A . 
M 7 HOH   102 402 106  HOH   HOH A . 
M 7 HOH   103 403 350  HOH   HOH A . 
M 7 HOH   104 404 429  HOH   HOH A . 
M 7 HOH   105 405 116  HOH   HOH A . 
M 7 HOH   106 406 339  HOH   HOH A . 
M 7 HOH   107 407 403  HOH   HOH A . 
M 7 HOH   108 408 110  HOH   HOH A . 
M 7 HOH   109 409 543  HOH   HOH A . 
M 7 HOH   110 410 806  HOH   HOH A . 
M 7 HOH   111 411 98   HOH   HOH A . 
M 7 HOH   112 412 294  HOH   HOH A . 
M 7 HOH   113 413 552  HOH   HOH A . 
M 7 HOH   114 414 140  HOH   HOH A . 
M 7 HOH   115 415 161  HOH   HOH A . 
M 7 HOH   116 416 324  HOH   HOH A . 
M 7 HOH   117 417 701  HOH   HOH A . 
M 7 HOH   118 418 814  HOH   HOH A . 
M 7 HOH   119 419 92   HOH   HOH A . 
M 7 HOH   120 420 497  HOH   HOH A . 
M 7 HOH   121 421 200  HOH   HOH A . 
M 7 HOH   122 422 281  HOH   HOH A . 
M 7 HOH   123 423 473  HOH   HOH A . 
M 7 HOH   124 424 424  HOH   HOH A . 
M 7 HOH   125 425 246  HOH   HOH A . 
M 7 HOH   126 426 62   HOH   HOH A . 
M 7 HOH   127 427 150  HOH   HOH A . 
M 7 HOH   128 428 534  HOH   HOH A . 
M 7 HOH   129 429 633  HOH   HOH A . 
M 7 HOH   130 430 11   HOH   HOH A . 
M 7 HOH   131 431 755  HOH   HOH A . 
M 7 HOH   132 432 183  HOH   HOH A . 
M 7 HOH   133 433 286  HOH   HOH A . 
M 7 HOH   134 434 119  HOH   HOH A . 
M 7 HOH   135 435 295  HOH   HOH A . 
M 7 HOH   136 436 597  HOH   HOH A . 
M 7 HOH   137 437 188  HOH   HOH A . 
M 7 HOH   138 438 327  HOH   HOH A . 
M 7 HOH   139 439 460  HOH   HOH A . 
M 7 HOH   140 440 432  HOH   HOH A . 
M 7 HOH   141 441 219  HOH   HOH A . 
M 7 HOH   142 442 371  HOH   HOH A . 
M 7 HOH   143 443 770  HOH   HOH A . 
M 7 HOH   144 444 517  HOH   HOH A . 
M 7 HOH   145 445 802  HOH   HOH A . 
M 7 HOH   146 446 650  HOH   HOH A . 
M 7 HOH   147 447 67   HOH   HOH A . 
M 7 HOH   148 448 261  HOH   HOH A . 
M 7 HOH   149 449 254  HOH   HOH A . 
M 7 HOH   150 450 652  HOH   HOH A . 
M 7 HOH   151 451 177  HOH   HOH A . 
M 7 HOH   152 452 581  HOH   HOH A . 
M 7 HOH   153 453 574  HOH   HOH A . 
M 7 HOH   154 454 334  HOH   HOH A . 
M 7 HOH   155 455 813  HOH   HOH A . 
M 7 HOH   156 456 622  HOH   HOH A . 
M 7 HOH   157 457 348  HOH   HOH A . 
M 7 HOH   158 458 681  HOH   HOH A . 
M 7 HOH   159 459 255  HOH   HOH A . 
M 7 HOH   160 460 678  HOH   HOH A . 
M 7 HOH   161 461 763  HOH   HOH A . 
M 7 HOH   162 462 340  HOH   HOH A . 
M 7 HOH   163 463 405  HOH   HOH A . 
M 7 HOH   164 464 153  HOH   HOH A . 
M 7 HOH   165 465 815  HOH   HOH A . 
M 7 HOH   166 466 572  HOH   HOH A . 
M 7 HOH   167 467 809  HOH   HOH A . 
M 7 HOH   168 468 354  HOH   HOH A . 
M 7 HOH   169 469 554  HOH   HOH A . 
M 7 HOH   170 470 476  HOH   HOH A . 
M 7 HOH   171 471 103  HOH   HOH A . 
M 7 HOH   172 472 303  HOH   HOH A . 
M 7 HOH   173 473 487  HOH   HOH A . 
M 7 HOH   174 474 202  HOH   HOH A . 
M 7 HOH   175 475 207  HOH   HOH A . 
M 7 HOH   176 476 396  HOH   HOH A . 
M 7 HOH   177 477 808  HOH   HOH A . 
M 7 HOH   178 478 753  HOH   HOH A . 
M 7 HOH   179 479 666  HOH   HOH A . 
M 7 HOH   180 480 414  HOH   HOH A . 
M 7 HOH   181 481 175  HOH   HOH A . 
M 7 HOH   182 482 376  HOH   HOH A . 
M 7 HOH   183 483 192  HOH   HOH A . 
M 7 HOH   184 484 576  HOH   HOH A . 
M 7 HOH   185 485 493  HOH   HOH A . 
M 7 HOH   186 486 555  HOH   HOH A . 
M 7 HOH   187 487 801  HOH   HOH A . 
M 7 HOH   188 488 133  HOH   HOH A . 
M 7 HOH   189 489 625  HOH   HOH A . 
M 7 HOH   190 490 326  HOH   HOH A . 
M 7 HOH   191 491 402  HOH   HOH A . 
M 7 HOH   192 492 816  HOH   HOH A . 
M 7 HOH   193 493 707  HOH   HOH A . 
M 7 HOH   194 494 420  HOH   HOH A . 
M 7 HOH   195 495 754  HOH   HOH A . 
M 7 HOH   196 496 734  HOH   HOH A . 
M 7 HOH   197 497 777  HOH   HOH A . 
M 7 HOH   198 498 731  HOH   HOH A . 
M 7 HOH   199 499 328  HOH   HOH A . 
M 7 HOH   200 500 407  HOH   HOH A . 
M 7 HOH   201 501 640  HOH   HOH A . 
M 7 HOH   202 502 715  HOH   HOH A . 
M 7 HOH   203 503 349  HOH   HOH A . 
M 7 HOH   204 504 511  HOH   HOH A . 
M 7 HOH   205 505 583  HOH   HOH A . 
M 7 HOH   206 506 645  HOH   HOH A . 
N 7 HOH   1   201 557  HOH   HOH D . 
N 7 HOH   2   202 449  HOH   HOH D . 
N 7 HOH   3   203 697  HOH   HOH D . 
N 7 HOH   4   204 264  HOH   HOH D . 
N 7 HOH   5   205 474  HOH   HOH D . 
N 7 HOH   6   206 342  HOH   HOH D . 
N 7 HOH   7   207 638  HOH   HOH D . 
N 7 HOH   8   208 649  HOH   HOH D . 
N 7 HOH   9   209 142  HOH   HOH D . 
N 7 HOH   10  210 99   HOH   HOH D . 
N 7 HOH   11  211 293  HOH   HOH D . 
N 7 HOH   12  212 702  HOH   HOH D . 
N 7 HOH   13  213 273  HOH   HOH D . 
N 7 HOH   14  214 739  HOH   HOH D . 
N 7 HOH   15  215 761  HOH   HOH D . 
N 7 HOH   16  216 58   HOH   HOH D . 
N 7 HOH   17  217 463  HOH   HOH D . 
N 7 HOH   18  218 794  HOH   HOH D . 
N 7 HOH   19  219 104  HOH   HOH D . 
N 7 HOH   20  220 462  HOH   HOH D . 
N 7 HOH   21  221 236  HOH   HOH D . 
N 7 HOH   22  222 689  HOH   HOH D . 
N 7 HOH   23  223 18   HOH   HOH D . 
N 7 HOH   24  224 696  HOH   HOH D . 
N 7 HOH   25  225 152  HOH   HOH D . 
N 7 HOH   26  226 2    HOH   HOH D . 
N 7 HOH   27  227 830  HOH   HOH D . 
N 7 HOH   28  228 77   HOH   HOH D . 
N 7 HOH   29  229 162  HOH   HOH D . 
N 7 HOH   30  230 128  HOH   HOH D . 
N 7 HOH   31  231 399  HOH   HOH D . 
N 7 HOH   32  232 180  HOH   HOH D . 
N 7 HOH   33  233 70   HOH   HOH D . 
N 7 HOH   34  234 78   HOH   HOH D . 
N 7 HOH   35  235 112  HOH   HOH D . 
N 7 HOH   36  236 693  HOH   HOH D . 
N 7 HOH   37  237 425  HOH   HOH D . 
N 7 HOH   38  238 144  HOH   HOH D . 
N 7 HOH   39  239 9    HOH   HOH D . 
N 7 HOH   40  240 32   HOH   HOH D . 
N 7 HOH   41  241 411  HOH   HOH D . 
N 7 HOH   42  242 225  HOH   HOH D . 
N 7 HOH   43  243 22   HOH   HOH D . 
N 7 HOH   44  244 51   HOH   HOH D . 
N 7 HOH   45  245 466  HOH   HOH D . 
N 7 HOH   46  246 12   HOH   HOH D . 
N 7 HOH   47  247 113  HOH   HOH D . 
N 7 HOH   48  248 60   HOH   HOH D . 
N 7 HOH   49  249 198  HOH   HOH D . 
N 7 HOH   50  250 452  HOH   HOH D . 
N 7 HOH   51  251 122  HOH   HOH D . 
N 7 HOH   52  252 383  HOH   HOH D . 
N 7 HOH   53  253 160  HOH   HOH D . 
N 7 HOH   54  254 74   HOH   HOH D . 
N 7 HOH   55  255 619  HOH   HOH D . 
N 7 HOH   56  256 213  HOH   HOH D . 
N 7 HOH   57  257 388  HOH   HOH D . 
N 7 HOH   58  258 391  HOH   HOH D . 
N 7 HOH   59  259 169  HOH   HOH D . 
N 7 HOH   60  260 700  HOH   HOH D . 
N 7 HOH   61  261 151  HOH   HOH D . 
N 7 HOH   62  262 201  HOH   HOH D . 
N 7 HOH   63  263 182  HOH   HOH D . 
N 7 HOH   64  264 199  HOH   HOH D . 
N 7 HOH   65  265 174  HOH   HOH D . 
N 7 HOH   66  266 274  HOH   HOH D . 
N 7 HOH   67  267 172  HOH   HOH D . 
N 7 HOH   68  268 25   HOH   HOH D . 
N 7 HOH   69  269 59   HOH   HOH D . 
N 7 HOH   70  270 10   HOH   HOH D . 
N 7 HOH   71  271 525  HOH   HOH D . 
N 7 HOH   72  272 536  HOH   HOH D . 
N 7 HOH   73  273 16   HOH   HOH D . 
N 7 HOH   74  274 63   HOH   HOH D . 
N 7 HOH   75  275 680  HOH   HOH D . 
N 7 HOH   76  276 372  HOH   HOH D . 
N 7 HOH   77  277 308  HOH   HOH D . 
N 7 HOH   78  278 351  HOH   HOH D . 
N 7 HOH   79  279 124  HOH   HOH D . 
N 7 HOH   80  280 563  HOH   HOH D . 
N 7 HOH   81  281 118  HOH   HOH D . 
N 7 HOH   82  282 291  HOH   HOH D . 
N 7 HOH   83  283 83   HOH   HOH D . 
N 7 HOH   84  284 621  HOH   HOH D . 
N 7 HOH   85  285 242  HOH   HOH D . 
N 7 HOH   86  286 380  HOH   HOH D . 
N 7 HOH   87  287 170  HOH   HOH D . 
N 7 HOH   88  288 283  HOH   HOH D . 
N 7 HOH   89  289 379  HOH   HOH D . 
N 7 HOH   90  290 43   HOH   HOH D . 
N 7 HOH   91  291 720  HOH   HOH D . 
N 7 HOH   92  292 520  HOH   HOH D . 
N 7 HOH   93  293 87   HOH   HOH D . 
N 7 HOH   94  294 73   HOH   HOH D . 
N 7 HOH   95  295 190  HOH   HOH D . 
N 7 HOH   96  296 319  HOH   HOH D . 
N 7 HOH   97  297 228  HOH   HOH D . 
N 7 HOH   98  298 370  HOH   HOH D . 
N 7 HOH   99  299 393  HOH   HOH D . 
N 7 HOH   100 300 178  HOH   HOH D . 
N 7 HOH   101 301 19   HOH   HOH D . 
N 7 HOH   102 302 386  HOH   HOH D . 
N 7 HOH   103 303 68   HOH   HOH D . 
N 7 HOH   104 304 253  HOH   HOH D . 
N 7 HOH   105 305 434  HOH   HOH D . 
N 7 HOH   106 306 694  HOH   HOH D . 
N 7 HOH   107 307 137  HOH   HOH D . 
N 7 HOH   108 308 615  HOH   HOH D . 
N 7 HOH   109 309 357  HOH   HOH D . 
N 7 HOH   110 310 570  HOH   HOH D . 
N 7 HOH   111 311 304  HOH   HOH D . 
N 7 HOH   112 312 585  HOH   HOH D . 
N 7 HOH   113 313 519  HOH   HOH D . 
N 7 HOH   114 314 451  HOH   HOH D . 
N 7 HOH   115 315 639  HOH   HOH D . 
N 7 HOH   116 316 643  HOH   HOH D . 
N 7 HOH   117 317 29   HOH   HOH D . 
N 7 HOH   118 318 179  HOH   HOH D . 
N 7 HOH   119 319 266  HOH   HOH D . 
N 7 HOH   120 320 568  HOH   HOH D . 
N 7 HOH   121 321 163  HOH   HOH D . 
N 7 HOH   122 322 409  HOH   HOH D . 
N 7 HOH   123 323 79   HOH   HOH D . 
N 7 HOH   124 324 390  HOH   HOH D . 
N 7 HOH   125 325 298  HOH   HOH D . 
N 7 HOH   126 326 135  HOH   HOH D . 
N 7 HOH   127 327 320  HOH   HOH D . 
N 7 HOH   128 328 831  HOH   HOH D . 
N 7 HOH   129 329 469  HOH   HOH D . 
N 7 HOH   130 330 718  HOH   HOH D . 
N 7 HOH   131 331 121  HOH   HOH D . 
N 7 HOH   132 332 241  HOH   HOH D . 
N 7 HOH   133 333 565  HOH   HOH D . 
N 7 HOH   134 334 88   HOH   HOH D . 
N 7 HOH   135 335 716  HOH   HOH D . 
N 7 HOH   136 336 315  HOH   HOH D . 
N 7 HOH   137 337 478  HOH   HOH D . 
N 7 HOH   138 338 54   HOH   HOH D . 
N 7 HOH   139 339 571  HOH   HOH D . 
N 7 HOH   140 340 272  HOH   HOH D . 
N 7 HOH   141 341 378  HOH   HOH D . 
N 7 HOH   142 342 307  HOH   HOH D . 
N 7 HOH   143 343 817  HOH   HOH D . 
N 7 HOH   144 344 626  HOH   HOH D . 
N 7 HOH   145 345 540  HOH   HOH D . 
N 7 HOH   146 346 406  HOH   HOH D . 
N 7 HOH   147 347 669  HOH   HOH D . 
N 7 HOH   148 348 599  HOH   HOH D . 
N 7 HOH   149 349 829  HOH   HOH D . 
N 7 HOH   150 350 592  HOH   HOH D . 
N 7 HOH   151 351 367  HOH   HOH D . 
N 7 HOH   152 352 833  HOH   HOH D . 
N 7 HOH   153 353 717  HOH   HOH D . 
N 7 HOH   154 354 551  HOH   HOH D . 
N 7 HOH   155 355 768  HOH   HOH D . 
N 7 HOH   156 356 812  HOH   HOH D . 
N 7 HOH   157 357 637  HOH   HOH D . 
N 7 HOH   158 358 627  HOH   HOH D . 
N 7 HOH   159 359 584  HOH   HOH D . 
N 7 HOH   160 360 248  HOH   HOH D . 
N 7 HOH   161 361 729  HOH   HOH D . 
N 7 HOH   162 362 598  HOH   HOH D . 
N 7 HOH   163 363 93   HOH   HOH D . 
N 7 HOH   164 364 537  HOH   HOH D . 
N 7 HOH   165 365 522  HOH   HOH D . 
N 7 HOH   166 366 630  HOH   HOH D . 
N 7 HOH   167 367 698  HOH   HOH D . 
N 7 HOH   168 368 441  HOH   HOH D . 
N 7 HOH   169 369 229  HOH   HOH D . 
N 7 HOH   170 370 795  HOH   HOH D . 
N 7 HOH   171 371 252  HOH   HOH D . 
N 7 HOH   172 372 778  HOH   HOH D . 
N 7 HOH   173 373 323  HOH   HOH D . 
N 7 HOH   174 374 789  HOH   HOH D . 
N 7 HOH   175 375 634  HOH   HOH D . 
N 7 HOH   176 376 600  HOH   HOH D . 
N 7 HOH   177 377 751  HOH   HOH D . 
N 7 HOH   178 378 567  HOH   HOH D . 
N 7 HOH   179 379 788  HOH   HOH D . 
N 7 HOH   180 380 436  HOH   HOH D . 
N 7 HOH   181 381 458  HOH   HOH D . 
N 7 HOH   182 382 767  HOH   HOH D . 
N 7 HOH   183 383 262  HOH   HOH D . 
N 7 HOH   184 384 624  HOH   HOH D . 
N 7 HOH   185 385 428  HOH   HOH D . 
N 7 HOH   186 386 711  HOH   HOH D . 
N 7 HOH   187 387 786  HOH   HOH D . 
N 7 HOH   188 388 665  HOH   HOH D . 
N 7 HOH   189 389 375  HOH   HOH D . 
N 7 HOH   190 390 471  HOH   HOH D . 
N 7 HOH   191 391 641  HOH   HOH D . 
N 7 HOH   192 392 245  HOH   HOH D . 
N 7 HOH   193 393 250  HOH   HOH D . 
N 7 HOH   194 394 722  HOH   HOH D . 
O 7 HOH   1   301 472  HOH   HOH B . 
O 7 HOH   2   302 724  HOH   HOH B . 
O 7 HOH   3   303 603  HOH   HOH B . 
O 7 HOH   4   304 683  HOH   HOH B . 
O 7 HOH   5   305 532  HOH   HOH B . 
O 7 HOH   6   306 623  HOH   HOH B . 
O 7 HOH   7   307 796  HOH   HOH B . 
O 7 HOH   8   308 616  HOH   HOH B . 
O 7 HOH   9   309 480  HOH   HOH B . 
O 7 HOH   10  310 593  HOH   HOH B . 
O 7 HOH   11  311 410  HOH   HOH B . 
O 7 HOH   12  312 454  HOH   HOH B . 
O 7 HOH   13  313 736  HOH   HOH B . 
O 7 HOH   14  314 561  HOH   HOH B . 
O 7 HOH   15  315 159  HOH   HOH B . 
O 7 HOH   16  316 184  HOH   HOH B . 
O 7 HOH   17  317 491  HOH   HOH B . 
O 7 HOH   18  318 750  HOH   HOH B . 
O 7 HOH   19  319 455  HOH   HOH B . 
O 7 HOH   20  320 300  HOH   HOH B . 
O 7 HOH   21  321 456  HOH   HOH B . 
O 7 HOH   22  322 120  HOH   HOH B . 
O 7 HOH   23  323 197  HOH   HOH B . 
O 7 HOH   24  324 632  HOH   HOH B . 
O 7 HOH   25  325 212  HOH   HOH B . 
O 7 HOH   26  326 398  HOH   HOH B . 
O 7 HOH   27  327 50   HOH   HOH B . 
O 7 HOH   28  328 363  HOH   HOH B . 
O 7 HOH   29  329 81   HOH   HOH B . 
O 7 HOH   30  330 271  HOH   HOH B . 
O 7 HOH   31  331 288  HOH   HOH B . 
O 7 HOH   32  332 416  HOH   HOH B . 
O 7 HOH   33  333 610  HOH   HOH B . 
O 7 HOH   34  334 238  HOH   HOH B . 
O 7 HOH   35  335 721  HOH   HOH B . 
O 7 HOH   36  336 373  HOH   HOH B . 
O 7 HOH   37  337 695  HOH   HOH B . 
O 7 HOH   38  338 5    HOH   HOH B . 
O 7 HOH   39  339 312  HOH   HOH B . 
O 7 HOH   40  340 17   HOH   HOH B . 
O 7 HOH   41  341 20   HOH   HOH B . 
O 7 HOH   42  342 171  HOH   HOH B . 
O 7 HOH   43  343 501  HOH   HOH B . 
O 7 HOH   44  344 765  HOH   HOH B . 
O 7 HOH   45  345 400  HOH   HOH B . 
O 7 HOH   46  346 488  HOH   HOH B . 
O 7 HOH   47  347 662  HOH   HOH B . 
O 7 HOH   48  348 438  HOH   HOH B . 
O 7 HOH   49  349 76   HOH   HOH B . 
O 7 HOH   50  350 47   HOH   HOH B . 
O 7 HOH   51  351 235  HOH   HOH B . 
O 7 HOH   52  352 302  HOH   HOH B . 
O 7 HOH   53  353 524  HOH   HOH B . 
O 7 HOH   54  354 486  HOH   HOH B . 
O 7 HOH   55  355 193  HOH   HOH B . 
O 7 HOH   56  356 36   HOH   HOH B . 
O 7 HOH   57  357 21   HOH   HOH B . 
O 7 HOH   58  358 629  HOH   HOH B . 
O 7 HOH   59  359 614  HOH   HOH B . 
O 7 HOH   60  360 276  HOH   HOH B . 
O 7 HOH   61  361 275  HOH   HOH B . 
O 7 HOH   62  362 728  HOH   HOH B . 
O 7 HOH   63  363 465  HOH   HOH B . 
O 7 HOH   64  364 503  HOH   HOH B . 
O 7 HOH   65  365 260  HOH   HOH B . 
O 7 HOH   66  366 27   HOH   HOH B . 
O 7 HOH   67  367 514  HOH   HOH B . 
O 7 HOH   68  368 127  HOH   HOH B . 
O 7 HOH   69  369 820  HOH   HOH B . 
O 7 HOH   70  370 355  HOH   HOH B . 
O 7 HOH   71  371 660  HOH   HOH B . 
O 7 HOH   72  372 45   HOH   HOH B . 
O 7 HOH   73  373 14   HOH   HOH B . 
O 7 HOH   74  374 102  HOH   HOH B . 
O 7 HOH   75  375 322  HOH   HOH B . 
O 7 HOH   76  376 671  HOH   HOH B . 
O 7 HOH   77  377 268  HOH   HOH B . 
O 7 HOH   78  378 139  HOH   HOH B . 
O 7 HOH   79  379 560  HOH   HOH B . 
O 7 HOH   80  380 227  HOH   HOH B . 
O 7 HOH   81  381 628  HOH   HOH B . 
O 7 HOH   82  382 82   HOH   HOH B . 
O 7 HOH   83  383 53   HOH   HOH B . 
O 7 HOH   84  384 38   HOH   HOH B . 
O 7 HOH   85  385 450  HOH   HOH B . 
O 7 HOH   86  386 134  HOH   HOH B . 
O 7 HOH   87  387 130  HOH   HOH B . 
O 7 HOH   88  388 495  HOH   HOH B . 
O 7 HOH   89  389 8    HOH   HOH B . 
O 7 HOH   90  390 674  HOH   HOH B . 
O 7 HOH   91  391 805  HOH   HOH B . 
O 7 HOH   92  392 685  HOH   HOH B . 
O 7 HOH   93  393 515  HOH   HOH B . 
O 7 HOH   94  394 828  HOH   HOH B . 
O 7 HOH   95  395 732  HOH   HOH B . 
O 7 HOH   96  396 481  HOH   HOH B . 
O 7 HOH   97  397 699  HOH   HOH B . 
O 7 HOH   98  398 518  HOH   HOH B . 
O 7 HOH   99  399 590  HOH   HOH B . 
O 7 HOH   100 400 267  HOH   HOH B . 
O 7 HOH   101 401 129  HOH   HOH B . 
O 7 HOH   102 402 313  HOH   HOH B . 
O 7 HOH   103 403 377  HOH   HOH B . 
O 7 HOH   104 404 499  HOH   HOH B . 
O 7 HOH   105 405 132  HOH   HOH B . 
O 7 HOH   106 406 547  HOH   HOH B . 
O 7 HOH   107 407 309  HOH   HOH B . 
O 7 HOH   108 408 419  HOH   HOH B . 
O 7 HOH   109 409 314  HOH   HOH B . 
O 7 HOH   110 410 587  HOH   HOH B . 
O 7 HOH   111 411 173  HOH   HOH B . 
O 7 HOH   112 412 263  HOH   HOH B . 
O 7 HOH   113 413 387  HOH   HOH B . 
O 7 HOH   114 414 332  HOH   HOH B . 
O 7 HOH   115 415 40   HOH   HOH B . 
O 7 HOH   116 416 335  HOH   HOH B . 
O 7 HOH   117 417 360  HOH   HOH B . 
O 7 HOH   118 418 196  HOH   HOH B . 
O 7 HOH   119 419 670  HOH   HOH B . 
O 7 HOH   120 420 430  HOH   HOH B . 
O 7 HOH   121 421 479  HOH   HOH B . 
O 7 HOH   122 422 667  HOH   HOH B . 
O 7 HOH   123 423 464  HOH   HOH B . 
O 7 HOH   124 424 344  HOH   HOH B . 
O 7 HOH   125 425 453  HOH   HOH B . 
O 7 HOH   126 426 35   HOH   HOH B . 
O 7 HOH   127 427 485  HOH   HOH B . 
O 7 HOH   128 428 347  HOH   HOH B . 
O 7 HOH   129 429 145  HOH   HOH B . 
O 7 HOH   130 430 336  HOH   HOH B . 
O 7 HOH   131 431 30   HOH   HOH B . 
O 7 HOH   132 432 819  HOH   HOH B . 
O 7 HOH   133 433 677  HOH   HOH B . 
O 7 HOH   134 434 766  HOH   HOH B . 
O 7 HOH   135 435 310  HOH   HOH B . 
O 7 HOH   136 436 709  HOH   HOH B . 
O 7 HOH   137 437 439  HOH   HOH B . 
O 7 HOH   138 438 299  HOH   HOH B . 
O 7 HOH   139 439 317  HOH   HOH B . 
O 7 HOH   140 440 148  HOH   HOH B . 
O 7 HOH   141 441 287  HOH   HOH B . 
O 7 HOH   142 442 663  HOH   HOH B . 
O 7 HOH   143 443 187  HOH   HOH B . 
O 7 HOH   144 444 822  HOH   HOH B . 
O 7 HOH   145 445 440  HOH   HOH B . 
O 7 HOH   146 446 194  HOH   HOH B . 
O 7 HOH   147 447 401  HOH   HOH B . 
O 7 HOH   148 448 222  HOH   HOH B . 
O 7 HOH   149 449 115  HOH   HOH B . 
O 7 HOH   150 450 221  HOH   HOH B . 
O 7 HOH   151 451 502  HOH   HOH B . 
O 7 HOH   152 452 279  HOH   HOH B . 
O 7 HOH   153 453 832  HOH   HOH B . 
O 7 HOH   154 454 737  HOH   HOH B . 
O 7 HOH   155 455 226  HOH   HOH B . 
O 7 HOH   156 456 741  HOH   HOH B . 
O 7 HOH   157 457 330  HOH   HOH B . 
O 7 HOH   158 458 285  HOH   HOH B . 
O 7 HOH   159 459 569  HOH   HOH B . 
O 7 HOH   160 460 594  HOH   HOH B . 
O 7 HOH   161 461 417  HOH   HOH B . 
O 7 HOH   162 462 821  HOH   HOH B . 
O 7 HOH   163 463 301  HOH   HOH B . 
O 7 HOH   164 464 617  HOH   HOH B . 
O 7 HOH   165 465 364  HOH   HOH B . 
O 7 HOH   166 466 512  HOH   HOH B . 
O 7 HOH   167 467 498  HOH   HOH B . 
O 7 HOH   168 468 705  HOH   HOH B . 
O 7 HOH   169 469 686  HOH   HOH B . 
O 7 HOH   170 470 657  HOH   HOH B . 
O 7 HOH   171 471 329  HOH   HOH B . 
O 7 HOH   172 472 690  HOH   HOH B . 
O 7 HOH   173 473 482  HOH   HOH B . 
O 7 HOH   174 474 181  HOH   HOH B . 
O 7 HOH   175 475 684  HOH   HOH B . 
O 7 HOH   176 476 325  HOH   HOH B . 
O 7 HOH   177 477 564  HOH   HOH B . 
O 7 HOH   178 478 773  HOH   HOH B . 
O 7 HOH   179 479 343  HOH   HOH B . 
O 7 HOH   180 480 655  HOH   HOH B . 
O 7 HOH   181 481 653  HOH   HOH B . 
O 7 HOH   182 482 589  HOH   HOH B . 
O 7 HOH   183 483 582  HOH   HOH B . 
O 7 HOH   184 484 748  HOH   HOH B . 
O 7 HOH   185 485 483  HOH   HOH B . 
O 7 HOH   186 486 783  HOH   HOH B . 
O 7 HOH   187 487 618  HOH   HOH B . 
O 7 HOH   188 488 723  HOH   HOH B . 
O 7 HOH   189 489 703  HOH   HOH B . 
O 7 HOH   190 490 257  HOH   HOH B . 
O 7 HOH   191 491 646  HOH   HOH B . 
O 7 HOH   192 492 606  HOH   HOH B . 
O 7 HOH   193 493 656  HOH   HOH B . 
O 7 HOH   194 494 204  HOH   HOH B . 
O 7 HOH   195 495 793  HOH   HOH B . 
O 7 HOH   196 496 803  HOH   HOH B . 
O 7 HOH   197 497 510  HOH   HOH B . 
O 7 HOH   198 498 749  HOH   HOH B . 
O 7 HOH   199 499 661  HOH   HOH B . 
O 7 HOH   200 500 804  HOH   HOH B . 
O 7 HOH   201 501 799  HOH   HOH B . 
O 7 HOH   202 502 818  HOH   HOH B . 
O 7 HOH   203 503 477  HOH   HOH B . 
O 7 HOH   204 504 611  HOH   HOH B . 
O 7 HOH   205 505 345  HOH   HOH B . 
O 7 HOH   206 506 496  HOH   HOH B . 
P 7 HOH   1   201 682  HOH   HOH C . 
P 7 HOH   2   202 418  HOH   HOH C . 
P 7 HOH   3   203 586  HOH   HOH C . 
P 7 HOH   4   204 284  HOH   HOH C . 
P 7 HOH   5   205 404  HOH   HOH C . 
P 7 HOH   6   206 147  HOH   HOH C . 
P 7 HOH   7   207 835  HOH   HOH C . 
P 7 HOH   8   208 435  HOH   HOH C . 
P 7 HOH   9   209 787  HOH   HOH C . 
P 7 HOH   10  210 823  HOH   HOH C . 
P 7 HOH   11  211 529  HOH   HOH C . 
P 7 HOH   12  212 366  HOH   HOH C . 
P 7 HOH   13  213 86   HOH   HOH C . 
P 7 HOH   14  214 56   HOH   HOH C . 
P 7 HOH   15  215 361  HOH   HOH C . 
P 7 HOH   16  216 215  HOH   HOH C . 
P 7 HOH   17  217 506  HOH   HOH C . 
P 7 HOH   18  218 146  HOH   HOH C . 
P 7 HOH   19  219 125  HOH   HOH C . 
P 7 HOH   20  220 269  HOH   HOH C . 
P 7 HOH   21  221 72   HOH   HOH C . 
P 7 HOH   22  222 189  HOH   HOH C . 
P 7 HOH   23  223 234  HOH   HOH C . 
P 7 HOH   24  224 185  HOH   HOH C . 
P 7 HOH   25  225 251  HOH   HOH C . 
P 7 HOH   26  226 675  HOH   HOH C . 
P 7 HOH   27  227 282  HOH   HOH C . 
P 7 HOH   28  228 46   HOH   HOH C . 
P 7 HOH   29  229 447  HOH   HOH C . 
P 7 HOH   30  230 89   HOH   HOH C . 
P 7 HOH   31  231 114  HOH   HOH C . 
P 7 HOH   32  232 467  HOH   HOH C . 
P 7 HOH   33  233 191  HOH   HOH C . 
P 7 HOH   34  234 642  HOH   HOH C . 
P 7 HOH   35  235 247  HOH   HOH C . 
P 7 HOH   36  236 203  HOH   HOH C . 
P 7 HOH   37  237 141  HOH   HOH C . 
P 7 HOH   38  238 55   HOH   HOH C . 
P 7 HOH   39  239 834  HOH   HOH C . 
P 7 HOH   40  240 176  HOH   HOH C . 
P 7 HOH   41  241 24   HOH   HOH C . 
P 7 HOH   42  242 233  HOH   HOH C . 
P 7 HOH   43  243 316  HOH   HOH C . 
P 7 HOH   44  244 595  HOH   HOH C . 
P 7 HOH   45  245 427  HOH   HOH C . 
P 7 HOH   46  246 231  HOH   HOH C . 
P 7 HOH   47  247 607  HOH   HOH C . 
P 7 HOH   48  248 96   HOH   HOH C . 
P 7 HOH   49  249 3    HOH   HOH C . 
P 7 HOH   50  250 208  HOH   HOH C . 
P 7 HOH   51  251 651  HOH   HOH C . 
P 7 HOH   52  252 23   HOH   HOH C . 
P 7 HOH   53  253 774  HOH   HOH C . 
P 7 HOH   54  254 270  HOH   HOH C . 
P 7 HOH   55  255 80   HOH   HOH C . 
P 7 HOH   56  256 825  HOH   HOH C . 
P 7 HOH   57  257 220  HOH   HOH C . 
P 7 HOH   58  258 167  HOH   HOH C . 
P 7 HOH   59  259 91   HOH   HOH C . 
P 7 HOH   60  260 602  HOH   HOH C . 
P 7 HOH   61  261 108  HOH   HOH C . 
P 7 HOH   62  262 90   HOH   HOH C . 
P 7 HOH   63  263 94   HOH   HOH C . 
P 7 HOH   64  264 492  HOH   HOH C . 
P 7 HOH   65  265 6    HOH   HOH C . 
P 7 HOH   66  266 28   HOH   HOH C . 
P 7 HOH   67  267 421  HOH   HOH C . 
P 7 HOH   68  268 359  HOH   HOH C . 
P 7 HOH   69  269 205  HOH   HOH C . 
P 7 HOH   70  270 95   HOH   HOH C . 
P 7 HOH   71  271 230  HOH   HOH C . 
P 7 HOH   72  272 710  HOH   HOH C . 
P 7 HOH   73  273 34   HOH   HOH C . 
P 7 HOH   74  274 647  HOH   HOH C . 
P 7 HOH   75  275 210  HOH   HOH C . 
P 7 HOH   76  276 541  HOH   HOH C . 
P 7 HOH   77  277 468  HOH   HOH C . 
P 7 HOH   78  278 211  HOH   HOH C . 
P 7 HOH   79  279 445  HOH   HOH C . 
P 7 HOH   80  280 759  HOH   HOH C . 
P 7 HOH   81  281 249  HOH   HOH C . 
P 7 HOH   82  282 333  HOH   HOH C . 
P 7 HOH   83  283 337  HOH   HOH C . 
P 7 HOH   84  284 143  HOH   HOH C . 
P 7 HOH   85  285 85   HOH   HOH C . 
P 7 HOH   86  286 258  HOH   HOH C . 
P 7 HOH   87  287 157  HOH   HOH C . 
P 7 HOH   88  288 459  HOH   HOH C . 
P 7 HOH   89  289 296  HOH   HOH C . 
P 7 HOH   90  290 394  HOH   HOH C . 
P 7 HOH   91  291 265  HOH   HOH C . 
P 7 HOH   92  292 217  HOH   HOH C . 
P 7 HOH   93  293 381  HOH   HOH C . 
P 7 HOH   94  294 37   HOH   HOH C . 
P 7 HOH   95  295 131  HOH   HOH C . 
P 7 HOH   96  296 232  HOH   HOH C . 
P 7 HOH   97  297 41   HOH   HOH C . 
P 7 HOH   98  298 365  HOH   HOH C . 
P 7 HOH   99  299 566  HOH   HOH C . 
P 7 HOH   100 300 392  HOH   HOH C . 
P 7 HOH   101 301 149  HOH   HOH C . 
P 7 HOH   102 302 239  HOH   HOH C . 
P 7 HOH   103 303 109  HOH   HOH C . 
P 7 HOH   104 304 117  HOH   HOH C . 
P 7 HOH   105 305 237  HOH   HOH C . 
P 7 HOH   106 306 679  HOH   HOH C . 
P 7 HOH   107 307 413  HOH   HOH C . 
P 7 HOH   108 308 206  HOH   HOH C . 
P 7 HOH   109 309 769  HOH   HOH C . 
P 7 HOH   110 310 733  HOH   HOH C . 
P 7 HOH   111 311 290  HOH   HOH C . 
P 7 HOH   112 312 688  HOH   HOH C . 
P 7 HOH   113 313 494  HOH   HOH C . 
P 7 HOH   114 314 66   HOH   HOH C . 
P 7 HOH   115 315 752  HOH   HOH C . 
P 7 HOH   116 316 384  HOH   HOH C . 
P 7 HOH   117 317 297  HOH   HOH C . 
P 7 HOH   118 318 782  HOH   HOH C . 
P 7 HOH   119 319 538  HOH   HOH C . 
P 7 HOH   120 320 549  HOH   HOH C . 
P 7 HOH   121 321 836  HOH   HOH C . 
P 7 HOH   122 322 331  HOH   HOH C . 
P 7 HOH   123 323 764  HOH   HOH C . 
P 7 HOH   124 324 505  HOH   HOH C . 
P 7 HOH   125 325 533  HOH   HOH C . 
P 7 HOH   126 326 214  HOH   HOH C . 
P 7 HOH   127 327 824  HOH   HOH C . 
P 7 HOH   128 328 742  HOH   HOH C . 
P 7 HOH   129 329 395  HOH   HOH C . 
P 7 HOH   130 330 588  HOH   HOH C . 
P 7 HOH   131 331 442  HOH   HOH C . 
P 7 HOH   132 332 382  HOH   HOH C . 
P 7 HOH   133 333 422  HOH   HOH C . 
P 7 HOH   134 334 580  HOH   HOH C . 
P 7 HOH   135 335 100  HOH   HOH C . 
P 7 HOH   136 336 431  HOH   HOH C . 
P 7 HOH   137 337 49   HOH   HOH C . 
P 7 HOH   138 338 504  HOH   HOH C . 
P 7 HOH   139 339 516  HOH   HOH C . 
P 7 HOH   140 340 826  HOH   HOH C . 
P 7 HOH   141 341 412  HOH   HOH C . 
P 7 HOH   142 342 726  HOH   HOH C . 
P 7 HOH   143 343 470  HOH   HOH C . 
P 7 HOH   144 344 792  HOH   HOH C . 
P 7 HOH   145 345 446  HOH   HOH C . 
P 7 HOH   146 346 523  HOH   HOH C . 
P 7 HOH   147 347 790  HOH   HOH C . 
P 7 HOH   148 348 747  HOH   HOH C . 
P 7 HOH   149 349 658  HOH   HOH C . 
P 7 HOH   150 350 744  HOH   HOH C . 
P 7 HOH   151 351 484  HOH   HOH C . 
P 7 HOH   152 352 591  HOH   HOH C . 
P 7 HOH   153 353 827  HOH   HOH C . 
P 7 HOH   154 354 358  HOH   HOH C . 
P 7 HOH   155 355 311  HOH   HOH C . 
P 7 HOH   156 356 605  HOH   HOH C . 
P 7 HOH   157 357 443  HOH   HOH C . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.170 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BFX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     66.250 
_cell.length_a_esd                 ? 
_cell.length_b                     47.620 
_cell.length_b_esd                 ? 
_cell.length_c                     101.790 
_cell.length_c_esd                 ? 
_cell.volume                       320638.262 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9BFX 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                3 
_symmetry.space_group_name_Hall            'P 2y' 
_symmetry.space_group_name_H-M             'P 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BFX 
_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             2.16 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          43.09 
_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% PEG3350, 0.1 M Bis-Tris, pH 5.5, 150 mM sodium chloride' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-10-28 
_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   1.00004 
_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                        'ALS BEAMLINE 5.0.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.00004 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   5.0.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          18.46 
_reflns.entry_id                                       9BFX 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               50.82 
_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                                     123895 
_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                           99.07 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.43 
_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                                .04501 
_reflns.pdbx_Rpim_I_all                                .0244 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .999 
_reflns.pdbx_CC_star                                   1 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              .03766 
_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                                    1.40 
_reflns_shell.d_res_low                                     1.45 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             12065 
_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                               2.7 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               .6501 
_reflns_shell.pdbx_Rpim_I_all                               .3773 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .69 
_reflns_shell.pdbx_CC_star                                  .904 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          97.12 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  .5251 
_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                               25.31 
_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                                 9BFX 
_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                            1.40 
_refine.ls_d_res_low                             50.82 
_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                     123889 
_refine.ls_number_reflns_R_free                  6010 
_refine.ls_number_reflns_R_work                  117879 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.07 
_refine.ls_percent_reflns_R_free                 4.85 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1814 
_refine.ls_R_factor_R_free                       0.2086 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1800 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.4030 
_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                            0.1580 
_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                       1.40 
_refine_hist.d_res_low                        50.82 
_refine_hist.number_atoms_solvent             763 
_refine_hist.number_atoms_total               6183 
_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        5206 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         214 
_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' ? 0.0106  ? 5567 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.2933  ? 7535 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.1064  ? 806  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0099  ? 973  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.8915 ? 2090 ? 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' 1.40 1.42  . . 202 3659 94.17 . . . . 0.2747 . . . . . . . . . . . 0.2844 
'X-RAY DIFFRACTION' 1.42 1.43  . . 195 3868 97.64 . . . . 0.2665 . . . . . . . . . . . 0.2705 
'X-RAY DIFFRACTION' 1.43 1.45  . . 219 3920 99.50 . . . . 0.2538 . . . . . . . . . . . 0.2721 
'X-RAY DIFFRACTION' 1.45 1.47  . . 178 3908 99.88 . . . . 0.2406 . . . . . . . . . . . 0.2890 
'X-RAY DIFFRACTION' 1.47 1.49  . . 210 3964 99.98 . . . . 0.2278 . . . . . . . . . . . 0.2452 
'X-RAY DIFFRACTION' 1.49 1.51  . . 215 3906 99.85 . . . . 0.2146 . . . . . . . . . . . 0.2281 
'X-RAY DIFFRACTION' 1.51 1.53  . . 178 3949 99.71 . . . . 0.2145 . . . . . . . . . . . 0.2451 
'X-RAY DIFFRACTION' 1.53 1.55  . . 212 3905 99.71 . . . . 0.2027 . . . . . . . . . . . 0.2486 
'X-RAY DIFFRACTION' 1.55 1.58  . . 176 4005 99.88 . . . . 0.2049 . . . . . . . . . . . 0.2539 
'X-RAY DIFFRACTION' 1.58 1.60  . . 200 3927 99.71 . . . . 0.2082 . . . . . . . . . . . 0.2139 
'X-RAY DIFFRACTION' 1.60 1.63  . . 187 3956 99.88 . . . . 0.1990 . . . . . . . . . . . 0.2425 
'X-RAY DIFFRACTION' 1.63 1.66  . . 204 3939 99.83 . . . . 0.2086 . . . . . . . . . . . 0.2574 
'X-RAY DIFFRACTION' 1.66 1.69  . . 208 3941 99.74 . . . . 0.2167 . . . . . . . . . . . 0.2671 
'X-RAY DIFFRACTION' 1.69 1.73  . . 197 3928 99.61 . . . . 0.2179 . . . . . . . . . . . 0.2411 
'X-RAY DIFFRACTION' 1.73 1.76  . . 214 3939 99.74 . . . . 0.2032 . . . . . . . . . . . 0.2382 
'X-RAY DIFFRACTION' 1.76 1.80  . . 200 3934 99.81 . . . . 0.1902 . . . . . . . . . . . 0.1950 
'X-RAY DIFFRACTION' 1.80 1.85  . . 224 3931 99.43 . . . . 0.1849 . . . . . . . . . . . 0.1987 
'X-RAY DIFFRACTION' 1.85 1.90  . . 201 3941 99.14 . . . . 0.1819 . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 1.90 1.96  . . 194 3897 99.39 . . . . 0.1785 . . . . . . . . . . . 0.1948 
'X-RAY DIFFRACTION' 1.96 2.02  . . 200 3934 99.23 . . . . 0.1857 . . . . . . . . . . . 0.2052 
'X-RAY DIFFRACTION' 2.02 2.09  . . 204 3936 99.30 . . . . 0.1866 . . . . . . . . . . . 0.1909 
'X-RAY DIFFRACTION' 2.09 2.17  . . 200 3925 99.02 . . . . 0.1790 . . . . . . . . . . . 0.2176 
'X-RAY DIFFRACTION' 2.18 2.27  . . 171 4002 99.03 . . . . 0.1754 . . . . . . . . . . . 0.2202 
'X-RAY DIFFRACTION' 2.27 2.39  . . 191 3905 98.68 . . . . 0.1785 . . . . . . . . . . . 0.2134 
'X-RAY DIFFRACTION' 2.39 2.54  . . 210 3910 98.31 . . . . 0.1806 . . . . . . . . . . . 0.2137 
'X-RAY DIFFRACTION' 2.54 2.74  . . 198 3921 98.78 . . . . 0.1872 . . . . . . . . . . . 0.2312 
'X-RAY DIFFRACTION' 2.74 3.02  . . 207 3976 98.80 . . . . 0.1851 . . . . . . . . . . . 0.2133 
'X-RAY DIFFRACTION' 3.02 3.45  . . 203 3901 97.90 . . . . 0.1696 . . . . . . . . . . . 0.2370 
'X-RAY DIFFRACTION' 3.45 4.35  . . 205 3975 98.19 . . . . 0.1467 . . . . . . . . . . . 0.1702 
'X-RAY DIFFRACTION' 4.35 50.82 . . 207 4077 98.32 . . . . 0.1636 . . . . . . . . . . . 0.1691 
# 
_struct.entry_id                     9BFX 
_struct.title                        'Tri-complex of Elironrasib (RMC-6291), 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        9BFX 
_struct_keywords.text            'inhibitor, complex, small GTPase, cancer, tricomplex, SIGNALING PROTEIN-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   'SIGNALING PROTEIN/INHIBITOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L N N 6 ? 
M N N 7 ? 
N N N 7 ? 
O N N 7 ? 
P 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 9BFX A 2 ? 170 ? P01116 1 ? 169 ? 1 169 
2 2 9BFX D 2 ? 166 ? P62937 1 ? 165 ? 1 165 
3 1 9BFX B 2 ? 170 ? P01116 1 ? 169 ? 1 169 
4 2 9BFX C 2 ? 166 ? P62937 1 ? 165 ? 1 165 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9BFX SER A 1   ? UNP P01116 ?   ?   'expression tag'      0   1  
1 9BFX CYS A 13  ? UNP P01116 GLY 12  'engineered mutation' 12  2  
1 9BFX SER A 52  ? UNP P01116 CYS 51  conflict              51  3  
1 9BFX LEU A 81  ? UNP P01116 CYS 80  conflict              80  4  
1 9BFX SER A 119 ? UNP P01116 CYS 118 conflict              118 5  
2 9BFX SER D 1   ? UNP P62937 ?   ?   'expression tag'      0   6  
3 9BFX SER B 1   ? UNP P01116 ?   ?   'expression tag'      0   7  
3 9BFX CYS B 13  ? UNP P01116 GLY 12  'engineered mutation' 12  8  
3 9BFX SER B 52  ? UNP P01116 CYS 51  conflict              51  9  
3 9BFX LEU B 81  ? UNP P01116 CYS 80  conflict              80  10 
3 9BFX SER B 119 ? UNP P01116 CYS 118 conflict              118 11 
4 9BFX SER C 1   ? UNP P62937 ?   ?   'expression tag'      0   12 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,M,N 
2 1 C,D,I,J,K,L,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 16  ? ASN A 27  ? GLY A 15  ASN A 26  1 ? 12 
HELX_P HELX_P2  AA2 TYR A 65  ? GLY A 76  ? TYR A 64  GLY A 75  1 ? 12 
HELX_P HELX_P3  AA3 ASN A 87  ? ASP A 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 
HELX_P HELX_P10 AB1 GLY C 16  ? ASN C 27  ? GLY B 15  ASN B 26  1 ? 12 
HELX_P HELX_P11 AB2 TYR C 65  ? GLY C 76  ? TYR B 64  GLY B 75  1 ? 12 
HELX_P HELX_P12 AB3 ASN C 87  ? ASP C 93  ? ASN B 86  ASP B 92  1 ? 7  
HELX_P HELX_P13 AB4 ASP C 93  ? ASP C 106 ? ASP B 92  ASP B 105 1 ? 14 
HELX_P HELX_P14 AB5 ASP C 127 ? GLY C 139 ? ASP B 126 GLY B 138 1 ? 13 
HELX_P HELX_P15 AB6 GLY C 152 ? LYS C 170 ? GLY B 151 LYS B 169 1 ? 19 
HELX_P HELX_P16 AB7 VAL D 30  ? GLY D 43  ? VAL C 29  GLY C 42  1 ? 14 
HELX_P HELX_P17 AB8 THR D 120 ? ASP D 124 ? THR C 119 ASP C 123 5 ? 5  
HELX_P HELX_P18 AB9 GLY D 136 ? ARG D 145 ? GLY C 135 ARG C 144 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale none ? A CYS 13 SG  ? ? ? 1_555 G A1AOD . C15 ? ? A CYS 12  A A1AOD 203 1_555 ? ? ? ? ? ? ? 1.683 ? ? 
covale2  covale none ? C CYS 13 SG  ? ? ? 1_555 K A1AOD . C15 ? ? B CYS 12  B A1AOD 203 1_555 ? ? ? ? ? ? ? 1.678 ? ? 
metalc1  metalc ?    ? A SER 18 OG  ? ? ? 1_555 F MG    . MG  ? ? A SER 17  A MG    202 1_555 ? ? ? ? ? ? ? 2.113 ? ? 
metalc2  metalc ?    ? A THR 36 OG1 ? ? ? 1_555 F MG    . MG  ? ? A THR 35  A MG    202 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc3  metalc ?    ? E GNP .  O1G ? ? ? 1_555 F MG    . MG  ? ? A GNP 201 A MG    202 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc4  metalc ?    ? E GNP .  O1B ? ? ? 1_555 F MG    . MG  ? ? A GNP 201 A MG    202 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc5  metalc ?    ? F MG  .  MG  ? ? ? 1_555 M HOH   . O   ? ? A MG  202 A HOH   314 1_555 ? ? ? ? ? ? ? 2.057 ? ? 
metalc6  metalc ?    ? F MG  .  MG  ? ? ? 1_555 M HOH   . O   ? ? A MG  202 A HOH   365 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc7  metalc ?    ? C SER 18 OG  ? ? ? 1_555 J MG    . MG  ? ? B SER 17  B MG    202 1_555 ? ? ? ? ? ? ? 2.114 ? ? 
metalc8  metalc ?    ? C THR 36 OG1 ? ? ? 1_555 J MG    . MG  ? ? B THR 35  B MG    202 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc9  metalc ?    ? I GNP .  O1G ? ? ? 1_555 J MG    . MG  ? ? B GNP 201 B MG    202 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc10 metalc ?    ? I GNP .  O1B ? ? ? 1_555 J MG    . MG  ? ? B GNP 201 B MG    202 1_555 ? ? ? ? ? ? ? 2.066 ? ? 
metalc11 metalc ?    ? J MG  .  MG  ? ? ? 1_555 O HOH   . O   ? ? B MG  202 B HOH   327 1_555 ? ? ? ? ? ? ? 2.069 ? ? 
metalc12 metalc ?    ? J MG  .  MG  ? ? ? 1_555 O HOH   . O   ? ? B MG  202 B HOH   356 1_555 ? ? ? ? ? ? ? 2.128 ? ? 
# 
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 ? F MG . ? A MG 202 ? 1_555 OG1 ? A THR 36 ? A THR 35  ? 1_555 83.7  ? 
2  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 173.2 ? 
3  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1G ? E GNP .  ? A GNP 201 ? 1_555 90.9  ? 
4  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 92.2  ? 
5  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 175.0 ? 
6  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O1B ? E GNP .  ? A GNP 201 ? 1_555 93.4  ? 
7  OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 314 ? 1_555 84.6  ? 
8  OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 314 ? 1_555 88.9  ? 
9  O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 314 ? 1_555 91.3  ? 
10 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 314 ? 1_555 93.5  ? 
11 OG  ? A SER 18 ? A SER 17  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 365 ? 1_555 89.2  ? 
12 OG1 ? A THR 36 ? A THR 35  ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 365 ? 1_555 87.7  ? 
13 O1G ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 365 ? 1_555 94.7  ? 
14 O1B ? E GNP .  ? A GNP 201 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 365 ? 1_555 89.4  ? 
15 O   ? M HOH .  ? A HOH 314 ? 1_555 MG ? F MG . ? A MG 202 ? 1_555 O   ? M HOH .  ? A HOH 365 ? 1_555 173.1 ? 
16 OG  ? C SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 OG1 ? C THR 36 ? B THR 35  ? 1_555 83.3  ? 
17 OG  ? C SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O1G ? I GNP .  ? B GNP 201 ? 1_555 173.1 ? 
18 OG1 ? C THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O1G ? I GNP .  ? B GNP 201 ? 1_555 90.6  ? 
19 OG  ? C SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O1B ? I GNP .  ? B GNP 201 ? 1_555 91.2  ? 
20 OG1 ? C THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O1B ? I GNP .  ? B GNP 201 ? 1_555 173.8 ? 
21 O1G ? I GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O1B ? I GNP .  ? B GNP 201 ? 1_555 95.1  ? 
22 OG  ? C SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 327 ? 1_555 84.1  ? 
23 OG1 ? C THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 327 ? 1_555 89.6  ? 
24 O1G ? I GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 327 ? 1_555 92.7  ? 
25 O1B ? I GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 327 ? 1_555 92.8  ? 
26 OG  ? C SER 18 ? B SER 17  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 356 ? 1_555 89.4  ? 
27 OG1 ? C THR 36 ? B THR 35  ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 356 ? 1_555 89.3  ? 
28 O1G ? I GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 356 ? 1_555 93.7  ? 
29 O1B ? I GNP .  ? B GNP 201 ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 356 ? 1_555 87.7  ? 
30 O   ? O HOH .  ? B HOH 327 ? 1_555 MG ? J MG . ? B MG 202 ? 1_555 O   ? O HOH .  ? B HOH 356 ? 1_555 173.5 ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1AOD G . ? CYS A 13 ? A1AOD A 203 ? 1_555 CYS A 12 ? 1_555 C15 SG CYS 1 A1AOD None 'Covalent chemical modification' 
2 A1AOD K . ? CYS C 13 ? A1AOD B 203 ? 1_555 CYS B 12 ? 1_555 C15 SG CYS 1 A1AOD None 'Covalent chemical modification' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 8 ? 
AA3 ? 6 ? 
AA4 ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA2 1 2 ? anti-parallel 
AA2 2 3 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA4 7 8 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 GLU A 38  ? ILE A 47  ? GLU A 37  ILE A 46  
AA1 2 GLU A 50  ? THR A 59  ? GLU A 49  THR A 58  
AA1 3 MET A 2   ? GLY A 11  ? MET A 1   GLY A 10  
AA1 4 GLY A 78  ? ALA A 84  ? GLY A 77  ALA A 83  
AA1 5 MET A 112 ? ASN A 117 ? MET A 111 ASN A 116 
AA1 6 PHE A 142 ? GLU A 144 ? PHE A 141 GLU A 143 
AA2 1 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 
AA3 1 GLU C 38  ? ILE C 47  ? GLU B 37  ILE B 46  
AA3 2 GLU C 50  ? THR C 59  ? GLU B 49  THR B 58  
AA3 3 THR C 3   ? GLY C 11  ? THR B 2   GLY B 10  
AA3 4 GLY C 78  ? ALA C 84  ? GLY B 77  ALA B 83  
AA3 5 MET C 112 ? ASN C 117 ? MET B 111 ASN B 116 
AA3 6 PHE C 142 ? GLU C 144 ? PHE B 141 GLU B 143 
AA4 1 ARG D 56  ? ILE D 58  ? ARG C 55  ILE C 57  
AA4 2 MET D 62  ? GLY D 65  ? MET C 61  GLY C 64  
AA4 3 PHE D 113 ? CYS D 116 ? PHE C 112 CYS C 115 
AA4 4 ILE D 98  ? MET D 101 ? ILE C 97  MET C 100 
AA4 5 VAL D 129 ? VAL D 133 ? VAL C 128 VAL C 132 
AA4 6 GLU D 16  ? LEU D 25  ? GLU C 15  LEU C 24  
AA4 7 THR D 6   ? VAL D 13  ? THR C 5   VAL C 12  
AA4 8 ILE D 157 ? LEU D 165 ? ILE C 156 LEU C 164 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 43  ? N LYS A 42  O LEU A 54  ? O LEU A 53  
AA1 2 3 O ASP A 55  ? O ASP A 54  N TYR A 5   ? N TYR A 4   
AA1 3 4 N VAL A 10  ? N VAL A 9   O VAL A 82  ? O VAL A 81  
AA1 4 5 N PHE A 83  ? N PHE A 82  O ASN A 117 ? O ASN A 116 
AA1 5 6 N LEU A 114 ? N LEU A 113 O ILE A 143 ? O ILE A 142 
AA2 1 2 N 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 
AA3 1 2 N ASP C 39  ? N ASP B 38  O ASP C 58  ? O ASP B 57  
AA3 2 3 O LEU C 57  ? O LEU B 56  N LEU C 7   ? N LEU B 6   
AA3 3 4 N VAL C 10  ? N VAL B 9   O VAL C 82  ? O VAL B 81  
AA3 4 5 N PHE C 83  ? N PHE B 82  O ASN C 117 ? O ASN B 116 
AA3 5 6 N LEU C 114 ? N LEU B 113 O ILE C 143 ? O ILE B 142 
AA4 1 2 N ARG D 56  ? N ARG C 55  O GLN D 64  ? O GLN C 63  
AA4 2 3 N CYS D 63  ? N CYS C 62  O ILE D 115 ? O ILE C 114 
AA4 3 4 O CYS D 116 ? O CYS C 115 N ILE D 98  ? N ILE C 97  
AA4 4 5 N LEU D 99  ? N LEU C 98  O GLY D 131 ? O GLY C 130 
AA4 5 6 O LYS D 132 ? O LYS C 131 N GLU D 24  ? N GLU C 23  
AA4 6 7 O LEU D 18  ? O LEU C 17  N ILE D 11  ? N ILE C 10  
AA4 7 8 N ASP D 10  ? N ASP C 9   O ASP D 161 ? O ASP C 160 
# 
_pdbx_entry_details.entry_id                   9BFX 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ILE A 36  ? ? -93.34  -62.83 
2  1 ARG A 149 ? ? 79.96   -1.33  
3  1 PHE D 60  ? ? -127.86 -71.00 
4  1 LYS D 133 ? ? -95.97  -61.87 
5  1 ILE B 36  ? ? -94.70  -62.85 
6  1 LYS B 117 ? ? 72.36   35.84  
7  1 ARG B 149 ? ? 78.55   -0.90  
8  1 PHE C 60  ? ? -128.47 -71.06 
9  1 ASN C 71  ? ? -140.19 14.87  
10 1 LYS C 133 ? ? -99.00  -71.67 
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 N2 ? A A1AOD 203 ? PLANAR . 
2 1 N7 ? A A1AOD 203 ? PLANAR . 
3 1 N2 ? B A1AOD 203 ? PLANAR . 
4 1 N7 ? B A1AOD 203 ? PLANAR . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z   
2 -x,y,-z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined 19.3103849964 27.4897258031 -9.20758900338 0.106010754978 ? -0.0144195476848 ? -0.00537445466447 ? 
0.116174431899  ? 0.00248983223791 ? 0.14281580909  ? 1.6862430815  ? 0.274146210069  ? 0.0743759162623 ? 1.49967502727 ? 
-0.0700659005866 ? 1.99436485829 ? -0.103751637337  ? 0.152844566007   ? 0.0190254308431 ? -0.0918249093071 ? 0.065496482177   ? 
0.162025290071   ? -0.0440350631242 ? -0.191031123664  ? 0.0378666289867 ? 
2 'X-RAY DIFFRACTION' ? refined 13.2889170865 5.20783907103 14.8144347477  0.105665903593 ? 0.00652665825957 ? 0.0164766064026   ? 
0.0986817166639 ? 0.00796833179554 ? 0.144520533571 ? 1.74670835473 ? -0.562685963021 ? -0.811283972585 ? 2.1538431632  ? 
0.242623053499   ? 2.07729482799 ? -0.0931686716744 ? -0.022905555118  ? -0.171035533016 ? 0.0393923769431  ? 0.00217379497857 ? 
0.0822753578532  ? 0.129835339174   ? -0.0999058661026 ? 0.0799458864932 ? 
3 'X-RAY DIFFRACTION' ? refined 10.3401953666 19.9597922604 40.8066555731  0.125698602243 ? 0.0283614724231  ? -0.00513070904126 ? 
0.129413379926  ? 0.0160290055809  ? 0.129892616205 ? 1.38601754833 ? -0.041229056354 ? -0.954842921196 ? 1.52213976311 ? 
0.654759475184   ? 3.07631449267 ? -0.108564831611  ? -0.0432286711173 ? -0.10858078792  ? -0.0133933720421 ? 0.0352878670516  ? 
-0.0445332395569 ? 0.24933616016    ? 0.275964421636   ? 0.0580061201653 ? 
4 'X-RAY DIFFRACTION' ? refined 17.5909443152 42.8765523332 64.9212997796  0.140179639638 ? -0.0447824447009 ? -0.0174934358832  ? 
0.181509099301  ? 0.036884767349   ? 0.119732047353 ? 2.06313893677 ? -0.525528093085 ? 1.13645986285   ? 1.55935595927 ? 
0.196931634634   ? 2.2835709567  ? -0.155533190758  ? 0.199037340422   ? 0.142782138512  ? 0.0251439679117  ? 0.0222139214858  ? 
-0.0743632050495 ? -0.212426927429  ? 0.316901110064   ? 0.115632511772  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 A 1 A 0 ? B ?   A 201 ? ? 
;(chain 'A' and resid 0 through 201)
;
2 'X-RAY DIFFRACTION' 2 D 1 D 3 ? D 162 D 164 ? ? 
;(chain 'D' and resid 3 through 164)
;
3 'X-RAY DIFFRACTION' 3 F 1 B 0 ? G ?   B 201 ? ? 
;(chain 'B' and resid 0 through 201)
;
4 'X-RAY DIFFRACTION' 4 I 4 C 3 ? I 165 C 164 ? ? 
;(chain 'C' and resid 3 through 164)
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       506 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.73 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 168 ? A GLU 169 
2 1 Y 1 A LYS 169 ? A LYS 170 
3 1 Y 1 D SER 0   ? B SER 1   
4 1 Y 1 D MET 1   ? B MET 2   
5 1 Y 1 D VAL 2   ? B VAL 3   
6 1 Y 1 D GLU 165 ? B GLU 166 
7 1 Y 1 C GLU 165 ? D GLU 166 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AOD C1     C  N N 1   
A1AOD C10    C  N N 2   
A1AOD C11    C  N N 3   
A1AOD C12    C  N N 4   
A1AOD C13    C  N N 5   
A1AOD C14    C  N N 6   
A1AOD C15    C  N N 7   
A1AOD C16    C  N N 8   
A1AOD C17    C  N N 9   
A1AOD C18    C  N N 10  
A1AOD C19    C  N N 11  
A1AOD C2     C  N S 12  
A1AOD C20    C  N N 13  
A1AOD C21    C  N N 14  
A1AOD C22    C  N N 15  
A1AOD C23    C  N N 16  
A1AOD C24    C  N N 17  
A1AOD C25    C  N N 18  
A1AOD C26    C  N N 19  
A1AOD C27    C  N N 20  
A1AOD C28    C  N S 21  
A1AOD C29    C  N N 22  
A1AOD C3     C  N N 23  
A1AOD C30    C  N N 24  
A1AOD C31    C  Y N 25  
A1AOD C32    C  Y N 26  
A1AOD C33    C  Y N 27  
A1AOD C34    C  Y N 28  
A1AOD C35    C  Y N 29  
A1AOD C36    C  Y N 30  
A1AOD C37    C  N N 31  
A1AOD C38    C  N N 32  
A1AOD C39    C  Y N 33  
A1AOD C4     C  N N 34  
A1AOD C40    C  Y N 35  
A1AOD C41    C  Y N 36  
A1AOD C42    C  N S 37  
A1AOD C43    C  N N 38  
A1AOD C44    C  N N 39  
A1AOD C45    C  Y N 40  
A1AOD C46    C  Y N 41  
A1AOD C47    C  Y N 42  
A1AOD C48    C  Y N 43  
A1AOD C49    C  N N 44  
A1AOD C5     C  N N 45  
A1AOD C50    C  N N 46  
A1AOD C51    C  N N 47  
A1AOD C52    C  N N 48  
A1AOD C53    C  N N 49  
A1AOD C54    C  N N 50  
A1AOD C55    C  N N 51  
A1AOD C6     C  N S 52  
A1AOD C7     C  N N 53  
A1AOD C8     C  N S 54  
A1AOD C9     C  N N 55  
A1AOD F1     F  N N 56  
A1AOD N1     N  N N 57  
A1AOD N2     N  N R 58  
A1AOD N3     N  N N 59  
A1AOD N4     N  N N 60  
A1AOD N5     N  N N 61  
A1AOD N6     N  N N 62  
A1AOD N7     N  N S 63  
A1AOD N8     N  Y N 64  
A1AOD N9     N  Y N 65  
A1AOD O1     O  N N 66  
A1AOD O2     O  N N 67  
A1AOD O3     O  N N 68  
A1AOD O4     O  N N 69  
A1AOD O5     O  N N 70  
A1AOD O6     O  N N 71  
A1AOD O7     O  N N 72  
A1AOD O8     O  N N 73  
A1AOD H1     H  N N 74  
A1AOD H2     H  N N 75  
A1AOD H13    H  N N 76  
A1AOD H12    H  N N 77  
A1AOD H14    H  N N 78  
A1AOD H15    H  N N 79  
A1AOD H141   H  N N 80  
A1AOD H151   H  N N 81  
A1AOD H17    H  N N 82  
A1AOD H18    H  N N 83  
A1AOD H16    H  N N 84  
A1AOD H19    H  N N 85  
A1AOD H20    H  N N 86  
A1AOD H21    H  N N 87  
A1AOD H22    H  N N 88  
A1AOD H23    H  N N 89  
A1AOD H24    H  N N 90  
A1AOD H3     H  N N 91  
A1AOD H27    H  N N 92  
A1AOD H26    H  N N 93  
A1AOD H25    H  N N 94  
A1AOD H28    H  N N 95  
A1AOD H29    H  N N 96  
A1AOD H31    H  N N 97  
A1AOD H30    H  N N 98  
A1AOD H34    H  N N 99  
A1AOD H32    H  N N 100 
A1AOD H33    H  N N 101 
A1AOD H35    H  N N 102 
A1AOD H37    H  N N 103 
A1AOD H38    H  N N 104 
A1AOD H36    H  N N 105 
A1AOD H39    H  N N 106 
A1AOD H40    H  N N 107 
A1AOD H41    H  N N 108 
A1AOD H43    H  N N 109 
A1AOD H42    H  N N 110 
A1AOD H44    H  N N 111 
A1AOD H45    H  N N 112 
A1AOD H46    H  N N 113 
A1AOD H5     H  N N 114 
A1AOD H6     H  N N 115 
A1AOD H47    H  N N 116 
A1AOD H48    H  N N 117 
A1AOD H49    H  N N 118 
A1AOD H50    H  N N 119 
A1AOD H51    H  N N 120 
A1AOD H52    H  N N 121 
A1AOD H53    H  N N 122 
A1AOD H55    H  N N 123 
A1AOD H54    H  N N 124 
A1AOD H56    H  N N 125 
A1AOD H7     H  N N 126 
A1AOD H8     H  N N 127 
A1AOD H57    H  N N 128 
A1AOD H58    H  N N 129 
A1AOD H59    H  N N 130 
A1AOD H60    H  N N 131 
A1AOD H62    H  N N 132 
A1AOD H61    H  N N 133 
A1AOD H63    H  N N 134 
A1AOD H64    H  N N 135 
A1AOD H65    H  N N 136 
A1AOD H66    H  N N 137 
A1AOD H68    H  N N 138 
A1AOD H67    H  N N 139 
A1AOD H69    H  N N 140 
A1AOD H71    H  N N 141 
A1AOD H70    H  N N 142 
A1AOD H73    H  N N 143 
A1AOD H72    H  N N 144 
A1AOD H74    H  N N 145 
A1AOD H76    H  N N 146 
A1AOD H75    H  N N 147 
A1AOD H78    H  N N 148 
A1AOD H77    H  N N 149 
A1AOD H9     H  N N 150 
A1AOD H11    H  N N 151 
A1AOD H4     H  N N 152 
A1AOD H10    H  N N 153 
ALA   N      N  N N 154 
ALA   CA     C  N S 155 
ALA   C      C  N N 156 
ALA   O      O  N N 157 
ALA   CB     C  N N 158 
ALA   OXT    O  N N 159 
ALA   H      H  N N 160 
ALA   H2     H  N N 161 
ALA   HA     H  N N 162 
ALA   HB1    H  N N 163 
ALA   HB2    H  N N 164 
ALA   HB3    H  N N 165 
ALA   HXT    H  N N 166 
ARG   N      N  N N 167 
ARG   CA     C  N S 168 
ARG   C      C  N N 169 
ARG   O      O  N N 170 
ARG   CB     C  N N 171 
ARG   CG     C  N N 172 
ARG   CD     C  N N 173 
ARG   NE     N  N N 174 
ARG   CZ     C  N N 175 
ARG   NH1    N  N N 176 
ARG   NH2    N  N N 177 
ARG   OXT    O  N N 178 
ARG   H      H  N N 179 
ARG   H2     H  N N 180 
ARG   HA     H  N N 181 
ARG   HB2    H  N N 182 
ARG   HB3    H  N N 183 
ARG   HG2    H  N N 184 
ARG   HG3    H  N N 185 
ARG   HD2    H  N N 186 
ARG   HD3    H  N N 187 
ARG   HE     H  N N 188 
ARG   HH11   H  N N 189 
ARG   HH12   H  N N 190 
ARG   HH21   H  N N 191 
ARG   HH22   H  N N 192 
ARG   HXT    H  N N 193 
ASN   N      N  N N 194 
ASN   CA     C  N S 195 
ASN   C      C  N N 196 
ASN   O      O  N N 197 
ASN   CB     C  N N 198 
ASN   CG     C  N N 199 
ASN   OD1    O  N N 200 
ASN   ND2    N  N N 201 
ASN   OXT    O  N N 202 
ASN   H      H  N N 203 
ASN   H2     H  N N 204 
ASN   HA     H  N N 205 
ASN   HB2    H  N N 206 
ASN   HB3    H  N N 207 
ASN   HD21   H  N N 208 
ASN   HD22   H  N N 209 
ASN   HXT    H  N N 210 
ASP   N      N  N N 211 
ASP   CA     C  N S 212 
ASP   C      C  N N 213 
ASP   O      O  N N 214 
ASP   CB     C  N N 215 
ASP   CG     C  N N 216 
ASP   OD1    O  N N 217 
ASP   OD2    O  N N 218 
ASP   OXT    O  N N 219 
ASP   H      H  N N 220 
ASP   H2     H  N N 221 
ASP   HA     H  N N 222 
ASP   HB2    H  N N 223 
ASP   HB3    H  N N 224 
ASP   HD2    H  N N 225 
ASP   HXT    H  N N 226 
CL    CL     CL N N 227 
CYS   N      N  N N 228 
CYS   CA     C  N R 229 
CYS   C      C  N N 230 
CYS   O      O  N N 231 
CYS   CB     C  N N 232 
CYS   SG     S  N N 233 
CYS   OXT    O  N N 234 
CYS   H      H  N N 235 
CYS   H2     H  N N 236 
CYS   HA     H  N N 237 
CYS   HB2    H  N N 238 
CYS   HB3    H  N N 239 
CYS   HG     H  N N 240 
CYS   HXT    H  N N 241 
GLN   N      N  N N 242 
GLN   CA     C  N S 243 
GLN   C      C  N N 244 
GLN   O      O  N N 245 
GLN   CB     C  N N 246 
GLN   CG     C  N N 247 
GLN   CD     C  N N 248 
GLN   OE1    O  N N 249 
GLN   NE2    N  N N 250 
GLN   OXT    O  N N 251 
GLN   H      H  N N 252 
GLN   H2     H  N N 253 
GLN   HA     H  N N 254 
GLN   HB2    H  N N 255 
GLN   HB3    H  N N 256 
GLN   HG2    H  N N 257 
GLN   HG3    H  N N 258 
GLN   HE21   H  N N 259 
GLN   HE22   H  N N 260 
GLN   HXT    H  N N 261 
GLU   N      N  N N 262 
GLU   CA     C  N S 263 
GLU   C      C  N N 264 
GLU   O      O  N N 265 
GLU   CB     C  N N 266 
GLU   CG     C  N N 267 
GLU   CD     C  N N 268 
GLU   OE1    O  N N 269 
GLU   OE2    O  N N 270 
GLU   OXT    O  N N 271 
GLU   H      H  N N 272 
GLU   H2     H  N N 273 
GLU   HA     H  N N 274 
GLU   HB2    H  N N 275 
GLU   HB3    H  N N 276 
GLU   HG2    H  N N 277 
GLU   HG3    H  N N 278 
GLU   HE2    H  N N 279 
GLU   HXT    H  N N 280 
GLY   N      N  N N 281 
GLY   CA     C  N N 282 
GLY   C      C  N N 283 
GLY   O      O  N N 284 
GLY   OXT    O  N N 285 
GLY   H      H  N N 286 
GLY   H2     H  N N 287 
GLY   HA2    H  N N 288 
GLY   HA3    H  N N 289 
GLY   HXT    H  N N 290 
GNP   PG     P  N N 291 
GNP   O1G    O  N N 292 
GNP   O2G    O  N N 293 
GNP   O3G    O  N N 294 
GNP   N3B    N  N N 295 
GNP   PB     P  N R 296 
GNP   O1B    O  N N 297 
GNP   O2B    O  N N 298 
GNP   O3A    O  N N 299 
GNP   PA     P  N S 300 
GNP   O1A    O  N N 301 
GNP   O2A    O  N N 302 
GNP   "O5'"  O  N N 303 
GNP   "C5'"  C  N N 304 
GNP   "C4'"  C  N R 305 
GNP   "O4'"  O  N N 306 
GNP   "C3'"  C  N S 307 
GNP   "O3'"  O  N N 308 
GNP   "C2'"  C  N R 309 
GNP   "O2'"  O  N N 310 
GNP   "C1'"  C  N R 311 
GNP   N9     N  Y N 312 
GNP   C8     C  Y N 313 
GNP   N7     N  Y N 314 
GNP   C5     C  Y N 315 
GNP   C6     C  Y N 316 
GNP   O6     O  N N 317 
GNP   N1     N  Y N 318 
GNP   C2     C  Y N 319 
GNP   N2     N  N N 320 
GNP   N3     N  Y N 321 
GNP   C4     C  Y N 322 
GNP   HOG2   H  N N 323 
GNP   HOG3   H  N N 324 
GNP   HNB3   H  N N 325 
GNP   HOB2   H  N N 326 
GNP   HOA2   H  N N 327 
GNP   "H5'2" H  N N 328 
GNP   "H5'1" H  N N 329 
GNP   "H4'"  H  N N 330 
GNP   "H3'"  H  N N 331 
GNP   "HO3'" H  N N 332 
GNP   "H2'"  H  N N 333 
GNP   "HO2'" H  N N 334 
GNP   "H1'"  H  N N 335 
GNP   H8     H  N N 336 
GNP   HN1    H  N N 337 
GNP   HN21   H  N N 338 
GNP   HN22   H  N N 339 
HIS   N      N  N N 340 
HIS   CA     C  N S 341 
HIS   C      C  N N 342 
HIS   O      O  N N 343 
HIS   CB     C  N N 344 
HIS   CG     C  Y N 345 
HIS   ND1    N  Y N 346 
HIS   CD2    C  Y N 347 
HIS   CE1    C  Y N 348 
HIS   NE2    N  Y N 349 
HIS   OXT    O  N N 350 
HIS   H      H  N N 351 
HIS   H2     H  N N 352 
HIS   HA     H  N N 353 
HIS   HB2    H  N N 354 
HIS   HB3    H  N N 355 
HIS   HD1    H  N N 356 
HIS   HD2    H  N N 357 
HIS   HE1    H  N N 358 
HIS   HE2    H  N N 359 
HIS   HXT    H  N N 360 
HOH   O      O  N N 361 
HOH   H1     H  N N 362 
HOH   H2     H  N N 363 
ILE   N      N  N N 364 
ILE   CA     C  N S 365 
ILE   C      C  N N 366 
ILE   O      O  N N 367 
ILE   CB     C  N S 368 
ILE   CG1    C  N N 369 
ILE   CG2    C  N N 370 
ILE   CD1    C  N N 371 
ILE   OXT    O  N N 372 
ILE   H      H  N N 373 
ILE   H2     H  N N 374 
ILE   HA     H  N N 375 
ILE   HB     H  N N 376 
ILE   HG12   H  N N 377 
ILE   HG13   H  N N 378 
ILE   HG21   H  N N 379 
ILE   HG22   H  N N 380 
ILE   HG23   H  N N 381 
ILE   HD11   H  N N 382 
ILE   HD12   H  N N 383 
ILE   HD13   H  N N 384 
ILE   HXT    H  N N 385 
LEU   N      N  N N 386 
LEU   CA     C  N S 387 
LEU   C      C  N N 388 
LEU   O      O  N N 389 
LEU   CB     C  N N 390 
LEU   CG     C  N N 391 
LEU   CD1    C  N N 392 
LEU   CD2    C  N N 393 
LEU   OXT    O  N N 394 
LEU   H      H  N N 395 
LEU   H2     H  N N 396 
LEU   HA     H  N N 397 
LEU   HB2    H  N N 398 
LEU   HB3    H  N N 399 
LEU   HG     H  N N 400 
LEU   HD11   H  N N 401 
LEU   HD12   H  N N 402 
LEU   HD13   H  N N 403 
LEU   HD21   H  N N 404 
LEU   HD22   H  N N 405 
LEU   HD23   H  N N 406 
LEU   HXT    H  N N 407 
LYS   N      N  N N 408 
LYS   CA     C  N S 409 
LYS   C      C  N N 410 
LYS   O      O  N N 411 
LYS   CB     C  N N 412 
LYS   CG     C  N N 413 
LYS   CD     C  N N 414 
LYS   CE     C  N N 415 
LYS   NZ     N  N N 416 
LYS   OXT    O  N N 417 
LYS   H      H  N N 418 
LYS   H2     H  N N 419 
LYS   HA     H  N N 420 
LYS   HB2    H  N N 421 
LYS   HB3    H  N N 422 
LYS   HG2    H  N N 423 
LYS   HG3    H  N N 424 
LYS   HD2    H  N N 425 
LYS   HD3    H  N N 426 
LYS   HE2    H  N N 427 
LYS   HE3    H  N N 428 
LYS   HZ1    H  N N 429 
LYS   HZ2    H  N N 430 
LYS   HZ3    H  N N 431 
LYS   HXT    H  N N 432 
MET   N      N  N N 433 
MET   CA     C  N S 434 
MET   C      C  N N 435 
MET   O      O  N N 436 
MET   CB     C  N N 437 
MET   CG     C  N N 438 
MET   SD     S  N N 439 
MET   CE     C  N N 440 
MET   OXT    O  N N 441 
MET   H      H  N N 442 
MET   H2     H  N N 443 
MET   HA     H  N N 444 
MET   HB2    H  N N 445 
MET   HB3    H  N N 446 
MET   HG2    H  N N 447 
MET   HG3    H  N N 448 
MET   HE1    H  N N 449 
MET   HE2    H  N N 450 
MET   HE3    H  N N 451 
MET   HXT    H  N N 452 
MG    MG     MG N N 453 
PHE   N      N  N N 454 
PHE   CA     C  N S 455 
PHE   C      C  N N 456 
PHE   O      O  N N 457 
PHE   CB     C  N N 458 
PHE   CG     C  Y N 459 
PHE   CD1    C  Y N 460 
PHE   CD2    C  Y N 461 
PHE   CE1    C  Y N 462 
PHE   CE2    C  Y N 463 
PHE   CZ     C  Y N 464 
PHE   OXT    O  N N 465 
PHE   H      H  N N 466 
PHE   H2     H  N N 467 
PHE   HA     H  N N 468 
PHE   HB2    H  N N 469 
PHE   HB3    H  N N 470 
PHE   HD1    H  N N 471 
PHE   HD2    H  N N 472 
PHE   HE1    H  N N 473 
PHE   HE2    H  N N 474 
PHE   HZ     H  N N 475 
PHE   HXT    H  N N 476 
PRO   N      N  N N 477 
PRO   CA     C  N S 478 
PRO   C      C  N N 479 
PRO   O      O  N N 480 
PRO   CB     C  N N 481 
PRO   CG     C  N N 482 
PRO   CD     C  N N 483 
PRO   OXT    O  N N 484 
PRO   H      H  N N 485 
PRO   HA     H  N N 486 
PRO   HB2    H  N N 487 
PRO   HB3    H  N N 488 
PRO   HG2    H  N N 489 
PRO   HG3    H  N N 490 
PRO   HD2    H  N N 491 
PRO   HD3    H  N N 492 
PRO   HXT    H  N N 493 
SER   N      N  N N 494 
SER   CA     C  N S 495 
SER   C      C  N N 496 
SER   O      O  N N 497 
SER   CB     C  N N 498 
SER   OG     O  N N 499 
SER   OXT    O  N N 500 
SER   H      H  N N 501 
SER   H2     H  N N 502 
SER   HA     H  N N 503 
SER   HB2    H  N N 504 
SER   HB3    H  N N 505 
SER   HG     H  N N 506 
SER   HXT    H  N N 507 
THR   N      N  N N 508 
THR   CA     C  N S 509 
THR   C      C  N N 510 
THR   O      O  N N 511 
THR   CB     C  N R 512 
THR   OG1    O  N N 513 
THR   CG2    C  N N 514 
THR   OXT    O  N N 515 
THR   H      H  N N 516 
THR   H2     H  N N 517 
THR   HA     H  N N 518 
THR   HB     H  N N 519 
THR   HG1    H  N N 520 
THR   HG21   H  N N 521 
THR   HG22   H  N N 522 
THR   HG23   H  N N 523 
THR   HXT    H  N N 524 
TRP   N      N  N N 525 
TRP   CA     C  N S 526 
TRP   C      C  N N 527 
TRP   O      O  N N 528 
TRP   CB     C  N N 529 
TRP   CG     C  Y N 530 
TRP   CD1    C  Y N 531 
TRP   CD2    C  Y N 532 
TRP   NE1    N  Y N 533 
TRP   CE2    C  Y N 534 
TRP   CE3    C  Y N 535 
TRP   CZ2    C  Y N 536 
TRP   CZ3    C  Y N 537 
TRP   CH2    C  Y N 538 
TRP   OXT    O  N N 539 
TRP   H      H  N N 540 
TRP   H2     H  N N 541 
TRP   HA     H  N N 542 
TRP   HB2    H  N N 543 
TRP   HB3    H  N N 544 
TRP   HD1    H  N N 545 
TRP   HE1    H  N N 546 
TRP   HE3    H  N N 547 
TRP   HZ2    H  N N 548 
TRP   HZ3    H  N N 549 
TRP   HH2    H  N N 550 
TRP   HXT    H  N N 551 
TYR   N      N  N N 552 
TYR   CA     C  N S 553 
TYR   C      C  N N 554 
TYR   O      O  N N 555 
TYR   CB     C  N N 556 
TYR   CG     C  Y N 557 
TYR   CD1    C  Y N 558 
TYR   CD2    C  Y N 559 
TYR   CE1    C  Y N 560 
TYR   CE2    C  Y N 561 
TYR   CZ     C  Y N 562 
TYR   OH     O  N N 563 
TYR   OXT    O  N N 564 
TYR   H      H  N N 565 
TYR   H2     H  N N 566 
TYR   HA     H  N N 567 
TYR   HB2    H  N N 568 
TYR   HB3    H  N N 569 
TYR   HD1    H  N N 570 
TYR   HD2    H  N N 571 
TYR   HE1    H  N N 572 
TYR   HE2    H  N N 573 
TYR   HH     H  N N 574 
TYR   HXT    H  N N 575 
VAL   N      N  N N 576 
VAL   CA     C  N S 577 
VAL   C      C  N N 578 
VAL   O      O  N N 579 
VAL   CB     C  N N 580 
VAL   CG1    C  N N 581 
VAL   CG2    C  N N 582 
VAL   OXT    O  N N 583 
VAL   H      H  N N 584 
VAL   H2     H  N N 585 
VAL   HA     H  N N 586 
VAL   HB     H  N N 587 
VAL   HG11   H  N N 588 
VAL   HG12   H  N N 589 
VAL   HG13   H  N N 590 
VAL   HG21   H  N N 591 
VAL   HG22   H  N N 592 
VAL   HG23   H  N N 593 
VAL   HXT    H  N N 594 
# 
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 
A1AOD C1    C2     sing N N 1   
A1AOD C1    C4     sing N N 2   
A1AOD C2    N1     sing N N 3   
A1AOD C2    C54    sing N N 4   
A1AOD N1    N2     sing N N 5   
A1AOD N2    C3     sing N N 6   
A1AOD N2    C5     sing N N 7   
A1AOD C3    C4     sing N N 8   
A1AOD C5    O1     doub N N 9   
A1AOD C5    C6     sing N N 10  
A1AOD C6    N3     sing N N 11  
A1AOD C6    C27    sing N N 12  
A1AOD N3    C7     sing N N 13  
A1AOD C7    C8     sing N N 14  
A1AOD C7    O4     doub N N 15  
A1AOD C8    N4     sing N N 16  
A1AOD C8    C24    sing N N 17  
A1AOD N4    C9     sing N N 18  
A1AOD N4    C23    sing N N 19  
A1AOD C9    C10    sing N N 20  
A1AOD C9    O3     doub N N 21  
A1AOD C10   F1     sing N N 22  
A1AOD C10   C11    sing N N 23  
A1AOD C10   C22    sing N N 24  
A1AOD C11   C12    sing N N 25  
A1AOD C12   N5     sing N N 26  
A1AOD N5    C13    sing N N 27  
A1AOD N5    C21    sing N N 28  
A1AOD C13   C14    sing N N 29  
A1AOD C13   O2     doub N N 30  
A1AOD C14   C15    doub N E 31  
A1AOD C15   C16    sing N N 32  
A1AOD C16   N6     sing N N 33  
A1AOD C16   C19    sing N N 34  
A1AOD C16   C20    sing N N 35  
A1AOD N6    C17    sing N N 36  
A1AOD N6    C18    sing N N 37  
A1AOD C21   C22    sing N N 38  
A1AOD C24   C25    sing N N 39  
A1AOD C24   C26    sing N N 40  
A1AOD C27   C28    sing N N 41  
A1AOD C28   O5     sing N N 42  
A1AOD C28   C55    sing N N 43  
A1AOD O5    C29    sing N N 44  
A1AOD C29   C30    sing N N 45  
A1AOD C30   N7     sing N N 46  
A1AOD N7    C31    sing N N 47  
A1AOD N7    C55    sing N N 48  
A1AOD C31   C32    doub Y N 49  
A1AOD C31   C36    sing Y N 50  
A1AOD C32   C33    sing Y N 51  
A1AOD C33   C34    doub Y N 52  
A1AOD C33   C48    sing Y N 53  
A1AOD C34   C35    sing Y N 54  
A1AOD C34   N8     sing Y N 55  
A1AOD C35   C36    doub Y N 56  
A1AOD N8    C37    sing N N 57  
A1AOD N8    C39    sing Y N 58  
A1AOD C37   C38    sing N N 59  
A1AOD C39   C40    sing N N 60  
A1AOD C39   C48    doub Y N 61  
A1AOD C40   C41    doub Y N 62  
A1AOD C40   C47    sing Y N 63  
A1AOD C41   C42    sing N N 64  
A1AOD C41   N9     sing Y N 65  
A1AOD C42   O6     sing N N 66  
A1AOD C42   C44    sing N N 67  
A1AOD O6    C43    sing N N 68  
A1AOD N9    C45    doub Y N 69  
A1AOD C45   C46    sing Y N 70  
A1AOD C46   C47    doub Y N 71  
A1AOD C48   C49    sing N N 72  
A1AOD C49   C50    sing N N 73  
A1AOD C50   C51    sing N N 74  
A1AOD C50   C52    sing N N 75  
A1AOD C50   C53    sing N N 76  
A1AOD C53   O7     sing N N 77  
A1AOD O7    C54    sing N N 78  
A1AOD C54   O8     doub N N 79  
A1AOD C1    H1     sing N N 80  
A1AOD C1    H2     sing N N 81  
A1AOD C11   H13    sing N N 82  
A1AOD C11   H12    sing N N 83  
A1AOD C12   H14    sing N N 84  
A1AOD C12   H15    sing N N 85  
A1AOD C14   H141   sing N N 86  
A1AOD C15   H151   sing N N 87  
A1AOD C17   H17    sing N N 88  
A1AOD C17   H18    sing N N 89  
A1AOD C17   H16    sing N N 90  
A1AOD C18   H19    sing N N 91  
A1AOD C18   H20    sing N N 92  
A1AOD C18   H21    sing N N 93  
A1AOD C19   H22    sing N N 94  
A1AOD C19   H23    sing N N 95  
A1AOD C19   H24    sing N N 96  
A1AOD C2    H3     sing N N 97  
A1AOD C20   H27    sing N N 98  
A1AOD C20   H26    sing N N 99  
A1AOD C20   H25    sing N N 100 
A1AOD C21   H28    sing N N 101 
A1AOD C21   H29    sing N N 102 
A1AOD C22   H31    sing N N 103 
A1AOD C22   H30    sing N N 104 
A1AOD C23   H34    sing N N 105 
A1AOD C23   H32    sing N N 106 
A1AOD C23   H33    sing N N 107 
A1AOD C24   H35    sing N N 108 
A1AOD C25   H37    sing N N 109 
A1AOD C25   H38    sing N N 110 
A1AOD C25   H36    sing N N 111 
A1AOD C26   H39    sing N N 112 
A1AOD C26   H40    sing N N 113 
A1AOD C26   H41    sing N N 114 
A1AOD C27   H43    sing N N 115 
A1AOD C27   H42    sing N N 116 
A1AOD C28   H44    sing N N 117 
A1AOD C29   H45    sing N N 118 
A1AOD C29   H46    sing N N 119 
A1AOD C3    H5     sing N N 120 
A1AOD C3    H6     sing N N 121 
A1AOD C30   H47    sing N N 122 
A1AOD C30   H48    sing N N 123 
A1AOD C32   H49    sing N N 124 
A1AOD C35   H50    sing N N 125 
A1AOD C36   H51    sing N N 126 
A1AOD C37   H52    sing N N 127 
A1AOD C37   H53    sing N N 128 
A1AOD C38   H55    sing N N 129 
A1AOD C38   H54    sing N N 130 
A1AOD C38   H56    sing N N 131 
A1AOD C4    H7     sing N N 132 
A1AOD C4    H8     sing N N 133 
A1AOD C42   H57    sing N N 134 
A1AOD C43   H58    sing N N 135 
A1AOD C43   H59    sing N N 136 
A1AOD C43   H60    sing N N 137 
A1AOD C44   H62    sing N N 138 
A1AOD C44   H61    sing N N 139 
A1AOD C44   H63    sing N N 140 
A1AOD C45   H64    sing N N 141 
A1AOD C46   H65    sing N N 142 
A1AOD C47   H66    sing N N 143 
A1AOD C49   H68    sing N N 144 
A1AOD C49   H67    sing N N 145 
A1AOD C51   H69    sing N N 146 
A1AOD C51   H71    sing N N 147 
A1AOD C51   H70    sing N N 148 
A1AOD C52   H73    sing N N 149 
A1AOD C52   H72    sing N N 150 
A1AOD C52   H74    sing N N 151 
A1AOD C53   H76    sing N N 152 
A1AOD C53   H75    sing N N 153 
A1AOD C55   H78    sing N N 154 
A1AOD C55   H77    sing N N 155 
A1AOD C6    H9     sing N N 156 
A1AOD C8    H11    sing N N 157 
A1AOD N1    H4     sing N N 158 
A1AOD N3    H10    sing N N 159 
ALA   N     CA     sing N N 160 
ALA   N     H      sing N N 161 
ALA   N     H2     sing N N 162 
ALA   CA    C      sing N N 163 
ALA   CA    CB     sing N N 164 
ALA   CA    HA     sing N N 165 
ALA   C     O      doub N N 166 
ALA   C     OXT    sing N N 167 
ALA   CB    HB1    sing N N 168 
ALA   CB    HB2    sing N N 169 
ALA   CB    HB3    sing N N 170 
ALA   OXT   HXT    sing N N 171 
ARG   N     CA     sing N N 172 
ARG   N     H      sing N N 173 
ARG   N     H2     sing N N 174 
ARG   CA    C      sing N N 175 
ARG   CA    CB     sing N N 176 
ARG   CA    HA     sing N N 177 
ARG   C     O      doub N N 178 
ARG   C     OXT    sing N N 179 
ARG   CB    CG     sing N N 180 
ARG   CB    HB2    sing N N 181 
ARG   CB    HB3    sing N N 182 
ARG   CG    CD     sing N N 183 
ARG   CG    HG2    sing N N 184 
ARG   CG    HG3    sing N N 185 
ARG   CD    NE     sing N N 186 
ARG   CD    HD2    sing N N 187 
ARG   CD    HD3    sing N N 188 
ARG   NE    CZ     sing N N 189 
ARG   NE    HE     sing N N 190 
ARG   CZ    NH1    sing N N 191 
ARG   CZ    NH2    doub N N 192 
ARG   NH1   HH11   sing N N 193 
ARG   NH1   HH12   sing N N 194 
ARG   NH2   HH21   sing N N 195 
ARG   NH2   HH22   sing N N 196 
ARG   OXT   HXT    sing N N 197 
ASN   N     CA     sing N N 198 
ASN   N     H      sing N N 199 
ASN   N     H2     sing N N 200 
ASN   CA    C      sing N N 201 
ASN   CA    CB     sing N N 202 
ASN   CA    HA     sing N N 203 
ASN   C     O      doub N N 204 
ASN   C     OXT    sing N N 205 
ASN   CB    CG     sing N N 206 
ASN   CB    HB2    sing N N 207 
ASN   CB    HB3    sing N N 208 
ASN   CG    OD1    doub N N 209 
ASN   CG    ND2    sing N N 210 
ASN   ND2   HD21   sing N N 211 
ASN   ND2   HD22   sing N N 212 
ASN   OXT   HXT    sing N N 213 
ASP   N     CA     sing N N 214 
ASP   N     H      sing N N 215 
ASP   N     H2     sing N N 216 
ASP   CA    C      sing N N 217 
ASP   CA    CB     sing N N 218 
ASP   CA    HA     sing N N 219 
ASP   C     O      doub N N 220 
ASP   C     OXT    sing N N 221 
ASP   CB    CG     sing N N 222 
ASP   CB    HB2    sing N N 223 
ASP   CB    HB3    sing N N 224 
ASP   CG    OD1    doub N N 225 
ASP   CG    OD2    sing N N 226 
ASP   OD2   HD2    sing N N 227 
ASP   OXT   HXT    sing N N 228 
CYS   N     CA     sing N N 229 
CYS   N     H      sing N N 230 
CYS   N     H2     sing N N 231 
CYS   CA    C      sing N N 232 
CYS   CA    CB     sing N N 233 
CYS   CA    HA     sing N N 234 
CYS   C     O      doub N N 235 
CYS   C     OXT    sing N N 236 
CYS   CB    SG     sing N N 237 
CYS   CB    HB2    sing N N 238 
CYS   CB    HB3    sing N N 239 
CYS   SG    HG     sing N N 240 
CYS   OXT   HXT    sing N N 241 
GLN   N     CA     sing N N 242 
GLN   N     H      sing N N 243 
GLN   N     H2     sing N N 244 
GLN   CA    C      sing N N 245 
GLN   CA    CB     sing N N 246 
GLN   CA    HA     sing N N 247 
GLN   C     O      doub N N 248 
GLN   C     OXT    sing N N 249 
GLN   CB    CG     sing N N 250 
GLN   CB    HB2    sing N N 251 
GLN   CB    HB3    sing N N 252 
GLN   CG    CD     sing N N 253 
GLN   CG    HG2    sing N N 254 
GLN   CG    HG3    sing N N 255 
GLN   CD    OE1    doub N N 256 
GLN   CD    NE2    sing N N 257 
GLN   NE2   HE21   sing N N 258 
GLN   NE2   HE22   sing N N 259 
GLN   OXT   HXT    sing N N 260 
GLU   N     CA     sing N N 261 
GLU   N     H      sing N N 262 
GLU   N     H2     sing N N 263 
GLU   CA    C      sing N N 264 
GLU   CA    CB     sing N N 265 
GLU   CA    HA     sing N N 266 
GLU   C     O      doub N N 267 
GLU   C     OXT    sing N N 268 
GLU   CB    CG     sing N N 269 
GLU   CB    HB2    sing N N 270 
GLU   CB    HB3    sing N N 271 
GLU   CG    CD     sing N N 272 
GLU   CG    HG2    sing N N 273 
GLU   CG    HG3    sing N N 274 
GLU   CD    OE1    doub N N 275 
GLU   CD    OE2    sing N N 276 
GLU   OE2   HE2    sing N N 277 
GLU   OXT   HXT    sing N N 278 
GLY   N     CA     sing N N 279 
GLY   N     H      sing N N 280 
GLY   N     H2     sing N N 281 
GLY   CA    C      sing N N 282 
GLY   CA    HA2    sing N N 283 
GLY   CA    HA3    sing N N 284 
GLY   C     O      doub N N 285 
GLY   C     OXT    sing N N 286 
GLY   OXT   HXT    sing N N 287 
GNP   PG    O1G    doub N N 288 
GNP   PG    O2G    sing N N 289 
GNP   PG    O3G    sing N N 290 
GNP   PG    N3B    sing N N 291 
GNP   O2G   HOG2   sing N N 292 
GNP   O3G   HOG3   sing N N 293 
GNP   N3B   PB     sing N N 294 
GNP   N3B   HNB3   sing N N 295 
GNP   PB    O1B    doub N N 296 
GNP   PB    O2B    sing N N 297 
GNP   PB    O3A    sing N N 298 
GNP   O2B   HOB2   sing N N 299 
GNP   O3A   PA     sing N N 300 
GNP   PA    O1A    doub N N 301 
GNP   PA    O2A    sing N N 302 
GNP   PA    "O5'"  sing N N 303 
GNP   O2A   HOA2   sing N N 304 
GNP   "O5'" "C5'"  sing N N 305 
GNP   "C5'" "C4'"  sing N N 306 
GNP   "C5'" "H5'2" sing N N 307 
GNP   "C5'" "H5'1" sing N N 308 
GNP   "C4'" "O4'"  sing N N 309 
GNP   "C4'" "C3'"  sing N N 310 
GNP   "C4'" "H4'"  sing N N 311 
GNP   "O4'" "C1'"  sing N N 312 
GNP   "C3'" "O3'"  sing N N 313 
GNP   "C3'" "C2'"  sing N N 314 
GNP   "C3'" "H3'"  sing N N 315 
GNP   "O3'" "HO3'" sing N N 316 
GNP   "C2'" "O2'"  sing N N 317 
GNP   "C2'" "C1'"  sing N N 318 
GNP   "C2'" "H2'"  sing N N 319 
GNP   "O2'" "HO2'" sing N N 320 
GNP   "C1'" N9     sing N N 321 
GNP   "C1'" "H1'"  sing N N 322 
GNP   N9    C8     sing Y N 323 
GNP   N9    C4     sing Y N 324 
GNP   C8    N7     doub Y N 325 
GNP   C8    H8     sing N N 326 
GNP   N7    C5     sing Y N 327 
GNP   C5    C6     sing Y N 328 
GNP   C5    C4     doub Y N 329 
GNP   C6    O6     doub N N 330 
GNP   C6    N1     sing Y N 331 
GNP   N1    C2     sing Y N 332 
GNP   N1    HN1    sing N N 333 
GNP   C2    N2     sing N N 334 
GNP   C2    N3     doub Y N 335 
GNP   N2    HN21   sing N N 336 
GNP   N2    HN22   sing N N 337 
GNP   N3    C4     sing Y N 338 
HIS   N     CA     sing N N 339 
HIS   N     H      sing N N 340 
HIS   N     H2     sing N N 341 
HIS   CA    C      sing N N 342 
HIS   CA    CB     sing N N 343 
HIS   CA    HA     sing N N 344 
HIS   C     O      doub N N 345 
HIS   C     OXT    sing N N 346 
HIS   CB    CG     sing N N 347 
HIS   CB    HB2    sing N N 348 
HIS   CB    HB3    sing N N 349 
HIS   CG    ND1    sing Y N 350 
HIS   CG    CD2    doub Y N 351 
HIS   ND1   CE1    doub Y N 352 
HIS   ND1   HD1    sing N N 353 
HIS   CD2   NE2    sing Y N 354 
HIS   CD2   HD2    sing N N 355 
HIS   CE1   NE2    sing Y N 356 
HIS   CE1   HE1    sing N N 357 
HIS   NE2   HE2    sing N N 358 
HIS   OXT   HXT    sing N N 359 
HOH   O     H1     sing N N 360 
HOH   O     H2     sing N N 361 
ILE   N     CA     sing N N 362 
ILE   N     H      sing N N 363 
ILE   N     H2     sing N N 364 
ILE   CA    C      sing N N 365 
ILE   CA    CB     sing N N 366 
ILE   CA    HA     sing N N 367 
ILE   C     O      doub N N 368 
ILE   C     OXT    sing N N 369 
ILE   CB    CG1    sing N N 370 
ILE   CB    CG2    sing N N 371 
ILE   CB    HB     sing N N 372 
ILE   CG1   CD1    sing N N 373 
ILE   CG1   HG12   sing N N 374 
ILE   CG1   HG13   sing N N 375 
ILE   CG2   HG21   sing N N 376 
ILE   CG2   HG22   sing N N 377 
ILE   CG2   HG23   sing N N 378 
ILE   CD1   HD11   sing N N 379 
ILE   CD1   HD12   sing N N 380 
ILE   CD1   HD13   sing N N 381 
ILE   OXT   HXT    sing N N 382 
LEU   N     CA     sing N N 383 
LEU   N     H      sing N N 384 
LEU   N     H2     sing N N 385 
LEU   CA    C      sing N N 386 
LEU   CA    CB     sing N N 387 
LEU   CA    HA     sing N N 388 
LEU   C     O      doub N N 389 
LEU   C     OXT    sing N N 390 
LEU   CB    CG     sing N N 391 
LEU   CB    HB2    sing N N 392 
LEU   CB    HB3    sing N N 393 
LEU   CG    CD1    sing N N 394 
LEU   CG    CD2    sing N N 395 
LEU   CG    HG     sing N N 396 
LEU   CD1   HD11   sing N N 397 
LEU   CD1   HD12   sing N N 398 
LEU   CD1   HD13   sing N N 399 
LEU   CD2   HD21   sing N N 400 
LEU   CD2   HD22   sing N N 401 
LEU   CD2   HD23   sing N N 402 
LEU   OXT   HXT    sing N N 403 
LYS   N     CA     sing N N 404 
LYS   N     H      sing N N 405 
LYS   N     H2     sing N N 406 
LYS   CA    C      sing N N 407 
LYS   CA    CB     sing N N 408 
LYS   CA    HA     sing N N 409 
LYS   C     O      doub N N 410 
LYS   C     OXT    sing N N 411 
LYS   CB    CG     sing N N 412 
LYS   CB    HB2    sing N N 413 
LYS   CB    HB3    sing N N 414 
LYS   CG    CD     sing N N 415 
LYS   CG    HG2    sing N N 416 
LYS   CG    HG3    sing N N 417 
LYS   CD    CE     sing N N 418 
LYS   CD    HD2    sing N N 419 
LYS   CD    HD3    sing N N 420 
LYS   CE    NZ     sing N N 421 
LYS   CE    HE2    sing N N 422 
LYS   CE    HE3    sing N N 423 
LYS   NZ    HZ1    sing N N 424 
LYS   NZ    HZ2    sing N N 425 
LYS   NZ    HZ3    sing N N 426 
LYS   OXT   HXT    sing N N 427 
MET   N     CA     sing N N 428 
MET   N     H      sing N N 429 
MET   N     H2     sing N N 430 
MET   CA    C      sing N N 431 
MET   CA    CB     sing N N 432 
MET   CA    HA     sing N N 433 
MET   C     O      doub N N 434 
MET   C     OXT    sing N N 435 
MET   CB    CG     sing N N 436 
MET   CB    HB2    sing N N 437 
MET   CB    HB3    sing N N 438 
MET   CG    SD     sing N N 439 
MET   CG    HG2    sing N N 440 
MET   CG    HG3    sing N N 441 
MET   SD    CE     sing N N 442 
MET   CE    HE1    sing N N 443 
MET   CE    HE2    sing N N 444 
MET   CE    HE3    sing N N 445 
MET   OXT   HXT    sing N N 446 
PHE   N     CA     sing N N 447 
PHE   N     H      sing N N 448 
PHE   N     H2     sing N N 449 
PHE   CA    C      sing N N 450 
PHE   CA    CB     sing N N 451 
PHE   CA    HA     sing N N 452 
PHE   C     O      doub N N 453 
PHE   C     OXT    sing N N 454 
PHE   CB    CG     sing N N 455 
PHE   CB    HB2    sing N N 456 
PHE   CB    HB3    sing N N 457 
PHE   CG    CD1    doub Y N 458 
PHE   CG    CD2    sing Y N 459 
PHE   CD1   CE1    sing Y N 460 
PHE   CD1   HD1    sing N N 461 
PHE   CD2   CE2    doub Y N 462 
PHE   CD2   HD2    sing N N 463 
PHE   CE1   CZ     doub Y N 464 
PHE   CE1   HE1    sing N N 465 
PHE   CE2   CZ     sing Y N 466 
PHE   CE2   HE2    sing N N 467 
PHE   CZ    HZ     sing N N 468 
PHE   OXT   HXT    sing N N 469 
PRO   N     CA     sing N N 470 
PRO   N     CD     sing N N 471 
PRO   N     H      sing N N 472 
PRO   CA    C      sing N N 473 
PRO   CA    CB     sing N N 474 
PRO   CA    HA     sing N N 475 
PRO   C     O      doub N N 476 
PRO   C     OXT    sing N N 477 
PRO   CB    CG     sing N N 478 
PRO   CB    HB2    sing N N 479 
PRO   CB    HB3    sing N N 480 
PRO   CG    CD     sing N N 481 
PRO   CG    HG2    sing N N 482 
PRO   CG    HG3    sing N N 483 
PRO   CD    HD2    sing N N 484 
PRO   CD    HD3    sing N N 485 
PRO   OXT   HXT    sing N N 486 
SER   N     CA     sing N N 487 
SER   N     H      sing N N 488 
SER   N     H2     sing N N 489 
SER   CA    C      sing N N 490 
SER   CA    CB     sing N N 491 
SER   CA    HA     sing N N 492 
SER   C     O      doub N N 493 
SER   C     OXT    sing N N 494 
SER   CB    OG     sing N N 495 
SER   CB    HB2    sing N N 496 
SER   CB    HB3    sing N N 497 
SER   OG    HG     sing N N 498 
SER   OXT   HXT    sing N N 499 
THR   N     CA     sing N N 500 
THR   N     H      sing N N 501 
THR   N     H2     sing N N 502 
THR   CA    C      sing N N 503 
THR   CA    CB     sing N N 504 
THR   CA    HA     sing N N 505 
THR   C     O      doub N N 506 
THR   C     OXT    sing N N 507 
THR   CB    OG1    sing N N 508 
THR   CB    CG2    sing N N 509 
THR   CB    HB     sing N N 510 
THR   OG1   HG1    sing N N 511 
THR   CG2   HG21   sing N N 512 
THR   CG2   HG22   sing N N 513 
THR   CG2   HG23   sing N N 514 
THR   OXT   HXT    sing N N 515 
TRP   N     CA     sing N N 516 
TRP   N     H      sing N N 517 
TRP   N     H2     sing N N 518 
TRP   CA    C      sing N N 519 
TRP   CA    CB     sing N N 520 
TRP   CA    HA     sing N N 521 
TRP   C     O      doub N N 522 
TRP   C     OXT    sing N N 523 
TRP   CB    CG     sing N N 524 
TRP   CB    HB2    sing N N 525 
TRP   CB    HB3    sing N N 526 
TRP   CG    CD1    doub Y N 527 
TRP   CG    CD2    sing Y N 528 
TRP   CD1   NE1    sing Y N 529 
TRP   CD1   HD1    sing N N 530 
TRP   CD2   CE2    doub Y N 531 
TRP   CD2   CE3    sing Y N 532 
TRP   NE1   CE2    sing Y N 533 
TRP   NE1   HE1    sing N N 534 
TRP   CE2   CZ2    sing Y N 535 
TRP   CE3   CZ3    doub Y N 536 
TRP   CE3   HE3    sing N N 537 
TRP   CZ2   CH2    doub Y N 538 
TRP   CZ2   HZ2    sing N N 539 
TRP   CZ3   CH2    sing Y N 540 
TRP   CZ3   HZ3    sing N N 541 
TRP   CH2   HH2    sing N N 542 
TRP   OXT   HXT    sing N N 543 
TYR   N     CA     sing N N 544 
TYR   N     H      sing N N 545 
TYR   N     H2     sing N N 546 
TYR   CA    C      sing N N 547 
TYR   CA    CB     sing N N 548 
TYR   CA    HA     sing N N 549 
TYR   C     O      doub N N 550 
TYR   C     OXT    sing N N 551 
TYR   CB    CG     sing N N 552 
TYR   CB    HB2    sing N N 553 
TYR   CB    HB3    sing N N 554 
TYR   CG    CD1    doub Y N 555 
TYR   CG    CD2    sing Y N 556 
TYR   CD1   CE1    sing Y N 557 
TYR   CD1   HD1    sing N N 558 
TYR   CD2   CE2    doub Y N 559 
TYR   CD2   HD2    sing N N 560 
TYR   CE1   CZ     doub Y N 561 
TYR   CE1   HE1    sing N N 562 
TYR   CE2   CZ     sing Y N 563 
TYR   CE2   HE2    sing N N 564 
TYR   CZ    OH     sing N N 565 
TYR   OH    HH     sing N N 566 
TYR   OXT   HXT    sing N N 567 
VAL   N     CA     sing N N 568 
VAL   N     H      sing N N 569 
VAL   N     H2     sing N N 570 
VAL   CA    C      sing N N 571 
VAL   CA    CB     sing N N 572 
VAL   CA    HA     sing N N 573 
VAL   C     O      doub N N 574 
VAL   C     OXT    sing N N 575 
VAL   CB    CG1    sing N N 576 
VAL   CB    CG2    sing N N 577 
VAL   CB    HB     sing N N 578 
VAL   CG1   HG11   sing N N 579 
VAL   CG1   HG12   sing N N 580 
VAL   CG1   HG13   sing N N 581 
VAL   CG2   HG21   sing N N 582 
VAL   CG2   HG22   sing N N 583 
VAL   CG2   HG23   sing N N 584 
VAL   OXT   HXT    sing N N 585 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          In-house 
# 
_space_group.name_H-M_alt     'P 1 2 1' 
_space_group.name_Hall        'P 2y' 
_space_group.IT_number        3 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    9BFX 
_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]   0.015094 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000836 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021000 
_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]   0.009839 
_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.
;
? 
CL ? ? 9.50761 7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
F  ? ? 4.90428 4.07044 ? ? 12.99538 1.63651  ? ? 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   ? 43.83500  36.38200  -12.87300 1.000 41.34678 ? 0   SER   A N     1 
ATOM   2    C  CA    . SER   A 1 1   ? 43.78100  35.48800  -14.04100 1.000 37.14195 ? 0   SER   A CA    1 
ATOM   3    C  C     . SER   A 1 1   ? 42.70400  34.41900  -13.85800 1.000 31.33054 ? 0   SER   A C     1 
ATOM   4    O  O     . SER   A 1 1   ? 42.30800  33.70000  -14.79400 1.000 32.39354 ? 0   SER   A O     1 
ATOM   5    C  CB    . SER   A 1 1   ? 45.13800  34.83100  -14.27200 1.000 45.11776 ? 0   SER   A CB    1 
ATOM   6    O  OG    . SER   A 1 1   ? 45.17700  34.20000  -15.53800 1.000 43.02448 ? 0   SER   A OG    1 
ATOM   7    N  N     . MET   A 1 2   ? 42.24900  34.30500  -12.63200 1.000 26.32969 ? 1   MET   A N     1 
ATOM   8    C  CA    . MET   A 1 2   ? 41.09400  33.48600  -12.32000 1.000 19.29153 ? 1   MET   A CA    1 
ATOM   9    C  C     . MET   A 1 2   ? 40.13100  34.33600  -11.51200 1.000 18.53401 ? 1   MET   A C     1 
ATOM   10   O  O     . MET   A 1 2   ? 40.52700  35.36900  -10.95300 1.000 18.41948 ? 1   MET   A O     1 
ATOM   11   C  CB    . MET   A 1 2   ? 41.48300  32.28600  -11.43300 1.000 27.07569 ? 1   MET   A CB    1 
ATOM   12   C  CG    . MET   A 1 2   ? 40.80500  31.01400  -11.81800 1.000 34.91689 ? 1   MET   A CG    1 
ATOM   13   S  SD    . MET   A 1 2   ? 41.27300  29.82100  -10.58500 1.000 36.91880 ? 1   MET   A SD    1 
ATOM   14   C  CE    . MET   A 1 2   ? 42.91800  29.55300  -10.88300 1.000 27.75180 ? 1   MET   A CE    1 
ATOM   15   N  N     . THR   A 1 3   ? 38.88500  33.89100  -11.43600 1.000 17.43910 ? 2   THR   A N     1 
ATOM   16   C  CA    . THR   A 1 3   ? 37.92800  34.42000  -10.47800 1.000 15.20898 ? 2   THR   A CA    1 
ATOM   17   C  C     . THR   A 1 3   ? 37.25000  33.24800  -9.80400  1.000 15.74564 ? 2   THR   A C     1 
ATOM   18   O  O     . THR   A 1 3   ? 37.46800  32.10500  -10.19400 1.000 16.95780 ? 2   THR   A O     1 
ATOM   19   C  CB    . THR   A 1 3   ? 36.89900  35.30300  -11.18100 1.000 20.44343 ? 2   THR   A CB    1 
ATOM   20   O  OG1   . THR   A 1 3   ? 36.40100  34.60000  -12.31400 1.000 20.48784 ? 2   THR   A OG1   1 
ATOM   21   C  CG2   . THR   A 1 3   ? 37.48800  36.67000  -11.60000 1.000 22.50891 ? 2   THR   A CG2   1 
ATOM   22   N  N     . GLU   A 1 4   ? 36.39600  33.52000  -8.83000  1.000 15.80942 ? 3   GLU   A N     1 
ATOM   23   C  CA    . GLU   A 1 4   ? 35.69200  32.49100  -8.07800  1.000 14.58751 ? 3   GLU   A CA    1 
ATOM   24   C  C     . GLU   A 1 4   ? 34.33500  33.03900  -7.66500  1.000 16.42783 ? 3   GLU   A C     1 
ATOM   25   O  O     . GLU   A 1 4   ? 34.23400  34.20200  -7.25600  1.000 17.25562 ? 3   GLU   A O     1 
ATOM   26   C  CB    . GLU   A 1 4   ? 36.52900  32.12100  -6.83300  1.000 14.71349 ? 3   GLU   A CB    1 
ATOM   27   C  CG    . GLU   A 1 4   ? 35.85100  31.08800  -5.91900  1.000 14.38147 ? 3   GLU   A CG    1 
ATOM   28   C  CD    . GLU   A 1 4   ? 36.86100  30.41900  -4.98800  1.000 19.08232 ? 3   GLU   A CD    1 
ATOM   29   O  OE1   . GLU   A 1 4   ? 38.04300  30.81400  -4.93200  1.000 18.76066 ? 3   GLU   A OE1   1 
ATOM   30   O  OE2   . GLU   A 1 4   ? 36.47400  29.47500  -4.28100  1.000 22.46104 ? 3   GLU   A OE2   1 
ATOM   31   N  N     . TYR   A 1 5   ? 33.30900  32.19400  -7.72100  1.000 13.86232 ? 4   TYR   A N     1 
ATOM   32   C  CA    . TYR   A 1 5   ? 31.93400  32.60600  -7.47600  1.000 14.37417 ? 4   TYR   A CA    1 
ATOM   33   C  C     . TYR   A 1 5   ? 31.26000  31.62200  -6.53900  1.000 12.18369 ? 4   TYR   A C     1 
ATOM   34   O  O     . TYR   A 1 5   ? 31.38200  30.39600  -6.70600  1.000 14.77223 ? 4   TYR   A O     1 
ATOM   35   C  CB    . TYR   A 1 5   ? 31.10000  32.71000  -8.77700  1.000 14.98104 ? 4   TYR   A CB    1 
ATOM   36   C  CG    . TYR   A 1 5   ? 31.74600  33.65000  -9.74100  1.000 16.74357 ? 4   TYR   A CG    1 
ATOM   37   C  CD1   . TYR   A 1 5   ? 31.72200  35.03400  -9.53300  1.000 18.11370 ? 4   TYR   A CD1   1 
ATOM   38   C  CD2   . TYR   A 1 5   ? 32.47000  33.17200  -10.80900 1.000 15.76336 ? 4   TYR   A CD2   1 
ATOM   39   C  CE1   . TYR   A 1 5   ? 32.36300  35.91700  -10.41500 1.000 19.12590 ? 4   TYR   A CE1   1 
ATOM   40   C  CE2   . TYR   A 1 5   ? 33.08500  34.00300  -11.68900 1.000 17.60976 ? 4   TYR   A CE2   1 
ATOM   41   C  CZ    . TYR   A 1 5   ? 33.05800  35.36900  -11.48400 1.000 17.73718 ? 4   TYR   A CZ    1 
ATOM   42   O  OH    . TYR   A 1 5   ? 33.71300  36.18100  -12.38000 1.000 19.83457 ? 4   TYR   A OH    1 
ATOM   43   N  N     . LYS   A 1 6   ? 30.51600  32.15500  -5.58800  1.000 13.77630 ? 5   LYS   A N     1 
ATOM   44   C  CA    . LYS   A 1 6   ? 29.67900  31.36700  -4.69200  1.000 13.36145 ? 5   LYS   A CA    1 
ATOM   45   C  C     . LYS   A 1 6   ? 28.25700  31.38200  -5.24400  1.000 13.25102 ? 5   LYS   A C     1 
ATOM   46   O  O     . LYS   A 1 6   ? 27.55100  32.39600  -5.15400  1.000 14.09018 ? 5   LYS   A O     1 
ATOM   47   C  CB    . LYS   A 1 6   ? 29.73700  31.98000  -3.29200  1.000 15.75164 ? 5   LYS   A CB    1 
ATOM   48   C  CG    . LYS   A 1 6   ? 31.12600  31.89300  -2.60700  1.000 22.45582 ? 5   LYS   A CG    1 
ATOM   49   C  CD    . LYS   A 1 6   ? 31.16200  32.63700  -1.25600  1.000 27.94268 ? 5   LYS   A CD    1 
ATOM   50   C  CE    . LYS   A 1 6   ? 31.11600  34.14900  -1.46100  1.000 29.13961 ? 5   LYS   A CE    1 
ATOM   51   N  NZ    . LYS   A 1 6   ? 30.97600  34.88700  -0.15900  1.000 33.25334 ? 5   LYS   A NZ    1 
ATOM   52   N  N     . LEU   A 1 7   ? 27.80900  30.24900  -5.79600  1.000 11.83236 ? 6   LEU   A N     1 
ATOM   53   C  CA    . LEU   A 1 7   ? 26.49100  30.10800  -6.41000  1.000 12.50670 ? 6   LEU   A CA    1 
ATOM   54   C  C     . LEU   A 1 7   ? 25.65800  29.24900  -5.46800  1.000 13.88352 ? 6   LEU   A C     1 
ATOM   55   O  O     . LEU   A 1 7   ? 26.18100  28.32500  -4.82500  1.000 15.80891 ? 6   LEU   A O     1 
ATOM   56   C  CB    . LEU   A 1 7   ? 26.61600  29.38500  -7.75500  1.000 12.40676 ? 6   LEU   A CB    1 
ATOM   57   C  CG    . LEU   A 1 7   ? 27.60900  29.96000  -8.77300  1.000 13.29960 ? 6   LEU   A CG    1 
ATOM   58   C  CD1   . LEU   A 1 7   ? 27.47400  29.20300  -10.08900 1.000 15.76467 ? 6   LEU   A CD1   1 
ATOM   59   C  CD2   . LEU   A 1 7   ? 27.36000  31.45800  -8.99300  1.000 16.24256 ? 6   LEU   A CD2   1 
ATOM   60   N  N     . VAL   A 1 8   ? 24.37700  29.59300  -5.32700  1.000 12.42872 ? 7   VAL   A N     1 
ATOM   61   C  CA    . VAL   A 1 8   ? 23.46100  28.86900  -4.45300  1.000 12.62413 ? 7   VAL   A CA    1 
ATOM   62   C  C     . VAL   A 1 8   ? 22.24400  28.47100  -5.28300  1.000 12.65321 ? 7   VAL   A C     1 
ATOM   63   O  O     . VAL   A 1 8   ? 21.65400  29.31500  -5.97900  1.000 13.40756 ? 7   VAL   A O     1 
ATOM   64   C  CB    . VAL   A 1 8   ? 23.03100  29.77200  -3.28600  1.000 11.67279 ? 7   VAL   A CB    1 
ATOM   65   C  CG1   . VAL   A 1 8   ? 22.14400  29.01200  -2.32900  1.000 13.79642 ? 7   VAL   A CG1   1 
ATOM   66   C  CG2   . VAL   A 1 8   ? 24.25500  30.27700  -2.52400  1.000 13.94395 ? 7   VAL   A CG2   1 
ATOM   67   N  N     . VAL   A 1 9   ? 21.85300  27.20100  -5.18000  1.000 11.94662 ? 8   VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 9   ? 20.73400  26.68800  -5.95200  1.000 12.36216 ? 8   VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 9   ? 19.57400  26.53800  -4.97700  1.000 12.32211 ? 8   VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 9   ? 19.70500  25.81200  -3.97000  1.000 13.41552 ? 8   VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 9   ? 21.11100  25.33800  -6.58400  1.000 13.01929 ? 8   VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 9   ? 19.97000  24.86300  -7.49200  1.000 15.01316 ? 8   VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 9   ? 22.39100  25.44100  -7.37200  1.000 14.22510 ? 8   VAL   A CG2   1 
ATOM   74   N  N     . VAL   A 1 10  ? 18.45300  27.21200  -5.27100  1.000 11.62295 ? 9   VAL   A N     1 
ATOM   75   C  CA    . VAL   A 1 10  ? 17.27200  27.18700  -4.39900  1.000 12.98652 ? 9   VAL   A CA    1 
ATOM   76   C  C     . VAL   A 1 10  ? 16.01300  26.87100  -5.19700  1.000 15.62974 ? 9   VAL   A C     1 
ATOM   77   O  O     . VAL   A 1 10  ? 16.00100  26.93500  -6.42000  1.000 15.13465 ? 9   VAL   A O     1 
ATOM   78   C  CB    . VAL   A 1 10  ? 17.07100  28.51200  -3.61400  1.000 13.92989 ? 9   VAL   A CB    1 
ATOM   79   C  CG1   . VAL   A 1 10  ? 18.31500  28.82700  -2.80500  1.000 15.78274 ? 9   VAL   A CG1   1 
ATOM   80   C  CG2   . VAL   A 1 10  ? 16.72100  29.67700  -4.60400  1.000 16.44719 ? 9   VAL   A CG2   1 
ATOM   81   N  N     . GLY   A 1 11  ? 14.97800  26.45400  -4.47200  1.000 14.11721 ? 10  GLY   A N     1 
ATOM   82   C  CA    . GLY   A 1 11  ? 13.71800  26.10300  -5.12800  1.000 15.61204 ? 10  GLY   A CA    1 
ATOM   83   C  C     . GLY   A 1 11  ? 13.00800  25.01600  -4.36200  1.000 14.77649 ? 10  GLY   A C     1 
ATOM   84   O  O     . GLY   A 1 11  ? 13.60300  24.43600  -3.46300  1.000 16.25482 ? 10  GLY   A O     1 
ATOM   85   N  N     . ALA   A 1 12  ? 11.78100  24.74200  -4.78600  1.000 14.87965 ? 11  ALA   A N     1 
ATOM   86   C  CA    . ALA   A 1 12  ? 10.93900  23.77000  -4.06000  1.000 15.31026 ? 11  ALA   A CA    1 
ATOM   87   C  C     . ALA   A 1 12  ? 11.49700  22.35500  -4.10400  1.000 16.51054 ? 11  ALA   A C     1 
ATOM   88   O  O     . ALA   A 1 12  ? 12.34300  21.99700  -4.90100  1.000 17.46473 ? 11  ALA   A O     1 
ATOM   89   C  CB    . ALA   A 1 12  ? 9.52700   23.80900  -4.60500  1.000 16.79181 ? 11  ALA   A CB    1 
ATOM   90   N  N     . CYS   A 1 13  ? 10.93400  21.55700  -3.22000  1.000 17.84642 ? 12  CYS   A N     1 
ATOM   91   C  CA    . CYS   A 1 13  ? 11.34000  20.14100  -3.14700  1.000 19.77650 ? 12  CYS   A CA    1 
ATOM   92   C  C     . CYS   A 1 13  ? 11.12600  19.41400  -4.48100  1.000 17.21199 ? 12  CYS   A C     1 
ATOM   93   O  O     . CYS   A 1 13  ? 10.09200  19.62200  -5.11000  1.000 21.32719 ? 12  CYS   A O     1 
ATOM   94   C  CB    . CYS   A 1 13  ? 10.51600  19.42200  -2.08300  1.000 21.91437 ? 12  CYS   A CB    1 
ATOM   95   S  SG    . CYS   A 1 13  ? 8.72100   19.40900  -2.37400  1.000 28.87876 ? 12  CYS   A SG    1 
ATOM   96   N  N     . GLY   A 1 14  ? 12.11500  18.63500  -4.90200  1.000 18.37437 ? 13  GLY   A N     1 
ATOM   97   C  CA    . GLY   A 1 14  ? 11.96000  17.76200  -6.07600  1.000 18.58842 ? 13  GLY   A CA    1 
ATOM   98   C  C     . GLY   A 1 14  ? 12.01800  18.42000  -7.44300  1.000 16.70842 ? 13  GLY   A C     1 
ATOM   99   O  O     . GLY   A 1 14  ? 11.73000  17.73500  -8.41600  1.000 20.69165 ? 13  GLY   A O     1 
ATOM   100  N  N     . VAL   A 1 15  ? 12.43100  19.68400  -7.52600  1.000 16.97889 ? 14  VAL   A N     1 
ATOM   101  C  CA    . VAL   A 1 15  ? 12.40200  20.39800  -8.83300  1.000 15.27226 ? 14  VAL   A CA    1 
ATOM   102  C  C     . VAL   A 1 15  ? 13.63500  20.04300  -9.68500  1.000 15.97136 ? 14  VAL   A C     1 
ATOM   103  O  O     . VAL   A 1 15  ? 13.58900  20.31500  -10.88400 1.000 16.82076 ? 14  VAL   A O     1 
ATOM   104  C  CB    . VAL   A 1 15  ? 12.27300  21.91600  -8.64100  1.000 16.89816 ? 14  VAL   A CB    1 
ATOM   105  C  CG1   . VAL   A 1 15  ? 10.96500  22.28300  -7.96000  1.000 18.79093 ? 14  VAL   A CG1   1 
ATOM   106  C  CG2   . VAL   A 1 15  ? 13.45800  22.49900  -7.88400  1.000 16.09976 ? 14  VAL   A CG2   1 
ATOM   107  N  N     . GLY   A 1 16  ? 14.67500  19.48400  -9.06400  1.000 16.24158 ? 15  GLY   A N     1 
ATOM   108  C  CA    . GLY   A 1 16  ? 15.86100  19.13400  -9.80500  1.000 15.13237 ? 15  GLY   A CA    1 
ATOM   109  C  C     . GLY   A 1 16  ? 17.09300  19.94500  -9.45600  1.000 15.05498 ? 15  GLY   A C     1 
ATOM   110  O  O     . GLY   A 1 16  ? 18.03700  19.94800  -10.24800 1.000 15.31867 ? 15  GLY   A O     1 
ATOM   111  N  N     . LYS   A 1 17  ? 17.12400  20.57000  -8.29000  1.000 14.65890 ? 16  LYS   A N     1 
ATOM   112  C  CA    . LYS   A 1 17  ? 18.31400  21.36000  -7.86900  1.000 15.27988 ? 16  LYS   A CA    1 
ATOM   113  C  C     . LYS   A 1 17  ? 19.56300  20.46800  -7.86300  1.000 15.07658 ? 16  LYS   A C     1 
ATOM   114  O  O     . LYS   A 1 17  ? 20.58600  20.84400  -8.42900  1.000 14.84486 ? 16  LYS   A O     1 
ATOM   115  C  CB    . LYS   A 1 17  ? 18.06000  21.96400  -6.48700  1.000 14.87721 ? 16  LYS   A CB    1 
ATOM   116  C  CG    . LYS   A 1 17  ? 16.89400  22.93000  -6.40400  1.000 15.00682 ? 16  LYS   A CG    1 
ATOM   117  C  CD    . LYS   A 1 17  ? 16.69700  23.47400  -4.99600  1.000 15.40912 ? 16  LYS   A CD    1 
ATOM   118  C  CE    . LYS   A 1 17  ? 16.36900  22.42000  -3.99500  1.000 14.99802 ? 16  LYS   A CE    1 
ATOM   119  N  NZ    . LYS   A 1 17  ? 15.04200  21.82900  -4.18200  1.000 15.53933 ? 16  LYS   A NZ    1 
ATOM   120  N  N     . SER   A 1 18  ? 19.44000  19.32600  -7.21300  1.000 14.30731 ? 17  SER   A N     1 
ATOM   121  C  CA    . SER   A 1 18  ? 20.58400  18.42600  -7.14800  1.000 12.98534 ? 17  SER   A CA    1 
ATOM   122  C  C     . SER   A 1 18  ? 20.90900  17.82100  -8.50800  1.000 15.66897 ? 17  SER   A C     1 
ATOM   123  O  O     . SER   A 1 18  ? 22.08700  17.72900  -8.88500  1.000 15.47861 ? 17  SER   A O     1 
ATOM   124  C  CB    . SER   A 1 18  ? 20.34900  17.31600  -6.13800  1.000 15.46172 ? 17  SER   A CB    1 
ATOM   125  O  OG    . SER   A 1 18  ? 20.18800  17.87800  -4.83800  1.000 15.76527 ? 17  SER   A OG    1 
ATOM   126  N  N     . ALA   A 1 19  ? 19.89400  17.43900  -9.26700  1.000 14.81933 ? 18  ALA   A N     1 
ATOM   127  C  CA    . ALA   A 1 19  ? 20.16300  16.80900  -10.54700 1.000 15.11820 ? 18  ALA   A CA    1 
ATOM   128  C  C     . ALA   A 1 19  ? 20.86100  17.78100  -11.48200 1.000 16.42863 ? 18  ALA   A C     1 
ATOM   129  O  O     . ALA   A 1 19  ? 21.76600  17.38900  -12.23000 1.000 17.44655 ? 18  ALA   A O     1 
ATOM   130  C  CB    . ALA   A 1 19  ? 18.86700  16.29200  -11.15500 1.000 17.66924 ? 18  ALA   A CB    1 
ATOM   131  N  N     . LEU   A 1 20  ? 20.47800  19.05700  -11.43500 1.000 14.40737 ? 19  LEU   A N     1 
ATOM   132  C  CA    . LEU   A 1 20  ? 21.16000  20.06400  -12.24800 1.000 15.91393 ? 19  LEU   A CA    1 
ATOM   133  C  C     . LEU   A 1 20  ? 22.61200  20.21800  -11.83200 1.000 17.35003 ? 19  LEU   A C     1 
ATOM   134  O  O     . LEU   A 1 20  ? 23.51900  20.24400  -12.68900 1.000 16.68302 ? 19  LEU   A O     1 
ATOM   135  C  CB    . LEU   A 1 20  ? 20.43600  21.40100  -12.13200 1.000 16.61926 ? 19  LEU   A CB    1 
ATOM   136  C  CG    . LEU   A 1 20  ? 19.13800  21.53500  -12.92300 1.000 16.81476 ? 19  LEU   A CG    1 
ATOM   137  C  CD1   . LEU   A 1 20  ? 18.41600  22.79500  -12.50100 1.000 17.85056 ? 19  LEU   A CD1   1 
ATOM   138  C  CD2   . LEU   A 1 20  ? 19.42300  21.56400  -14.38800 1.000 18.44383 ? 19  LEU   A CD2   1 
ATOM   139  N  N     . THR   A 1 21  ? 22.84300  20.30600  -10.51400 1.000 14.28191 ? 20  THR   A N     1 
ATOM   140  C  CA    . THR   A 1 21  ? 24.18800  20.49700  -10.01000 1.000 16.68055 ? 20  THR   A CA    1 
ATOM   141  C  C     . THR   A 1 21  ? 25.07600  19.30800  -10.35800 1.000 17.28079 ? 20  THR   A C     1 
ATOM   142  O  O     . THR   A 1 21  ? 26.19000  19.48700  -10.85400 1.000 16.85923 ? 20  THR   A O     1 
ATOM   143  C  CB    . THR   A 1 21  ? 24.10300  20.70700  -8.51200  1.000 15.92879 ? 20  THR   A CB    1 
ATOM   144  O  OG1   . THR   A 1 21  ? 23.28100  21.85800  -8.21000  1.000 15.30322 ? 20  THR   A OG1   1 
ATOM   145  C  CG2   . THR   A 1 21  ? 25.50000  20.97600  -7.91600  1.000 17.68287 ? 20  THR   A CG2   1 
ATOM   146  N  N     . ILE   A 1 22  ? 24.57500  18.07800  -10.15700 1.000 16.05089 ? 21  ILE   A N     1 
ATOM   147  C  CA    . ILE   A 1 22  ? 25.36200  16.87300  -10.40800 1.000 17.01712 ? 21  ILE   A CA    1 
ATOM   148  C  C     . ILE   A 1 22  ? 25.66100  16.74200  -11.88300 1.000 18.30693 ? 21  ILE   A C     1 
ATOM   149  O  O     . ILE   A 1 22  ? 26.76100  16.31800  -12.25600 1.000 18.21901 ? 21  ILE   A O     1 
ATOM   150  C  CB    . ILE   A 1 22  ? 24.67600  15.62500  -9.80100  1.000 17.18829 ? 21  ILE   A CB    1 
ATOM   151  C  CG1   . ILE   A 1 22  ? 24.71600  15.73800  -8.27100  1.000 19.58142 ? 21  ILE   A CG1   1 
ATOM   152  C  CG2   . ILE   A 1 22  ? 25.33500  14.33100  -10.29500 1.000 20.63054 ? 21  ILE   A CG2   1 
ATOM   153  C  CD1   . ILE   A 1 22  ? 23.68800  14.86600  -7.58400  1.000 24.66096 ? 21  ILE   A CD1   1 
ATOM   154  N  N     . GLN   A 1 23  ? 24.71500  17.11500  -12.75000 1.000 15.97211 ? 22  GLN   A N     1 
ATOM   155  C  CA    . GLN   A 1 23  ? 25.00000  17.15900  -14.17800 1.000 19.40872 ? 22  GLN   A CA    1 
ATOM   156  C  C     . GLN   A 1 23  ? 26.13800  18.12400  -14.48500 1.000 19.74733 ? 22  GLN   A C     1 
ATOM   157  O  O     . GLN   A 1 23  ? 27.05100  17.78800  -15.25500 1.000 21.52876 ? 22  GLN   A O     1 
ATOM   158  C  CB    . GLN   A 1 23  ? 23.74300  17.52700  -14.94400 1.000 20.37823 ? 22  GLN   A CB    1 
ATOM   159  C  CG    . GLN   A 1 23  ? 22.99800  16.32100  -15.39700 1.000 27.17853 ? 22  GLN   A CG    1 
ATOM   160  C  CD    . GLN   A 1 23  ? 23.61100  15.57900  -16.62600 1.000 23.80001 ? 22  GLN   A CD    1 
ATOM   161  O  OE1   . GLN   A 1 23  ? 24.80500  15.67700  -17.00800 1.000 26.05454 ? 22  GLN   A OE1   1 
ATOM   162  N  NE2   . GLN   A 1 23  ? 22.76300  14.83000  -17.23100 1.000 28.23325 ? 22  GLN   A NE2   1 
ATOM   163  N  N     . LEU   A 1 24  ? 26.09900  19.33600  -13.91800 1.000 18.25167 ? 23  LEU   A N     1 
ATOM   164  C  CA    . LEU   A 1 24  ? 27.19200  20.27100  -14.15500 1.000 19.37541 ? 23  LEU   A CA    1 
ATOM   165  C  C     . LEU   A 1 24  ? 28.51900  19.69200  -13.69500 1.000 17.96989 ? 23  LEU   A C     1 
ATOM   166  O  O     . LEU   A 1 24  ? 29.52100  19.76400  -14.42200 1.000 22.25979 ? 23  LEU   A O     1 
ATOM   167  C  CB    . LEU   A 1 24  ? 26.92000  21.57700  -13.40700 1.000 18.09566 ? 23  LEU   A CB    1 
ATOM   168  C  CG    . LEU   A 1 24  ? 27.95600  22.66500  -13.67800 1.000 21.03061 ? 23  LEU   A CG    1 
ATOM   169  C  CD1   . LEU   A 1 24  ? 27.69700  23.26400  -15.07600 1.000 23.70181 ? 23  LEU   A CD1   1 
ATOM   170  C  CD2   . LEU   A 1 24  ? 27.96200  23.69600  -12.56200 1.000 21.81800 ? 23  LEU   A CD2   1 
ATOM   171  N  N     . ILE   A 1 25  ? 28.55200  19.16100  -12.47400 1.000 19.60791 ? 24  ILE   A N     1 
ATOM   172  C  CA    . ILE   A 1 25  ? 29.79500  18.78500  -11.80300 1.000 22.10802 ? 24  ILE   A CA    1 
ATOM   173  C  C     . ILE   A 1 25  ? 30.31000  17.43400  -12.28800 1.000 23.23116 ? 24  ILE   A C     1 
ATOM   174  O  O     . ILE   A 1 25  ? 31.51600  17.27200  -12.52400 1.000 24.07802 ? 24  ILE   A O     1 
ATOM   175  C  CB    . ILE   A 1 25  ? 29.58800  18.76500  -10.28100 1.000 23.47537 ? 24  ILE   A CB    1 
ATOM   176  C  CG1   . ILE   A 1 25  ? 29.12200  20.13700  -9.77300  1.000 21.14127 ? 24  ILE   A CG1   1 
ATOM   177  C  CG2   . ILE   A 1 25  ? 30.85600  18.24200  -9.59800  1.000 26.85920 ? 24  ILE   A CG2   1 
ATOM   178  C  CD1   . ILE   A 1 25  ? 30.17100  21.21000  -9.86700  1.000 23.58158 ? 24  ILE   A CD1   1 
ATOM   179  N  N     . GLN   A 1 26  ? 29.41900  16.42900  -12.37900 1.000 21.42540 ? 25  GLN   A N     1 
ATOM   180  C  CA    . GLN   A 1 26  ? 29.79300  15.03500  -12.59300 1.000 25.20486 ? 25  GLN   A CA    1 
ATOM   181  C  C     . GLN   A 1 26  ? 29.34800  14.47200  -13.93900 1.000 24.05740 ? 25  GLN   A C     1 
ATOM   182  O  O     . GLN   A 1 26  ? 29.69900  13.32500  -14.26500 1.000 26.11687 ? 25  GLN   A O     1 
ATOM   183  C  CB    . GLN   A 1 26  ? 29.22100  14.16400  -11.45500 1.000 23.32374 ? 25  GLN   A CB    1 
ATOM   184  C  CG    . GLN   A 1 26  ? 29.64700  14.66800  -10.07900 1.000 25.20232 ? 25  GLN   A CG    1 
ATOM   185  C  CD    . GLN   A 1 26  ? 29.14600  13.82900  -8.91300  1.000 29.94993 ? 25  GLN   A CD    1 
ATOM   186  O  OE1   . GLN   A 1 26  ? 28.35300  12.90100  -9.08000  1.000 34.54639 ? 25  GLN   A OE1   1 
ATOM   187  N  NE2   . GLN   A 1 26  ? 29.62600  14.15000  -7.72000  1.000 30.90321 ? 25  GLN   A NE2   1 
ATOM   188  N  N     A ASN   A 1 27  ? 28.58400  15.24000  -14.71700 0.500 23.31293 ? 26  ASN   A N     1 
ATOM   189  N  N     B ASN   A 1 27  ? 28.58500  15.22800  -14.73000 0.500 23.29389 ? 26  ASN   A N     1 
ATOM   190  C  CA    A ASN   A 1 27  ? 28.16200  14.87400  -16.06400 0.500 23.97690 ? 26  ASN   A CA    1 
ATOM   191  C  CA    B ASN   A 1 27  ? 28.21300  14.83800  -16.08900 0.500 23.99223 ? 26  ASN   A CA    1 
ATOM   192  C  C     A ASN   A 1 27  ? 27.40000  13.55300  -16.09900 0.500 23.72994 ? 26  ASN   A C     1 
ATOM   193  C  C     B ASN   A 1 27  ? 27.39100  13.54700  -16.11900 0.500 23.73710 ? 26  ASN   A C     1 
ATOM   194  O  O     A ASN   A 1 27  ? 27.62700  12.71200  -16.96700 0.500 26.32027 ? 26  ASN   A O     1 
ATOM   195  O  O     B ASN   A 1 27  ? 27.56400  12.71300  -17.00500 0.500 26.31262 ? 26  ASN   A O     1 
ATOM   196  C  CB    A ASN   A 1 27  ? 29.33200  14.88800  -17.04700 0.500 25.11230 ? 26  ASN   A CB    1 
ATOM   197  C  CB    B ASN   A 1 27  ? 29.44900  14.74000  -16.99900 0.500 25.07562 ? 26  ASN   A CB    1 
ATOM   198  C  CG    A ASN   A 1 27  ? 30.20400  16.10700  -16.87500 0.500 26.27942 ? 26  ASN   A CG    1 
ATOM   199  C  CG    B ASN   A 1 27  ? 29.11900  14.86800  -18.48200 0.500 26.93578 ? 26  ASN   A CG    1 
ATOM   200  O  OD1   A ASN   A 1 27  ? 29.82500  17.20700  -17.26400 0.500 36.94811 ? 26  ASN   A OD1   1 
ATOM   201  O  OD1   B ASN   A 1 27  ? 28.18700  15.56800  -18.86900 0.500 30.58586 ? 26  ASN   A OD1   1 
ATOM   202  N  ND2   A ASN   A 1 27  ? 31.37500  15.92200  -16.27800 0.500 29.10915 ? 26  ASN   A ND2   1 
ATOM   203  N  ND2   B ASN   A 1 27  ? 29.89700  14.18700  -19.31800 0.500 27.02264 ? 26  ASN   A ND2   1 
ATOM   204  N  N     . HIS   A 1 28  ? 26.48400  13.36800  -15.15600 1.000 22.87840 ? 27  HIS   A N     1 
ATOM   205  C  CA    . HIS   A 1 28  ? 25.54500  12.25200  -15.23800 1.000 24.40658 ? 27  HIS   A CA    1 
ATOM   206  C  C     . HIS   A 1 28  ? 24.24000  12.63500  -14.55300 1.000 22.03704 ? 27  HIS   A C     1 
ATOM   207  O  O     . HIS   A 1 28  ? 24.16200  13.63000  -13.83500 1.000 21.31119 ? 27  HIS   A O     1 
ATOM   208  C  CB    . HIS   A 1 28  ? 26.12000  10.92200  -14.70700 1.000 27.80706 ? 27  HIS   A CB    1 
ATOM   209  C  CG    . HIS   A 1 28  ? 26.39600  10.93300  -13.23900 1.000 29.56581 ? 27  HIS   A CG    1 
ATOM   210  N  ND1   . HIS   A 1 28  ? 25.44700  10.57600  -12.30200 1.000 32.28647 ? 27  HIS   A ND1   1 
ATOM   211  C  CD2   . HIS   A 1 28  ? 27.50100  11.28600  -12.54000 1.000 32.81375 ? 27  HIS   A CD2   1 
ATOM   212  C  CE1   . HIS   A 1 28  ? 25.95900  10.70500  -11.09000 1.000 36.72155 ? 27  HIS   A CE1   1 
ATOM   213  N  NE2   . HIS   A 1 28  ? 27.20400  11.13500  -11.20600 1.000 36.88925 ? 27  HIS   A NE2   1 
ATOM   214  N  N     . PHE   A 1 29  ? 23.21400  11.82000  -14.80300 1.000 23.99527 ? 28  PHE   A N     1 
ATOM   215  C  CA    . PHE   A 1 29  ? 21.85800  11.91700  -14.26300 1.000 23.09004 ? 28  PHE   A CA    1 
ATOM   216  C  C     . PHE   A 1 29  ? 21.43800  10.53300  -13.75500 1.000 26.85840 ? 28  PHE   A C     1 
ATOM   217  O  O     . PHE   A 1 29  ? 21.71500  9.53100   -14.40200 1.000 37.24820 ? 28  PHE   A O     1 
ATOM   218  C  CB    . PHE   A 1 29  ? 20.89600  12.29800  -15.42400 1.000 25.01799 ? 28  PHE   A CB    1 
ATOM   219  C  CG    . PHE   A 1 29  ? 19.44700  12.37300  -15.02000 1.000 23.65601 ? 28  PHE   A CG    1 
ATOM   220  C  CD1   . PHE   A 1 29  ? 18.98400  13.42900  -14.25100 1.000 23.83185 ? 28  PHE   A CD1   1 
ATOM   221  C  CD2   . PHE   A 1 29  ? 18.55000  11.39300  -15.40600 1.000 25.23859 ? 28  PHE   A CD2   1 
ATOM   222  C  CE1   . PHE   A 1 29  ? 17.65400  13.48600  -13.86500 1.000 26.66415 ? 28  PHE   A CE1   1 
ATOM   223  C  CE2   . PHE   A 1 29  ? 17.22800  11.45500  -15.04000 1.000 24.93906 ? 28  PHE   A CE2   1 
ATOM   224  C  CZ    . PHE   A 1 29  ? 16.78400  12.50800  -14.25500 1.000 25.84651 ? 28  PHE   A CZ    1 
ATOM   225  N  N     . VAL   A 1 30  ? 20.78300  10.47900  -12.59200 1.000 37.90224 ? 29  VAL   A N     1 
ATOM   226  C  CA    . VAL   A 1 30  ? 20.06800  9.28600   -12.14100 1.000 36.36158 ? 29  VAL   A CA    1 
ATOM   227  C  C     . VAL   A 1 30  ? 18.65700  9.69000   -11.74500 1.000 27.93898 ? 29  VAL   A C     1 
ATOM   228  O  O     . VAL   A 1 30  ? 18.43700  10.78900  -11.21400 1.000 39.59112 ? 29  VAL   A O     1 
ATOM   229  C  CB    . VAL   A 1 30  ? 20.77000  8.54800   -10.97900 1.000 42.84589 ? 29  VAL   A CB    1 
ATOM   230  C  CG1   . VAL   A 1 30  ? 22.03600  7.83200   -11.47100 1.000 41.60912 ? 29  VAL   A CG1   1 
ATOM   231  C  CG2   . VAL   A 1 30  ? 21.05100  9.50100   -9.82100  1.000 43.88573 ? 29  VAL   A CG2   1 
ATOM   232  N  N     . ASP   A 1 31  ? 17.70600  8.80700   -12.04500 1.000 38.61459 ? 30  ASP   A N     1 
ATOM   233  C  CA    . ASP   A 1 31  ? 16.30200  8.99900   -11.75500 1.000 35.73057 ? 30  ASP   A CA    1 
ATOM   234  C  C     . ASP   A 1 31  ? 16.02100  8.98300   -10.26600 1.000 31.71725 ? 30  ASP   A C     1 
ATOM   235  O  O     . ASP   A 1 31  ? 14.95100  9.43700   -9.85200  1.000 31.66043 ? 30  ASP   A O     1 
ATOM   236  C  CB    . ASP   A 1 31  ? 15.50000  7.85100   -12.38500 1.000 37.92246 ? 30  ASP   A CB    1 
ATOM   237  C  CG    . ASP   A 1 31  ? 15.32000  8.00200   -13.88500 1.000 37.73704 ? 30  ASP   A CG    1 
ATOM   238  O  OD1   . ASP   A 1 31  ? 15.10200  9.13300   -14.35800 1.000 41.34224 ? 30  ASP   A OD1   1 
ATOM   239  O  OD2   . ASP   A 1 31  ? 15.36500  6.97300   -14.59500 1.000 53.16527 ? 30  ASP   A OD2   1 
ATOM   240  N  N     . GLU   A 1 32  ? 16.90700  8.40200   -9.45900  1.000 42.42915 ? 31  GLU   A N     1 
ATOM   241  C  CA    . GLU   A 1 32  ? 16.56100  8.18100   -8.06000  1.000 38.37396 ? 31  GLU   A CA    1 
ATOM   242  C  C     . GLU   A 1 32  ? 16.58800  9.50600   -7.32100  1.000 29.22393 ? 31  GLU   A C     1 
ATOM   243  O  O     . GLU   A 1 32  ? 17.49000  10.32200  -7.50900  1.000 34.63032 ? 31  GLU   A O     1 
ATOM   244  C  CB    . GLU   A 1 32  ? 17.48200  7.15100   -7.39000  1.000 41.55711 ? 31  GLU   A CB    1 
ATOM   245  C  CG    . GLU   A 1 32  ? 16.74600  5.86200   -6.96900  1.000 53.09404 ? 31  GLU   A CG    1 
ATOM   246  C  CD    . GLU   A 1 32  ? 17.41100  5.07300   -5.83100  1.000 47.14627 ? 31  GLU   A CD    1 
ATOM   247  O  OE1   . GLU   A 1 32  ? 18.50200  5.45300   -5.35600  1.000 51.60168 ? 31  GLU   A OE1   1 
ATOM   248  O  OE2   . GLU   A 1 32  ? 16.82200  4.05700   -5.41000  1.000 54.63849 ? 31  GLU   A OE2   1 
ATOM   249  N  N     . TYR   A 1 33  ? 15.55500  9.70400   -6.50800  1.000 27.28965 ? 32  TYR   A N     1 
ATOM   250  C  CA    . TYR   A 1 33  ? 15.44500  10.93900  -5.68900  1.000 23.85717 ? 32  TYR   A CA    1 
ATOM   251  C  C     . TYR   A 1 33  ? 16.11000  10.70100  -4.36300  1.000 22.99396 ? 32  TYR   A C     1 
ATOM   252  O  O     . TYR   A 1 33  ? 15.72600  9.78300   -3.63900  1.000 26.25669 ? 32  TYR   A O     1 
ATOM   253  C  CB    . TYR   A 1 33  ? 13.98600  11.36900  -5.51900  1.000 25.05836 ? 32  TYR   A CB    1 
ATOM   254  C  CG    . TYR   A 1 33  ? 13.66200  12.65200  -4.76400  1.000 25.39958 ? 32  TYR   A CG    1 
ATOM   255  C  CD1   . TYR   A 1 33  ? 14.63600  13.58400  -4.43100  1.000 24.66676 ? 32  TYR   A CD1   1 
ATOM   256  C  CD2   . TYR   A 1 33  ? 12.35600  12.93300  -4.39200  1.000 31.89360 ? 32  TYR   A CD2   1 
ATOM   257  C  CE1   . TYR   A 1 33  ? 14.32100  14.74100  -3.74000  1.000 25.45993 ? 32  TYR   A CE1   1 
ATOM   258  C  CE2   . TYR   A 1 33  ? 12.02500  14.08900  -3.70800  1.000 32.19469 ? 32  TYR   A CE2   1 
ATOM   259  C  CZ    . TYR   A 1 33  ? 13.01000  15.00000  -3.38100  1.000 25.70765 ? 32  TYR   A CZ    1 
ATOM   260  O  OH    . TYR   A 1 33  ? 12.66700  16.13400  -2.70600  1.000 28.12034 ? 32  TYR   A OH    1 
ATOM   261  N  N     . ASP   A 1 34  ? 17.13500  11.48400  -4.07000  1.000 21.18974 ? 33  ASP   A N     1 
ATOM   262  C  CA    . ASP   A 1 34  ? 17.79600  11.41700  -2.76900  1.000 20.54467 ? 33  ASP   A CA    1 
ATOM   263  C  C     . ASP   A 1 34  ? 17.66400  12.79900  -2.15800  1.000 18.07882 ? 33  ASP   A C     1 
ATOM   264  O  O     . ASP   A 1 34  ? 18.41800  13.70600  -2.53600  1.000 17.24798 ? 33  ASP   A O     1 
ATOM   265  C  CB    . ASP   A 1 34  ? 19.26600  11.06200  -2.94600  1.000 24.63752 ? 33  ASP   A CB    1 
ATOM   266  C  CG    . ASP   A 1 34  ? 20.01000  10.96400  -1.63000  1.000 30.53192 ? 33  ASP   A CG    1 
ATOM   267  O  OD1   . ASP   A 1 34  ? 19.35300  10.90800  -0.57700  1.000 31.82694 ? 33  ASP   A OD1   1 
ATOM   268  O  OD2   . ASP   A 1 34  ? 21.25800  10.93300  -1.66100  1.000 37.76098 ? 33  ASP   A OD2   1 
ATOM   269  N  N     . PRO   A 1 35  ? 16.73800  13.00500  -1.22100  1.000 19.19302 ? 34  PRO   A N     1 
ATOM   270  C  CA    . PRO   A 1 35  ? 16.47900  14.36000  -0.71900  1.000 18.94386 ? 34  PRO   A CA    1 
ATOM   271  C  C     . PRO   A 1 35  ? 17.70900  14.98800  -0.08200  1.000 18.09110 ? 34  PRO   A C     1 
ATOM   272  O  O     . PRO   A 1 35  ? 18.44600  14.33700  0.66300   1.000 20.64771 ? 34  PRO   A O     1 
ATOM   273  C  CB    . PRO   A 1 35  ? 15.35300  14.14300  0.30300   1.000 21.67205 ? 34  PRO   A CB    1 
ATOM   274  C  CG    . PRO   A 1 35  ? 14.70800  12.90700  -0.14700  1.000 26.55917 ? 34  PRO   A CG    1 
ATOM   275  C  CD    . PRO   A 1 35  ? 15.78200  12.03200  -0.69100  1.000 22.61215 ? 34  PRO   A CD    1 
ATOM   276  N  N     . THR   A 1 36  ? 17.93300  16.25200  -0.40700  1.000 16.87706 ? 35  THR   A N     1 
ATOM   277  C  CA    . THR   A 1 36  ? 19.10400  16.95500  0.08500   1.000 17.08356 ? 35  THR   A CA    1 
ATOM   278  C  C     . THR   A 1 36  ? 18.94600  17.41000  1.53100   1.000 15.97047 ? 35  THR   A C     1 
ATOM   279  O  O     . THR   A 1 36  ? 17.87200  17.85300  1.95200   1.000 17.15366 ? 35  THR   A O     1 
ATOM   280  C  CB    . THR   A 1 36  ? 19.37700  18.14300  -0.81400  1.000 15.49598 ? 35  THR   A CB    1 
ATOM   281  O  OG1   . THR   A 1 36  ? 19.60600  17.61500  -2.12800  1.000 16.23560 ? 35  THR   A OG1   1 
ATOM   282  C  CG2   . THR   A 1 36  ? 20.60600  18.93200  -0.35700  1.000 15.38786 ? 35  THR   A CG2   1 
ATOM   283  N  N     . ILE   A 1 37  ? 20.03100  17.24200  2.28600   1.000 15.66041 ? 36  ILE   A N     1 
ATOM   284  C  CA    . ILE   A 1 37  ? 20.24000  17.99300  3.52500   1.000 15.23078 ? 36  ILE   A CA    1 
ATOM   285  C  C     . ILE   A 1 37  ? 21.06100  19.23000  3.17200   1.000 15.52769 ? 36  ILE   A C     1 
ATOM   286  O  O     . ILE   A 1 37  ? 20.56000  20.35200  3.30100   1.000 15.78588 ? 36  ILE   A O     1 
ATOM   287  C  CB    . ILE   A 1 37  ? 20.91600  17.13600  4.62500   1.000 15.75314 ? 36  ILE   A CB    1 
ATOM   288  C  CG1   . ILE   A 1 37  ? 20.02600  15.97900  5.13500   1.000 17.38321 ? 36  ILE   A CG1   1 
ATOM   289  C  CG2   . ILE   A 1 37  ? 21.31200  18.01800  5.81000   1.000 15.43998 ? 36  ILE   A CG2   1 
ATOM   290  C  CD1   . ILE   A 1 37  ? 18.91400  16.41000  6.00200   1.000 19.32900 ? 36  ILE   A CD1   1 
ATOM   291  N  N     . GLU   A 1 38  ? 22.29200  19.05300  2.68700   1.000 14.85626 ? 37  GLU   A N     1 
ATOM   292  C  CA    . GLU   A 1 38  ? 23.10700  20.16300  2.19100   1.000 14.71290 ? 37  GLU   A CA    1 
ATOM   293  C  C     . GLU   A 1 38  ? 24.29100  19.53600  1.48600   1.000 13.61709 ? 37  GLU   A C     1 
ATOM   294  O  O     . GLU   A 1 38  ? 24.86100  18.57500  1.99200   1.000 15.85436 ? 37  GLU   A O     1 
ATOM   295  C  CB    . GLU   A 1 38  ? 23.63900  21.01200  3.35600   1.000 15.25359 ? 37  GLU   A CB    1 
ATOM   296  C  CG    . GLU   A 1 38  ? 24.31500  22.30600  2.90500   1.000 15.22923 ? 37  GLU   A CG    1 
ATOM   297  C  CD    . GLU   A 1 38  ? 25.11500  22.92400  4.00900   1.000 16.42320 ? 37  GLU   A CD    1 
ATOM   298  O  OE1   . GLU   A 1 38  ? 24.54100  23.63800  4.86000   1.000 15.92951 ? 37  GLU   A OE1   1 
ATOM   299  O  OE2   . GLU   A 1 38  ? 26.31400  22.57600  4.10700   1.000 18.41745 ? 37  GLU   A OE2   1 
ATOM   300  N  N     . ASP   A 1 39  ? 24.64200  20.05400  0.30900   1.000 14.41886 ? 38  ASP   A N     1 
ATOM   301  C  CA    . ASP   A 1 39  ? 25.84100  19.58900  -0.37500  1.000 14.84225 ? 38  ASP   A CA    1 
ATOM   302  C  C     . ASP   A 1 39  ? 26.55500  20.77100  -1.00000  1.000 14.73325 ? 38  ASP   A C     1 
ATOM   303  O  O     . ASP   A 1 39  ? 25.92600  21.75200  -1.38900  1.000 15.37037 ? 38  ASP   A O     1 
ATOM   304  C  CB    . ASP   A 1 39  ? 25.50800  18.56200  -1.45600  1.000 15.49447 ? 38  ASP   A CB    1 
ATOM   305  C  CG    . ASP   A 1 39  ? 25.11000  17.23200  -0.87400  1.000 19.88393 ? 38  ASP   A CG    1 
ATOM   306  O  OD1   . ASP   A 1 39  ? 25.98200  16.51800  -0.32800  1.000 20.71429 ? 38  ASP   A OD1   1 
ATOM   307  O  OD2   . ASP   A 1 39  ? 23.90000  16.95900  -0.89500  1.000 23.10066 ? 38  ASP   A OD2   1 
ATOM   308  N  N     . SER   A 1 40  ? 27.87500  20.64900  -1.12700  1.000 15.36403 ? 39  SER   A N     1 
ATOM   309  C  CA    . SER   A 1 40  ? 28.72500  21.68900  -1.68400  1.000 16.88749 ? 39  SER   A CA    1 
ATOM   310  C  C     . SER   A 1 40  ? 29.63400  21.04700  -2.72200  1.000 17.53085 ? 39  SER   A C     1 
ATOM   311  O  O     . SER   A 1 40  ? 30.13700  19.93700  -2.52300  1.000 18.74050 ? 39  SER   A O     1 
ATOM   312  C  CB    . SER   A 1 40  ? 29.59200  22.26600  -0.58600  1.000 17.95654 ? 39  SER   A CB    1 
ATOM   313  O  OG    . SER   A 1 40  ? 28.81300  22.99700  0.34300   1.000 23.64364 ? 39  SER   A OG    1 
ATOM   314  N  N     . TYR   A 1 41  ? 29.85700  21.75800  -3.83800  1.000 14.71663 ? 40  TYR   A N     1 
ATOM   315  C  CA    . TYR   A 1 41  ? 30.64700  21.25700  -4.94100  1.000 15.68896 ? 40  TYR   A CA    1 
ATOM   316  C  C     . TYR   A 1 41  ? 31.58900  22.36600  -5.36800  1.000 15.17227 ? 40  TYR   A C     1 
ATOM   317  O  O     . TYR   A 1 41  ? 31.34900  23.55100  -5.10600  1.000 14.21151 ? 40  TYR   A O     1 
ATOM   318  C  CB    . TYR   A 1 41  ? 29.76000  20.85200  -6.12200  1.000 17.92249 ? 40  TYR   A CB    1 
ATOM   319  C  CG    . TYR   A 1 41  ? 28.77000  19.77300  -5.74200  1.000 18.31639 ? 40  TYR   A CG    1 
ATOM   320  C  CD1   . TYR   A 1 41  ? 29.12600  18.43100  -5.81900  1.000 20.31489 ? 40  TYR   A CD1   1 
ATOM   321  C  CD2   . TYR   A 1 41  ? 27.50400  20.08800  -5.27900  1.000 17.62442 ? 40  TYR   A CD2   1 
ATOM   322  C  CE1   . TYR   A 1 41  ? 28.24300  17.41600  -5.46400  1.000 24.87744 ? 40  TYR   A CE1   1 
ATOM   323  C  CE2   . TYR   A 1 41  ? 26.61500  19.08600  -4.92700  1.000 19.61652 ? 40  TYR   A CE2   1 
ATOM   324  C  CZ    . TYR   A 1 41  ? 26.99100  17.75900  -5.02000  1.000 24.06246 ? 40  TYR   A CZ    1 
ATOM   325  O  OH    . TYR   A 1 41  ? 26.10800  16.74700  -4.66100  1.000 25.63445 ? 40  TYR   A OH    1 
ATOM   326  N  N     . ARG   A 1 42  ? 32.65700  21.97700  -6.04400  1.000 16.24247 ? 41  ARG   A N     1 
ATOM   327  C  CA    . ARG   A 1 42  ? 33.65100  22.93600  -6.51200  1.000 16.53517 ? 41  ARG   A CA    1 
ATOM   328  C  C     . ARG   A 1 42  ? 34.16600  22.45000  -7.85700  1.000 16.69654 ? 41  ARG   A C     1 
ATOM   329  O  O     . ARG   A 1 42  ? 34.52900  21.28300  -7.99000  1.000 18.47291 ? 41  ARG   A O     1 
ATOM   330  C  CB    . ARG   A 1 42  ? 34.76600  22.96000  -5.46400  1.000 20.55787 ? 41  ARG   A CB    1 
ATOM   331  C  CG    . ARG   A 1 42  ? 35.85100  23.96800  -5.61100  1.000 19.35788 ? 41  ARG   A CG    1 
ATOM   332  C  CD    . ARG   A 1 42  ? 36.61400  23.96200  -4.24100  1.000 23.51668 ? 41  ARG   A CD    1 
ATOM   333  N  NE    . ARG   A 1 42  ? 37.94000  24.54500  -4.31100  1.000 22.46906 ? 41  ARG   A NE    1 
ATOM   334  C  CZ    . ARG   A 1 42  ? 38.20300  25.83800  -4.17300  1.000 20.81381 ? 41  ARG   A CZ    1 
ATOM   335  N  NH1   . ARG   A 1 42  ? 37.23700  26.72700  -3.98500  1.000 24.52756 ? 41  ARG   A NH1   1 
ATOM   336  N  NH2   . ARG   A 1 42  ? 39.46400  26.24700  -4.21500  1.000 21.20511 ? 41  ARG   A NH2   1 
ATOM   337  N  N     . LYS   A 1 43  ? 34.20300  23.33100  -8.86400  1.000 15.28613 ? 42  LYS   A N     1 
ATOM   338  C  CA    . LYS   A 1 43  ? 34.66300  22.93900  -10.19200 1.000 16.46993 ? 42  LYS   A CA    1 
ATOM   339  C  C     . LYS   A 1 43  ? 35.31400  24.12900  -10.87400 1.000 17.07454 ? 42  LYS   A C     1 
ATOM   340  O  O     . LYS   A 1 43  ? 34.82600  25.25100  -10.74400 1.000 16.74554 ? 42  LYS   A O     1 
ATOM   341  C  CB    . LYS   A 1 43  ? 33.44200  22.52800  -11.03500 1.000 21.46249 ? 42  LYS   A CB    1 
ATOM   342  C  CG    . LYS   A 1 43  ? 33.76600  22.03600  -12.46100 1.000 23.29066 ? 42  LYS   A CG    1 
ATOM   343  C  CD    . LYS   A 1 43  ? 32.49200  21.82200  -13.27100 1.000 27.34568 ? 42  LYS   A CD    1 
ATOM   344  C  CE    . LYS   A 1 43  ? 32.76500  21.20300  -14.62400 1.000 29.23238 ? 42  LYS   A CE    1 
ATOM   345  N  NZ    . LYS   A 1 43  ? 33.53500  19.92000  -14.55300 1.000 31.45373 ? 42  LYS   A NZ    1 
ATOM   346  N  N     . GLN   A 1 44  ? 36.35600  23.87600  -11.64100 1.000 16.57118 ? 43  GLN   A N     1 
ATOM   347  C  CA    . GLN   A 1 44  ? 36.98500  24.89000  -12.46900 1.000 16.74105 ? 43  GLN   A CA    1 
ATOM   348  C  C     . GLN   A 1 44  ? 36.33300  24.84200  -13.84200 1.000 19.96732 ? 43  GLN   A C     1 
ATOM   349  O  O     . GLN   A 1 44  ? 36.18500  23.75500  -14.42900 1.000 22.83144 ? 43  GLN   A O     1 
ATOM   350  C  CB    . GLN   A 1 44  ? 38.47900  24.59300  -12.56300 1.000 17.40061 ? 43  GLN   A CB    1 
ATOM   351  C  CG    . GLN   A 1 44  ? 39.25500  25.57600  -13.42200 1.000 21.41890 ? 43  GLN   A CG    1 
ATOM   352  C  CD    . GLN   A 1 44  ? 40.73900  25.30100  -13.38600 1.000 23.32485 ? 43  GLN   A CD    1 
ATOM   353  O  OE1   . GLN   A 1 44  ? 41.33500  25.35000  -12.32600 1.000 32.98116 ? 43  GLN   A OE1   1 
ATOM   354  N  NE2   . GLN   A 1 44  ? 41.34000  25.01400  -14.53400 1.000 29.98776 ? 43  GLN   A NE2   1 
ATOM   355  N  N     . VAL   A 1 45  ? 35.96200  26.02000  -14.36500 1.000 17.61304 ? 44  VAL   A N     1 
ATOM   356  C  CA    . VAL   A 1 45  ? 35.29900  26.16600  -15.66300 1.000 19.89482 ? 44  VAL   A CA    1 
ATOM   357  C  C     . VAL   A 1 45  ? 35.91800  27.32800  -16.42400 1.000 20.15026 ? 44  VAL   A C     1 
ATOM   358  O  O     . VAL   A 1 45  ? 36.66800  28.13500  -15.87800 1.000 19.70921 ? 44  VAL   A O     1 
ATOM   359  C  CB    . VAL   A 1 45  ? 33.78600  26.42000  -15.52600 1.000 20.76909 ? 44  VAL   A CB    1 
ATOM   360  C  CG1   . VAL   A 1 45  ? 33.13900  25.30000  -14.70300 1.000 22.73551 ? 44  VAL   A CG1   1 
ATOM   361  C  CG2   . VAL   A 1 45  ? 33.55500  27.77600  -14.82400 1.000 19.17694 ? 44  VAL   A CG2   1 
ATOM   362  N  N     . VAL   A 1 46  ? 35.63400  27.40300  -17.71900 1.000 18.57981 ? 45  VAL   A N     1 
ATOM   363  C  CA    . VAL   A 1 46  ? 35.96700  28.55800  -18.53500 1.000 19.70908 ? 45  VAL   A CA    1 
ATOM   364  C  C     . VAL   A 1 46  ? 34.65500  29.06300  -19.09900 1.000 23.05337 ? 45  VAL   A C     1 
ATOM   365  O  O     . VAL   A 1 46  ? 33.91700  28.30000  -19.73800 1.000 25.03344 ? 45  VAL   A O     1 
ATOM   366  C  CB    . VAL   A 1 46  ? 36.91900  28.20600  -19.68200 1.000 23.32649 ? 45  VAL   A CB    1 
ATOM   367  C  CG1   . VAL   A 1 46  ? 37.24700  29.45800  -20.49800 1.000 24.27278 ? 45  VAL   A CG1   1 
ATOM   368  C  CG2   . VAL   A 1 46  ? 38.20100  27.58800  -19.14700 1.000 24.77928 ? 45  VAL   A CG2   1 
ATOM   369  N  N     . ILE   A 1 47  ? 34.33700  30.32300  -18.83300 1.000 18.90272 ? 46  ILE   A N     1 
ATOM   370  C  CA    . ILE   A 1 47  ? 33.10700  30.94400  -19.29700 1.000 19.05068 ? 46  ILE   A CA    1 
ATOM   371  C  C     . ILE   A 1 47  ? 33.50700  32.20300  -20.05200 1.000 21.80171 ? 46  ILE   A C     1 
ATOM   372  O  O     . ILE   A 1 47  ? 34.16500  33.09000  -19.49200 1.000 20.26899 ? 46  ILE   A O     1 
ATOM   373  C  CB    . ILE   A 1 47  ? 32.16600  31.27500  -18.13300 1.000 20.14669 ? 46  ILE   A CB    1 
ATOM   374  C  CG1   . ILE   A 1 47  ? 31.75300  29.98400  -17.42400 1.000 17.59814 ? 46  ILE   A CG1   1 
ATOM   375  C  CG2   . ILE   A 1 47  ? 30.92000  32.02000  -18.66700 1.000 24.24823 ? 46  ILE   A CG2   1 
ATOM   376  C  CD1   . ILE   A 1 47  ? 31.08700  30.23400  -16.11600 1.000 19.35519 ? 46  ILE   A CD1   1 
ATOM   377  N  N     . ASP   A 1 48  ? 33.13800  32.28100  -21.33300 1.000 20.15565 ? 47  ASP   A N     1 
ATOM   378  C  CA    . ASP   A 1 48  ? 33.44600  33.46600  -22.14200 1.000 22.65033 ? 47  ASP   A CA    1 
ATOM   379  C  C     . ASP   A 1 48  ? 34.94800  33.74000  -22.15800 1.000 22.81789 ? 47  ASP   A C     1 
ATOM   380  O  O     . ASP   A 1 48  ? 35.39900  34.89400  -22.18400 1.000 23.93047 ? 47  ASP   A O     1 
ATOM   381  C  CB    . ASP   A 1 48  ? 32.67300  34.70400  -21.66300 1.000 24.44825 ? 47  ASP   A CB    1 
ATOM   382  C  CG    . ASP   A 1 48  ? 31.17900  34.55300  -21.78200 1.000 25.10955 ? 47  ASP   A CG    1 
ATOM   383  O  OD1   . ASP   A 1 48  ? 30.70600  33.60100  -22.46200 1.000 23.66759 ? 47  ASP   A OD1   1 
ATOM   384  O  OD2   . ASP   A 1 48  ? 30.46200  35.36800  -21.17100 1.000 24.66886 ? 47  ASP   A OD2   1 
ATOM   385  N  N     . GLY   A 1 49  ? 35.73400  32.66900  -22.17100 1.000 22.43763 ? 48  GLY   A N     1 
ATOM   386  C  CA    . GLY   A 1 49  ? 37.16500  32.79000  -22.21900 1.000 24.42520 ? 48  GLY   A CA    1 
ATOM   387  C  C     . GLY   A 1 49  ? 37.83900  33.08700  -20.89700 1.000 26.65611 ? 48  GLY   A C     1 
ATOM   388  O  O     . GLY   A 1 49  ? 39.06400  33.22800  -20.88100 1.000 30.14509 ? 48  GLY   A O     1 
ATOM   389  N  N     . GLU   A 1 50  ? 37.08500  33.22200  -19.80800 1.000 21.66172 ? 49  GLU   A N     1 
ATOM   390  C  CA    . GLU   A 1 50  ? 37.62000  33.57100  -18.49300 1.000 21.35172 ? 49  GLU   A CA    1 
ATOM   391  C  C     . GLU   A 1 50  ? 37.48500  32.37800  -17.54800 1.000 19.13711 ? 49  GLU   A C     1 
ATOM   392  O  O     . GLU   A 1 50  ? 36.38900  31.84500  -17.37000 1.000 19.58654 ? 49  GLU   A O     1 
ATOM   393  C  CB    . GLU   A 1 50  ? 36.84100  34.75500  -17.90700 1.000 24.03932 ? 49  GLU   A CB    1 
ATOM   394  C  CG    . GLU   A 1 50  ? 37.03200  36.01100  -18.79300 1.000 25.41428 ? 49  GLU   A CG    1 
ATOM   395  C  CD    . GLU   A 1 50  ? 36.11800  37.19600  -18.44000 1.000 36.89193 ? 49  GLU   A CD    1 
ATOM   396  O  OE1   . GLU   A 1 50  ? 35.51400  37.24400  -17.34400 1.000 35.02041 ? 49  GLU   A OE1   1 
ATOM   397  O  OE2   . GLU   A 1 50  ? 36.02800  38.11400  -19.29000 1.000 38.59902 ? 49  GLU   A OE2   1 
ATOM   398  N  N     . THR   A 1 51  ? 38.60100  31.97000  -16.93500 1.000 19.71597 ? 50  THR   A N     1 
ATOM   399  C  CA    . THR   A 1 51  ? 38.58700  30.79900  -16.04900 1.000 16.98465 ? 50  THR   A CA    1 
ATOM   400  C  C     . THR   A 1 51  ? 38.09200  31.17100  -14.66900 1.000 18.19703 ? 50  THR   A C     1 
ATOM   401  O  O     . THR   A 1 51  ? 38.46600  32.22500  -14.11400 1.000 19.04726 ? 50  THR   A O     1 
ATOM   402  C  CB    . THR   A 1 51  ? 39.99800  30.21600  -15.94500 1.000 23.47948 ? 50  THR   A CB    1 
ATOM   403  O  OG1   . THR   A 1 51  ? 40.49300  29.93900  -17.26900 1.000 26.59924 ? 50  THR   A OG1   1 
ATOM   404  C  CG2   . THR   A 1 51  ? 39.99600  28.93400  -15.06900 1.000 22.68286 ? 50  THR   A CG2   1 
ATOM   405  N  N     . SER   A 1 52  ? 37.26200  30.29400  -14.12000 1.000 16.41089 ? 51  SER   A N     1 
ATOM   406  C  CA    . SER   A 1 52  ? 36.70400  30.56900  -12.81400 1.000 15.86563 ? 51  SER   A CA    1 
ATOM   407  C  C     . SER   A 1 52  ? 36.57900  29.29100  -11.99900 1.000 17.71284 ? 51  SER   A C     1 
ATOM   408  O  O     . SER   A 1 52  ? 36.38600  28.20700  -12.56100 1.000 18.48974 ? 51  SER   A O     1 
ATOM   409  C  CB    . SER   A 1 52  ? 35.30900  31.17500  -12.93400 1.000 18.26065 ? 51  SER   A CB    1 
ATOM   410  O  OG    . SER   A 1 52  ? 35.41600  32.43400  -13.57900 1.000 19.31453 ? 51  SER   A OG    1 
ATOM   411  N  N     . LEU   A 1 53  ? 36.62600  29.42400  -10.67500 1.000 14.86539 ? 52  LEU   A N     1 
ATOM   412  C  CA    . LEU   A 1 53  ? 36.20400  28.34500  -9.79500  1.000 14.56847 ? 52  LEU   A CA    1 
ATOM   413  C  C     . LEU   A 1 53  ? 34.76000  28.59800  -9.41300  1.000 15.31834 ? 52  LEU   A C     1 
ATOM   414  O  O     . LEU   A 1 53  ? 34.43800  29.67700  -8.92300  1.000 15.25073 ? 52  LEU   A O     1 
ATOM   415  C  CB    . LEU   A 1 53  ? 37.06400  28.34200  -8.52900  1.000 17.18906 ? 52  LEU   A CB    1 
ATOM   416  C  CG    . LEU   A 1 53  ? 38.52900  27.99900  -8.69800  1.000 21.55026 ? 52  LEU   A CG    1 
ATOM   417  C  CD1   . LEU   A 1 53  ? 39.37700  28.16500  -7.40600  1.000 23.09828 ? 52  LEU   A CD1   1 
ATOM   418  C  CD2   . LEU   A 1 53  ? 38.59800  26.55800  -9.16600  1.000 29.61063 ? 52  LEU   A CD2   1 
ATOM   419  N  N     . LEU   A 1 54  ? 33.87700  27.62900  -9.61100  1.000 13.94289 ? 53  LEU   A N     1 
ATOM   420  C  CA    . LEU   A 1 54  ? 32.51600  27.71800  -9.09600  1.000 14.59334 ? 53  LEU   A CA    1 
ATOM   421  C  C     . LEU   A 1 54  ? 32.40600  26.94500  -7.78300  1.000 15.64380 ? 53  LEU   A C     1 
ATOM   422  O  O     . LEU   A 1 54  ? 32.72800  25.75000  -7.73700  1.000 15.80948 ? 53  LEU   A O     1 
ATOM   423  C  CB    . LEU   A 1 54  ? 31.52500  27.13900  -10.10300 1.000 13.57167 ? 53  LEU   A CB    1 
ATOM   424  C  CG    . LEU   A 1 54  ? 31.63700  27.71600  -11.48400 1.000 15.42569 ? 53  LEU   A CG    1 
ATOM   425  C  CD1   . LEU   A 1 54  ? 30.50600  27.18200  -12.38000 1.000 19.55000 ? 53  LEU   A CD1   1 
ATOM   426  C  CD2   . LEU   A 1 54  ? 31.66700  29.25800  -11.53700 1.000 16.34609 ? 53  LEU   A CD2   1 
ATOM   427  N  N     . ASP   A 1 55  ? 31.96600  27.59800  -6.73700  1.000 14.34177 ? 54  ASP   A N     1 
ATOM   428  C  CA    . ASP   A 1 55  ? 31.63800  26.93300  -5.48800  1.000 14.07634 ? 54  ASP   A CA    1 
ATOM   429  C  C     . ASP   A 1 55  ? 30.12400  26.90500  -5.41300  1.000 14.32985 ? 54  ASP   A C     1 
ATOM   430  O  O     . ASP   A 1 55  ? 29.50500  27.96300  -5.25800  1.000 16.42362 ? 54  ASP   A O     1 
ATOM   431  C  CB    . ASP   A 1 55  ? 32.18200  27.72000  -4.30900  1.000 15.45476 ? 54  ASP   A CB    1 
ATOM   432  C  CG    . ASP   A 1 55  ? 33.64700  27.84500  -4.35000  1.000 25.31224 ? 54  ASP   A CG    1 
ATOM   433  O  OD1   . ASP   A 1 55  ? 34.33900  26.81300  -4.52100  1.000 27.24101 ? 54  ASP   A OD1   1 
ATOM   434  O  OD2   . ASP   A 1 55  ? 34.09400  28.99300  -4.23500  1.000 22.87095 ? 54  ASP   A OD2   1 
ATOM   435  N  N     . ILE   A 1 56  ? 29.52600  25.72100  -5.52600  1.000 13.46927 ? 55  ILE   A N     1 
ATOM   436  C  CA    . ILE   A 1 56  ? 28.07600  25.60500  -5.67100  1.000 12.34328 ? 55  ILE   A CA    1 
ATOM   437  C  C     . ILE   A 1 56  ? 27.51800  25.01200  -4.38700  1.000 14.68928 ? 55  ILE   A C     1 
ATOM   438  O  O     . ILE   A 1 56  ? 27.96100  23.93700  -3.96200  1.000 15.50540 ? 55  ILE   A O     1 
ATOM   439  C  CB    . ILE   A 1 56  ? 27.69400  24.75200  -6.88600  1.000 14.64826 ? 55  ILE   A CB    1 
ATOM   440  C  CG1   . ILE   A 1 56  ? 28.31600  25.39700  -8.13900  1.000 20.09978 ? 55  ILE   A CG1   1 
ATOM   441  C  CG2   . ILE   A 1 56  ? 26.17200  24.64400  -6.99000  1.000 16.70914 ? 55  ILE   A CG2   1 
ATOM   442  C  CD1   . ILE   A 1 56  ? 28.12900  24.64800  -9.38700  1.000 23.31261 ? 55  ILE   A CD1   1 
ATOM   443  N  N     . LEU   A 1 57  ? 26.57300  25.70700  -3.76800  1.000 12.58821 ? 56  LEU   A N     1 
ATOM   444  C  CA    . LEU   A 1 57  ? 25.84800  25.20200  -2.61100  1.000 12.99011 ? 56  LEU   A CA    1 
ATOM   445  C  C     . LEU   A 1 57  ? 24.48100  24.72100  -3.07100  1.000 12.37869 ? 56  LEU   A C     1 
ATOM   446  O  O     . LEU   A 1 57  ? 23.67500  25.50700  -3.58700  1.000 13.47634 ? 56  LEU   A O     1 
ATOM   447  C  CB    . LEU   A 1 57  ? 25.72600  26.29400  -1.54000  1.000 13.74765 ? 56  LEU   A CB    1 
ATOM   448  C  CG    . LEU   A 1 57  ? 24.96600  25.87600  -0.28600  1.000 14.06182 ? 56  LEU   A CG    1 
ATOM   449  C  CD1   . LEU   A 1 57  ? 25.74000  24.89800  0.55700   1.000 16.13730 ? 56  LEU   A CD1   1 
ATOM   450  C  CD2   . LEU   A 1 57  ? 24.63100  27.05100  0.54600   1.000 17.09018 ? 56  LEU   A CD2   1 
ATOM   451  N  N     . ASP   A 1 58  ? 24.23800  23.42700  -2.89100  1.000 13.23477 ? 57  ASP   A N     1 
ATOM   452  C  CA    . ASP   A 1 58  ? 22.98000  22.80000  -3.26100  1.000 14.94872 ? 57  ASP   A CA    1 
ATOM   453  C  C     . ASP   A 1 58  ? 22.14800  22.71000  -1.97200  1.000 14.86069 ? 57  ASP   A C     1 
ATOM   454  O  O     . ASP   A 1 58  ? 22.53800  22.02500  -1.01300  1.000 14.93467 ? 57  ASP   A O     1 
ATOM   455  C  CB    . ASP   A 1 58  ? 23.30400  21.43000  -3.85900  1.000 16.94818 ? 57  ASP   A CB    1 
ATOM   456  C  CG    . ASP   A 1 58  ? 22.10400  20.67500  -4.30700  1.000 18.21674 ? 57  ASP   A CG    1 
ATOM   457  O  OD1   . ASP   A 1 58  ? 21.02400  21.31200  -4.53600  1.000 19.59631 ? 57  ASP   A OD1   1 
ATOM   458  O  OD2   . ASP   A 1 58  ? 22.24100  19.41900  -4.39900  1.000 19.14333 ? 57  ASP   A OD2   1 
ATOM   459  N  N     . THR   A 1 59  ? 21.04700  23.46000  -1.90300  1.000 13.93192 ? 58  THR   A N     1 
ATOM   460  C  CA    . THR   A 1 59  ? 20.24800  23.56000  -0.68700  1.000 14.34962 ? 58  THR   A CA    1 
ATOM   461  C  C     . THR   A 1 59  ? 19.07300  22.60100  -0.74500  1.000 15.33666 ? 58  THR   A C     1 
ATOM   462  O  O     . THR   A 1 59  ? 18.65700  22.17600  -1.81800  1.000 14.93260 ? 58  THR   A O     1 
ATOM   463  C  CB    . THR   A 1 59  ? 19.72700  24.99400  -0.48400  1.000 14.64945 ? 58  THR   A CB    1 
ATOM   464  O  OG1   . THR   A 1 59  ? 18.72000  25.29800  -1.47100  1.000 15.37050 ? 58  THR   A OG1   1 
ATOM   465  C  CG2   . THR   A 1 59  ? 20.85000  25.99100  -0.54100  1.000 14.37317 ? 58  THR   A CG2   1 
ATOM   466  N  N     . ALA   A 1 60  ? 18.54900  22.24600  0.43300   1.000 15.45704 ? 59  ALA   A N     1 
ATOM   467  C  CA    . ALA   A 1 60  ? 17.30500  21.49100  0.51700   1.000 15.08066 ? 59  ALA   A CA    1 
ATOM   468  C  C     . ALA   A 1 60  ? 16.12800  22.39100  0.15200   1.000 17.14602 ? 59  ALA   A C     1 
ATOM   469  O  O     . ALA   A 1 60  ? 16.11300  23.58200  0.47700   1.000 18.93144 ? 59  ALA   A O     1 
ATOM   470  C  CB    . ALA   A 1 60  ? 17.13400  21.01000  1.96700   1.000 17.39132 ? 59  ALA   A CB    1 
ATOM   471  N  N     . GLY   A 1 61  ? 15.09500  21.81400  -0.46000  1.000 16.54163 ? 60  GLY   A N     1 
ATOM   472  C  CA    . GLY   A 1 61  ? 13.87800  22.55800  -0.83100  1.000 21.06547 ? 60  GLY   A CA    1 
ATOM   473  C  C     . GLY   A 1 61  ? 12.87700  22.67800  0.30000   1.000 27.12622 ? 60  GLY   A C     1 
ATOM   474  O  O     . GLY   A 1 61  ? 11.75500  22.17800  0.14000   1.000 39.84734 ? 60  GLY   A O     1 
ATOM   475  N  N     . GLN   A 1 62  ? 13.29500  23.18300  1.42400   1.000 26.76444 ? 61  GLN   A N     1 
ATOM   476  C  CA    . GLN   A 1 62  ? 12.47700  23.45700  2.58800   1.000 29.77816 ? 61  GLN   A CA    1 
ATOM   477  C  C     . GLN   A 1 62  ? 12.85700  24.85300  3.02200   1.000 29.60055 ? 61  GLN   A C     1 
ATOM   478  O  O     . GLN   A 1 62  ? 13.98600  25.28000  2.80500   1.000 33.54277 ? 61  GLN   A O     1 
ATOM   479  C  CB    . GLN   A 1 62  ? 12.86300  22.48900  3.70000   1.000 31.96473 ? 61  GLN   A CB    1 
ATOM   480  C  CG    . GLN   A 1 62  ? 14.34200  22.53200  4.11500   1.000 29.46250 ? 61  GLN   A CG    1 
ATOM   481  C  CD    . GLN   A 1 62  ? 14.57700  23.28100  5.42300   1.000 39.36201 ? 61  GLN   A CD    1 
ATOM   482  O  OE1   . GLN   A 1 62  ? 13.94300  22.99200  6.44300   1.000 41.70263 ? 61  GLN   A OE1   1 
ATOM   483  N  NE2   . GLN   A 1 62  ? 15.50500  24.23000  5.40300   1.000 28.15065 ? 61  GLN   A NE2   1 
ATOM   484  N  N     . GLU   A 1 63  ? 11.90800  25.58300  3.59600   1.000 38.16572 ? 62  GLU   A N     1 
ATOM   485  C  CA    . GLU   A 1 63  ? 12.20000  26.92500  4.07100   1.000 42.86391 ? 62  GLU   A CA    1 
ATOM   486  C  C     . GLU   A 1 63  ? 12.31400  27.00700  5.58600   1.000 41.20019 ? 62  GLU   A C     1 
ATOM   487  O  O     . GLU   A 1 63  ? 12.55600  28.09800  6.11500   1.000 44.68871 ? 62  GLU   A O     1 
ATOM   488  C  CB    . GLU   A 1 63  ? 11.18600  27.93800  3.52700   1.000 41.19368 ? 62  GLU   A CB    1 
ATOM   489  C  CG    . GLU   A 1 63  ? 11.27800  28.17200  2.03000   1.000 39.05583 ? 62  GLU   A CG    1 
ATOM   490  C  CD    . GLU   A 1 63  ? 9.91200   28.24800  1.37700   1.000 49.37589 ? 62  GLU   A CD    1 
ATOM   491  O  OE1   . GLU   A 1 63  ? 9.17800   27.22900  1.38400   1.000 50.35972 ? 62  GLU   A OE1   1 
ATOM   492  O  OE2   . GLU   A 1 63  ? 9.56500   29.33400  0.87400   1.000 47.79459 ? 62  GLU   A OE2   1 
ATOM   493  N  N     . GLU   A 1 64  ? 12.14900  25.89100  6.29600   1.000 39.58341 ? 63  GLU   A N     1 
ATOM   494  C  CA    . GLU   A 1 64  ? 12.48200  25.87200  7.70900   1.000 42.24919 ? 63  GLU   A CA    1 
ATOM   495  C  C     . GLU   A 1 64  ? 13.99800  26.02800  7.87800   1.000 30.39394 ? 63  GLU   A C     1 
ATOM   496  O  O     . GLU   A 1 64  ? 14.78300  25.97200  6.91700   1.000 35.15849 ? 63  GLU   A O     1 
ATOM   497  C  CB    . GLU   A 1 64  ? 11.90900  24.61900  8.39200   1.000 41.42211 ? 63  GLU   A CB    1 
ATOM   498  C  CG    . GLU   A 1 64  ? 11.82000  24.68600  9.92700   1.000 47.20111 ? 63  GLU   A CG    1 
ATOM   499  C  CD    . GLU   A 1 64  ? 11.07200  23.50200  10.57000  1.000 51.29867 ? 63  GLU   A CD    1 
ATOM   500  O  OE1   . GLU   A 1 64  ? 11.41600  22.33100  10.29500  1.000 49.62437 ? 63  GLU   A OE1   1 
ATOM   501  O  OE2   . GLU   A 1 64  ? 10.13200  23.74800  11.35700  1.000 55.22110 ? 63  GLU   A OE2   1 
ATOM   502  N  N     . TYR   A 1 65  ? 14.40000  26.25500  9.11700   1.000 26.47756 ? 64  TYR   A N     1 
ATOM   503  C  CA    . TYR   A 1 65  ? 15.78000  26.52900  9.49600   1.000 23.77565 ? 64  TYR   A CA    1 
ATOM   504  C  C     . TYR   A 1 65  ? 16.24200  27.88000  8.96700   1.000 23.47278 ? 64  TYR   A C     1 
ATOM   505  O  O     . TYR   A 1 65  ? 17.25300  27.99600  8.27900   1.000 22.20919 ? 64  TYR   A O     1 
ATOM   506  C  CB    . TYR   A 1 65  ? 16.73100  25.36900  9.18100   1.000 22.59279 ? 64  TYR   A CB    1 
ATOM   507  C  CG    . TYR   A 1 65  ? 16.21400  24.08200  9.86800   1.000 18.67721 ? 64  TYR   A CG    1 
ATOM   508  C  CD1   . TYR   A 1 65  ? 16.14200  23.99000  11.26100  1.000 20.77846 ? 64  TYR   A CD1   1 
ATOM   509  C  CD2   . TYR   A 1 65  ? 15.74400  23.01600  9.11800   1.000 18.34352 ? 64  TYR   A CD2   1 
ATOM   510  C  CE1   . TYR   A 1 65  ? 15.66700  22.84200  11.91600  1.000 19.73439 ? 64  TYR   A CE1   1 
ATOM   511  C  CE2   . TYR   A 1 65  ? 15.24200  21.86000  9.73000   1.000 17.00731 ? 64  TYR   A CE2   1 
ATOM   512  C  CZ    . TYR   A 1 65  ? 15.21100  21.77600  11.12500  1.000 19.18731 ? 64  TYR   A CZ    1 
ATOM   513  O  OH    . TYR   A 1 65  ? 14.72100  20.65600  11.76600  1.000 19.00451 ? 64  TYR   A OH    1 
ATOM   514  N  N     . SER   A 1 66  ? 15.49900  28.91700  9.36200   1.000 27.74302 ? 65  SER   A N     1 
ATOM   515  C  CA    . SER   A 1 66  ? 15.73800  30.24100  8.80400   1.000 24.33833 ? 65  SER   A CA    1 
ATOM   516  C  C     . SER   A 1 66  ? 17.14100  30.75300  9.11400   1.000 23.85257 ? 65  SER   A C     1 
ATOM   517  O  O     . SER   A 1 66  ? 17.71900  31.48400  8.30900   1.000 22.20240 ? 65  SER   A O     1 
ATOM   518  C  CB    . SER   A 1 66  ? 14.68000  31.23200  9.30200   1.000 30.42988 ? 65  SER   A CB    1 
ATOM   519  O  OG    . SER   A 1 66  ? 14.68600  31.31000  10.71400  1.000 39.63220 ? 65  SER   A OG    1 
ATOM   520  N  N     . ALA   A 1 67  ? 17.68700  30.44700  10.28600  1.000 20.30468 ? 66  ALA   A N     1 
ATOM   521  C  CA    . ALA   A 1 67  ? 19.03800  30.90500  10.60700  1.000 25.49447 ? 66  ALA   A CA    1 
ATOM   522  C  C     . ALA   A 1 67  ? 20.03400  30.36500  9.58500   1.000 21.96965 ? 66  ALA   A C     1 
ATOM   523  O  O     . ALA   A 1 67  ? 20.86300  31.10500  9.03800   1.000 20.57316 ? 66  ALA   A O     1 
ATOM   524  C  CB    . ALA   A 1 67  ? 19.41100  30.50000  12.03800  1.000 27.54684 ? 66  ALA   A CB    1 
ATOM   525  N  N     A MET   A 1 68  ? 19.93700  29.07300  9.28100   0.500 17.99573 ? 67  MET   A N     1 
ATOM   526  N  N     B MET   A 1 68  ? 19.93200  29.07400  9.28100   0.500 17.99861 ? 67  MET   A N     1 
ATOM   527  C  CA    A MET   A 1 68  ? 20.84800  28.48200  8.31100   0.500 18.69334 ? 67  MET   A CA    1 
ATOM   528  C  CA    B MET   A 1 68  ? 20.83100  28.47000  8.31000   0.500 18.70399 ? 67  MET   A CA    1 
ATOM   529  C  C     A MET   A 1 68  ? 20.57600  29.02600  6.91600   0.500 16.88116 ? 67  MET   A C     1 
ATOM   530  C  C     B MET   A 1 68  ? 20.57200  29.01900  6.91800   0.500 16.87616 ? 67  MET   A C     1 
ATOM   531  O  O     A MET   A 1 68  ? 21.50700  29.41400  6.20200   0.500 16.85757 ? 67  MET   A O     1 
ATOM   532  O  O     B MET   A 1 68  ? 21.50900  29.40200  6.20800   0.500 16.89135 ? 67  MET   A O     1 
ATOM   533  C  CB    A MET   A 1 68  ? 20.70900  26.96000  8.33400   0.500 21.42331 ? 67  MET   A CB    1 
ATOM   534  C  CB    B MET   A 1 68  ? 20.64600  26.95400  8.34100   0.500 21.40177 ? 67  MET   A CB    1 
ATOM   535  C  CG    A MET   A 1 68  ? 21.77000  26.26400  7.51900   0.500 15.40986 ? 67  MET   A CG    1 
ATOM   536  C  CG    B MET   A 1 68  ? 21.49300  26.30200  9.41300   0.500 21.07284 ? 67  MET   A CG    1 
ATOM   537  S  SD    A MET   A 1 68  ? 23.47100  26.53600  8.09600   0.500 18.57493 ? 67  MET   A SD    1 
ATOM   538  S  SD    B MET   A 1 68  ? 23.23900  26.36000  9.05200   0.500 24.34985 ? 67  MET   A SD    1 
ATOM   539  C  CE    A MET   A 1 68  ? 23.26500  25.86500  9.74900   0.500 25.60916 ? 67  MET   A CE    1 
ATOM   540  C  CE    B MET   A 1 68  ? 23.33100  25.08600  7.78800   0.500 26.47771 ? 67  MET   A CE    1 
ATOM   541  N  N     . ARG   A 1 69  ? 19.30700  29.06700  6.50300   1.000 17.42708 ? 68  ARG   A N     1 
ATOM   542  C  CA    . ARG   A 1 69  ? 19.00700  29.52700  5.14800   1.000 19.09384 ? 68  ARG   A CA    1 
ATOM   543  C  C     . ARG   A 1 69  ? 19.35300  30.99600  4.95700   1.000 15.80359 ? 68  ARG   A C     1 
ATOM   544  O  O     . ARG   A 1 69  ? 19.86800  31.37800  3.89200   1.000 16.48868 ? 68  ARG   A O     1 
ATOM   545  C  CB    . ARG   A 1 69  ? 17.56700  29.24300  4.77000   1.000 23.16542 ? 68  ARG   A CB    1 
ATOM   546  C  CG    . ARG   A 1 69  ? 17.26700  27.75300  4.75500   1.000 25.51794 ? 68  ARG   A CG    1 
ATOM   547  C  CD    . ARG   A 1 69  ? 15.88200  27.48100  4.19600   1.000 26.41292 ? 68  ARG   A CD    1 
ATOM   548  N  NE    . ARG   A 1 69  ? 15.69000  28.04600  2.86400   1.000 27.55045 ? 68  ARG   A NE    1 
ATOM   549  C  CZ    . ARG   A 1 69  ? 15.99800  27.42100  1.73100   1.000 28.38534 ? 68  ARG   A CZ    1 
ATOM   550  N  NH1   . ARG   A 1 69  ? 16.59100  26.23200  1.72900   1.000 25.87036 ? 68  ARG   A NH1   1 
ATOM   551  N  NH2   . ARG   A 1 69  ? 15.70800  28.00600  0.57100   1.000 27.91377 ? 68  ARG   A NH2   1 
ATOM   552  N  N     . ASP   A 1 70  ? 19.16700  31.81100  5.99700   1.000 16.98280 ? 69  ASP   A N     1 
ATOM   553  C  CA    . ASP   A 1 70  ? 19.60200  33.20600  5.89900   1.000 17.43732 ? 69  ASP   A CA    1 
ATOM   554  C  C     . ASP   A 1 70  ? 21.10500  33.28700  5.65400   1.000 18.10302 ? 69  ASP   A C     1 
ATOM   555  O  O     . ASP   A 1 70  ? 21.57500  34.13100  4.87800   1.000 15.66149 ? 69  ASP   A O     1 
ATOM   556  C  CB    . ASP   A 1 70  ? 19.23300  34.00300  7.15500   1.000 19.00942 ? 69  ASP   A CB    1 
ATOM   557  C  CG    . ASP   A 1 70  ? 17.72700  34.24800  7.32400   1.000 20.20957 ? 69  ASP   A CG    1 
ATOM   558  O  OD1   . ASP   A 1 70  ? 16.95700  33.90000  6.42400   1.000 21.20833 ? 69  ASP   A OD1   1 
ATOM   559  O  OD2   . ASP   A 1 70  ? 17.34000  34.80900  8.36600   1.000 24.51409 ? 69  ASP   A OD2   1 
ATOM   560  N  N     . GLN   A 1 71  ? 21.88500  32.47900  6.36300   1.000 15.90559 ? 70  GLN   A N     1 
ATOM   561  C  CA    . GLN   A 1 71  ? 23.32400  32.49900  6.14500   1.000 15.44965 ? 70  GLN   A CA    1 
ATOM   562  C  C     . GLN   A 1 71  ? 23.66200  32.05600  4.72800   1.000 15.13697 ? 70  GLN   A C     1 
ATOM   563  O  O     . GLN   A 1 71  ? 24.55700  32.63600  4.09400   1.000 15.29143 ? 70  GLN   A O     1 
ATOM   564  C  CB    . GLN   A 1 71  ? 24.04700  31.64400  7.19400   1.000 16.46513 ? 70  GLN   A CB    1 
ATOM   565  C  CG    . GLN   A 1 71  ? 25.58100  31.83600  7.14500   1.000 18.04623 ? 70  GLN   A CG    1 
ATOM   566  C  CD    . GLN   A 1 71  ? 26.01300  33.30200  7.29100   1.000 18.50480 ? 70  GLN   A CD    1 
ATOM   567  O  OE1   . GLN   A 1 71  ? 25.75000  33.92600  8.29800   1.000 20.37474 ? 70  GLN   A OE1   1 
ATOM   568  N  NE2   . GLN   A 1 71  ? 26.70100  33.82500  6.28900   1.000 21.10788 ? 70  GLN   A NE2   1 
ATOM   569  N  N     . TYR   A 1 72  ? 22.94300  31.06500  4.17700   1.000 14.85670 ? 71  TYR   A N     1 
ATOM   570  C  CA    . TYR   A 1 72  ? 23.20900  30.67600  2.78900   1.000 14.76876 ? 71  TYR   A CA    1 
ATOM   571  C  C     . TYR   A 1 72  ? 23.07200  31.87300  1.86400   1.000 14.05652 ? 71  TYR   A C     1 
ATOM   572  O  O     . TYR   A 1 72  ? 23.88000  32.06000  0.94200   1.000 16.06965 ? 71  TYR   A O     1 
ATOM   573  C  CB    . TYR   A 1 72  ? 22.18400  29.64200  2.30900   1.000 15.84123 ? 71  TYR   A CB    1 
ATOM   574  C  CG    . TYR   A 1 72  ? 22.18700  28.27000  2.95900   1.000 14.02355 ? 71  TYR   A CG    1 
ATOM   575  C  CD1   . TYR   A 1 72  ? 23.28900  27.77700  3.66500   1.000 15.47112 ? 71  TYR   A CD1   1 
ATOM   576  C  CD2   . TYR   A 1 72  ? 21.05300  27.48600  2.88400   1.000 14.92184 ? 71  TYR   A CD2   1 
ATOM   577  C  CE1   . TYR   A 1 72  ? 23.25600  26.51100  4.20600   1.000 16.41230 ? 71  TYR   A CE1   1 
ATOM   578  C  CE2   . TYR   A 1 72  ? 21.01800  26.20900  3.41600   1.000 14.61137 ? 71  TYR   A CE2   1 
ATOM   579  C  CZ    . TYR   A 1 72  ? 22.11800  25.75000  4.04200   1.000 14.12886 ? 71  TYR   A CZ    1 
ATOM   580  O  OH    . TYR   A 1 72  ? 22.04400  24.44900  4.53400   1.000 15.48070 ? 71  TYR   A OH    1 
ATOM   581  N  N     . MET   A 1 73  ? 22.04000  32.68500  2.10600   1.000 14.21934 ? 72  MET   A N     1 
ATOM   582  C  CA    . MET   A 1 73  ? 21.74400  33.81700  1.24600   1.000 14.54479 ? 72  MET   A CA    1 
ATOM   583  C  C     . MET   A 1 73  ? 22.71000  34.96600  1.47600   1.000 16.62000 ? 72  MET   A C     1 
ATOM   584  O  O     . MET   A 1 73  ? 23.09900  35.62200  0.50200   1.000 16.33462 ? 72  MET   A O     1 
ATOM   585  C  CB    . MET   A 1 73  ? 20.29400  34.21800  1.41900   1.000 15.39446 ? 72  MET   A CB    1 
ATOM   586  C  CG    . MET   A 1 73  ? 19.37900  33.12900  0.90600   1.000 19.25955 ? 72  MET   A CG    1 
ATOM   587  S  SD    . MET   A 1 73  ? 17.66900  33.55100  1.22600   1.000 20.47917 ? 72  MET   A SD    1 
ATOM   588  C  CE    . MET   A 1 73  ? 16.90700  32.09800  0.50600   1.000 20.33338 ? 72  MET   A CE    1 
ATOM   589  N  N     . ARG   A 1 74  ? 23.20200  35.15000  2.70400   1.000 15.13664 ? 73  ARG   A N     1 
ATOM   590  C  CA    . ARG   A 1 74  ? 24.18200  36.20800  2.94300   1.000 17.03175 ? 73  ARG   A CA    1 
ATOM   591  C  C     . ARG   A 1 74  ? 25.49400  35.88800  2.24900   1.000 15.71310 ? 73  ARG   A C     1 
ATOM   592  O  O     . ARG   A 1 74  ? 26.11500  36.78000  1.66500   1.000 18.39067 ? 73  ARG   A O     1 
ATOM   593  C  CB    . ARG   A 1 74  ? 24.43100  36.39900  4.44000   1.000 17.16453 ? 73  ARG   A CB    1 
ATOM   594  C  CG    . ARG   A 1 74  ? 23.31400  37.16000  5.09800   1.000 17.71186 ? 73  ARG   A CG    1 
ATOM   595  C  CD    . ARG   A 1 74  ? 23.74700  37.66800  6.45200   1.000 23.33350 ? 73  ARG   A CD    1 
ATOM   596  N  NE    . ARG   A 1 74  ? 23.88600  36.56200  7.37500   1.000 24.05562 ? 73  ARG   A NE    1 
ATOM   597  C  CZ    . ARG   A 1 74  ? 22.91300  36.12600  8.16400   1.000 21.18081 ? 73  ARG   A CZ    1 
ATOM   598  N  NH1   . ARG   A 1 74  ? 21.72200  36.70700  8.18900   1.000 24.75978 ? 73  ARG   A NH1   1 
ATOM   599  N  NH2   . ARG   A 1 74  ? 23.13900  35.08900  8.95800   1.000 22.58137 ? 73  ARG   A NH2   1 
ATOM   600  N  N     . THR   A 1 75  ? 25.91800  34.62800  2.29200   1.000 15.17442 ? 74  THR   A N     1 
ATOM   601  C  CA    . THR   A 1 75  ? 27.19200  34.21700  1.70800   1.000 17.25845 ? 74  THR   A CA    1 
ATOM   602  C  C     . THR   A 1 75  ? 27.11600  34.10900  0.18900   1.000 18.36020 ? 74  THR   A C     1 
ATOM   603  O  O     . THR   A 1 75  ? 28.09900  34.39100  -0.49400  1.000 17.41299 ? 74  THR   A O     1 
ATOM   604  C  CB    . THR   A 1 75  ? 27.59100  32.86600  2.32800   1.000 16.52332 ? 74  THR   A CB    1 
ATOM   605  O  OG1   . THR   A 1 75  ? 27.84700  33.05700  3.72100   1.000 20.39720 ? 74  THR   A OG1   1 
ATOM   606  C  CG2   . THR   A 1 75  ? 28.85500  32.31400  1.68300   1.000 21.32631 ? 74  THR   A CG2   1 
ATOM   607  N  N     . GLY   A 1 76  ? 25.96700  33.71100  -0.35600  1.000 13.99836 ? 75  GLY   A N     1 
ATOM   608  C  CA    . GLY   A 1 76  ? 25.85700  33.46100  -1.79800  1.000 14.86890 ? 75  GLY   A CA    1 
ATOM   609  C  C     . GLY   A 1 76  ? 25.95200  34.75800  -2.59700  1.000 13.51914 ? 75  GLY   A C     1 
ATOM   610  O  O     . GLY   A 1 76  ? 25.42800  35.80300  -2.20300  1.000 15.53581 ? 75  GLY   A O     1 
ATOM   611  N  N     . GLU   A 1 77  ? 26.64500  34.67700  -3.72800  1.000 13.54970 ? 76  GLU   A N     1 
ATOM   612  C  CA    . GLU   A 1 77  ? 26.77300  35.81500  -4.63400  1.000 13.41680 ? 76  GLU   A CA    1 
ATOM   613  C  C     . GLU   A 1 77  ? 25.71200  35.83400  -5.71500  1.000 14.31731 ? 76  GLU   A C     1 
ATOM   614  O  O     . GLU   A 1 77  ? 25.42700  36.90400  -6.30100  1.000 15.80586 ? 76  GLU   A O     1 
ATOM   615  C  CB    . GLU   A 1 77  ? 28.16800  35.82500  -5.28300  1.000 15.47057 ? 76  GLU   A CB    1 
ATOM   616  C  CG    . GLU   A 1 77  ? 29.28900  36.13000  -4.32000  1.000 17.40210 ? 76  GLU   A CG    1 
ATOM   617  C  CD    . GLU   A 1 77  ? 30.61500  36.02400  -4.99500  1.000 20.75660 ? 76  GLU   A CD    1 
ATOM   618  O  OE1   . GLU   A 1 77  ? 31.15900  34.90100  -5.08000  1.000 19.85392 ? 76  GLU   A OE1   1 
ATOM   619  O  OE2   . GLU   A 1 77  ? 31.11100  37.07200  -5.46300  1.000 28.39692 ? 76  GLU   A OE2   1 
ATOM   620  N  N     . GLY   A 1 78  ? 25.19300  34.67600  -6.05900  1.000 13.82752 ? 77  GLY   A N     1 
ATOM   621  C  CA    . GLY   A 1 78  ? 24.17300  34.58700  -7.08400  1.000 13.70156 ? 77  GLY   A CA    1 
ATOM   622  C  C     . GLY   A 1 78  ? 23.37200  33.32500  -6.85300  1.000 11.95001 ? 77  GLY   A C     1 
ATOM   623  O  O     . GLY   A 1 78  ? 23.85300  32.35300  -6.24500  1.000 13.17328 ? 77  GLY   A O     1 
ATOM   624  N  N     . PHE   A 1 79  ? 22.12500  33.35100  -7.33400  1.000 12.68315 ? 78  PHE   A N     1 
ATOM   625  C  CA    . PHE   A 1 79  ? 21.14200  32.31900  -7.00100  1.000 11.60726 ? 78  PHE   A CA    1 
ATOM   626  C  C     . PHE   A 1 79  ? 20.46100  31.80000  -8.25900  1.000 12.26535 ? 78  PHE   A C     1 
ATOM   627  O  O     . PHE   A 1 79  ? 19.96400  32.59000  -9.07700  1.000 13.38680 ? 78  PHE   A O     1 
ATOM   628  C  CB    . PHE   A 1 79  ? 20.09500  32.88000  -6.00500  1.000 13.27865 ? 78  PHE   A CB    1 
ATOM   629  C  CG    . PHE   A 1 79  ? 20.73600  33.40500  -4.76600  1.000 12.93847 ? 78  PHE   A CG    1 
ATOM   630  C  CD1   . PHE   A 1 79  ? 21.29100  34.67600  -4.74600  1.000 14.43721 ? 78  PHE   A CD1   1 
ATOM   631  C  CD2   . PHE   A 1 79  ? 20.86900  32.58700  -3.64800  1.000 14.76034 ? 78  PHE   A CD2   1 
ATOM   632  C  CE1   . PHE   A 1 79  ? 21.97600  35.12400  -3.64000  1.000 14.57724 ? 78  PHE   A CE1   1 
ATOM   633  C  CE2   . PHE   A 1 79  ? 21.56600  33.04400  -2.50800  1.000 13.56322 ? 78  PHE   A CE2   1 
ATOM   634  C  CZ    . PHE   A 1 79  ? 22.09900  34.30600  -2.50800  1.000 15.82682 ? 78  PHE   A CZ    1 
ATOM   635  N  N     . LEU   A 1 80  ? 20.39600  30.47000  -8.38400  1.000 12.99875 ? 79  LEU   A N     1 
ATOM   636  C  CA    . LEU   A 1 80  ? 19.47600  29.85700  -9.33500  1.000 13.51122 ? 79  LEU   A CA    1 
ATOM   637  C  C     . LEU   A 1 80  ? 18.14700  29.62400  -8.64400  1.000 14.72479 ? 79  LEU   A C     1 
ATOM   638  O  O     . LEU   A 1 80  ? 18.10600  28.95900  -7.60300  1.000 14.96959 ? 79  LEU   A O     1 
ATOM   639  C  CB    . LEU   A 1 80  ? 20.00400  28.50500  -9.81600  1.000 16.25401 ? 79  LEU   A CB    1 
ATOM   640  C  CG    . LEU   A 1 80  ? 21.20500  28.48900  -10.75600 1.000 17.14879 ? 79  LEU   A CG    1 
ATOM   641  C  CD1   . LEU   A 1 80  ? 21.43800  27.09500  -11.27800 1.000 19.18017 ? 79  LEU   A CD1   1 
ATOM   642  C  CD2   . LEU   A 1 80  ? 20.98900  29.46400  -11.92400 1.000 16.91829 ? 79  LEU   A CD2   1 
ATOM   643  N  N     . LEU   A 1 81  ? 17.07100  30.16700  -9.19700  1.000 13.69296 ? 80  LEU   A N     1 
ATOM   644  C  CA    . LEU   A 1 81  ? 15.70600  29.99700  -8.68700  1.000 14.99591 ? 80  LEU   A CA    1 
ATOM   645  C  C     . LEU   A 1 81  ? 15.10400  28.91000  -9.56700  1.000 15.55356 ? 80  LEU   A C     1 
ATOM   646  O  O     . LEU   A 1 81  ? 14.66500  29.18700  -10.69900 1.000 15.65210 ? 80  LEU   A O     1 
ATOM   647  C  CB    . LEU   A 1 81  ? 14.89200  31.27600  -8.84200  1.000 17.80778 ? 80  LEU   A CB    1 
ATOM   648  C  CG    . LEU   A 1 81  ? 15.47600  32.59400  -8.34300  1.000 17.92052 ? 80  LEU   A CG    1 
ATOM   649  C  CD1   . LEU   A 1 81  ? 14.56900  33.81600  -8.63800  1.000 19.98597 ? 80  LEU   A CD1   1 
ATOM   650  C  CD2   . LEU   A 1 81  ? 15.73800  32.45300  -6.87500  1.000 21.11901 ? 80  LEU   A CD2   1 
ATOM   651  N  N     . VAL   A 1 82  ? 15.01600  27.67700  -9.04100  1.000 13.54280 ? 81  VAL   A N     1 
ATOM   652  C  CA    . VAL   A 1 82  ? 14.60800  26.52700  -9.84700  1.000 14.49541 ? 81  VAL   A CA    1 
ATOM   653  C  C     . VAL   A 1 82  ? 13.15900  26.17000  -9.55900  1.000 14.97252 ? 81  VAL   A C     1 
ATOM   654  O  O     . VAL   A 1 82  ? 12.76400  26.03000  -8.39500  1.000 16.13727 ? 81  VAL   A O     1 
ATOM   655  C  CB    . VAL   A 1 82  ? 15.50600  25.31600  -9.57500  1.000 13.27502 ? 81  VAL   A CB    1 
ATOM   656  C  CG1   . VAL   A 1 82  ? 15.14300  24.15000  -10.55800 1.000 17.38705 ? 81  VAL   A CG1   1 
ATOM   657  C  CG2   . VAL   A 1 82  ? 16.98600  25.66600  -9.73300  1.000 15.90211 ? 81  VAL   A CG2   1 
ATOM   658  N  N     . PHE   A 1 83  ? 12.36800  26.01400  -10.62000 1.000 15.04516 ? 82  PHE   A N     1 
ATOM   659  C  CA    . PHE   A 1 83  ? 11.07800  25.33600  -10.50400 1.000 16.55843 ? 82  PHE   A CA    1 
ATOM   660  C  C     . PHE   A 1 83  ? 11.02000  24.22800  -11.54300 1.000 17.21988 ? 82  PHE   A C     1 
ATOM   661  O  O     . PHE   A 1 83  ? 11.90600  24.12000  -12.39400 1.000 16.37545 ? 82  PHE   A O     1 
ATOM   662  C  CB    . PHE   A 1 83  ? 9.90000   26.30900  -10.66500 1.000 16.88002 ? 82  PHE   A CB    1 
ATOM   663  C  CG    . PHE   A 1 83  ? 9.72000   26.82700  -12.06000 1.000 17.38274 ? 82  PHE   A CG    1 
ATOM   664  C  CD1   . PHE   A 1 83  ? 10.48400  27.87200  -12.50300 1.000 18.60724 ? 82  PHE   A CD1   1 
ATOM   665  C  CD2   . PHE   A 1 83  ? 8.80600   26.25200  -12.92600 1.000 18.64545 ? 82  PHE   A CD2   1 
ATOM   666  C  CE1   . PHE   A 1 83  ? 10.33400  28.37600  -13.78500 1.000 18.91639 ? 82  PHE   A CE1   1 
ATOM   667  C  CE2   . PHE   A 1 83  ? 8.64200   26.72700  -14.22700 1.000 21.06805 ? 82  PHE   A CE2   1 
ATOM   668  C  CZ    . PHE   A 1 83  ? 9.43600   27.80600  -14.65600 1.000 17.65137 ? 82  PHE   A CZ    1 
ATOM   669  N  N     . ALA   A 1 84  ? 10.01300  23.36700  -11.42800 1.000 16.28755 ? 83  ALA   A N     1 
ATOM   670  C  CA    . ALA   A 1 84  ? 9.81500   22.30800  -12.41700 1.000 17.32902 ? 83  ALA   A CA    1 
ATOM   671  C  C     . ALA   A 1 84  ? 8.60300   22.63200  -13.27600 1.000 19.45569 ? 83  ALA   A C     1 
ATOM   672  O  O     . ALA   A 1 84  ? 7.55500   23.00400  -12.75200 1.000 18.47830 ? 83  ALA   A O     1 
ATOM   673  C  CB    . ALA   A 1 84  ? 9.65600   20.93400  -11.75400 1.000 18.72282 ? 83  ALA   A CB    1 
ATOM   674  N  N     . ILE   A 1 85  ? 8.73000   22.44500  -14.59300 1.000 20.35191 ? 84  ILE   A N     1 
ATOM   675  C  CA    . ILE   A 1 85  ? 7.66100   22.84000  -15.49700 1.000 19.68662 ? 84  ILE   A CA    1 
ATOM   676  C  C     . ILE   A 1 85  ? 6.42100   21.98400  -15.33900 1.000 23.05782 ? 84  ILE   A C     1 
ATOM   677  O  O     . ILE   A 1 85  ? 5.36400   22.34700  -15.85400 1.000 22.87033 ? 84  ILE   A O     1 
ATOM   678  C  CB    . ILE   A 1 85  ? 8.14000   22.84900  -16.96500 1.000 21.88634 ? 84  ILE   A CB    1 
ATOM   679  C  CG1   . ILE   A 1 85  ? 8.64800   21.45400  -17.36000 1.000 22.58660 ? 84  ILE   A CG1   1 
ATOM   680  C  CG2   . ILE   A 1 85  ? 9.23300   23.89800  -17.14400 1.000 21.78767 ? 84  ILE   A CG2   1 
ATOM   681  C  CD1   . ILE   A 1 85  ? 7.76200   20.68600  -18.24400 1.000 29.81148 ? 84  ILE   A CD1   1 
ATOM   682  N  N     . ASN   A 1 86  ? 6.51300   20.88800  -14.59000 1.000 23.05108 ? 85  ASN   A N     1 
ATOM   683  C  CA    . ASN   A 1 86  ? 5.35600   20.04100  -14.34800 1.000 22.84304 ? 85  ASN   A CA    1 
ATOM   684  C  C     . ASN   A 1 86  ? 4.90200   20.10400  -12.89300 1.000 26.61627 ? 85  ASN   A C     1 
ATOM   685  O  O     . ASN   A 1 86  ? 4.25300   19.17300  -12.40300 1.000 27.62456 ? 85  ASN   A O     1 
ATOM   686  C  CB    . ASN   A 1 86  ? 5.64600   18.59900  -14.76100 1.000 23.74676 ? 85  ASN   A CB    1 
ATOM   687  C  CG    . ASN   A 1 86  ? 6.69800   17.95400  -13.87400 1.000 25.35936 ? 85  ASN   A CG    1 
ATOM   688  O  OD1   . ASN   A 1 86  ? 7.51200   18.62900  -13.23900 1.000 22.83454 ? 85  ASN   A OD1   1 
ATOM   689  N  ND2   . ASN   A 1 86  ? 6.65700   16.62200  -13.80100 1.000 32.36108 ? 85  ASN   A ND2   1 
ATOM   690  N  N     . ASN   A 1 87  ? 5.23300   21.19500  -12.21400 1.000 22.05167 ? 86  ASN   A N     1 
ATOM   691  C  CA    . ASN   A 1 87  ? 4.86000   21.38700  -10.79200 1.000 21.83348 ? 86  ASN   A CA    1 
ATOM   692  C  C     . ASN   A 1 87  ? 4.44800   22.85300  -10.65900 1.000 21.54780 ? 86  ASN   A C     1 
ATOM   693  O  O     . ASN   A 1 87  ? 5.31000   23.72200  -10.53200 1.000 20.31865 ? 86  ASN   A O     1 
ATOM   694  C  CB    . ASN   A 1 87  ? 5.95900   20.89900  -9.84700  1.000 22.46841 ? 86  ASN   A CB    1 
ATOM   695  C  CG    . ASN   A 1 87  ? 5.67900   21.11700  -8.37900  1.000 25.15007 ? 86  ASN   A CG    1 
ATOM   696  O  OD1   . ASN   A 1 87  ? 4.76900   21.85300  -7.99600  1.000 24.90715 ? 86  ASN   A OD1   1 
ATOM   697  N  ND2   . ASN   A 1 87  ? 6.49000   20.50900  -7.53000  1.000 33.79401 ? 86  ASN   A ND2   1 
ATOM   698  N  N     . THR   A 1 88  ? 3.14000   23.09900  -10.70700 1.000 22.55153 ? 87  THR   A N     1 
ATOM   699  C  CA    . THR   A 1 88  ? 2.66000   24.47800  -10.65300 1.000 25.13410 ? 87  THR   A CA    1 
ATOM   700  C  C     . THR   A 1 88  ? 2.98200   25.13000  -9.31500  1.000 23.61995 ? 87  THR   A C     1 
ATOM   701  O  O     . THR   A 1 88  ? 3.40600   26.29000  -9.27600  1.000 22.09936 ? 87  THR   A O     1 
ATOM   702  C  CB    . THR   A 1 88  ? 1.16400   24.53300  -10.96100 1.000 26.91986 ? 87  THR   A CB    1 
ATOM   703  O  OG1   . THR   A 1 88  ? 0.91600   24.17200  -12.33200 1.000 29.09424 ? 87  THR   A OG1   1 
ATOM   704  C  CG2   . THR   A 1 88  ? 0.57400   25.93000  -10.68300 1.000 28.68991 ? 87  THR   A CG2   1 
ATOM   705  N  N     . LYS   A 1 89  ? 2.79600   24.40500  -8.20600  1.000 23.23165 ? 88  LYS   A N     1 
ATOM   706  C  CA    . LYS   A 1 89  ? 3.14300   24.96300  -6.90600  1.000 23.24042 ? 88  LYS   A CA    1 
ATOM   707  C  C     . LYS   A 1 89  ? 4.59600   25.42500  -6.86200  1.000 21.59231 ? 88  LYS   A C     1 
ATOM   708  O  O     . LYS   A 1 89  ? 4.91400   26.45000  -6.24600  1.000 21.76514 ? 88  LYS   A O     1 
ATOM   709  C  CB    . LYS   A 1 89  ? 2.87700   23.91700  -5.81800  1.000 25.78032 ? 88  LYS   A CB    1 
ATOM   710  C  CG    . LYS   A 1 89  ? 3.20300   24.38000  -4.43200  1.000 30.78143 ? 88  LYS   A CG    1 
ATOM   711  C  CD    . LYS   A 1 89  ? 2.19000   25.37300  -3.93300  1.000 35.90688 ? 88  LYS   A CD    1 
ATOM   712  C  CE    . LYS   A 1 89  ? 2.54400   25.82900  -2.51900  1.000 39.67144 ? 88  LYS   A CE    1 
ATOM   713  N  NZ    . LYS   A 1 89  ? 3.37000   24.79900  -1.83200  1.000 40.91733 ? 88  LYS   A NZ    1 
ATOM   714  N  N     . SER   A 1 90  ? 5.51100   24.67000  -7.48300  1.000 19.15016 ? 89  SER   A N     1 
ATOM   715  C  CA    . SER   A 1 90  ? 6.91900   25.07700  -7.43300  1.000 18.10037 ? 89  SER   A CA    1 
ATOM   716  C  C     . SER   A 1 90  ? 7.15500   26.39700  -8.14700  1.000 18.20517 ? 89  SER   A C     1 
ATOM   717  O  O     . SER   A 1 90  ? 8.01700   27.17100  -7.73400  1.000 19.75205 ? 89  SER   A O     1 
ATOM   718  C  CB    . SER   A 1 90  ? 7.84800   23.99100  -7.96700  1.000 18.63409 ? 89  SER   A CB    1 
ATOM   719  O  OG    . SER   A 1 90  ? 7.82000   23.89700  -9.40600  1.000 19.03476 ? 89  SER   A OG    1 
ATOM   720  N  N     . PHE   A 1 91  ? 6.39200   26.66700  -9.19700  1.000 19.17328 ? 90  PHE   A N     1 
ATOM   721  C  CA    . PHE   A 1 91  ? 6.47600   27.94900  -9.87600  1.000 20.96832 ? 90  PHE   A CA    1 
ATOM   722  C  C     . PHE   A 1 91  ? 5.85400   29.06300  -9.04100  1.000 23.21134 ? 90  PHE   A C     1 
ATOM   723  O  O     . PHE   A 1 91  ? 6.42400   30.15400  -8.95000  1.000 20.48507 ? 90  PHE   A O     1 
ATOM   724  C  CB    . PHE   A 1 91  ? 5.79000   27.82500  -11.23600 1.000 22.31359 ? 90  PHE   A CB    1 
ATOM   725  C  CG    . PHE   A 1 91  ? 5.76400   29.11700  -12.01800 1.000 22.57623 ? 90  PHE   A CG    1 
ATOM   726  C  CD1   . PHE   A 1 91  ? 6.91800   29.59700  -12.58100 1.000 22.23201 ? 90  PHE   A CD1   1 
ATOM   727  C  CD2   . PHE   A 1 91  ? 4.60400   29.85200  -12.15300 1.000 24.67332 ? 90  PHE   A CD2   1 
ATOM   728  C  CE1   . PHE   A 1 91  ? 6.93100   30.78500  -13.28400 1.000 22.90048 ? 90  PHE   A CE1   1 
ATOM   729  C  CE2   . PHE   A 1 91  ? 4.60200   31.04100  -12.86200 1.000 28.97306 ? 90  PHE   A CE2   1 
ATOM   730  C  CZ    . PHE   A 1 91  ? 5.78000   31.50300  -13.42600 1.000 28.21019 ? 90  PHE   A CZ    1 
ATOM   731  N  N     . GLU   A 1 92  ? 4.69100   28.80600  -8.42500  1.000 22.32461 ? 91  GLU   A N     1 
ATOM   732  C  CA    . GLU   A 1 92  ? 4.07600   29.76900  -7.52000  1.000 23.23296 ? 91  GLU   A CA    1 
ATOM   733  C  C     . GLU   A 1 92  ? 4.97400   30.04100  -6.31600  1.000 23.06015 ? 91  GLU   A C     1 
ATOM   734  O  O     . GLU   A 1 92  ? 4.86400   31.10600  -5.69700  1.000 29.90312 ? 91  GLU   A O     1 
ATOM   735  C  CB    . GLU   A 1 92  ? 2.70700   29.22800  -7.09700  1.000 27.26649 ? 91  GLU   A CB    1 
ATOM   736  C  CG    . GLU   A 1 92  ? 1.76100   29.02300  -8.30100  1.000 29.90984 ? 91  GLU   A CG    1 
ATOM   737  C  CD    . GLU   A 1 92  ? 0.41900   28.38900  -7.92700  1.000 38.66694 ? 91  GLU   A CD    1 
ATOM   738  O  OE1   . GLU   A 1 92  ? 0.37000   27.62400  -6.93200  1.000 36.48121 ? 91  GLU   A OE1   1 
ATOM   739  O  OE2   . GLU   A 1 92  ? -0.58500  28.65700  -8.63400  1.000 42.09041 ? 91  GLU   A OE2   1 
ATOM   740  N  N     . ASP   A 1 93  ? 5.84500   29.09900  -5.96000  1.000 23.01204 ? 92  ASP   A N     1 
ATOM   741  C  CA    . ASP   A 1 93  ? 6.77000   29.31100  -4.84900  1.000 24.10896 ? 92  ASP   A CA    1 
ATOM   742  C  C     . ASP   A 1 93  ? 7.89700   30.28300  -5.17700  1.000 22.03841 ? 92  ASP   A C     1 
ATOM   743  O  O     . ASP   A 1 93  ? 8.58400   30.74700  -4.25600  1.000 22.44459 ? 92  ASP   A O     1 
ATOM   744  C  CB    . ASP   A 1 93  ? 7.43500   27.99200  -4.44900  1.000 27.44634 ? 92  ASP   A CB    1 
ATOM   745  C  CG    . ASP   A 1 93  ? 6.53700   27.09700  -3.61400  1.000 35.18963 ? 92  ASP   A CG    1 
ATOM   746  O  OD1   . ASP   A 1 93  ? 5.43200   27.53000  -3.18400  1.000 31.92523 ? 92  ASP   A OD1   1 
ATOM   747  O  OD2   . ASP   A 1 93  ? 6.95100   25.93900  -3.39000  1.000 36.76174 ? 92  ASP   A OD2   1 
ATOM   748  N  N     . ILE   A 1 94  ? 8.16000   30.54200  -6.46000  1.000 20.62305 ? 93  ILE   A N     1 
ATOM   749  C  CA    . ILE   A 1 94  ? 9.38400   31.25500  -6.84200  1.000 19.03754 ? 93  ILE   A CA    1 
ATOM   750  C  C     . ILE   A 1 94  ? 9.46800   32.61700  -6.16500  1.000 23.26307 ? 93  ILE   A C     1 
ATOM   751  O  O     . ILE   A 1 94  ? 10.53700  33.02100  -5.68100  1.000 22.21688 ? 93  ILE   A O     1 
ATOM   752  C  CB    . ILE   A 1 94  ? 9.48400   31.39400  -8.37300  1.000 20.32715 ? 93  ILE   A CB    1 
ATOM   753  C  CG1   . ILE   A 1 94  ? 9.84500   30.05600  -9.01900  1.000 20.04235 ? 93  ILE   A CG1   1 
ATOM   754  C  CG2   . ILE   A 1 94  ? 10.56000  32.43800  -8.78200  1.000 20.96819 ? 93  ILE   A CG2   1 
ATOM   755  C  CD1   . ILE   A 1 94  ? 11.22800  29.54000  -8.67900  1.000 20.56413 ? 93  ILE   A CD1   1 
ATOM   756  N  N     . HIS   A 1 95  ? 8.36500   33.34300  -6.11900  1.000 22.35858 ? 94  HIS   A N     1 
ATOM   757  C  CA    . HIS   A 1 95  ? 8.42700   34.71000  -5.60000  1.000 24.79351 ? 94  HIS   A CA    1 
ATOM   758  C  C     . HIS   A 1 95  ? 8.88500   34.72000  -4.15400  1.000 26.86171 ? 94  HIS   A C     1 
ATOM   759  O  O     . HIS   A 1 95  ? 9.58500   35.65000  -3.74400  1.000 24.76609 ? 94  HIS   A O     1 
ATOM   760  C  CB    . HIS   A 1 95  ? 7.10800   35.46600  -5.79800  1.000 28.97780 ? 94  HIS   A CB    1 
ATOM   761  C  CG    . HIS   A 1 95  ? 6.00300   34.99000  -4.92000  1.000 35.56099 ? 94  HIS   A CG    1 
ATOM   762  N  ND1   . HIS   A 1 95  ? 5.52900   35.72400  -3.85500  1.000 36.56523 ? 94  HIS   A ND1   1 
ATOM   763  C  CD2   . HIS   A 1 95  ? 5.27600   33.84800  -4.94600  1.000 32.07136 ? 94  HIS   A CD2   1 
ATOM   764  C  CE1   . HIS   A 1 95  ? 4.54700   35.06000  -3.26900  1.000 42.20682 ? 94  HIS   A CE1   1 
ATOM   765  N  NE2   . HIS   A 1 95  ? 4.37100   33.92100  -3.91400  1.000 42.00139 ? 94  HIS   A NE2   1 
ATOM   766  N  N     . HIS   A 1 96  ? 8.55700   33.67200  -3.39200  1.000 25.10446 ? 95  HIS   A N     1 
ATOM   767  C  CA    . HIS   A 1 96  ? 8.96600   33.61900  -1.98900  1.000 23.09366 ? 95  HIS   A CA    1 
ATOM   768  C  C     . HIS   A 1 96  ? 10.48100  33.47700  -1.85600  1.000 23.35411 ? 95  HIS   A C     1 
ATOM   769  O  O     . HIS   A 1 96  ? 11.09300  34.07500  -0.96300  1.000 23.16206 ? 95  HIS   A O     1 
ATOM   770  C  CB    . HIS   A 1 96  ? 8.28100   32.44900  -1.27900  1.000 30.36656 ? 95  HIS   A CB    1 
ATOM   771  C  CG    . HIS   A 1 96  ? 6.81200   32.63000  -1.08200  1.000 40.11405 ? 95  HIS   A CG    1 
ATOM   772  N  ND1   . HIS   A 1 96  ? 6.28100   33.66400  -0.33700  1.000 43.27081 ? 95  HIS   A ND1   1 
ATOM   773  C  CD2   . HIS   A 1 96  ? 5.75900   31.89100  -1.50400  1.000 42.13683 ? 95  HIS   A CD2   1 
ATOM   774  C  CE1   . HIS   A 1 96  ? 4.96300   33.56700  -0.33200  1.000 46.59442 ? 95  HIS   A CE1   1 
ATOM   775  N  NE2   . HIS   A 1 96  ? 4.62100   32.49800  -1.02900  1.000 41.77241 ? 95  HIS   A NE2   1 
ATOM   776  N  N     . TYR   A 1 97  ? 11.10400  32.68300  -2.72900  1.000 19.04338 ? 96  TYR   A N     1 
ATOM   777  C  CA    . TYR   A 1 97  ? 12.55700  32.54100  -2.67100  1.000 17.99631 ? 96  TYR   A CA    1 
ATOM   778  C  C     . TYR   A 1 97  ? 13.21900  33.86100  -3.02600  1.000 20.05824 ? 96  TYR   A C     1 
ATOM   779  O  O     . TYR   A 1 97  ? 14.17100  34.30600  -2.37000  1.000 20.75929 ? 96  TYR   A O     1 
ATOM   780  C  CB    . TYR   A 1 97  ? 13.02800  31.42900  -3.62300  1.000 20.67071 ? 96  TYR   A CB    1 
ATOM   781  C  CG    . TYR   A 1 97  ? 12.64600  30.03100  -3.15700  1.000 21.49184 ? 96  TYR   A CG    1 
ATOM   782  C  CD1   . TYR   A 1 97  ? 13.41100  29.34700  -2.22500  1.000 21.34732 ? 96  TYR   A CD1   1 
ATOM   783  C  CD2   . TYR   A 1 97  ? 11.50600  29.40300  -3.64400  1.000 22.67482 ? 96  TYR   A CD2   1 
ATOM   784  C  CE1   . TYR   A 1 97  ? 13.03700  28.11000  -1.78500  1.000 24.78542 ? 96  TYR   A CE1   1 
ATOM   785  C  CE2   . TYR   A 1 97  ? 11.12100  28.15300  -3.20000  1.000 21.68117 ? 96  TYR   A CE2   1 
ATOM   786  C  CZ    . TYR   A 1 97  ? 11.90800  27.51400  -2.25700  1.000 24.62824 ? 96  TYR   A CZ    1 
ATOM   787  O  OH    . TYR   A 1 97  ? 11.55900  26.26800  -1.76400  1.000 27.99516 ? 96  TYR   A OH    1 
ATOM   788  N  N     . ARG   A 1 98  ? 12.69300  34.53400  -4.03500  1.000 18.93137 ? 97  ARG   A N     1 
ATOM   789  C  CA    . ARG   A 1 98  ? 13.25000  35.82400  -4.41100  1.000 20.25191 ? 97  ARG   A CA    1 
ATOM   790  C  C     . ARG   A 1 98  ? 13.09200  36.84200  -3.29400  1.000 22.19743 ? 97  ARG   A C     1 
ATOM   791  O  O     . ARG   A 1 98  ? 14.01700  37.61500  -3.01700  1.000 22.14749 ? 97  ARG   A O     1 
ATOM   792  C  CB    . ARG   A 1 98  ? 12.61200  36.32200  -5.70600  1.000 23.24776 ? 97  ARG   A CB    1 
ATOM   793  C  CG    . ARG   A 1 98  ? 13.11600  37.66700  -6.12700  1.000 25.86977 ? 97  ARG   A CG    1 
ATOM   794  C  CD    . ARG   A 1 98  ? 12.63100  38.01600  -7.51400  1.000 26.70392 ? 97  ARG   A CD    1 
ATOM   795  N  NE    . ARG   A 1 98  ? 13.03400  39.36000  -7.89600  1.000 29.09264 ? 97  ARG   A NE    1 
ATOM   796  C  CZ    . ARG   A 1 98  ? 12.35200  40.45600  -7.61300  1.000 33.58617 ? 97  ARG   A CZ    1 
ATOM   797  N  NH1   . ARG   A 1 98  ? 11.21900  40.41400  -6.92400  1.000 39.68379 ? 97  ARG   A NH1   1 
ATOM   798  N  NH2   . ARG   A 1 98  ? 12.81000  41.62900  -8.04000  1.000 42.90241 ? 97  ARG   A NH2   1 
ATOM   799  N  N     . GLU   A 1 99  ? 11.92800  36.86300  -2.64800  1.000 20.95523 ? 98  GLU   A N     1 
ATOM   800  C  CA    . GLU   A 1 99  ? 11.69600  37.81600  -1.57000  1.000 21.66908 ? 98  GLU   A CA    1 
ATOM   801  C  C     . GLU   A 1 99  ? 12.63400  37.56300  -0.40000  1.000 19.86269 ? 98  GLU   A C     1 
ATOM   802  O  O     . GLU   A 1 99  ? 13.13300  38.51400  0.21700   1.000 22.27895 ? 98  GLU   A O     1 
ATOM   803  C  CB    . GLU   A 1 99  ? 10.24500  37.70500  -1.09000  1.000 23.68104 ? 98  GLU   A CB    1 
ATOM   804  C  CG    . GLU   A 1 99  ? 9.20300   38.24000  -2.05300  1.000 32.73220 ? 98  GLU   A CG    1 
ATOM   805  C  CD    . GLU   A 1 99  ? 7.80600   37.66400  -1.80700  1.000 43.41942 ? 98  GLU   A CD    1 
ATOM   806  O  OE1   . GLU   A 1 99  ? 7.59300   37.02600  -0.74700  1.000 43.18758 ? 98  GLU   A OE1   1 
ATOM   807  O  OE2   . GLU   A 1 99  ? 6.91900   37.83700  -2.68200  1.000 43.02102 ? 98  GLU   A OE2   1 
ATOM   808  N  N     . GLN   A 1 100 ? 12.85000  36.29100  -0.05900  1.000 19.20013 ? 99  GLN   A N     1 
ATOM   809  C  CA    . GLN   A 1 100 ? 13.78000  35.95500  1.01400   1.000 20.06641 ? 99  GLN   A CA    1 
ATOM   810  C  C     . GLN   A 1 100 ? 15.19200  36.42300  0.69600   1.000 19.80629 ? 99  GLN   A C     1 
ATOM   811  O  O     . GLN   A 1 100 ? 15.89000  36.94100  1.57100   1.000 19.80854 ? 99  GLN   A O     1 
ATOM   812  C  CB    . GLN   A 1 100 ? 13.76900  34.45100  1.27800   1.000 24.98618 ? 99  GLN   A CB    1 
ATOM   813  C  CG    . GLN   A 1 100 ? 12.70500  34.01400  2.25100   1.000 31.27996 ? 99  GLN   A CG    1 
ATOM   814  C  CD    . GLN   A 1 100 ? 12.87700  34.65900  3.62800   1.000 36.37889 ? 99  GLN   A CD    1 
ATOM   815  O  OE1   . GLN   A 1 100 ? 12.12800  35.54500  3.99800   1.000 39.65068 ? 99  GLN   A OE1   1 
ATOM   816  N  NE2   . GLN   A 1 100 ? 13.88000  34.21900  4.37400   1.000 36.21912 ? 99  GLN   A NE2   1 
ATOM   817  N  N     . ILE   A 1 101 ? 15.64500  36.24300  -0.54500  1.000 17.23866 ? 100 ILE   A N     1 
ATOM   818  C  CA    . ILE   A 1 101 ? 16.99600  36.68600  -0.88300  1.000 17.26827 ? 100 ILE   A CA    1 
ATOM   819  C  C     . ILE   A 1 101 ? 17.11400  38.20000  -0.78200  1.000 17.42243 ? 100 ILE   A C     1 
ATOM   820  O  O     . ILE   A 1 101 ? 18.08600  38.72900  -0.22600  1.000 18.39600 ? 100 ILE   A O     1 
ATOM   821  C  CB    . ILE   A 1 101 ? 17.37300  36.18600  -2.28400  1.000 19.34837 ? 100 ILE   A CB    1 
ATOM   822  C  CG1   . ILE   A 1 101 ? 17.48500  34.66400  -2.30600  1.000 17.23769 ? 100 ILE   A CG1   1 
ATOM   823  C  CG2   . ILE   A 1 101 ? 18.67300  36.86200  -2.73200  1.000 19.78812 ? 100 ILE   A CG2   1 
ATOM   824  C  CD1   . ILE   A 1 101 ? 17.32500  34.10800  -3.70900  1.000 18.18027 ? 100 ILE   A CD1   1 
ATOM   825  N  N     . LYS   A 1 102 ? 16.12100  38.93200  -1.29000  1.000 16.76715 ? 101 LYS   A N     1 
ATOM   826  C  CA    . LYS   A 1 102 ? 16.13100  40.39200  -1.19500  1.000 17.99911 ? 101 LYS   A CA    1 
ATOM   827  C  C     . LYS   A 1 102 ? 16.14800  40.85800  0.25000   1.000 18.59698 ? 101 LYS   A C     1 
ATOM   828  O  O     . LYS   A 1 102 ? 16.74400  41.88500  0.58100   1.000 19.62247 ? 101 LYS   A O     1 
ATOM   829  C  CB    . LYS   A 1 102 ? 14.90400  40.98700  -1.89700  1.000 20.71880 ? 101 LYS   A CB    1 
ATOM   830  C  CG    . LYS   A 1 102 ? 15.03100  40.88800  -3.42400  1.000 24.50215 ? 101 LYS   A CG    1 
ATOM   831  C  CD    . LYS   A 1 102 ? 13.78500  41.35200  -4.14900  1.000 32.98360 ? 101 LYS   A CD    1 
ATOM   832  C  CE    . LYS   A 1 102 ? 13.22600  42.60900  -3.57400  1.000 38.13966 ? 101 LYS   A CE    1 
ATOM   833  N  NZ    . LYS   A 1 102 ? 11.87200  42.93100  -4.13900  1.000 34.92088 ? 101 LYS   A NZ    1 
ATOM   834  N  N     . ARG   A 1 103 ? 15.39100  40.18600  1.10700   1.000 19.29540 ? 102 ARG   A N     1 
ATOM   835  C  CA    . ARG   A 1 103 ? 15.28000  40.64800  2.47800   1.000 20.85198 ? 102 ARG   A CA    1 
ATOM   836  C  C     . ARG   A 1 103 ? 16.57300  40.36700  3.23100   1.000 18.68809 ? 102 ARG   A C     1 
ATOM   837  O  O     . ARG   A 1 103 ? 17.05200  41.20900  3.99100   1.000 21.94338 ? 102 ARG   A O     1 
ATOM   838  C  CB    . ARG   A 1 103 ? 14.08600  39.91900  3.09200   1.000 25.35533 ? 102 ARG   A CB    1 
ATOM   839  C  CG    . ARG   A 1 103 ? 13.88400  39.93500  4.57400   1.000 33.45819 ? 102 ARG   A CG    1 
ATOM   840  C  CD    . ARG   A 1 103 ? 12.93100  38.74000  4.85400   1.000 38.15753 ? 102 ARG   A CD    1 
ATOM   841  N  NE    . ARG   A 1 103 ? 11.53100  39.11900  4.67300   1.000 43.68285 ? 102 ARG   A NE    1 
ATOM   842  C  CZ    . ARG   A 1 103 ? 10.69300  38.63100  3.76200   1.000 34.08088 ? 102 ARG   A CZ    1 
ATOM   843  N  NH1   . ARG   A 1 103 ? 11.06200  37.68900  2.90800   1.000 38.82926 ? 102 ARG   A NH1   1 
ATOM   844  N  NH2   . ARG   A 1 103 ? 9.43700   39.08500  3.72900   1.000 38.20704 ? 102 ARG   A NH2   1 
ATOM   845  N  N     . VAL   A 1 104 ? 17.15100  39.19300  3.01900   1.000 18.49947 ? 103 VAL   A N     1 
ATOM   846  C  CA    . VAL   A 1 104 ? 18.35000  38.82100  3.74900   1.000 18.92046 ? 103 VAL   A CA    1 
ATOM   847  C  C     . VAL   A 1 104 ? 19.53500  39.63900  3.28100   1.000 19.40879 ? 103 VAL   A C     1 
ATOM   848  O  O     . VAL   A 1 104 ? 20.36600  40.07200  4.09200   1.000 20.99255 ? 103 VAL   A O     1 
ATOM   849  C  CB    . VAL   A 1 104 ? 18.61100  37.32100  3.57100   1.000 18.09814 ? 103 VAL   A CB    1 
ATOM   850  C  CG1   . VAL   A 1 104 ? 19.98900  36.99400  4.02300   1.000 19.48156 ? 103 VAL   A CG1   1 
ATOM   851  C  CG2   . VAL   A 1 104 ? 17.58300  36.53100  4.34800   1.000 18.34715 ? 103 VAL   A CG2   1 
ATOM   852  N  N     . LYS   A 1 105 ? 19.64000  39.86000  1.97600   1.000 18.76031 ? 104 LYS   A N     1 
ATOM   853  C  CA    . LYS   A 1 105 ? 20.73800  40.64700  1.42900   1.000 19.39968 ? 104 LYS   A CA    1 
ATOM   854  C  C     . LYS   A 1 105 ? 20.42900  42.14100  1.40200   1.000 21.23904 ? 104 LYS   A C     1 
ATOM   855  O  O     . LYS   A 1 105 ? 21.31000  42.95000  1.07900   1.000 22.45957 ? 104 LYS   A O     1 
ATOM   856  C  CB    . LYS   A 1 105 ? 21.13500  40.10300  0.05600   1.000 21.09837 ? 104 LYS   A CB    1 
ATOM   857  C  CG    . LYS   A 1 105 ? 21.42300  38.56800  0.11900   1.000 20.88114 ? 104 LYS   A CG    1 
ATOM   858  C  CD    . LYS   A 1 105 ? 21.91200  37.98400  -1.23400  1.000 20.50914 ? 104 LYS   A CD    1 
ATOM   859  C  CE    . LYS   A 1 105 ? 23.39200  38.32300  -1.62900  1.000 16.84808 ? 104 LYS   A CE    1 
ATOM   860  N  NZ    . LYS   A 1 105 ? 24.43200  37.96500  -0.59900  1.000 17.40488 ? 104 LYS   A NZ    1 
ATOM   861  N  N     . ASP   A 1 106 ? 19.20700  42.54100  1.79800   1.000 20.16269 ? 105 ASP   A N     1 
ATOM   862  C  CA    . ASP   A 1 106 ? 18.82400  43.94600  1.91900   1.000 20.88863 ? 105 ASP   A CA    1 
ATOM   863  C  C     . ASP   A 1 106 ? 19.07200  44.68700  0.60500   1.000 19.87279 ? 105 ASP   A C     1 
ATOM   864  O  O     . ASP   A 1 106 ? 19.70100  45.74100  0.55800   1.000 23.85503 ? 105 ASP   A O     1 
ATOM   865  C  CB    . ASP   A 1 106 ? 19.49800  44.63700  3.11000   1.000 21.11039 ? 105 ASP   A CB    1 
ATOM   866  C  CG    . ASP   A 1 106 ? 18.97400  46.00800  3.32800   1.000 23.46243 ? 105 ASP   A CG    1 
ATOM   867  O  OD1   . ASP   A 1 106 ? 17.75000  46.21400  3.15000   1.000 24.48080 ? 105 ASP   A OD1   1 
ATOM   868  O  OD2   . ASP   A 1 106 ? 19.76900  46.89900  3.67500   1.000 24.29621 ? 105 ASP   A OD2   1 
ATOM   869  N  N     . SER   A 1 107 ? 18.57500  44.10600  -0.48100  1.000 21.60653 ? 106 SER   A N     1 
ATOM   870  C  CA    . SER   A 1 107 ? 18.91400  44.64500  -1.79100  1.000 21.43169 ? 106 SER   A CA    1 
ATOM   871  C  C     . SER   A 1 107 ? 17.83100  44.27500  -2.78500  1.000 22.93433 ? 106 SER   A C     1 
ATOM   872  O  O     . SER   A 1 107 ? 17.32400  43.14700  -2.75900  1.000 26.05278 ? 106 SER   A O     1 
ATOM   873  C  CB    . SER   A 1 107 ? 20.25800  44.07100  -2.24600  1.000 23.68439 ? 106 SER   A CB    1 
ATOM   874  O  OG    . SER   A 1 107 ? 20.60600  44.57500  -3.51500  1.000 32.25322 ? 106 SER   A OG    1 
ATOM   875  N  N     . GLU   A 1 108 ? 17.53800  45.20800  -3.69700  1.000 26.90585 ? 107 GLU   A N     1 
ATOM   876  C  CA    . GLU   A 1 108 ? 16.65100  44.93500  -4.82100  1.000 28.61326 ? 107 GLU   A CA    1 
ATOM   877  C  C     . GLU   A 1 108 ? 17.38400  44.39500  -6.03600  1.000 29.96979 ? 107 GLU   A C     1 
ATOM   878  O  O     . GLU   A 1 108 ? 16.73000  44.00500  -7.00900  1.000 37.20682 ? 107 GLU   A O     1 
ATOM   879  C  CB    . GLU   A 1 108 ? 15.89600  46.19400  -5.21900  1.000 36.14936 ? 107 GLU   A CB    1 
ATOM   880  C  CG    . GLU   A 1 108 ? 14.90200  46.60700  -4.18500  1.000 39.92883 ? 107 GLU   A CG    1 
ATOM   881  C  CD    . GLU   A 1 108 ? 13.96400  47.63300  -4.70300  1.000 38.49228 ? 107 GLU   A CD    1 
ATOM   882  O  OE1   . GLU   A 1 108 ? 14.41200  48.49500  -5.49600  1.000 47.26770 ? 107 GLU   A OE1   1 
ATOM   883  O  OE2   . GLU   A 1 108 ? 12.77900  47.58100  -4.31800  1.000 40.43981 ? 107 GLU   A OE2   1 
ATOM   884  N  N     . ASP   A 1 109 ? 18.71200  44.37600  -6.01400  1.000 25.89749 ? 108 ASP   A N     1 
ATOM   885  C  CA    . ASP   A 1 109 ? 19.51200  43.97800  -7.17400  1.000 29.71130 ? 108 ASP   A CA    1 
ATOM   886  C  C     . ASP   A 1 109 ? 20.50700  42.89600  -6.75800  1.000 29.66290 ? 108 ASP   A C     1 
ATOM   887  O  O     . ASP   A 1 109 ? 21.68300  43.15300  -6.51200  1.000 33.35872 ? 108 ASP   A O     1 
ATOM   888  C  CB    . ASP   A 1 109 ? 20.20700  45.22600  -7.80000  1.000 34.46587 ? 108 ASP   A CB    1 
ATOM   889  C  CG    . ASP   A 1 109 ? 21.23200  44.86300  -8.86600  1.000 46.71490 ? 108 ASP   A CG    1 
ATOM   890  O  OD1   . ASP   A 1 109 ? 20.90700  44.07200  -9.78000  1.000 46.69824 ? 108 ASP   A OD1   1 
ATOM   891  O  OD2   . ASP   A 1 109 ? 22.36800  45.38000  -8.78500  1.000 48.14852 ? 108 ASP   A OD2   1 
ATOM   892  N  N     . VAL   A 1 110 ? 20.02200  41.64900  -6.69000  1.000 24.13849 ? 109 VAL   A N     1 
ATOM   893  C  CA    . VAL   A 1 110 ? 20.85700  40.49600  -6.39200  1.000 19.58698 ? 109 VAL   A CA    1 
ATOM   894  C  C     . VAL   A 1 110 ? 20.90800  39.64700  -7.65300  1.000 18.07251 ? 109 VAL   A C     1 
ATOM   895  O  O     . VAL   A 1 110 ? 19.85500  39.35700  -8.23300  1.000 19.53453 ? 109 VAL   A O     1 
ATOM   896  C  CB    . VAL   A 1 110 ? 20.30600  39.67000  -5.21700  1.000 18.84929 ? 109 VAL   A CB    1 
ATOM   897  C  CG1   . VAL   A 1 110 ? 21.18100  38.45400  -4.96800  1.000 19.11360 ? 109 VAL   A CG1   1 
ATOM   898  C  CG2   . VAL   A 1 110 ? 20.20000  40.50700  -3.94200  1.000 22.22729 ? 109 VAL   A CG2   1 
ATOM   899  N  N     . PRO   A 1 111 ? 22.08700  39.17200  -8.07600  1.000 16.03166 ? 110 PRO   A N     1 
ATOM   900  C  CA    . PRO   A 1 111 ? 22.15600  38.26800  -9.24800  1.000 16.10318 ? 110 PRO   A CA    1 
ATOM   901  C  C     . PRO   A 1 111 ? 21.34800  36.97900  -9.08100  1.000 14.41026 ? 110 PRO   A C     1 
ATOM   902  O  O     . PRO   A 1 111 ? 21.52400  36.20000  -8.12000  1.000 14.35576 ? 110 PRO   A O     1 
ATOM   903  C  CB    . PRO   A 1 111 ? 23.65100  37.95000  -9.36900  1.000 15.62098 ? 110 PRO   A CB    1 
ATOM   904  C  CG    . PRO   A 1 111 ? 24.32800  39.14800  -8.72300  1.000 17.18917 ? 110 PRO   A CG    1 
ATOM   905  C  CD    . PRO   A 1 111 ? 23.42000  39.53700  -7.56800  1.000 18.47415 ? 110 PRO   A CD    1 
ATOM   906  N  N     . MET   A 1 112 ? 20.44900  36.75600  -10.02800 1.000 15.26232 ? 111 MET   A N     1 
ATOM   907  C  CA    . MET   A 1 112 ? 19.59500  35.58500  -9.99400  1.000 16.22061 ? 111 MET   A CA    1 
ATOM   908  C  C     . MET   A 1 112 ? 19.21400  35.20500  -11.41600 1.000 14.40962 ? 111 MET   A C     1 
ATOM   909  O  O     . MET   A 1 112 ? 19.10400  36.07400  -12.29100 1.000 16.16213 ? 111 MET   A O     1 
ATOM   910  C  CB    . MET   A 1 112 ? 18.26500  35.86100  -9.28800  1.000 19.75503 ? 111 MET   A CB    1 
ATOM   911  C  CG    . MET   A 1 112 ? 18.31800  36.39200  -7.85900  1.000 20.48299 ? 111 MET   A CG    1 
ATOM   912  S  SD    . MET   A 1 112 ? 16.63000  36.66700  -7.23700  1.000 24.27609 ? 111 MET   A SD    1 
ATOM   913  C  CE    . MET   A 1 112 ? 16.95600  37.69800  -5.79800  1.000 31.21653 ? 111 MET   A CE    1 
ATOM   914  N  N     . VAL   A 1 113 ? 18.90800  33.90700  -11.59900 1.000 15.35978 ? 112 VAL   A N     1 
ATOM   915  C  CA    . VAL   A 1 113 ? 18.40600  33.37100  -12.86800 1.000 16.08070 ? 112 VAL   A CA    1 
ATOM   916  C  C     . VAL   A 1 113 ? 17.23800  32.45500  -12.55300 1.000 14.25170 ? 112 VAL   A C     1 
ATOM   917  O  O     . VAL   A 1 113 ? 17.32000  31.66600  -11.60900 1.000 15.19971 ? 112 VAL   A O     1 
ATOM   918  C  CB    . VAL   A 1 113 ? 19.52800  32.60700  -13.60300 1.000 14.65882 ? 112 VAL   A CB    1 
ATOM   919  C  CG1   . VAL   A 1 113 ? 19.01800  31.83900  -14.81800 1.000 16.97006 ? 112 VAL   A CG1   1 
ATOM   920  C  CG2   . VAL   A 1 113 ? 20.65900  33.56100  -14.01400 1.000 16.48795 ? 112 VAL   A CG2   1 
ATOM   921  N  N     . LEU   A 1 114 ? 16.15100  32.57700  -13.31000 1.000 15.64282 ? 113 LEU   A N     1 
ATOM   922  C  CA    . LEU   A 1 114 ? 14.99200  31.69600  -13.18200 1.000 16.83883 ? 113 LEU   A CA    1 
ATOM   923  C  C     . LEU   A 1 114 ? 15.22900  30.49700  -14.08600 1.000 14.84149 ? 113 LEU   A C     1 
ATOM   924  O  O     . LEU   A 1 114 ? 15.54100  30.65300  -15.27100 1.000 16.99027 ? 113 LEU   A O     1 
ATOM   925  C  CB    . LEU   A 1 114 ? 13.73500  32.44600  -13.62100 1.000 16.91897 ? 113 LEU   A CB    1 
ATOM   926  C  CG    . LEU   A 1 114 ? 12.43700  31.65200  -13.50200 1.000 17.19372 ? 113 LEU   A CG    1 
ATOM   927  C  CD1   . LEU   A 1 114 ? 12.11000  31.41400  -12.06100 1.000 19.72820 ? 113 LEU   A CD1   1 
ATOM   928  C  CD2   . LEU   A 1 114 ? 11.32500  32.38800  -14.15400 1.000 20.17156 ? 113 LEU   A CD2   1 
ATOM   929  N  N     . VAL   A 1 115 ? 15.07000  29.30600  -13.52300 1.000 16.39991 ? 114 VAL   A N     1 
ATOM   930  C  CA    . VAL   A 1 115 ? 15.34000  28.05700  -14.21800 1.000 17.41657 ? 114 VAL   A CA    1 
ATOM   931  C  C     . VAL   A 1 115 ? 14.09200  27.20400  -14.19500 1.000 14.78825 ? 114 VAL   A C     1 
ATOM   932  O  O     . VAL   A 1 115 ? 13.60400  26.83000  -13.11600 1.000 17.22224 ? 114 VAL   A O     1 
ATOM   933  C  CB    . VAL   A 1 115 ? 16.49600  27.32400  -13.54900 1.000 16.11983 ? 114 VAL   A CB    1 
ATOM   934  C  CG1   . VAL   A 1 115 ? 16.75000  26.02500  -14.21300 1.000 19.26602 ? 114 VAL   A CG1   1 
ATOM   935  C  CG2   . VAL   A 1 115 ? 17.72000  28.18900  -13.63700 1.000 16.01363 ? 114 VAL   A CG2   1 
ATOM   936  N  N     . GLY   A 1 116 ? 13.56200  26.92200  -15.38600 1.000 17.11292 ? 115 GLY   A N     1 
ATOM   937  C  CA    . GLY   A 1 116 ? 12.42500  26.01900  -15.51400 1.000 18.58734 ? 115 GLY   A CA    1 
ATOM   938  C  C     . GLY   A 1 116 ? 12.91200  24.64500  -15.91000 1.000 19.83662 ? 115 GLY   A C     1 
ATOM   939  O  O     . GLY   A 1 116 ? 13.25900  24.43600  -17.06700 1.000 18.57835 ? 115 GLY   A O     1 
ATOM   940  N  N     . ASN   A 1 117 ? 12.99900  23.72300  -14.95600 1.000 17.43729 ? 116 ASN   A N     1 
ATOM   941  C  CA    . ASN   A 1 117 ? 13.63300  22.42900  -15.16800 1.000 16.83766 ? 116 ASN   A CA    1 
ATOM   942  C  C     . ASN   A 1 117 ? 12.59200  21.36000  -15.50100 1.000 17.96359 ? 116 ASN   A C     1 
ATOM   943  O  O     . ASN   A 1 117 ? 11.38100  21.58500  -15.41800 1.000 19.74909 ? 116 ASN   A O     1 
ATOM   944  C  CB    . ASN   A 1 117 ? 14.40600  22.04100  -13.90400 1.000 16.04716 ? 116 ASN   A CB    1 
ATOM   945  C  CG    . ASN   A 1 117 ? 15.30700  20.83100  -14.09900 1.000 15.99249 ? 116 ASN   A CG    1 
ATOM   946  O  OD1   . ASN   A 1 117 ? 16.01900  20.70200  -15.13100 1.000 17.94578 ? 116 ASN   A OD1   1 
ATOM   947  N  ND2   . ASN   A 1 117 ? 15.26400  19.90200  -13.12800 1.000 17.77975 ? 116 ASN   A ND2   1 
ATOM   948  N  N     . LYS   A 1 118 ? 13.09900  20.18200  -15.90000 1.000 19.36121 ? 117 LYS   A N     1 
ATOM   949  C  CA    . LYS   A 1 118 ? 12.28800  19.02500  -16.33600 1.000 19.95258 ? 117 LYS   A CA    1 
ATOM   950  C  C     . LYS   A 1 118 ? 11.61300  19.27900  -17.67200 1.000 21.53357 ? 117 LYS   A C     1 
ATOM   951  O  O     . LYS   A 1 118 ? 10.52000  18.76400  -17.93300 1.000 21.74648 ? 117 LYS   A O     1 
ATOM   952  C  CB    . LYS   A 1 118 ? 11.29100  18.50800  -15.27800 1.000 20.44320 ? 117 LYS   A CB    1 
ATOM   953  C  CG    . LYS   A 1 118 ? 11.93000  18.33200  -13.88700 1.000 18.47095 ? 117 LYS   A CG    1 
ATOM   954  C  CD    . LYS   A 1 118 ? 11.05800  17.47300  -12.96600 1.000 19.26074 ? 117 LYS   A CD    1 
ATOM   955  C  CE    . LYS   A 1 118 ? 11.74500  17.34000  -11.62900 1.000 18.87168 ? 117 LYS   A CE    1 
ATOM   956  N  NZ    . LYS   A 1 118 ? 10.88700  16.47100  -10.75600 1.000 20.32253 ? 117 LYS   A NZ    1 
ATOM   957  N  N     . SER   A 1 119 ? 12.28600  20.06000  -18.54100 1.000 21.89126 ? 118 SER   A N     1 
ATOM   958  C  CA    A SER   A 1 119 ? 11.69600  20.40700  -19.83400 0.500 23.36960 ? 118 SER   A CA    1 
ATOM   959  C  CA    B SER   A 1 119 ? 11.70100  20.40900  -19.83700 0.500 23.37165 ? 118 SER   A CA    1 
ATOM   960  C  C     . SER   A 1 119 ? 11.52800  19.20600  -20.76500 1.000 23.14106 ? 118 SER   A C     1 
ATOM   961  O  O     . SER   A 1 119 ? 10.80100  19.30400  -21.76200 1.000 25.60832 ? 118 SER   A O     1 
ATOM   962  C  CB    A SER   A 1 119 ? 12.53200  21.47800  -20.53200 0.500 23.10265 ? 118 SER   A CB    1 
ATOM   963  C  CB    B SER   A 1 119 ? 12.55200  21.46100  -20.55200 0.500 23.09944 ? 118 SER   A CB    1 
ATOM   964  O  OG    A SER   A 1 119 ? 12.59400  22.64700  -19.74300 0.500 20.04997 ? 118 SER   A OG    1 
ATOM   965  O  OG    B SER   A 1 119 ? 13.76800  20.90000  -21.01500 0.500 31.17170 ? 118 SER   A OG    1 
ATOM   966  N  N     . ASP   A 1 120 ? 12.19400  18.08600  -20.48700 1.000 22.38284 ? 119 ASP   A N     1 
ATOM   967  C  CA    . ASP   A 1 120 ? 11.99800  16.84600  -21.23800 1.000 24.83142 ? 119 ASP   A CA    1 
ATOM   968  C  C     . ASP   A 1 120 ? 10.63600  16.19000  -20.98700 1.000 27.04580 ? 119 ASP   A C     1 
ATOM   969  O  O     . ASP   A 1 120 ? 10.23400  15.31100  -21.75900 1.000 30.01669 ? 119 ASP   A O     1 
ATOM   970  C  CB    . ASP   A 1 120 ? 13.11500  15.88500  -20.82900 1.000 23.53581 ? 119 ASP   A CB    1 
ATOM   971  C  CG    . ASP   A 1 120 ? 13.10200  15.57800  -19.32600 1.000 24.32492 ? 119 ASP   A CG    1 
ATOM   972  O  OD1   . ASP   A 1 120 ? 13.50700  16.44900  -18.52400 1.000 24.80466 ? 119 ASP   A OD1   1 
ATOM   973  O  OD2   . ASP   A 1 120 ? 12.65600  14.45500  -18.98700 1.000 25.74884 ? 119 ASP   A OD2   1 
ATOM   974  N  N     . LEU   A 1 121 ? 9.87200   16.63000  -19.90200 1.000 25.12722 ? 120 LEU   A N     1 
ATOM   975  C  CA    . LEU   A 1 121 ? 8.75400   15.76000  -19.57800 1.000 25.83482 ? 120 LEU   A CA    1 
ATOM   976  C  C     . LEU   A 1 121 ? 7.48900   16.19300  -20.29600 1.000 28.05972 ? 120 LEU   A C     1 
ATOM   977  O  O     . LEU   A 1 121 ? 7.25900   17.39300  -20.50000 1.000 30.81974 ? 120 LEU   A O     1 
ATOM   978  C  CB    . LEU   A 1 121 ? 8.48700   15.80400  -18.08100 1.000 29.90290 ? 120 LEU   A CB    1 
ATOM   979  C  CG    . LEU   A 1 121 ? 9.50300   15.10700  -17.20500 1.000 27.69657 ? 120 LEU   A CG    1 
ATOM   980  C  CD1   . LEU   A 1 121 ? 9.12700   15.35800  -15.77500 1.000 27.65588 ? 120 LEU   A CD1   1 
ATOM   981  C  CD2   . LEU   A 1 121 ? 9.50400   13.62000  -17.51100 1.000 33.65293 ? 120 LEU   A CD2   1 
ATOM   982  N  N     . PRO   A 1 122 ? 6.62600   15.19600  -20.58900 1.000 27.14180 ? 121 PRO   A N     1 
ATOM   983  C  CA    . PRO   A 1 122 ? 5.37800   15.46900  -21.30700 1.000 29.89746 ? 121 PRO   A CA    1 
ATOM   984  C  C     . PRO   A 1 122 ? 4.20300   15.84800  -20.41500 1.000 29.12382 ? 121 PRO   A C     1 
ATOM   985  O  O     . PRO   A 1 122 ? 3.05100   15.79700  -20.86500 1.000 30.82564 ? 121 PRO   A O     1 
ATOM   986  C  CB    . PRO   A 1 122 ? 5.10700   14.13300  -22.01300 1.000 30.56317 ? 121 PRO   A CB    1 
ATOM   987  C  CG    . PRO   A 1 122 ? 5.62000   13.11500  -21.05800 1.000 29.94541 ? 121 PRO   A CG    1 
ATOM   988  C  CD    . PRO   A 1 122 ? 6.85100   13.74400  -20.42500 1.000 27.85963 ? 121 PRO   A CD    1 
ATOM   989  N  N     . SER   A 1 123 ? 4.47700   16.24800  -19.16300 1.000 27.64509 ? 122 SER   A N     1 
ATOM   990  C  CA    . SER   A 1 123 ? 3.43900   16.53100  -18.17400 1.000 29.76071 ? 122 SER   A CA    1 
ATOM   991  C  C     . SER   A 1 123 ? 3.40800   18.00000  -17.76500 1.000 29.23243 ? 122 SER   A C     1 
ATOM   992  O  O     . SER   A 1 123 ? 3.04900   18.34100  -16.62800 1.000 26.58094 ? 122 SER   A O     1 
ATOM   993  C  CB    . SER   A 1 123 ? 3.59700   15.63000  -16.95300 1.000 30.90091 ? 122 SER   A CB    1 
ATOM   994  O  OG    . SER   A 1 123 ? 4.95200   15.55700  -16.56100 1.000 28.15076 ? 122 SER   A OG    1 
ATOM   995  N  N     . ARG   A 1 124 ? 3.76100   18.88100  -18.69500 1.000 26.87015 ? 123 ARG   A N     1 
ATOM   996  C  CA    . ARG   A 1 124 ? 3.86200   20.29700  -18.37600 1.000 27.07256 ? 123 ARG   A CA    1 
ATOM   997  C  C     . ARG   A 1 124 ? 2.57900   20.84000  -17.75100 1.000 26.98376 ? 123 ARG   A C     1 
ATOM   998  O  O     . ARG   A 1 124 ? 1.47200   20.55900  -18.21100 1.000 28.75153 ? 123 ARG   A O     1 
ATOM   999  C  CB    . ARG   A 1 124 ? 4.18600   21.07700  -19.65500 1.000 32.73451 ? 123 ARG   A CB    1 
ATOM   1000 C  CG    . ARG   A 1 124 ? 4.20000   22.56900  -19.47200 1.000 27.42567 ? 123 ARG   A CG    1 
ATOM   1001 C  CD    . ARG   A 1 124 ? 4.57800   23.27800  -20.78600 1.000 30.05914 ? 123 ARG   A CD    1 
ATOM   1002 N  NE    . ARG   A 1 124 ? 5.95100   23.00300  -21.19800 1.000 30.91043 ? 123 ARG   A NE    1 
ATOM   1003 C  CZ    . ARG   A 1 124 ? 7.00800   23.70400  -20.81300 1.000 35.07702 ? 123 ARG   A CZ    1 
ATOM   1004 N  NH1   . ARG   A 1 124 ? 6.90200   24.68800  -19.93500 1.000 28.77512 ? 123 ARG   A NH1   1 
ATOM   1005 N  NH2   . ARG   A 1 124 ? 8.20900   23.39100  -21.29900 1.000 33.22175 ? 123 ARG   A NH2   1 
ATOM   1006 N  N     . THR   A 1 125 ? 2.74000   21.62300  -16.67500 1.000 26.49511 ? 124 THR   A N     1 
ATOM   1007 C  CA    . THR   A 1 125 ? 1.64200   22.38500  -16.09900 1.000 27.46737 ? 124 THR   A CA    1 
ATOM   1008 C  C     . THR   A 1 125 ? 1.88400   23.89200  -16.10700 1.000 26.77209 ? 124 THR   A C     1 
ATOM   1009 O  O     . THR   A 1 125 ? 0.92100   24.65200  -15.94400 1.000 30.81900 ? 124 THR   A O     1 
ATOM   1010 C  CB    . THR   A 1 125 ? 1.36700   21.94700  -14.64800 1.000 30.14394 ? 124 THR   A CB    1 
ATOM   1011 O  OG1   . THR   A 1 125 ? 2.51600   22.19500  -13.83700 1.000 27.40143 ? 124 THR   A OG1   1 
ATOM   1012 C  CG2   . THR   A 1 125 ? 1.00100   20.46300  -14.57300 1.000 30.63985 ? 124 THR   A CG2   1 
ATOM   1013 N  N     . VAL   A 1 126 ? 3.12100   24.33600  -16.30100 1.000 28.15441 ? 125 VAL   A N     1 
ATOM   1014 C  CA    . VAL   A 1 126 ? 3.48400   25.75000  -16.30300 1.000 27.30309 ? 125 VAL   A CA    1 
ATOM   1015 C  C     . VAL   A 1 126 ? 3.86200   26.13400  -17.72700 1.000 26.13856 ? 125 VAL   A C     1 
ATOM   1016 O  O     . VAL   A 1 126 ? 4.78200   25.55000  -18.30200 1.000 29.51523 ? 125 VAL   A O     1 
ATOM   1017 C  CB    . VAL   A 1 126 ? 4.66800   26.00000  -15.36500 1.000 28.23233 ? 125 VAL   A CB    1 
ATOM   1018 C  CG1   . VAL   A 1 126 ? 5.00900   27.50400  -15.28800 1.000 24.47777 ? 125 VAL   A CG1   1 
ATOM   1019 C  CG2   . VAL   A 1 126 ? 4.39300   25.40500  -13.97700 1.000 25.90937 ? 125 VAL   A CG2   1 
ATOM   1020 N  N     . ASP   A 1 127 ? 3.16300   27.11600  -18.29300 1.000 30.74208 ? 126 ASP   A N     1 
ATOM   1021 C  CA    . ASP   A 1 127 ? 3.47000   27.55500  -19.64900 1.000 29.09814 ? 126 ASP   A CA    1 
ATOM   1022 C  C     . ASP   A 1 127 ? 4.74900   28.37000  -19.68100 1.000 29.02328 ? 126 ASP   A C     1 
ATOM   1023 O  O     . ASP   A 1 127 ? 5.02300   29.16800  -18.77500 1.000 30.36476 ? 126 ASP   A O     1 
ATOM   1024 C  CB    . ASP   A 1 127 ? 2.35800   28.44200  -20.19100 1.000 34.39954 ? 126 ASP   A CB    1 
ATOM   1025 C  CG    . ASP   A 1 127 ? 1.10800   27.67700  -20.50000 1.000 42.28209 ? 126 ASP   A CG    1 
ATOM   1026 O  OD1   . ASP   A 1 127 ? 1.13900   26.83900  -21.42500 1.000 49.27680 ? 126 ASP   A OD1   1 
ATOM   1027 O  OD2   . ASP   A 1 127 ? 0.10100   27.90500  -19.80300 1.000 50.76929 ? 126 ASP   A OD2   1 
ATOM   1028 N  N     . THR   A 1 128 ? 5.52700   28.18300  -20.75100 1.000 29.81093 ? 127 THR   A N     1 
ATOM   1029 C  CA    . THR   A 1 128 ? 6.75600   28.95700  -20.91400 1.000 27.95041 ? 127 THR   A CA    1 
ATOM   1030 C  C     . THR   A 1 128 ? 6.47900   30.45000  -20.85400 1.000 27.66062 ? 127 THR   A C     1 
ATOM   1031 O  O     . THR   A 1 128 ? 7.24700   31.21300  -20.25500 1.000 25.95581 ? 127 THR   A O     1 
ATOM   1032 C  CB    . THR   A 1 128 ? 7.42100   28.58500  -22.24200 1.000 34.19033 ? 127 THR   A CB    1 
ATOM   1033 O  OG1   . THR   A 1 128 ? 7.93600   27.25000  -22.15300 1.000 39.19449 ? 127 THR   A OG1   1 
ATOM   1034 C  CG2   . THR   A 1 128 ? 8.55600   29.53600  -22.57500 1.000 36.92008 ? 127 THR   A CG2   1 
ATOM   1035 N  N     . LYS   A 1 129 ? 5.38700   30.89200  -21.48700 1.000 29.56781 ? 128 LYS   A N     1 
ATOM   1036 C  CA    . LYS   A 1 129 ? 5.06600   32.31400  -21.48200 1.000 32.78959 ? 128 LYS   A CA    1 
ATOM   1037 C  C     . LYS   A 1 129 ? 4.91100   32.85500  -20.06500 1.000 30.86372 ? 128 LYS   A C     1 
ATOM   1038 O  O     . LYS   A 1 129 ? 5.36300   33.96400  -19.77100 1.000 29.46287 ? 128 LYS   A O     1 
ATOM   1039 C  CB    . LYS   A 1 129 ? 3.81300   32.59100  -22.31700 1.000 31.49236 ? 128 LYS   A CB    1 
ATOM   1040 C  CG    . LYS   A 1 129 ? 3.71400   34.04600  -22.76600 1.000 41.33983 ? 128 LYS   A CG    1 
ATOM   1041 C  CD    . LYS   A 1 129 ? 4.67300   34.32200  -23.93900 1.000 48.39467 ? 128 LYS   A CD    1 
ATOM   1042 C  CE    . LYS   A 1 129 ? 5.22900   35.74800  -23.94000 1.000 47.51499 ? 128 LYS   A CE    1 
ATOM   1043 N  NZ    . LYS   A 1 129 ? 6.32800   35.91100  -22.93900 1.000 36.23151 ? 128 LYS   A NZ    1 
ATOM   1044 N  N     . GLN   A 1 130 ? 4.27300   32.09500  -19.16700 1.000 30.36388 ? 129 GLN   A N     1 
ATOM   1045 C  CA    . GLN   A 1 130 ? 4.13000   32.57700  -17.79600 1.000 32.03193 ? 129 GLN   A CA    1 
ATOM   1046 C  C     . GLN   A 1 130 ? 5.49100   32.77500  -17.14800 1.000 26.69196 ? 129 GLN   A C     1 
ATOM   1047 O  O     . GLN   A 1 130 ? 5.69200   33.71300  -16.36500 1.000 27.00395 ? 129 GLN   A O     1 
ATOM   1048 C  CB    . GLN   A 1 130 ? 3.34100   31.58400  -16.94000 1.000 29.72124 ? 129 GLN   A CB    1 
ATOM   1049 C  CG    . GLN   A 1 130 ? 2.19300   30.84400  -17.59600 1.000 41.10122 ? 129 GLN   A CG    1 
ATOM   1050 C  CD    . GLN   A 1 130 ? 1.65000   29.79000  -16.64500 1.000 43.88717 ? 129 GLN   A CD    1 
ATOM   1051 O  OE1   . GLN   A 1 130 ? 1.21000   28.71700  -17.05800 1.000 46.34135 ? 129 GLN   A OE1   1 
ATOM   1052 N  NE2   . GLN   A 1 130 ? 1.70100   30.09600  -15.35000 1.000 40.24854 ? 129 GLN   A NE2   1 
ATOM   1053 N  N     . ALA   A 1 131 ? 6.42300   31.86800  -17.42700 1.000 23.69477 ? 130 ALA   A N     1 
ATOM   1054 C  CA    . ALA   A 1 131 ? 7.74000   31.94500  -16.81100 1.000 22.47275 ? 130 ALA   A CA    1 
ATOM   1055 C  C     . ALA   A 1 131 ? 8.55300   33.09500  -17.39000 1.000 22.30673 ? 130 ALA   A C     1 
ATOM   1056 O  O     . ALA   A 1 131 ? 9.23800   33.81800  -16.65400 1.000 22.84368 ? 130 ALA   A O     1 
ATOM   1057 C  CB    . ALA   A 1 131 ? 8.46800   30.61400  -17.00300 1.000 26.08236 ? 130 ALA   A CB    1 
ATOM   1058 N  N     . GLN   A 1 132 ? 8.52000   33.24800  -18.71000 1.000 26.87976 ? 131 GLN   A N     1 
ATOM   1059 C  CA    . GLN   A 1 132 ? 9.16500   34.39100  -19.34500 1.000 28.19378 ? 131 GLN   A CA    1 
ATOM   1060 C  C     . GLN   A 1 132 ? 8.60600   35.70400  -18.81400 1.000 27.71552 ? 131 GLN   A C     1 
ATOM   1061 O  O     . GLN   A 1 132 ? 9.36300   36.65000  -18.56900 1.000 30.03284 ? 131 GLN   A O     1 
ATOM   1062 C  CB    . GLN   A 1 132 ? 8.96300   34.31800  -20.85100 1.000 32.52038 ? 131 GLN   A CB    1 
ATOM   1063 C  CG    . GLN   A 1 132 ? 9.58500   33.10900  -21.53400 1.000 30.96372 ? 131 GLN   A CG    1 
ATOM   1064 C  CD    . GLN   A 1 132 ? 9.16200   33.01200  -22.99100 1.000 37.36633 ? 131 GLN   A CD    1 
ATOM   1065 O  OE1   . GLN   A 1 132 ? 8.07300   33.45200  -23.35900 1.000 36.36513 ? 131 GLN   A OE1   1 
ATOM   1066 N  NE2   . GLN   A 1 132 ? 10.01800  32.42700  -23.82200 1.000 46.19443 ? 131 GLN   A NE2   1 
ATOM   1067 N  N     . ASP   A 1 133 ? 7.28700   35.78900  -18.62900 1.000 27.42604 ? 132 ASP   A N     1 
ATOM   1068 C  CA    . ASP   A 1 133 ? 6.70800   37.02400  -18.10200 1.000 30.61242 ? 132 ASP   A CA    1 
ATOM   1069 C  C     . ASP   A 1 133 ? 7.20900   37.29900  -16.68300 1.000 30.68705 ? 132 ASP   A C     1 
ATOM   1070 O  O     . ASP   A 1 133 ? 7.53700   38.43900  -16.34300 1.000 30.69808 ? 132 ASP   A O     1 
ATOM   1071 C  CB    . ASP   A 1 133 ? 5.17300   36.98700  -18.15400 1.000 34.06036 ? 132 ASP   A CB    1 
ATOM   1072 C  CG    . ASP   A 1 133 ? 4.61300   37.05900  -19.57900 1.000 37.02191 ? 132 ASP   A CG    1 
ATOM   1073 O  OD1   . ASP   A 1 133 ? 5.36200   37.40500  -20.51700 1.000 38.87791 ? 132 ASP   A OD1   1 
ATOM   1074 O  OD2   . ASP   A 1 133 ? 3.40500   36.76700  -19.77200 1.000 37.78017 ? 132 ASP   A OD2   1 
ATOM   1075 N  N     . LEU   A 1 134 ? 7.28100   36.27000  -15.84100 1.000 26.30942 ? 133 LEU   A N     1 
ATOM   1076 C  CA    . LEU   A 1 134 ? 7.75500   36.48500  -14.48200 1.000 26.86827 ? 133 LEU   A CA    1 
ATOM   1077 C  C     . LEU   A 1 134 ? 9.21500   36.92400  -14.47800 1.000 24.14563 ? 133 LEU   A C     1 
ATOM   1078 O  O     . LEU   A 1 134 ? 9.58300   37.87900  -13.79100 1.000 27.60616 ? 133 LEU   A O     1 
ATOM   1079 C  CB    . LEU   A 1 134 ? 7.61200   35.20900  -13.66300 1.000 28.91495 ? 133 LEU   A CB    1 
ATOM   1080 C  CG    . LEU   A 1 134 ? 7.99300   35.35300  -12.19100 1.000 27.75507 ? 133 LEU   A CG    1 
ATOM   1081 C  CD1   . LEU   A 1 134 ? 7.02500   36.27400  -11.52200 1.000 33.36211 ? 133 LEU   A CD1   1 
ATOM   1082 C  CD2   . LEU   A 1 134 ? 7.97600   33.97800  -11.55800 1.000 25.48875 ? 133 LEU   A CD2   1 
ATOM   1083 N  N     . ALA   A 1 135 ? 10.06100  36.25700  -15.26300 1.000 24.43525 ? 134 ALA   A N     1 
ATOM   1084 C  CA    . ALA   A 1 135 ? 11.46400  36.66300  -15.28800 1.000 23.05484 ? 134 ALA   A CA    1 
ATOM   1085 C  C     . ALA   A 1 135 ? 11.61900  38.09400  -15.80400 1.000 24.47894 ? 134 ALA   A C     1 
ATOM   1086 O  O     . ALA   A 1 135 ? 12.41500  38.86900  -15.26600 1.000 23.60940 ? 134 ALA   A O     1 
ATOM   1087 C  CB    . ALA   A 1 135 ? 12.30000  35.68800  -16.11300 1.000 22.29340 ? 134 ALA   A CB    1 
ATOM   1088 N  N     . ARG   A 1 136 ? 10.87300  38.45000  -16.84500 1.000 26.56811 ? 135 ARG   A N     1 
ATOM   1089 C  CA    . ARG   A 1 136 ? 10.92500  39.81400  -17.35300 1.000 27.14379 ? 135 ARG   A CA    1 
ATOM   1090 C  C     . ARG   A 1 136 ? 10.51800  40.80600  -16.27000 1.000 30.33628 ? 135 ARG   A C     1 
ATOM   1091 O  O     . ARG   A 1 136 ? 11.13100  41.87500  -16.13800 1.000 31.26121 ? 135 ARG   A O     1 
ATOM   1092 C  CB    . ARG   A 1 136 ? 10.05900  39.95700  -18.61600 1.000 28.30489 ? 135 ARG   A CB    1 
ATOM   1093 C  CG    . ARG   A 1 136 ? 10.19400  41.29100  -19.30500 1.000 36.32170 ? 135 ARG   A CG    1 
ATOM   1094 C  CD    . ARG   A 1 136 ? 9.36600   41.30700  -20.57300 1.000 38.35267 ? 135 ARG   A CD    1 
ATOM   1095 N  NE    . ARG   A 1 136 ? 9.96100   40.52100  -21.64700 1.000 48.05947 ? 135 ARG   A NE    1 
ATOM   1096 C  CZ    . ARG   A 1 136 ? 11.04600  40.88100  -22.32400 1.000 49.68499 ? 135 ARG   A CZ    1 
ATOM   1097 N  NH1   . ARG   A 1 136 ? 11.73100  41.96800  -22.00700 1.000 53.50006 ? 135 ARG   A NH1   1 
ATOM   1098 N  NH2   . ARG   A 1 136 ? 11.45200  40.13500  -23.34900 1.000 43.77869 ? 135 ARG   A NH2   1 
ATOM   1099 N  N     . SER   A 1 137 ? 9.50400   40.45800  -15.46500 1.000 29.83656 ? 136 SER   A N     1 
ATOM   1100 C  CA    . SER   A 1 137 ? 9.04400   41.37100  -14.41700 1.000 34.00450 ? 136 SER   A CA    1 
ATOM   1101 C  C     . SER   A 1 137 ? 10.11400  41.59900  -13.35700 1.000 32.92014 ? 136 SER   A C     1 
ATOM   1102 O  O     . SER   A 1 137 ? 10.15400  42.66700  -12.72500 1.000 32.49335 ? 136 SER   A O     1 
ATOM   1103 C  CB    . SER   A 1 137 ? 7.73200   40.87300  -13.79500 1.000 34.76430 ? 136 SER   A CB    1 
ATOM   1104 O  OG    . SER   A 1 137 ? 7.91800   39.76200  -12.95600 1.000 41.10576 ? 136 SER   A OG    1 
ATOM   1105 N  N     . TYR   A 1 138 ? 10.98300  40.62500  -13.16900 1.000 25.98506 ? 137 TYR   A N     1 
ATOM   1106 C  CA    . TYR   A 1 138 ? 12.06800  40.65400  -12.19300 1.000 29.89182 ? 137 TYR   A CA    1 
ATOM   1107 C  C     . TYR   A 1 138 ? 13.35600  41.20600  -12.77200 1.000 23.93439 ? 137 TYR   A C     1 
ATOM   1108 O  O     . TYR   A 1 138 ? 14.32800  41.37400  -12.02100 1.000 29.17457 ? 137 TYR   A O     1 
ATOM   1109 C  CB    . TYR   A 1 138 ? 12.41000  39.23400  -11.71200 1.000 27.56142 ? 137 TYR   A CB    1 
ATOM   1110 C  CG    . TYR   A 1 138 ? 11.38900  38.51800  -10.85900 1.000 26.85134 ? 137 TYR   A CG    1 
ATOM   1111 C  CD1   . TYR   A 1 138 ? 10.35800  39.21000  -10.24300 1.000 29.75535 ? 137 TYR   A CD1   1 
ATOM   1112 C  CD2   . TYR   A 1 138 ? 11.47100  37.14200  -10.67100 1.000 24.94632 ? 137 TYR   A CD2   1 
ATOM   1113 C  CE1   . TYR   A 1 138 ? 9.43400   38.54900  -9.44400  1.000 31.58404 ? 137 TYR   A CE1   1 
ATOM   1114 C  CE2   . TYR   A 1 138 ? 10.55900  36.47300  -9.87300  1.000 28.88458 ? 137 TYR   A CE2   1 
ATOM   1115 C  CZ    . TYR   A 1 138 ? 9.53600   37.19200  -9.28000  1.000 28.22212 ? 137 TYR   A CZ    1 
ATOM   1116 O  OH    . TYR   A 1 138 ? 8.62500   36.52200  -8.48800  1.000 34.51017 ? 137 TYR   A OH    1 
ATOM   1117 N  N     . GLY   A 1 139 ? 13.39500  41.41200  -14.08600 1.000 26.02943 ? 138 GLY   A N     1 
ATOM   1118 C  CA    . GLY   A 1 139 ? 14.60200  41.84000  -14.78900 1.000 27.27091 ? 138 GLY   A CA    1 
ATOM   1119 C  C     . GLY   A 1 139 ? 15.72800  40.82500  -14.74400 1.000 27.28291 ? 138 GLY   A C     1 
ATOM   1120 O  O     . GLY   A 1 139 ? 16.89700  41.20200  -14.61400 1.000 28.07029 ? 138 GLY   A O     1 
ATOM   1121 N  N     . ILE   A 1 140 ? 15.40200  39.53700  -14.80400 1.000 21.05874 ? 139 ILE   A N     1 
ATOM   1122 C  CA    . ILE   A 1 140 ? 16.42000  38.48900  -14.72700 1.000 21.94978 ? 139 ILE   A CA    1 
ATOM   1123 C  C     . ILE   A 1 140 ? 16.21200  37.53000  -15.89100 1.000 18.93086 ? 139 ILE   A C     1 
ATOM   1124 O  O     . ILE   A 1 140 ? 15.11700  37.45700  -16.46000 1.000 23.56148 ? 139 ILE   A O     1 
ATOM   1125 C  CB    . ILE   A 1 140 ? 16.37800  37.72400  -13.37300 1.000 19.67218 ? 139 ILE   A CB    1 
ATOM   1126 C  CG1   . ILE   A 1 140 ? 15.08100  36.90100  -13.22100 1.000 19.62418 ? 139 ILE   A CG1   1 
ATOM   1127 C  CG2   . ILE   A 1 140 ? 16.55700  38.69800  -12.22400 1.000 23.18024 ? 139 ILE   A CG2   1 
ATOM   1128 C  CD1   . ILE   A 1 140 ? 15.03400  35.99000  -11.95000 1.000 18.85856 ? 139 ILE   A CD1   1 
ATOM   1129 N  N     . PRO   A 1 141 ? 17.24400  36.76700  -16.24600 1.000 21.95763 ? 140 PRO   A N     1 
ATOM   1130 C  CA    . PRO   A 1 141 ? 17.11600  35.78600  -17.33100 1.000 20.53364 ? 140 PRO   A CA    1 
ATOM   1131 C  C     . PRO   A 1 141 ? 16.23600  34.60200  -16.93900 1.000 17.58207 ? 140 PRO   A C     1 
ATOM   1132 O  O     . PRO   A 1 141 ? 16.12700  34.23000  -15.76300 1.000 18.43160 ? 140 PRO   A O     1 
ATOM   1133 C  CB    . PRO   A 1 141 ? 18.56200  35.32200  -17.54200 1.000 21.97407 ? 140 PRO   A CB    1 
ATOM   1134 C  CG    . PRO   A 1 141 ? 19.41200  36.44800  -17.02200 1.000 22.29402 ? 140 PRO   A CG    1 
ATOM   1135 C  CD    . PRO   A 1 141 ? 18.64100  36.92300  -15.80800 1.000 21.88594 ? 140 PRO   A CD    1 
ATOM   1136 N  N     . PHE   A 1 142 ? 15.63700  33.98900  -17.96400 1.000 19.71269 ? 141 PHE   A N     1 
ATOM   1137 C  CA    . PHE   A 1 142 ? 14.93200  32.72100  -17.81600 1.000 21.49917 ? 141 PHE   A CA    1 
ATOM   1138 C  C     . PHE   A 1 142 ? 15.56500  31.66500  -18.71100 1.000 20.82369 ? 141 PHE   A C     1 
ATOM   1139 O  O     . PHE   A 1 142 ? 15.72000  31.87700  -19.91700 1.000 23.66438 ? 141 PHE   A O     1 
ATOM   1140 C  CB    . PHE   A 1 142 ? 13.46500  32.88400  -18.19200 1.000 20.88358 ? 141 PHE   A CB    1 
ATOM   1141 C  CG    . PHE   A 1 142 ? 12.72500  31.58500  -18.27300 1.000 22.14874 ? 141 PHE   A CG    1 
ATOM   1142 C  CD1   . PHE   A 1 142 ? 12.66200  30.74900  -17.16900 1.000 22.40088 ? 141 PHE   A CD1   1 
ATOM   1143 C  CD2   . PHE   A 1 142 ? 12.09200  31.20000  -19.44200 1.000 27.63421 ? 141 PHE   A CD2   1 
ATOM   1144 C  CE1   . PHE   A 1 142 ? 12.00700  29.52800  -17.23300 1.000 20.30890 ? 141 PHE   A CE1   1 
ATOM   1145 C  CE2   . PHE   A 1 142 ? 11.42300  29.98600  -19.50700 1.000 25.15870 ? 141 PHE   A CE2   1 
ATOM   1146 C  CZ    . PHE   A 1 142 ? 11.35500  29.16400  -18.40000 1.000 23.76325 ? 141 PHE   A CZ    1 
ATOM   1147 N  N     . ILE   A 1 143 ? 15.91000  30.52600  -18.12800 1.000 19.64423 ? 142 ILE   A N     1 
ATOM   1148 C  CA    . ILE   A 1 143 ? 16.52000  29.42000  -18.87200 1.000 20.86604 ? 142 ILE   A CA    1 
ATOM   1149 C  C     . ILE   A 1 143 ? 15.67000  28.17200  -18.68200 1.000 20.44576 ? 142 ILE   A C     1 
ATOM   1150 O  O     . ILE   A 1 143 ? 15.35500  27.81500  -17.54400 1.000 19.01994 ? 142 ILE   A O     1 
ATOM   1151 C  CB    . ILE   A 1 143 ? 17.95100  29.13900  -18.37300 1.000 22.43126 ? 142 ILE   A CB    1 
ATOM   1152 C  CG1   . ILE   A 1 143 ? 18.79800  30.41200  -18.39200 1.000 24.98493 ? 142 ILE   A CG1   1 
ATOM   1153 C  CG2   . ILE   A 1 143 ? 18.61500  28.02600  -19.19000 1.000 25.33319 ? 142 ILE   A CG2   1 
ATOM   1154 C  CD1   . ILE   A 1 143 ? 19.02600  30.95100  -19.79000 1.000 28.86888 ? 142 ILE   A CD1   1 
ATOM   1155 N  N     . GLU   A 1 144 ? 15.33900  27.49600  -19.78300 1.000 20.67356 ? 143 GLU   A N     1 
ATOM   1156 C  CA    . GLU   A 1 144 ? 14.68000  26.19100  -19.74700 1.000 20.53333 ? 143 GLU   A CA    1 
ATOM   1157 C  C     . GLU   A 1 144 ? 15.72600  25.08900  -19.69500 1.000 21.64715 ? 143 GLU   A C     1 
ATOM   1158 O  O     . GLU   A 1 144 ? 16.66500  25.08200  -20.49700 1.000 25.41562 ? 143 GLU   A O     1 
ATOM   1159 C  CB    . GLU   A 1 144 ? 13.86800  26.01300  -21.02900 1.000 24.53739 ? 143 GLU   A CB    1 
ATOM   1160 C  CG    . GLU   A 1 144 ? 12.85900  27.11100  -21.28100 1.000 30.60675 ? 143 GLU   A CG    1 
ATOM   1161 C  CD    . GLU   A 1 144 ? 12.08700  26.87000  -22.55000 1.000 40.33371 ? 143 GLU   A CD    1 
ATOM   1162 O  OE1   . GLU   A 1 144 ? 11.42200  25.81500  -22.64800 1.000 36.85458 ? 143 GLU   A OE1   1 
ATOM   1163 O  OE2   . GLU   A 1 144 ? 12.16000  27.72300  -23.46400 1.000 40.76492 ? 143 GLU   A OE2   1 
ATOM   1164 N  N     . THR   A 1 145 ? 15.57100  24.14400  -18.77200 1.000 20.02170 ? 144 THR   A N     1 
ATOM   1165 C  CA    . THR   A 1 145 ? 16.60700  23.13300  -18.60800 1.000 18.59362 ? 144 THR   A CA    1 
ATOM   1166 C  C     . THR   A 1 145 ? 15.98700  21.75700  -18.51700 1.000 19.23268 ? 144 THR   A C     1 
ATOM   1167 O  O     . THR   A 1 145 ? 14.79400  21.60200  -18.23200 1.000 19.72124 ? 144 THR   A O     1 
ATOM   1168 C  CB    . THR   A 1 145 ? 17.46900  23.34400  -17.34500 1.000 17.17077 ? 144 THR   A CB    1 
ATOM   1169 O  OG1   . THR   A 1 145 ? 16.66700  23.21000  -16.14700 1.000 17.65715 ? 144 THR   A OG1   1 
ATOM   1170 C  CG2   . THR   A 1 145 ? 18.09900  24.76400  -17.34900 1.000 19.17430 ? 144 THR   A CG2   1 
ATOM   1171 N  N     . SER   A 1 146 ? 16.83300  20.75700  -18.73200 1.000 20.79745 ? 145 SER   A N     1 
ATOM   1172 C  CA    . SER   A 1 146 ? 16.52400  19.38200  -18.34200 1.000 19.08182 ? 145 SER   A CA    1 
ATOM   1173 C  C     . SER   A 1 146 ? 17.80200  18.76300  -17.80900 1.000 19.89543 ? 145 SER   A C     1 
ATOM   1174 O  O     . SER   A 1 146 ? 18.76500  18.58500  -18.56500 1.000 20.98223 ? 145 SER   A O     1 
ATOM   1175 C  CB    . SER   A 1 146 ? 15.99500  18.55900  -19.51000 1.000 20.98152 ? 145 SER   A CB    1 
ATOM   1176 O  OG    . SER   A 1 146 ? 16.00700  17.17200  -19.19500 1.000 23.54549 ? 145 SER   A OG    1 
ATOM   1177 N  N     . ALA   A 1 147 ? 17.83400  18.47200  -16.50900 1.000 18.49716 ? 146 ALA   A N     1 
ATOM   1178 C  CA    . ALA   A 1 147 ? 18.95600  17.70900  -15.97900 1.000 19.09803 ? 146 ALA   A CA    1 
ATOM   1179 C  C     . ALA   A 1 147 ? 19.08800  16.34100  -16.63700 1.000 21.81772 ? 146 ALA   A C     1 
ATOM   1180 O  O     . ALA   A 1 147 ? 20.18100  15.78200  -16.67700 1.000 24.65588 ? 146 ALA   A O     1 
ATOM   1181 C  CB    . ALA   A 1 147 ? 18.85000  17.55800  -14.45200 1.000 20.15707 ? 146 ALA   A CB    1 
ATOM   1182 N  N     . LYS   A 1 148 ? 18.01000  15.79300  -17.17900 1.000 20.86612 ? 147 LYS   A N     1 
ATOM   1183 C  CA    . LYS   A 1 148 ? 18.09000  14.43400  -17.70300 1.000 22.39439 ? 147 LYS   A CA    1 
ATOM   1184 C  C     . LYS   A 1 148 ? 18.80200  14.40400  -19.05000 1.000 27.74780 ? 147 LYS   A C     1 
ATOM   1185 O  O     . LYS   A 1 148 ? 19.58500  13.48400  -19.32800 1.000 28.81207 ? 147 LYS   A O     1 
ATOM   1186 C  CB    . LYS   A 1 148 ? 16.68500  13.83500  -17.80600 1.000 24.30450 ? 147 LYS   A CB    1 
ATOM   1187 C  CG    . LYS   A 1 148 ? 16.58200  12.51100  -18.57000 1.000 27.81780 ? 147 LYS   A CG    1 
ATOM   1188 C  CD    . LYS   A 1 148 ? 15.18600  11.97100  -18.42400 1.000 27.08663 ? 147 LYS   A CD    1 
ATOM   1189 C  CE    . LYS   A 1 148 ? 15.10900  10.61300  -19.06000 1.000 31.01601 ? 147 LYS   A CE    1 
ATOM   1190 N  NZ    . LYS   A 1 148 ? 13.72100  10.03900  -19.01400 1.000 41.49170 ? 147 LYS   A NZ    1 
ATOM   1191 N  N     . THR   A 1 149 ? 18.49100  15.35300  -19.92800 1.000 26.06515 ? 148 THR   A N     1 
ATOM   1192 C  CA    . THR   A 1 149 ? 19.07900  15.38500  -21.26400 1.000 28.34491 ? 148 THR   A CA    1 
ATOM   1193 C  C     . THR   A 1 149 ? 20.27300  16.32100  -21.33000 1.000 24.56502 ? 148 THR   A C     1 
ATOM   1194 O  O     . THR   A 1 149 ? 20.91800  16.39700  -22.38900 1.000 25.83870 ? 148 THR   A O     1 
ATOM   1195 C  CB    . THR   A 1 149 ? 18.05700  15.86400  -22.30300 1.000 27.35421 ? 148 THR   A CB    1 
ATOM   1196 O  OG1   . THR   A 1 149 ? 17.77600  17.26800  -22.10600 1.000 23.30537 ? 148 THR   A OG1   1 
ATOM   1197 C  CG2   . THR   A 1 149 ? 16.77700  15.00700  -22.27400 1.000 26.39816 ? 148 THR   A CG2   1 
ATOM   1198 N  N     . ARG   A 1 150 ? 20.49900  17.09900  -20.27000 1.000 21.46653 ? 149 ARG   A N     1 
ATOM   1199 C  CA    . ARG   A 1 150 ? 21.59800  18.11000  -20.20400 1.000 23.68475 ? 149 ARG   A CA    1 
ATOM   1200 C  C     . ARG   A 1 150 ? 21.20900  19.40800  -20.94700 1.000 22.92749 ? 149 ARG   A C     1 
ATOM   1201 O  O     . ARG   A 1 150 ? 21.99100  20.35900  -20.87400 1.000 24.25496 ? 149 ARG   A O     1 
ATOM   1202 C  CB    . ARG   A 1 150 ? 22.98600  17.55000  -20.55200 1.000 27.52377 ? 149 ARG   A CB    1 
ATOM   1203 C  CG    . ARG   A 1 150 ? 24.02500  18.17200  -19.62700 1.000 36.10175 ? 149 ARG   A CG    1 
ATOM   1204 C  CD    . ARG   A 1 150 ? 25.36900  17.45700  -19.58200 1.000 38.16294 ? 149 ARG   A CD    1 
ATOM   1205 N  NE    . ARG   A 1 150 ? 26.33800  18.03600  -18.64200 1.000 33.14247 ? 149 ARG   A NE    1 
ATOM   1206 C  CZ    . ARG   A 1 150 ? 26.90700  19.23200  -18.73800 1.000 39.60282 ? 149 ARG   A CZ    1 
ATOM   1207 N  NH1   . ARG   A 1 150 ? 26.65500  20.01200  -19.77100 1.000 39.92037 ? 149 ARG   A NH1   1 
ATOM   1208 N  NH2   . ARG   A 1 150 ? 27.74700  19.64300  -17.80700 1.000 38.70092 ? 149 ARG   A NH2   1 
ATOM   1209 N  N     . GLN   A 1 151 ? 20.02800  19.48900  -21.55700 1.000 23.61685 ? 150 GLN   A N     1 
ATOM   1210 C  CA    . GLN   A 1 151 ? 19.57300  20.74700  -22.14800 1.000 26.31808 ? 150 GLN   A CA    1 
ATOM   1211 C  C     . GLN   A 1 151 ? 19.68600  21.90700  -21.16300 1.000 23.95235 ? 150 GLN   A C     1 
ATOM   1212 O  O     . GLN   A 1 151 ? 19.12900  21.86500  -20.06500 1.000 21.91680 ? 150 GLN   A O     1 
ATOM   1213 C  CB    . GLN   A 1 151 ? 18.11500  20.62400  -22.57700 1.000 26.69348 ? 150 GLN   A CB    1 
ATOM   1214 C  CG    . GLN   A 1 151 ? 17.49400  22.00200  -22.89600 1.000 30.61281 ? 150 GLN   A CG    1 
ATOM   1215 C  CD    . GLN   A 1 151 ? 15.98800  21.98900  -23.04600 1.000 37.87067 ? 150 GLN   A CD    1 
ATOM   1216 O  OE1   . GLN   A 1 151 ? 15.33200  20.95600  -22.87800 1.000 37.61887 ? 150 GLN   A OE1   1 
ATOM   1217 N  NE2   . GLN   A 1 151 ? 15.42500  23.15000  -23.37500 1.000 43.80164 ? 150 GLN   A NE2   1 
ATOM   1218 N  N     . GLY   A 1 152 ? 20.39800  22.95700  -21.56600 1.000 22.67004 ? 151 GLY   A N     1 
ATOM   1219 C  CA    . GLY   A 1 152 ? 20.43200  24.19800  -20.79900 1.000 20.69756 ? 151 GLY   A CA    1 
ATOM   1220 C  C     . GLY   A 1 152 ? 21.20600  24.16900  -19.50000 1.000 19.44730 ? 151 GLY   A C     1 
ATOM   1221 O  O     . GLY   A 1 152 ? 21.21400  25.17800  -18.79100 1.000 19.15743 ? 151 GLY   A O     1 
ATOM   1222 N  N     . VAL   A 1 153 ? 21.83600  23.04800  -19.12900 1.000 18.30822 ? 152 VAL   A N     1 
ATOM   1223 C  CA    . VAL   A 1 153 ? 22.46800  22.95600  -17.80900 1.000 21.37403 ? 152 VAL   A CA    1 
ATOM   1224 C  C     . VAL   A 1 153 ? 23.64800  23.91900  -17.70200 1.000 17.65068 ? 152 VAL   A C     1 
ATOM   1225 O  O     . VAL   A 1 153 ? 23.72700  24.75200  -16.77700 1.000 17.66063 ? 152 VAL   A O     1 
ATOM   1226 C  CB    . VAL   A 1 153 ? 22.88000  21.51100  -17.48600 1.000 19.36141 ? 152 VAL   A CB    1 
ATOM   1227 C  CG1   . VAL   A 1 153 ? 23.74200  21.47300  -16.21100 1.000 23.28825 ? 152 VAL   A CG1   1 
ATOM   1228 C  CG2   . VAL   A 1 153 ? 21.67400  20.63500  -17.32900 1.000 20.60471 ? 152 VAL   A CG2   1 
ATOM   1229 N  N     . ASP   A 1 154 ? 24.61800  23.80000  -18.62200 1.000 19.72268 ? 153 ASP   A N     1 
ATOM   1230 C  CA    . ASP   A 1 154 ? 25.73500  24.75500  -18.60400 1.000 18.12823 ? 153 ASP   A CA    1 
ATOM   1231 C  C     . ASP   A 1 154 ? 25.21200  26.17700  -18.72000 1.000 18.35619 ? 153 ASP   A C     1 
ATOM   1232 O  O     . ASP   A 1 154 ? 25.64100  27.07000  -17.97900 1.000 18.87236 ? 153 ASP   A O     1 
ATOM   1233 C  CB    . ASP   A 1 154 ? 26.72300  24.49300  -19.73900 1.000 22.31592 ? 153 ASP   A CB    1 
ATOM   1234 C  CG    . ASP   A 1 154 ? 27.55100  23.25000  -19.51400 1.000 32.11367 ? 153 ASP   A CG    1 
ATOM   1235 O  OD1   . ASP   A 1 154 ? 27.54900  22.69800  -18.40300 1.000 32.85003 ? 153 ASP   A OD1   1 
ATOM   1236 O  OD2   . ASP   A 1 154 ? 28.19800  22.81300  -20.48400 1.000 32.47187 ? 153 ASP   A OD2   1 
ATOM   1237 N  N     . ASP   A 1 155 ? 24.24300  26.37700  -19.60400 1.000 18.76180 ? 154 ASP   A N     1 
ATOM   1238 C  CA    . ASP   A 1 155 ? 23.66900  27.69500  -19.84900 1.000 20.42614 ? 154 ASP   A CA    1 
ATOM   1239 C  C     . ASP   A 1 155 ? 23.14900  28.32300  -18.55600 1.000 20.92749 ? 154 ASP   A C     1 
ATOM   1240 O  O     . ASP   A 1 155 ? 23.38900  29.50700  -18.28700 1.000 19.31678 ? 154 ASP   A O     1 
ATOM   1241 C  CB    . ASP   A 1 155 ? 22.56400  27.54000  -20.89400 1.000 22.75016 ? 154 ASP   A CB    1 
ATOM   1242 C  CG    . ASP   A 1 155 ? 22.07200  28.86300  -21.42800 1.000 32.33193 ? 154 ASP   A CG    1 
ATOM   1243 O  OD1   . ASP   A 1 155 ? 22.80400  29.87200  -21.30100 1.000 31.78669 ? 154 ASP   A OD1   1 
ATOM   1244 O  OD2   . ASP   A 1 155 ? 20.95400  28.88700  -21.98300 1.000 34.66783 ? 154 ASP   A OD2   1 
ATOM   1245 N  N     . ALA   A 1 156 ? 22.47400  27.54600  -17.72500 1.000 17.38035 ? 155 ALA   A N     1 
ATOM   1246 C  CA    . ALA   A 1 156 ? 21.90000  28.11600  -16.51900 1.000 17.50531 ? 155 ALA   A CA    1 
ATOM   1247 C  C     . ALA   A 1 156 ? 22.98900  28.63600  -15.58100 1.000 17.89379 ? 155 ALA   A C     1 
ATOM   1248 O  O     . ALA   A 1 156 ? 22.92900  29.78100  -15.09000 1.000 16.08239 ? 155 ALA   A O     1 
ATOM   1249 C  CB    . ALA   A 1 156 ? 21.06200  27.04600  -15.83400 1.000 18.09265 ? 155 ALA   A CB    1 
ATOM   1250 N  N     . PHE   A 1 157 ? 24.00200  27.81200  -15.32800 1.000 16.85180 ? 156 PHE   A N     1 
ATOM   1251 C  CA    . PHE   A 1 157 ? 25.04000  28.22100  -14.39300 1.000 16.38898 ? 156 PHE   A CA    1 
ATOM   1252 C  C     . PHE   A 1 157 ? 25.90300  29.32000  -14.98100 1.000 14.41746 ? 156 PHE   A C     1 
ATOM   1253 O  O     . PHE   A 1 157 ? 26.27700  30.26600  -14.26700 1.000 13.91760 ? 156 PHE   A O     1 
ATOM   1254 C  CB    . PHE   A 1 157 ? 25.88800  27.01200  -13.99200 1.000 14.86794 ? 156 PHE   A CB    1 
ATOM   1255 C  CG    . PHE   A 1 157 ? 25.19000  26.07100  -13.06100 1.000 14.93008 ? 156 PHE   A CG    1 
ATOM   1256 C  CD1   . PHE   A 1 157 ? 25.18300  26.31100  -11.66900 1.000 15.01078 ? 156 PHE   A CD1   1 
ATOM   1257 C  CD2   . PHE   A 1 157 ? 24.50800  24.97400  -13.55300 1.000 17.57206 ? 156 PHE   A CD2   1 
ATOM   1258 C  CE1   . PHE   A 1 157 ? 24.52700  25.44500  -10.78200 1.000 15.69866 ? 156 PHE   A CE1   1 
ATOM   1259 C  CE2   . PHE   A 1 157 ? 23.83600  24.11600  -12.66400 1.000 16.88041 ? 156 PHE   A CE2   1 
ATOM   1260 C  CZ    . PHE   A 1 157 ? 23.87600  24.33900  -11.26900 1.000 16.03832 ? 156 PHE   A CZ    1 
ATOM   1261 N  N     . TYR   A 1 158 ? 26.20700  29.22800  -16.27900 1.000 16.79154 ? 157 TYR   A N     1 
ATOM   1262 C  CA    . TYR   A 1 158 ? 27.04700  30.24300  -16.89900 1.000 16.66887 ? 157 TYR   A CA    1 
ATOM   1263 C  C     . TYR   A 1 158 ? 26.32500  31.57700  -16.95900 1.000 16.30617 ? 157 TYR   A C     1 
ATOM   1264 O  O     . TYR   A 1 158 ? 26.94600  32.63000  -16.78900 1.000 16.33123 ? 157 TYR   A O     1 
ATOM   1265 C  CB    . TYR   A 1 158 ? 27.46600  29.82900  -18.31100 1.000 19.76441 ? 157 TYR   A CB    1 
ATOM   1266 C  CG    . TYR   A 1 158 ? 28.44300  28.66400  -18.38900 1.000 21.59599 ? 157 TYR   A CG    1 
ATOM   1267 C  CD1   . TYR   A 1 158 ? 28.79700  27.93400  -17.26900 1.000 24.22636 ? 157 TYR   A CD1   1 
ATOM   1268 C  CD2   . TYR   A 1 158 ? 28.99900  28.31200  -19.59900 1.000 25.03642 ? 157 TYR   A CD2   1 
ATOM   1269 C  CE1   . TYR   A 1 158 ? 29.70200  26.86300  -17.36100 1.000 22.84961 ? 157 TYR   A CE1   1 
ATOM   1270 C  CE2   . TYR   A 1 158 ? 29.90500  27.23400  -19.70500 1.000 24.62897 ? 157 TYR   A CE2   1 
ATOM   1271 C  CZ    . TYR   A 1 158 ? 30.23900  26.52900  -18.56700 1.000 26.07283 ? 157 TYR   A CZ    1 
ATOM   1272 O  OH    . TYR   A 1 158 ? 31.12900  25.47100  -18.66300 1.000 33.09859 ? 157 TYR   A OH    1 
ATOM   1273 N  N     . THR   A 1 159 ? 25.02200  31.56000  -17.25100 1.000 16.69306 ? 158 THR   A N     1 
ATOM   1274 C  CA    . THR   A 1 159 ? 24.25300  32.80600  -17.28800 1.000 15.36280 ? 158 THR   A CA    1 
ATOM   1275 C  C     . THR   A 1 159 ? 24.23300  33.44800  -15.90400 1.000 15.03026 ? 158 THR   A C     1 
ATOM   1276 O  O     . THR   A 1 159 ? 24.37300  34.67200  -15.78100 1.000 16.32327 ? 158 THR   A O     1 
ATOM   1277 C  CB    . THR   A 1 159 ? 22.82800  32.51900  -17.78300 1.000 16.42472 ? 158 THR   A CB    1 
ATOM   1278 O  OG1   . THR   A 1 159 ? 22.90100  32.05600  -19.14900 1.000 20.05779 ? 158 THR   A OG1   1 
ATOM   1279 C  CG2   . THR   A 1 159 ? 21.96200  33.77400  -17.74000 1.000 20.26328 ? 158 THR   A CG2   1 
ATOM   1280 N  N     . LEU   A 1 160 ? 24.14200  32.63100  -14.84900 1.000 15.09703 ? 159 LEU   A N     1 
ATOM   1281 C  CA    . LEU   A 1 160 ? 24.21500  33.18600  -13.50200 1.000 14.46170 ? 159 LEU   A CA    1 
ATOM   1282 C  C     . LEU   A 1 160 ? 25.56800  33.83300  -13.24500 1.000 14.85868 ? 159 LEU   A C     1 
ATOM   1283 O  O     . LEU   A 1 160 ? 25.63900  34.93900  -12.68900 1.000 15.02922 ? 159 LEU   A O     1 
ATOM   1284 C  CB    . LEU   A 1 160 ? 23.94600  32.10000  -12.48100 1.000 13.88029 ? 159 LEU   A CB    1 
ATOM   1285 C  CG    . LEU   A 1 160 ? 23.98200  32.60800  -11.03800 1.000 13.73291 ? 159 LEU   A CG    1 
ATOM   1286 C  CD1   . LEU   A 1 160 ? 22.98000  33.75600  -10.77900 1.000 15.14558 ? 159 LEU   A CD1   1 
ATOM   1287 C  CD2   . LEU   A 1 160 ? 23.68400  31.45300  -10.10500 1.000 14.13610 ? 159 LEU   A CD2   1 
ATOM   1288 N  N     . VAL   A 1 161 ? 26.65300  33.19800  -13.69600 1.000 13.93308 ? 160 VAL   A N     1 
ATOM   1289 C  CA    . VAL   A 1 161 ? 27.96600  33.84600  -13.56000 1.000 15.20739 ? 160 VAL   A CA    1 
ATOM   1290 C  C     . VAL   A 1 161 ? 27.99500  35.18000  -14.30800 1.000 17.84517 ? 160 VAL   A C     1 
ATOM   1291 O  O     . VAL   A 1 161 ? 28.51400  36.18500  -13.80700 1.000 18.07252 ? 160 VAL   A O     1 
ATOM   1292 C  CB    . VAL   A 1 161 ? 29.08600  32.90000  -14.03100 1.000 15.88321 ? 160 VAL   A CB    1 
ATOM   1293 C  CG1   . VAL   A 1 161 ? 30.40600  33.66700  -14.12300 1.000 19.11884 ? 160 VAL   A CG1   1 
ATOM   1294 C  CG2   . VAL   A 1 161 ? 29.23300  31.72500  -13.06200 1.000 18.14849 ? 160 VAL   A CG2   1 
ATOM   1295 N  N     . ARG   A 1 162 ? 27.43700  35.22400  -15.52500 1.000 16.49382 ? 161 ARG   A N     1 
ATOM   1296 C  CA    . ARG   A 1 162 ? 27.39000  36.50200  -16.24500 1.000 16.54680 ? 161 ARG   A CA    1 
ATOM   1297 C  C     . ARG   A 1 162 ? 26.60200  37.55400  -15.48100 1.000 18.54046 ? 161 ARG   A C     1 
ATOM   1298 O  O     . ARG   A 1 162 ? 27.00400  38.72900  -15.44900 1.000 21.40403 ? 161 ARG   A O     1 
ATOM   1299 C  CB    . ARG   A 1 162 ? 26.79700  36.32400  -17.63700 1.000 19.87374 ? 161 ARG   A CB    1 
ATOM   1300 C  CG    . ARG   A 1 162 ? 27.65100  35.45000  -18.53600 1.000 19.49750 ? 161 ARG   A CG    1 
ATOM   1301 C  CD    . ARG   A 1 162 ? 27.14300  35.45100  -19.94700 1.000 24.99890 ? 161 ARG   A CD    1 
ATOM   1302 N  NE    . ARG   A 1 162 ? 27.88500  34.46700  -20.71200 1.000 24.89583 ? 161 ARG   A NE    1 
ATOM   1303 C  CZ    . ARG   A 1 162 ? 27.45100  33.24300  -20.96100 1.000 23.85901 ? 161 ARG   A CZ    1 
ATOM   1304 N  NH1   . ARG   A 1 162 ? 26.21200  32.87900  -20.67300 1.000 23.42413 ? 161 ARG   A NH1   1 
ATOM   1305 N  NH2   . ARG   A 1 162 ? 28.28000  32.36700  -21.50900 1.000 21.80879 ? 161 ARG   A NH2   1 
ATOM   1306 N  N     . GLU   A 1 163 ? 25.49500  37.15700  -14.83900 1.000 18.40500 ? 162 GLU   A N     1 
ATOM   1307 C  CA    . GLU   A 1 163 ? 24.71500  38.08400  -14.01900 1.000 19.40169 ? 162 GLU   A CA    1 
ATOM   1308 C  C     . GLU   A 1 163 ? 25.52200  38.61900  -12.83800 1.000 18.83969 ? 162 GLU   A C     1 
ATOM   1309 O  O     . GLU   A 1 163 ? 25.39400  39.80500  -12.49100 1.000 21.62022 ? 162 GLU   A O     1 
ATOM   1310 C  CB    . GLU   A 1 163 ? 23.41300  37.42800  -13.53800 1.000 19.74672 ? 162 GLU   A CB    1 
ATOM   1311 C  CG    . GLU   A 1 163 ? 22.37000  37.14500  -14.60600 1.000 21.87284 ? 162 GLU   A CG    1 
ATOM   1312 C  CD    . GLU   A 1 163 ? 21.92100  38.38000  -15.30700 1.000 28.34598 ? 162 GLU   A CD    1 
ATOM   1313 O  OE1   . GLU   A 1 163 ? 21.23400  39.19600  -14.66000 1.000 28.56249 ? 162 GLU   A OE1   1 
ATOM   1314 O  OE2   . GLU   A 1 163 ? 22.25300  38.52800  -16.50000 1.000 28.32462 ? 162 GLU   A OE2   1 
ATOM   1315 N  N     . ILE   A 1 164 ? 26.35500  37.77800  -12.21600 1.000 17.11679 ? 163 ILE   A N     1 
ATOM   1316 C  CA    . ILE   A 1 164 ? 27.23700  38.25800  -11.15400 1.000 19.76727 ? 163 ILE   A CA    1 
ATOM   1317 C  C     . ILE   A 1 164 ? 28.28500  39.21600  -11.70500 1.000 24.61942 ? 163 ILE   A C     1 
ATOM   1318 O  O     . ILE   A 1 164 ? 28.50900  40.29500  -11.13700 1.000 25.11529 ? 163 ILE   A O     1 
ATOM   1319 C  CB    . ILE   A 1 164 ? 27.90700  37.09100  -10.42200 1.000 17.27962 ? 163 ILE   A CB    1 
ATOM   1320 C  CG1   . ILE   A 1 164 ? 26.87300  36.23300  -9.68800  1.000 15.20331 ? 163 ILE   A CG1   1 
ATOM   1321 C  CG2   . ILE   A 1 164 ? 28.94200  37.64900  -9.42500  1.000 20.22277 ? 163 ILE   A CG2   1 
ATOM   1322 C  CD1   . ILE   A 1 164 ? 27.47700  34.92400  -9.23300  1.000 17.25630 ? 163 ILE   A CD1   1 
ATOM   1323 N  N     . ARG   A 1 165 ? 28.98400  38.80400  -12.78100 1.000 21.52770 ? 164 ARG   A N     1 
ATOM   1324 C  CA    . ARG   A 1 165 ? 30.01400  39.64000  -13.39500 1.000 24.60980 ? 164 ARG   A CA    1 
ATOM   1325 C  C     . ARG   A 1 165 ? 29.40700  40.97800  -13.82900 1.000 26.19533 ? 164 ARG   A C     1 
ATOM   1326 O  O     . ARG   A 1 165 ? 30.02300  42.03900  -13.64500 1.000 33.00678 ? 164 ARG   A O     1 
ATOM   1327 C  CB    . ARG   A 1 165 ? 30.68600  38.88100  -14.57400 1.000 21.24373 ? 164 ARG   A CB    1 
ATOM   1328 C  CG    . ARG   A 1 165 ? 31.49100  37.59100  -14.24300 1.000 28.60677 ? 164 ARG   A CG    1 
ATOM   1329 C  CD    . ARG   A 1 165 ? 32.08800  36.88200  -15.51900 1.000 24.99723 ? 164 ARG   A CD    1 
ATOM   1330 N  NE    . ARG   A 1 165 ? 32.90400  35.68500  -15.26100 1.000 24.68033 ? 164 ARG   A NE    1 
ATOM   1331 C  CZ    . ARG   A 1 165 ? 33.27900  34.81100  -16.19700 1.000 24.36183 ? 164 ARG   A CZ    1 
ATOM   1332 N  NH1   . ARG   A 1 165 ? 32.87600  34.93600  -17.44800 1.000 22.99475 ? 164 ARG   A NH1   1 
ATOM   1333 N  NH2   . ARG   A 1 165 ? 34.04200  33.75400  -15.85900 1.000 22.73350 ? 164 ARG   A NH2   1 
ATOM   1334 N  N     . LYS   A 1 166 ? 28.17700  40.96400  -14.36200 1.000 27.60522 ? 165 LYS   A N     1 
ATOM   1335 C  CA    . LYS   A 1 166 ? 27.48900  42.20100  -14.74400 1.000 34.71478 ? 165 LYS   A CA    1 
ATOM   1336 C  C     . LYS   A 1 166 ? 27.15500  43.05200  -13.52400 1.000 33.62810 ? 165 LYS   A C     1 
ATOM   1337 O  O     . LYS   A 1 166 ? 27.38400  44.27200  -13.52000 1.000 40.78546 ? 165 LYS   A O     1 
ATOM   1338 C  CB    . LYS   A 1 166 ? 26.20600  41.87700  -15.51000 1.000 39.43425 ? 165 LYS   A CB    1 
ATOM   1339 C  CG    . LYS   A 1 166 ? 26.41600  41.54200  -16.97700 1.000 41.26886 ? 165 LYS   A CG    1 
ATOM   1340 C  CD    . LYS   A 1 166 ? 25.23500  40.73300  -17.52000 1.000 44.92016 ? 165 LYS   A CD    1 
ATOM   1341 C  CE    . LYS   A 1 166 ? 23.94100  41.54700  -17.50300 1.000 47.50082 ? 165 LYS   A CE    1 
ATOM   1342 N  NZ    . LYS   A 1 166 ? 22.79300  40.80900  -18.10000 1.000 46.77125 ? 165 LYS   A NZ    1 
ATOM   1343 N  N     . HIS   A 1 167 ? 26.60800  42.41400  -12.47700 1.000 32.99469 ? 166 HIS   A N     1 
ATOM   1344 C  CA    . HIS   A 1 167 ? 26.18000  43.12700  -11.27600 1.000 34.27553 ? 166 HIS   A CA    1 
ATOM   1345 C  C     . HIS   A 1 167 ? 27.32400  43.90100  -10.66200 1.000 30.42599 ? 166 HIS   A C     1 
ATOM   1346 O  O     . HIS   A 1 167 ? 27.13900  45.03500  -10.20400 1.000 31.78193 ? 166 HIS   A O     1 
ATOM   1347 C  CB    . HIS   A 1 167 ? 25.69000  42.13300  -10.23100 1.000 27.56690 ? 166 HIS   A CB    1 
ATOM   1348 C  CG    . HIS   A 1 167 ? 25.62000  42.70800  -8.85000  1.000 31.00774 ? 166 HIS   A CG    1 
ATOM   1349 N  ND1   . HIS   A 1 167 ? 24.62600  43.57800  -8.45700  1.000 42.39716 ? 166 HIS   A ND1   1 
ATOM   1350 C  CD2   . HIS   A 1 167 ? 26.41400  42.52900  -7.76800  1.000 28.85368 ? 166 HIS   A CD2   1 
ATOM   1351 C  CE1   . HIS   A 1 167 ? 24.81000  43.91100  -7.18900  1.000 40.14446 ? 166 HIS   A CE1   1 
ATOM   1352 N  NE2   . HIS   A 1 167 ? 25.88200  43.27900  -6.74400  1.000 39.85802 ? 166 HIS   A NE2   1 
ATOM   1353 N  N     . LYS   A 1 168 ? 28.49200  43.28200  -10.58400 1.000 27.90268 ? 167 LYS   A N     1 
ATOM   1354 C  CA    . LYS   A 1 168 ? 29.67500  43.95700  -10.07600 1.000 30.70358 ? 167 LYS   A CA    1 
ATOM   1355 C  C     . LYS   A 1 168 ? 30.10300  45.09700  -11.01300 1.000 38.35632 ? 167 LYS   A C     1 
ATOM   1356 O  O     . LYS   A 1 168 ? 29.47200  45.34400  -12.04200 1.000 35.93152 ? 167 LYS   A O     1 
ATOM   1357 C  CB    . LYS   A 1 168 ? 30.83000  42.96000  -9.93000  1.000 29.14308 ? 167 LYS   A CB    1 
ATOM   1358 C  CG    . LYS   A 1 168 ? 30.64500  41.75800  -8.98900  1.000 29.24508 ? 167 LYS   A CG    1 
ATOM   1359 C  CD    . LYS   A 1 168 ? 31.84100  40.85200  -9.26300  1.000 34.56630 ? 167 LYS   A CD    1 
ATOM   1360 C  CE    . LYS   A 1 168 ? 32.14900  39.79300  -8.25400  1.000 33.90622 ? 167 LYS   A CE    1 
ATOM   1361 N  NZ    . LYS   A 1 168 ? 33.55600  39.30400  -8.52900  1.000 31.17989 ? 167 LYS   A NZ    1 
ATOM   1362 N  N     . ASN   B 2 4   ? 3.87200   -0.52600  29.25800  1.000 30.76449 ? 3   ASN   D N     1 
ATOM   1363 C  CA    . ASN   B 2 4   ? 4.58700   -0.11500  28.04800  1.000 27.63880 ? 3   ASN   D CA    1 
ATOM   1364 C  C     . ASN   B 2 4   ? 5.52700   -1.21300  27.53800  1.000 26.76966 ? 3   ASN   D C     1 
ATOM   1365 O  O     . ASN   B 2 4   ? 6.35900   -1.72400  28.31000  1.000 30.27285 ? 3   ASN   D O     1 
ATOM   1366 C  CB    . ASN   B 2 4   ? 5.39700   1.17300   28.27900  1.000 25.38200 ? 3   ASN   D CB    1 
ATOM   1367 C  CG    . ASN   B 2 4   ? 4.52200   2.42400   28.29400  1.000 25.49662 ? 3   ASN   D CG    1 
ATOM   1368 O  OD1   . ASN   B 2 4   ? 3.36400   2.38800   27.89100  1.000 27.96700 ? 3   ASN   D OD1   1 
ATOM   1369 N  ND2   . ASN   B 2 4   ? 5.07600   3.52500   28.76200  1.000 27.09450 ? 3   ASN   D ND2   1 
ATOM   1370 N  N     . PRO   B 2 5   ? 5.37600   -1.59600  26.27300  1.000 23.86149 ? 4   PRO   D N     1 
ATOM   1371 C  CA    . PRO   B 2 5   ? 6.25400   -2.63500  25.71600  1.000 25.39125 ? 4   PRO   D CA    1 
ATOM   1372 C  C     . PRO   B 2 5   ? 7.67800   -2.13400  25.52200  1.000 22.66332 ? 4   PRO   D C     1 
ATOM   1373 O  O     . PRO   B 2 5   ? 7.94500   -0.92800  25.45300  1.000 22.58382 ? 4   PRO   D O     1 
ATOM   1374 C  CB    . PRO   B 2 5   ? 5.59600   -2.97800  24.37600  1.000 29.61428 ? 4   PRO   D CB    1 
ATOM   1375 C  CG    . PRO   B 2 5   ? 4.87200   -1.73900  23.98000  1.000 32.05990 ? 4   PRO   D CG    1 
ATOM   1376 C  CD    . PRO   B 2 5   ? 4.38300   -1.14700  25.27800  1.000 24.88081 ? 4   PRO   D CD    1 
ATOM   1377 N  N     . THR   B 2 6   ? 8.60500   -3.08300  25.42700  1.000 24.29920 ? 5   THR   D N     1 
ATOM   1378 C  CA    . THR   B 2 6   ? 10.01600  -2.79900  25.18500  1.000 20.98337 ? 5   THR   D CA    1 
ATOM   1379 C  C     . THR   B 2 6   ? 10.42400  -3.53100  23.91400  1.000 21.31223 ? 5   THR   D C     1 
ATOM   1380 O  O     . THR   B 2 6   ? 10.15100  -4.72700  23.77400  1.000 23.81115 ? 5   THR   D O     1 
ATOM   1381 C  CB    . THR   B 2 6   ? 10.88300  -3.31600  26.35700  1.000 27.35520 ? 5   THR   D CB    1 
ATOM   1382 O  OG1   . THR   B 2 6   ? 10.54300  -2.65800  27.59500  1.000 30.26730 ? 5   THR   D OG1   1 
ATOM   1383 C  CG2   . THR   B 2 6   ? 12.36600  -3.08100  26.06500  1.000 28.77331 ? 5   THR   D CG2   1 
ATOM   1384 N  N     . VAL   B 2 7   ? 11.10800  -2.84900  23.01000  1.000 21.17282 ? 6   VAL   D N     1 
ATOM   1385 C  CA    . VAL   B 2 7   ? 11.61200  -3.53600  21.83300  1.000 21.80135 ? 6   VAL   D CA    1 
ATOM   1386 C  C     . VAL   B 2 7   ? 13.11300  -3.30600  21.77500  1.000 21.80718 ? 6   VAL   D C     1 
ATOM   1387 O  O     . VAL   B 2 7   ? 13.65600  -2.40500  22.42000  1.000 21.44286 ? 6   VAL   D O     1 
ATOM   1388 C  CB    . VAL   B 2 7   ? 10.90000  -3.06200  20.54900  1.000 23.88404 ? 6   VAL   D CB    1 
ATOM   1389 C  CG1   . VAL   B 2 7   ? 9.40800   -3.40400  20.63900  1.000 26.26279 ? 6   VAL   D CG1   1 
ATOM   1390 C  CG2   . VAL   B 2 7   ? 11.11900  -1.66100  20.39600  1.000 23.89301 ? 6   VAL   D CG2   1 
ATOM   1391 N  N     . PHE   B 2 8   ? 13.80000  -4.16000  21.01600  1.000 22.35365 ? 7   PHE   D N     1 
ATOM   1392 C  CA    . PHE   B 2 8   ? 15.23500  -4.00400  20.85800  1.000 21.22319 ? 7   PHE   D CA    1 
ATOM   1393 C  C     . PHE   B 2 8   ? 15.60900  -3.96500  19.38600  1.000 19.78283 ? 7   PHE   D C     1 
ATOM   1394 O  O     . PHE   B 2 8   ? 14.95600  -4.58900  18.54100  1.000 20.50328 ? 7   PHE   D O     1 
ATOM   1395 C  CB    . PHE   B 2 8   ? 16.02000  -5.13600  21.56000  1.000 24.01940 ? 7   PHE   D CB    1 
ATOM   1396 C  CG    . PHE   B 2 8   ? 15.92700  -6.47100  20.85700  1.000 23.19565 ? 7   PHE   D CG    1 
ATOM   1397 C  CD1   . PHE   B 2 8   ? 14.89400  -7.36100  21.14500  1.000 23.51550 ? 7   PHE   D CD1   1 
ATOM   1398 C  CD2   . PHE   B 2 8   ? 16.84300  -6.82300  19.86500  1.000 22.63836 ? 7   PHE   D CD2   1 
ATOM   1399 C  CE1   . PHE   B 2 8   ? 14.80000  -8.58300  20.49200  1.000 24.55355 ? 7   PHE   D CE1   1 
ATOM   1400 C  CE2   . PHE   B 2 8   ? 16.74900  -8.04200  19.21100  1.000 23.81298 ? 7   PHE   D CE2   1 
ATOM   1401 C  CZ    . PHE   B 2 8   ? 15.73100  -8.90300  19.51300  1.000 23.97576 ? 7   PHE   D CZ    1 
ATOM   1402 N  N     . PHE   B 2 9   ? 16.69400  -3.25100  19.10500  1.000 20.10113 ? 8   PHE   D N     1 
ATOM   1403 C  CA    . PHE   B 2 9   ? 17.42600  -3.33400  17.84100  1.000 18.59220 ? 8   PHE   D CA    1 
ATOM   1404 C  C     . PHE   B 2 9   ? 18.83500  -3.83600  18.14400  1.000 18.74030 ? 8   PHE   D C     1 
ATOM   1405 O  O     . PHE   B 2 9   ? 19.51200  -3.28500  19.03300  1.000 19.48641 ? 8   PHE   D O     1 
ATOM   1406 C  CB    . PHE   B 2 9   ? 17.60800  -1.94600  17.23000  1.000 18.46013 ? 8   PHE   D CB    1 
ATOM   1407 C  CG    . PHE   B 2 9   ? 16.37700  -1.32700  16.64700  1.000 16.75486 ? 8   PHE   D CG    1 
ATOM   1408 C  CD1   . PHE   B 2 9   ? 15.16900  -2.00000  16.55900  1.000 17.72583 ? 8   PHE   D CD1   1 
ATOM   1409 C  CD2   . PHE   B 2 9   ? 16.45300  -0.00800  16.19700  1.000 18.48346 ? 8   PHE   D CD2   1 
ATOM   1410 C  CE1   . PHE   B 2 9   ? 14.04300  -1.34600  15.99200  1.000 15.23729 ? 8   PHE   D CE1   1 
ATOM   1411 C  CE2   . PHE   B 2 9   ? 15.35100  0.64300   15.65300  1.000 18.74987 ? 8   PHE   D CE2   1 
ATOM   1412 C  CZ    . PHE   B 2 9   ? 14.14500  -0.01000  15.55600  1.000 16.48503 ? 8   PHE   D CZ    1 
ATOM   1413 N  N     . ASP   B 2 10  ? 19.29500  -4.85500  17.39500  1.000 18.27565 ? 9   ASP   D N     1 
ATOM   1414 C  CA    . ASP   B 2 10  ? 20.71200  -5.21500  17.38100  1.000 18.18382 ? 9   ASP   D CA    1 
ATOM   1415 C  C     . ASP   B 2 10  ? 21.33100  -4.50400  16.17800  1.000 19.30126 ? 9   ASP   D C     1 
ATOM   1416 O  O     . ASP   B 2 10  ? 20.97800  -4.80200  15.03600  1.000 20.26602 ? 9   ASP   D O     1 
ATOM   1417 C  CB    . ASP   B 2 10  ? 20.88700  -6.73100  17.32600  1.000 20.29179 ? 9   ASP   D CB    1 
ATOM   1418 C  CG    . ASP   B 2 10  ? 20.51800  -7.38200  18.63000  1.000 25.59229 ? 9   ASP   D CG    1 
ATOM   1419 O  OD1   . ASP   B 2 10  ? 20.84300  -6.80300  19.69600  1.000 25.57769 ? 9   ASP   D OD1   1 
ATOM   1420 O  OD2   . ASP   B 2 10  ? 19.90400  -8.46700  18.61200  1.000 30.00167 ? 9   ASP   D OD2   1 
ATOM   1421 N  N     . ILE   B 2 11  ? 22.16700  -3.50900  16.44300  1.000 17.79966 ? 10  ILE   D N     1 
ATOM   1422 C  CA    . ILE   B 2 11  ? 22.74300  -2.65800  15.40700  1.000 16.81518 ? 10  ILE   D CA    1 
ATOM   1423 C  C     . ILE   B 2 11  ? 24.04400  -3.27200  14.89400  1.000 16.06588 ? 10  ILE   D C     1 
ATOM   1424 O  O     . ILE   B 2 11  ? 24.85600  -3.75600  15.68200  1.000 18.94529 ? 10  ILE   D O     1 
ATOM   1425 C  CB    . ILE   B 2 11  ? 23.03100  -1.25700  15.97900  1.000 16.28503 ? 10  ILE   D CB    1 
ATOM   1426 C  CG1   . ILE   B 2 11  ? 21.76800  -0.61600  16.58600  1.000 18.16764 ? 10  ILE   D CG1   1 
ATOM   1427 C  CG2   . ILE   B 2 11  ? 23.64700  -0.33000  14.92600  1.000 18.16437 ? 10  ILE   D CG2   1 
ATOM   1428 C  CD1   . ILE   B 2 11  ? 20.67300  -0.42800  15.60000  1.000 19.54371 ? 10  ILE   D CD1   1 
ATOM   1429 N  N     . ALA   B 2 12  ? 24.26700  -3.22000  13.56700  1.000 17.64117 ? 11  ALA   D N     1 
ATOM   1430 C  CA    . ALA   B 2 12  ? 25.48700  -3.71700  12.94900  1.000 16.00491 ? 11  ALA   D CA    1 
ATOM   1431 C  C     . ALA   B 2 12  ? 26.12300  -2.63100  12.08700  1.000 17.05412 ? 11  ALA   D C     1 
ATOM   1432 O  O     . ALA   B 2 12  ? 25.44200  -1.73700  11.56800  1.000 17.17329 ? 11  ALA   D O     1 
ATOM   1433 C  CB    . ALA   B 2 12  ? 25.19700  -4.93300  12.08400  1.000 18.78481 ? 11  ALA   D CB    1 
ATOM   1434 N  N     . VAL   B 2 13  ? 27.44400  -2.71100  11.96500  1.000 17.86847 ? 12  VAL   D N     1 
ATOM   1435 C  CA    . VAL   B 2 13  ? 28.25900  -1.79800  11.16600  1.000 17.39858 ? 12  VAL   D CA    1 
ATOM   1436 C  C     . VAL   B 2 13  ? 28.90200  -2.68500  10.11000  1.000 19.53769 ? 12  VAL   D C     1 
ATOM   1437 O  O     . VAL   B 2 13  ? 29.72200  -3.54600  10.44600  1.000 19.99953 ? 12  VAL   D O     1 
ATOM   1438 C  CB    . VAL   B 2 13  ? 29.32800  -1.11700  12.03500  1.000 19.22273 ? 12  VAL   D CB    1 
ATOM   1439 C  CG1   . VAL   B 2 13  ? 30.33900  -0.34300  11.15900  1.000 24.79742 ? 12  VAL   D CG1   1 
ATOM   1440 C  CG2   . VAL   B 2 13  ? 28.68800  -0.23700  13.05900  1.000 21.88494 ? 12  VAL   D CG2   1 
ATOM   1441 N  N     . ASP   B 2 14  ? 28.53700  -2.48100  8.83000   1.000 19.71345 ? 13  ASP   D N     1 
ATOM   1442 C  CA    . ASP   B 2 14  ? 28.98700  -3.36500  7.74500   1.000 19.34588 ? 13  ASP   D CA    1 
ATOM   1443 C  C     . ASP   B 2 14  ? 28.81200  -4.84400  8.14600   1.000 20.49452 ? 13  ASP   D C     1 
ATOM   1444 O  O     . ASP   B 2 14  ? 29.66000  -5.69400  7.87500   1.000 22.72218 ? 13  ASP   D O     1 
ATOM   1445 C  CB    . ASP   B 2 14  ? 30.42500  -3.02600  7.29400   1.000 25.28921 ? 13  ASP   D CB    1 
ATOM   1446 C  CG    . ASP   B 2 14  ? 30.51100  -1.73400  6.46700   1.000 27.05408 ? 13  ASP   D CG    1 
ATOM   1447 O  OD1   . ASP   B 2 14  ? 29.49600  -1.23100  5.92800   1.000 24.98242 ? 13  ASP   D OD1   1 
ATOM   1448 O  OD2   . ASP   B 2 14  ? 31.64100  -1.22800  6.32000   1.000 30.33156 ? 13  ASP   D OD2   1 
ATOM   1449 N  N     . GLY   B 2 15  ? 27.69100  -5.14000  8.80300   1.000 22.24361 ? 14  GLY   D N     1 
ATOM   1450 C  CA    . GLY   B 2 15  ? 27.33700  -6.48000  9.21400   1.000 19.94779 ? 14  GLY   D CA    1 
ATOM   1451 C  C     . GLY   B 2 15  ? 27.92900  -6.93800  10.53800  1.000 22.79035 ? 14  GLY   D C     1 
ATOM   1452 O  O     . GLY   B 2 15  ? 27.53700  -8.00000  11.03900  1.000 25.03437 ? 14  GLY   D O     1 
ATOM   1453 N  N     . GLU   B 2 16  ? 28.85900  -6.18500  11.11200  1.000 19.63027 ? 15  GLU   D N     1 
ATOM   1454 C  CA    . GLU   B 2 16  ? 29.47500  -6.58100  12.37500  1.000 20.96806 ? 15  GLU   D CA    1 
ATOM   1455 C  C     . GLU   B 2 16  ? 28.65400  -6.04400  13.54000  1.000 19.71778 ? 15  GLU   D C     1 
ATOM   1456 O  O     . GLU   B 2 16  ? 28.30300  -4.85800  13.54900  1.000 18.52178 ? 15  GLU   D O     1 
ATOM   1457 C  CB    . GLU   B 2 16  ? 30.87100  -5.99000  12.48700  1.000 21.58968 ? 15  GLU   D CB    1 
ATOM   1458 C  CG    . GLU   B 2 16  ? 31.89100  -6.79700  11.77700  1.000 24.89419 ? 15  GLU   D CG    1 
ATOM   1459 C  CD    . GLU   B 2 16  ? 31.98500  -8.26800  12.27800  1.000 27.70617 ? 15  GLU   D CD    1 
ATOM   1460 O  OE1   . GLU   B 2 16  ? 31.76100  -8.59000  13.47000  1.000 27.59590 ? 15  GLU   D OE1   1 
ATOM   1461 O  OE2   . GLU   B 2 16  ? 32.25900  -9.11400  11.44000  1.000 29.46819 ? 15  GLU   D OE2   1 
ATOM   1462 N  N     . PRO   B 2 17  ? 28.35000  -6.85600  14.54500  1.000 20.45909 ? 16  PRO   D N     1 
ATOM   1463 C  CA    . PRO   B 2 17  ? 27.54400  -6.38400  15.67100  1.000 22.48713 ? 16  PRO   D CA    1 
ATOM   1464 C  C     . PRO   B 2 17  ? 28.23100  -5.23200  16.37700  1.000 21.60566 ? 16  PRO   D C     1 
ATOM   1465 O  O     . PRO   B 2 17  ? 29.42800  -5.29600  16.69000  1.000 24.78838 ? 16  PRO   D O     1 
ATOM   1466 C  CB    . PRO   B 2 17  ? 27.45200  -7.61100  16.57800  1.000 24.55223 ? 16  PRO   D CB    1 
ATOM   1467 C  CG    . PRO   B 2 17  ? 27.74800  -8.75500  15.72600  1.000 26.88129 ? 16  PRO   D CG    1 
ATOM   1468 C  CD    . PRO   B 2 17  ? 28.62500  -8.29600  14.61300  1.000 22.84836 ? 16  PRO   D CD    1 
ATOM   1469 N  N     . LEU   B 2 18  ? 27.46200  -4.17400  16.60400  1.000 21.72132 ? 17  LEU   D N     1 
ATOM   1470 C  CA    . LEU   B 2 18  ? 27.88700  -3.00500  17.35300  1.000 21.99938 ? 17  LEU   D CA    1 
ATOM   1471 C  C     . LEU   B 2 18  ? 27.34900  -3.06800  18.76400  1.000 22.61573 ? 17  LEU   D C     1 
ATOM   1472 O  O     . LEU   B 2 18  ? 28.11200  -2.96800  19.72400  1.000 25.96210 ? 17  LEU   D O     1 
ATOM   1473 C  CB    . LEU   B 2 18  ? 27.41000  -1.72600  16.66200  1.000 22.72319 ? 17  LEU   D CB    1 
ATOM   1474 C  CG    . LEU   B 2 18  ? 27.80900  -0.38600  17.28600  1.000 22.18886 ? 17  LEU   D CG    1 
ATOM   1475 C  CD1   . LEU   B 2 18  ? 29.32700  -0.26300  17.25800  1.000 25.69943 ? 17  LEU   D CD1   1 
ATOM   1476 C  CD2   . LEU   B 2 18  ? 27.11100  0.78400   16.58600  1.000 23.70464 ? 17  LEU   D CD2   1 
ATOM   1477 N  N     . GLY   B 2 19  ? 26.05900  -3.31000  18.89200  1.000 20.87894 ? 18  GLY   D N     1 
ATOM   1478 C  CA    . GLY   B 2 19  ? 25.48000  -3.42600  20.21200  1.000 24.82684 ? 18  GLY   D CA    1 
ATOM   1479 C  C     . GLY   B 2 19  ? 23.97800  -3.38400  20.11900  1.000 21.57836 ? 18  GLY   D C     1 
ATOM   1480 O  O     . GLY   B 2 19  ? 23.40300  -3.21400  19.04400  1.000 22.09392 ? 18  GLY   D O     1 
ATOM   1481 N  N     . ARG   B 2 20  ? 23.34800  -3.53300  21.27800  1.000 20.15693 ? 19  ARG   D N     1 
ATOM   1482 C  CA    . ARG   B 2 20  ? 21.89200  -3.55200  21.35500  1.000 19.49960 ? 19  ARG   D CA    1 
ATOM   1483 C  C     . ARG   B 2 20  ? 21.35800  -2.24400  21.93900  1.000 21.16095 ? 19  ARG   D C     1 
ATOM   1484 O  O     . ARG   B 2 20  ? 21.87300  -1.74400  22.94200  1.000 23.50499 ? 19  ARG   D O     1 
ATOM   1485 C  CB    . ARG   B 2 20  ? 21.41200  -4.73700  22.20600  1.000 21.88245 ? 19  ARG   D CB    1 
ATOM   1486 C  CG    . ARG   B 2 20  ? 19.88900  -4.67900  22.39900  1.000 21.20026 ? 19  ARG   D CG    1 
ATOM   1487 C  CD    . ARG   B 2 20  ? 19.37400  -5.95600  23.07300  1.000 24.78922 ? 19  ARG   D CD    1 
ATOM   1488 N  NE    . ARG   B 2 20  ? 19.48700  -7.09800  22.17300  1.000 24.00620 ? 19  ARG   D NE    1 
ATOM   1489 C  CZ    . ARG   B 2 20  ? 18.89000  -8.26900  22.35500  1.000 25.64884 ? 19  ARG   D CZ    1 
ATOM   1490 N  NH1   . ARG   B 2 20  ? 18.19300  -8.53100  23.44300  1.000 27.26899 ? 19  ARG   D NH1   1 
ATOM   1491 N  NH2   . ARG   B 2 20  ? 18.99900  -9.20000  21.41900  1.000 27.38487 ? 19  ARG   D NH2   1 
ATOM   1492 N  N     . VAL   B 2 21  ? 20.31700  -1.71500  21.31300  1.000 18.63017 ? 20  VAL   D N     1 
ATOM   1493 C  CA    . VAL   B 2 21  ? 19.55800  -0.57900  21.84000  1.000 18.84642 ? 20  VAL   D CA    1 
ATOM   1494 C  C     . VAL   B 2 21  ? 18.16300  -1.08800  22.17000  1.000 20.06115 ? 20  VAL   D C     1 
ATOM   1495 O  O     . VAL   B 2 21  ? 17.52600  -1.73600  21.33800  1.000 21.23550 ? 20  VAL   D O     1 
ATOM   1496 C  CB    . VAL   B 2 21  ? 19.48600  0.57900   20.82600  1.000 19.11923 ? 20  VAL   D CB    1 
ATOM   1497 C  CG1   . VAL   B 2 21  ? 18.74800  1.78500   21.44100  1.000 20.87636 ? 20  VAL   D CG1   1 
ATOM   1498 C  CG2   . VAL   B 2 21  ? 20.87200  0.98000   20.39600  1.000 19.54544 ? 20  VAL   D CG2   1 
ATOM   1499 N  N     . SER   B 2 22  ? 17.65700  -0.76500  23.36300  1.000 19.21904 ? 21  SER   D N     1 
ATOM   1500 C  CA    . SER   B 2 22  ? 16.28000  -1.11600  23.66000  1.000 19.38718 ? 21  SER   D CA    1 
ATOM   1501 C  C     . SER   B 2 22  ? 15.49400  0.15900   23.92000  1.000 20.77064 ? 21  SER   D C     1 
ATOM   1502 O  O     . SER   B 2 22  ? 16.06000  1.18300   24.32800  1.000 18.34698 ? 21  SER   D O     1 
ATOM   1503 C  CB    . SER   B 2 22  ? 16.14000  -2.05500  24.85600  1.000 23.24493 ? 21  SER   D CB    1 
ATOM   1504 O  OG    . SER   B 2 22  ? 16.50600  -1.41000  26.05600  1.000 25.79096 ? 21  SER   D OG    1 
ATOM   1505 N  N     . PHE   B 2 23  ? 14.18900  0.09500   23.65200  1.000 17.95950 ? 22  PHE   D N     1 
ATOM   1506 C  CA    . PHE   B 2 23  ? 13.32800  1.26600   23.73400  1.000 17.20011 ? 22  PHE   D CA    1 
ATOM   1507 C  C     . PHE   B 2 23  ? 12.09200  0.92700   24.53200  1.000 19.15915 ? 22  PHE   D C     1 
ATOM   1508 O  O     . PHE   B 2 23  ? 11.51400  -0.14500  24.34200  1.000 21.75936 ? 22  PHE   D O     1 
ATOM   1509 C  CB    . PHE   B 2 23  ? 12.79300  1.64300   22.35400  1.000 17.52697 ? 22  PHE   D CB    1 
ATOM   1510 C  CG    . PHE   B 2 23  ? 13.86500  1.82800   21.28900  1.000 15.43990 ? 22  PHE   D CG    1 
ATOM   1511 C  CD1   . PHE   B 2 23  ? 14.53700  3.05100   21.15600  1.000 16.99430 ? 22  PHE   D CD1   1 
ATOM   1512 C  CD2   . PHE   B 2 23  ? 14.19500  0.79600   20.42400  1.000 17.94094 ? 22  PHE   D CD2   1 
ATOM   1513 C  CE1   . PHE   B 2 23  ? 15.51700  3.23400   20.18100  1.000 17.69736 ? 22  PHE   D CE1   1 
ATOM   1514 C  CE2   . PHE   B 2 23  ? 15.15300  0.98300   19.43700  1.000 19.67604 ? 22  PHE   D CE2   1 
ATOM   1515 C  CZ    . PHE   B 2 23  ? 15.80400  2.20100   19.33300  1.000 17.89438 ? 22  PHE   D CZ    1 
ATOM   1516 N  N     . GLU   B 2 24  ? 11.67700  1.85600   25.40000  1.000 19.20247 ? 23  GLU   D N     1 
ATOM   1517 C  CA    . GLU   B 2 24  ? 10.33700  1.80400   25.97400  1.000 19.05903 ? 23  GLU   D CA    1 
ATOM   1518 C  C     . GLU   B 2 24  ? 9.42100   2.50100   24.98100  1.000 18.14231 ? 23  GLU   D C     1 
ATOM   1519 O  O     . GLU   B 2 24  ? 9.73700   3.59000   24.51600  1.000 18.83710 ? 23  GLU   D O     1 
ATOM   1520 C  CB    . GLU   B 2 24  ? 10.29200  2.56400   27.29800  1.000 23.49028 ? 23  GLU   D CB    1 
ATOM   1521 C  CG    . GLU   B 2 24  ? 8.86300   2.71300   27.85500  1.000 20.69267 ? 23  GLU   D CG    1 
ATOM   1522 C  CD    . GLU   B 2 24  ? 8.77300   3.44400   29.18200  1.000 32.77295 ? 23  GLU   D CD    1 
ATOM   1523 O  OE1   . GLU   B 2 24  ? 9.81500   3.88200   29.69300  1.000 31.57292 ? 23  GLU   D OE1   1 
ATOM   1524 O  OE2   . GLU   B 2 24  ? 7.64700   3.54600   29.72400  1.000 31.63382 ? 23  GLU   D OE2   1 
ATOM   1525 N  N     . LEU   B 2 25  ? 8.29300   1.88800   24.65600  1.000 18.02642 ? 24  LEU   D N     1 
ATOM   1526 C  CA    . LEU   B 2 25  ? 7.32400   2.49500   23.74800  1.000 19.14483 ? 24  LEU   D CA    1 
ATOM   1527 C  C     . LEU   B 2 25  ? 6.11800   2.96200   24.55200  1.000 17.57217 ? 24  LEU   D C     1 
ATOM   1528 O  O     . LEU   B 2 25  ? 5.52900   2.17300   25.31600  1.000 20.16792 ? 24  LEU   D O     1 
ATOM   1529 C  CB    . LEU   B 2 25  ? 6.86100   1.50500   22.68200  1.000 19.22096 ? 24  LEU   D CB    1 
ATOM   1530 C  CG    . LEU   B 2 25  ? 7.95800   0.81600   21.87300  1.000 19.03417 ? 24  LEU   D CG    1 
ATOM   1531 C  CD1   . LEU   B 2 25  ? 7.34800   -0.14800  20.82900  1.000 20.04141 ? 24  LEU   D CD1   1 
ATOM   1532 C  CD2   . LEU   B 2 25  ? 8.90100   1.84900   21.21100  1.000 19.41065 ? 24  LEU   D CD2   1 
ATOM   1533 N  N     . PHE   B 2 26  ? 5.74500   4.23500   24.37600  1.000 18.06682 ? 25  PHE   D N     1 
ATOM   1534 C  CA    . PHE   B 2 26  ? 4.71100   4.84900   25.20500  1.000 20.73732 ? 25  PHE   D CA    1 
ATOM   1535 C  C     . PHE   B 2 26  ? 3.31700   4.47700   24.70900  1.000 21.34081 ? 25  PHE   D C     1 
ATOM   1536 O  O     . PHE   B 2 26  ? 2.52400   5.32500   24.29200  1.000 20.89153 ? 25  PHE   D O     1 
ATOM   1537 C  CB    . PHE   B 2 26  ? 4.92300   6.34900   25.26000  1.000 20.70459 ? 25  PHE   D CB    1 
ATOM   1538 C  CG    . PHE   B 2 26  ? 6.29700   6.75900   25.69100  1.000 19.47132 ? 25  PHE   D CG    1 
ATOM   1539 C  CD1   . PHE   B 2 26  ? 6.99500   6.10900   26.68500  1.000 26.22733 ? 25  PHE   D CD1   1 
ATOM   1540 C  CD2   . PHE   B 2 26  ? 6.87800   7.82300   25.07500  1.000 21.69258 ? 25  PHE   D CD2   1 
ATOM   1541 C  CE1   . PHE   B 2 26  ? 8.27300   6.55700   27.04400  1.000 24.02102 ? 25  PHE   D CE1   1 
ATOM   1542 C  CE2   . PHE   B 2 26  ? 8.13100   8.28600   25.45100  1.000 25.02539 ? 25  PHE   D CE2   1 
ATOM   1543 C  CZ    . PHE   B 2 26  ? 8.81300   7.64900   26.43000  1.000 22.92466 ? 25  PHE   D CZ    1 
ATOM   1544 N  N     . ALA   B 2 27  ? 3.00900   3.17800   24.84100  1.000 20.57822 ? 26  ALA   D N     1 
ATOM   1545 C  CA    . ALA   B 2 27  ? 1.68400   2.67900   24.50600  1.000 21.64799 ? 26  ALA   D CA    1 
ATOM   1546 C  C     . ALA   B 2 27  ? 0.61500   3.32400   25.37400  1.000 25.06155 ? 26  ALA   D C     1 
ATOM   1547 O  O     . ALA   B 2 27  ? -0.51800  3.46800   24.91900  1.000 25.20849 ? 26  ALA   D O     1 
ATOM   1548 C  CB    . ALA   B 2 27  ? 1.62300   1.15100   24.62500  1.000 23.91765 ? 26  ALA   D CB    1 
ATOM   1549 N  N     . ASP   B 2 28  ? 0.97700   3.76500   26.58900  1.000 21.67198 ? 27  ASP   D N     1 
ATOM   1550 C  CA    . ASP   B 2 28  ? 0.02100   4.40000   27.49700  1.000 23.23003 ? 27  ASP   D CA    1 
ATOM   1551 C  C     . ASP   B 2 28  ? -0.48700  5.72500   26.96400  1.000 25.89393 ? 27  ASP   D C     1 
ATOM   1552 O  O     . ASP   B 2 28  ? -1.63000  6.11000   27.25400  1.000 30.03149 ? 27  ASP   D O     1 
ATOM   1553 C  CB    . ASP   B 2 28  ? 0.61800   4.55100   28.90100  1.000 28.41262 ? 27  ASP   D CB    1 
ATOM   1554 C  CG    . ASP   B 2 28  ? 2.02100   5.19200   28.92600  1.000 29.86700 ? 27  ASP   D CG    1 
ATOM   1555 O  OD1   . ASP   B 2 28  ? 2.58000   5.62300   27.88100  1.000 28.03876 ? 27  ASP   D OD1   1 
ATOM   1556 O  OD2   . ASP   B 2 28  ? 2.56800   5.23700   30.05900  1.000 36.86248 ? 27  ASP   D OD2   1 
ATOM   1557 N  N     . LYS   B 2 29  ? 0.34000   6.44900   26.21300  1.000 24.72830 ? 28  LYS   D N     1 
ATOM   1558 C  CA    . LYS   B 2 29  ? -0.01400  7.77300   25.72500  1.000 27.64109 ? 28  LYS   D CA    1 
ATOM   1559 C  C     . LYS   B 2 29  ? -0.18400  7.82400   24.22200  1.000 23.55442 ? 28  LYS   D C     1 
ATOM   1560 O  O     . LYS   B 2 29  ? -0.97000  8.62800   23.71900  1.000 23.14036 ? 28  LYS   D O     1 
ATOM   1561 C  CB    . LYS   B 2 29  ? 1.07000   8.79100   26.10600  1.000 28.30977 ? 28  LYS   D CB    1 
ATOM   1562 C  CG    . LYS   B 2 29  ? 1.05200   9.18800   27.55900  1.000 36.22315 ? 28  LYS   D CG    1 
ATOM   1563 C  CD    . LYS   B 2 29  ? -0.28000  9.81600   27.94600  1.000 39.78050 ? 28  LYS   D CD    1 
ATOM   1564 C  CE    . LYS   B 2 29  ? -0.64600  9.44600   29.35800  1.000 43.96732 ? 28  LYS   D CE    1 
ATOM   1565 N  NZ    . LYS   B 2 29  ? -1.99200  9.93600   29.73800  1.000 45.78661 ? 28  LYS   D NZ    1 
ATOM   1566 N  N     . VAL   B 2 30  ? 0.51400   6.96600   23.49500  1.000 21.91523 ? 29  VAL   D N     1 
ATOM   1567 C  CA    . VAL   B 2 30  ? 0.50800   7.02600   22.03600  1.000 21.03646 ? 29  VAL   D CA    1 
ATOM   1568 C  C     . VAL   B 2 30  ? 0.26500   5.61800   21.49700  1.000 19.62619 ? 29  VAL   D C     1 
ATOM   1569 O  O     . VAL   B 2 30  ? 1.14900   5.05600   20.83600  1.000 20.78807 ? 29  VAL   D O     1 
ATOM   1570 C  CB    . VAL   B 2 30  ? 1.79700   7.67600   21.49800  1.000 23.80709 ? 29  VAL   D CB    1 
ATOM   1571 C  CG1   . VAL   B 2 30  ? 1.43700   8.54500   20.35600  1.000 26.63189 ? 29  VAL   D CG1   1 
ATOM   1572 C  CG2   . VAL   B 2 30  ? 2.48800   8.55000   22.59500  1.000 27.13238 ? 29  VAL   D CG2   1 
ATOM   1573 N  N     . PRO   B 2 31  ? -0.90000  4.99800   21.75300  1.000 21.18005 ? 30  PRO   D N     1 
ATOM   1574 C  CA    . PRO   B 2 31  ? -1.04300  3.54900   21.45900  1.000 21.90343 ? 30  PRO   D CA    1 
ATOM   1575 C  C     . PRO   B 2 31  ? -0.92900  3.14800   19.99100  1.000 24.32849 ? 30  PRO   D C     1 
ATOM   1576 O  O     . PRO   B 2 31  ? -0.33800  2.09800   19.69100  1.000 23.07361 ? 30  PRO   D O     1 
ATOM   1577 C  CB    . PRO   B 2 31  ? -2.42300  3.19300   22.05300  1.000 25.22781 ? 30  PRO   D CB    1 
ATOM   1578 C  CG    . PRO   B 2 31  ? -3.11300  4.52100   22.19500  1.000 23.86788 ? 30  PRO   D CG    1 
ATOM   1579 C  CD    . PRO   B 2 31  ? -2.04500  5.47700   22.56200  1.000 21.34421 ? 30  PRO   D CD    1 
ATOM   1580 N  N     . LYS   B 2 32  ? -1.52100  3.90800   19.06800  1.000 22.84232 ? 31  LYS   D N     1 
ATOM   1581 C  CA    . LYS   B 2 32  ? -1.48000  3.53200   17.65300  1.000 22.43356 ? 31  LYS   D CA    1 
ATOM   1582 C  C     . LYS   B 2 32  ? -0.06800  3.62400   17.09100  1.000 21.46124 ? 31  LYS   D C     1 
ATOM   1583 O  O     . LYS   B 2 32  ? 0.36200   2.77400   16.28900  1.000 21.69991 ? 31  LYS   D O     1 
ATOM   1584 C  CB    . LYS   B 2 32  ? -2.41000  4.45200   16.86800  1.000 24.73393 ? 31  LYS   D CB    1 
ATOM   1585 C  CG    . LYS   B 2 32  ? -2.75500  3.98700   15.46900  1.000 32.04970 ? 31  LYS   D CG    1 
ATOM   1586 C  CD    . LYS   B 2 32  ? -3.84600  4.88800   14.87700  1.000 32.13821 ? 31  LYS   D CD    1 
ATOM   1587 C  CE    . LYS   B 2 32  ? -3.80900  4.96600   13.34700  1.000 38.60589 ? 31  LYS   D CE    1 
ATOM   1588 N  NZ    . LYS   B 2 32  ? -4.48200  6.24400   12.89800  1.000 36.34126 ? 31  LYS   D NZ    1 
ATOM   1589 N  N     . THR   B 2 33  ? 0.65800   4.66100   17.48300  1.000 18.84243 ? 32  THR   D N     1 
ATOM   1590 C  CA    . THR   B 2 33  ? 2.01500   4.86100   16.99500  1.000 18.02446 ? 32  THR   D CA    1 
ATOM   1591 C  C     . THR   B 2 33  ? 2.97400   3.85200   17.61400  1.000 19.03399 ? 32  THR   D C     1 
ATOM   1592 O  O     . THR   B 2 33  ? 3.84200   3.30600   16.91900  1.000 17.87835 ? 32  THR   D O     1 
ATOM   1593 C  CB    . THR   B 2 33  ? 2.44400   6.28900   17.31200  1.000 18.08679 ? 32  THR   D CB    1 
ATOM   1594 O  OG1   . THR   B 2 33  ? 1.46700   7.18700   16.78700  1.000 19.29090 ? 32  THR   D OG1   1 
ATOM   1595 C  CG2   . THR   B 2 33  ? 3.77900   6.60300   16.63800  1.000 17.31703 ? 32  THR   D CG2   1 
ATOM   1596 N  N     . ALA   B 2 34  ? 2.81200   3.59500   18.91400  1.000 18.75542 ? 33  ALA   D N     1 
ATOM   1597 C  CA    . ALA   B 2 34  ? 3.62000   2.58900   19.60200  1.000 18.79028 ? 33  ALA   D CA    1 
ATOM   1598 C  C     . ALA   B 2 34  ? 3.37700   1.21300   19.01200  1.000 20.61578 ? 33  ALA   D C     1 
ATOM   1599 O  O     . ALA   B 2 34  ? 4.32800   0.46300   18.77800  1.000 20.50852 ? 33  ALA   D O     1 
ATOM   1600 C  CB    . ALA   B 2 34  ? 3.29100   2.60000   21.10600  1.000 20.47873 ? 33  ALA   D CB    1 
ATOM   1601 N  N     . GLU   B 2 35  ? 2.11900   0.87900   18.72700  1.000 21.81117 ? 34  GLU   D N     1 
ATOM   1602 C  CA    . GLU   B 2 35  ? 1.82900   -0.44700  18.19200  1.000 22.14197 ? 34  GLU   D CA    1 
ATOM   1603 C  C     . GLU   B 2 35  ? 2.43100   -0.62500  16.80500  1.000 25.02782 ? 34  GLU   D C     1 
ATOM   1604 O  O     . GLU   B 2 35  ? 2.88900   -1.71800  16.46300  1.000 21.49450 ? 34  GLU   D O     1 
ATOM   1605 C  CB    . GLU   B 2 35  ? 0.31900   -0.69900  18.17500  1.000 22.98421 ? 34  GLU   D CB    1 
ATOM   1606 C  CG    . GLU   B 2 35  ? -0.11600  -1.97100  17.44100  1.000 24.50716 ? 34  GLU   D CG    1 
ATOM   1607 C  CD    . GLU   B 2 35  ? 0.38200   -3.26000  18.09800  1.000 30.21578 ? 34  GLU   D CD    1 
ATOM   1608 O  OE1   . GLU   B 2 35  ? 0.90700   -3.21200  19.22900  1.000 31.42519 ? 34  GLU   D OE1   1 
ATOM   1609 O  OE2   . GLU   B 2 35  ? 0.24200   -4.33200  17.47600  1.000 36.09074 ? 34  GLU   D OE2   1 
ATOM   1610 N  N     . ASN   B 2 36  ? 2.43900   0.43100   15.99100  1.000 19.68520 ? 35  ASN   D N     1 
ATOM   1611 C  CA    . ASN   B 2 36  ? 3.05600   0.33500   14.66800  1.000 20.57414 ? 35  ASN   D CA    1 
ATOM   1612 C  C     . ASN   B 2 36  ? 4.52100   -0.02700  14.79200  1.000 18.73487 ? 35  ASN   D C     1 
ATOM   1613 O  O     . ASN   B 2 36  ? 4.98900   -0.98400  14.17200  1.000 18.60858 ? 35  ASN   D O     1 
ATOM   1614 C  CB    . ASN   B 2 36  ? 2.84700   1.65600   13.92000  1.000 18.61150 ? 35  ASN   D CB    1 
ATOM   1615 C  CG    . ASN   B 2 36  ? 3.49100   1.69100   12.54900  1.000 18.21416 ? 35  ASN   D CG    1 
ATOM   1616 O  OD1   . ASN   B 2 36  ? 3.14200   0.92300   11.65300  1.000 20.14857 ? 35  ASN   D OD1   1 
ATOM   1617 N  ND2   . ASN   B 2 36  ? 4.41400   2.62100   12.37300  1.000 18.66019 ? 35  ASN   D ND2   1 
ATOM   1618 N  N     . PHE   B 2 37  ? 5.25300   0.70800   15.62200  1.000 18.84330 ? 36  PHE   D N     1 
ATOM   1619 C  CA    . PHE   B 2 37  ? 6.68200   0.45200   15.78700  1.000 16.02244 ? 36  PHE   D CA    1 
ATOM   1620 C  C     . PHE   B 2 37  ? 6.93100   -0.92500  16.40000  1.000 17.17111 ? 36  PHE   D C     1 
ATOM   1621 O  O     . PHE   B 2 37  ? 7.84700   -1.63300  15.97600  1.000 18.06146 ? 36  PHE   D O     1 
ATOM   1622 C  CB    . PHE   B 2 37  ? 7.28200   1.57300   16.64700  1.000 18.20841 ? 36  PHE   D CB    1 
ATOM   1623 C  CG    . PHE   B 2 37  ? 8.81100   1.58400   16.70900  1.000 15.75739 ? 36  PHE   D CG    1 
ATOM   1624 C  CD1   . PHE   B 2 37  ? 9.47400   0.86200   17.69000  1.000 17.90938 ? 36  PHE   D CD1   1 
ATOM   1625 C  CD2   . PHE   B 2 37  ? 9.58800   2.31500   15.79000  1.000 16.71084 ? 36  PHE   D CD2   1 
ATOM   1626 C  CE1   . PHE   B 2 37  ? 10.87500  0.90100   17.76400  1.000 15.85284 ? 36  PHE   D CE1   1 
ATOM   1627 C  CE2   . PHE   B 2 37  ? 10.98200  2.32200   15.88400  1.000 17.15581 ? 36  PHE   D CE2   1 
ATOM   1628 C  CZ    . PHE   B 2 37  ? 11.61400  1.63100   16.86600  1.000 16.37650 ? 36  PHE   D CZ    1 
ATOM   1629 N  N     . ARG   B 2 38  ? 6.11800   -1.32900  17.38500  1.000 19.09037 ? 37  ARG   D N     1 
ATOM   1630 C  CA    . ARG   B 2 38  ? 6.28200   -2.64500  17.98100  1.000 18.41266 ? 37  ARG   D CA    1 
ATOM   1631 C  C     . ARG   B 2 38  ? 6.13200   -3.73000  16.92700  1.000 20.50923 ? 37  ARG   D C     1 
ATOM   1632 O  O     . ARG   B 2 38  ? 6.97400   -4.62900  16.82700  1.000 21.43588 ? 37  ARG   D O     1 
ATOM   1633 C  CB    . ARG   B 2 38  ? 5.23100   -2.83800  19.07600  1.000 21.02419 ? 37  ARG   D CB    1 
ATOM   1634 C  CG    . ARG   B 2 38  ? 5.44100   -4.09900  19.91900  1.000 22.25677 ? 37  ARG   D CG    1 
ATOM   1635 C  CD    . ARG   B 2 38  ? 4.18500   -4.50200  20.64500  1.000 23.08565 ? 37  ARG   D CD    1 
ATOM   1636 N  NE    . ARG   B 2 38  ? 3.15000   -4.88400  19.68900  1.000 25.09936 ? 37  ARG   D NE    1 
ATOM   1637 C  CZ    . ARG   B 2 38  ? 3.14000   -5.99500  18.96600  1.000 25.33546 ? 37  ARG   D CZ    1 
ATOM   1638 N  NH1   . ARG   B 2 38  ? 4.05800   -6.94000  19.12100  1.000 28.40885 ? 37  ARG   D NH1   1 
ATOM   1639 N  NH2   . ARG   B 2 38  ? 2.16900   -6.17600  18.08000  1.000 28.88954 ? 37  ARG   D NH2   1 
ATOM   1640 N  N     . ALA   B 2 39  ? 5.04700   -3.67500  16.14600  1.000 20.85387 ? 38  ALA   D N     1 
ATOM   1641 C  CA    . ALA   B 2 39  ? 4.79800   -4.71000  15.14000  1.000 21.03628 ? 38  ALA   D CA    1 
ATOM   1642 C  C     . ALA   B 2 39  ? 5.85200   -4.70800  14.03400  1.000 19.67691 ? 38  ALA   D C     1 
ATOM   1643 O  O     . ALA   B 2 39  ? 6.23700   -5.77400  13.53700  1.000 22.88925 ? 38  ALA   D O     1 
ATOM   1644 C  CB    . ALA   B 2 39  ? 3.39700   -4.55000  14.55300  1.000 24.68782 ? 38  ALA   D CB    1 
ATOM   1645 N  N     . LEU   B 2 40  ? 6.29400   -3.52100  13.58300  1.000 20.29473 ? 39  LEU   D N     1 
ATOM   1646 C  CA    . LEU   B 2 40  ? 7.38300   -3.46400  12.58600  1.000 19.36469 ? 39  LEU   D CA    1 
ATOM   1647 C  C     . LEU   B 2 40  ? 8.67000   -4.07600  13.13700  1.000 23.53012 ? 39  LEU   D C     1 
ATOM   1648 O  O     . LEU   B 2 40  ? 9.48600   -4.61600  12.37500  1.000 21.97577 ? 39  LEU   D O     1 
ATOM   1649 C  CB    . LEU   B 2 40  ? 7.61200   -2.00900  12.11900  1.000 21.01414 ? 39  LEU   D CB    1 
ATOM   1650 C  CG    . LEU   B 2 40  ? 6.41100   -1.47900  11.32600  1.000 20.02947 ? 39  LEU   D CG    1 
ATOM   1651 C  CD1   . LEU   B 2 40  ? 6.64700   -0.02600  11.04900  1.000 18.71406 ? 39  LEU   D CD1   1 
ATOM   1652 C  CD2   . LEU   B 2 40  ? 6.20600   -2.23200  10.02100  1.000 21.79060 ? 39  LEU   D CD2   1 
ATOM   1653 N  N     . SER   B 2 41  ? 8.85600   -4.02200  14.45300  1.000 19.70562 ? 40  SER   D N     1 
ATOM   1654 C  CA    . SER   B 2 41  ? 10.05600  -4.55100  15.07900  1.000 20.81041 ? 40  SER   D CA    1 
ATOM   1655 C  C     . SER   B 2 41  ? 10.01700  -6.06000  15.23400  1.000 19.89065 ? 40  SER   D C     1 
ATOM   1656 O  O     . SER   B 2 41  ? 11.06400  -6.70500  15.13400  1.000 22.56296 ? 40  SER   D O     1 
ATOM   1657 C  CB    . SER   B 2 41  ? 10.26200  -3.89600  16.45000  1.000 19.09014 ? 40  SER   D CB    1 
ATOM   1658 O  OG    . SER   B 2 41  ? 10.56300  -2.53000  16.35600  1.000 21.07144 ? 40  SER   D OG    1 
ATOM   1659 N  N     . THR   B 2 42  ? 8.84500   -6.64800  15.48700  1.000 22.79178 ? 41  THR   D N     1 
ATOM   1660 C  CA    . THR   B 2 42  ? 8.77400   -8.10200  15.53400  1.000 22.79984 ? 41  THR   D CA    1 
ATOM   1661 C  C     . THR   B 2 42  ? 8.66500   -8.71200  14.14800  1.000 24.44920 ? 41  THR   D C     1 
ATOM   1662 O  O     . THR   B 2 42  ? 8.88100   -9.91900  14.00000  1.000 28.05009 ? 41  THR   D O     1 
ATOM   1663 C  CB    . THR   B 2 42  ? 7.54900   -8.56100  16.32800  1.000 28.11489 ? 41  THR   D CB    1 
ATOM   1664 O  OG1   . THR   B 2 42  ? 6.35900   -8.15600  15.63600  1.000 26.52834 ? 41  THR   D OG1   1 
ATOM   1665 C  CG2   . THR   B 2 42  ? 7.55400   -7.99400  17.74100  1.000 25.65646 ? 41  THR   D CG2   1 
ATOM   1666 N  N     . GLY   B 2 43  ? 8.29900   -7.91800  13.15000  1.000 22.86573 ? 42  GLY   D N     1 
ATOM   1667 C  CA    . GLY   B 2 43  ? 8.02700   -8.44500  11.83200  1.000 26.30933 ? 42  GLY   D CA    1 
ATOM   1668 C  C     . GLY   B 2 43  ? 6.75900   -9.25200  11.70100  1.000 28.35115 ? 42  GLY   D C     1 
ATOM   1669 O  O     . GLY   B 2 43  ? 6.58900   -9.93900  10.69700  1.000 33.11131 ? 42  GLY   D O     1 
ATOM   1670 N  N     . GLU   B 2 44  ? 5.83600   -9.16700  12.66300  1.000 25.36016 ? 43  GLU   D N     1 
ATOM   1671 C  CA    . GLU   B 2 44  ? 4.72300   -10.12100 12.68200  1.000 28.70029 ? 43  GLU   D CA    1 
ATOM   1672 C  C     . GLU   B 2 44  ? 3.73000   -9.92500  11.53800  1.000 29.53440 ? 43  GLU   D C     1 
ATOM   1673 O  O     . GLU   B 2 44  ? 2.97600   -10.86000 11.23300  1.000 33.53213 ? 43  GLU   D O     1 
ATOM   1674 C  CB    . GLU   B 2 44  ? 3.99400   -10.09200 14.02000  1.000 30.70458 ? 43  GLU   D CB    1 
ATOM   1675 C  CG    . GLU   B 2 44  ? 3.33400   -8.76600  14.29000  1.000 29.47039 ? 43  GLU   D CG    1 
ATOM   1676 C  CD    . GLU   B 2 44  ? 2.96100   -8.60100  15.75500  1.000 33.24700 ? 43  GLU   D CD    1 
ATOM   1677 O  OE1   . GLU   B 2 44  ? 3.86700   -8.69600  16.61100  1.000 30.92022 ? 43  GLU   D OE1   1 
ATOM   1678 O  OE2   . GLU   B 2 44  ? 1.76800   -8.38400  16.03500  1.000 33.22241 ? 43  GLU   D OE2   1 
ATOM   1679 N  N     . LYS   B 2 45  ? 3.71100   -8.74100  10.90800  1.000 30.15214 ? 44  LYS   D N     1 
ATOM   1680 C  CA    . LYS   B 2 45  ? 2.86700   -8.54500  9.73400   1.000 32.91739 ? 44  LYS   D CA    1 
ATOM   1681 C  C     . LYS   B 2 45  ? 3.51500   -9.04000  8.44500   1.000 29.87190 ? 44  LYS   D C     1 
ATOM   1682 O  O     . LYS   B 2 45  ? 2.86800   -8.99200  7.39300   1.000 34.85472 ? 44  LYS   D O     1 
ATOM   1683 C  CB    . LYS   B 2 45  ? 2.47900   -7.07000  9.57800   1.000 31.31825 ? 44  LYS   D CB    1 
ATOM   1684 C  CG    . LYS   B 2 45  ? 1.93700   -6.38900  10.83900  1.000 30.49642 ? 44  LYS   D CG    1 
ATOM   1685 C  CD    . LYS   B 2 45  ? 0.55700   -6.90600  11.24600  1.000 35.92266 ? 44  LYS   D CD    1 
ATOM   1686 C  CE    . LYS   B 2 45  ? 0.03100   -6.14100  12.47500  1.000 40.58146 ? 44  LYS   D CE    1 
ATOM   1687 N  NZ    . LYS   B 2 45  ? -1.21500  -6.75600  13.01400  1.000 44.88264 ? 44  LYS   D NZ    1 
ATOM   1688 N  N     . GLY   B 2 46  ? 4.75400   -9.53600  8.49400   1.000 30.84433 ? 45  GLY   D N     1 
ATOM   1689 C  CA    . GLY   B 2 46  ? 5.43200   -10.03200 7.31100   1.000 31.22120 ? 45  GLY   D CA    1 
ATOM   1690 C  C     . GLY   B 2 46  ? 6.36300   -9.02900  6.67800   1.000 27.60924 ? 45  GLY   D C     1 
ATOM   1691 O  O     . GLY   B 2 46  ? 6.93900   -9.30600  5.62000   1.000 33.07285 ? 45  GLY   D O     1 
ATOM   1692 N  N     . PHE   B 2 47  ? 6.52300   -7.87400  7.29700   1.000 26.54131 ? 46  PHE   D N     1 
ATOM   1693 C  CA    . PHE   B 2 47  ? 7.47500   -6.88000  6.84200   1.000 25.84790 ? 46  PHE   D CA    1 
ATOM   1694 C  C     . PHE   B 2 47  ? 7.86900   -6.09200  8.07400   1.000 25.35686 ? 46  PHE   D C     1 
ATOM   1695 O  O     . PHE   B 2 47  ? 7.20000   -6.17000  9.11200   1.000 26.72522 ? 46  PHE   D O     1 
ATOM   1696 C  CB    . PHE   B 2 47  ? 6.86600   -5.97100  5.76700   1.000 26.21844 ? 46  PHE   D CB    1 
ATOM   1697 C  CG    . PHE   B 2 47  ? 5.52300   -5.40800  6.13700   1.000 30.13814 ? 46  PHE   D CG    1 
ATOM   1698 C  CD1   . PHE   B 2 47  ? 5.42600   -4.27100  6.95500   1.000 26.98918 ? 46  PHE   D CD1   1 
ATOM   1699 C  CD2   . PHE   B 2 47  ? 4.36300   -5.99200  5.65100   1.000 31.97733 ? 46  PHE   D CD2   1 
ATOM   1700 C  CE1   . PHE   B 2 47  ? 4.18300   -3.76800  7.30500   1.000 25.41869 ? 46  PHE   D CE1   1 
ATOM   1701 C  CE2   . PHE   B 2 47  ? 3.11800   -5.47700  5.99400   1.000 31.02807 ? 46  PHE   D CE2   1 
ATOM   1702 C  CZ    . PHE   B 2 47  ? 3.02300   -4.37000  6.82500   1.000 28.25645 ? 46  PHE   D CZ    1 
ATOM   1703 N  N     . GLY   B 2 48  ? 8.96600   -5.35300  7.96700   1.000 21.71481 ? 47  GLY   D N     1 
ATOM   1704 C  CA    . GLY   B 2 48  ? 9.37700   -4.51400  9.07800   1.000 19.03420 ? 47  GLY   D CA    1 
ATOM   1705 C  C     . GLY   B 2 48  ? 10.85700  -4.15500  9.01900   1.000 19.11446 ? 47  GLY   D C     1 
ATOM   1706 O  O     . GLY   B 2 48  ? 11.49000  -4.22200  7.97100   1.000 20.76771 ? 47  GLY   D O     1 
ATOM   1707 N  N     . TYR   B 2 49  ? 11.38000  -3.77200  10.17800  1.000 20.39948 ? 48  TYR   D N     1 
ATOM   1708 C  CA    . TYR   B 2 49  ? 12.67500  -3.11500  10.25400  1.000 17.64757 ? 48  TYR   D CA    1 
ATOM   1709 C  C     . TYR   B 2 49  ? 13.87100  -4.04600  10.06500  1.000 16.84193 ? 48  TYR   D C     1 
ATOM   1710 O  O     . TYR   B 2 49  ? 14.95400  -3.55000  9.71800   1.000 17.12824 ? 48  TYR   D O     1 
ATOM   1711 C  CB    . TYR   B 2 49  ? 12.81800  -2.42600  11.60900  1.000 18.62923 ? 48  TYR   D CB    1 
ATOM   1712 C  CG    . TYR   B 2 49  ? 11.87100  -1.28100  11.84200  1.000 15.80752 ? 48  TYR   D CG    1 
ATOM   1713 C  CD1   . TYR   B 2 49  ? 11.72000  -0.28000  10.87400  1.000 15.84975 ? 48  TYR   D CD1   1 
ATOM   1714 C  CD2   . TYR   B 2 49  ? 11.17400  -1.16400  13.02700  1.000 17.14572 ? 48  TYR   D CD2   1 
ATOM   1715 C  CE1   . TYR   B 2 49  ? 10.88000  0.80200   11.07700  1.000 16.79915 ? 48  TYR   D CE1   1 
ATOM   1716 C  CE2   . TYR   B 2 49  ? 10.32400  -0.06600  13.24200  1.000 15.90573 ? 48  TYR   D CE2   1 
ATOM   1717 C  CZ    . TYR   B 2 49  ? 10.17500  0.88800   12.25200  1.000 16.03921 ? 48  TYR   D CZ    1 
ATOM   1718 O  OH    . TYR   B 2 49  ? 9.31500   1.96200   12.47400  1.000 16.99158 ? 48  TYR   D OH    1 
ATOM   1719 N  N     . LYS   B 2 50  ? 13.73400  -5.36500  10.27700  1.000 18.65944 ? 49  LYS   D N     1 
ATOM   1720 C  CA    . LYS   B 2 50  ? 14.92200  -6.19700  10.24300  1.000 19.01126 ? 49  LYS   D CA    1 
ATOM   1721 C  C     . LYS   B 2 50  ? 15.60000  -6.12100  8.88300   1.000 19.14279 ? 49  LYS   D C     1 
ATOM   1722 O  O     . LYS   B 2 50  ? 14.97100  -6.40600  7.85900   1.000 21.21045 ? 49  LYS   D O     1 
ATOM   1723 C  CB    . LYS   B 2 50  ? 14.55700  -7.64500  10.56800  1.000 23.11394 ? 49  LYS   D CB    1 
ATOM   1724 C  CG    . LYS   B 2 50  ? 15.79100  -8.53100  10.82300  1.000 22.34751 ? 49  LYS   D CG    1 
ATOM   1725 C  CD    . LYS   B 2 50  ? 15.42200  -9.86100  11.50900  1.000 29.19122 ? 49  LYS   D CD    1 
ATOM   1726 C  CE    . LYS   B 2 50  ? 15.17400  -10.91400 10.48900  1.000 36.73249 ? 49  LYS   D CE    1 
ATOM   1727 N  NZ    . LYS   B 2 50  ? 14.78700  -12.19500 11.15400  1.000 42.43829 ? 49  LYS   D NZ    1 
ATOM   1728 N  N     . GLY   B 2 51  ? 16.89500  -5.76500  8.88700   1.000 17.49693 ? 50  GLY   D N     1 
ATOM   1729 C  CA    . GLY   B 2 51  ? 17.68900  -5.62300  7.68400   1.000 19.92068 ? 50  GLY   D CA    1 
ATOM   1730 C  C     . GLY   B 2 51  ? 17.81900  -4.20000  7.18100   1.000 18.68386 ? 50  GLY   D C     1 
ATOM   1731 O  O     . GLY   B 2 51  ? 18.74200  -3.91700  6.40700   1.000 18.25066 ? 50  GLY   D O     1 
ATOM   1732 N  N     . SER   B 2 52  ? 16.94800  -3.29200  7.62200   1.000 16.66162 ? 51  SER   D N     1 
ATOM   1733 C  CA    . SER   B 2 52  ? 16.93300  -1.94200  7.09200   1.000 16.85151 ? 51  SER   D CA    1 
ATOM   1734 C  C     . SER   B 2 52  ? 18.04600  -1.11800  7.72000   1.000 16.72564 ? 51  SER   D C     1 
ATOM   1735 O  O     . SER   B 2 52  ? 18.69000  -1.50800  8.69400   1.000 17.31045 ? 51  SER   D O     1 
ATOM   1736 C  CB    . SER   B 2 52  ? 15.55200  -1.31500  7.27200   1.000 16.64050 ? 51  SER   D CB    1 
ATOM   1737 O  OG    . SER   B 2 52  ? 15.28400  -1.09800  8.65600   1.000 17.39242 ? 51  SER   D OG    1 
ATOM   1738 N  N     . CYS   B 2 53  ? 18.29300  0.04000   7.14200   1.000 16.37453 ? 52  CYS   D N     1 
ATOM   1739 C  CA    . CYS   B 2 53  ? 19.45400  0.79500   7.57600   1.000 18.21599 ? 52  CYS   D CA    1 
ATOM   1740 C  C     . CYS   B 2 53  ? 19.09500  2.13800   8.20600   1.000 15.50373 ? 52  CYS   D C     1 
ATOM   1741 O  O     . CYS   B 2 53  ? 17.99500  2.67700   8.02400   1.000 17.60192 ? 52  CYS   D O     1 
ATOM   1742 C  CB    . CYS   B 2 53  ? 20.43700  0.98000   6.42700   1.000 21.17525 ? 52  CYS   D CB    1 
ATOM   1743 S  SG    . CYS   B 2 53  ? 20.21200  2.39900   5.41300   1.000 25.15852 ? 52  CYS   D SG    1 
ATOM   1744 N  N     . PHE   B 2 54  ? 20.02100  2.66100   8.99400   1.000 14.24412 ? 53  PHE   D N     1 
ATOM   1745 C  CA    . PHE   B 2 54  ? 19.97300  4.04800   9.43600   1.000 15.35566 ? 53  PHE   D CA    1 
ATOM   1746 C  C     . PHE   B 2 54  ? 20.62600  4.83100   8.32500   1.000 15.34157 ? 53  PHE   D C     1 
ATOM   1747 O  O     . PHE   B 2 54  ? 21.84300  4.89900   8.22500   1.000 17.54301 ? 53  PHE   D O     1 
ATOM   1748 C  CB    . PHE   B 2 54  ? 20.72600  4.20300   10.74300  1.000 15.23077 ? 53  PHE   D CB    1 
ATOM   1749 C  CG    . PHE   B 2 54  ? 19.91200  3.80600   11.94700  1.000 14.63359 ? 53  PHE   D CG    1 
ATOM   1750 C  CD1   . PHE   B 2 54  ? 19.82600  2.48700   12.38100  1.000 16.05254 ? 53  PHE   D CD1   1 
ATOM   1751 C  CD2   . PHE   B 2 54  ? 19.14000  4.76800   12.61600  1.000 14.64814 ? 53  PHE   D CD2   1 
ATOM   1752 C  CE1   . PHE   B 2 54  ? 19.03200  2.14900   13.48900  1.000 18.38424 ? 53  PHE   D CE1   1 
ATOM   1753 C  CE2   . PHE   B 2 54  ? 18.37000  4.43800   13.72700  1.000 15.78069 ? 53  PHE   D CE2   1 
ATOM   1754 C  CZ    . PHE   B 2 54  ? 18.33100  3.13200   14.14800  1.000 16.68349 ? 53  PHE   D CZ    1 
ATOM   1755 N  N     . HIS   B 2 55  ? 19.81500  5.41100   7.47100   1.000 15.31838 ? 54  HIS   D N     1 
ATOM   1756 C  CA    . HIS   B 2 55  ? 20.32300  6.08700   6.28500   1.000 15.95190 ? 54  HIS   D CA    1 
ATOM   1757 C  C     . HIS   B 2 55  ? 20.81100  7.51200   6.53500   1.000 14.47698 ? 54  HIS   D C     1 
ATOM   1758 O  O     . HIS   B 2 55  ? 21.58200  8.04200   5.73100   1.000 17.26456 ? 54  HIS   D O     1 
ATOM   1759 C  CB    . HIS   B 2 55  ? 19.26100  6.09900   5.18100   1.000 17.42688 ? 54  HIS   D CB    1 
ATOM   1760 C  CG    . HIS   B 2 55  ? 18.02900  6.87400   5.52000   1.000 17.03603 ? 54  HIS   D CG    1 
ATOM   1761 N  ND1   . HIS   B 2 55  ? 17.02200  6.38600   6.33000   1.000 17.43416 ? 54  HIS   D ND1   1 
ATOM   1762 C  CD2   . HIS   B 2 55  ? 17.66500  8.13600   5.17900   1.000 18.46736 ? 54  HIS   D CD2   1 
ATOM   1763 C  CE1   . HIS   B 2 55  ? 16.07800  7.31100   6.44400   1.000 18.33823 ? 54  HIS   D CE1   1 
ATOM   1764 N  NE2   . HIS   B 2 55  ? 16.44800  8.37000   5.75500   1.000 18.93500 ? 54  HIS   D NE2   1 
ATOM   1765 N  N     . ARG   B 2 56  ? 20.41400  8.15300   7.63700   1.000 13.81768 ? 55  ARG   D N     1 
ATOM   1766 C  CA    . ARG   B 2 56  ? 20.74300  9.55900   7.86600   1.000 14.39768 ? 55  ARG   D CA    1 
ATOM   1767 C  C     . ARG   B 2 56  ? 21.15600  9.71300   9.32300   1.000 12.34976 ? 55  ARG   D C     1 
ATOM   1768 O  O     . ARG   B 2 56  ? 20.31500  9.57600   10.22700  1.000 13.89479 ? 55  ARG   D O     1 
ATOM   1769 C  CB    . ARG   B 2 56  ? 19.54500  10.42000  7.50600   1.000 14.43473 ? 55  ARG   D CB    1 
ATOM   1770 C  CG    . ARG   B 2 56  ? 19.86800  11.93600  7.62900   1.000 15.90489 ? 55  ARG   D CG    1 
ATOM   1771 C  CD    . ARG   B 2 56  ? 18.62300  12.83500  7.43800   1.000 16.38684 ? 55  ARG   D CD    1 
ATOM   1772 N  NE    . ARG   B 2 56  ? 18.21000  12.71300  6.05000   1.000 16.43369 ? 55  ARG   D NE    1 
ATOM   1773 C  CZ    . ARG   B 2 56  ? 16.96300  12.81800  5.62800   1.000 18.98553 ? 55  ARG   D CZ    1 
ATOM   1774 N  NH1   . ARG   B 2 56  ? 15.99100  13.17600  6.45500   1.000 21.73897 ? 55  ARG   D NH1   1 
ATOM   1775 N  NH2   . ARG   B 2 56  ? 16.70800  12.62900  4.32300   1.000 25.94756 ? 55  ARG   D NH2   1 
ATOM   1776 N  N     . ILE   B 2 57  ? 22.43700  9.95800   9.55300   1.000 12.55481 ? 56  ILE   D N     1 
ATOM   1777 C  CA    . ILE   B 2 57  ? 22.98900  10.11700  10.89900  1.000 13.76064 ? 56  ILE   D CA    1 
ATOM   1778 C  C     . ILE   B 2 57  ? 23.72700  11.45100  10.90300  1.000 14.02647 ? 56  ILE   D C     1 
ATOM   1779 O  O     . ILE   B 2 57  ? 24.72000  11.62300  10.19100  1.000 14.18982 ? 56  ILE   D O     1 
ATOM   1780 C  CB    . ILE   B 2 57  ? 23.90700  8.94300   11.29900  1.000 14.67727 ? 56  ILE   D CB    1 
ATOM   1781 C  CG1   . ILE   B 2 57  ? 23.11000  7.62400   11.31000  1.000 16.34017 ? 56  ILE   D CG1   1 
ATOM   1782 C  CG2   . ILE   B 2 57  ? 24.55800  9.23800   12.64600  1.000 16.24489 ? 56  ILE   D CG2   1 
ATOM   1783 C  CD1   . ILE   B 2 57  ? 24.00200  6.44100   11.67900  1.000 17.47449 ? 56  ILE   D CD1   1 
ATOM   1784 N  N     . ILE   B 2 58  ? 23.21500  12.39600  11.68600  1.000 13.59787 ? 57  ILE   D N     1 
ATOM   1785 C  CA    . ILE   B 2 58  ? 23.79200  13.73900  11.71400  1.000 13.76063 ? 57  ILE   D CA    1 
ATOM   1786 C  C     . ILE   B 2 58  ? 24.24400  13.99800  13.14200  1.000 13.23862 ? 57  ILE   D C     1 
ATOM   1787 O  O     . ILE   B 2 58  ? 23.39600  14.15800  14.03700  1.000 15.15693 ? 57  ILE   D O     1 
ATOM   1788 C  CB    . ILE   B 2 58  ? 22.83000  14.82100  11.19400  1.000 15.48790 ? 57  ILE   D CB    1 
ATOM   1789 C  CG1   . ILE   B 2 58  ? 22.42900  14.53600  9.73300   1.000 14.86919 ? 57  ILE   D CG1   1 
ATOM   1790 C  CG2   . ILE   B 2 58  ? 23.50600  16.17100  11.31400  1.000 17.02193 ? 57  ILE   D CG2   1 
ATOM   1791 C  CD1   . ILE   B 2 58  ? 21.52400  15.60300  9.14200   1.000 16.85091 ? 57  ILE   D CD1   1 
ATOM   1792 N  N     . PRO   B 2 59  ? 25.54600  14.02000  13.38600  1.000 16.37590 ? 58  PRO   D N     1 
ATOM   1793 C  CA    . PRO   B 2 59  ? 26.05800  14.16800  14.75200  1.000 18.85194 ? 58  PRO   D CA    1 
ATOM   1794 C  C     . PRO   B 2 59  ? 25.56500  15.45200  15.38400  1.000 18.18988 ? 58  PRO   D C     1 
ATOM   1795 O  O     . PRO   B 2 59  ? 25.52000  16.51100  14.75400  1.000 18.71140 ? 58  PRO   D O     1 
ATOM   1796 C  CB    . PRO   B 2 59  ? 27.58100  14.17800  14.56700  1.000 21.48433 ? 58  PRO   D CB    1 
ATOM   1797 C  CG    . PRO   B 2 59  ? 27.81100  13.40600  13.28600  1.000 21.69666 ? 58  PRO   D CG    1 
ATOM   1798 C  CD    . PRO   B 2 59  ? 26.60600  13.72600  12.41000  1.000 17.36240 ? 58  PRO   D CD    1 
ATOM   1799 N  N     . GLY   B 2 60  ? 25.18200  15.33200  16.64500  1.000 19.79190 ? 59  GLY   D N     1 
ATOM   1800 C  CA    . GLY   B 2 60  ? 24.61900  16.42800  17.38800  1.000 18.49803 ? 59  GLY   D CA    1 
ATOM   1801 C  C     . GLY   B 2 60  ? 23.13200  16.56800  17.23500  1.000 16.00596 ? 59  GLY   D C     1 
ATOM   1802 O  O     . GLY   B 2 60  ? 22.53800  17.43700  17.89000  1.000 20.16458 ? 59  GLY   D O     1 
ATOM   1803 N  N     . PHE   B 2 61  ? 22.51000  15.77000  16.37700  1.000 14.55204 ? 60  PHE   D N     1 
ATOM   1804 C  CA    . PHE   B 2 61  ? 21.07600  15.88500  16.15300  1.000 14.75973 ? 60  PHE   D CA    1 
ATOM   1805 C  C     . PHE   B 2 61  ? 20.33600  14.56100  16.30300  1.000 15.27677 ? 60  PHE   D C     1 
ATOM   1806 O  O     . PHE   B 2 61  ? 19.55000  14.40300  17.24700  1.000 15.00789 ? 60  PHE   D O     1 
ATOM   1807 C  CB    . PHE   B 2 61  ? 20.79400  16.52000  14.77400  1.000 15.01941 ? 60  PHE   D CB    1 
ATOM   1808 C  CG    . PHE   B 2 61  ? 21.21900  17.96100  14.67000  1.000 13.69123 ? 60  PHE   D CG    1 
ATOM   1809 C  CD1   . PHE   B 2 61  ? 20.36900  18.97300  15.12600  1.000 16.02339 ? 60  PHE   D CD1   1 
ATOM   1810 C  CD2   . PHE   B 2 61  ? 22.46700  18.32000  14.15400  1.000 16.73897 ? 60  PHE   D CD2   1 
ATOM   1811 C  CE1   . PHE   B 2 61  ? 20.72100  20.28600  15.01700  1.000 18.48821 ? 60  PHE   D CE1   1 
ATOM   1812 C  CE2   . PHE   B 2 61  ? 22.81600  19.65200  14.04200  1.000 17.98579 ? 60  PHE   D CE2   1 
ATOM   1813 C  CZ    . PHE   B 2 61  ? 21.93100  20.64700  14.49400  1.000 16.28946 ? 60  PHE   D CZ    1 
ATOM   1814 N  N     . MET   B 2 62  ? 20.51000  13.62900  15.36700  1.000 13.78021 ? 61  MET   D N     1 
ATOM   1815 C  CA    . MET   B 2 62  ? 19.68400  12.41800  15.40800  1.000 13.93418 ? 61  MET   D CA    1 
ATOM   1816 C  C     . MET   B 2 62  ? 20.22700  11.33100  14.50200  1.000 14.21542 ? 61  MET   D C     1 
ATOM   1817 O  O     . MET   B 2 62  ? 21.05800  11.56500  13.59900  1.000 15.13739 ? 61  MET   D O     1 
ATOM   1818 C  CB    . MET   B 2 62  ? 18.22800  12.68600  15.00100  1.000 16.10973 ? 61  MET   D CB    1 
ATOM   1819 C  CG    . MET   B 2 62  ? 17.97000  12.57200  13.45900  1.000 18.72858 ? 61  MET   D CG    1 
ATOM   1820 S  SD    . MET   B 2 62  ? 18.75500  13.94100  12.54800  1.000 17.36167 ? 61  MET   D SD    1 
ATOM   1821 C  CE    . MET   B 2 62  ? 18.88000  13.05300  11.00500  1.000 15.82138 ? 61  MET   D CE    1 
ATOM   1822 N  N     . CYS   B 2 63  ? 19.68000  10.13200  14.73600  1.000 13.62517 ? 62  CYS   D N     1 
ATOM   1823 C  CA    . CYS   B 2 63  ? 19.87900  8.96400   13.88500  1.000 13.01395 ? 62  CYS   D CA    1 
ATOM   1824 C  C     . CYS   B 2 63  ? 18.51600  8.56800   13.33000  1.000 14.87100 ? 62  CYS   D C     1 
ATOM   1825 O  O     . CYS   B 2 63  ? 17.59500  8.26300   14.10900  1.000 14.42563 ? 62  CYS   D O     1 
ATOM   1826 C  CB    . CYS   B 2 63  ? 20.43600  7.78500   14.70400  1.000 16.40904 ? 62  CYS   D CB    1 
ATOM   1827 S  SG    . CYS   B 2 63  ? 22.09700  8.06300   15.42500  1.000 19.01174 ? 62  CYS   D SG    1 
ATOM   1828 N  N     . GLN   B 2 64  ? 18.38400  8.53700   12.01100  1.000 13.27029 ? 63  GLN   D N     1 
ATOM   1829 C  CA    . GLN   B 2 64  ? 17.12200  8.28200   11.31600  1.000 12.10618 ? 63  GLN   D CA    1 
ATOM   1830 C  C     . GLN   B 2 64  ? 17.19400  7.01300   10.49000  1.000 12.36116 ? 63  GLN   D C     1 
ATOM   1831 O  O     . GLN   B 2 64  ? 18.16700  6.79500   9.75700   1.000 14.25016 ? 63  GLN   D O     1 
ATOM   1832 C  CB    . GLN   B 2 64  ? 16.75900  9.47400   10.44300  1.000 13.54107 ? 63  GLN   D CB    1 
ATOM   1833 C  CG    . GLN   B 2 64  ? 15.44500  9.32200   9.69300   1.000 13.12832 ? 63  GLN   D CG    1 
ATOM   1834 C  CD    . GLN   B 2 64  ? 15.07000  10.55100  8.93600   1.000 15.27563 ? 63  GLN   D CD    1 
ATOM   1835 O  OE1   . GLN   B 2 64  ? 15.56600  11.64700  9.20100   1.000 15.82385 ? 63  GLN   D OE1   1 
ATOM   1836 N  NE2   . GLN   B 2 64  ? 14.21300  10.38800  7.97900   1.000 14.71974 ? 63  GLN   D NE2   1 
ATOM   1837 N  N     . GLY   B 2 65  ? 16.16900  6.18500   10.61800  1.000 12.18257 ? 64  GLY   D N     1 
ATOM   1838 C  CA    . GLY   B 2 65  ? 16.08800  4.96100   9.82300   1.000 14.08549 ? 64  GLY   D CA    1 
ATOM   1839 C  C     . GLY   B 2 65  ? 14.67100  4.56900   9.48000   1.000 14.30458 ? 64  GLY   D C     1 
ATOM   1840 O  O     . GLY   B 2 65  ? 13.73700  5.36600   9.60500   1.000 14.80141 ? 64  GLY   D O     1 
ATOM   1841 N  N     . GLY   B 2 66  ? 14.51000  3.33200   9.02400   1.000 16.67857 ? 65  GLY   D N     1 
ATOM   1842 C  CA    . GLY   B 2 66  ? 13.19600  2.75300   8.88200   1.000 16.83880 ? 65  GLY   D CA    1 
ATOM   1843 C  C     . GLY   B 2 66  ? 12.67300  2.59200   7.47900   1.000 16.45058 ? 65  GLY   D C     1 
ATOM   1844 O  O     . GLY   B 2 66  ? 11.53000  2.14900   7.33700   1.000 17.06503 ? 65  GLY   D O     1 
ATOM   1845 N  N     . ASP   B 2 67  ? 13.45400  2.89800   6.43300   1.000 16.06977 ? 66  ASP   D N     1 
ATOM   1846 C  CA    . ASP   B 2 67  ? 12.94800  2.67900   5.07500   1.000 16.03623 ? 66  ASP   D CA    1 
ATOM   1847 C  C     . ASP   B 2 67  ? 13.24600  1.24500   4.64900   1.000 17.35903 ? 66  ASP   D C     1 
ATOM   1848 O  O     . ASP   B 2 67  ? 14.30700  0.96300   4.08600   1.000 18.54562 ? 66  ASP   D O     1 
ATOM   1849 C  CB    . ASP   B 2 67  ? 13.60300  3.63200   4.08100   1.000 17.39820 ? 66  ASP   D CB    1 
ATOM   1850 C  CG    . ASP   B 2 67  ? 13.10700  3.42900   2.66300   1.000 17.79703 ? 66  ASP   D CG    1 
ATOM   1851 O  OD1   . ASP   B 2 67  ? 12.29800  2.49000   2.40400   1.000 19.76996 ? 66  ASP   D OD1   1 
ATOM   1852 O  OD2   . ASP   B 2 67  ? 13.58100  4.13600   1.74500   1.000 18.95955 ? 66  ASP   D OD2   1 
ATOM   1853 N  N     . PHE   B 2 68  ? 12.27500  0.35700   4.83700   1.000 16.18832 ? 67  PHE   D N     1 
ATOM   1854 C  CA    . PHE   B 2 68  ? 12.39800  -1.02300  4.37700   1.000 18.15782 ? 67  PHE   D CA    1 
ATOM   1855 C  C     . PHE   B 2 68  ? 11.70500  -1.29900  3.03500   1.000 21.01473 ? 67  PHE   D C     1 
ATOM   1856 O  O     . PHE   B 2 68  ? 11.76900  -2.42900  2.54500   1.000 22.73977 ? 67  PHE   D O     1 
ATOM   1857 C  CB    . PHE   B 2 68  ? 11.92300  -2.02400  5.45700   1.000 21.94162 ? 67  PHE   D CB    1 
ATOM   1858 C  CG    . PHE   B 2 68  ? 10.50600  -1.82900  5.89800   1.000 18.85188 ? 67  PHE   D CG    1 
ATOM   1859 C  CD1   . PHE   B 2 68  ? 9.46900   -2.32400  5.14200   1.000 22.06732 ? 67  PHE   D CD1   1 
ATOM   1860 C  CD2   . PHE   B 2 68  ? 10.19600  -1.14000  7.08500   1.000 19.80565 ? 67  PHE   D CD2   1 
ATOM   1861 C  CE1   . PHE   B 2 68  ? 8.14900   -2.13900  5.52500   1.000 21.44177 ? 67  PHE   D CE1   1 
ATOM   1862 C  CE2   . PHE   B 2 68  ? 8.87200   -0.99000  7.47700   1.000 21.43836 ? 67  PHE   D CE2   1 
ATOM   1863 C  CZ    . PHE   B 2 68  ? 7.86000   -1.46100  6.68800   1.000 21.70007 ? 67  PHE   D CZ    1 
ATOM   1864 N  N     . THR   B 2 69  ? 11.04600  -0.31000  2.42500   1.000 21.19171 ? 68  THR   D N     1 
ATOM   1865 C  CA    . THR   B 2 69  ? 10.37600  -0.53300  1.14200   1.000 21.25486 ? 68  THR   D CA    1 
ATOM   1866 C  C     . THR   B 2 69  ? 11.17700  -0.07100  -0.06300  1.000 23.40605 ? 68  THR   D C     1 
ATOM   1867 O  O     . THR   B 2 69  ? 11.13900  -0.72600  -1.08900  1.000 25.43607 ? 68  THR   D O     1 
ATOM   1868 C  CB    . THR   B 2 69  ? 8.97600   0.09600   1.07500   1.000 22.83198 ? 68  THR   D CB    1 
ATOM   1869 O  OG1   . THR   B 2 69  ? 9.08700   1.53200   1.08300   1.000 24.23811 ? 68  THR   D OG1   1 
ATOM   1870 C  CG2   . THR   B 2 69  ? 8.11400   -0.36600  2.25200   1.000 25.17502 ? 68  THR   D CG2   1 
ATOM   1871 N  N     . ARG   B 2 70  ? 11.86400  1.06000   0.00800   1.000 23.06006 ? 69  ARG   D N     1 
ATOM   1872 C  CA    . ARG   B 2 70  ? 12.66400  1.52700   -1.11600  1.000 23.21213 ? 69  ARG   D CA    1 
ATOM   1873 C  C     . ARG   B 2 70  ? 14.15400  1.46800   -0.84900  1.000 21.44378 ? 69  ARG   D C     1 
ATOM   1874 O  O     . ARG   B 2 70  ? 14.93400  1.55000   -1.80600  1.000 24.17009 ? 69  ARG   D O     1 
ATOM   1875 C  CB    . ARG   B 2 70  ? 12.30300  2.97400   -1.48600  1.000 25.30959 ? 69  ARG   D CB    1 
ATOM   1876 C  CG    . ARG   B 2 70  ? 10.85400  3.17100   -1.88300  1.000 27.82299 ? 69  ARG   D CG    1 
ATOM   1877 C  CD    . ARG   B 2 70  ? 10.53100  2.55000   -3.23400  1.000 34.44119 ? 69  ARG   D CD    1 
ATOM   1878 N  NE    . ARG   B 2 70  ? 11.66300  2.49100   -4.15500  1.000 38.25611 ? 69  ARG   D NE    1 
ATOM   1879 C  CZ    . ARG   B 2 70  ? 12.18500  3.53600   -4.78800  1.000 35.93472 ? 69  ARG   D CZ    1 
ATOM   1880 N  NH1   . ARG   B 2 70  ? 11.77000  4.76800   -4.54800  1.000 43.32647 ? 69  ARG   D NH1   1 
ATOM   1881 N  NH2   . ARG   B 2 70  ? 13.14800  3.33700   -5.68700  1.000 43.83262 ? 69  ARG   D NH2   1 
ATOM   1882 N  N     . HIS   B 2 71  ? 14.56200  1.32600   0.40900   1.000 19.91129 ? 70  HIS   D N     1 
ATOM   1883 C  CA    . HIS   B 2 71  ? 15.96800  1.15800   0.77400   1.000 21.80297 ? 70  HIS   D CA    1 
ATOM   1884 C  C     . HIS   B 2 71  ? 16.80400  2.33900   0.31600   1.000 22.57527 ? 70  HIS   D C     1 
ATOM   1885 O  O     . HIS   B 2 71  ? 17.97500  2.18600   -0.03100  1.000 25.11606 ? 70  HIS   D O     1 
ATOM   1886 C  CB    . HIS   B 2 71  ? 16.54600  -0.15200  0.21200   1.000 23.31005 ? 70  HIS   D CB    1 
ATOM   1887 C  CG    . HIS   B 2 71  ? 15.65900  -1.34400  0.40100   1.000 22.17434 ? 70  HIS   D CG    1 
ATOM   1888 N  ND1   . HIS   B 2 71  ? 15.65800  -2.07600  1.56400   1.000 21.16124 ? 70  HIS   D ND1   1 
ATOM   1889 C  CD2   . HIS   B 2 71  ? 14.74500  -1.92400  -0.41300  1.000 21.85610 ? 70  HIS   D CD2   1 
ATOM   1890 C  CE1   . HIS   B 2 71  ? 14.77900  -3.05800  1.46300   1.000 20.57778 ? 70  HIS   D CE1   1 
ATOM   1891 N  NE2   . HIS   B 2 71  ? 14.21500  -2.99300  0.27000   1.000 25.01585 ? 70  HIS   D NE2   1 
ATOM   1892 N  N     . ASN   B 2 72  ? 16.20000  3.51900   0.26900   1.000 21.99836 ? 71  ASN   D N     1 
ATOM   1893 C  CA    . ASN   B 2 72  ? 16.95000  4.67400   -0.21900  1.000 22.79183 ? 71  ASN   D CA    1 
ATOM   1894 C  C     . ASN   B 2 72  ? 16.65200  5.94100   0.58000   1.000 20.97434 ? 71  ASN   D C     1 
ATOM   1895 O  O     . ASN   B 2 72  ? 17.03400  7.03400   0.13200   1.000 24.81063 ? 71  ASN   D O     1 
ATOM   1896 C  CB    . ASN   B 2 72  ? 16.74200  4.90000   -1.73200  1.000 24.11146 ? 71  ASN   D CB    1 
ATOM   1897 C  CG    . ASN   B 2 72  ? 15.32300  5.26800   -2.08300  1.000 22.86239 ? 71  ASN   D CG    1 
ATOM   1898 O  OD1   . ASN   B 2 72  ? 14.51600  5.61100   -1.20800  1.000 21.17071 ? 71  ASN   D OD1   1 
ATOM   1899 N  ND2   . ASN   B 2 72  ? 15.00500  5.23100   -3.37800  1.000 31.98408 ? 71  ASN   D ND2   1 
ATOM   1900 N  N     . GLY   B 2 73  ? 15.93800  5.85100   1.69800   1.000 17.80609 ? 72  GLY   D N     1 
ATOM   1901 C  CA    . GLY   B 2 73  ? 15.58800  6.98300   2.53400   1.000 18.44079 ? 72  GLY   D CA    1 
ATOM   1902 C  C     . GLY   B 2 73  ? 14.26900  7.64900   2.20800   1.000 20.78227 ? 72  GLY   D C     1 
ATOM   1903 O  O     . GLY   B 2 73  ? 13.87800  8.58700   2.91000   1.000 23.04794 ? 72  GLY   D O     1 
ATOM   1904 N  N     . THR   B 2 74  ? 13.58000  7.21700   1.15600   1.000 20.68893 ? 73  THR   D N     1 
ATOM   1905 C  CA    . THR   B 2 74  ? 12.34200  7.84600   0.71900   1.000 19.61371 ? 73  THR   D CA    1 
ATOM   1906 C  C     . THR   B 2 74  ? 11.10100  7.03800   1.05200   1.000 21.42245 ? 73  THR   D C     1 
ATOM   1907 O  O     . THR   B 2 74  ? 9.98700   7.57300   0.94900   1.000 23.54769 ? 73  THR   D O     1 
ATOM   1908 C  CB    . THR   B 2 74  ? 12.37600  8.10900   -0.80200  1.000 21.86084 ? 73  THR   D CB    1 
ATOM   1909 O  OG1   . THR   B 2 74  ? 12.32300  6.87900   -1.53100  1.000 23.03615 ? 73  THR   D OG1   1 
ATOM   1910 C  CG2   . THR   B 2 74  ? 13.63100  8.91200   -1.22400  1.000 25.81406 ? 73  THR   D CG2   1 
ATOM   1911 N  N     . GLY   B 2 75  ? 11.25400  5.78100   1.44600   1.000 18.68570 ? 74  GLY   D N     1 
ATOM   1912 C  CA    . GLY   B 2 75  ? 10.11700  4.90600   1.57400   1.000 20.38877 ? 74  GLY   D CA    1 
ATOM   1913 C  C     . GLY   B 2 75  ? 9.74700   4.53500   2.99300   1.000 19.79241 ? 74  GLY   D C     1 
ATOM   1914 O  O     . GLY   B 2 75  ? 9.96700   5.29000   3.95300   1.000 19.45283 ? 74  GLY   D O     1 
ATOM   1915 N  N     . GLY   B 2 76  ? 9.16800   3.35100   3.12300   1.000 23.04844 ? 75  GLY   D N     1 
ATOM   1916 C  CA    . GLY   B 2 76  ? 8.60800   2.87500   4.37100   1.000 23.41813 ? 75  GLY   D CA    1 
ATOM   1917 C  C     . GLY   B 2 76  ? 7.08900   2.78300   4.29900   1.000 22.99416 ? 75  GLY   D C     1 
ATOM   1918 O  O     . GLY   B 2 76  ? 6.43400   3.34400   3.41800   1.000 24.28991 ? 75  GLY   D O     1 
ATOM   1919 N  N     . LYS   B 2 77  ? 6.53000   2.04200   5.24600   1.000 21.91780 ? 76  LYS   D N     1 
ATOM   1920 C  CA    . LYS   B 2 77  ? 5.08500   1.88000   5.29700   1.000 23.84679 ? 76  LYS   D CA    1 
ATOM   1921 C  C     . LYS   B 2 77  ? 4.70200   1.44600   6.70100   1.000 20.84130 ? 76  LYS   D C     1 
ATOM   1922 O  O     . LYS   B 2 77  ? 5.49800   0.83500   7.41900   1.000 22.23673 ? 76  LYS   D O     1 
ATOM   1923 C  CB    . LYS   B 2 77  ? 4.56900   0.90800   4.23200   1.000 30.04189 ? 76  LYS   D CB    1 
ATOM   1924 C  CG    . LYS   B 2 77  ? 4.86400   -0.55200  4.44900   1.000 29.87449 ? 76  LYS   D CG    1 
ATOM   1925 C  CD    . LYS   B 2 77  ? 4.17700   -1.32400  3.33700   1.000 29.17477 ? 76  LYS   D CD    1 
ATOM   1926 C  CE    . LYS   B 2 77  ? 4.58300   -2.78100  3.30300   1.000 36.18710 ? 76  LYS   D CE    1 
ATOM   1927 N  NZ    . LYS   B 2 77  ? 3.84200   -3.53200  2.24100   1.000 37.25532 ? 76  LYS   D NZ    1 
ATOM   1928 N  N     . SER   B 2 78  ? 3.50200   1.83900   7.10300   1.000 19.63068 ? 77  SER   D N     1 
ATOM   1929 C  CA    . SER   B 2 78  ? 2.97900   1.48400   8.40600   1.000 21.14614 ? 77  SER   D CA    1 
ATOM   1930 C  C     . SER   B 2 78  ? 2.20800   0.17600   8.31000   1.000 24.71408 ? 77  SER   D C     1 
ATOM   1931 O  O     . SER   B 2 78  ? 1.94300   -0.33500  7.21800   1.000 25.64279 ? 77  SER   D O     1 
ATOM   1932 C  CB    . SER   B 2 78  ? 2.07900   2.59800   8.92800   1.000 19.00711 ? 77  SER   D CB    1 
ATOM   1933 O  OG    . SER   B 2 78  ? 0.78600   2.50500   8.39400   1.000 23.75579 ? 77  SER   D OG    1 
ATOM   1934 N  N     . ILE   B 2 79  ? 1.84800   -0.37200  9.48000   1.000 22.46866 ? 78  ILE   D N     1 
ATOM   1935 C  CA    . ILE   B 2 79  ? 0.97100   -1.53200  9.55700   1.000 24.38159 ? 78  ILE   D CA    1 
ATOM   1936 C  C     . ILE   B 2 79  ? -0.47500  -1.20200  9.20600   1.000 26.42509 ? 78  ILE   D C     1 
ATOM   1937 O  O     . ILE   B 2 79  ? -1.28200  -2.12700  9.07100   1.000 31.24382 ? 78  ILE   D O     1 
ATOM   1938 C  CB    . ILE   B 2 79  ? 1.04100   -2.25800  10.92500  1.000 26.91743 ? 78  ILE   D CB    1 
ATOM   1939 C  CG1   . ILE   B 2 79  ? 0.38800   -1.42200  12.03700  1.000 25.67511 ? 78  ILE   D CG1   1 
ATOM   1940 C  CG2   . ILE   B 2 79  ? 2.48800   -2.64600  11.29600  1.000 23.17306 ? 78  ILE   D CG2   1 
ATOM   1941 C  CD1   . ILE   B 2 79  ? 0.20900   -2.16400  13.36100  1.000 27.02676 ? 78  ILE   D CD1   1 
ATOM   1942 N  N     . TYR   B 2 80  ? -0.80800  0.07800   9.02200   1.000 23.91297 ? 79  TYR   D N     1 
ATOM   1943 C  CA    . TYR   B 2 80  ? -2.17700  0.52200   8.76800   1.000 25.40685 ? 79  TYR   D CA    1 
ATOM   1944 C  C     . TYR   B 2 80  ? -2.41800  0.91200   7.31700   1.000 29.67237 ? 79  TYR   D C     1 
ATOM   1945 O  O     . TYR   B 2 80  ? -3.57200  1.09800   6.92700   1.000 38.31845 ? 79  TYR   D O     1 
ATOM   1946 C  CB    . TYR   B 2 80  ? -2.50800  1.72900   9.65700   1.000 29.40699 ? 79  TYR   D CB    1 
ATOM   1947 C  CG    . TYR   B 2 80  ? -2.17700  1.53300   11.11600  1.000 25.02108 ? 79  TYR   D CG    1 
ATOM   1948 C  CD1   . TYR   B 2 80  ? -2.85000  0.58700   11.87400  1.000 30.43224 ? 79  TYR   D CD1   1 
ATOM   1949 C  CD2   . TYR   B 2 80  ? -1.20200  2.29800   11.73400  1.000 24.36901 ? 79  TYR   D CD2   1 
ATOM   1950 C  CE1   . TYR   B 2 80  ? -2.54600  0.40300   13.21000  1.000 25.49744 ? 79  TYR   D CE1   1 
ATOM   1951 C  CE2   . TYR   B 2 80  ? -0.89600  2.11700   13.05800  1.000 26.64554 ? 79  TYR   D CE2   1 
ATOM   1952 C  CZ    . TYR   B 2 80  ? -1.57000  1.16700   13.78800  1.000 26.27646 ? 79  TYR   D CZ    1 
ATOM   1953 O  OH    . TYR   B 2 80  ? -1.24200  1.00600   15.12100  1.000 26.69850 ? 79  TYR   D OH    1 
ATOM   1954 N  N     . GLY   B 2 81  ? -1.35300  1.08000   6.52600   1.000 35.79609 ? 80  GLY   D N     1 
ATOM   1955 C  CA    . GLY   B 2 81  ? -1.44500  1.64200   5.19200   1.000 33.13569 ? 80  GLY   D CA    1 
ATOM   1956 C  C     . GLY   B 2 81  ? -0.14200  2.34100   4.88700   1.000 33.19292 ? 80  GLY   D C     1 
ATOM   1957 O  O     . GLY   B 2 81  ? 0.78300   2.27200   5.70400   1.000 30.50142 ? 80  GLY   D O     1 
ATOM   1958 N  N     . GLU   B 2 82  ? -0.03300  3.01000   3.73500   1.000 35.56756 ? 81  GLU   D N     1 
ATOM   1959 C  CA    . GLU   B 2 82  ? 1.19000   3.75900   3.47100   1.000 37.23497 ? 81  GLU   D CA    1 
ATOM   1960 C  C     . GLU   B 2 82  ? 1.41000   4.86500   4.49700   1.000 36.22780 ? 81  GLU   D C     1 
ATOM   1961 O  O     . GLU   B 2 82  ? 2.56000   5.14500   4.83900   1.000 34.26376 ? 81  GLU   D O     1 
ATOM   1962 C  CB    . GLU   B 2 82  ? 1.25400   4.29200   2.03300   1.000 35.38747 ? 81  GLU   D CB    1 
ATOM   1963 C  CG    . GLU   B 2 82  ? 1.52200   3.21500   0.97000   1.000 50.23952 ? 81  GLU   D CG    1 
ATOM   1964 C  CD    . GLU   B 2 82  ? 1.71800   3.78800   -0.43700  1.000 53.92500 ? 81  GLU   D CD    1 
ATOM   1965 O  OE1   . GLU   B 2 82  ? 1.81900   5.02700   -0.58000  1.000 49.49321 ? 81  GLU   D OE1   1 
ATOM   1966 O  OE2   . GLU   B 2 82  ? 1.76300   2.98900   -1.40300  1.000 53.97441 ? 81  GLU   D OE2   1 
ATOM   1967 N  N     . LYS   B 2 83  ? 0.33900   5.48400   5.01600   1.000 36.05413 ? 82  LYS   D N     1 
ATOM   1968 C  CA    . LYS   B 2 83  ? 0.49400   6.58900   5.96500   1.000 28.73200 ? 82  LYS   D CA    1 
ATOM   1969 C  C     . LYS   B 2 83  ? -0.64400  6.59900   6.98400   1.000 29.20758 ? 82  LYS   D C     1 
ATOM   1970 O  O     . LYS   B 2 83  ? -1.77200  6.19500   6.67700   1.000 33.88149 ? 82  LYS   D O     1 
ATOM   1971 C  CB    . LYS   B 2 83  ? 0.51300   7.94600   5.25300   1.000 30.46095 ? 82  LYS   D CB    1 
ATOM   1972 C  CG    . LYS   B 2 83  ? 1.57200   8.09800   4.16500   1.000 36.20867 ? 82  LYS   D CG    1 
ATOM   1973 C  CD    . LYS   B 2 83  ? 2.96500   8.13300   4.75100   1.000 38.02573 ? 82  LYS   D CD    1 
ATOM   1974 C  CE    . LYS   B 2 83  ? 4.02300   7.80100   3.71100   1.000 42.89537 ? 82  LYS   D CE    1 
ATOM   1975 N  NZ    . LYS   B 2 83  ? 4.65200   6.48900   4.02500   1.000 42.30292 ? 82  LYS   D NZ    1 
ATOM   1976 N  N     . PHE   B 2 84  ? -0.35500  7.11200   8.19200   1.000 23.57500 ? 83  PHE   D N     1 
ATOM   1977 C  CA    . PHE   B 2 84  ? -1.37600  7.28800   9.22200   1.000 25.22665 ? 83  PHE   D CA    1 
ATOM   1978 C  C     . PHE   B 2 84  ? -1.26200  8.66200   9.89200   1.000 22.40128 ? 83  PHE   D C     1 
ATOM   1979 O  O     . PHE   B 2 84  ? -0.21400  9.30900   9.87300   1.000 21.63683 ? 83  PHE   D O     1 
ATOM   1980 C  CB    . PHE   B 2 84  ? -1.46400  6.09900   10.22600  1.000 25.72362 ? 83  PHE   D CB    1 
ATOM   1981 C  CG    . PHE   B 2 84  ? -0.26100  5.92400   11.15500  1.000 24.67175 ? 83  PHE   D CG    1 
ATOM   1982 C  CD1   . PHE   B 2 84  ? 0.87400   5.26000   10.72800  1.000 21.35348 ? 83  PHE   D CD1   1 
ATOM   1983 C  CD2   . PHE   B 2 84  ? -0.34300  6.29800   12.47800  1.000 21.47449 ? 83  PHE   D CD2   1 
ATOM   1984 C  CE1   . PHE   B 2 84  ? 1.97200   5.04600   11.56500  1.000 20.88896 ? 83  PHE   D CE1   1 
ATOM   1985 C  CE2   . PHE   B 2 84  ? 0.74400   6.09900   13.35300  1.000 22.72514 ? 83  PHE   D CE2   1 
ATOM   1986 C  CZ    . PHE   B 2 84  ? 1.90200   5.46300   12.89500  1.000 21.82754 ? 83  PHE   D CZ    1 
ATOM   1987 N  N     . GLU   B 2 85  ? -2.35700  9.09800   10.51500  1.000 24.68277 ? 84  GLU   D N     1 
ATOM   1988 C  CA    . GLU   B 2 85  ? -2.41200  10.45700  11.05200  1.000 23.62797 ? 84  GLU   D CA    1 
ATOM   1989 C  C     . GLU   B 2 85  ? -1.50700  10.63900  12.26800  1.000 23.48651 ? 84  GLU   D C     1 
ATOM   1990 O  O     . GLU   B 2 85  ? -1.15300  9.69200   12.96400  1.000 22.79635 ? 84  GLU   D O     1 
ATOM   1991 C  CB    . GLU   B 2 85  ? -3.86100  10.82200  11.43400  1.000 25.71944 ? 84  GLU   D CB    1 
ATOM   1992 C  CG    . GLU   B 2 85  ? -4.75900  11.11100  10.21400  1.000 33.90060 ? 84  GLU   D CG    1 
ATOM   1993 C  CD    . GLU   B 2 85  ? -6.21400  11.44500  10.56300  1.000 50.13637 ? 84  GLU   D CD    1 
ATOM   1994 O  OE1   . GLU   B 2 85  ? -6.64600  11.18400  11.70500  1.000 51.27565 ? 84  GLU   D OE1   1 
ATOM   1995 O  OE2   . GLU   B 2 85  ? -6.92600  11.97100  9.67900   1.000 53.86953 ? 84  GLU   D OE2   1 
ATOM   1996 N  N     . ASP   B 2 86  ? -1.16100  11.90300  12.54000  1.000 20.81655 ? 85  ASP   D N     1 
ATOM   1997 C  CA    . ASP   B 2 86  ? -0.44100  12.24500  13.76100  1.000 20.88133 ? 85  ASP   D CA    1 
ATOM   1998 C  C     . ASP   B 2 86  ? -1.38800  12.03000  14.94400  1.000 21.14159 ? 85  ASP   D C     1 
ATOM   1999 O  O     . ASP   B 2 86  ? -2.40600  12.72900  15.10400  1.000 22.99450 ? 85  ASP   D O     1 
ATOM   2000 C  CB    . ASP   B 2 86  ? 0.03400   13.69100  13.70000  1.000 18.95190 ? 85  ASP   D CB    1 
ATOM   2001 C  CG    . ASP   B 2 86  ? 1.09400   13.92400  12.61600  1.000 20.26430 ? 85  ASP   D CG    1 
ATOM   2002 O  OD1   . ASP   B 2 86  ? 2.06400   13.13000  12.51600  1.000 20.94110 ? 85  ASP   D OD1   1 
ATOM   2003 O  OD2   . ASP   B 2 86  ? 0.93600   14.93100  11.88700  1.000 20.65808 ? 85  ASP   D OD2   1 
ATOM   2004 N  N     . GLU   B 2 87  ? -1.01900  11.07700  15.79600  1.000 20.94536 ? 86  GLU   D N     1 
ATOM   2005 C  CA    . GLU   B 2 87  ? -1.92000  10.62000  16.84300  1.000 22.36575 ? 86  GLU   D CA    1 
ATOM   2006 C  C     . GLU   B 2 87  ? -2.14100  11.69500  17.90100  1.000 21.69048 ? 86  GLU   D C     1 
ATOM   2007 O  O     . GLU   B 2 87  ? -3.28300  12.01700  18.25200  1.000 22.77364 ? 86  GLU   D O     1 
ATOM   2008 C  CB    . GLU   B 2 87  ? -1.36000  9.34300   17.47100  1.000 21.94035 ? 86  GLU   D CB    1 
ATOM   2009 C  CG    . GLU   B 2 87  ? -2.25200  8.70900   18.50600  1.000 21.52301 ? 86  GLU   D CG    1 
ATOM   2010 C  CD    . GLU   B 2 87  ? -1.76600  7.33100   18.90500  1.000 23.10734 ? 86  GLU   D CD    1 
ATOM   2011 O  OE1   . GLU   B 2 87  ? -0.59300  7.00300   18.56500  1.000 22.15081 ? 86  GLU   D OE1   1 
ATOM   2012 O  OE2   . GLU   B 2 87  ? -2.57200  6.57900   19.51500  1.000 27.32917 ? 86  GLU   D OE2   1 
ATOM   2013 N  N     . ASN   B 2 88  ? -1.05200  12.21000  18.46300  1.000 19.81475 ? 87  ASN   D N     1 
ATOM   2014 C  CA    . ASN   B 2 88  ? -1.10900  13.33900  19.38900  1.000 20.45465 ? 87  ASN   D CA    1 
ATOM   2015 C  C     . ASN   B 2 88  ? 0.30100   13.91500  19.48500  1.000 19.10421 ? 87  ASN   D C     1 
ATOM   2016 O  O     . ASN   B 2 88  ? 1.26300   13.33600  18.97400  1.000 18.19076 ? 87  ASN   D O     1 
ATOM   2017 C  CB    . ASN   B 2 88  ? -1.68100  12.94000  20.76500  1.000 22.33859 ? 87  ASN   D CB    1 
ATOM   2018 C  CG    . ASN   B 2 88  ? -0.78800  11.94500  21.51100  1.000 21.41529 ? 87  ASN   D CG    1 
ATOM   2019 O  OD1   . ASN   B 2 88  ? 0.35400   12.24100  21.81400  1.000 19.78178 ? 87  ASN   D OD1   1 
ATOM   2020 N  ND2   . ASN   B 2 88  ? -1.35800  10.79300  21.89100  1.000 23.61386 ? 87  ASN   D ND2   1 
ATOM   2021 N  N     . PHE   B 2 89  ? 0.41200   15.07700  20.11200  1.000 21.27420 ? 88  PHE   D N     1 
ATOM   2022 C  CA    . PHE   B 2 89  ? 1.70500   15.69600  20.37300  1.000 20.88980 ? 88  PHE   D CA    1 
ATOM   2023 C  C     . PHE   B 2 89  ? 1.92100   15.86800  21.87500  1.000 20.07520 ? 88  PHE   D C     1 
ATOM   2024 O  O     . PHE   B 2 89  ? 2.49900   16.85300  22.33000  1.000 23.61510 ? 88  PHE   D O     1 
ATOM   2025 C  CB    . PHE   B 2 89  ? 1.89000   17.00600  19.59400  1.000 19.94486 ? 88  PHE   D CB    1 
ATOM   2026 C  CG    . PHE   B 2 89  ? 1.83200   16.82100  18.10200  1.000 18.26533 ? 88  PHE   D CG    1 
ATOM   2027 C  CD1   . PHE   B 2 89  ? 2.84600   16.12900  17.42700  1.000 19.19585 ? 88  PHE   D CD1   1 
ATOM   2028 C  CD2   . PHE   B 2 89  ? 0.75200   17.30700  17.36500  1.000 21.06252 ? 88  PHE   D CD2   1 
ATOM   2029 C  CE1   . PHE   B 2 89  ? 2.79300   15.94600  16.06000  1.000 20.18461 ? 88  PHE   D CE1   1 
ATOM   2030 C  CE2   . PHE   B 2 89  ? 0.71100   17.09800  16.01400  1.000 24.33180 ? 88  PHE   D CE2   1 
ATOM   2031 C  CZ    . PHE   B 2 89  ? 1.70400   16.43300  15.37200  1.000 21.05187 ? 88  PHE   D CZ    1 
ATOM   2032 N  N     . ILE   B 2 90  ? 1.42900   14.90800  22.66500  1.000 18.63923 ? 89  ILE   D N     1 
ATOM   2033 C  CA    . ILE   B 2 90  ? 1.53300   15.00500  24.11800  1.000 21.06734 ? 89  ILE   D CA    1 
ATOM   2034 C  C     . ILE   B 2 90  ? 2.98700   15.01600  24.56800  1.000 19.60003 ? 89  ILE   D C     1 
ATOM   2035 O  O     . ILE   B 2 90  ? 3.37400   15.83000  25.42100  1.000 21.83661 ? 89  ILE   D O     1 
ATOM   2036 C  CB    . ILE   B 2 90  ? 0.72900   13.87500  24.78600  1.000 21.63100 ? 89  ILE   D CB    1 
ATOM   2037 C  CG1   . ILE   B 2 90  ? -0.76100  14.03500  24.48200  1.000 24.50281 ? 89  ILE   D CG1   1 
ATOM   2038 C  CG2   . ILE   B 2 90  ? 1.02300   13.82100  26.30900  1.000 27.04525 ? 89  ILE   D CG2   1 
ATOM   2039 C  CD1   . ILE   B 2 90  ? -1.61800  12.83900  24.92300  1.000 29.13937 ? 89  ILE   D CD1   1 
ATOM   2040 N  N     . LEU   B 2 91  ? 3.80800   14.13700  24.00800  1.000 18.02322 ? 90  LEU   D N     1 
ATOM   2041 C  CA    . LEU   B 2 91  ? 5.19300   14.03200  24.41500  1.000 17.05690 ? 90  LEU   D CA    1 
ATOM   2042 C  C     . LEU   B 2 91  ? 6.08100   14.91100  23.53700  1.000 16.67252 ? 90  LEU   D C     1 
ATOM   2043 O  O     . LEU   B 2 91  ? 5.76100   15.21400  22.38200  1.000 16.86288 ? 90  LEU   D O     1 
ATOM   2044 C  CB    . LEU   B 2 91  ? 5.59600   12.56700  24.38900  1.000 18.49786 ? 90  LEU   D CB    1 
ATOM   2045 C  CG    . LEU   B 2 91  ? 4.60900   11.76500  25.25000  1.000 21.76444 ? 90  LEU   D CG    1 
ATOM   2046 C  CD1   . LEU   B 2 91  ? 4.90200   10.32100  25.11700  1.000 28.61860 ? 90  LEU   D CD1   1 
ATOM   2047 C  CD2   . LEU   B 2 91  ? 4.63100   12.21100  26.74800  1.000 22.88797 ? 90  LEU   D CD2   1 
ATOM   2048 N  N     . LYS   B 2 92  ? 7.16400   15.38400  24.13300  1.000 18.99291 ? 91  LYS   D N     1 
ATOM   2049 C  CA    . LYS   B 2 92  ? 8.04800   16.36700  23.53300  1.000 17.90905 ? 91  LYS   D CA    1 
ATOM   2050 C  C     . LYS   B 2 92  ? 9.46000   15.80700  23.36200  1.000 17.56884 ? 91  LYS   D C     1 
ATOM   2051 O  O     . LYS   B 2 92  ? 9.85300   14.78600  23.95300  1.000 18.11642 ? 91  LYS   D O     1 
ATOM   2052 C  CB    . LYS   B 2 92  ? 8.07100   17.65500  24.39900  1.000 18.22999 ? 91  LYS   D CB    1 
ATOM   2053 C  CG    . LYS   B 2 92  ? 6.71100   18.21600  24.81300  1.000 24.59089 ? 91  LYS   D CG    1 
ATOM   2054 C  CD    . LYS   B 2 92  ? 5.85800   18.59700  23.63900  1.000 26.49423 ? 91  LYS   D CD    1 
ATOM   2055 C  CE    . LYS   B 2 92  ? 4.55100   19.25900  24.14900  1.000 25.38721 ? 91  LYS   D CE    1 
ATOM   2056 N  NZ    . LYS   B 2 92  ? 4.75900   20.60700  24.73600  1.000 41.65555 ? 91  LYS   D NZ    1 
ATOM   2057 N  N     . HIS   B 2 93  ? 10.22700  16.49200  22.50200  1.000 17.10024 ? 92  HIS   D N     1 
ATOM   2058 C  CA    . HIS   B 2 93  ? 11.59600  16.08700  22.17200  1.000 16.31737 ? 92  HIS   D CA    1 
ATOM   2059 C  C     . HIS   B 2 93  ? 12.54700  16.70400  23.18700  1.000 17.32605 ? 92  HIS   D C     1 
ATOM   2060 O  O     . HIS   B 2 93  ? 13.20800  17.71300  22.92900  1.000 23.35339 ? 92  HIS   D O     1 
ATOM   2061 C  CB    . HIS   B 2 93  ? 11.96300  16.55400  20.75900  1.000 15.01012 ? 92  HIS   D CB    1 
ATOM   2062 C  CG    . HIS   B 2 93  ? 11.09500  15.98900  19.66200  1.000 13.55744 ? 92  HIS   D CG    1 
ATOM   2063 N  ND1   . HIS   B 2 93  ? 9.84600   16.50100  19.38900  1.000 14.02499 ? 92  HIS   D ND1   1 
ATOM   2064 C  CD2   . HIS   B 2 93  ? 11.26800  14.94600  18.81100  1.000 15.29616 ? 92  HIS   D CD2   1 
ATOM   2065 C  CE1   . HIS   B 2 93  ? 9.29600   15.82700  18.39200  1.000 12.66201 ? 92  HIS   D CE1   1 
ATOM   2066 N  NE2   . HIS   B 2 93  ? 10.13000  14.85800  18.03700  1.000 13.76000 ? 92  HIS   D NE2   1 
ATOM   2067 N  N     . THR   B 2 94  ? 12.59400  16.11100  24.37900  1.000 15.42723 ? 93  THR   D N     1 
ATOM   2068 C  CA    . THR   B 2 94  ? 13.19600  16.78200  25.52700  1.000 17.35613 ? 93  THR   D CA    1 
ATOM   2069 C  C     . THR   B 2 94  ? 14.69300  16.52200  25.69600  1.000 14.87105 ? 93  THR   D C     1 
ATOM   2070 O  O     . THR   B 2 94  ? 15.33900  17.20500  26.49900  1.000 18.08126 ? 93  THR   D O     1 
ATOM   2071 C  CB    . THR   B 2 94  ? 12.48700  16.31300  26.79900  1.000 17.79150 ? 93  THR   D CB    1 
ATOM   2072 O  OG1   . THR   B 2 94  ? 12.35700  14.87200  26.76400  1.000 17.92652 ? 93  THR   D OG1   1 
ATOM   2073 C  CG2   . THR   B 2 94  ? 11.09600  16.97500  26.93200  1.000 18.62148 ? 93  THR   D CG2   1 
ATOM   2074 N  N     . GLY   B 2 95  ? 15.24000  15.51900  25.05100  1.000 14.95691 ? 94  GLY   D N     1 
ATOM   2075 C  CA    . GLY   B 2 95  ? 16.66700  15.33300  25.11700  1.000 16.80959 ? 94  GLY   D CA    1 
ATOM   2076 C  C     . GLY   B 2 95  ? 17.08500  14.05100  24.40900  1.000 16.65518 ? 94  GLY   D C     1 
ATOM   2077 O  O     . GLY   B 2 95  ? 16.28300  13.37300  23.74900  1.000 17.00250 ? 94  GLY   D O     1 
ATOM   2078 N  N     . PRO   B 2 96  ? 18.37300  13.71400  24.52300  1.000 15.64152 ? 95  PRO   D N     1 
ATOM   2079 C  CA    . PRO   B 2 96  ? 18.89900  12.50700  23.86300  1.000 16.03467 ? 95  PRO   D CA    1 
ATOM   2080 C  C     . PRO   B 2 96  ? 18.14500  11.25600  24.28000  1.000 16.06989 ? 95  PRO   D C     1 
ATOM   2081 O  O     . PRO   B 2 96  ? 17.79600  11.07200  25.45700  1.000 17.84021 ? 95  PRO   D O     1 
ATOM   2082 C  CB    . PRO   B 2 96  ? 20.35900  12.44700  24.33500  1.000 17.92013 ? 95  PRO   D CB    1 
ATOM   2083 C  CG    . PRO   B 2 96  ? 20.68100  13.81900  24.88500  1.000 20.36739 ? 95  PRO   D CG    1 
ATOM   2084 C  CD    . PRO   B 2 96  ? 19.37700  14.46100  25.30100  1.000 17.79966 ? 95  PRO   D CD    1 
ATOM   2085 N  N     . GLY   B 2 97  ? 17.88200  10.39700  23.30000  1.000 15.43157 ? 96  GLY   D N     1 
ATOM   2086 C  CA    . GLY   B 2 97  ? 17.21600  9.13200   23.49200  1.000 15.37711 ? 96  GLY   D CA    1 
ATOM   2087 C  C     . GLY   B 2 97  ? 15.74600  9.14000   23.12000  1.000 15.80680 ? 96  GLY   D C     1 
ATOM   2088 O  O     . GLY   B 2 97  ? 15.14000  8.07800   23.06000  1.000 15.44618 ? 96  GLY   D O     1 
ATOM   2089 N  N     . ILE   B 2 98  ? 15.15800  10.29900  22.83900  1.000 14.83980 ? 97  ILE   D N     1 
ATOM   2090 C  CA    . ILE   B 2 98  ? 13.76300  10.33700  22.42500  1.000 15.32665 ? 97  ILE   D CA    1 
ATOM   2091 C  C     . ILE   B 2 98  ? 13.61000  9.65200   21.07200  1.000 13.96496 ? 97  ILE   D C     1 
ATOM   2092 O  O     . ILE   B 2 98  ? 14.42000  9.86900   20.14300  1.000 13.79239 ? 97  ILE   D O     1 
ATOM   2093 C  CB    . ILE   B 2 98  ? 13.31400  11.81300  22.38900  1.000 15.49443 ? 97  ILE   D CB    1 
ATOM   2094 C  CG1   . ILE   B 2 98  ? 13.13800  12.37800  23.81500  1.000 20.48719 ? 97  ILE   D CG1   1 
ATOM   2095 C  CG2   . ILE   B 2 98  ? 12.03100  12.00400  21.52800  1.000 19.15173 ? 97  ILE   D CG2   1 
ATOM   2096 C  CD1   . ILE   B 2 98  ? 11.97200  11.77400  24.56500  1.000 21.21451 ? 97  ILE   D CD1   1 
ATOM   2097 N  N     . LEU   B 2 99  ? 12.55000  8.85600   20.94500  1.000 13.61316 ? 98  LEU   D N     1 
ATOM   2098 C  CA    . LEU   B 2 99  ? 12.18100  8.12800   19.73800  1.000 13.87536 ? 98  LEU   D CA    1 
ATOM   2099 C  C     . LEU   B 2 99  ? 10.90300  8.73900   19.17900  1.000 12.58442 ? 98  LEU   D C     1 
ATOM   2100 O  O     . LEU   B 2 99  ? 9.90300   8.85700   19.89600  1.000 13.83291 ? 98  LEU   D O     1 
ATOM   2101 C  CB    . LEU   B 2 99  ? 11.98900  6.63800   20.08100  1.000 14.26086 ? 98  LEU   D CB    1 
ATOM   2102 C  CG    . LEU   B 2 99  ? 11.47200  5.71300   18.97600  1.000 12.99420 ? 98  LEU   D CG    1 
ATOM   2103 C  CD1   . LEU   B 2 99  ? 12.53500  5.54600   17.88200  1.000 15.40687 ? 98  LEU   D CD1   1 
ATOM   2104 C  CD2   . LEU   B 2 99  ? 11.17000  4.39000   19.60400  1.000 17.17854 ? 98  LEU   D CD2   1 
ATOM   2105 N  N     . SER   B 2 100 ? 10.96600  9.19500   17.92900  1.000 12.56524 ? 99  SER   D N     1 
ATOM   2106 C  CA    . SER   B 2 100 ? 9.90600   9.97500   17.34600  1.000 11.36128 ? 99  SER   D CA    1 
ATOM   2107 C  C     . SER   B 2 100 ? 9.75100   9.62300   15.86900  1.000 13.65443 ? 99  SER   D C     1 
ATOM   2108 O  O     . SER   B 2 100 ? 10.67800  9.07300   15.23800  1.000 13.29892 ? 99  SER   D O     1 
ATOM   2109 C  CB    . SER   B 2 100 ? 10.32800  11.43500  17.51200  1.000 12.57817 ? 99  SER   D CB    1 
ATOM   2110 O  OG    . SER   B 2 100 ? 9.35700   12.30300  16.99900  1.000 14.36536 ? 99  SER   D OG    1 
ATOM   2111 N  N     . MET   B 2 101 ? 8.56200   9.91000   15.30700  1.000 13.03878 ? 100 MET   D N     1 
ATOM   2112 C  CA    . MET   B 2 101 ? 8.32200   9.54300   13.92400  1.000 13.50407 ? 100 MET   D CA    1 
ATOM   2113 C  C     . MET   B 2 101 ? 8.85500   10.59700  12.95800  1.000 14.80014 ? 100 MET   D C     1 
ATOM   2114 O  O     . MET   B 2 101 ? 8.62500   11.79900  13.12600  1.000 15.26164 ? 100 MET   D O     1 
ATOM   2115 C  CB    . MET   B 2 101 ? 6.84000   9.39800   13.64800  1.000 14.50154 ? 100 MET   D CB    1 
ATOM   2116 C  CG    . MET   B 2 101 ? 6.17400   8.24900   14.36000  1.000 15.07902 ? 100 MET   D CG    1 
ATOM   2117 S  SD    . MET   B 2 101 ? 6.92000   6.65500   13.87800  1.000 17.44780 ? 100 MET   D SD    1 
ATOM   2118 C  CE    . MET   B 2 101 ? 6.22700   6.32200   12.26200  1.000 19.89536 ? 100 MET   D CE    1 
ATOM   2119 N  N     . ALA   B 2 102 ? 9.56600   10.14100  11.94400  1.000 13.93667 ? 101 ALA   D N     1 
ATOM   2120 C  CA    . ALA   B 2 102 ? 9.90700   10.98400  10.80900  1.000 14.33139 ? 101 ALA   D CA    1 
ATOM   2121 C  C     . ALA   B 2 102 ? 8.67700   11.09400  9.90000   1.000 14.66183 ? 101 ALA   D C     1 
ATOM   2122 O  O     . ALA   B 2 102 ? 7.76900   10.25300  9.95500   1.000 15.85929 ? 101 ALA   D O     1 
ATOM   2123 C  CB    . ALA   B 2 102 ? 11.07600  10.34000  10.05300  1.000 13.89524 ? 101 ALA   D CB    1 
ATOM   2124 N  N     . ASN   B 2 103 ? 8.59100   12.16900  9.12100   1.000 14.53287 ? 102 ASN   D N     1 
ATOM   2125 C  CA    . ASN   B 2 103 ? 7.42300   12.29600  8.25300   1.000 15.46241 ? 102 ASN   D CA    1 
ATOM   2126 C  C     . ASN   B 2 103 ? 7.73200   13.27200  7.13700   1.000 18.22630 ? 102 ASN   D C     1 
ATOM   2127 O  O     . ASN   B 2 103 ? 8.78300   13.91100  7.11500   1.000 16.94084 ? 102 ASN   D O     1 
ATOM   2128 C  CB    . ASN   B 2 103 ? 6.17900   12.72100  9.06700   1.000 15.94883 ? 102 ASN   D CB    1 
ATOM   2129 C  CG    . ASN   B 2 103 ? 6.34600   14.10000  9.72100   1.000 18.26146 ? 102 ASN   D CG    1 
ATOM   2130 O  OD1   . ASN   B 2 103 ? 6.67800   15.07300  9.05900   1.000 17.60896 ? 102 ASN   D OD1   1 
ATOM   2131 N  ND2   . ASN   B 2 103 ? 6.12400   14.16900  11.02300  1.000 15.88946 ? 102 ASN   D ND2   1 
ATOM   2132 N  N     . ALA   B 2 104 ? 6.79700   13.36900  6.19200   1.000 17.53903 ? 103 ALA   D N     1 
ATOM   2133 C  CA    . ALA   B 2 104 ? 6.89000   14.32100  5.08800   1.000 18.63853 ? 103 ALA   D CA    1 
ATOM   2134 C  C     . ALA   B 2 104 ? 5.86000   15.42500  5.22700   1.000 22.21518 ? 103 ALA   D C     1 
ATOM   2135 O  O     . ALA   B 2 104 ? 5.36800   15.95500  4.22900   1.000 26.21647 ? 103 ALA   D O     1 
ATOM   2136 C  CB    . ALA   B 2 104 ? 6.69600   13.59500  3.76700   1.000 23.21675 ? 103 ALA   D CB    1 
ATOM   2137 N  N     . GLY   B 2 105 ? 5.52800   15.80200  6.46300   1.000 20.30381 ? 104 GLY   D N     1 
ATOM   2138 C  CA    . GLY   B 2 105 ? 4.47500   16.76100  6.68900   1.000 22.59562 ? 104 GLY   D CA    1 
ATOM   2139 C  C     . GLY   B 2 105 ? 3.35900   16.18200  7.53300   1.000 21.96525 ? 104 GLY   D C     1 
ATOM   2140 O  O     . GLY   B 2 105 ? 3.43100   15.03300  7.96900   1.000 20.09994 ? 104 GLY   D O     1 
ATOM   2141 N  N     . PRO   B 2 106 ? 2.32500   16.97500  7.80100   1.000 22.00287 ? 105 PRO   D N     1 
ATOM   2142 C  CA    . PRO   B 2 106 ? 1.24500   16.51200  8.68700   1.000 24.52795 ? 105 PRO   D CA    1 
ATOM   2143 C  C     . PRO   B 2 106 ? 0.61300   15.22000  8.18900   1.000 21.58540 ? 105 PRO   D C     1 
ATOM   2144 O  O     . PRO   B 2 106 ? 0.34800   15.06100  6.99700   1.000 23.40471 ? 105 PRO   D O     1 
ATOM   2145 C  CB    . PRO   B 2 106 ? 0.23600   17.66700  8.63300   1.000 27.37528 ? 105 PRO   D CB    1 
ATOM   2146 C  CG    . PRO   B 2 106 ? 1.09800   18.87600  8.38600   1.000 26.43674 ? 105 PRO   D CG    1 
ATOM   2147 C  CD    . PRO   B 2 106 ? 2.16600   18.38600  7.41200   1.000 21.93445 ? 105 PRO   D CD    1 
ATOM   2148 N  N     . ASN   B 2 107 ? 0.39700   14.28500  9.11800   1.000 19.46615 ? 106 ASN   D N     1 
ATOM   2149 C  CA    . ASN   B 2 107 ? -0.37900  13.06900  8.88100   1.000 20.29545 ? 106 ASN   D CA    1 
ATOM   2150 C  C     . ASN   B 2 107 ? 0.23300   12.18200  7.79200   1.000 21.01831 ? 106 ASN   D C     1 
ATOM   2151 O  O     . ASN   B 2 107 ? -0.46900  11.68200  6.90900   1.000 24.69623 ? 106 ASN   D O     1 
ATOM   2152 C  CB    . ASN   B 2 107 ? -1.83800  13.40200  8.58400   1.000 22.16836 ? 106 ASN   D CB    1 
ATOM   2153 C  CG    . ASN   B 2 107 ? -2.43000  14.26300  9.67300   1.000 25.06310 ? 106 ASN   D CG    1 
ATOM   2154 O  OD1   . ASN   B 2 107 ? -2.39900  13.88000  10.84500  1.000 26.39111 ? 106 ASN   D OD1   1 
ATOM   2155 N  ND2   . ASN   B 2 107 ? -2.91700  15.44600  9.31700   1.000 30.15375 ? 106 ASN   D ND2   1 
ATOM   2156 N  N     . THR   B 2 108 ? 1.55100   12.00200  7.84800   1.000 19.90427 ? 107 THR   D N     1 
ATOM   2157 C  CA    . THR   B 2 108 ? 2.22000   11.15600  6.86300   1.000 20.55264 ? 107 THR   D CA    1 
ATOM   2158 C  C     . THR   B 2 108 ? 3.14600   10.14400  7.54100   1.000 20.81312 ? 107 THR   D C     1 
ATOM   2159 O  O     . THR   B 2 108 ? 4.18100   9.77200   6.98000   1.000 23.84778 ? 107 THR   D O     1 
ATOM   2160 C  CB    . THR   B 2 108 ? 3.00500   11.97800  5.82900   1.000 22.16473 ? 107 THR   D CB    1 
ATOM   2161 O  OG1   . THR   B 2 108 ? 4.06000   12.69900  6.48000   1.000 20.10778 ? 107 THR   D OG1   1 
ATOM   2162 C  CG2   . THR   B 2 108 ? 2.08700   12.91600  4.98600   1.000 22.16235 ? 107 THR   D CG2   1 
ATOM   2163 N  N     . ASN   B 2 109 ? 2.75100   9.63200   8.70100   1.000 20.52829 ? 108 ASN   D N     1 
ATOM   2164 C  CA    . ASN   B 2 109 ? 3.55000   8.63400   9.39800   1.000 19.28395 ? 108 ASN   D CA    1 
ATOM   2165 C  C     . ASN   B 2 109 ? 3.54300   7.31600   8.63700   1.000 18.35523 ? 108 ASN   D C     1 
ATOM   2166 O  O     . ASN   B 2 109 ? 2.49600   6.84400   8.18700   1.000 19.87126 ? 108 ASN   D O     1 
ATOM   2167 C  CB    . ASN   B 2 109 ? 2.98500   8.42200   10.79600  1.000 19.90465 ? 108 ASN   D CB    1 
ATOM   2168 C  CG    . ASN   B 2 109 ? 3.05400   9.66200   11.60900  1.000 17.80856 ? 108 ASN   D CG    1 
ATOM   2169 O  OD1   . ASN   B 2 109 ? 4.14000   10.09400  11.98200  1.000 18.95996 ? 108 ASN   D OD1   1 
ATOM   2170 N  ND2   . ASN   B 2 109 ? 1.89800   10.26300  11.87800  1.000 20.60904 ? 108 ASN   D ND2   1 
ATOM   2171 N  N     . GLY   B 2 110 ? 4.71700   6.72500   8.49100   1.000 16.74782 ? 109 GLY   D N     1 
ATOM   2172 C  CA    . GLY   B 2 110 ? 4.80800   5.42000   7.85800   1.000 18.44468 ? 109 GLY   D CA    1 
ATOM   2173 C  C     . GLY   B 2 110 ? 5.58800   4.49700   8.76700   1.000 18.90732 ? 109 GLY   D C     1 
ATOM   2174 O  O     . GLY   B 2 110 ? 5.04300   3.96500   9.73000   1.000 18.91979 ? 109 GLY   D O     1 
ATOM   2175 N  N     . SER   B 2 111 ? 6.85800   4.28100   8.44500   1.000 16.43585 ? 110 SER   D N     1 
ATOM   2176 C  CA    . SER   B 2 111 ? 7.76700   3.50300   9.27500   1.000 14.94417 ? 110 SER   D CA    1 
ATOM   2177 C  C     . SER   B 2 111 ? 9.01600   4.28100   9.66400   1.000 14.40303 ? 110 SER   D C     1 
ATOM   2178 O  O     . SER   B 2 111 ? 9.69300   3.89000   10.60900  1.000 14.94663 ? 110 SER   D O     1 
ATOM   2179 C  CB    . SER   B 2 111 ? 8.15400   2.18100   8.56700   1.000 16.84698 ? 110 SER   D CB    1 
ATOM   2180 O  OG    . SER   B 2 111 ? 8.80000   2.47900   7.34100   1.000 17.65765 ? 110 SER   D OG    1 
ATOM   2181 N  N     . GLN   B 2 112 ? 9.39000   5.32600   8.94000   1.000 15.38734 ? 111 GLN   D N     1 
ATOM   2182 C  CA    . GLN   B 2 112 ? 10.63100  5.99900   9.29800   1.000 14.02400 ? 111 GLN   D CA    1 
ATOM   2183 C  C     . GLN   B 2 112 ? 10.51600  6.68100   10.66200  1.000 12.97328 ? 111 GLN   D C     1 
ATOM   2184 O  O     . GLN   B 2 112 ? 9.47600   7.22300   11.03700  1.000 14.39436 ? 111 GLN   D O     1 
ATOM   2185 C  CB    . GLN   B 2 112 ? 11.06100  7.00600   8.23700   1.000 12.84142 ? 111 GLN   D CB    1 
ATOM   2186 C  CG    . GLN   B 2 112 ? 11.54400  6.31200   6.94800   1.000 15.10696 ? 111 GLN   D CG    1 
ATOM   2187 C  CD    . GLN   B 2 112 ? 12.31600  7.26500   6.06700   1.000 15.02786 ? 111 GLN   D CD    1 
ATOM   2188 O  OE1   . GLN   B 2 112 ? 13.13900  8.03700   6.55700   1.000 16.57232 ? 111 GLN   D OE1   1 
ATOM   2189 N  NE2   . GLN   B 2 112 ? 12.04600  7.24700   4.77600   1.000 14.76715 ? 111 GLN   D NE2   1 
ATOM   2190 N  N     . PHE   B 2 113 ? 11.62400  6.65300   11.39700  1.000 13.30884 ? 112 PHE   D N     1 
ATOM   2191 C  CA    . PHE   B 2 113 ? 11.66500  7.13800   12.77000  1.000 13.63104 ? 112 PHE   D CA    1 
ATOM   2192 C  C     . PHE   B 2 113 ? 13.04800  7.75200   12.97300  1.000 12.72246 ? 112 PHE   D C     1 
ATOM   2193 O  O     . PHE   B 2 113 ? 13.96800  7.54400   12.17800  1.000 12.63118 ? 112 PHE   D O     1 
ATOM   2194 C  CB    . PHE   B 2 113 ? 11.48500  5.96900   13.75800  1.000 13.66546 ? 112 PHE   D CB    1 
ATOM   2195 C  CG    . PHE   B 2 113 ? 12.58300  4.96700   13.64000  1.000 13.64723 ? 112 PHE   D CG    1 
ATOM   2196 C  CD1   . PHE   B 2 113 ? 12.50000  3.93000   12.72400  1.000 15.36124 ? 112 PHE   D CD1   1 
ATOM   2197 C  CD2   . PHE   B 2 113 ? 13.73400  5.08400   14.43300  1.000 14.54977 ? 112 PHE   D CD2   1 
ATOM   2198 C  CE1   . PHE   B 2 113 ? 13.55600  3.04000   12.58600  1.000 16.32919 ? 112 PHE   D CE1   1 
ATOM   2199 C  CE2   . PHE   B 2 113 ? 14.79900  4.20000   14.28600  1.000 15.85870 ? 112 PHE   D CE2   1 
ATOM   2200 C  CZ    . PHE   B 2 113 ? 14.69900  3.17000   13.33700  1.000 17.51124 ? 112 PHE   D CZ    1 
ATOM   2201 N  N     . PHE   B 2 114 ? 13.21100  8.44400   14.10200  1.000 11.68444 ? 113 PHE   D N     1 
ATOM   2202 C  CA    . PHE   B 2 114 ? 14.51400  8.96600   14.45400  1.000 12.62870 ? 113 PHE   D CA    1 
ATOM   2203 C  C     . PHE   B 2 114 ? 14.69700  8.87400   15.95700  1.000 12.13262 ? 113 PHE   D C     1 
ATOM   2204 O  O     . PHE   B 2 114 ? 13.72900  8.89700   16.74600  1.000 13.29104 ? 113 PHE   D O     1 
ATOM   2205 C  CB    . PHE   B 2 114 ? 14.79700  10.39800  13.91800  1.000 12.86417 ? 113 PHE   D CB    1 
ATOM   2206 C  CG    . PHE   B 2 114 ? 13.86900  11.45300  14.44700  1.000 12.00623 ? 113 PHE   D CG    1 
ATOM   2207 C  CD1   . PHE   B 2 114 ? 12.58000  11.55100  13.95800  1.000 12.03230 ? 113 PHE   D CD1   1 
ATOM   2208 C  CD2   . PHE   B 2 114 ? 14.31300  12.35100  15.45400  1.000 12.54925 ? 113 PHE   D CD2   1 
ATOM   2209 C  CE1   . PHE   B 2 114 ? 11.70900  12.58000  14.44300  1.000 12.97645 ? 113 PHE   D CE1   1 
ATOM   2210 C  CE2   . PHE   B 2 114 ? 13.47900  13.36600  15.91100  1.000 13.34660 ? 113 PHE   D CE2   1 
ATOM   2211 C  CZ    . PHE   B 2 114 ? 12.18100  13.47300  15.41900  1.000 13.21960 ? 113 PHE   D CZ    1 
ATOM   2212 N  N     . ILE   B 2 115 ? 15.96300  8.74300   16.34500  1.000 13.49994 ? 114 ILE   D N     1 
ATOM   2213 C  CA    . ILE   B 2 115 ? 16.38800  8.73300   17.73500  1.000 13.65651 ? 114 ILE   D CA    1 
ATOM   2214 C  C     . ILE   B 2 115 ? 17.18800  10.00400  17.97500  1.000 12.71356 ? 114 ILE   D C     1 
ATOM   2215 O  O     . ILE   B 2 115 ? 18.22700  10.22500  17.34300  1.000 13.70463 ? 114 ILE   D O     1 
ATOM   2216 C  CB    . ILE   B 2 115 ? 17.26200  7.52500   18.04700  1.000 14.18045 ? 114 ILE   D CB    1 
ATOM   2217 C  CG1   . ILE   B 2 115 ? 16.58900  6.21100   17.59800  1.000 14.92299 ? 114 ILE   D CG1   1 
ATOM   2218 C  CG2   . ILE   B 2 115 ? 17.54300  7.56000   19.53300  1.000 15.57973 ? 114 ILE   D CG2   1 
ATOM   2219 C  CD1   . ILE   B 2 115 ? 17.51300  4.99200   17.65000  1.000 17.37137 ? 114 ILE   D CD1   1 
ATOM   2220 N  N     . CYS   B 2 116 ? 16.71000  10.85400  18.86700  1.000 14.58113 ? 115 CYS   D N     1 
ATOM   2221 C  CA    . CYS   B 2 116 ? 17.42100  12.09400  19.14500  1.000 14.13160 ? 115 CYS   D CA    1 
ATOM   2222 C  C     . CYS   B 2 116 ? 18.73500  11.81600  19.86400  1.000 14.87683 ? 115 CYS   D C     1 
ATOM   2223 O  O     . CYS   B 2 116 ? 18.81400  10.97300  20.75500  1.000 16.78501 ? 115 CYS   D O     1 
ATOM   2224 C  CB    . CYS   B 2 116 ? 16.56600  12.99300  20.04000  1.000 16.19262 ? 115 CYS   D CB    1 
ATOM   2225 S  SG    . CYS   B 2 116 ? 15.00500  13.46600  19.25800  1.000 19.49800 ? 115 CYS   D SG    1 
ATOM   2226 N  N     . THR   B 2 117 ? 19.77500  12.55500  19.47600  1.000 15.72020 ? 116 THR   D N     1 
ATOM   2227 C  CA    . THR   B 2 117 ? 21.01000  12.57000  20.24100  1.000 17.13765 ? 116 THR   D CA    1 
ATOM   2228 C  C     . THR   B 2 117 ? 21.21300  13.91000  20.90400  1.000 19.19954 ? 116 THR   D C     1 
ATOM   2229 O  O     . THR   B 2 117 ? 22.31400  14.21800  21.35700  1.000 20.52535 ? 116 THR   D O     1 
ATOM   2230 C  CB    . THR   B 2 117 ? 22.19100  12.16800  19.36400  1.000 17.09007 ? 116 THR   D CB    1 
ATOM   2231 O  OG1   . THR   B 2 117 ? 22.33600  13.11400  18.27700  1.000 18.08001 ? 116 THR   D OG1   1 
ATOM   2232 C  CG2   . THR   B 2 117 ? 21.96200  10.76200  18.81700  1.000 18.41305 ? 116 THR   D CG2   1 
ATOM   2233 N  N     . ALA   B 2 118 ? 20.16000  14.70700  20.95300  1.000 16.73694 ? 117 ALA   D N     1 
ATOM   2234 C  CA    . ALA   B 2 118 ? 20.17200  16.04300  21.53000  1.000 16.87688 ? 117 ALA   D CA    1 
ATOM   2235 C  C     . ALA   B 2 118 ? 18.73400  16.41800  21.84100  1.000 16.20900 ? 117 ALA   D C     1 
ATOM   2236 O  O     . ALA   B 2 118 ? 17.79600  15.77700  21.38000  1.000 17.80454 ? 117 ALA   D O     1 
ATOM   2237 C  CB    . ALA   B 2 118 ? 20.82000  17.06200  20.58200  1.000 20.67300 ? 117 ALA   D CB    1 
ATOM   2238 N  N     . LYS   B 2 119 ? 18.56700  17.48200  22.61000  1.000 17.48358 ? 118 LYS   D N     1 
ATOM   2239 C  CA    . LYS   B 2 119 ? 17.25200  18.10000  22.76500  1.000 16.77762 ? 118 LYS   D CA    1 
ATOM   2240 C  C     . LYS   B 2 119 ? 16.92100  18.78900  21.45000  1.000 21.21784 ? 118 LYS   D C     1 
ATOM   2241 O  O     . LYS   B 2 119 ? 17.73800  19.55800  20.94000  1.000 23.97803 ? 118 LYS   D O     1 
ATOM   2242 C  CB    . LYS   B 2 119 ? 17.30700  19.09800  23.93200  1.000 20.90034 ? 118 LYS   D CB    1 
ATOM   2243 C  CG    . LYS   B 2 119 ? 16.02900  19.89800  24.21900  1.000 23.53613 ? 118 LYS   D CG    1 
ATOM   2244 C  CD    . LYS   B 2 119 ? 16.19200  20.87700  25.38700  1.000 23.79169 ? 118 LYS   D CD    1 
ATOM   2245 C  CE    . LYS   B 2 119 ? 17.02600  22.11900  25.05500  1.000 24.89118 ? 118 LYS   D CE    1 
ATOM   2246 N  NZ    . LYS   B 2 119 ? 16.90800  23.15400  26.14700  1.000 25.96746 ? 118 LYS   D NZ    1 
ATOM   2247 N  N     . THR   B 2 120 ? 15.76500  18.46300  20.86500  1.000 16.87834 ? 119 THR   D N     1 
ATOM   2248 C  CA    . THR   B 2 120 ? 15.37600  18.97000  19.53700  1.000 17.89770 ? 119 THR   D CA    1 
ATOM   2249 C  C     . THR   B 2 120 ? 13.97400  19.57100  19.63300  1.000 18.58953 ? 119 THR   D C     1 
ATOM   2250 O  O     . THR   B 2 120 ? 13.03700  19.14200  18.94900  1.000 17.04886 ? 119 THR   D O     1 
ATOM   2251 C  CB    . THR   B 2 120 ? 15.45600  17.93300  18.40900  1.000 18.11491 ? 119 THR   D CB    1 
ATOM   2252 O  OG1   . THR   B 2 120 ? 14.53000  16.87000  18.68800  1.000 15.96041 ? 119 THR   D OG1   1 
ATOM   2253 C  CG2   . THR   B 2 120 ? 16.85800  17.34200  18.28900  1.000 18.28111 ? 119 THR   D CG2   1 
ATOM   2254 N  N     . GLU   B 2 121 ? 13.84800  20.60500  20.45100  1.000 19.37508 ? 120 GLU   D N     1 
ATOM   2255 C  CA    . GLU   B 2 121 ? 12.53700  21.11500  20.82200  1.000 20.85240 ? 120 GLU   D CA    1 
ATOM   2256 C  C     . GLU   B 2 121 ? 11.79800  21.76300  19.65700  1.000 16.98102 ? 120 GLU   D C     1 
ATOM   2257 O  O     . GLU   B 2 121 ? 10.56900  21.81900  19.67100  1.000 19.33532 ? 120 GLU   D O     1 
ATOM   2258 C  CB    . GLU   B 2 121 ? 12.64800  22.05100  22.03500  1.000 24.80401 ? 120 GLU   D CB    1 
ATOM   2259 C  CG    . GLU   B 2 121 ? 13.30500  23.40300  21.75900  1.000 26.59749 ? 120 GLU   D CG    1 
ATOM   2260 C  CD    . GLU   B 2 121 ? 14.78700  23.37500  21.29800  1.000 31.18128 ? 120 GLU   D CD    1 
ATOM   2261 O  OE1   . GLU   B 2 121 ? 15.57200  22.42600  21.60000  1.000 28.06591 ? 120 GLU   D OE1   1 
ATOM   2262 O  OE2   . GLU   B 2 121 ? 15.18200  24.35800  20.61500  1.000 41.75753 ? 120 GLU   D OE2   1 
ATOM   2263 N  N     . TRP   B 2 122 ? 12.50200  22.19900  18.60600  1.000 16.47376 ? 121 TRP   D N     1 
ATOM   2264 C  CA    . TRP   B 2 122 ? 11.81900  22.78200  17.45400  1.000 17.06804 ? 121 TRP   D CA    1 
ATOM   2265 C  C     . TRP   B 2 122 ? 10.98400  21.77200  16.67000  1.000 16.77185 ? 121 TRP   D C     1 
ATOM   2266 O  O     . TRP   B 2 122 ? 10.17300  22.16900  15.82400  1.000 20.75055 ? 121 TRP   D O     1 
ATOM   2267 C  CB    . TRP   B 2 122 ? 12.83700  23.45200  16.51200  1.000 18.54377 ? 121 TRP   D CB    1 
ATOM   2268 C  CG    . TRP   B 2 122 ? 13.85100  22.45700  15.93700  1.000 16.21644 ? 121 TRP   D CG    1 
ATOM   2269 C  CD1   . TRP   B 2 122 ? 13.75500  21.76600  14.78000  1.000 17.79880 ? 121 TRP   D CD1   1 
ATOM   2270 C  CD2   . TRP   B 2 122 ? 15.07600  22.03700  16.53800  1.000 16.61752 ? 121 TRP   D CD2   1 
ATOM   2271 N  NE1   . TRP   B 2 122 ? 14.82900  20.94600  14.60100  1.000 17.45345 ? 121 TRP   D NE1   1 
ATOM   2272 C  CE2   . TRP   B 2 122 ? 15.67400  21.10200  15.67100  1.000 17.51783 ? 121 TRP   D CE2   1 
ATOM   2273 C  CE3   . TRP   B 2 122 ? 15.74500  22.38600  17.71600  1.000 18.63485 ? 121 TRP   D CE3   1 
ATOM   2274 C  CZ2   . TRP   B 2 122 ? 16.89400  20.47900  15.97300  1.000 16.65821 ? 121 TRP   D CZ2   1 
ATOM   2275 C  CZ3   . TRP   B 2 122 ? 16.93900  21.75300  18.00900  1.000 18.29213 ? 121 TRP   D CZ3   1 
ATOM   2276 C  CH2   . TRP   B 2 122 ? 17.51300  20.84300  17.14400  1.000 17.87620 ? 121 TRP   D CH2   1 
ATOM   2277 N  N     . LEU   B 2 123 ? 11.18100  20.47500  16.90000  1.000 15.09689 ? 122 LEU   D N     1 
ATOM   2278 C  CA    . LEU   B 2 123 ? 10.37200  19.44100  16.26100  1.000 15.85440 ? 122 LEU   D CA    1 
ATOM   2279 C  C     . LEU   B 2 123 ? 9.06700   19.18700  17.01500  1.000 16.98030 ? 122 LEU   D C     1 
ATOM   2280 O  O     . LEU   B 2 123 ? 8.19100   18.47100  16.50100  1.000 16.69102 ? 122 LEU   D O     1 
ATOM   2281 C  CB    . LEU   B 2 123 ? 11.15800  18.13500  16.17400  1.000 15.42920 ? 122 LEU   D CB    1 
ATOM   2282 C  CG    . LEU   B 2 123 ? 12.46400  18.24500  15.36500  1.000 15.69238 ? 122 LEU   D CG    1 
ATOM   2283 C  CD1   . LEU   B 2 123 ? 13.21000  16.91700  15.40700  1.000 16.63885 ? 122 LEU   D CD1   1 
ATOM   2284 C  CD2   . LEU   B 2 123 ? 12.11800  18.69100  13.94900  1.000 18.34792 ? 122 LEU   D CD2   1 
ATOM   2285 N  N     . ASP   B 2 124 ? 8.90900   19.76000  18.20500  1.000 16.32105 ? 123 ASP   D N     1 
ATOM   2286 C  CA    . ASP   B 2 124 ? 7.68900   19.55200  18.99100  1.000 16.74553 ? 123 ASP   D CA    1 
ATOM   2287 C  C     . ASP   B 2 124 ? 6.46900   20.01800  18.19600  1.000 17.88589 ? 123 ASP   D C     1 
ATOM   2288 O  O     . ASP   B 2 124 ? 6.46800   21.08900  17.57500  1.000 19.46865 ? 123 ASP   D O     1 
ATOM   2289 C  CB    . ASP   B 2 124 ? 7.74700   20.33400  20.31500  1.000 16.37031 ? 123 ASP   D CB    1 
ATOM   2290 C  CG    . ASP   B 2 124 ? 8.74100   19.75800  21.32000  1.000 17.89024 ? 123 ASP   D CG    1 
ATOM   2291 O  OD1   . ASP   B 2 124 ? 9.26100   18.63800  21.11400  1.000 18.36653 ? 123 ASP   D OD1   1 
ATOM   2292 O  OD2   . ASP   B 2 124 ? 8.98900   20.47300  22.32600  1.000 20.74734 ? 123 ASP   D OD2   1 
ATOM   2293 N  N     . GLY   B 2 125 ? 5.42100   19.21100  18.21600  1.000 17.36336 ? 124 GLY   D N     1 
ATOM   2294 C  CA    . GLY   B 2 125 ? 4.22200   19.54700  17.48800  1.000 19.00679 ? 124 GLY   D CA    1 
ATOM   2295 C  C     . GLY   B 2 125 ? 4.27400   19.24800  16.01000  1.000 18.17640 ? 124 GLY   D C     1 
ATOM   2296 O  O     . GLY   B 2 125 ? 3.26300   19.45300  15.32400  1.000 22.12376 ? 124 GLY   D O     1 
ATOM   2297 N  N     . LYS   B 2 126 ? 5.38400   18.73700  15.49400  1.000 17.55476 ? 125 LYS   D N     1 
ATOM   2298 C  CA    . LYS   B 2 126 ? 5.45700   18.35400  14.09600  1.000 17.79707 ? 125 LYS   D CA    1 
ATOM   2299 C  C     . LYS   B 2 126 ? 5.81700   16.89800  13.90800  1.000 15.39525 ? 125 LYS   D C     1 
ATOM   2300 O  O     . LYS   B 2 126 ? 5.58800   16.35100  12.82300  1.000 20.33064 ? 125 LYS   D O     1 
ATOM   2301 C  CB    . LYS   B 2 126 ? 6.48500   19.24300  13.37200  1.000 18.91077 ? 125 LYS   D CB    1 
ATOM   2302 C  CG    . LYS   B 2 126 ? 5.93000   20.68000  13.20500  1.000 31.77811 ? 125 LYS   D CG    1 
ATOM   2303 C  CD    . LYS   B 2 126 ? 6.93800   21.66500  12.67300  1.000 41.13639 ? 125 LYS   D CD    1 
ATOM   2304 C  CE    . LYS   B 2 126 ? 6.32000   23.05600  12.67200  1.000 36.81375 ? 125 LYS   D CE    1 
ATOM   2305 N  NZ    . LYS   B 2 126 ? 7.04300   23.96100  11.74100  1.000 49.31546 ? 125 LYS   D NZ    1 
ATOM   2306 N  N     . HIS   B 2 127 ? 6.42400   16.26400  14.89900  1.000 14.77799 ? 126 HIS   D N     1 
ATOM   2307 C  CA    . HIS   B 2 127 ? 6.75000   14.85000  14.86300  1.000 14.58818 ? 126 HIS   D CA    1 
ATOM   2308 C  C     . HIS   B 2 127 ? 6.20100   14.21300  16.12700  1.000 15.88068 ? 126 HIS   D C     1 
ATOM   2309 O  O     . HIS   B 2 127 ? 6.29500   14.80100  17.21600  1.000 16.40679 ? 126 HIS   D O     1 
ATOM   2310 C  CB    . HIS   B 2 127 ? 8.26400   14.70400  14.84300  1.000 13.92376 ? 126 HIS   D CB    1 
ATOM   2311 C  CG    . HIS   B 2 127 ? 8.83700   15.23100  13.58600  1.000 14.75665 ? 126 HIS   D CG    1 
ATOM   2312 N  ND1   . HIS   B 2 127 ? 9.04800   14.44300  12.47500  1.000 15.05506 ? 126 HIS   D ND1   1 
ATOM   2313 C  CD2   . HIS   B 2 127 ? 9.14500   16.49800  13.23000  1.000 16.16138 ? 126 HIS   D CD2   1 
ATOM   2314 C  CE1   . HIS   B 2 127 ? 9.49700   15.21100  11.49200  1.000 15.41641 ? 126 HIS   D CE1   1 
ATOM   2315 N  NE2   . HIS   B 2 127 ? 9.54500   16.46200  11.92100  1.000 16.88068 ? 126 HIS   D NE2   1 
ATOM   2316 N  N     . VAL   B 2 128 ? 5.62000   13.02300  15.99500  1.000 14.37473 ? 127 VAL   D N     1 
ATOM   2317 C  CA    . VAL   B 2 128 ? 4.98500   12.33600  17.12500  1.000 15.05134 ? 127 VAL   D CA    1 
ATOM   2318 C  C     . VAL   B 2 128 ? 6.04400   11.55300  17.90200  1.000 12.31647 ? 127 VAL   D C     1 
ATOM   2319 O  O     . VAL   B 2 128 ? 6.61700   10.59200  17.38700  1.000 13.20135 ? 127 VAL   D O     1 
ATOM   2320 C  CB    . VAL   B 2 128 ? 3.84500   11.41300  16.66900  1.000 15.31063 ? 127 VAL   D CB    1 
ATOM   2321 C  CG1   . VAL   B 2 128 ? 3.28100   10.61000  17.87600  1.000 17.32628 ? 127 VAL   D CG1   1 
ATOM   2322 C  CG2   . VAL   B 2 128 ? 2.73200   12.23600  15.98000  1.000 17.15609 ? 127 VAL   D CG2   1 
ATOM   2323 N  N     . VAL   B 2 129 ? 6.28900   11.96800  19.13900  1.000 13.26475 ? 128 VAL   D N     1 
ATOM   2324 C  CA    . VAL   B 2 129 ? 7.16000   11.25200  20.07000  1.000 13.26439 ? 128 VAL   D CA    1 
ATOM   2325 C  C     . VAL   B 2 129 ? 6.40400   10.06400  20.64700  1.000 13.97797 ? 128 VAL   D C     1 
ATOM   2326 O  O     . VAL   B 2 129 ? 5.27600   10.19800  21.15600  1.000 15.82823 ? 128 VAL   D O     1 
ATOM   2327 C  CB    . VAL   B 2 129 ? 7.59400   12.18000  21.21700  1.000 13.36087 ? 128 VAL   D CB    1 
ATOM   2328 C  CG1   . VAL   B 2 129 ? 8.30500   11.37900  22.30700  1.000 18.07642 ? 128 VAL   D CG1   1 
ATOM   2329 C  CG2   . VAL   B 2 129 ? 8.45500   13.33800  20.67400  1.000 14.76618 ? 128 VAL   D CG2   1 
ATOM   2330 N  N     . PHE   B 2 130 ? 7.02500   8.88600   20.57400  1.000 13.26112 ? 129 PHE   D N     1 
ATOM   2331 C  CA    . PHE   B 2 130 ? 6.32400   7.70100   21.05400  1.000 16.25831 ? 129 PHE   D CA    1 
ATOM   2332 C  C     . PHE   B 2 130 ? 7.20300   6.73400   21.84700  1.000 16.42309 ? 129 PHE   D C     1 
ATOM   2333 O  O     . PHE   B 2 130 ? 6.72100   5.66100   22.23300  1.000 18.02400 ? 129 PHE   D O     1 
ATOM   2334 C  CB    . PHE   B 2 130 ? 5.66700   6.95700   19.88600  1.000 16.93803 ? 129 PHE   D CB    1 
ATOM   2335 C  CG    . PHE   B 2 130 ? 6.66700   6.39900   18.90800  1.000 16.03401 ? 129 PHE   D CG    1 
ATOM   2336 C  CD1   . PHE   B 2 130 ? 7.20500   7.19100   17.88300  1.000 14.16277 ? 129 PHE   D CD1   1 
ATOM   2337 C  CD2   . PHE   B 2 130 ? 7.10200   5.07300   19.03200  1.000 16.30166 ? 129 PHE   D CD2   1 
ATOM   2338 C  CE1   . PHE   B 2 130 ? 8.16300   6.68600   17.01300  1.000 15.20482 ? 129 PHE   D CE1   1 
ATOM   2339 C  CE2   . PHE   B 2 130 ? 8.03500   4.55400   18.15000  1.000 16.58828 ? 129 PHE   D CE2   1 
ATOM   2340 C  CZ    . PHE   B 2 130 ? 8.57400   5.36300   17.14200  1.000 15.49091 ? 129 PHE   D CZ    1 
ATOM   2341 N  N     . GLY   B 2 131 ? 8.45300   7.06100   22.13600  1.000 14.97437 ? 130 GLY   D N     1 
ATOM   2342 C  CA    . GLY   B 2 131 ? 9.23100   6.16100   22.97900  1.000 17.96677 ? 130 GLY   D CA    1 
ATOM   2343 C  C     . GLY   B 2 131 ? 10.50200  6.84100   23.42400  1.000 15.34726 ? 130 GLY   D C     1 
ATOM   2344 O  O     . GLY   B 2 131 ? 10.75600  8.00100   23.09400  1.000 14.77114 ? 130 GLY   D O     1 
ATOM   2345 N  N     . LYS   B 2 132 ? 11.35200  6.08000   24.11700  1.000 15.52347 ? 131 LYS   D N     1 
ATOM   2346 C  CA    . LYS   B 2 132 ? 12.68400  6.58600   24.44100  1.000 16.88923 ? 131 LYS   D CA    1 
ATOM   2347 C  C     . LYS   B 2 132 ? 13.61700  5.40200   24.64900  1.000 17.34527 ? 131 LYS   D C     1 
ATOM   2348 O  O     . LYS   B 2 132 ? 13.18400  4.30300   24.98400  1.000 17.88774 ? 131 LYS   D O     1 
ATOM   2349 C  CB    . LYS   B 2 132 ? 12.66000  7.48800   25.69200  1.000 19.33380 ? 131 LYS   D CB    1 
ATOM   2350 C  CG    . LYS   B 2 132 ? 12.38300  6.74400   26.96800  1.000 24.58067 ? 131 LYS   D CG    1 
ATOM   2351 C  CD    . LYS   B 2 132 ? 12.32500  7.72600   28.14600  1.000 25.35795 ? 131 LYS   D CD    1 
ATOM   2352 C  CE    . LYS   B 2 132 ? 11.87100  7.12500   29.47400  1.000 29.52966 ? 131 LYS   D CE    1 
ATOM   2353 N  NZ    . LYS   B 2 132 ? 11.78900  8.21600   30.49500  1.000 33.84703 ? 131 LYS   D NZ    1 
ATOM   2354 N  N     . VAL   B 2 133 ? 14.91100  5.65000   24.46200  1.000 17.57626 ? 132 VAL   D N     1 
ATOM   2355 C  CA    . VAL   B 2 133 ? 15.93200  4.63000   24.71000  1.000 17.09706 ? 132 VAL   D CA    1 
ATOM   2356 C  C     . VAL   B 2 133 ? 15.91700  4.25400   26.19000  1.000 20.09173 ? 132 VAL   D C     1 
ATOM   2357 O  O     . VAL   B 2 133 ? 15.93700  5.11900   27.08200  1.000 18.88913 ? 132 VAL   D O     1 
ATOM   2358 C  CB    . VAL   B 2 133 ? 17.30600  5.17400   24.29300  1.000 16.14362 ? 132 VAL   D CB    1 
ATOM   2359 C  CG1   . VAL   B 2 133 ? 18.41700  4.19500   24.74000  1.000 17.35063 ? 132 VAL   D CG1   1 
ATOM   2360 C  CG2   . VAL   B 2 133 ? 17.36600  5.34600   22.78100  1.000 16.01132 ? 132 VAL   D CG2   1 
ATOM   2361 N  N     . LYS   B 2 134 ? 15.88900  2.94800   26.45500  1.000 18.75984 ? 133 LYS   D N     1 
ATOM   2362 C  CA    . LYS   B 2 134 ? 15.97000  2.38400   27.79600  1.000 22.77608 ? 133 LYS   D CA    1 
ATOM   2363 C  C     . LYS   B 2 134 ? 17.40800  1.99600   28.10300  1.000 23.47377 ? 133 LYS   D C     1 
ATOM   2364 O  O     . LYS   B 2 134 ? 18.00200  2.49400   29.06300  1.000 29.43370 ? 133 LYS   D O     1 
ATOM   2365 C  CB    . LYS   B 2 134 ? 15.03700  1.17000   27.82400  1.000 26.41261 ? 133 LYS   D CB    1 
ATOM   2366 C  CG    . LYS   B 2 134 ? 14.90200  0.51400   29.18500  1.000 33.29397 ? 133 LYS   D CG    1 
ATOM   2367 C  CD    . LYS   B 2 134 ? 13.86700  -0.60100  29.13500  1.000 32.71992 ? 133 LYS   D CD    1 
ATOM   2368 C  CE    . LYS   B 2 134 ? 12.47300  -0.02900  28.96900  1.000 35.49977 ? 133 LYS   D CE    1 
ATOM   2369 N  NZ    . LYS   B 2 134 ? 11.55700  -0.66400  29.97100  1.000 44.36878 ? 133 LYS   D NZ    1 
ATOM   2370 N  N     . GLU   B 2 135 ? 17.95400  1.07000   27.32800  1.000 23.31617 ? 134 GLU   D N     1 
ATOM   2371 C  CA    . GLU   B 2 135 ? 19.32500  0.62000   27.48600  1.000 23.01928 ? 134 GLU   D CA    1 
ATOM   2372 C  C     . GLU   B 2 135 ? 20.02800  0.85200   26.15600  1.000 22.57431 ? 134 GLU   D C     1 
ATOM   2373 O  O     . GLU   B 2 135 ? 19.39400  0.85600   25.10800  1.000 22.50454 ? 134 GLU   D O     1 
ATOM   2374 C  CB    . GLU   B 2 135 ? 19.35900  -0.86600  27.83200  1.000 25.50660 ? 134 GLU   D CB    1 
ATOM   2375 C  CG    . GLU   B 2 135 ? 18.63000  -1.19600  29.11100  1.000 35.79222 ? 134 GLU   D CG    1 
ATOM   2376 C  CD    . GLU   B 2 135 ? 19.57900  -1.42200  30.25300  1.000 52.99102 ? 134 GLU   D CD    1 
ATOM   2377 O  OE1   . GLU   B 2 135 ? 20.14400  -0.42900  30.76700  1.000 56.15892 ? 134 GLU   D OE1   1 
ATOM   2378 O  OE2   . GLU   B 2 135 ? 19.77800  -2.60000  30.62400  1.000 57.75631 ? 134 GLU   D OE2   1 
ATOM   2379 N  N     . GLY   B 2 136 ? 21.33200  1.08500   26.22300  1.000 24.27664 ? 135 GLY   D N     1 
ATOM   2380 C  CA    . GLY   B 2 136 ? 22.13000  1.19200   25.02200  1.000 23.25735 ? 135 GLY   D CA    1 
ATOM   2381 C  C     . GLY   B 2 136 ? 22.25500  2.57300   24.43100  1.000 21.37508 ? 135 GLY   D C     1 
ATOM   2382 O  O     . GLY   B 2 136 ? 22.51800  2.69700   23.23000  1.000 18.98095 ? 135 GLY   D O     1 
ATOM   2383 N  N     . MET   B 2 137 ? 22.07500  3.64300   25.21900  1.000 19.09009 ? 136 MET   D N     1 
ATOM   2384 C  CA    . MET   B 2 137 ? 22.29700  4.97400   24.65900  1.000 17.87869 ? 136 MET   D CA    1 
ATOM   2385 C  C     . MET   B 2 137 ? 23.73400  5.11300   24.16900  1.000 19.88873 ? 136 MET   D C     1 
ATOM   2386 O  O     . MET   B 2 137 ? 23.99800  5.85700   23.21600  1.000 19.00578 ? 136 MET   D O     1 
ATOM   2387 C  CB    . MET   B 2 137 ? 21.93300  6.05700   25.69000  1.000 19.40477 ? 136 MET   D CB    1 
ATOM   2388 C  CG    . MET   B 2 137 ? 21.90700  7.45600   25.09000  1.000 20.20594 ? 136 MET   D CG    1 
ATOM   2389 S  SD    . MET   B 2 137 ? 20.60700  7.68700   23.87000  1.000 19.99759 ? 136 MET   D SD    1 
ATOM   2390 C  CE    . MET   B 2 137 ? 21.27400  8.98000   22.80200  1.000 19.89489 ? 136 MET   D CE    1 
ATOM   2391 N  N     . ASN   B 2 138 ? 24.64700  4.34600   24.76100  1.000 20.27793 ? 137 ASN   D N     1 
ATOM   2392 C  CA    . ASN   B 2 138 ? 26.04500  4.36200   24.34200  1.000 21.92558 ? 137 ASN   D CA    1 
ATOM   2393 C  C     . ASN   B 2 138 ? 26.19700  3.79200   22.93200  1.000 19.95631 ? 137 ASN   D C     1 
ATOM   2394 O  O     . ASN   B 2 138 ? 27.09700  4.21800   22.20100  1.000 21.15309 ? 137 ASN   D O     1 
ATOM   2395 C  CB    . ASN   B 2 138 ? 26.94500  3.66200   25.37500  1.000 24.57036 ? 137 ASN   D CB    1 
ATOM   2396 C  CG    . ASN   B 2 138 ? 26.64600  2.17800   25.51300  1.000 28.87886 ? 137 ASN   D CG    1 
ATOM   2397 O  OD1   . ASN   B 2 138 ? 25.49100  1.76700   25.56000  1.000 30.58437 ? 137 ASN   D OD1   1 
ATOM   2398 N  ND2   . ASN   B 2 138 ? 27.69500  1.36100   25.58400  1.000 30.42688 ? 137 ASN   D ND2   1 
ATOM   2399 N  N     . ILE   B 2 139 ? 25.30500  2.87200   22.53300  1.000 19.20013 ? 138 ILE   D N     1 
ATOM   2400 C  CA    . ILE   B 2 139 ? 25.29600  2.35300   21.16400  1.000 19.05329 ? 138 ILE   D CA    1 
ATOM   2401 C  C     . ILE   B 2 139 ? 24.82000  3.42900   20.20100  1.000 19.38025 ? 138 ILE   D C     1 
ATOM   2402 O  O     . ILE   B 2 139 ? 25.37800  3.59700   19.11200  1.000 17.24593 ? 138 ILE   D O     1 
ATOM   2403 C  CB    . ILE   B 2 139 ? 24.42100  1.08600   21.09000  1.000 18.35071 ? 138 ILE   D CB    1 
ATOM   2404 C  CG1   . ILE   B 2 139 ? 24.87500  -0.01000  22.05900  1.000 24.31047 ? 138 ILE   D CG1   1 
ATOM   2405 C  CG2   . ILE   B 2 139 ? 24.44600  0.46900   19.70400  1.000 20.27024 ? 138 ILE   D CG2   1 
ATOM   2406 C  CD1   . ILE   B 2 139 ? 26.31100  -0.29700  22.07300  1.000 26.41811 ? 138 ILE   D CD1   1 
ATOM   2407 N  N     . VAL   B 2 140 ? 23.79900  4.19600   20.59900  1.000 17.08412 ? 139 VAL   D N     1 
ATOM   2408 C  CA    . VAL   B 2 140 ? 23.32400  5.29600   19.75900  1.000 17.47223 ? 139 VAL   D CA    1 
ATOM   2409 C  C     . VAL   B 2 140 ? 24.41900  6.34600   19.58100  1.000 16.56442 ? 139 VAL   D C     1 
ATOM   2410 O  O     . VAL   B 2 140 ? 24.63700  6.85200   18.47300  1.000 16.71074 ? 139 VAL   D O     1 
ATOM   2411 C  CB    . VAL   B 2 140 ? 22.00200  5.90000   20.29400  1.000 15.83563 ? 139 VAL   D CB    1 
ATOM   2412 C  CG1   . VAL   B 2 140 ? 21.53000  7.05800   19.37600  1.000 19.41569 ? 139 VAL   D CG1   1 
ATOM   2413 C  CG2   . VAL   B 2 140 ? 20.98100  4.80100   20.38200  1.000 17.30404 ? 139 VAL   D CG2   1 
ATOM   2414 N  N     . GLU   B 2 141 ? 25.13100  6.67300   20.66000  1.000 18.48839 ? 140 GLU   D N     1 
ATOM   2415 C  CA    . GLU   B 2 141 ? 26.22200  7.63700   20.58000  1.000 19.34706 ? 140 GLU   D CA    1 
ATOM   2416 C  C     . GLU   B 2 141 ? 27.32900  7.11800   19.67900  1.000 18.70692 ? 140 GLU   D C     1 
ATOM   2417 O  O     . GLU   B 2 141 ? 27.93500  7.88100   18.91800  1.000 21.72836 ? 140 GLU   D O     1 
ATOM   2418 C  CB    . GLU   B 2 141 ? 26.76900  7.91800   21.99000  1.000 22.16072 ? 140 GLU   D CB    1 
ATOM   2419 C  CG    . GLU   B 2 141 ? 25.72600  8.63200   22.88100  1.000 20.11384 ? 140 GLU   D CG    1 
ATOM   2420 C  CD    . GLU   B 2 141 ? 26.06700  8.61200   24.35500  1.000 29.49469 ? 140 GLU   D CD    1 
ATOM   2421 O  OE1   . GLU   B 2 141 ? 26.99200  7.87000   24.80300  1.000 31.38495 ? 140 GLU   D OE1   1 
ATOM   2422 O  OE2   . GLU   B 2 141 ? 25.36500  9.34900   25.08300  1.000 30.39472 ? 140 GLU   D OE2   1 
ATOM   2423 N  N     . ALA   B 2 142 ? 27.56500  5.80700   19.70700  1.000 17.32366 ? 141 ALA   D N     1 
ATOM   2424 C  CA    . ALA   B 2 142 ? 28.57800  5.23800   18.81700  1.000 17.45940 ? 141 ALA   D CA    1 
ATOM   2425 C  C     . ALA   B 2 142 ? 28.14600  5.32300   17.36100  1.000 16.15438 ? 141 ALA   D C     1 
ATOM   2426 O  O     . ALA   B 2 142 ? 29.00200  5.49000   16.48100  1.000 19.54389 ? 141 ALA   D O     1 
ATOM   2427 C  CB    . ALA   B 2 142 ? 28.88000  3.78600   19.20300  1.000 20.97931 ? 141 ALA   D CB    1 
ATOM   2428 N  N     . MET   B 2 143 ? 26.86300  5.14700   17.08500  1.000 17.26913 ? 142 MET   D N     1 
ATOM   2429 C  CA    . MET   B 2 143 ? 26.39100  5.28900   15.71000  1.000 18.97715 ? 142 MET   D CA    1 
ATOM   2430 C  C     . MET   B 2 143 ? 26.72800  6.66700   15.13400  1.000 21.42607 ? 142 MET   D C     1 
ATOM   2431 O  O     . MET   B 2 143 ? 27.00900  6.78800   13.93600  1.000 19.31363 ? 142 MET   D O     1 
ATOM   2432 C  CB    . MET   B 2 143 ? 24.89900  4.99300   15.62600  1.000 18.38660 ? 142 MET   D CB    1 
ATOM   2433 C  CG    . MET   B 2 143 ? 24.57300  3.54600   16.00700  1.000 20.79244 ? 142 MET   D CG    1 
ATOM   2434 S  SD    . MET   B 2 143 ? 22.81500  3.29800   16.38500  1.000 22.85712 ? 142 MET   D SD    1 
ATOM   2435 C  CE    . MET   B 2 143 ? 22.21000  3.80600   14.78100  1.000 22.06466 ? 142 MET   D CE    1 
ATOM   2436 N  N     . GLU   B 2 144 ? 26.77100  7.71200   15.97700  1.000 24.91632 ? 143 GLU   D N     1 
ATOM   2437 C  CA    . GLU   B 2 144 ? 27.13000  9.05000   15.46700  1.000 27.37526 ? 143 GLU   D CA    1 
ATOM   2438 C  C     . GLU   B 2 144 ? 28.50600  9.14500   14.79300  1.000 32.70717 ? 143 GLU   D C     1 
ATOM   2439 O  O     . GLU   B 2 144 ? 28.69900  9.98200   13.89700  1.000 28.14738 ? 143 GLU   D O     1 
ATOM   2440 C  CB    . GLU   B 2 144 ? 27.06500  10.09900  16.57500  1.000 28.10494 ? 143 GLU   D CB    1 
ATOM   2441 C  CG    . GLU   B 2 144 ? 25.68500  10.31200  17.11700  1.000 26.81363 ? 143 GLU   D CG    1 
ATOM   2442 C  CD    . GLU   B 2 144 ? 25.59100  11.53900  18.03800  1.000 29.35500 ? 143 GLU   D CD    1 
ATOM   2443 O  OE1   . GLU   B 2 144 ? 26.08500  11.46100  19.18500  1.000 29.39824 ? 143 GLU   D OE1   1 
ATOM   2444 O  OE2   . GLU   B 2 144 ? 25.02700  12.57700  17.62500  1.000 30.04808 ? 143 GLU   D OE2   1 
ATOM   2445 N  N     . ARG   B 2 145 ? 29.50400  8.35800   15.22900  1.000 28.03548 ? 144 ARG   D N     1 
ATOM   2446 C  CA    . ARG   B 2 145 ? 30.81800  8.42300   14.59000  1.000 33.35839 ? 144 ARG   D CA    1 
ATOM   2447 C  C     . ARG   B 2 145 ? 30.75800  8.14300   13.09200  1.000 32.50118 ? 144 ARG   D C     1 
ATOM   2448 O  O     . ARG   B 2 145 ? 31.66200  8.55100   12.34700  1.000 33.18680 ? 144 ARG   D O     1 
ATOM   2449 C  CB    . ARG   B 2 145 ? 31.79400  7.45900   15.29300  1.000 34.79534 ? 144 ARG   D CB    1 
ATOM   2450 C  CG    . ARG   B 2 145 ? 33.21100  7.47100   14.73600  1.000 39.37341 ? 144 ARG   D CG    1 
ATOM   2451 C  CD    . ARG   B 2 145 ? 34.15600  6.52100   15.47400  1.000 33.60417 ? 144 ARG   D CD    1 
ATOM   2452 N  NE    . ARG   B 2 145 ? 33.84100  5.10600   15.31800  1.000 33.79318 ? 144 ARG   D NE    1 
ATOM   2453 C  CZ    . ARG   B 2 145 ? 34.44400  4.28900   14.46400  1.000 40.63176 ? 144 ARG   D CZ    1 
ATOM   2454 N  NH1   . ARG   B 2 145 ? 35.32300  4.73500   13.58200  1.000 42.32144 ? 144 ARG   D NH1   1 
ATOM   2455 N  NH2   . ARG   B 2 145 ? 34.17300  2.98700   14.50700  1.000 42.52500 ? 144 ARG   D NH2   1 
ATOM   2456 N  N     . PHE   B 2 146 ? 29.70400  7.46800   12.62800  1.000 23.07298 ? 145 PHE   D N     1 
ATOM   2457 C  CA    . PHE   B 2 146 ? 29.60100  7.07900   11.24400  1.000 25.55421 ? 145 PHE   D CA    1 
ATOM   2458 C  C     . PHE   B 2 146 ? 28.82600  8.08400   10.41100  1.000 25.17897 ? 145 PHE   D C     1 
ATOM   2459 O  O     . PHE   B 2 146 ? 28.73400  7.90400   9.19600   1.000 25.09948 ? 145 PHE   D O     1 
ATOM   2460 C  CB    . PHE   B 2 146 ? 28.98400  5.67900   11.14800  1.000 26.02152 ? 145 PHE   D CB    1 
ATOM   2461 C  CG    . PHE   B 2 146 ? 29.77000  4.63800   11.89400  1.000 24.66212 ? 145 PHE   D CG    1 
ATOM   2462 C  CD1   . PHE   B 2 146 ? 30.87400  4.06900   11.32100  1.000 24.60123 ? 145 PHE   D CD1   1 
ATOM   2463 C  CD2   . PHE   B 2 146 ? 29.39400  4.25100   13.16800  1.000 21.91674 ? 145 PHE   D CD2   1 
ATOM   2464 C  CE1   . PHE   B 2 146 ? 31.60400  3.11100   12.01800  1.000 25.08624 ? 145 PHE   D CE1   1 
ATOM   2465 C  CE2   . PHE   B 2 146 ? 30.09400  3.30700   13.85700  1.000 23.46330 ? 145 PHE   D CE2   1 
ATOM   2466 C  CZ    . PHE   B 2 146 ? 31.19600  2.73700   13.28200  1.000 23.33419 ? 145 PHE   D CZ    1 
ATOM   2467 N  N     . GLY   B 2 147 ? 28.27500  9.12200   11.03800  1.000 22.02915 ? 146 GLY   D N     1 
ATOM   2468 C  CA    . GLY   B 2 147 ? 27.50800  10.12200  10.33100  1.000 20.98294 ? 146 GLY   D CA    1 
ATOM   2469 C  C     . GLY   B 2 147 ? 28.34400  11.30600  9.87100   1.000 22.10502 ? 146 GLY   D C     1 
ATOM   2470 O  O     . GLY   B 2 147 ? 29.57700  11.31200  9.91000   1.000 25.25967 ? 146 GLY   D O     1 
ATOM   2471 N  N     . SER   B 2 148 ? 27.63700  12.32400  9.40100   1.000 19.14857 ? 147 SER   D N     1 
ATOM   2472 C  CA    . SER   B 2 148 ? 28.28900  13.45600  8.76200   1.000 19.17536 ? 147 SER   D CA    1 
ATOM   2473 C  C     . SER   B 2 148 ? 27.26800  14.58500  8.70800   1.000 16.09970 ? 147 SER   D C     1 
ATOM   2474 O  O     . SER   B 2 148 ? 26.08700  14.40000  9.02000   1.000 16.68813 ? 147 SER   D O     1 
ATOM   2475 C  CB    . SER   B 2 148 ? 28.78800  13.11500  7.34700   1.000 19.99633 ? 147 SER   D CB    1 
ATOM   2476 O  OG    . SER   B 2 148 ? 27.68300  12.90100  6.48900   1.000 20.14632 ? 147 SER   D OG    1 
ATOM   2477 N  N     . ARG   B 2 149 ? 27.74400  15.76500  8.25900   1.000 19.69319 ? 148 ARG   D N     1 
ATOM   2478 C  CA    . ARG   B 2 149 ? 26.89900  16.94400  8.29000   1.000 21.47154 ? 148 ARG   D CA    1 
ATOM   2479 C  C     . ARG   B 2 149 ? 25.65000  16.78000  7.42600   1.000 17.74038 ? 148 ARG   D C     1 
ATOM   2480 O  O     . ARG   B 2 149 ? 24.59200  17.30300  7.76600   1.000 19.73732 ? 148 ARG   D O     1 
ATOM   2481 C  CB    . ARG   B 2 149 ? 27.73800  18.14400  7.84400   1.000 23.75383 ? 148 ARG   D CB    1 
ATOM   2482 C  CG    . ARG   B 2 149 ? 27.11400  19.40100  8.25500   1.000 32.07077 ? 148 ARG   D CG    1 
ATOM   2483 C  CD    . ARG   B 2 149 ? 28.10600  20.51200  8.69400   1.000 36.22006 ? 148 ARG   D CD    1 
ATOM   2484 N  NE    . ARG   B 2 149 ? 27.33000  21.74000  8.76400   1.000 33.86367 ? 148 ARG   D NE    1 
ATOM   2485 C  CZ    . ARG   B 2 149 ? 26.86100  22.29600  7.66100   1.000 29.81923 ? 148 ARG   D CZ    1 
ATOM   2486 N  NH1   . ARG   B 2 149 ? 27.21800  21.84400  6.48900   1.000 27.93437 ? 148 ARG   D NH1   1 
ATOM   2487 N  NH2   . ARG   B 2 149 ? 25.99000  23.29700  7.74100   1.000 28.28105 ? 148 ARG   D NH2   1 
ATOM   2488 N  N     . ASN   B 2 150 ? 25.75400  16.08500  6.29800   1.000 18.30867 ? 149 ASN   D N     1 
ATOM   2489 C  CA    . ASN   B 2 150 ? 24.59100  15.84400  5.45300   1.000 20.01553 ? 149 ASN   D CA    1 
ATOM   2490 C  C     . ASN   B 2 150 ? 23.91500  14.53000  5.72900   1.000 21.14705 ? 149 ASN   D C     1 
ATOM   2491 O  O     . ASN   B 2 150 ? 23.02900  14.13000  4.96500   1.000 22.81016 ? 149 ASN   D O     1 
ATOM   2492 C  CB    . ASN   B 2 150 ? 24.90500  15.98600  3.96300   1.000 23.00221 ? 149 ASN   D CB    1 
ATOM   2493 C  CG    . ASN   B 2 150 ? 25.84300  14.90500  3.43800   1.000 25.42511 ? 149 ASN   D CG    1 
ATOM   2494 O  OD1   . ASN   B 2 150 ? 26.18400  13.93000  4.13400   1.000 23.88523 ? 149 ASN   D OD1   1 
ATOM   2495 N  ND2   . ASN   B 2 150 ? 26.28000  15.07400  2.17000   1.000 26.86041 ? 149 ASN   D ND2   1 
ATOM   2496 N  N     . GLY   B 2 151 ? 24.33600  13.83600  6.77800   1.000 16.51555 ? 150 GLY   D N     1 
ATOM   2497 C  CA    . GLY   B 2 151 ? 23.69700  12.59800  7.19300   1.000 16.56652 ? 150 GLY   D CA    1 
ATOM   2498 C  C     . GLY   B 2 151 ? 24.19400  11.34900  6.51600   1.000 17.22371 ? 150 GLY   D C     1 
ATOM   2499 O  O     . GLY   B 2 151 ? 23.86100  10.24900  6.97400   1.000 15.83966 ? 150 GLY   D O     1 
ATOM   2500 N  N     . LYS   B 2 152 ? 25.00500  11.46200  5.46900   1.000 18.43191 ? 151 LYS   D N     1 
ATOM   2501 C  CA    . LYS   B 2 152 ? 25.54700  10.26700  4.82300   1.000 20.28272 ? 151 LYS   D CA    1 
ATOM   2502 C  C     . LYS   B 2 152 ? 26.47700  9.53400   5.77200   1.000 19.42912 ? 151 LYS   D C     1 
ATOM   2503 O  O     . LYS   B 2 152 ? 27.25800  10.15100  6.49800   1.000 19.65759 ? 151 LYS   D O     1 
ATOM   2504 C  CB    . LYS   B 2 152 ? 26.27500  10.65300  3.52900   1.000 23.17377 ? 151 LYS   D CB    1 
ATOM   2505 C  CG    . LYS   B 2 152 ? 25.28900  11.06600  2.48200   1.000 26.27064 ? 151 LYS   D CG    1 
ATOM   2506 C  CD    . LYS   B 2 152 ? 24.25300  9.96900   2.26500   1.000 34.50218 ? 151 LYS   D CD    1 
ATOM   2507 C  CE    . LYS   B 2 152 ? 23.31000  10.30800  1.10500   1.000 42.25704 ? 151 LYS   D CE    1 
ATOM   2508 N  NZ    . LYS   B 2 152 ? 22.02600  9.51900   1.20700   1.000 40.37738 ? 151 LYS   D NZ    1 
ATOM   2509 N  N     . THR   B 2 153 ? 26.37100  8.19700   5.78800   1.000 21.38988 ? 152 THR   D N     1 
ATOM   2510 C  CA    . THR   B 2 153 ? 27.18500  7.39600   6.68700   1.000 21.37315 ? 152 THR   D CA    1 
ATOM   2511 C  C     . THR   B 2 153 ? 28.41000  6.80200   5.99200   1.000 21.53338 ? 152 THR   D C     1 
ATOM   2512 O  O     . THR   B 2 153 ? 28.37700  6.46000   4.80600   1.000 28.82753 ? 152 THR   D O     1 
ATOM   2513 C  CB    . THR   B 2 153 ? 26.36000  6.29300   7.37800   1.000 22.46728 ? 152 THR   D CB    1 
ATOM   2514 O  OG1   . THR   B 2 153 ? 25.86400  5.35800   6.42300   1.000 23.64608 ? 152 THR   D OG1   1 
ATOM   2515 C  CG2   . THR   B 2 153 ? 25.18700  6.90300   8.13600   1.000 21.75610 ? 152 THR   D CG2   1 
ATOM   2516 N  N     . SER   B 2 154 ? 29.48400  6.68000   6.76100   1.000 23.61713 ? 153 SER   D N     1 
ATOM   2517 C  CA    . SER   B 2 154 ? 30.76100  6.20000   6.22600   1.000 23.90610 ? 153 SER   D CA    1 
ATOM   2518 C  C     . SER   B 2 154 ? 30.84000  4.67700   6.14600   1.000 23.98110 ? 153 SER   D C     1 
ATOM   2519 O  O     . SER   B 2 154 ? 31.68300  4.15000   5.40600   1.000 25.14629 ? 153 SER   D O     1 
ATOM   2520 C  CB    . SER   B 2 154 ? 31.93000  6.77000   7.03900   1.000 33.58933 ? 153 SER   D CB    1 
ATOM   2521 O  OG    . SER   B 2 154 ? 31.81200  6.43800   8.40800   1.000 29.59021 ? 153 SER   D OG    1 
ATOM   2522 N  N     . LYS   B 2 155 ? 29.97600  3.97300   6.88500   1.000 25.42596 ? 154 LYS   D N     1 
ATOM   2523 C  CA    . LYS   B 2 155 ? 29.79900  2.52500   6.80900   1.000 24.06660 ? 154 LYS   D CA    1 
ATOM   2524 C  C     . LYS   B 2 155 ? 28.30600  2.28000   6.90100   1.000 20.66302 ? 154 LYS   D C     1 
ATOM   2525 O  O     . LYS   B 2 155 ? 27.53900  3.17100   7.30100   1.000 21.34641 ? 154 LYS   D O     1 
ATOM   2526 C  CB    . LYS   B 2 155 ? 30.53800  1.81200   7.94400   1.000 24.29173 ? 154 LYS   D CB    1 
ATOM   2527 C  CG    . LYS   B 2 155 ? 32.02700  1.98400   7.86700   1.000 26.19735 ? 154 LYS   D CG    1 
ATOM   2528 C  CD    . LYS   B 2 155 ? 32.78400  0.99900   8.72900   1.000 31.22701 ? 154 LYS   D CD    1 
ATOM   2529 C  CE    . LYS   B 2 155 ? 34.26900  1.08800   8.45300   1.000 37.25246 ? 154 LYS   D CE    1 
ATOM   2530 N  NZ    . LYS   B 2 155 ? 35.04900  0.13100   9.26700   1.000 37.19373 ? 154 LYS   D NZ    1 
ATOM   2531 N  N     . LYS   B 2 156 ? 27.87000  1.09400   6.53400   1.000 20.64257 ? 155 LYS   D N     1 
ATOM   2532 C  CA    . LYS   B 2 156 ? 26.44900  0.80000   6.51800   1.000 21.30953 ? 155 LYS   D CA    1 
ATOM   2533 C  C     . LYS   B 2 156 ? 25.98800  0.41300   7.91900   1.000 18.80132 ? 155 LYS   D C     1 
ATOM   2534 O  O     . LYS   B 2 156 ? 26.48200  -0.56700  8.49400   1.000 17.74558 ? 155 LYS   D O     1 
ATOM   2535 C  CB    . LYS   B 2 156 ? 26.09500  -0.28800  5.51500   1.000 24.09254 ? 155 LYS   D CB    1 
ATOM   2536 C  CG    . LYS   B 2 156 ? 24.62300  -0.12400  5.20200   1.000 32.07119 ? 155 LYS   D CG    1 
ATOM   2537 C  CD    . LYS   B 2 156 ? 24.21800  -0.73500  3.89600   1.000 29.05237 ? 155 LYS   D CD    1 
ATOM   2538 C  CE    . LYS   B 2 156 ? 22.70500  -0.76400  3.83000   1.000 27.17522 ? 155 LYS   D CE    1 
ATOM   2539 N  NZ    . LYS   B 2 156 ? 22.33400  -1.30800  2.49600   1.000 43.51968 ? 155 LYS   D NZ    1 
ATOM   2540 N  N     . ILE   B 2 157 ? 25.05500  1.17900   8.45700   1.000 16.71396 ? 156 ILE   D N     1 
ATOM   2541 C  CA    . ILE   B 2 157 ? 24.57100  0.98100   9.82100   1.000 15.93770 ? 156 ILE   D CA    1 
ATOM   2542 C  C     . ILE   B 2 157 ? 23.19100  0.34500   9.72100   1.000 17.64611 ? 156 ILE   D C     1 
ATOM   2543 O  O     . ILE   B 2 157 ? 22.26700  0.95000   9.17700   1.000 17.52781 ? 156 ILE   D O     1 
ATOM   2544 C  CB    . ILE   B 2 157 ? 24.50300  2.30400   10.60400  1.000 15.80491 ? 156 ILE   D CB    1 
ATOM   2545 C  CG1   . ILE   B 2 157 ? 25.82100  3.09000   10.53800  1.000 17.12741 ? 156 ILE   D CG1   1 
ATOM   2546 C  CG2   . ILE   B 2 157 ? 24.08100  2.01700   12.02100  1.000 16.98140 ? 156 ILE   D CG2   1 
ATOM   2547 C  CD1   . ILE   B 2 157 ? 27.06300  2.32600   10.99600  1.000 22.02311 ? 156 ILE   D CD1   1 
ATOM   2548 N  N     . THR   B 2 158 ? 23.05200  -0.91100  10.15500  1.000 16.73458 ? 157 THR   D N     1 
ATOM   2549 C  CA    . THR   B 2 158 ? 21.79900  -1.62100  9.91900   1.000 16.41634 ? 157 THR   D CA    1 
ATOM   2550 C  C     . THR   B 2 158 ? 21.18900  -2.16800  11.20800  1.000 18.22627 ? 157 THR   D C     1 
ATOM   2551 O  O     . THR   B 2 158 ? 21.85900  -2.35600  12.22800  1.000 18.19501 ? 157 THR   D O     1 
ATOM   2552 C  CB    . THR   B 2 158 ? 21.94500  -2.76900  8.93100   1.000 20.00311 ? 157 THR   D CB    1 
ATOM   2553 O  OG1   . THR   B 2 158 ? 22.90500  -3.69600  9.44800   1.000 20.50555 ? 157 THR   D OG1   1 
ATOM   2554 C  CG2   . THR   B 2 158 ? 22.38100  -2.20000  7.59500   1.000 21.28460 ? 157 THR   D CG2   1 
ATOM   2555 N  N     . ILE   B 2 159 ? 19.89200  -2.45700  11.12900  1.000 16.65408 ? 158 ILE   D N     1 
ATOM   2556 C  CA    . ILE   B 2 159 ? 19.19000  -3.19700  12.17400  1.000 17.08379 ? 158 ILE   D CA    1 
ATOM   2557 C  C     . ILE   B 2 159 ? 19.32200  -4.67600  11.81700  1.000 18.34939 ? 158 ILE   D C     1 
ATOM   2558 O  O     . ILE   B 2 159 ? 18.56400  -5.20300  11.00900  1.000 21.58065 ? 158 ILE   D O     1 
ATOM   2559 C  CB    . ILE   B 2 159 ? 17.73800  -2.74900  12.29800  1.000 17.36856 ? 158 ILE   D CB    1 
ATOM   2560 C  CG1   . ILE   B 2 159 ? 17.68800  -1.23500  12.51200  1.000 16.52670 ? 158 ILE   D CG1   1 
ATOM   2561 C  CG2   . ILE   B 2 159 ? 17.02100  -3.51100  13.40000  1.000 20.19776 ? 158 ILE   D CG2   1 
ATOM   2562 C  CD1   . ILE   B 2 159 ? 16.29600  -0.66200  12.46400  1.000 18.84284 ? 158 ILE   D CD1   1 
ATOM   2563 N  N     . ALA   B 2 160 ? 20.35800  -5.33300  12.35400  1.000 17.19042 ? 159 ALA   D N     1 
ATOM   2564 C  CA    . ALA   B 2 160 ? 20.63400  -6.72700  12.01600  1.000 21.28053 ? 159 ALA   D CA    1 
ATOM   2565 C  C     . ALA   B 2 160 ? 19.58700  -7.66500  12.60200  1.000 21.91171 ? 159 ALA   D C     1 
ATOM   2566 O  O     . ALA   B 2 160 ? 19.25300  -8.69200  12.00300  1.000 26.06704 ? 159 ALA   D O     1 
ATOM   2567 C  CB    . ALA   B 2 160 ? 22.00200  -7.12500  12.56700  1.000 20.18588 ? 159 ALA   D CB    1 
ATOM   2568 N  N     . ASP   B 2 161 ? 19.05600  -7.32400  13.77200  1.000 19.96032 ? 160 ASP   D N     1 
ATOM   2569 C  CA    . ASP   B 2 161 ? 17.97400  -8.08400  14.37900  1.000 20.47437 ? 160 ASP   D CA    1 
ATOM   2570 C  C     . ASP   B 2 161 ? 17.13500  -7.08800  15.15800  1.000 19.68574 ? 160 ASP   D C     1 
ATOM   2571 O  O     . ASP   B 2 161 ? 17.61000  -6.03100  15.56400  1.000 19.45357 ? 160 ASP   D O     1 
ATOM   2572 C  CB    . ASP   B 2 161 ? 18.50700  -9.17100  15.33400  1.000 25.45664 ? 160 ASP   D CB    1 
ATOM   2573 C  CG    . ASP   B 2 161 ? 17.48400  -10.28800 15.59800  1.000 33.85553 ? 160 ASP   D CG    1 
ATOM   2574 O  OD1   . ASP   B 2 161 ? 16.39700  -10.31000 14.95400  1.000 26.11316 ? 160 ASP   D OD1   1 
ATOM   2575 O  OD2   . ASP   B 2 161 ? 17.78100  -11.15800 16.46100  1.000 30.71352 ? 160 ASP   D OD2   1 
ATOM   2576 N  N     . CYS   B 2 162 ? 15.88100  -7.45400  15.39500  1.000 20.87234 ? 161 CYS   D N     1 
ATOM   2577 C  CA    . CYS   B 2 162 ? 15.00200  -6.61200  16.18800  1.000 19.66307 ? 161 CYS   D CA    1 
ATOM   2578 C  C     . CYS   B 2 162 ? 13.83500  -7.46600  16.64500  1.000 20.70866 ? 161 CYS   D C     1 
ATOM   2579 O  O     . CYS   B 2 162 ? 13.55000  -8.51200  16.05200  1.000 23.05272 ? 161 CYS   D O     1 
ATOM   2580 C  CB    . CYS   B 2 162 ? 14.54900  -5.33900  15.44400  1.000 20.40504 ? 161 CYS   D CB    1 
ATOM   2581 S  SG    . CYS   B 2 162 ? 13.86800  -5.64200  13.77900  1.000 21.25258 ? 161 CYS   D SG    1 
ATOM   2582 N  N     . GLY   B 2 163 ? 13.18000  -7.01700  17.71200  1.000 21.09757 ? 162 GLY   D N     1 
ATOM   2583 C  CA    . GLY   B 2 163 ? 12.11000  -7.80200  18.29200  1.000 19.67788 ? 162 GLY   D CA    1 
ATOM   2584 C  C     . GLY   B 2 163 ? 11.61200  -7.15100  19.56600  1.000 19.66267 ? 162 GLY   D C     1 
ATOM   2585 O  O     . GLY   B 2 163 ? 11.99000  -6.02900  19.90300  1.000 21.31649 ? 162 GLY   D O     1 
ATOM   2586 N  N     . GLN   B 2 164 ? 10.74100  -7.87200  20.24600  1.000 23.38815 ? 163 GLN   D N     1 
ATOM   2587 C  CA    . GLN   B 2 164 ? 10.11700  -7.38100  21.45800  1.000 21.81086 ? 163 GLN   D CA    1 
ATOM   2588 C  C     . GLN   B 2 164 ? 10.67000  -8.18500  22.62300  1.000 24.41642 ? 163 GLN   D C     1 
ATOM   2589 O  O     . GLN   B 2 164 ? 10.75800  -9.41500  22.54800  1.000 30.11506 ? 163 GLN   D O     1 
ATOM   2590 C  CB    . GLN   B 2 164 ? 8.60600   -7.58500  21.36400  1.000 26.06511 ? 163 GLN   D CB    1 
ATOM   2591 C  CG    . GLN   B 2 164 ? 7.87800   -7.09200  22.60400  1.000 25.99370 ? 163 GLN   D CG    1 
ATOM   2592 C  CD    . GLN   B 2 164 ? 6.38400   -6.99400  22.42200  1.000 29.17907 ? 163 GLN   D CD    1 
ATOM   2593 O  OE1   . GLN   B 2 164 ? 5.83500   -7.35400  21.38300  1.000 27.55455 ? 163 GLN   D OE1   1 
ATOM   2594 N  NE2   . GLN   B 2 164 ? 5.71700   -6.48700  23.43900  1.000 25.01924 ? 163 GLN   D NE2   1 
ATOM   2595 N  N     . LEU   B 2 165 ? 11.04500  -7.48800  23.68900  1.000 26.41390 ? 164 LEU   D N     1 
ATOM   2596 C  CA    . LEU   B 2 165 ? 11.50100  -8.11500  24.92700  1.000 28.35764 ? 164 LEU   D CA    1 
ATOM   2597 C  C     . LEU   B 2 165 ? 10.35800  -8.30600  25.90200  1.000 33.38748 ? 164 LEU   D C     1 
ATOM   2598 O  O     . LEU   B 2 165 ? 9.40300   -7.55100  25.90000  1.000 33.97731 ? 164 LEU   D O     1 
ATOM   2599 C  CB    . LEU   B 2 165 ? 12.58100  -7.24000  25.54900  1.000 34.71164 ? 164 LEU   D CB    1 
ATOM   2600 C  CG    . LEU   B 2 165 ? 13.78200  -6.97900  24.63800  1.000 31.39626 ? 164 LEU   D CG    1 
ATOM   2601 C  CD1   . LEU   B 2 165 ? 14.75000  -6.03600  25.32600  1.000 34.94911 ? 164 LEU   D CD1   1 
ATOM   2602 C  CD2   . LEU   B 2 165 ? 14.45800  -8.27800  24.31900  1.000 33.60256 ? 164 LEU   D CD2   1 
ATOM   2603 N  N     . SER   C 1 1   ? -14.54500 12.18200  36.20000  1.000 42.80206 ? 0   SER   B N     1 
ATOM   2604 C  CA    . SER   C 1 1   ? -14.42000 12.83100  37.50600  1.000 37.58134 ? 0   SER   B CA    1 
ATOM   2605 C  C     . SER   C 1 1   ? -13.12000 13.64800  37.60500  1.000 33.17875 ? 0   SER   B C     1 
ATOM   2606 O  O     . SER   C 1 1   ? -12.39900 13.80500  36.63100  1.000 39.46770 ? 0   SER   B O     1 
ATOM   2607 C  CB    . SER   C 1 1   ? -14.46000 11.78100  38.62400  1.000 40.82612 ? 0   SER   B CB    1 
ATOM   2608 O  OG    . SER   C 1 1   ? -13.15100 11.44300  39.07100  1.000 45.52771 ? 0   SER   B OG    1 
ATOM   2609 N  N     . MET   C 1 2   ? -12.82100 14.15500  38.79000  1.000 31.63127 ? 1   MET   B N     1 
ATOM   2610 C  CA    . MET   C 1 2   ? -11.59500 14.89400  39.01900  1.000 28.54868 ? 1   MET   B CA    1 
ATOM   2611 C  C     . MET   C 1 2   ? -10.54100 13.99700  39.65200  1.000 24.43972 ? 1   MET   B C     1 
ATOM   2612 O  O     . MET   C 1 2   ? -10.83200 12.91300  40.17400  1.000 26.41821 ? 1   MET   B O     1 
ATOM   2613 C  CB    . MET   C 1 2   ? -11.84300 16.06900  39.97000  1.000 29.10033 ? 1   MET   B CB    1 
ATOM   2614 C  CG    . MET   C 1 2   ? -12.81800 17.10700  39.48400  1.000 29.52319 ? 1   MET   B CG    1 
ATOM   2615 S  SD    . MET   C 1 2   ? -12.77100 18.56700  40.57100  1.000 35.98919 ? 1   MET   B SD    1 
ATOM   2616 C  CE    . MET   C 1 2   ? -11.15500 19.15800  40.22300  1.000 38.55703 ? 1   MET   B CE    1 
ATOM   2617 N  N     . THR   C 1 3   ? -9.30600  14.48600  39.62300  1.000 22.55883 ? 2   THR   B N     1 
ATOM   2618 C  CA    . THR   C 1 3   ? -8.21000  13.91400  40.37700  1.000 23.65184 ? 2   THR   B CA    1 
ATOM   2619 C  C     . THR   C 1 3   ? -7.53000  15.06400  41.10600  1.000 24.06718 ? 2   THR   B C     1 
ATOM   2620 O  O     . THR   C 1 3   ? -7.80800  16.23000  40.82700  1.000 22.96758 ? 2   THR   B O     1 
ATOM   2621 C  CB    . THR   C 1 3   ? -7.21800  13.20100  39.45800  1.000 23.99342 ? 2   THR   B CB    1 
ATOM   2622 O  OG1   . THR   C 1 3   ? -6.95700  14.01100  38.30000  1.000 27.04217 ? 2   THR   B OG1   1 
ATOM   2623 C  CG2   . THR   C 1 3   ? -7.77000  11.80800  39.03400  1.000 29.67385 ? 2   THR   B CG2   1 
ATOM   2624 N  N     . GLU   C 1 4   ? -6.63000  14.73500  42.03400  1.000 20.78340 ? 3   GLU   B N     1 
ATOM   2625 C  CA    . GLU   C 1 4   ? -5.88800  15.73300  42.79900  1.000 18.95544 ? 3   GLU   B CA    1 
ATOM   2626 C  C     . GLU   C 1 4   ? -4.51200  15.16300  43.12600  1.000 17.82084 ? 3   GLU   B C     1 
ATOM   2627 O  O     . GLU   C 1 4   ? -4.39300  13.96500  43.40100  1.000 20.91496 ? 3   GLU   B O     1 
ATOM   2628 C  CB    . GLU   C 1 4   ? -6.69200  16.12000  44.06100  1.000 18.90131 ? 3   GLU   B CB    1 
ATOM   2629 C  CG    . GLU   C 1 4   ? -5.95200  17.08400  44.97100  1.000 19.29817 ? 3   GLU   B CG    1 
ATOM   2630 C  CD    . GLU   C 1 4   ? -6.87100  17.77900  45.97400  1.000 21.24162 ? 3   GLU   B CD    1 
ATOM   2631 O  OE1   . GLU   C 1 4   ? -8.03300  17.40300  46.08900  1.000 21.64281 ? 3   GLU   B OE1   1 
ATOM   2632 O  OE2   . GLU   C 1 4   ? -6.42900  18.74300  46.61600  1.000 21.72219 ? 3   GLU   B OE2   1 
ATOM   2633 N  N     . TYR   C 1 5   ? -3.47700  16.00300  43.08500  1.000 16.88708 ? 4   TYR   B N     1 
ATOM   2634 C  CA    . TYR   C 1 5   ? -2.10500  15.55800  43.28200  1.000 16.86680 ? 4   TYR   B CA    1 
ATOM   2635 C  C     . TYR   C 1 5   ? -1.37500  16.53500  44.17500  1.000 18.14765 ? 4   TYR   B C     1 
ATOM   2636 O  O     . TYR   C 1 5   ? -1.48800  17.74600  43.98100  1.000 17.20503 ? 4   TYR   B O     1 
ATOM   2637 C  CB    . TYR   C 1 5   ? -1.35300  15.47000  41.93100  1.000 18.44924 ? 4   TYR   B CB    1 
ATOM   2638 C  CG    . TYR   C 1 5   ? -2.08900  14.58300  41.00800  1.000 18.75666 ? 4   TYR   B CG    1 
ATOM   2639 C  CD1   . TYR   C 1 5   ? -1.98400  13.21500  41.12700  1.000 20.38565 ? 4   TYR   B CD1   1 
ATOM   2640 C  CD2   . TYR   C 1 5   ? -2.97400  15.09400  40.06100  1.000 18.38870 ? 4   TYR   B CD2   1 
ATOM   2641 C  CE1   . TYR   C 1 5   ? -2.73400  12.35500  40.30300  1.000 21.40706 ? 4   TYR   B CE1   1 
ATOM   2642 C  CE2   . TYR   C 1 5   ? -3.71700  14.25900  39.24200  1.000 20.09106 ? 4   TYR   B CE2   1 
ATOM   2643 C  CZ    . TYR   C 1 5   ? -3.58700  12.88700  39.36200  1.000 20.52572 ? 4   TYR   B CZ    1 
ATOM   2644 O  OH    . TYR   C 1 5   ? -4.33500  12.06600  38.54200  1.000 23.54478 ? 4   TYR   B OH    1 
ATOM   2645 N  N     . LYS   C 1 6   ? -0.58900  16.01900  45.11500  1.000 17.65682 ? 5   LYS   B N     1 
ATOM   2646 C  CA    . LYS   C 1 6   ? 0.29400   16.81900  45.95700  1.000 17.35717 ? 5   LYS   B CA    1 
ATOM   2647 C  C     . LYS   C 1 6   ? 1.69900   16.78600  45.36300  1.000 15.82434 ? 5   LYS   B C     1 
ATOM   2648 O  O     . LYS   C 1 6   ? 2.37900   15.75600  45.41600  1.000 16.76218 ? 5   LYS   B O     1 
ATOM   2649 C  CB    . LYS   C 1 6   ? 0.29800   16.25400  47.37900  1.000 20.50459 ? 5   LYS   B CB    1 
ATOM   2650 C  CG    . LYS   C 1 6   ? -1.06200  16.31200  48.05200  1.000 26.77865 ? 5   LYS   B CG    1 
ATOM   2651 C  CD    . LYS   C 1 6   ? -1.01700  15.96400  49.53800  1.000 34.26249 ? 5   LYS   B CD    1 
ATOM   2652 C  CE    . LYS   C 1 6   ? -1.15300  14.46800  49.77300  1.000 42.65953 ? 5   LYS   B CE    1 
ATOM   2653 N  NZ    . LYS   C 1 6   ? -2.51200  13.94800  49.42000  1.000 44.28607 ? 5   LYS   B NZ    1 
ATOM   2654 N  N     . LEU   C 1 7   ? 2.13200   17.90700  44.81400  1.000 14.45543 ? 6   LEU   B N     1 
ATOM   2655 C  CA    . LEU   C 1 7   ? 3.43000   18.01500  44.14300  1.000 14.87653 ? 6   LEU   B CA    1 
ATOM   2656 C  C     . LEU   C 1 7   ? 4.35500   18.85300  45.00800  1.000 17.41176 ? 6   LEU   B C     1 
ATOM   2657 O  O     . LEU   C 1 7   ? 3.92700   19.85700  45.57800  1.000 17.87587 ? 6   LEU   B O     1 
ATOM   2658 C  CB    . LEU   C 1 7   ? 3.29000   18.69500  42.77800  1.000 15.70049 ? 6   LEU   B CB    1 
ATOM   2659 C  CG    . LEU   C 1 7   ? 2.22300   18.12300  41.86400  1.000 14.99039 ? 6   LEU   B CG    1 
ATOM   2660 C  CD1   . LEU   C 1 7   ? 2.24600   18.85500  40.51800  1.000 18.21036 ? 6   LEU   B CD1   1 
ATOM   2661 C  CD2   . LEU   C 1 7   ? 2.41300   16.62600  41.64600  1.000 16.89043 ? 6   LEU   B CD2   1 
ATOM   2662 N  N     . VAL   C 1 8   ? 5.61800   18.45100  45.11200  1.000 14.05336 ? 7   VAL   B N     1 
ATOM   2663 C  CA    . VAL   C 1 8   ? 6.58000   19.13600  45.95700  1.000 14.81881 ? 7   VAL   B CA    1 
ATOM   2664 C  C     . VAL   C 1 8   ? 7.77000   19.49900  45.09100  1.000 15.54307 ? 7   VAL   B C     1 
ATOM   2665 O  O     . VAL   C 1 8   ? 8.28500   18.64100  44.37100  1.000 16.22717 ? 7   VAL   B O     1 
ATOM   2666 C  CB    . VAL   C 1 8   ? 7.00100   18.24400  47.12500  1.000 15.70420 ? 7   VAL   B CB    1 
ATOM   2667 C  CG1   . VAL   C 1 8   ? 8.00600   18.97400  48.00700  1.000 16.94722 ? 7   VAL   B CG1   1 
ATOM   2668 C  CG2   . VAL   C 1 8   ? 5.76600   17.84100  47.94400  1.000 17.17886 ? 7   VAL   B CG2   1 
ATOM   2669 N  N     . VAL   C 1 9   ? 8.20600   20.75200  45.16500  1.000 14.10924 ? 8   VAL   B N     1 
ATOM   2670 C  CA    . VAL   C 1 9   ? 9.31900   21.25000  44.35500  1.000 15.27926 ? 8   VAL   B CA    1 
ATOM   2671 C  C     . VAL   C 1 9   ? 10.54100  21.41000  45.25800  1.000 15.00735 ? 8   VAL   B C     1 
ATOM   2672 O  O     . VAL   C 1 9   ? 10.49100  22.15800  46.25100  1.000 15.13749 ? 8   VAL   B O     1 
ATOM   2673 C  CB    . VAL   C 1 9   ? 8.95700   22.59000  43.69600  1.000 14.19839 ? 8   VAL   B CB    1 
ATOM   2674 C  CG1   . VAL   C 1 9   ? 10.02200  22.99700  42.70200  1.000 15.80616 ? 8   VAL   B CG1   1 
ATOM   2675 C  CG2   . VAL   C 1 9   ? 7.63500   22.53200  42.92400  1.000 15.02927 ? 8   VAL   B CG2   1 
ATOM   2676 N  N     . VAL   C 1 10  ? 11.63700  20.69400  44.94800  1.000 14.74704 ? 9   VAL   B N     1 
ATOM   2677 C  CA    . VAL   C 1 10  ? 12.85300  20.70100  45.75200  1.000 14.36491 ? 9   VAL   B CA    1 
ATOM   2678 C  C     . VAL   C 1 10  ? 14.05500  21.00400  44.86200  1.000 15.06216 ? 9   VAL   B C     1 
ATOM   2679 O  O     . VAL   C 1 10  ? 14.00300  20.88500  43.63100  1.000 16.58637 ? 9   VAL   B O     1 
ATOM   2680 C  CB    . VAL   C 1 10  ? 13.07400  19.38200  46.52000  1.000 16.16048 ? 9   VAL   B CB    1 
ATOM   2681 C  CG1   . VAL   C 1 10  ? 11.85600  19.05600  47.39600  1.000 19.84089 ? 9   VAL   B CG1   1 
ATOM   2682 C  CG2   . VAL   C 1 10  ? 13.43900  18.22400  45.54000  1.000 18.71359 ? 9   VAL   B CG2   1 
ATOM   2683 N  N     . GLY   C 1 11  ? 15.14200  21.37900  45.51800  1.000 15.34340 ? 10  GLY   B N     1 
ATOM   2684 C  CA    . GLY   C 1 11  ? 16.36000  21.72400  44.78700  1.000 18.39540 ? 10  GLY   B CA    1 
ATOM   2685 C  C     . GLY   C 1 11  ? 17.11800  22.82100  45.49000  1.000 17.31102 ? 10  GLY   B C     1 
ATOM   2686 O  O     . GLY   C 1 11  ? 16.56100  23.44600  46.39300  1.000 19.57930 ? 10  GLY   B O     1 
ATOM   2687 N  N     . ALA   C 1 12  ? 18.34600  23.06100  45.05600  1.000 18.70170 ? 11  ALA   B N     1 
ATOM   2688 C  CA    . ALA   C 1 12  ? 19.21400  24.05100  45.71600  1.000 17.69130 ? 11  ALA   B CA    1 
ATOM   2689 C  C     . ALA   C 1 12  ? 18.66000  25.46900  45.65600  1.000 19.06664 ? 11  ALA   B C     1 
ATOM   2690 O  O     . ALA   C 1 12  ? 17.78800  25.79400  44.86500  1.000 17.95354 ? 11  ALA   B O     1 
ATOM   2691 C  CB    . ALA   C 1 12  ? 20.58200  23.99400  45.08500  1.000 21.68015 ? 11  ALA   B CB    1 
ATOM   2692 N  N     . CYS   C 1 13  ? 19.23200  26.30900  46.49100  1.000 19.87732 ? 12  CYS   B N     1 
ATOM   2693 C  CA    . CYS   C 1 13  ? 18.83200  27.72700  46.52000  1.000 22.16819 ? 12  CYS   B CA    1 
ATOM   2694 C  C     . CYS   C 1 13  ? 19.05000  28.43100  45.17400  1.000 20.33394 ? 12  CYS   B C     1 
ATOM   2695 O  O     . CYS   C 1 13  ? 20.07100  28.17500  44.52400  1.000 23.71213 ? 12  CYS   B O     1 
ATOM   2696 C  CB    . CYS   C 1 13  ? 19.64600  28.47100  47.56400  1.000 24.50877 ? 12  CYS   B CB    1 
ATOM   2697 S  SG    . CYS   C 1 13  ? 21.42300  28.52100  47.21500  1.000 33.09639 ? 12  CYS   B SG    1 
ATOM   2698 N  N     . GLY   C 1 14  ? 18.09400  29.25500  44.77400  1.000 18.84890 ? 13  GLY   B N     1 
ATOM   2699 C  CA    . GLY   C 1 14  ? 18.25000  30.07800  43.56400  1.000 19.25745 ? 13  GLY   B CA    1 
ATOM   2700 C  C     . GLY   C 1 14  ? 18.09900  29.36500  42.22400  1.000 19.16580 ? 13  GLY   B C     1 
ATOM   2701 O  O     . GLY   C 1 14  ? 18.32000  30.03200  41.22900  1.000 21.41779 ? 13  GLY   B O     1 
ATOM   2702 N  N     . VAL   C 1 15  ? 17.69100  28.10100  42.20000  1.000 18.86631 ? 14  VAL   B N     1 
ATOM   2703 C  CA    . VAL   C 1 15  ? 17.63600  27.35500  40.90800  1.000 16.78974 ? 14  VAL   B CA    1 
ATOM   2704 C  C     . VAL   C 1 15  ? 16.37000  27.74200  40.12500  1.000 19.11992 ? 14  VAL   B C     1 
ATOM   2705 O  O     . VAL   C 1 15  ? 16.32800  27.47200  38.93000  1.000 18.14171 ? 14  VAL   B O     1 
ATOM   2706 C  CB    . VAL   C 1 15  ? 17.72400  25.83100  41.09200  1.000 17.81556 ? 14  VAL   B CB    1 
ATOM   2707 C  CG1   . VAL   C 1 15  ? 19.04300  25.41800  41.72300  1.000 19.07576 ? 14  VAL   B CG1   1 
ATOM   2708 C  CG2   . VAL   C 1 15  ? 16.55500  25.28100  41.89600  1.000 18.15975 ? 14  VAL   B CG2   1 
ATOM   2709 N  N     . GLY   C 1 16  ? 15.38800  28.31900  40.80500  1.000 17.49721 ? 15  GLY   B N     1 
ATOM   2710 C  CA    . GLY   C 1 16  ? 14.15000  28.69200  40.15800  1.000 14.66632 ? 15  GLY   B CA    1 
ATOM   2711 C  C     . GLY   C 1 16  ? 12.91600  27.91600  40.57500  1.000 14.82128 ? 15  GLY   B C     1 
ATOM   2712 O  O     . GLY   C 1 16  ? 11.92800  27.91000  39.81700  1.000 16.09193 ? 15  GLY   B O     1 
ATOM   2713 N  N     . LYS   C 1 17  ? 12.91800  27.25700  41.72100  1.000 15.22525 ? 16  LYS   B N     1 
ATOM   2714 C  CA    . LYS   C 1 17  ? 11.72200  26.52300  42.18200  1.000 14.78968 ? 16  LYS   B CA    1 
ATOM   2715 C  C     . LYS   C 1 17  ? 10.50300  27.45000  42.23000  1.000 14.70639 ? 16  LYS   B C     1 
ATOM   2716 O  O     . LYS   C 1 17  ? 9.45200   27.08600  41.71100  1.000 14.73169 ? 16  LYS   B O     1 
ATOM   2717 C  CB    . LYS   C 1 17  ? 12.01100  25.97400  43.57800  1.000 15.18700 ? 16  LYS   B CB    1 
ATOM   2718 C  CG    . LYS   C 1 17  ? 13.14900  24.96700  43.62600  1.000 16.18696 ? 16  LYS   B CG    1 
ATOM   2719 C  CD    . LYS   C 1 17  ? 13.36900  24.37000  45.00800  1.000 17.91584 ? 16  LYS   B CD    1 
ATOM   2720 C  CE    . LYS   C 1 17  ? 13.79400  25.38100  46.01800  1.000 15.40826 ? 16  LYS   B CE    1 
ATOM   2721 N  NZ    . LYS   C 1 17  ? 15.10600  25.96800  45.73400  1.000 16.56734 ? 16  LYS   B NZ    1 
ATOM   2722 N  N     . SER   C 1 18  ? 10.66100  28.59200  42.87200  1.000 14.59122 ? 17  SER   B N     1 
ATOM   2723 C  CA    . SER   C 1 18  ? 9.54200   29.51400  43.00700  1.000 14.48324 ? 17  SER   B CA    1 
ATOM   2724 C  C     . SER   C 1 18  ? 9.17100   30.11300  41.66200  1.000 15.47151 ? 17  SER   B C     1 
ATOM   2725 O  O     . SER   C 1 18  ? 7.98400   30.22000  41.32600  1.000 16.13948 ? 17  SER   B O     1 
ATOM   2726 C  CB    . SER   C 1 18  ? 9.89000   30.61300  43.99800  1.000 15.85944 ? 17  SER   B CB    1 
ATOM   2727 O  OG    . SER   C 1 18  ? 10.07900  30.03600  45.27800  1.000 15.97886 ? 17  SER   B OG    1 
ATOM   2728 N  N     . ALA   C 1 19  ? 10.16900  30.44800  40.85100  1.000 15.88279 ? 18  ALA   B N     1 
ATOM   2729 C  CA    . ALA   C 1 19  ? 9.83900   31.05000  39.56000  1.000 14.35692 ? 18  ALA   B CA    1 
ATOM   2730 C  C     . ALA   C 1 19  ? 9.06700   30.06000  38.69400  1.000 15.37698 ? 18  ALA   B C     1 
ATOM   2731 O  O     . ALA   C 1 19  ? 8.12100   30.44200  38.00600  1.000 16.55089 ? 18  ALA   B O     1 
ATOM   2732 C  CB    . ALA   C 1 19  ? 11.10700  31.55000  38.84700  1.000 17.15574 ? 18  ALA   B CB    1 
ATOM   2733 N  N     . LEU   C 1 20  ? 9.42400   28.76200  38.74700  1.000 13.91396 ? 19  LEU   B N     1 
ATOM   2734 C  CA    . LEU   C 1 20  ? 8.68600   27.78800  37.94500  1.000 15.04917 ? 19  LEU   B CA    1 
ATOM   2735 C  C     . LEU   C 1 20  ? 7.25800   27.65500  38.44800  1.000 15.62433 ? 19  LEU   B C     1 
ATOM   2736 O  O     . LEU   C 1 20  ? 6.31100   27.63700  37.66400  1.000 16.16455 ? 19  LEU   B O     1 
ATOM   2737 C  CB    . LEU   C 1 20  ? 9.37600   26.42200  38.04500  1.000 15.70659 ? 19  LEU   B CB    1 
ATOM   2738 C  CG    . LEU   C 1 20  ? 10.63600  26.30000  37.20200  1.000 15.71886 ? 19  LEU   B CG    1 
ATOM   2739 C  CD1   . LEU   C 1 20  ? 11.27700  25.00000  37.59500  1.000 19.73220 ? 19  LEU   B CD1   1 
ATOM   2740 C  CD2   . LEU   C 1 20  ? 10.30400  26.35600  35.70200  1.000 17.75755 ? 19  LEU   B CD2   1 
ATOM   2741 N  N     . THR   C 1 21  ? 7.09600   27.61900  39.77100  1.000 16.15337 ? 20  THR   B N     1 
ATOM   2742 C  CA    . THR   C 1 21  ? 5.78000   27.44800  40.36400  1.000 16.72138 ? 20  THR   B CA    1 
ATOM   2743 C  C     . THR   C 1 21  ? 4.90200   28.66200  40.10000  1.000 16.34964 ? 20  THR   B C     1 
ATOM   2744 O  O     . THR   C 1 21  ? 3.74200   28.52100  39.70800  1.000 16.26785 ? 20  THR   B O     1 
ATOM   2745 C  CB    . THR   C 1 21  ? 5.94700   27.23900  41.86000  1.000 15.79798 ? 20  THR   B CB    1 
ATOM   2746 O  OG1   . THR   C 1 21  ? 6.74400   26.05800  42.12000  1.000 18.42202 ? 20  THR   B OG1   1 
ATOM   2747 C  CG2   . THR   C 1 21  ? 4.56800   27.07000  42.51900  1.000 19.10421 ? 20  THR   B CG2   1 
ATOM   2748 N  N     . ILE   C 1 22  ? 5.46200   29.86200  40.23600  1.000 15.14422 ? 21  ILE   B N     1 
ATOM   2749 C  CA    . ILE   C 1 22  ? 4.68300   31.07300  39.99600  1.000 17.18444 ? 21  ILE   B CA    1 
ATOM   2750 C  C     . ILE   C 1 22  ? 4.30600   31.20500  38.51400  1.000 17.07017 ? 21  ILE   B C     1 
ATOM   2751 O  O     . ILE   C 1 22  ? 3.21600   31.70000  38.18000  1.000 19.54630 ? 21  ILE   B O     1 
ATOM   2752 C  CB    . ILE   C 1 22  ? 5.44500   32.28800  40.53800  1.000 17.12952 ? 21  ILE   B CB    1 
ATOM   2753 C  CG1   . ILE   C 1 22  ? 5.42200   32.23300  42.07300  1.000 17.23545 ? 21  ILE   B CG1   1 
ATOM   2754 C  CG2   . ILE   C 1 22  ? 4.78300   33.56400  40.08500  1.000 20.74234 ? 21  ILE   B CG2   1 
ATOM   2755 C  CD1   . ILE   C 1 22  ? 6.43900   33.08000  42.79200  1.000 22.93027 ? 21  ILE   B CD1   1 
ATOM   2756 N  N     . GLN   C 1 23  ? 5.18600   30.79100  37.59500  1.000 15.72580 ? 22  GLN   B N     1 
ATOM   2757 C  CA    . GLN   C 1 23  ? 4.79200   30.76900  36.18800  1.000 17.62651 ? 22  GLN   B CA    1 
ATOM   2758 C  C     . GLN   C 1 23  ? 3.61300   29.82800  35.97200  1.000 19.68304 ? 22  GLN   B C     1 
ATOM   2759 O  O     . GLN   C 1 23  ? 2.64400   30.18700  35.29600  1.000 20.55227 ? 22  GLN   B O     1 
ATOM   2760 C  CB    . GLN   C 1 23  ? 5.95200   30.34400  35.29500  1.000 19.91970 ? 22  GLN   B CB    1 
ATOM   2761 C  CG    . GLN   C 1 23  ? 6.78700   31.44300  34.80700  1.000 24.63525 ? 22  GLN   B CG    1 
ATOM   2762 C  CD    . GLN   C 1 23  ? 6.16400   32.27700  33.68200  1.000 24.83912 ? 22  GLN   B CD    1 
ATOM   2763 O  OE1   . GLN   C 1 23  ? 4.93500   32.29900  33.43900  1.000 22.94561 ? 22  GLN   B OE1   1 
ATOM   2764 N  NE2   . GLN   C 1 23  ? 7.03100   32.98500  33.00000  1.000 26.48717 ? 22  GLN   B NE2   1 
ATOM   2765 N  N     . LEU   C 1 24  ? 3.68200   28.61700  36.53800  1.000 18.33972 ? 23  LEU   B N     1 
ATOM   2766 C  CA    . LEU   C 1 24  ? 2.59200   27.66700  36.36200  1.000 17.35591 ? 23  LEU   B CA    1 
ATOM   2767 C  C     . LEU   C 1 24  ? 1.27800   28.23500  36.88600  1.000 19.03676 ? 23  LEU   B C     1 
ATOM   2768 O  O     . LEU   C 1 24  ? 0.24100   28.16800  36.21100  1.000 21.39109 ? 23  LEU   B O     1 
ATOM   2769 C  CB    . LEU   C 1 24  ? 2.92500   26.36100  37.06900  1.000 19.43168 ? 23  LEU   B CB    1 
ATOM   2770 C  CG    . LEU   C 1 24  ? 1.80500   25.33900  36.96900  1.000 22.94795 ? 23  LEU   B CG    1 
ATOM   2771 C  CD1   . LEU   C 1 24  ? 1.99700   24.60800  35.66000  1.000 25.00101 ? 23  LEU   B CD1   1 
ATOM   2772 C  CD2   . LEU   C 1 24  ? 1.89300   24.38600  38.12100  1.000 25.17991 ? 23  LEU   B CD2   1 
ATOM   2773 N  N     . ILE   C 1 25  ? 1.29800   28.78200  38.10100  1.000 19.48168 ? 24  ILE   B N     1 
ATOM   2774 C  CA    . ILE   C 1 25  ? 0.07200   29.15400  38.81100  1.000 21.15098 ? 24  ILE   B CA    1 
ATOM   2775 C  C     . ILE   C 1 25  ? -0.41900  30.52600  38.39100  1.000 24.42870 ? 24  ILE   B C     1 
ATOM   2776 O  O     . ILE   C 1 25  ? -1.61800  30.72200  38.17800  1.000 26.52167 ? 24  ILE   B O     1 
ATOM   2777 C  CB    . ILE   C 1 25  ? 0.27600   29.09000  40.34200  1.000 23.73048 ? 24  ILE   B CB    1 
ATOM   2778 C  CG1   . ILE   C 1 25  ? 0.72200   27.69800  40.79900  1.000 21.37780 ? 24  ILE   B CG1   1 
ATOM   2779 C  CG2   . ILE   C 1 25  ? -0.98700  29.66800  41.08400  1.000 22.43467 ? 24  ILE   B CG2   1 
ATOM   2780 C  CD1   . ILE   C 1 25  ? -0.36700  26.63500  40.79100  1.000 26.40872 ? 24  ILE   B CD1   1 
ATOM   2781 N  N     . GLN   C 1 26  ? 0.49400   31.49500  38.25000  1.000 22.51793 ? 25  GLN   B N     1 
ATOM   2782 C  CA    . GLN   C 1 26  ? 0.12900   32.89600  38.09300  1.000 24.57127 ? 25  GLN   B CA    1 
ATOM   2783 C  C     . GLN   C 1 26  ? 0.52100   33.47100  36.74300  1.000 25.47605 ? 25  GLN   B C     1 
ATOM   2784 O  O     . GLN   C 1 26  ? 0.16000   34.61000  36.44300  1.000 27.27664 ? 25  GLN   B O     1 
ATOM   2785 C  CB    . GLN   C 1 26  ? 0.72600   33.71500  39.24300  1.000 24.91436 ? 25  GLN   B CB    1 
ATOM   2786 C  CG    . GLN   C 1 26  ? 0.26000   33.23700  40.63200  1.000 25.08902 ? 25  GLN   B CG    1 
ATOM   2787 C  CD    . GLN   C 1 26  ? 0.86600   34.06900  41.76900  1.000 23.06690 ? 25  GLN   B CD    1 
ATOM   2788 O  OE1   . GLN   C 1 26  ? 1.61100   35.01600  41.51200  1.000 28.73384 ? 25  GLN   B OE1   1 
ATOM   2789 N  NE2   . GLN   C 1 26  ? 0.55000   33.71200  43.02000  1.000 28.26974 ? 25  GLN   B NE2   1 
ATOM   2790 N  N     . ASN   C 1 27  ? 1.24000   32.70500  35.91400  1.000 24.91075 ? 26  ASN   B N     1 
ATOM   2791 C  CA    . ASN   C 1 27  ? 1.58100   33.10300  34.54500  1.000 24.51108 ? 26  ASN   B CA    1 
ATOM   2792 C  C     . ASN   C 1 27  ? 2.36900   34.40400  34.47200  1.000 23.79268 ? 26  ASN   B C     1 
ATOM   2793 O  O     . ASN   C 1 27  ? 2.13000   35.24600  33.60400  1.000 26.81923 ? 26  ASN   B O     1 
ATOM   2794 C  CB    . ASN   C 1 27  ? 0.35300   33.15800  33.63700  1.000 26.59416 ? 26  ASN   B CB    1 
ATOM   2795 C  CG    . ASN   C 1 27  ? -0.05600  31.79200  33.14900  1.000 34.40094 ? 26  ASN   B CG    1 
ATOM   2796 O  OD1   . ASN   C 1 27  ? -0.94300  31.15800  33.71700  1.000 44.44583 ? 26  ASN   B OD1   1 
ATOM   2797 N  ND2   . ASN   C 1 27  ? 0.61700   31.31000  32.11200  1.000 41.27366 ? 26  ASN   B ND2   1 
ATOM   2798 N  N     . HIS   C 1 28  ? 3.32900   34.57300  35.37100  1.000 23.60940 ? 27  HIS   B N     1 
ATOM   2799 C  CA    . HIS   C 1 28  ? 4.27700   35.66600  35.18300  1.000 24.82556 ? 27  HIS   B CA    1 
ATOM   2800 C  C     . HIS   C 1 28  ? 5.61100   35.23600  35.76500  1.000 20.57049 ? 27  HIS   B C     1 
ATOM   2801 O  O     . HIS   C 1 28  ? 5.68500   34.29000  36.54900  1.000 20.90786 ? 27  HIS   B O     1 
ATOM   2802 C  CB    . HIS   C 1 28  ? 3.79300   36.99100  35.78300  1.000 30.04428 ? 27  HIS   B CB    1 
ATOM   2803 C  CG    . HIS   C 1 28  ? 3.49100   36.89900  37.23500  1.000 30.16174 ? 27  HIS   B CG    1 
ATOM   2804 N  ND1   . HIS   C 1 28  ? 4.39200   37.27000  38.21200  1.000 34.42592 ? 27  HIS   B ND1   1 
ATOM   2805 C  CD2   . HIS   C 1 28  ? 2.40600   36.41800  37.88900  1.000 31.59761 ? 27  HIS   B CD2   1 
ATOM   2806 C  CE1   . HIS   C 1 28  ? 3.86400   37.04600  39.40200  1.000 32.58177 ? 27  HIS   B CE1   1 
ATOM   2807 N  NE2   . HIS   C 1 28  ? 2.65400   36.54000  39.23500  1.000 37.82527 ? 27  HIS   B NE2   1 
ATOM   2808 N  N     . PHE   C 1 29  ? 6.66800   35.91800  35.33000  1.000 27.23466 ? 28  PHE   B N     1 
ATOM   2809 C  CA    . PHE   C 1 29  ? 8.03100   35.61400  35.74800  1.000 24.85019 ? 28  PHE   B CA    1 
ATOM   2810 C  C     . PHE   C 1 29  ? 8.49200   36.60300  36.80400  1.000 29.22883 ? 28  PHE   B C     1 
ATOM   2811 O  O     . PHE   C 1 29  ? 8.44000   37.81900  36.59000  1.000 30.06593 ? 28  PHE   B O     1 
ATOM   2812 C  CB    . PHE   C 1 29  ? 8.99300   35.64300  34.56800  1.000 24.63382 ? 28  PHE   B CB    1 
ATOM   2813 C  CG    . PHE   C 1 29  ? 10.43400  35.47100  34.96600  1.000 22.41680 ? 28  PHE   B CG    1 
ATOM   2814 C  CD1   . PHE   C 1 29  ? 10.86200  34.30900  35.61400  1.000 21.14747 ? 28  PHE   B CD1   1 
ATOM   2815 C  CD2   . PHE   C 1 29  ? 11.35200  36.45400  34.67800  1.000 25.55288 ? 28  PHE   B CD2   1 
ATOM   2816 C  CE1   . PHE   C 1 29  ? 12.18700  34.15300  35.95500  1.000 20.48714 ? 28  PHE   B CE1   1 
ATOM   2817 C  CE2   . PHE   C 1 29  ? 12.67300  36.31500  35.02200  1.000 24.84744 ? 28  PHE   B CE2   1 
ATOM   2818 C  CZ    . PHE   C 1 29  ? 13.09900  35.15000  35.65300  1.000 20.65449 ? 28  PHE   B CZ    1 
ATOM   2819 N  N     . VAL   C 1 30  ? 8.97500   36.06300  37.92400  1.000 30.47323 ? 29  VAL   B N     1 
ATOM   2820 C  CA    . VAL   C 1 30  ? 9.52500   36.85000  39.02200  1.000 30.54677 ? 29  VAL   B CA    1 
ATOM   2821 C  C     . VAL   C 1 30  ? 11.02500  37.07100  38.77800  1.000 30.44790 ? 29  VAL   B C     1 
ATOM   2822 O  O     . VAL   C 1 30  ? 11.82100  36.12800  38.82500  1.000 31.40246 ? 29  VAL   B O     1 
ATOM   2823 C  CB    . VAL   C 1 30  ? 9.23900   36.17100  40.36700  1.000 34.62649 ? 29  VAL   B CB    1 
ATOM   2824 C  CG1   . VAL   C 1 30  ? 7.73300   36.19300  40.65100  1.000 34.58046 ? 29  VAL   B CG1   1 
ATOM   2825 C  CG2   . VAL   C 1 30  ? 9.70800   34.71400  40.35000  1.000 36.00519 ? 29  VAL   B CG2   1 
ATOM   2826 N  N     . ASP   C 1 31  ? 11.40800  38.32200  38.51300  1.000 31.14228 ? 30  ASP   B N     1 
ATOM   2827 C  CA    . ASP   C 1 31  ? 12.80900  38.67000  38.23500  1.000 26.71764 ? 30  ASP   B CA    1 
ATOM   2828 C  C     . ASP   C 1 31  ? 13.63500  38.82200  39.51500  1.000 31.99547 ? 30  ASP   B C     1 
ATOM   2829 O  O     . ASP   C 1 31  ? 14.82800  38.48400  39.54800  1.000 29.48010 ? 30  ASP   B O     1 
ATOM   2830 C  CB    . ASP   C 1 31  ? 12.87600  39.96500  37.43000  1.000 37.29839 ? 30  ASP   B CB    1 
ATOM   2831 C  CG    . ASP   C 1 31  ? 14.26200  40.23500  36.87300  1.000 44.92515 ? 30  ASP   B CG    1 
ATOM   2832 O  OD1   . ASP   C 1 31  ? 14.64000  39.58500  35.86800  1.000 42.13569 ? 30  ASP   B OD1   1 
ATOM   2833 O  OD2   . ASP   C 1 31  ? 14.97100  41.10100  37.43500  1.000 51.76870 ? 30  ASP   B OD2   1 
ATOM   2834 N  N     . GLU   C 1 32  ? 13.03700  39.36600  40.55900  1.000 34.62215 ? 31  GLU   B N     1 
ATOM   2835 C  CA    . GLU   C 1 32  ? 13.74800  39.53900  41.81200  1.000 31.43818 ? 31  GLU   B CA    1 
ATOM   2836 C  C     . GLU   C 1 32  ? 13.79300  38.20000  42.54200  1.000 27.86540 ? 31  GLU   B C     1 
ATOM   2837 O  O     . GLU   C 1 32  ? 12.91600  37.35100  42.37200  1.000 33.49605 ? 31  GLU   B O     1 
ATOM   2838 C  CB    . GLU   C 1 32  ? 13.03700  40.59800  42.64900  1.000 38.76582 ? 31  GLU   B CB    1 
ATOM   2839 C  CG    . GLU   C 1 32  ? 11.54500  40.32800  42.81500  1.000 51.36777 ? 31  GLU   B CG    1 
ATOM   2840 C  CD    . GLU   C 1 32  ? 10.76900  41.49300  43.42200  1.000 67.13808 ? 31  GLU   B CD    1 
ATOM   2841 O  OE1   . GLU   C 1 32  ? 11.38100  42.54400  43.74700  1.000 62.50199 ? 31  GLU   B OE1   1 
ATOM   2842 O  OE2   . GLU   C 1 32  ? 9.53300   41.34600  43.57300  1.000 67.74813 ? 31  GLU   B OE2   1 
ATOM   2843 N  N     . TYR   C 1 33  ? 14.85400  38.02000  43.31700  1.000 29.21393 ? 32  TYR   B N     1 
ATOM   2844 C  CA    . TYR   C 1 33  ? 15.00700  36.79200  44.13300  1.000 26.78035 ? 32  TYR   B CA    1 
ATOM   2845 C  C     . TYR   C 1 33  ? 14.48900  37.06800  45.52800  1.000 23.30527 ? 32  TYR   B C     1 
ATOM   2846 O  O     . TYR   C 1 33  ? 15.09000  37.85700  46.24800  1.000 26.48605 ? 32  TYR   B O     1 
ATOM   2847 C  CB    . TYR   C 1 33  ? 16.46500  36.32100  44.14700  1.000 26.26422 ? 32  TYR   B CB    1 
ATOM   2848 C  CG    . TYR   C 1 33  ? 16.82300  35.08100  44.95800  1.000 24.94336 ? 32  TYR   B CG    1 
ATOM   2849 C  CD1   . TYR   C 1 33  ? 15.85600  34.21000  45.43800  1.000 20.91197 ? 32  TYR   B CD1   1 
ATOM   2850 C  CD2   . TYR   C 1 33  ? 18.15000  34.77800  45.23300  1.000 29.21343 ? 32  TYR   B CD2   1 
ATOM   2851 C  CE1   . TYR   C 1 33  ? 16.19600  33.09000  46.17500  1.000 24.35481 ? 32  TYR   B CE1   1 
ATOM   2852 C  CE2   . TYR   C 1 33  ? 18.50500  33.66100  45.96700  1.000 29.58159 ? 32  TYR   B CE2   1 
ATOM   2853 C  CZ    . TYR   C 1 33  ? 17.52400  32.81400  46.44500  1.000 26.21466 ? 32  TYR   B CZ    1 
ATOM   2854 O  OH    . TYR   C 1 33  ? 17.88600  31.71400  47.15900  1.000 25.66862 ? 32  TYR   B OH    1 
ATOM   2855 N  N     . ASP   C 1 34  ? 13.37500  36.44800  45.87000  1.000 19.30757 ? 33  ASP   B N     1 
ATOM   2856 C  CA    . ASP   C 1 34  ? 12.80000  36.53300  47.21100  1.000 21.13540 ? 33  ASP   B CA    1 
ATOM   2857 C  C     . ASP   C 1 34  ? 12.93000  35.13800  47.79400  1.000 21.27400 ? 33  ASP   B C     1 
ATOM   2858 O  O     . ASP   C 1 34  ? 12.13000  34.26500  47.46200  1.000 18.21482 ? 33  ASP   B O     1 
ATOM   2859 C  CB    . ASP   C 1 34  ? 11.32400  36.93000  47.09600  1.000 24.33515 ? 33  ASP   B CB    1 
ATOM   2860 C  CG    . ASP   C 1 34  ? 10.59100  36.96600  48.43900  1.000 30.82750 ? 33  ASP   B CG    1 
ATOM   2861 O  OD1   . ASP   C 1 34  ? 11.24900  37.07200  49.49400  1.000 28.49243 ? 33  ASP   B OD1   1 
ATOM   2862 O  OD2   . ASP   C 1 34  ? 9.34000   36.84500  48.41100  1.000 34.23234 ? 33  ASP   B OD2   1 
ATOM   2863 N  N     . PRO   C 1 35  ? 13.92400  34.88200  48.65000  1.000 19.88789 ? 34  PRO   B N     1 
ATOM   2864 C  CA    . PRO   C 1 35  ? 14.13800  33.51400  49.15600  1.000 20.39362 ? 34  PRO   B CA    1 
ATOM   2865 C  C     . PRO   C 1 35  ? 12.92100  32.93800  49.88500  1.000 19.12124 ? 34  PRO   B C     1 
ATOM   2866 O  O     . PRO   C 1 35  ? 12.27200  33.59700  50.70600  1.000 21.40453 ? 34  PRO   B O     1 
ATOM   2867 C  CB    . PRO   C 1 35  ? 15.35400  33.67000  50.08300  1.000 25.22880 ? 34  PRO   B CB    1 
ATOM   2868 C  CG    . PRO   C 1 35  ? 16.09300  34.89100  49.52800  1.000 27.59283 ? 34  PRO   B CG    1 
ATOM   2869 C  CD    . PRO   C 1 35  ? 14.98400  35.81300  49.06800  1.000 24.40835 ? 34  PRO   B CD    1 
ATOM   2870 N  N     . THR   C 1 36  ? 12.62400  31.68400  49.59400  1.000 16.99847 ? 35  THR   B N     1 
ATOM   2871 C  CA    . THR   C 1 36  ? 11.42600  31.05000  50.14200  1.000 17.41896 ? 35  THR   B CA    1 
ATOM   2872 C  C     . THR   C 1 36  ? 11.61500  30.57500  51.57800  1.000 18.35836 ? 35  THR   B C     1 
ATOM   2873 O  O     . THR   C 1 36  ? 12.67500  30.07800  51.95400  1.000 17.31819 ? 35  THR   B O     1 
ATOM   2874 C  CB    . THR   C 1 36  ? 11.05600  29.86000  49.26000  1.000 16.05039 ? 35  THR   B CB    1 
ATOM   2875 O  OG1   . THR   C 1 36  ? 10.80600  30.32700  47.91900  1.000 16.26165 ? 35  THR   B OG1   1 
ATOM   2876 C  CG2   . THR   C 1 36  ? 9.81000   29.11000  49.79200  1.000 17.23476 ? 35  THR   B CG2   1 
ATOM   2877 N  N     . ILE   C 1 37  ? 10.56500  30.74100  52.38800  1.000 17.01908 ? 36  ILE   B N     1 
ATOM   2878 C  CA    . ILE   C 1 37  ? 10.43500  30.05400  53.66800  1.000 16.16283 ? 36  ILE   B CA    1 
ATOM   2879 C  C     . ILE   C 1 37  ? 9.60600   28.81700  53.36000  1.000 16.00702 ? 36  ILE   B C     1 
ATOM   2880 O  O     . ILE   C 1 37  ? 10.10500  27.69100  53.46700  1.000 18.07449 ? 36  ILE   B O     1 
ATOM   2881 C  CB    . ILE   C 1 37  ? 9.78900   30.94900  54.74000  1.000 16.68057 ? 36  ILE   B CB    1 
ATOM   2882 C  CG1   . ILE   C 1 37  ? 10.74200  32.06500  55.14500  1.000 21.79871 ? 36  ILE   B CG1   1 
ATOM   2883 C  CG2   . ILE   C 1 37  ? 9.41800   30.11400  55.99300  1.000 16.09342 ? 36  ILE   B CG2   1 
ATOM   2884 C  CD1   . ILE   C 1 37  ? 11.82400  31.56100  55.96600  1.000 27.90357 ? 36  ILE   B CD1   1 
ATOM   2885 N  N     . GLU   C 1 38  ? 8.36100   29.01100  52.91700  1.000 16.07417 ? 37  GLU   B N     1 
ATOM   2886 C  CA    . GLU   C 1 38  ? 7.50700   27.93200  52.43000  1.000 14.99456 ? 37  GLU   B CA    1 
ATOM   2887 C  C     . GLU   C 1 38  ? 6.28200   28.56600  51.77900  1.000 14.73409 ? 37  GLU   B C     1 
ATOM   2888 O  O     . GLU   C 1 38  ? 5.71100   29.52300  52.32000  1.000 17.82606 ? 37  GLU   B O     1 
ATOM   2889 C  CB    . GLU   C 1 38  ? 7.05300   27.06000  53.61500  1.000 16.67243 ? 37  GLU   B CB    1 
ATOM   2890 C  CG    . GLU   C 1 38  ? 6.24700   25.83500  53.19400  1.000 16.26191 ? 37  GLU   B CG    1 
ATOM   2891 C  CD    . GLU   C 1 38  ? 5.45200   25.21600  54.34500  1.000 16.52419 ? 37  GLU   B CD    1 
ATOM   2892 O  OE1   . GLU   C 1 38  ? 6.00700   24.40900  55.11800  1.000 18.32441 ? 37  GLU   B OE1   1 
ATOM   2893 O  OE2   . GLU   C 1 38  ? 4.26000   25.59800  54.49500  1.000 19.43637 ? 37  GLU   B OE2   1 
ATOM   2894 N  N     . ASP   C 1 39  ? 5.85300   28.02500  50.64800  1.000 15.54101 ? 38  ASP   B N     1 
ATOM   2895 C  CA    . ASP   C 1 39  ? 4.63400   28.52500  50.03100  1.000 17.80993 ? 38  ASP   B CA    1 
ATOM   2896 C  C     . ASP   C 1 39  ? 3.84800   27.37300  49.43500  1.000 17.62065 ? 38  ASP   B C     1 
ATOM   2897 O  O     . ASP   C 1 39  ? 4.42500   26.37100  49.01500  1.000 16.96958 ? 38  ASP   B O     1 
ATOM   2898 C  CB    . ASP   C 1 39  ? 4.94000   29.53100  48.94800  1.000 18.16198 ? 38  ASP   B CB    1 
ATOM   2899 C  CG    . ASP   C 1 39  ? 5.39500   30.87300  49.51300  1.000 20.33317 ? 38  ASP   B CG    1 
ATOM   2900 O  OD1   . ASP   C 1 39  ? 4.54000   31.64500  49.98200  1.000 23.65204 ? 38  ASP   B OD1   1 
ATOM   2901 O  OD2   . ASP   C 1 39  ? 6.60700   31.11900  49.52700  1.000 23.35241 ? 38  ASP   B OD2   1 
ATOM   2902 N  N     . SER   C 1 40  ? 2.51500   27.51300  49.44000  1.000 16.98107 ? 39  SER   B N     1 
ATOM   2903 C  CA    . SER   C 1 40  ? 1.60600   26.48300  48.97200  1.000 17.34598 ? 39  SER   B CA    1 
ATOM   2904 C  C     . SER   C 1 40  ? 0.66400   27.10800  47.97000  1.000 16.58676 ? 39  SER   B C     1 
ATOM   2905 O  O     . SER   C 1 40  ? 0.14900   28.20500  48.18900  1.000 19.55561 ? 39  SER   B O     1 
ATOM   2906 C  CB    . SER   C 1 40  ? 0.78100   25.93900  50.14600  1.000 18.57023 ? 39  SER   B CB    1 
ATOM   2907 O  OG    . SER   C 1 40  ? 1.58500   25.15300  51.01600  1.000 23.78024 ? 39  SER   B OG    1 
ATOM   2908 N  N     . TYR   C 1 41  ? 0.39700   26.39500  46.88300  1.000 14.88577 ? 40  TYR   B N     1 
ATOM   2909 C  CA    . TYR   C 1 41  ? -0.45600  26.88200  45.81800  1.000 15.04847 ? 40  TYR   B CA    1 
ATOM   2910 C  C     . TYR   C 1 41  ? -1.44000  25.79000  45.43300  1.000 15.96831 ? 40  TYR   B C     1 
ATOM   2911 O  O     . TYR   C 1 41  ? -1.21500  24.60200  45.68700  1.000 16.51857 ? 40  TYR   B O     1 
ATOM   2912 C  CB    . TYR   C 1 41  ? 0.38000   27.25200  44.57600  1.000 18.26719 ? 40  TYR   B CB    1 
ATOM   2913 C  CG    . TYR   C 1 41  ? 1.43300   28.29700  44.85500  1.000 16.43022 ? 40  TYR   B CG    1 
ATOM   2914 C  CD1   . TYR   C 1 41  ? 2.72700   27.94800  45.29000  1.000 18.90940 ? 40  TYR   B CD1   1 
ATOM   2915 C  CD2   . TYR   C 1 41  ? 1.13100   29.64100  44.68000  1.000 21.67451 ? 40  TYR   B CD2   1 
ATOM   2916 C  CE1   . TYR   C 1 41  ? 3.68600   28.96000  45.57500  1.000 17.91552 ? 40  TYR   B CE1   1 
ATOM   2917 C  CE2   . TYR   C 1 41  ? 2.06700   30.63700  44.94400  1.000 24.77867 ? 40  TYR   B CE2   1 
ATOM   2918 C  CZ    . TYR   C 1 41  ? 3.33000   30.28600  45.38900  1.000 24.89069 ? 40  TYR   B CZ    1 
ATOM   2919 O  OH    . TYR   C 1 41  ? 4.23000   31.29900  45.63500  1.000 26.69396 ? 40  TYR   B OH    1 
ATOM   2920 N  N     . ARG   C 1 42  ? -2.53500  26.20300  44.80200  1.000 16.14049 ? 41  ARG   B N     1 
ATOM   2921 C  CA    . ARG   C 1 42  ? -3.61900  25.28500  44.47000  1.000 14.95408 ? 41  ARG   B CA    1 
ATOM   2922 C  C     . ARG   C 1 42  ? -4.26700  25.80700  43.20700  1.000 17.59861 ? 41  ARG   B C     1 
ATOM   2923 O  O     . ARG   C 1 42  ? -4.65000  26.98500  43.15400  1.000 19.52509 ? 41  ARG   B O     1 
ATOM   2924 C  CB    . ARG   C 1 42  ? -4.63600  25.26800  45.62200  1.000 18.29022 ? 41  ARG   B CB    1 
ATOM   2925 C  CG    . ARG   C 1 42  ? -5.78900  24.33800  45.47300  1.000 18.20475 ? 41  ARG   B CG    1 
ATOM   2926 C  CD    . ARG   C 1 42  ? -6.54900  24.33100  46.81700  1.000 19.61875 ? 41  ARG   B CD    1 
ATOM   2927 N  NE    . ARG   C 1 42  ? -7.86600  23.73600  46.74500  1.000 21.13547 ? 41  ARG   B NE    1 
ATOM   2928 C  CZ    . ARG   C 1 42  ? -8.13000  22.43600  46.84000  1.000 18.86416 ? 41  ARG   B CZ    1 
ATOM   2929 N  NH1   . ARG   C 1 42  ? -7.15900  21.53400  46.87400  1.000 22.61086 ? 41  ARG   B NH1   1 
ATOM   2930 N  NH2   . ARG   C 1 42  ? -9.39800  22.03300  46.91100  1.000 21.31424 ? 41  ARG   B NH2   1 
ATOM   2931 N  N     . LYS   C 1 43  ? -4.40000  24.94800  42.20100  1.000 16.82645 ? 42  LYS   B N     1 
ATOM   2932 C  CA    . LYS   C 1 43  ? -4.97200  25.37000  40.92200  1.000 17.51414 ? 42  LYS   B CA    1 
ATOM   2933 C  C     . LYS   C 1 43  ? -5.61400  24.18000  40.23800  1.000 17.34176 ? 42  LYS   B C     1 
ATOM   2934 O  O     . LYS   C 1 43  ? -5.09100  23.06500  40.31100  1.000 18.86111 ? 42  LYS   B O     1 
ATOM   2935 C  CB    . LYS   C 1 43  ? -3.86700  25.89800  40.01700  1.000 24.02728 ? 42  LYS   B CB    1 
ATOM   2936 C  CG    . LYS   C 1 43  ? -4.31600  26.58600  38.74500  1.000 28.77454 ? 42  LYS   B CG    1 
ATOM   2937 C  CD    . LYS   C 1 43  ? -3.04200  27.00100  37.98400  1.000 31.89465 ? 42  LYS   B CD    1 
ATOM   2938 C  CE    . LYS   C 1 43  ? -3.30800  27.35300  36.53800  1.000 33.90167 ? 42  LYS   B CE    1 
ATOM   2939 N  NZ    . LYS   C 1 43  ? -4.12300  28.56200  36.48000  1.000 39.42351 ? 42  LYS   B NZ    1 
ATOM   2940 N  N     . GLN   C 1 44  ? -6.70100  24.44400  39.51400  1.000 18.08180 ? 43  GLN   B N     1 
ATOM   2941 C  CA    . GLN   C 1 44  ? -7.36500  23.43500  38.69100  1.000 17.73638 ? 43  GLN   B CA    1 
ATOM   2942 C  C     . GLN   C 1 44  ? -6.80500  23.52100  37.28000  1.000 24.22039 ? 43  GLN   B C     1 
ATOM   2943 O  O     . GLN   C 1 44  ? -6.72500  24.60900  36.70900  1.000 24.17745 ? 43  GLN   B O     1 
ATOM   2944 C  CB    . GLN   C 1 44  ? -8.87400  23.65700  38.67000  1.000 19.77387 ? 43  GLN   B CB    1 
ATOM   2945 C  CG    . GLN   C 1 44  ? -9.58900  22.64200  37.82000  1.000 22.41964 ? 43  GLN   B CG    1 
ATOM   2946 C  CD    . GLN   C 1 44  ? -11.08300 22.85100  37.84400  1.000 26.87742 ? 43  GLN   B CD    1 
ATOM   2947 O  OE1   . GLN   C 1 44  ? -11.69900 22.74400  38.89200  1.000 30.93898 ? 43  GLN   B OE1   1 
ATOM   2948 N  NE2   . GLN   C 1 44  ? -11.68100 23.15100  36.68900  1.000 32.07236 ? 43  GLN   B NE2   1 
ATOM   2949 N  N     . VAL   C 1 45  ? -6.40700  22.37500  36.73600  1.000 18.92360 ? 44  VAL   B N     1 
ATOM   2950 C  CA    . VAL   C 1 45  ? -5.85700  22.27700  35.38200  1.000 22.39725 ? 44  VAL   B CA    1 
ATOM   2951 C  C     . VAL   C 1 45  ? -6.55700  21.14100  34.64200  1.000 22.29534 ? 44  VAL   B C     1 
ATOM   2952 O  O     . VAL   C 1 45  ? -7.19300  20.27200  35.23600  1.000 24.08839 ? 44  VAL   B O     1 
ATOM   2953 C  CB    . VAL   C 1 45  ? -4.33700  22.01400  35.43100  1.000 23.81845 ? 44  VAL   B CB    1 
ATOM   2954 C  CG1   . VAL   C 1 45  ? -3.62600  23.09300  36.23900  1.000 25.39953 ? 44  VAL   B CG1   1 
ATOM   2955 C  CG2   . VAL   C 1 45  ? -4.06900  20.62600  36.02800  1.000 25.00975 ? 44  VAL   B CG2   1 
ATOM   2956 N  N     . VAL   C 1 46  ? -6.42400  21.13800  33.31700  1.000 22.55546 ? 45  VAL   B N     1 
ATOM   2957 C  CA    . VAL   C 1 46  ? -6.83300  19.99100  32.50200  1.000 23.94924 ? 45  VAL   B CA    1 
ATOM   2958 C  C     . VAL   C 1 46  ? -5.57600  19.38300  31.89200  1.000 28.36808 ? 45  VAL   B C     1 
ATOM   2959 O  O     . VAL   C 1 46  ? -4.78900  20.09400  31.25700  1.000 33.59155 ? 45  VAL   B O     1 
ATOM   2960 C  CB    . VAL   C 1 46  ? -7.87000  20.35500  31.42300  1.000 30.74941 ? 45  VAL   B CB    1 
ATOM   2961 C  CG1   . VAL   C 1 46  ? -8.24200  19.10000  30.61500  1.000 33.46014 ? 45  VAL   B CG1   1 
ATOM   2962 C  CG2   . VAL   C 1 46  ? -9.09600  20.96900  32.06100  1.000 32.03791 ? 45  VAL   B CG2   1 
ATOM   2963 N  N     . ILE   C 1 47  ? -5.37100  18.08500  32.11600  1.000 27.45407 ? 46  ILE   B N     1 
ATOM   2964 C  CA    . ILE   C 1 47  ? -4.18200  17.37500  31.63700  1.000 26.22978 ? 46  ILE   B CA    1 
ATOM   2965 C  C     . ILE   C 1 47  ? -4.67300  16.13200  30.91200  1.000 29.70443 ? 46  ILE   B C     1 
ATOM   2966 O  O     . ILE   C 1 47  ? -5.27700  15.24800  31.53400  1.000 28.84043 ? 46  ILE   B O     1 
ATOM   2967 C  CB    . ILE   C 1 47  ? -3.21700  16.98200  32.76700  1.000 22.67807 ? 46  ILE   B CB    1 
ATOM   2968 C  CG1   . ILE   C 1 47  ? -2.68700  18.20700  33.54900  1.000 19.89751 ? 46  ILE   B CG1   1 
ATOM   2969 C  CG2   . ILE   C 1 47  ? -2.04100  16.15300  32.21900  1.000 25.82280 ? 46  ILE   B CG2   1 
ATOM   2970 C  CD1   . ILE   C 1 47  ? -2.09400  17.82900  34.91900  1.000 22.33375 ? 46  ILE   B CD1   1 
ATOM   2971 N  N     . ASP   C 1 48  ? -4.38700  16.04400  29.61300  1.000 31.84716 ? 47  ASP   B N     1 
ATOM   2972 C  CA    . ASP   C 1 48  ? -4.82800  14.91200  28.78800  1.000 37.18390 ? 47  ASP   B CA    1 
ATOM   2973 C  C     . ASP   C 1 48  ? -6.33000  14.65000  28.94300  1.000 34.13408 ? 47  ASP   B C     1 
ATOM   2974 O  O     . ASP   C 1 48  ? -6.77800  13.51600  29.13200  1.000 38.12425 ? 47  ASP   B O     1 
ATOM   2975 C  CB    . ASP   C 1 48  ? -3.98900  13.64500  29.03000  1.000 34.91136 ? 47  ASP   B CB    1 
ATOM   2976 C  CG    . ASP   C 1 48  ? -2.48400  13.90600  28.96700  1.000 37.69510 ? 47  ASP   B CG    1 
ATOM   2977 O  OD1   . ASP   C 1 48  ? -2.06800  14.87200  28.29600  1.000 37.56373 ? 47  ASP   B OD1   1 
ATOM   2978 O  OD2   . ASP   C 1 48  ? -1.71400  13.15100  29.60200  1.000 32.61169 ? 47  ASP   B OD2   1 
ATOM   2979 N  N     . GLY   C 1 49  ? -7.11700  15.72000  28.86100  1.000 32.43615 ? 48  GLY   B N     1 
ATOM   2980 C  CA    . GLY   C 1 49  ? -8.55900  15.63700  28.93100  1.000 32.72357 ? 48  GLY   B CA    1 
ATOM   2981 C  C     . GLY   C 1 49  ? -9.13900  15.29400  30.28600  1.000 34.53293 ? 48  GLY   B C     1 
ATOM   2982 O  O     . GLY   C 1 49  ? -10.34300 15.02100  30.37900  1.000 44.68979 ? 48  GLY   B O     1 
ATOM   2983 N  N     . GLU   C 1 50  ? -8.33000  15.28600  31.33300  1.000 33.64599 ? 49  GLU   B N     1 
ATOM   2984 C  CA    . GLU   C 1 50  ? -8.77200  14.93700  32.67300  1.000 31.66465 ? 49  GLU   B CA    1 
ATOM   2985 C  C     . GLU   C 1 50  ? -8.52400  16.13500  33.57800  1.000 28.06097 ? 49  GLU   B C     1 
ATOM   2986 O  O     . GLU   C 1 50  ? -7.41900  16.68300  33.59000  1.000 29.27527 ? 49  GLU   B O     1 
ATOM   2987 C  CB    . GLU   C 1 50  ? -8.00600  13.71100  33.17400  1.000 36.17737 ? 49  GLU   B CB    1 
ATOM   2988 C  CG    . GLU   C 1 50  ? -8.34500  12.45500  32.35700  1.000 38.26555 ? 49  GLU   B CG    1 
ATOM   2989 C  CD    . GLU   C 1 50  ? -7.44500  11.26500  32.65600  1.000 53.57257 ? 49  GLU   B CD    1 
ATOM   2990 O  OE1   . GLU   C 1 50  ? -6.64000  11.33800  33.61200  1.000 53.16795 ? 49  GLU   B OE1   1 
ATOM   2991 O  OE2   . GLU   C 1 50  ? -7.55000  10.25100  31.92700  1.000 57.58663 ? 49  GLU   B OE2   1 
ATOM   2992 N  N     . THR   C 1 51  ? -9.55900  16.54500  34.31500  1.000 30.33259 ? 50  THR   B N     1 
ATOM   2993 C  CA    . THR   C 1 51  ? -9.48400  17.70500  35.19600  1.000 26.93559 ? 50  THR   B CA    1 
ATOM   2994 C  C     . THR   C 1 51  ? -8.81900  17.30200  36.49500  1.000 24.78542 ? 50  THR   B C     1 
ATOM   2995 O  O     . THR   C 1 51  ? -9.15800  16.26300  37.06500  1.000 25.82312 ? 50  THR   B O     1 
ATOM   2996 C  CB    . THR   C 1 51  ? -10.89300 18.18800  35.51600  1.000 29.43546 ? 50  THR   B CB    1 
ATOM   2997 O  OG1   . THR   C 1 51  ? -11.55400 18.50800  34.29200  1.000 34.77925 ? 50  THR   B OG1   1 
ATOM   2998 C  CG2   . THR   C 1 51  ? -10.81600 19.42400  36.35900  1.000 29.07857 ? 50  THR   B CG2   1 
ATOM   2999 N  N     . SER   C 1 52  ? -7.88200  18.11700  36.95600  1.000 23.78679 ? 51  SER   B N     1 
ATOM   3000 C  CA    . SER   C 1 52  ? -7.13700  17.80600  38.16800  1.000 19.55871 ? 51  SER   B CA    1 
ATOM   3001 C  C     . SER   C 1 52  ? -6.91800  19.05900  38.99900  1.000 21.54496 ? 51  SER   B C     1 
ATOM   3002 O  O     . SER   C 1 52  ? -6.73300  20.15700  38.46600  1.000 23.89377 ? 51  SER   B O     1 
ATOM   3003 C  CB    . SER   C 1 52  ? -5.74100  17.25800  37.86000  1.000 24.10989 ? 51  SER   B CB    1 
ATOM   3004 O  OG    . SER   C 1 52  ? -5.83500  15.94800  37.31600  1.000 27.75345 ? 51  SER   B OG    1 
ATOM   3005 N  N     . LEU   C 1 53  ? -6.91000  18.87900  40.31400  1.000 19.81458 ? 52  LEU   B N     1 
ATOM   3006 C  CA    . LEU   C 1 53  ? -6.42300  19.89600  41.24300  1.000 17.86476 ? 52  LEU   B CA    1 
ATOM   3007 C  C     . LEU   C 1 53  ? -4.96500  19.61300  41.57300  1.000 19.15095 ? 52  LEU   B C     1 
ATOM   3008 O  O     . LEU   C 1 53  ? -4.61600  18.48800  41.95200  1.000 18.62223 ? 52  LEU   B O     1 
ATOM   3009 C  CB    . LEU   C 1 53  ? -7.26400  19.95300  42.53200  1.000 20.18206 ? 52  LEU   B CB    1 
ATOM   3010 C  CG    . LEU   C 1 53  ? -8.75800  20.27100  42.39700  1.000 26.05420 ? 52  LEU   B CG    1 
ATOM   3011 C  CD1   . LEU   C 1 53  ? -9.51200  20.09300  43.72800  1.000 24.45565 ? 52  LEU   B CD1   1 
ATOM   3012 C  CD2   . LEU   C 1 53  ? -8.96800  21.67100  41.88500  1.000 29.67835 ? 52  LEU   B CD2   1 
ATOM   3013 N  N     . LEU   C 1 54  ? -4.10500  20.60300  41.36000  1.000 16.14616 ? 53  LEU   B N     1 
ATOM   3014 C  CA    . LEU   C 1 54  ? -2.70000  20.51600  41.74600  1.000 16.73008 ? 53  LEU   B CA    1 
ATOM   3015 C  C     . LEU   C 1 54  ? -2.49800  21.30400  43.02500  1.000 17.55748 ? 53  LEU   B C     1 
ATOM   3016 O  O     . LEU   C 1 54  ? -2.78700  22.50100  43.07200  1.000 17.18532 ? 53  LEU   B O     1 
ATOM   3017 C  CB    . LEU   C 1 54  ? -1.74400  21.03800  40.66700  1.000 15.94015 ? 53  LEU   B CB    1 
ATOM   3018 C  CG    . LEU   C 1 54  ? -1.98800  20.42900  39.29800  1.000 16.39355 ? 53  LEU   B CG    1 
ATOM   3019 C  CD1   . LEU   C 1 54  ? -0.95200  20.90000  38.28500  1.000 18.86844 ? 53  LEU   B CD1   1 
ATOM   3020 C  CD2   . LEU   C 1 54  ? -2.06800  18.92800  39.33900  1.000 20.98656 ? 53  LEU   B CD2   1 
ATOM   3021 N  N     . ASP   C 1 55  ? -2.00300  20.64000  44.04800  1.000 15.60572 ? 54  ASP   B N     1 
ATOM   3022 C  CA    . ASP   C 1 55  ? -1.57300  21.28700  45.27500  1.000 15.29221 ? 54  ASP   B CA    1 
ATOM   3023 C  C     . ASP   C 1 55  ? -0.05800  21.26700  45.26100  1.000 17.39411 ? 54  ASP   B C     1 
ATOM   3024 O  O     . ASP   C 1 55  ? 0.54000   20.19700  45.32800  1.000 21.07141 ? 54  ASP   B O     1 
ATOM   3025 C  CB    . ASP   C 1 55  ? -2.07100  20.51600  46.49500  1.000 16.81221 ? 54  ASP   B CB    1 
ATOM   3026 C  CG    . ASP   C 1 55  ? -3.56700  20.36600  46.53000  1.000 22.47567 ? 54  ASP   B CG    1 
ATOM   3027 O  OD1   . ASP   C 1 55  ? -4.27400  21.40200  46.54800  1.000 22.14592 ? 54  ASP   B OD1   1 
ATOM   3028 O  OD2   . ASP   C 1 55  ? -4.01000  19.19900  46.56200  1.000 23.78311 ? 54  ASP   B OD2   1 
ATOM   3029 N  N     . ILE   C 1 56  ? 0.57200   22.43000  45.18900  1.000 15.16655 ? 55  ILE   B N     1 
ATOM   3030 C  CA    . ILE   C 1 56  ? 2.01900   22.49600  44.99400  1.000 15.16583 ? 55  ILE   B CA    1 
ATOM   3031 C  C     . ILE   C 1 56  ? 2.65700   23.09300  46.23000  1.000 15.01632 ? 55  ILE   B C     1 
ATOM   3032 O  O     . ILE   C 1 56  ? 2.25900   24.18200  46.65900  1.000 17.04607 ? 55  ILE   B O     1 
ATOM   3033 C  CB    . ILE   C 1 56  ? 2.37300   23.30200  43.73700  1.000 18.47286 ? 55  ILE   B CB    1 
ATOM   3034 C  CG1   . ILE   C 1 56  ? 1.75400   22.59700  42.50600  1.000 22.83674 ? 55  ILE   B CG1   1 
ATOM   3035 C  CG2   . ILE   C 1 56  ? 3.89600   23.42200  43.57100  1.000 19.73260 ? 55  ILE   B CG2   1 
ATOM   3036 C  CD1   . ILE   C 1 56  ? 1.66700   23.45300  41.30900  1.000 29.17733 ? 55  ILE   B CD1   1 
ATOM   3037 N  N     . LEU   C 1 57  ? 3.59500   22.37400  46.82100  1.000 13.71774 ? 56  LEU   B N     1 
ATOM   3038 C  CA    . LEU   C 1 57  ? 4.40800   22.86400  47.93600  1.000 13.74603 ? 56  LEU   B CA    1 
ATOM   3039 C  C     . LEU   C 1 57  ? 5.74400   23.32100  47.36700  1.000 14.07715 ? 56  LEU   B C     1 
ATOM   3040 O  O     . LEU   C 1 57  ? 6.49300   22.51800  46.78100  1.000 16.52413 ? 56  LEU   B O     1 
ATOM   3041 C  CB    . LEU   C 1 57  ? 4.62100   21.76200  48.97500  1.000 17.34903 ? 56  LEU   B CB    1 
ATOM   3042 C  CG    . LEU   C 1 57  ? 5.46800   22.20300  50.18300  1.000 16.85936 ? 56  LEU   B CG    1 
ATOM   3043 C  CD1   . LEU   C 1 57  ? 4.75200   23.26700  50.98800  1.000 20.95503 ? 56  LEU   B CD1   1 
ATOM   3044 C  CD2   . LEU   C 1 57  ? 5.76000   21.04600  51.05200  1.000 19.86383 ? 56  LEU   B CD2   1 
ATOM   3045 N  N     . ASP   C 1 58  ? 6.02100   24.61400  47.50300  1.000 15.80725 ? 57  ASP   B N     1 
ATOM   3046 C  CA    . ASP   C 1 58  ? 7.27800   25.23800  47.07600  1.000 16.75132 ? 57  ASP   B CA    1 
ATOM   3047 C  C     . ASP   C 1 58  ? 8.15700   25.34300  48.32300  1.000 17.75798 ? 57  ASP   B C     1 
ATOM   3048 O  O     . ASP   C 1 58  ? 7.83100   26.06900  49.27600  1.000 18.18072 ? 57  ASP   B O     1 
ATOM   3049 C  CB    . ASP   C 1 58  ? 6.96400   26.62800  46.54000  1.000 19.37148 ? 57  ASP   B CB    1 
ATOM   3050 C  CG    . ASP   C 1 58  ? 8.16500   27.33800  45.97400  1.000 22.85474 ? 57  ASP   B CG    1 
ATOM   3051 O  OD1   . ASP   C 1 58  ? 9.16900   26.66400  45.65300  1.000 21.07593 ? 57  ASP   B OD1   1 
ATOM   3052 O  OD2   . ASP   C 1 58  ? 8.08200   28.58500  45.85600  1.000 21.63529 ? 57  ASP   B OD2   1 
ATOM   3053 N  N     . THR   C 1 59  ? 9.24100   24.57400  48.35700  1.000 16.22813 ? 58  THR   B N     1 
ATOM   3054 C  CA    . THR   C 1 59  ? 10.12800  24.49100  49.51400  1.000 17.12962 ? 58  THR   B CA    1 
ATOM   3055 C  C     . THR   C 1 59  ? 11.31900  25.43600  49.40900  1.000 18.06583 ? 58  THR   B C     1 
ATOM   3056 O  O     . THR   C 1 59  ? 11.69800  25.90100  48.33300  1.000 17.96089 ? 58  THR   B O     1 
ATOM   3057 C  CB    . THR   C 1 59  ? 10.64300  23.06100  49.71600  1.000 18.22896 ? 58  THR   B CB    1 
ATOM   3058 O  OG1   . THR   C 1 59  ? 11.57700  22.73200  48.66300  1.000 18.68908 ? 58  THR   B OG1   1 
ATOM   3059 C  CG2   . THR   C 1 59  ? 9.48300   22.05000  49.73800  1.000 18.45927 ? 58  THR   B CG2   1 
ATOM   3060 N  N     . ALA   C 1 60  ? 11.90900  25.72900  50.54600  1.000 17.55964 ? 59  ALA   B N     1 
ATOM   3061 C  CA    . ALA   C 1 60  ? 13.16400  26.46000  50.59900  1.000 19.62744 ? 59  ALA   B CA    1 
ATOM   3062 C  C     . ALA   C 1 60  ? 14.31700  25.56600  50.16000  1.000 21.48558 ? 59  ALA   B C     1 
ATOM   3063 O  O     . ALA   C 1 60  ? 14.35100  24.36700  50.46500  1.000 23.72831 ? 59  ALA   B O     1 
ATOM   3064 C  CB    . ALA   C 1 60  ? 13.42500  26.93700  52.03600  1.000 20.58913 ? 59  ALA   B CB    1 
ATOM   3065 N  N     . GLY   C 1 61  ? 15.30500  26.18300  49.51600  1.000 17.67627 ? 60  GLY   B N     1 
ATOM   3066 C  CA    . GLY   C 1 61  ? 16.53000  25.48300  49.09900  1.000 20.68339 ? 60  GLY   B CA    1 
ATOM   3067 C  C     . GLY   C 1 61  ? 17.56100  25.47200  50.21000  1.000 30.58608 ? 60  GLY   B C     1 
ATOM   3068 O  O     . GLY   C 1 61  ? 18.59700  26.14000  50.04200  1.000 44.42738 ? 60  GLY   B O     1 
ATOM   3069 N  N     . GLN   C 1 62  ? 17.25400  24.83000  51.30900  1.000 29.25915 ? 61  GLN   B N     1 
ATOM   3070 C  CA    . GLN   C 1 62  ? 18.11600  24.57800  52.45000  1.000 38.05440 ? 61  GLN   B CA    1 
ATOM   3071 C  C     . GLN   C 1 62  ? 17.77400  23.18100  52.93200  1.000 30.46180 ? 61  GLN   B C     1 
ATOM   3072 O  O     . GLN   C 1 62  ? 16.61900  22.76900  52.84800  1.000 33.56652 ? 61  GLN   B O     1 
ATOM   3073 C  CB    . GLN   C 1 62  ? 17.78800  25.57100  53.56500  1.000 37.54238 ? 61  GLN   B CB    1 
ATOM   3074 C  CG    . GLN   C 1 62  ? 16.29300  25.61200  53.94800  1.000 29.90391 ? 61  GLN   B CG    1 
ATOM   3075 C  CD    . GLN   C 1 62  ? 15.99000  24.90400  55.23600  1.000 43.15102 ? 61  GLN   B CD    1 
ATOM   3076 O  OE1   . GLN   C 1 62  ? 16.60500  25.20100  56.25000  1.000 41.95027 ? 61  GLN   B OE1   1 
ATOM   3077 N  NE2   . GLN   C 1 62  ? 15.02100  23.98100  55.21900  1.000 33.68262 ? 61  GLN   B NE2   1 
ATOM   3078 N  N     . GLU   C 1 63  ? 18.76500  22.43700  53.41200  1.000 39.17252 ? 62  GLU   B N     1 
ATOM   3079 C  CA    . GLU   C 1 63  ? 18.47900  21.10400  53.92200  1.000 43.78566 ? 62  GLU   B CA    1 
ATOM   3080 C  C     . GLU   C 1 63  ? 18.46200  21.03900  55.44800  1.000 43.79214 ? 62  GLU   B C     1 
ATOM   3081 O  O     . GLU   C 1 63  ? 18.40600  19.94200  56.01300  1.000 39.94990 ? 62  GLU   B O     1 
ATOM   3082 C  CB    . GLU   C 1 63  ? 19.37300  20.04200  53.26500  1.000 43.95258 ? 62  GLU   B CB    1 
ATOM   3083 C  CG    . GLU   C 1 63  ? 19.01800  19.83700  51.77900  1.000 43.15375 ? 62  GLU   B CG    1 
ATOM   3084 C  CD    . GLU   C 1 63  ? 19.79300  18.70800  51.09900  1.000 49.55972 ? 62  GLU   B CD    1 
ATOM   3085 O  OE1   . GLU   C 1 63  ? 21.02400  18.83600  50.91200  1.000 48.93746 ? 62  GLU   B OE1   1 
ATOM   3086 O  OE2   . GLU   C 1 63  ? 19.16200  17.68800  50.73900  1.000 45.62506 ? 62  GLU   B OE2   1 
ATOM   3087 N  N     . GLU   C 1 64  ? 18.49800  22.19200  56.12000  1.000 37.89624 ? 63  GLU   B N     1 
ATOM   3088 C  CA    . GLU   C 1 64  ? 18.22600  22.25300  57.54500  1.000 45.66261 ? 63  GLU   B CA    1 
ATOM   3089 C  C     . GLU   C 1 64  ? 16.74900  21.95600  57.80900  1.000 33.79077 ? 63  GLU   B C     1 
ATOM   3090 O  O     . GLU   C 1 64  ? 15.92500  21.87000  56.89900  1.000 38.16895 ? 63  GLU   B O     1 
ATOM   3091 C  CB    . GLU   C 1 64  ? 18.56300  23.63700  58.09900  1.000 45.03099 ? 63  GLU   B CB    1 
ATOM   3092 C  CG    . GLU   C 1 64  ? 19.77900  24.30800  57.48400  1.000 48.20486 ? 63  GLU   B CG    1 
ATOM   3093 C  CD    . GLU   C 1 64  ? 21.08600  23.69900  57.95100  1.000 57.33350 ? 63  GLU   B CD    1 
ATOM   3094 O  OE1   . GLU   C 1 64  ? 21.41400  22.57100  57.51500  1.000 59.79955 ? 63  GLU   B OE1   1 
ATOM   3095 O  OE2   . GLU   C 1 64  ? 21.78600  24.35200  58.75300  1.000 54.94456 ? 63  GLU   B OE2   1 
ATOM   3096 N  N     . TYR   C 1 65  ? 16.42500  21.80100  59.08200  1.000 39.27848 ? 64  TYR   B N     1 
ATOM   3097 C  CA    . TYR   C 1 65  ? 15.07200  21.49500  59.53700  1.000 31.23697 ? 64  TYR   B CA    1 
ATOM   3098 C  C     . TYR   C 1 65  ? 14.58900  20.15800  58.97300  1.000 32.58262 ? 64  TYR   B C     1 
ATOM   3099 O  O     . TYR   C 1 65  ? 13.56300  20.06700  58.30600  1.000 30.30887 ? 64  TYR   B O     1 
ATOM   3100 C  CB    . TYR   C 1 65  ? 14.11400  22.65900  59.25600  1.000 30.78655 ? 64  TYR   B CB    1 
ATOM   3101 C  CG    . TYR   C 1 65  ? 14.62800  23.93200  59.90100  1.000 26.37918 ? 64  TYR   B CG    1 
ATOM   3102 C  CD1   . TYR   C 1 65  ? 14.70400  24.04300  61.26100  1.000 25.91176 ? 64  TYR   B CD1   1 
ATOM   3103 C  CD2   . TYR   C 1 65  ? 15.04000  25.00900  59.11100  1.000 23.68440 ? 64  TYR   B CD2   1 
ATOM   3104 C  CE1   . TYR   C 1 65  ? 15.20200  25.19600  61.88100  1.000 23.78692 ? 64  TYR   B CE1   1 
ATOM   3105 C  CE2   . TYR   C 1 65  ? 15.54300  26.17400  59.69200  1.000 22.43251 ? 64  TYR   B CE2   1 
ATOM   3106 C  CZ    . TYR   C 1 65  ? 15.61000  26.27400  61.07100  1.000 22.50193 ? 64  TYR   B CZ    1 
ATOM   3107 O  OH    . TYR   C 1 65  ? 16.08800  27.38400  61.76500  1.000 25.55833 ? 64  TYR   B OH    1 
ATOM   3108 N  N     . SER   C 1 66  ? 15.35300  19.10600  59.29000  1.000 38.62265 ? 65  SER   B N     1 
ATOM   3109 C  CA    . SER   C 1 66  ? 15.12300  17.79000  58.69000  1.000 32.60999 ? 65  SER   B CA    1 
ATOM   3110 C  C     . SER   C 1 66  ? 13.74200  17.24600  59.04900  1.000 29.61531 ? 65  SER   B C     1 
ATOM   3111 O  O     . SER   C 1 66  ? 13.09000  16.63100  58.19400  1.000 33.83669 ? 65  SER   B O     1 
ATOM   3112 C  CB    . SER   C 1 66  ? 16.22600  16.80900  59.11800  1.000 38.83455 ? 65  SER   B CB    1 
ATOM   3113 O  OG    . SER   C 1 66  ? 16.38000  16.82000  60.50300  1.000 45.65782 ? 65  SER   B OG    1 
ATOM   3114 N  N     . ALA   C 1 67  ? 13.25800  17.54500  60.25600  1.000 28.80947 ? 66  ALA   B N     1 
ATOM   3115 C  CA    . ALA   C 1 67  ? 11.93300  17.08800  60.69400  1.000 27.97714 ? 66  ALA   B CA    1 
ATOM   3116 C  C     . ALA   C 1 67  ? 10.84000  17.67900  59.80400  1.000 34.28070 ? 66  ALA   B C     1 
ATOM   3117 O  O     . ALA   C 1 67  ? 9.95200   16.96600  59.32300  1.000 29.86037 ? 66  ALA   B O     1 
ATOM   3118 C  CB    . ALA   C 1 67  ? 11.68300  17.42100  62.16200  1.000 36.94570 ? 66  ALA   B CB    1 
ATOM   3119 N  N     . MET   C 1 68  ? 10.89700  18.98800  59.55400  1.000 28.44451 ? 67  MET   B N     1 
ATOM   3120 C  CA    . MET   C 1 68  ? 9.95200   19.57900  58.61600  1.000 27.11372 ? 67  MET   B CA    1 
ATOM   3121 C  C     . MET   C 1 68  ? 10.13000  18.99800  57.21500  1.000 24.60473 ? 67  MET   B C     1 
ATOM   3122 O  O     . MET   C 1 68  ? 9.15500   18.65500  56.53800  1.000 27.04757 ? 67  MET   B O     1 
ATOM   3123 C  CB    . MET   C 1 68  ? 10.11800  21.10200  58.58400  1.000 24.29578 ? 67  MET   B CB    1 
ATOM   3124 C  CG    . MET   C 1 68  ? 9.02900   21.76800  57.77700  1.000 23.01073 ? 67  MET   B CG    1 
ATOM   3125 S  SD    . MET   C 1 68  ? 7.45100   21.56000  58.62800  1.000 32.23214 ? 67  MET   B SD    1 
ATOM   3126 C  CE    . MET   C 1 68  ? 7.85200   22.27000  60.15200  1.000 33.29055 ? 67  MET   B CE    1 
ATOM   3127 N  N     . ARG   C 1 69  ? 11.36600  18.91200  56.73100  1.000 24.88400 ? 68  ARG   B N     1 
ATOM   3128 C  CA    . ARG   C 1 69  ? 11.54500  18.44900  55.36100  1.000 24.64114 ? 68  ARG   B CA    1 
ATOM   3129 C  C     . ARG   C 1 69  ? 11.16700  16.98100  55.19000  1.000 26.05198 ? 68  ARG   B C     1 
ATOM   3130 O  O     . ARG   C 1 69  ? 10.64800  16.60500  54.12500  1.000 23.64016 ? 68  ARG   B O     1 
ATOM   3131 C  CB    . ARG   C 1 69  ? 12.95200  18.72900  54.84200  1.000 29.44772 ? 68  ARG   B CB    1 
ATOM   3132 C  CG    . ARG   C 1 69  ? 13.25200  20.21800  54.79600  1.000 26.41249 ? 68  ARG   B CG    1 
ATOM   3133 C  CD    . ARG   C 1 69  ? 14.66400  20.47800  54.32800  1.000 35.60688 ? 68  ARG   B CD    1 
ATOM   3134 N  NE    . ARG   C 1 69  ? 14.89000  19.98800  52.97600  1.000 34.72497 ? 68  ARG   B NE    1 
ATOM   3135 C  CZ    . ARG   C 1 69  ? 14.47900  20.60900  51.88100  1.000 33.74430 ? 68  ARG   B CZ    1 
ATOM   3136 N  NH1   . ARG   C 1 69  ? 13.78000  21.72800  51.94100  1.000 29.40466 ? 68  ARG   B NH1   1 
ATOM   3137 N  NH2   . ARG   C 1 69  ? 14.77500  20.09200  50.69400  1.000 29.82070 ? 68  ARG   B NH2   1 
ATOM   3138 N  N     . ASP   C 1 70  ? 11.41400  16.15000  56.21000  1.000 28.21570 ? 69  ASP   B N     1 
ATOM   3139 C  CA    . ASP   C 1 70  ? 10.96100  14.76300  56.14000  1.000 27.87896 ? 69  ASP   B CA    1 
ATOM   3140 C  C     . ASP   C 1 70  ? 9.44400   14.70900  55.97000  1.000 27.82565 ? 69  ASP   B C     1 
ATOM   3141 O  O     . ASP   C 1 70  ? 8.92500   13.91300  55.18400  1.000 22.84872 ? 69  ASP   B O     1 
ATOM   3142 C  CB    . ASP   C 1 70  ? 11.40700  13.95600  57.36900  1.000 27.85267 ? 69  ASP   B CB    1 
ATOM   3143 C  CG    . ASP   C 1 70  ? 12.91800  13.73300  57.44100  1.000 31.11116 ? 69  ASP   B CG    1 
ATOM   3144 O  OD1   . ASP   C 1 70  ? 13.62800  14.06300  56.46200  1.000 32.79367 ? 69  ASP   B OD1   1 
ATOM   3145 O  OD2   . ASP   C 1 70  ? 13.36600  13.23700  58.50000  1.000 34.04718 ? 69  ASP   B OD2   1 
ATOM   3146 N  N     . GLN   C 1 71  ? 8.71700   15.58700  56.65700  1.000 25.61444 ? 70  GLN   B N     1 
ATOM   3147 C  CA    . GLN   C 1 71  ? 7.26300   15.57000  56.51300  1.000 21.25249 ? 70  GLN   B CA    1 
ATOM   3148 C  C     . GLN   C 1 71  ? 6.84900   16.00200  55.12300  1.000 24.90596 ? 70  GLN   B C     1 
ATOM   3149 O  O     . GLN   C 1 71  ? 5.89800   15.45200  54.56100  1.000 21.10214 ? 70  GLN   B O     1 
ATOM   3150 C  CB    . GLN   C 1 71  ? 6.58700   16.44600  57.57300  1.000 24.24793 ? 70  GLN   B CB    1 
ATOM   3151 C  CG    . GLN   C 1 71  ? 5.09200   16.25900  57.59500  1.000 24.89143 ? 70  GLN   B CG    1 
ATOM   3152 C  CD    . GLN   C 1 71  ? 4.68400   14.82400  57.84500  1.000 27.14767 ? 70  GLN   B CD    1 
ATOM   3153 O  OE1   . GLN   C 1 71  ? 5.08600   14.22000  58.82400  1.000 28.36180 ? 70  GLN   B OE1   1 
ATOM   3154 N  NE2   . GLN   C 1 71  ? 3.90500   14.26800  56.93200  1.000 26.77367 ? 70  GLN   B NE2   1 
ATOM   3155 N  N     . TYR   C 1 72  ? 7.55400   16.97700  54.54000  1.000 19.80178 ? 71  TYR   B N     1 
ATOM   3156 C  CA    . TYR   C 1 72  ? 7.24500   17.36800  53.17500  1.000 18.67194 ? 71  TYR   B CA    1 
ATOM   3157 C  C     . TYR   C 1 72  ? 7.34400   16.16200  52.26200  1.000 21.14964 ? 71  TYR   B C     1 
ATOM   3158 O  O     . TYR   C 1 72  ? 6.51800   15.99000  51.35100  1.000 21.87559 ? 71  TYR   B O     1 
ATOM   3159 C  CB    . TYR   C 1 72  ? 8.26400   18.37800  52.63700  1.000 19.69571 ? 71  TYR   B CB    1 
ATOM   3160 C  CG    . TYR   C 1 72  ? 8.30000   19.76000  53.25000  1.000 20.33385 ? 71  TYR   B CG    1 
ATOM   3161 C  CD1   . TYR   C 1 72  ? 7.26000   20.26500  54.02800  1.000 22.88226 ? 71  TYR   B CD1   1 
ATOM   3162 C  CD2   . TYR   C 1 72  ? 9.40000   20.55500  53.03100  1.000 20.57514 ? 71  TYR   B CD2   1 
ATOM   3163 C  CE1   . TYR   C 1 72  ? 7.33700   21.54500  54.54600  1.000 21.82190 ? 71  TYR   B CE1   1 
ATOM   3164 C  CE2   . TYR   C 1 72  ? 9.48500   21.81900  53.54200  1.000 20.17011 ? 71  TYR   B CE2   1 
ATOM   3165 C  CZ    . TYR   C 1 72  ? 8.44300   22.32400  54.26700  1.000 20.49626 ? 71  TYR   B CZ    1 
ATOM   3166 O  OH    . TYR   C 1 72  ? 8.53800   23.60500  54.78100  1.000 18.95592 ? 71  TYR   B OH    1 
ATOM   3167 N  N     . MET   C 1 73  ? 8.36500   15.32400  52.48300  1.000 21.87916 ? 72  MET   B N     1 
ATOM   3168 C  CA    . MET   C 1 73  ? 8.58700   14.18900  51.60900  1.000 21.51784 ? 72  MET   B CA    1 
ATOM   3169 C  C     . MET   C 1 73  ? 7.60100   13.06600  51.90200  1.000 21.02448 ? 72  MET   B C     1 
ATOM   3170 O  O     . MET   C 1 73  ? 7.15900   12.39600  50.96300  1.000 22.10946 ? 72  MET   B O     1 
ATOM   3171 C  CB    . MET   C 1 73  ? 10.04400  13.72300  51.72100  1.000 20.04898 ? 72  MET   B CB    1 
ATOM   3172 C  CG    . MET   C 1 73  ? 10.94700  14.75500  51.05900  1.000 25.16026 ? 72  MET   B CG    1 
ATOM   3173 S  SD    . MET   C 1 73  ? 12.66800  14.39700  51.35300  1.000 26.64050 ? 72  MET   B SD    1 
ATOM   3174 C  CE    . MET   C 1 73  ? 13.40100  15.78400  50.45800  1.000 26.52765 ? 72  MET   B CE    1 
ATOM   3175 N  N     . ARG   C 1 74  ? 7.19200   12.90000  53.16400  1.000 20.29498 ? 73  ARG   B N     1 
ATOM   3176 C  CA    . ARG   C 1 74  ? 6.18100   11.91900  53.51100  1.000 21.53364 ? 73  ARG   B CA    1 
ATOM   3177 C  C     . ARG   C 1 74  ? 4.85100   12.24300  52.81900  1.000 23.72409 ? 73  ARG   B C     1 
ATOM   3178 O  O     . ARG   C 1 74  ? 4.17900   11.35400  52.27800  1.000 24.10852 ? 73  ARG   B O     1 
ATOM   3179 C  CB    . ARG   C 1 74  ? 6.06100   11.94300  55.04300  1.000 25.83050 ? 73  ARG   B CB    1 
ATOM   3180 C  CG    . ARG   C 1 74  ? 5.19100   10.99800  55.72400  1.000 39.42171 ? 73  ARG   B CG    1 
ATOM   3181 C  CD    . ARG   C 1 74  ? 5.52200   11.04700  57.26400  1.000 33.87681 ? 73  ARG   B CD    1 
ATOM   3182 N  NE    . ARG   C 1 74  ? 6.94600   10.86700  57.54400  1.000 32.52888 ? 73  ARG   B NE    1 
ATOM   3183 C  CZ    . ARG   C 1 74  ? 7.71600   11.63500  58.32100  1.000 29.42353 ? 73  ARG   B CZ    1 
ATOM   3184 N  NH1   . ARG   C 1 74  ? 7.24500   12.68800  58.97300  1.000 30.92384 ? 73  ARG   B NH1   1 
ATOM   3185 N  NH2   . ARG   C 1 74  ? 8.99900   11.32100  58.46700  1.000 29.27512 ? 73  ARG   B NH2   1 
ATOM   3186 N  N     . THR   C 1 75  ? 4.43000   13.50400  52.89200  1.000 20.29619 ? 74  THR   B N     1 
ATOM   3187 C  CA    . THR   C 1 75  ? 3.14500   13.94500  52.35000  1.000 21.48543 ? 74  THR   B CA    1 
ATOM   3188 C  C     . THR   C 1 75  ? 3.13300   14.07200  50.81500  1.000 20.35161 ? 74  THR   B C     1 
ATOM   3189 O  O     . THR   C 1 75  ? 2.09700   13.80700  50.18700  1.000 21.62057 ? 74  THR   B O     1 
ATOM   3190 C  CB    . THR   C 1 75  ? 2.75600   15.28700  53.01300  1.000 22.26260 ? 74  THR   B CB    1 
ATOM   3191 O  OG1   . THR   C 1 75  ? 2.61600   15.13000  54.42900  1.000 25.23970 ? 74  THR   B OG1   1 
ATOM   3192 C  CG2   . THR   C 1 75  ? 1.43200   15.80900  52.47000  1.000 28.15787 ? 74  THR   B CG2   1 
ATOM   3193 N  N     . GLY   C 1 76  ? 4.25300   14.45000  50.19500  1.000 18.17870 ? 75  GLY   B N     1 
ATOM   3194 C  CA    . GLY   C 1 76  ? 4.27000   14.65800  48.74300  1.000 17.71163 ? 75  GLY   B CA    1 
ATOM   3195 C  C     . GLY   C 1 76  ? 4.08500   13.35800  47.96900  1.000 18.77800 ? 75  GLY   B C     1 
ATOM   3196 O  O     . GLY   C 1 76  ? 4.57700   12.28900  48.34500  1.000 19.83242 ? 75  GLY   B O     1 
ATOM   3197 N  N     . GLU   C 1 77  ? 3.32300   13.45300  46.88700  1.000 16.61733 ? 76  GLU   B N     1 
ATOM   3198 C  CA    . GLU   C 1 77  ? 3.11800   12.31500  46.00900  1.000 18.21999 ? 76  GLU   B CA    1 
ATOM   3199 C  C     . GLU   C 1 77  ? 4.11900   12.25800  44.86100  1.000 17.62250 ? 76  GLU   B C     1 
ATOM   3200 O  O     . GLU   C 1 77  ? 4.39800   11.15000  44.35200  1.000 19.15420 ? 76  GLU   B O     1 
ATOM   3201 C  CB    . GLU   C 1 77  ? 1.69400   12.34800  45.44600  1.000 20.04556 ? 76  GLU   B CB    1 
ATOM   3202 C  CG    . GLU   C 1 77  ? 0.61000   12.08000  46.50100  1.000 23.41529 ? 76  GLU   B CG    1 
ATOM   3203 C  CD    . GLU   C 1 77  ? -0.77700  12.17600  45.91200  1.000 30.85908 ? 76  GLU   B CD    1 
ATOM   3204 O  OE1   . GLU   C 1 77  ? -1.26200  13.30700  45.67700  1.000 25.62564 ? 76  GLU   B OE1   1 
ATOM   3205 O  OE2   . GLU   C 1 77  ? -1.39700  11.12100  45.67100  1.000 38.44705 ? 76  GLU   B OE2   1 
ATOM   3206 N  N     . GLY   C 1 78  ? 4.61000   13.40700  44.43600  1.000 15.78676 ? 77  GLY   B N     1 
ATOM   3207 C  CA    . GLY   C 1 78  ? 5.59800   13.45900  43.36600  1.000 16.38324 ? 77  GLY   B CA    1 
ATOM   3208 C  C     . GLY   C 1 78  ? 6.46600   14.67700  43.56700  1.000 16.32842 ? 77  GLY   B C     1 
ATOM   3209 O  O     . GLY   C 1 78  ? 6.05400   15.64100  44.20900  1.000 15.22853 ? 77  GLY   B O     1 
ATOM   3210 N  N     . PHE   C 1 79  ? 7.69200   14.62200  43.03700  1.000 16.29331 ? 78  PHE   B N     1 
ATOM   3211 C  CA    . PHE   C 1 79  ? 8.72500   15.61400  43.33200  1.000 14.61052 ? 78  PHE   B CA    1 
ATOM   3212 C  C     . PHE   C 1 79  ? 9.35800   16.11100  42.05400  1.000 15.18274 ? 78  PHE   B C     1 
ATOM   3213 O  O     . PHE   C 1 79  ? 9.70200   15.30600  41.18600  1.000 16.54236 ? 78  PHE   B O     1 
ATOM   3214 C  CB    . PHE   C 1 79  ? 9.78400   14.99800  44.26600  1.000 16.02980 ? 78  PHE   B CB    1 
ATOM   3215 C  CG    . PHE   C 1 79  ? 9.20100   14.53200  45.54100  1.000 16.48414 ? 78  PHE   B CG    1 
ATOM   3216 C  CD1   . PHE   C 1 79  ? 8.60700   13.29600  45.61500  1.000 17.69777 ? 78  PHE   B CD1   1 
ATOM   3217 C  CD2   . PHE   C 1 79  ? 9.16300   15.36300  46.64800  1.000 16.00622 ? 78  PHE   B CD2   1 
ATOM   3218 C  CE1   . PHE   C 1 79  ? 7.97800   12.89600  46.78100  1.000 19.52503 ? 78  PHE   B CE1   1 
ATOM   3219 C  CE2   . PHE   C 1 79  ? 8.54300   14.97200  47.83000  1.000 16.59379 ? 78  PHE   B CE2   1 
ATOM   3220 C  CZ    . PHE   C 1 79  ? 7.96400   13.74100  47.90700  1.000 18.88943 ? 78  PHE   B CZ    1 
ATOM   3221 N  N     . LEU   C 1 80  ? 9.45100   17.43600  41.91600  1.000 14.59733 ? 79  LEU   B N     1 
ATOM   3222 C  CA    . LEU   C 1 80  ? 10.30100  18.02900  40.88400  1.000 14.59961 ? 79  LEU   B CA    1 
ATOM   3223 C  C     . LEU   C 1 80  ? 11.65700  18.24500  41.50600  1.000 17.70339 ? 79  LEU   B C     1 
ATOM   3224 O  O     . LEU   C 1 80  ? 11.76600  18.88500  42.55900  1.000 16.92018 ? 79  LEU   B O     1 
ATOM   3225 C  CB    . LEU   C 1 80  ? 9.81000   19.38900  40.42900  1.000 17.09597 ? 79  LEU   B CB    1 
ATOM   3226 C  CG    . LEU   C 1 80  ? 8.56500   19.43100  39.59000  1.000 15.90091 ? 79  LEU   B CG    1 
ATOM   3227 C  CD1   . LEU   C 1 80  ? 8.52100   20.88300  39.05300  1.000 18.39154 ? 79  LEU   B CD1   1 
ATOM   3228 C  CD2   . LEU   C 1 80  ? 8.56500   18.41200  38.39900  1.000 18.15722 ? 79  LEU   B CD2   1 
ATOM   3229 N  N     . LEU   C 1 81  ? 12.67700  17.67100  40.90300  1.000 15.42930 ? 80  LEU   B N     1 
ATOM   3230 C  CA    . LEU   C 1 81  ? 14.05300  17.80300  41.36800  1.000 16.79735 ? 80  LEU   B CA    1 
ATOM   3231 C  C     . LEU   C 1 81  ? 14.68000  18.85700  40.47100  1.000 17.29407 ? 80  LEU   B C     1 
ATOM   3232 O  O     . LEU   C 1 81  ? 15.00100  18.57300  39.31300  1.000 17.94807 ? 80  LEU   B O     1 
ATOM   3233 C  CB    . LEU   C 1 81  ? 14.79700  16.48700  41.21100  1.000 19.23967 ? 80  LEU   B CB    1 
ATOM   3234 C  CG    . LEU   C 1 81  ? 14.24700  15.20500  41.83700  1.000 21.53852 ? 80  LEU   B CG    1 
ATOM   3235 C  CD1   . LEU   C 1 81  ? 15.26600  14.03500  41.69100  1.000 28.54556 ? 80  LEU   B CD1   1 
ATOM   3236 C  CD2   . LEU   C 1 81  ? 13.79900  15.39900  43.28400  1.000 22.77836 ? 80  LEU   B CD2   1 
ATOM   3237 N  N     . VAL   C 1 82  ? 14.84500  20.07800  40.97400  1.000 15.38008 ? 81  VAL   B N     1 
ATOM   3238 C  CA    . VAL   C 1 82  ? 15.22600  21.20200  40.12000  1.000 14.71809 ? 81  VAL   B CA    1 
ATOM   3239 C  C     . VAL   C 1 82  ? 16.68800  21.55500  40.33400  1.000 17.15995 ? 81  VAL   B C     1 
ATOM   3240 O  O     . VAL   C 1 82  ? 17.14200  21.71200  41.47600  1.000 17.26709 ? 81  VAL   B O     1 
ATOM   3241 C  CB    . VAL   C 1 82  ? 14.32900  22.42700  40.36900  1.000 14.23274 ? 81  VAL   B CB    1 
ATOM   3242 C  CG1   . VAL   C 1 82  ? 14.59700  23.52400  39.32400  1.000 16.07242 ? 81  VAL   B CG1   1 
ATOM   3243 C  CG2   . VAL   C 1 82  ? 12.83800  22.01800  40.35400  1.000 15.89222 ? 81  VAL   B CG2   1 
ATOM   3244 N  N     . PHE   C 1 83  ? 17.43900  21.68800  39.22400  1.000 15.35578 ? 82  PHE   B N     1 
ATOM   3245 C  CA    . PHE   C 1 83  ? 18.75600  22.30800  39.26400  1.000 16.76048 ? 82  PHE   B CA    1 
ATOM   3246 C  C     . PHE   C 1 83  ? 18.76600  23.42000  38.23100  1.000 16.88465 ? 82  PHE   B C     1 
ATOM   3247 O  O     . PHE   C 1 83  ? 17.83200  23.53900  37.44800  1.000 16.80366 ? 82  PHE   B O     1 
ATOM   3248 C  CB    . PHE   C 1 83  ? 19.87800  21.29000  39.04100  1.000 17.41799 ? 82  PHE   B CB    1 
ATOM   3249 C  CG    . PHE   C 1 83  ? 19.93400  20.71900  37.63600  1.000 17.93216 ? 82  PHE   B CG    1 
ATOM   3250 C  CD1   . PHE   C 1 83  ? 19.12800  19.65100  37.28900  1.000 20.00139 ? 82  PHE   B CD1   1 
ATOM   3251 C  CD2   . PHE   C 1 83  ? 20.79000  21.26500  36.67000  1.000 18.33902 ? 82  PHE   B CD2   1 
ATOM   3252 C  CE1   . PHE   C 1 83  ? 19.18000  19.11000  35.99500  1.000 18.37132 ? 82  PHE   B CE1   1 
ATOM   3253 C  CE2   . PHE   C 1 83  ? 20.82700  20.74400  35.41000  1.000 19.10852 ? 82  PHE   B CE2   1 
ATOM   3254 C  CZ    . PHE   C 1 83  ? 20.03800  19.66100  35.06500  1.000 19.96122 ? 82  PHE   B CZ    1 
ATOM   3255 N  N     . ALA   C 1 84  ? 19.79500  24.25700  38.24900  1.000 17.51521 ? 83  ALA   B N     1 
ATOM   3256 C  CA    . ALA   C 1 84  ? 19.95400  25.27400  37.21700  1.000 18.91833 ? 83  ALA   B CA    1 
ATOM   3257 C  C     . ALA   C 1 84  ? 21.09100  24.87400  36.28800  1.000 19.16425 ? 83  ALA   B C     1 
ATOM   3258 O  O     . ALA   C 1 84  ? 22.16300  24.48400  36.75900  1.000 21.45838 ? 83  ALA   B O     1 
ATOM   3259 C  CB    . ALA   C 1 84  ? 20.28500  26.62500  37.84900  1.000 19.21128 ? 83  ALA   B CB    1 
ATOM   3260 N  N     . ILE   C 1 85  ? 20.86800  24.98700  34.97600  1.000 19.02980 ? 84  ILE   B N     1 
ATOM   3261 C  CA    . ILE   C 1 85  ? 21.86300  24.51800  33.99600  1.000 21.75636 ? 84  ILE   B CA    1 
ATOM   3262 C  C     . ILE   C 1 85  ? 23.17100  25.30600  34.00200  1.000 22.47595 ? 84  ILE   B C     1 
ATOM   3263 O  O     . ILE   C 1 85  ? 24.14000  24.86600  33.38300  1.000 23.79609 ? 84  ILE   B O     1 
ATOM   3264 C  CB    . ILE   C 1 85  ? 21.28800  24.42600  32.56300  1.000 22.69252 ? 84  ILE   B CB    1 
ATOM   3265 C  CG1   . ILE   C 1 85  ? 20.93900  25.81700  32.04400  1.000 24.70329 ? 84  ILE   B CG1   1 
ATOM   3266 C  CG2   . ILE   C 1 85  ? 20.10600  23.45100  32.52600  1.000 21.49135 ? 84  ILE   B CG2   1 
ATOM   3267 C  CD1   . ILE   C 1 85  ? 20.67300  25.84200  30.55800  1.000 27.82531 ? 84  ILE   B CD1   1 
ATOM   3268 N  N     . ASN   C 1 86  ? 23.22500  26.45300  34.68000  1.000 22.02384 ? 85  ASN   B N     1 
ATOM   3269 C  CA    . ASN   C 1 86  ? 24.44100  27.25300  34.80500  1.000 25.93598 ? 85  ASN   B CA    1 
ATOM   3270 C  C     . ASN   C 1 86  ? 25.03200  27.17200  36.20900  1.000 27.54195 ? 85  ASN   B C     1 
ATOM   3271 O  O     . ASN   C 1 86  ? 25.86300  28.00700  36.58500  1.000 28.45556 ? 85  ASN   B O     1 
ATOM   3272 C  CB    . ASN   C 1 86  ? 24.13900  28.70600  34.44600  1.000 25.09735 ? 85  ASN   B CB    1 
ATOM   3273 C  CG    . ASN   C 1 86  ? 23.19500  29.35400  35.45600  1.000 23.39813 ? 85  ASN   B CG    1 
ATOM   3274 O  OD1   . ASN   C 1 86  ? 22.46900  28.65900  36.16500  1.000 24.19118 ? 85  ASN   B OD1   1 
ATOM   3275 N  ND2   . ASN   C 1 86  ? 23.21600  30.67800  35.53700  1.000 28.56264 ? 85  ASN   B ND2   1 
ATOM   3276 N  N     . ASN   C 1 87  ? 24.61900  26.18600  36.99700  1.000 23.51352 ? 86  ASN   B N     1 
ATOM   3277 C  CA    . ASN   C 1 87  ? 25.04700  26.08500  38.40000  1.000 28.18557 ? 86  ASN   B CA    1 
ATOM   3278 C  C     . ASN   C 1 87  ? 25.41300  24.61800  38.61400  1.000 24.05644 ? 86  ASN   B C     1 
ATOM   3279 O  O     . ASN   C 1 87  ? 24.54800  23.79000  38.90500  1.000 23.86618 ? 86  ASN   B O     1 
ATOM   3280 C  CB    . ASN   C 1 87  ? 23.89900  26.56700  39.28700  1.000 26.69181 ? 86  ASN   B CB    1 
ATOM   3281 C  CG    . ASN   C 1 87  ? 24.18100  26.46700  40.77600  1.000 29.60126 ? 86  ASN   B CG    1 
ATOM   3282 O  OD1   . ASN   C 1 87  ? 25.10200  25.78400  41.22700  1.000 27.07389 ? 86  ASN   B OD1   1 
ATOM   3283 N  ND2   . ASN   C 1 87  ? 23.33100  27.12400  41.55900  1.000 32.84629 ? 86  ASN   B ND2   1 
ATOM   3284 N  N     . THR   C 1 88  ? 26.69900  24.29600  38.42800  1.000 28.18820 ? 87  THR   B N     1 
ATOM   3285 C  CA    . THR   C 1 88  ? 27.12500  22.90400  38.53500  1.000 27.67986 ? 87  THR   B CA    1 
ATOM   3286 C  C     . THR   C 1 88  ? 26.86700  22.34600  39.93000  1.000 27.99269 ? 87  THR   B C     1 
ATOM   3287 O  O     . THR   C 1 88  ? 26.47900  21.18300  40.08200  1.000 25.50881 ? 87  THR   B O     1 
ATOM   3288 C  CB    . THR   C 1 88  ? 28.60700  22.77400  38.15700  1.000 31.04748 ? 87  THR   B CB    1 
ATOM   3289 O  OG1   . THR   C 1 88  ? 28.77400  23.10000  36.77400  1.000 36.85880 ? 87  THR   B OG1   1 
ATOM   3290 C  CG2   . THR   C 1 88  ? 29.08900  21.35700  38.40000  1.000 39.44030 ? 87  THR   B CG2   1 
ATOM   3291 N  N     . LYS   C 1 89  ? 27.09100  23.15700  40.96800  1.000 26.69121 ? 88  LYS   B N     1 
ATOM   3292 C  CA    . LYS   C 1 89  ? 26.85100  22.67100  42.31700  1.000 31.30241 ? 88  LYS   B CA    1 
ATOM   3293 C  C     . LYS   C 1 89  ? 25.40500  22.24100  42.48900  1.000 26.28445 ? 88  LYS   B C     1 
ATOM   3294 O  O     . LYS   C 1 89  ? 25.13100  21.20600  43.10700  1.000 25.21840 ? 88  LYS   B O     1 
ATOM   3295 C  CB    . LYS   C 1 89  ? 27.23900  23.73700  43.34300  1.000 32.03452 ? 88  LYS   B CB    1 
ATOM   3296 C  CG    . LYS   C 1 89  ? 26.90200  23.35700  44.77200  1.000 33.29983 ? 88  LYS   B CG    1 
ATOM   3297 C  CD    . LYS   C 1 89  ? 27.65400  22.10600  45.21800  1.000 41.95861 ? 88  LYS   B CD    1 
ATOM   3298 C  CE    . LYS   C 1 89  ? 27.73600  22.04200  46.74900  1.000 42.47702 ? 88  LYS   B CE    1 
ATOM   3299 N  NZ    . LYS   C 1 89  ? 26.40400  22.04100  47.43400  1.000 45.17977 ? 88  LYS   B NZ    1 
ATOM   3300 N  N     . SER   C 1 90  ? 24.45900  22.99700  41.92200  1.000 22.41395 ? 89  SER   B N     1 
ATOM   3301 C  CA    . SER   C 1 90  ? 23.05800  22.60500  42.06400  1.000 22.06251 ? 89  SER   B CA    1 
ATOM   3302 C  C     . SER   C 1 90  ? 22.77900  21.24600  41.42500  1.000 23.62684 ? 89  SER   B C     1 
ATOM   3303 O  O     . SER   C 1 90  ? 21.89700  20.51100  41.88000  1.000 21.52185 ? 89  SER   B O     1 
ATOM   3304 C  CB    . SER   C 1 90  ? 22.12700  23.70900  41.53700  1.000 22.71243 ? 89  SER   B CB    1 
ATOM   3305 O  OG    . SER   C 1 90  ? 22.05500  23.76400  40.08800  1.000 20.69986 ? 89  SER   B OG    1 
ATOM   3306 N  N     . PHE   C 1 91  ? 23.51200  20.88800  40.36200  1.000 23.46607 ? 90  PHE   B N     1 
ATOM   3307 C  CA    . PHE   C 1 91  ? 23.30600  19.57700  39.75700  1.000 22.37665 ? 90  PHE   B CA    1 
ATOM   3308 C  C     . PHE   C 1 91  ? 23.93000  18.47600  40.60700  1.000 23.92221 ? 90  PHE   B C     1 
ATOM   3309 O  O     . PHE   C 1 91  ? 23.36000  17.39500  40.74800  1.000 23.48317 ? 90  PHE   B O     1 
ATOM   3310 C  CB    . PHE   C 1 91  ? 23.87700  19.55000  38.33100  1.000 22.68864 ? 90  PHE   B CB    1 
ATOM   3311 C  CG    . PHE   C 1 91  ? 23.77000  18.19900  37.65200  1.000 22.58280 ? 90  PHE   B CG    1 
ATOM   3312 C  CD1   . PHE   C 1 91  ? 22.56900  17.76400  37.10900  1.000 22.82640 ? 90  PHE   B CD1   1 
ATOM   3313 C  CD2   . PHE   C 1 91  ? 24.88700  17.38100  37.52400  1.000 25.37816 ? 90  PHE   B CD2   1 
ATOM   3314 C  CE1   . PHE   C 1 91  ? 22.49000  16.51300  36.47100  1.000 23.68314 ? 90  PHE   B CE1   1 
ATOM   3315 C  CE2   . PHE   C 1 91  ? 24.81900  16.13400  36.89200  1.000 26.91978 ? 90  PHE   B CE2   1 
ATOM   3316 C  CZ    . PHE   C 1 91  ? 23.61300  15.70500  36.36400  1.000 25.75921 ? 90  PHE   B CZ    1 
ATOM   3317 N  N     . GLU   C 1 92  ? 25.10100  18.74300  41.18900  1.000 25.50358 ? 91  GLU   B N     1 
ATOM   3318 C  CA    . GLU   C 1 92  ? 25.73700  17.76500  42.06200  1.000 29.18761 ? 91  GLU   B CA    1 
ATOM   3319 C  C     . GLU   C 1 92  ? 24.90300  17.51300  43.30900  1.000 30.59230 ? 91  GLU   B C     1 
ATOM   3320 O  O     . GLU   C 1 92  ? 24.99600  16.43600  43.91600  1.000 35.83157 ? 91  GLU   B O     1 
ATOM   3321 C  CB    . GLU   C 1 92  ? 27.12300  18.27100  42.44400  1.000 33.57198 ? 91  GLU   B CB    1 
ATOM   3322 C  CG    . GLU   C 1 92  ? 28.01200  18.51300  41.23100  1.000 33.84208 ? 91  GLU   B CG    1 
ATOM   3323 C  CD    . GLU   C 1 92  ? 29.40100  19.04500  41.58800  1.000 39.54495 ? 91  GLU   B CD    1 
ATOM   3324 O  OE1   . GLU   C 1 92  ? 29.51400  19.81700  42.56700  1.000 48.71018 ? 91  GLU   B OE1   1 
ATOM   3325 O  OE2   . GLU   C 1 92  ? 30.36700  18.70200  40.88300  1.000 50.29304 ? 91  GLU   B OE2   1 
ATOM   3326 N  N     . ASP   C 1 93  ? 24.07800  18.49000  43.68800  1.000 27.09635 ? 92  ASP   B N     1 
ATOM   3327 C  CA    . ASP   C 1 93  ? 23.18800  18.37100  44.84100  1.000 28.02572 ? 92  ASP   B CA    1 
ATOM   3328 C  C     . ASP   C 1 93  ? 22.00500  17.44700  44.58400  1.000 30.62364 ? 92  ASP   B C     1 
ATOM   3329 O  O     . ASP   C 1 93  ? 21.35500  17.01600  45.54500  1.000 28.90357 ? 92  ASP   B O     1 
ATOM   3330 C  CB    . ASP   C 1 93  ? 22.61200  19.75100  45.20100  1.000 28.84343 ? 92  ASP   B CB    1 
ATOM   3331 C  CG    . ASP   C 1 93  ? 23.61300  20.63600  45.94700  1.000 37.46257 ? 92  ASP   B CG    1 
ATOM   3332 O  OD1   . ASP   C 1 93  ? 24.70600  20.14800  46.30900  1.000 39.01550 ? 92  ASP   B OD1   1 
ATOM   3333 O  OD2   . ASP   C 1 93  ? 23.29900  21.82600  46.17700  1.000 41.76397 ? 92  ASP   B OD2   1 
ATOM   3334 N  N     . ILE   C 1 94  ? 21.68700  17.16700  43.31700  1.000 24.64543 ? 93  ILE   B N     1 
ATOM   3335 C  CA    . ILE   C 1 94  ? 20.45000  16.46600  42.97300  1.000 24.34862 ? 93  ILE   B CA    1 
ATOM   3336 C  C     . ILE   C 1 94  ? 20.38100  15.10400  43.65100  1.000 30.26104 ? 93  ILE   B C     1 
ATOM   3337 O  O     . ILE   C 1 94  ? 19.35000  14.72400  44.23100  1.000 28.42694 ? 93  ILE   B O     1 
ATOM   3338 C  CB    . ILE   C 1 94  ? 20.32000  16.34300  41.44200  1.000 25.93567 ? 93  ILE   B CB    1 
ATOM   3339 C  CG1   . ILE   C 1 94  ? 19.93500  17.68900  40.82800  1.000 22.33167 ? 93  ILE   B CG1   1 
ATOM   3340 C  CG2   . ILE   C 1 94  ? 19.33200  15.25700  41.06900  1.000 24.43700 ? 93  ILE   B CG2   1 
ATOM   3341 C  CD1   . ILE   C 1 94  ? 18.50500  18.16700  41.14500  1.000 21.05041 ? 93  ILE   B CD1   1 
ATOM   3342 N  N     . HIS   C 1 95  ? 21.46500  14.34700  43.58300  1.000 26.52005 ? 94  HIS   B N     1 
ATOM   3343 C  CA    . HIS   C 1 95  ? 21.41100  12.99200  44.11300  1.000 27.04198 ? 94  HIS   B CA    1 
ATOM   3344 C  C     . HIS   C 1 95  ? 21.09200  12.98900  45.60200  1.000 32.06500 ? 94  HIS   B C     1 
ATOM   3345 O  O     . HIS   C 1 95  ? 20.41600  12.07500  46.08200  1.000 32.86508 ? 94  HIS   B O     1 
ATOM   3346 C  CB    . HIS   C 1 95  ? 22.67800  12.21800  43.76000  1.000 34.81328 ? 94  HIS   B CB    1 
ATOM   3347 C  CG    . HIS   C 1 95  ? 23.82600  12.49800  44.66400  1.000 43.01738 ? 94  HIS   B CG    1 
ATOM   3348 N  ND1   . HIS   C 1 95  ? 24.67500  13.56800  44.48400  1.000 48.33459 ? 94  HIS   B ND1   1 
ATOM   3349 C  CD2   . HIS   C 1 95  ? 24.27700  11.83500  45.75300  1.000 43.84221 ? 94  HIS   B CD2   1 
ATOM   3350 C  CE1   . HIS   C 1 95  ? 25.60400  13.55000  45.42400  1.000 44.41165 ? 94  HIS   B CE1   1 
ATOM   3351 N  NE2   . HIS   C 1 95  ? 25.38500  12.50800  46.20500  1.000 49.29947 ? 94  HIS   B NE2   1 
ATOM   3352 N  N     . HIS   C 1 96  ? 21.48700  14.03400  46.33500  1.000 29.89188 ? 95  HIS   B N     1 
ATOM   3353 C  CA    . HIS   C 1 96  ? 21.16200  14.07000  47.76200  1.000 30.18944 ? 95  HIS   B CA    1 
ATOM   3354 C  C     . HIS   C 1 96  ? 19.67100  14.30200  48.00400  1.000 30.23202 ? 95  HIS   B C     1 
ATOM   3355 O  O     . HIS   C 1 96  ? 19.08800  13.70500  48.92000  1.000 31.63197 ? 95  HIS   B O     1 
ATOM   3356 C  CB    . HIS   C 1 96  ? 22.02100  15.10700  48.48200  1.000 33.51566 ? 95  HIS   B CB    1 
ATOM   3357 C  CG    . HIS   C 1 96  ? 23.47700  14.77200  48.48100  1.000 49.96626 ? 95  HIS   B CG    1 
ATOM   3358 N  ND1   . HIS   C 1 96  ? 24.45200  15.67800  48.12000  1.000 54.52202 ? 95  HIS   B ND1   1 
ATOM   3359 C  CD2   . HIS   C 1 96  ? 24.12600  13.62500  48.79200  1.000 50.88029 ? 95  HIS   B CD2   1 
ATOM   3360 C  CE1   . HIS   C 1 96  ? 25.63900  15.10400  48.21500  1.000 48.35990 ? 95  HIS   B CE1   1 
ATOM   3361 N  NE2   . HIS   C 1 96  ? 25.46900  13.85800  48.62100  1.000 55.04469 ? 95  HIS   B NE2   1 
ATOM   3362 N  N     . TYR   C 1 97  ? 19.03100  15.15300  47.19800  1.000 26.95513 ? 96  TYR   B N     1 
ATOM   3363 C  CA    . TYR   C 1 97  ? 17.57700  15.30100  47.30600  1.000 24.63573 ? 96  TYR   B CA    1 
ATOM   3364 C  C     . TYR   C 1 97  ? 16.86900  13.99000  46.99100  1.000 28.73617 ? 96  TYR   B C     1 
ATOM   3365 O  O     . TYR   C 1 97  ? 15.93500  13.59000  47.70500  1.000 27.00351 ? 96  TYR   B O     1 
ATOM   3366 C  CB    . TYR   C 1 97  ? 17.04700  16.41000  46.38200  1.000 25.50382 ? 96  TYR   B CB    1 
ATOM   3367 C  CG    . TYR   C 1 97  ? 17.45800  17.79400  46.82400  1.000 28.94960 ? 96  TYR   B CG    1 
ATOM   3368 C  CD1   . TYR   C 1 97  ? 16.73600  18.49700  47.79500  1.000 25.49549 ? 96  TYR   B CD1   1 
ATOM   3369 C  CD2   . TYR   C 1 97  ? 18.57100  18.41100  46.26700  1.000 28.09223 ? 96  TYR   B CD2   1 
ATOM   3370 C  CE1   . TYR   C 1 97  ? 17.15200  19.75100  48.20900  1.000 26.31143 ? 96  TYR   B CE1   1 
ATOM   3371 C  CE2   . TYR   C 1 97  ? 18.98700  19.65700  46.67400  1.000 26.50932 ? 96  TYR   B CE2   1 
ATOM   3372 C  CZ    . TYR   C 1 97  ? 18.27000  20.33500  47.64600  1.000 33.08385 ? 96  TYR   B CZ    1 
ATOM   3373 O  OH    . TYR   C 1 97  ? 18.69900  21.59200  48.05500  1.000 29.80975 ? 96  TYR   B OH    1 
ATOM   3374 N  N     . ARG   C 1 98  ? 17.28400  13.31000  45.92400  1.000 27.29172 ? 97  ARG   B N     1 
ATOM   3375 C  CA    . ARG   C 1 98  ? 16.68200  12.01500  45.62100  1.000 27.06750 ? 97  ARG   B CA    1 
ATOM   3376 C  C     . ARG   C 1 98  ? 16.89500  11.01700  46.75500  1.000 31.45175 ? 97  ARG   B C     1 
ATOM   3377 O  O     . ARG   C 1 98  ? 15.97400  10.27200  47.11000  1.000 29.07430 ? 97  ARG   B O     1 
ATOM   3378 C  CB    . ARG   C 1 98  ? 17.20300  11.46500  44.30100  1.000 27.77485 ? 97  ARG   B CB    1 
ATOM   3379 C  CG    . ARG   C 1 98  ? 16.62400  10.10200  43.96800  1.000 29.69340 ? 97  ARG   B CG    1 
ATOM   3380 C  CD    . ARG   C 1 98  ? 17.06700  9.67100   42.58800  1.000 29.44719 ? 97  ARG   B CD    1 
ATOM   3381 N  NE    . ARG   C 1 98  ? 16.93800  8.23700   42.39700  1.000 31.90594 ? 97  ARG   B NE    1 
ATOM   3382 C  CZ    . ARG   C 1 98  ? 15.84300  7.63200   41.95600  1.000 42.62745 ? 97  ARG   B CZ    1 
ATOM   3383 N  NH1   . ARG   C 1 98  ? 14.74900  8.31800   41.64900  1.000 41.31184 ? 97  ARG   B NH1   1 
ATOM   3384 N  NH2   . ARG   C 1 98  ? 15.84600  6.30700   41.81900  1.000 43.12385 ? 97  ARG   B NH2   1 
ATOM   3385 N  N     . GLU   C 1 99  ? 18.09700  10.97600  47.34000  1.000 27.78284 ? 98  GLU   B N     1 
ATOM   3386 C  CA    . GLU   C 1 99  ? 18.35700  10.00300  48.40100  1.000 28.65056 ? 98  GLU   B CA    1 
ATOM   3387 C  C     . GLU   C 1 99  ? 17.48100  10.29200  49.61600  1.000 26.18848 ? 98  GLU   B C     1 
ATOM   3388 O  O     . GLU   C 1 99  ? 16.97200  9.35800   50.25000  1.000 28.24759 ? 98  GLU   B O     1 
ATOM   3389 C  CB    . GLU   C 1 99  ? 19.84200  9.99900   48.77100  1.000 30.71965 ? 98  GLU   B CB    1 
ATOM   3390 C  CG    . GLU   C 1 99  ? 20.71200  8.99100   47.99300  1.000 43.64825 ? 98  GLU   B CG    1 
ATOM   3391 C  CD    . GLU   C 1 99  ? 22.20500  9.25900   48.16100  1.000 51.78859 ? 98  GLU   B CD    1 
ATOM   3392 O  OE1   . GLU   C 1 99  ? 22.54400  10.18000  48.93800  1.000 55.48556 ? 98  GLU   B OE1   1 
ATOM   3393 O  OE2   . GLU   C 1 99  ? 23.03900  8.56500   47.52300  1.000 49.12670 ? 98  GLU   B OE2   1 
ATOM   3394 N  N     . GLN   C 1 100 ? 17.31000  11.57100  49.96100  1.000 27.29183 ? 99  GLN   B N     1 
ATOM   3395 C  CA    . GLN   C 1 100 ? 16.41700  11.94700  51.05600  1.000 27.50963 ? 99  GLN   B CA    1 
ATOM   3396 C  C     . GLN   C 1 100 ? 14.99900  11.45400  50.81200  1.000 26.75747 ? 99  GLN   B C     1 
ATOM   3397 O  O     . GLN   C 1 100 ? 14.34000  10.95300  51.72900  1.000 25.92249 ? 99  GLN   B O     1 
ATOM   3398 C  CB    . GLN   C 1 100 ? 16.43100  13.46000  51.26200  1.000 30.40756 ? 99  GLN   B CB    1 
ATOM   3399 C  CG    . GLN   C 1 100 ? 17.59500  13.91200  52.06800  1.000 32.37110 ? 99  GLN   B CG    1 
ATOM   3400 C  CD    . GLN   C 1 100 ? 17.58900  13.22200  53.40500  1.000 45.13656 ? 99  GLN   B CD    1 
ATOM   3401 O  OE1   . GLN   C 1 100 ? 16.62200  13.32400  54.16600  1.000 45.69736 ? 99  GLN   B OE1   1 
ATOM   3402 N  NE2   . GLN   C 1 100 ? 18.63600  12.47600  53.67800  1.000 42.93299 ? 99  GLN   B NE2   1 
ATOM   3403 N  N     . ILE   C 1 101 ? 14.50500  11.58100  49.58500  1.000 25.19014 ? 100 ILE   B N     1 
ATOM   3404 C  CA    . ILE   C 1 101 ? 13.13000  11.17600  49.31100  1.000 22.87280 ? 100 ILE   B CA    1 
ATOM   3405 C  C     . ILE   C 1 101 ? 12.99200  9.67200   49.42100  1.000 22.98268 ? 100 ILE   B C     1 
ATOM   3406 O  O     . ILE   C 1 101 ? 12.04200  9.15800   50.03000  1.000 24.08092 ? 100 ILE   B O     1 
ATOM   3407 C  CB    . ILE   C 1 101 ? 12.74300  11.66100  47.90600  1.000 26.06227 ? 100 ILE   B CB    1 
ATOM   3408 C  CG1   . ILE   C 1 101 ? 12.71300  13.17900  47.88500  1.000 21.91932 ? 100 ILE   B CG1   1 
ATOM   3409 C  CG2   . ILE   C 1 101 ? 11.41700  11.04600  47.46300  1.000 27.42530 ? 100 ILE   B CG2   1 
ATOM   3410 C  CD1   . ILE   C 1 101 ? 12.69900  13.75500  46.43200  1.000 21.81260 ? 100 ILE   B CD1   1 
ATOM   3411 N  N     . LYS   C 1 102 ? 13.95700  8.93200   48.86700  1.000 22.94379 ? 101 LYS   B N     1 
ATOM   3412 C  CA    . LYS   C 1 102 ? 13.94200  7.47300   49.00000  1.000 26.08111 ? 101 LYS   B CA    1 
ATOM   3413 C  C     . LYS   C 1 102 ? 14.00500  7.03900   50.45900  1.000 26.37910 ? 101 LYS   B C     1 
ATOM   3414 O  O     . LYS   C 1 102 ? 13.38900  6.03700   50.83800  1.000 27.77097 ? 101 LYS   B O     1 
ATOM   3415 C  CB    . LYS   C 1 102 ? 15.10400  6.82700   48.23000  1.000 26.13230 ? 101 LYS   B CB    1 
ATOM   3416 C  CG    . LYS   C 1 102 ? 15.00800  7.05100   46.69800  1.000 28.75287 ? 101 LYS   B CG    1 
ATOM   3417 C  CD    . LYS   C 1 102 ? 16.31700  6.71500   45.92900  1.000 38.21488 ? 101 LYS   B CD    1 
ATOM   3418 C  CE    . LYS   C 1 102 ? 16.92600  5.43900   46.39000  1.000 37.83361 ? 101 LYS   B CE    1 
ATOM   3419 N  NZ    . LYS   C 1 102 ? 18.33800  5.22000   45.90700  1.000 36.55998 ? 101 LYS   B NZ    1 
ATOM   3420 N  N     . ARG   C 1 103 ? 14.80600  7.73500   51.27100  1.000 26.41174 ? 102 ARG   B N     1 
ATOM   3421 C  CA    . ARG   C 1 103 ? 14.97300  7.36700   52.67800  1.000 28.08647 ? 102 ARG   B CA    1 
ATOM   3422 C  C     . ARG   C 1 103 ? 13.68300  7.59900   53.43700  1.000 27.38355 ? 102 ARG   B C     1 
ATOM   3423 O  O     . ARG   C 1 103 ? 13.24400  6.74100   54.21300  1.000 28.88585 ? 102 ARG   B O     1 
ATOM   3424 C  CB    . ARG   C 1 103 ? 16.11800  8.19600   53.28200  1.000 31.91827 ? 102 ARG   B CB    1 
ATOM   3425 C  CG    . ARG   C 1 103 ? 16.47000  7.91400   54.74000  1.000 39.60160 ? 102 ARG   B CG    1 
ATOM   3426 C  CD    . ARG   C 1 103 ? 17.53600  8.91200   55.26900  1.000 45.28442 ? 102 ARG   B CD    1 
ATOM   3427 N  NE    . ARG   C 1 103 ? 18.77900  8.95000   54.49000  1.000 52.71285 ? 102 ARG   B NE    1 
ATOM   3428 C  CZ    . ARG   C 1 103 ? 19.88600  8.25200   54.74900  1.000 48.66749 ? 102 ARG   B CZ    1 
ATOM   3429 N  NH1   . ARG   C 1 103 ? 19.94500  7.34900   55.73400  1.000 43.70282 ? 102 ARG   B NH1   1 
ATOM   3430 N  NH2   . ARG   C 1 103 ? 20.96600  8.45400   53.99400  1.000 46.96864 ? 102 ARG   B NH2   1 
ATOM   3431 N  N     . VAL   C 1 104 ? 13.06300  8.74800   53.21700  1.000 25.28090 ? 103 VAL   B N     1 
ATOM   3432 C  CA    . VAL   C 1 104 ? 11.86800  9.13300   53.96500  1.000 27.14024 ? 103 VAL   B CA    1 
ATOM   3433 C  C     . VAL   C 1 104 ? 10.67000  8.29900   53.54100  1.000 24.70303 ? 103 VAL   B C     1 
ATOM   3434 O  O     . VAL   C 1 104 ? 9.86100   7.87700   54.38700  1.000 28.87281 ? 103 VAL   B O     1 
ATOM   3435 C  CB    . VAL   C 1 104 ? 11.58700  10.63800  53.79600  1.000 26.85971 ? 103 VAL   B CB    1 
ATOM   3436 C  CG1   . VAL   C 1 104 ? 10.17300  10.94700  54.25600  1.000 30.37389 ? 103 VAL   B CG1   1 
ATOM   3437 C  CG2   . VAL   C 1 104 ? 12.61500  11.44500  54.57600  1.000 28.03989 ? 103 VAL   B CG2   1 
ATOM   3438 N  N     . LYS   C 1 105 ? 10.49800  8.11200   52.23500  1.000 26.20680 ? 104 LYS   B N     1 
ATOM   3439 C  CA    . LYS   C 1 105 ? 9.43200   7.26000   51.73000  1.000 30.38970 ? 104 LYS   B CA    1 
ATOM   3440 C  C     . LYS   C 1 105 ? 9.79500   5.77600   51.69900  1.000 29.44769 ? 104 LYS   B C     1 
ATOM   3441 O  O     . LYS   C 1 105 ? 8.92500   4.94600   51.40800  1.000 29.38303 ? 104 LYS   B O     1 
ATOM   3442 C  CB    . LYS   C 1 105 ? 8.92400   7.79500   50.39900  1.000 32.73558 ? 104 LYS   B CB    1 
ATOM   3443 C  CG    . LYS   C 1 105 ? 8.51800   9.26800   50.53000  1.000 30.15399 ? 104 LYS   B CG    1 
ATOM   3444 C  CD    . LYS   C 1 105 ? 8.10600   9.93200   49.22300  1.000 28.33995 ? 104 LYS   B CD    1 
ATOM   3445 C  CE    . LYS   C 1 105 ? 6.61200   9.74800   48.89700  1.000 23.34357 ? 104 LYS   B CE    1 
ATOM   3446 N  NZ    . LYS   C 1 105 ? 5.68900   10.22500  49.96000  1.000 24.06171 ? 104 LYS   B NZ    1 
ATOM   3447 N  N     . ASP   C 1 106 ? 11.03400  5.41100   52.05600  1.000 27.80138 ? 105 ASP   B N     1 
ATOM   3448 C  CA    . ASP   C 1 106 ? 11.45100  4.01200   52.13400  1.000 30.22786 ? 105 ASP   B CA    1 
ATOM   3449 C  C     . ASP   C 1 106 ? 11.12200  3.25200   50.85000  1.000 30.36666 ? 105 ASP   B C     1 
ATOM   3450 O  O     . ASP   C 1 106 ? 10.47900  2.20500   50.85800  1.000 31.81465 ? 105 ASP   B O     1 
ATOM   3451 C  CB    . ASP   C 1 106 ? 10.86100  3.32300   53.36400  1.000 31.97732 ? 105 ASP   B CB    1 
ATOM   3452 C  CG    . ASP   C 1 106 ? 11.43100  1.93700   53.55900  1.000 34.79896 ? 105 ASP   B CG    1 
ATOM   3453 O  OD1   . ASP   C 1 106 ? 12.65000  1.78400   53.31000  1.000 35.59312 ? 105 ASP   B OD1   1 
ATOM   3454 O  OD2   . ASP   C 1 106 ? 10.68100  0.99400   53.90900  1.000 36.37711 ? 105 ASP   B OD2   1 
ATOM   3455 N  N     . SER   C 1 107 ? 11.56700  3.80100   49.72100  1.000 30.53733 ? 106 SER   B N     1 
ATOM   3456 C  CA    . SER   C 1 107 ? 11.22800  3.21400   48.43200  1.000 31.33335 ? 106 SER   B CA    1 
ATOM   3457 C  C     . SER   C 1 107 ? 12.20500  3.70000   47.37100  1.000 30.25778 ? 106 SER   B C     1 
ATOM   3458 O  O     . SER   C 1 107 ? 12.64800  4.85800   47.38800  1.000 31.15163 ? 106 SER   B O     1 
ATOM   3459 C  CB    . SER   C 1 107 ? 9.81400   3.63800   48.01200  1.000 37.72523 ? 106 SER   B CB    1 
ATOM   3460 O  OG    . SER   C 1 107 ? 9.57200   3.28000   46.66300  1.000 38.96332 ? 106 SER   B OG    1 
ATOM   3461 N  N     . GLU   C 1 108 ? 12.47300  2.81700   46.40900  1.000 33.18008 ? 107 GLU   B N     1 
ATOM   3462 C  CA    . GLU   C 1 108 ? 13.25200  3.14200   45.22400  1.000 33.17029 ? 107 GLU   B CA    1 
ATOM   3463 C  C     . GLU   C 1 108 ? 12.39500  3.62400   44.06200  1.000 33.41742 ? 107 GLU   B C     1 
ATOM   3464 O  O     . GLU   C 1 108 ? 12.94400  3.99200   43.01800  1.000 45.19249 ? 107 GLU   B O     1 
ATOM   3465 C  CB    . GLU   C 1 108 ? 14.04400  1.91600   44.76500  1.000 39.48117 ? 107 GLU   B CB    1 
ATOM   3466 C  CG    . GLU   C 1 108 ? 15.12200  1.46400   45.71100  1.000 39.62356 ? 107 GLU   B CG    1 
ATOM   3467 C  CD    . GLU   C 1 108 ? 16.05700  0.46100   45.07500  1.000 49.62242 ? 107 GLU   B CD    1 
ATOM   3468 O  OE1   . GLU   C 1 108 ? 15.63200  -0.23100  44.12100  1.000 56.16366 ? 107 GLU   B OE1   1 
ATOM   3469 O  OE2   . GLU   C 1 108 ? 17.22000  0.37400   45.52300  1.000 50.44890 ? 107 GLU   B OE2   1 
ATOM   3470 N  N     . ASP   C 1 109 ? 11.07300  3.59500   44.19600  1.000 32.53752 ? 108 ASP   B N     1 
ATOM   3471 C  CA    . ASP   C 1 109 ? 10.14600  3.92400   43.11200  1.000 35.02417 ? 108 ASP   B CA    1 
ATOM   3472 C  C     . ASP   C 1 109 ? 9.20300   5.02500   43.59200  1.000 36.22646 ? 108 ASP   B C     1 
ATOM   3473 O  O     . ASP   C 1 109 ? 8.05700   4.76500   43.96500  1.000 41.51849 ? 108 ASP   B O     1 
ATOM   3474 C  CB    . ASP   C 1 109 ? 9.37200   2.66200   42.68800  1.000 44.22505 ? 108 ASP   B CB    1 
ATOM   3475 C  CG    . ASP   C 1 109 ? 8.37100   2.92900   41.57500  1.000 48.37320 ? 108 ASP   B CG    1 
ATOM   3476 O  OD1   . ASP   C 1 109 ? 8.54400   3.91700   40.82800  1.000 48.14185 ? 108 ASP   B OD1   1 
ATOM   3477 O  OD2   . ASP   C 1 109 ? 7.41100   2.13800   41.45800  1.000 52.78097 ? 108 ASP   B OD2   1 
ATOM   3478 N  N     . VAL   C 1 110 ? 9.68700   6.25700   43.59000  1.000 28.39249 ? 109 VAL   B N     1 
ATOM   3479 C  CA    . VAL   C 1 110 ? 8.89800   7.42800   43.97000  1.000 24.72071 ? 109 VAL   B CA    1 
ATOM   3480 C  C     . VAL   C 1 110 ? 8.75000   8.30900   42.73200  1.000 23.65892 ? 109 VAL   B C     1 
ATOM   3481 O  O     . VAL   C 1 110 ? 9.75000   8.56700   42.05800  1.000 22.99564 ? 109 VAL   B O     1 
ATOM   3482 C  CB    . VAL   C 1 110 ? 9.58200   8.22400   45.09400  1.000 24.62534 ? 109 VAL   B CB    1 
ATOM   3483 C  CG1   . VAL   C 1 110 ? 8.73100   9.41900   45.45200  1.000 22.38121 ? 109 VAL   B CG1   1 
ATOM   3484 C  CG2   . VAL   C 1 110 ? 9.89400   7.34800   46.32100  1.000 26.70591 ? 109 VAL   B CG2   1 
ATOM   3485 N  N     . PRO   C 1 111 ? 7.55100   8.79900   42.40800  1.000 21.83232 ? 110 PRO   B N     1 
ATOM   3486 C  CA    . PRO   C 1 111 ? 7.40700   9.68000   41.22900  1.000 19.91526 ? 110 PRO   B CA    1 
ATOM   3487 C  C     . PRO   C 1 111 ? 8.24500   10.94400  41.35800  1.000 18.50887 ? 110 PRO   B C     1 
ATOM   3488 O  O     . PRO   C 1 111 ? 8.09900   11.72000  42.31500  1.000 18.39382 ? 110 PRO   B O     1 
ATOM   3489 C  CB    . PRO   C 1 111 ? 5.90900   9.99700   41.20300  1.000 21.55912 ? 110 PRO   B CB    1 
ATOM   3490 C  CG    . PRO   C 1 111 ? 5.27200   8.82500   41.91300  1.000 21.29633 ? 110 PRO   B CG    1 
ATOM   3491 C  CD    . PRO   C 1 111 ? 6.25100   8.44800   43.00900  1.000 24.23190 ? 110 PRO   B CD    1 
ATOM   3492 N  N     . MET   C 1 112 ? 9.12000   11.16300  40.37100  1.000 20.24548 ? 111 MET   B N     1 
ATOM   3493 C  CA    . MET   C 1 112 ? 9.95500   12.35100  40.31500  1.000 18.12940 ? 111 MET   B CA    1 
ATOM   3494 C  C     . MET   C 1 112 ? 10.25700  12.68100  38.86300  1.000 17.32091 ? 111 MET   B C     1 
ATOM   3495 O  O     . MET   C 1 112 ? 10.25000  11.79700  37.98700  1.000 19.11328 ? 111 MET   B O     1 
ATOM   3496 C  CB    . MET   C 1 112 ? 11.32100  12.15900  40.99600  1.000 23.00580 ? 111 MET   B CB    1 
ATOM   3497 C  CG    . MET   C 1 112 ? 11.33300  11.53300  42.38500  1.000 25.91984 ? 111 MET   B CG    1 
ATOM   3498 S  SD    . MET   C 1 112 ? 13.02000  11.20800  42.94700  1.000 32.85247 ? 111 MET   B SD    1 
ATOM   3499 C  CE    . MET   C 1 112 ? 12.70800  10.16900  44.36000  1.000 34.75933 ? 111 MET   B CE    1 
ATOM   3500 N  N     . VAL   C 1 113 ? 10.56700  13.95200  38.63200  1.000 16.07349 ? 112 VAL   B N     1 
ATOM   3501 C  CA    . VAL   C 1 113 ? 11.00800  14.44900  37.32500  1.000 17.32986 ? 112 VAL   B CA    1 
ATOM   3502 C  C     . VAL   C 1 113 ? 12.22200  15.32200  37.57700  1.000 18.65842 ? 112 VAL   B C     1 
ATOM   3503 O  O     . VAL   C 1 113 ? 12.21300  16.13000  38.50600  1.000 17.60073 ? 112 VAL   B O     1 
ATOM   3504 C  CB    . VAL   C 1 113 ? 9.89300   15.24000  36.63100  1.000 17.82360 ? 112 VAL   B CB    1 
ATOM   3505 C  CG1   . VAL   C 1 113 ? 10.42800  15.91300  35.34600  1.000 17.41763 ? 112 VAL   B CG1   1 
ATOM   3506 C  CG2   . VAL   C 1 113 ? 8.74300   14.31200  36.30100  1.000 19.32858 ? 112 VAL   B CG2   1 
ATOM   3507 N  N     . LEU   C 1 114 ? 13.28900  15.12400  36.80200  1.000 18.28534 ? 113 LEU   B N     1 
ATOM   3508 C  CA    . LEU   C 1 114 ? 14.48500  15.95900  36.86800  1.000 18.00662 ? 113 LEU   B CA    1 
ATOM   3509 C  C     . LEU   C 1 114 ? 14.27100  17.17700  35.97100  1.000 16.31596 ? 113 LEU   B C     1 
ATOM   3510 O  O     . LEU   C 1 114 ? 13.88100  17.02400  34.81600  1.000 17.47002 ? 113 LEU   B O     1 
ATOM   3511 C  CB    . LEU   C 1 114 ? 15.70400  15.16000  36.38800  1.000 19.81317 ? 113 LEU   B CB    1 
ATOM   3512 C  CG    . LEU   C 1 114 ? 17.04100  15.89000  36.48100  1.000 18.98329 ? 113 LEU   B CG    1 
ATOM   3513 C  CD1   . LEU   C 1 114 ? 17.39600  16.19100  37.94900  1.000 20.46358 ? 113 LEU   B CD1   1 
ATOM   3514 C  CD2   . LEU   C 1 114 ? 18.11000  15.04100  35.80300  1.000 23.00571 ? 113 LEU   B CD2   1 
ATOM   3515 N  N     . VAL   C 1 115 ? 14.44900  18.37200  36.52600  1.000 15.37865 ? 114 VAL   B N     1 
ATOM   3516 C  CA    . VAL   C 1 115 ? 14.22500  19.62500  35.81000  1.000 14.91611 ? 114 VAL   B CA    1 
ATOM   3517 C  C     . VAL   C 1 115 ? 15.52500  20.42000  35.79700  1.000 16.30490 ? 114 VAL   B C     1 
ATOM   3518 O  O     . VAL   C 1 115 ? 16.04500  20.79500  36.85600  1.000 16.79960 ? 114 VAL   B O     1 
ATOM   3519 C  CB    . VAL   C 1 115 ? 13.12700  20.45400  36.49000  1.000 15.11747 ? 114 VAL   B CB    1 
ATOM   3520 C  CG1   . VAL   C 1 115 ? 12.95000  21.76300  35.76600  1.000 18.33050 ? 114 VAL   B CG1   1 
ATOM   3521 C  CG2   . VAL   C 1 115 ? 11.81600  19.71500  36.51500  1.000 16.80223 ? 114 VAL   B CG2   1 
ATOM   3522 N  N     . GLY   C 1 116 ? 16.03700  20.70800  34.59900  1.000 16.81621 ? 115 GLY   B N     1 
ATOM   3523 C  CA    . GLY   C 1 116 ? 17.16500  21.61800  34.44200  1.000 16.95947 ? 115 GLY   B CA    1 
ATOM   3524 C  C     . GLY   C 1 116 ? 16.63700  22.96300  34.02100  1.000 14.77437 ? 115 GLY   B C     1 
ATOM   3525 O  O     . GLY   C 1 116 ? 16.24600  23.15000  32.85800  1.000 16.69855 ? 115 GLY   B O     1 
ATOM   3526 N  N     . ASN   C 1 117 ? 16.60400  23.90600  34.94400  1.000 16.19064 ? 116 ASN   B N     1 
ATOM   3527 C  CA    . ASN   C 1 117 ? 15.99500  25.20000  34.71200  1.000 14.91973 ? 116 ASN   B CA    1 
ATOM   3528 C  C     . ASN   C 1 117 ? 17.03200  26.21700  34.23500  1.000 15.31584 ? 116 ASN   B C     1 
ATOM   3529 O  O     . ASN   C 1 117 ? 18.24300  25.97800  34.27700  1.000 17.00607 ? 116 ASN   B O     1 
ATOM   3530 C  CB    . ASN   C 1 117 ? 15.29600  25.68600  35.99800  1.000 15.94297 ? 116 ASN   B CB    1 
ATOM   3531 C  CG    . ASN   C 1 117 ? 14.43400  26.89700  35.75700  1.000 15.00212 ? 116 ASN   B CG    1 
ATOM   3532 O  OD1   . ASN   C 1 117 ? 13.69700  26.96700  34.77800  1.000 16.44962 ? 116 ASN   B OD1   1 
ATOM   3533 N  ND2   . ASN   C 1 117 ? 14.52600  27.87600  36.66800  1.000 15.53191 ? 116 ASN   B ND2   1 
ATOM   3534 N  N     . LYS   C 1 118 ? 16.52000  27.37200  33.78600  1.000 16.61916 ? 117 LYS   B N     1 
ATOM   3535 C  CA    . LYS   C 1 118 ? 17.27700  28.50000  33.23200  1.000 17.65196 ? 117 LYS   B CA    1 
ATOM   3536 C  C     . LYS   C 1 118 ? 17.83700  28.21800  31.83600  1.000 20.75276 ? 117 LYS   B C     1 
ATOM   3537 O  O     . LYS   C 1 118 ? 18.90200  28.72600  31.44500  1.000 22.42517 ? 117 LYS   B O     1 
ATOM   3538 C  CB    . LYS   C 1 118 ? 18.36600  29.01300  34.19100  1.000 18.61645 ? 117 LYS   B CB    1 
ATOM   3539 C  CG    . LYS   C 1 118 ? 17.86200  29.22600  35.62500  1.000 17.11197 ? 117 LYS   B CG    1 
ATOM   3540 C  CD    . LYS   C 1 118 ? 18.82700  30.10400  36.43400  1.000 18.51557 ? 117 LYS   B CD    1 
ATOM   3541 C  CE    . LYS   C 1 118 ? 18.29800  30.15600  37.87600  1.000 21.23289 ? 117 LYS   B CE    1 
ATOM   3542 N  NZ    . LYS   C 1 118 ? 19.12300  31.11900  38.67400  1.000 21.32997 ? 117 LYS   B NZ    1 
ATOM   3543 N  N     . SER   C 1 119 ? 17.07000  27.47600  31.03700  1.000 19.41598 ? 118 SER   B N     1 
ATOM   3544 C  CA    . SER   C 1 119 ? 17.50800  27.12000  29.68400  1.000 21.19793 ? 118 SER   B CA    1 
ATOM   3545 C  C     . SER   C 1 119 ? 17.68800  28.32200  28.75900  1.000 22.89536 ? 118 SER   B C     1 
ATOM   3546 O  O     . SER   C 1 119 ? 18.27200  28.17500  27.67600  1.000 27.23889 ? 118 SER   B O     1 
ATOM   3547 C  CB    . SER   C 1 119 ? 16.54400  26.10600  29.06600  1.000 19.81894 ? 118 SER   B CB    1 
ATOM   3548 O  OG    . SER   C 1 119 ? 15.30500  26.66800  28.72400  1.000 26.75936 ? 118 SER   B OG    1 
ATOM   3549 N  N     . ASP   C 1 120 ? 17.22400  29.48800  29.16900  1.000 22.69101 ? 119 ASP   B N     1 
ATOM   3550 C  CA    . ASP   C 1 120 ? 17.32000  30.71900  28.34500  1.000 24.18350 ? 119 ASP   B CA    1 
ATOM   3551 C  C     . ASP   C 1 120 ? 18.68900  31.38200  28.50400  1.000 27.62579 ? 119 ASP   B C     1 
ATOM   3552 O  O     . ASP   C 1 120 ? 18.96700  32.32600  27.75100  1.000 30.73652 ? 119 ASP   B O     1 
ATOM   3553 C  CB    . ASP   C 1 120 ? 16.26900  31.68500  28.83200  1.000 26.39409 ? 119 ASP   B CB    1 
ATOM   3554 C  CG    . ASP   C 1 120 ? 16.39100  32.01200  30.31300  1.000 23.91140 ? 119 ASP   B CG    1 
ATOM   3555 O  OD1   . ASP   C 1 120 ? 16.03800  31.14500  31.13200  1.000 21.61545 ? 119 ASP   B OD1   1 
ATOM   3556 O  OD2   . ASP   C 1 120 ? 16.90200  33.09800  30.63000  1.000 26.98468 ? 119 ASP   B OD2   1 
ATOM   3557 N  N     . LEU   C 1 121 ? 19.52200  30.92100  29.42200  1.000 26.37630 ? 120 LEU   B N     1 
ATOM   3558 C  CA    . LEU   C 1 121 ? 20.80100  31.62000  29.70900  1.000 27.39860 ? 120 LEU   B CA    1 
ATOM   3559 C  C     . LEU   C 1 121 ? 21.88600  31.21000  28.70200  1.000 41.22760 ? 120 LEU   B C     1 
ATOM   3560 O  O     . LEU   C 1 121 ? 21.57100  30.41700  27.79000  1.000 41.80510 ? 120 LEU   B O     1 
ATOM   3561 C  CB    . LEU   C 1 121 ? 21.19100  31.30100  31.14400  1.000 29.56129 ? 120 LEU   B CB    1 
ATOM   3562 C  CG    . LEU   C 1 121 ? 20.38200  32.02000  32.22600  1.000 25.89215 ? 120 LEU   B CG    1 
ATOM   3563 C  CD1   . LEU   C 1 121 ? 20.93100  31.67700  33.58700  1.000 33.91084 ? 120 LEU   B CD1   1 
ATOM   3564 C  CD2   . LEU   C 1 121 ? 20.40500  33.51900  32.00700  1.000 28.83646 ? 120 LEU   B CD2   1 
ATOM   3565 N  N     . PRO   C 1 122 ? 23.06454  31.87424  28.72298  1.000 34.75308 ? 121 PRO   B N     1 
ATOM   3566 C  CA    . PRO   C 1 122 ? 24.19320  31.45232  27.87840  1.000 38.02352 ? 121 PRO   B CA    1 
ATOM   3567 C  C     . PRO   C 1 122 ? 25.20444  30.44441  28.42216  1.000 43.49560 ? 121 PRO   B C     1 
ATOM   3568 O  O     . PRO   C 1 122 ? 25.53037  29.51095  27.69432  1.000 48.27931 ? 121 PRO   B O     1 
ATOM   3569 C  CB    . PRO   C 1 122 ? 24.91388  32.79080  27.66965  1.000 34.91901 ? 121 PRO   B CB    1 
ATOM   3570 C  CG    . PRO   C 1 122 ? 24.66430  33.55113  28.92637  1.000 39.31752 ? 121 PRO   B CG    1 
ATOM   3571 C  CD    . PRO   C 1 122 ? 23.26879  33.20392  29.34546  1.000 33.30484 ? 121 PRO   B CD    1 
ATOM   3572 N  N     . SER   C 1 123 ? 25.77500  30.63900  29.62900  1.000 46.58541 ? 122 SER   B N     1 
ATOM   3573 C  CA    . SER   C 1 123 ? 26.93400  29.86100  30.14400  1.000 48.31531 ? 122 SER   B CA    1 
ATOM   3574 C  C     . SER   C 1 123 ? 26.49000  28.53200  30.74400  1.000 45.05162 ? 122 SER   B C     1 
ATOM   3575 O  O     . SER   C 1 123 ? 26.74700  28.26900  31.92900  1.000 40.03722 ? 122 SER   B O     1 
ATOM   3576 C  CB    . SER   C 1 123 ? 27.74400  30.67100  31.12600  1.000 38.25954 ? 122 SER   B CB    1 
ATOM   3577 O  OG    . SER   C 1 123 ? 27.77000  32.03200  30.72800  1.000 45.81407 ? 122 SER   B OG    1 
ATOM   3578 N  N     . ARG   C 1 124 ? 25.76400  27.76800  29.95400  1.000 34.96657 ? 123 ARG   B N     1 
ATOM   3579 C  CA    . ARG   C 1 124 ? 25.49700  26.44000  30.45800  1.000 33.35093 ? 123 ARG   B CA    1 
ATOM   3580 C  C     . ARG   C 1 124 ? 26.79300  25.86300  30.99800  1.000 32.60002 ? 123 ARG   B C     1 
ATOM   3581 O  O     . ARG   C 1 124 ? 27.85500  25.97500  30.37200  1.000 31.03666 ? 123 ARG   B O     1 
ATOM   3582 C  CB    . ARG   C 1 124 ? 24.98700  25.54200  29.32400  1.000 37.22970 ? 123 ARG   B CB    1 
ATOM   3583 C  CG    . ARG   C 1 124 ? 24.86200  24.07900  29.73600  1.000 39.98901 ? 123 ARG   B CG    1 
ATOM   3584 C  CD    . ARG   C 1 124 ? 24.52000  23.20400  28.54400  1.000 36.40307 ? 123 ARG   B CD    1 
ATOM   3585 N  NE    . ARG   C 1 124 ? 23.22100  23.55400  27.99100  1.000 37.20719 ? 123 ARG   B NE    1 
ATOM   3586 C  CZ    . ARG   C 1 124 ? 22.05600  23.06100  28.40000  1.000 27.17435 ? 123 ARG   B CZ    1 
ATOM   3587 N  NH1   . ARG   C 1 124 ? 21.96800  22.21600  29.42400  1.000 27.24294 ? 123 ARG   B NH1   1 
ATOM   3588 N  NH2   . ARG   C 1 124 ? 20.94900  23.42500  27.76300  1.000 24.76896 ? 123 ARG   B NH2   1 
ATOM   3589 N  N     . THR   C 1 125 ? 26.71700  25.28900  32.18600  1.000 28.40429 ? 124 THR   B N     1 
ATOM   3590 C  CA    . THR   C 1 125 ? 27.80300  24.50000  32.72700  1.000 33.30887 ? 124 THR   B CA    1 
ATOM   3591 C  C     . THR   C 1 125 ? 27.43900  23.04200  32.89900  1.000 27.94616 ? 124 THR   B C     1 
ATOM   3592 O  O     . THR   C 1 125 ? 28.33900  22.22200  33.07100  1.000 35.00945 ? 124 THR   B O     1 
ATOM   3593 C  CB    . THR   C 1 125 ? 28.29700  25.08500  34.06400  1.000 29.24469 ? 124 THR   B CB    1 
ATOM   3594 O  OG1   . THR   C 1 125 ? 27.18800  25.21500  34.96700  1.000 30.94069 ? 124 THR   B OG1   1 
ATOM   3595 C  CG2   . THR   C 1 125 ? 28.87400  26.45800  33.83300  1.000 35.01861 ? 124 THR   B CG2   1 
ATOM   3596 N  N     . VAL   C 1 126 ? 26.15300  22.69500  32.83500  1.000 27.75509 ? 125 VAL   B N     1 
ATOM   3597 C  CA    . VAL   C 1 126 ? 25.69100  21.31700  32.94000  1.000 26.01641 ? 125 VAL   B CA    1 
ATOM   3598 C  C     . VAL   C 1 126 ? 25.16700  20.88600  31.57000  1.000 27.18064 ? 125 VAL   B C     1 
ATOM   3599 O  O     . VAL   C 1 126 ? 24.16800  21.43300  31.08200  1.000 26.66662 ? 125 VAL   B O     1 
ATOM   3600 C  CB    . VAL   C 1 126 ? 24.60400  21.19200  34.01800  1.000 25.83715 ? 125 VAL   B CB    1 
ATOM   3601 C  CG1   . VAL   C 1 126 ? 24.20700  19.75300  34.19200  1.000 27.54129 ? 125 VAL   B CG1   1 
ATOM   3602 C  CG2   . VAL   C 1 126 ? 25.08200  21.82100  35.34300  1.000 29.14150 ? 125 VAL   B CG2   1 
ATOM   3603 N  N     . ASP   C 1 127 ? 25.82800  19.89800  30.95600  1.000 25.51512 ? 126 ASP   B N     1 
ATOM   3604 C  CA    . ASP   C 1 127 ? 25.42100  19.45200  29.62800  1.000 25.65956 ? 126 ASP   B CA    1 
ATOM   3605 C  C     . ASP   C 1 127 ? 24.09700  18.71000  29.71000  1.000 24.03703 ? 126 ASP   B C     1 
ATOM   3606 O  O     . ASP   C 1 127 ? 23.84900  17.97400  30.66400  1.000 24.75261 ? 126 ASP   B O     1 
ATOM   3607 C  CB    . ASP   C 1 127 ? 26.45400  18.48800  28.99900  1.000 27.61087 ? 126 ASP   B CB    1 
ATOM   3608 C  CG    . ASP   C 1 127 ? 27.82100  19.11300  28.74100  1.000 35.58492 ? 126 ASP   B CG    1 
ATOM   3609 O  OD1   . ASP   C 1 127 ? 27.94800  20.35000  28.67500  1.000 40.72125 ? 126 ASP   B OD1   1 
ATOM   3610 O  OD2   . ASP   C 1 127 ? 28.77700  18.32700  28.56900  1.000 40.29896 ? 126 ASP   B OD2   1 
ATOM   3611 N  N     . THR   C 1 128 ? 23.26500  18.86600  28.67700  1.000 24.36907 ? 127 THR   B N     1 
ATOM   3612 C  CA    . THR   C 1 128 ? 22.02500  18.09200  28.58400  1.000 22.73967 ? 127 THR   B CA    1 
ATOM   3613 C  C     . THR   C 1 128 ? 22.30800  16.58700  28.67100  1.000 23.68204 ? 127 THR   B C     1 
ATOM   3614 O  O     . THR   C 1 128 ? 21.58300  15.83900  29.35300  1.000 21.91320 ? 127 THR   B O     1 
ATOM   3615 C  CB    . THR   C 1 128 ? 21.34800  18.42100  27.24000  1.000 25.26781 ? 127 THR   B CB    1 
ATOM   3616 O  OG1   . THR   C 1 128 ? 21.08500  19.82800  27.17600  1.000 24.55871 ? 127 THR   B OG1   1 
ATOM   3617 C  CG2   . THR   C 1 128 ? 20.02700  17.68300  27.06800  1.000 23.23352 ? 127 THR   B CG2   1 
ATOM   3618 N  N     . LYS   C 1 129 ? 23.35900  16.12700  27.98000  1.000 24.41671 ? 128 LYS   B N     1 
ATOM   3619 C  CA    . LYS   C 1 129 ? 23.69400  14.70600  28.00800  1.000 24.79799 ? 128 LYS   B CA    1 
ATOM   3620 C  C     . LYS   C 1 129 ? 23.93500  14.23400  29.44000  1.000 26.40972 ? 128 LYS   B C     1 
ATOM   3621 O  O     . LYS   C 1 129 ? 23.45500  13.16800  29.84400  1.000 24.63406 ? 128 LYS   B O     1 
ATOM   3622 C  CB    . LYS   C 1 129 ? 24.92400  14.41800  27.15400  1.000 27.65082 ? 128 LYS   B CB    1 
ATOM   3623 C  CG    . LYS   C 1 129 ? 25.44100  13.02800  27.39500  1.000 28.62546 ? 128 LYS   B CG    1 
ATOM   3624 C  CD    . LYS   C 1 129 ? 26.56900  12.65900  26.41400  1.000 29.46496 ? 128 LYS   B CD    1 
ATOM   3625 C  CE    . LYS   C 1 129 ? 27.55500  11.63900  26.99700  1.000 34.34787 ? 128 LYS   B CE    1 
ATOM   3626 N  NZ    . LYS   C 1 129 ? 26.93300  10.34000  27.38500  1.000 34.39533 ? 128 LYS   B NZ    1 
ATOM   3627 N  N     . GLN   C 1 130 ? 24.66900  15.02200  30.22700  1.000 25.22165 ? 129 GLN   B N     1 
ATOM   3628 C  CA    . GLN   C 1 130 ? 24.98500  14.57600  31.58500  1.000 28.65830 ? 129 GLN   B CA    1 
ATOM   3629 C  C     . GLN   C 1 130 ? 23.72700  14.45700  32.42700  1.000 24.54203 ? 129 GLN   B C     1 
ATOM   3630 O  O     . GLN   C 1 130 ? 23.57200  13.50400  33.21200  1.000 25.72583 ? 129 GLN   B O     1 
ATOM   3631 C  CB    . GLN   C 1 130 ? 25.96400  15.53100  32.25900  1.000 33.17541 ? 129 GLN   B CB    1 
ATOM   3632 C  CG    . GLN   C 1 130 ? 26.35300  15.07100  33.65100  1.000 35.76916 ? 129 GLN   B CG    1 
ATOM   3633 C  CD    . GLN   C 1 130 ? 27.28100  16.03800  34.36000  1.000 44.35356 ? 129 GLN   B CD    1 
ATOM   3634 O  OE1   . GLN   C 1 130 ? 27.35000  17.22000  34.01900  1.000 41.37133 ? 129 GLN   B OE1   1 
ATOM   3635 N  NE2   . GLN   C 1 130 ? 28.00800  15.53400  35.35100  1.000 48.05608 ? 129 GLN   B NE2   1 
ATOM   3636 N  N     . ALA   C 1 131 ? 22.83000  15.43200  32.30000  1.000 21.16940 ? 130 ALA   B N     1 
ATOM   3637 C  CA    . ALA   C 1 131 ? 21.59300  15.38300  33.07400  1.000 20.36888 ? 130 ALA   B CA    1 
ATOM   3638 C  C     . ALA   C 1 131 ? 20.66200  14.29700  32.55300  1.000 22.11506 ? 130 ALA   B C     1 
ATOM   3639 O  O     . ALA   C 1 131 ? 20.00300  13.59600  33.33700  1.000 20.70887 ? 130 ALA   B O     1 
ATOM   3640 C  CB    . ALA   C 1 131 ? 20.89800  16.74400  33.05200  1.000 23.36989 ? 130 ALA   B CB    1 
ATOM   3641 N  N     . GLN   C 1 132 ? 20.62400  14.10900  31.22600  1.000 20.55424 ? 131 GLN   B N     1 
ATOM   3642 C  CA    . GLN   C 1 132 ? 19.76700  13.06700  30.67000  1.000 20.91536 ? 131 GLN   B CA    1 
ATOM   3643 C  C     . GLN   C 1 132 ? 20.25800  11.68600  31.08500  1.000 21.99162 ? 131 GLN   B C     1 
ATOM   3644 O  O     . GLN   C 1 132 ? 19.45600  10.79300  31.38200  1.000 22.40943 ? 131 GLN   B O     1 
ATOM   3645 C  CB    . GLN   C 1 132 ? 19.70900  13.20800  29.14200  1.000 21.55371 ? 131 GLN   B CB    1 
ATOM   3646 C  CG    . GLN   C 1 132 ? 18.87900  12.15000  28.45100  1.000 20.63351 ? 131 GLN   B CG    1 
ATOM   3647 C  CD    . GLN   C 1 132 ? 17.41200  12.36700  28.68300  1.000 22.13216 ? 131 GLN   B CD    1 
ATOM   3648 O  OE1   . GLN   C 1 132 ? 16.76400  11.60300  29.42100  1.000 26.18931 ? 131 GLN   B OE1   1 
ATOM   3649 N  NE2   . GLN   C 1 132 ? 16.87700  13.44200  28.11800  1.000 19.88280 ? 131 GLN   B NE2   1 
ATOM   3650 N  N     . ASP   C 1 133 ? 21.58300  11.49100  31.08900  1.000 22.78958 ? 132 ASP   B N     1 
ATOM   3651 C  CA    . ASP   C 1 133 ? 22.18100  10.24300  31.55300  1.000 24.40640 ? 132 ASP   B CA    1 
ATOM   3652 C  C     . ASP   C 1 133 ? 21.78700  9.95500   32.99800  1.000 24.14801 ? 132 ASP   B C     1 
ATOM   3653 O  O     . ASP   C 1 133 ? 21.43900  8.82200   33.33300  1.000 27.42664 ? 132 ASP   B O     1 
ATOM   3654 C  CB    . ASP   C 1 133 ? 23.71000  10.30200  31.42900  1.000 26.20671 ? 132 ASP   B CB    1 
ATOM   3655 C  CG    . ASP   C 1 133 ? 24.20500  10.13400  30.01100  1.000 28.65502 ? 132 ASP   B CG    1 
ATOM   3656 O  OD1   . ASP   C 1 133 ? 23.39300  9.77400   29.12600  1.000 29.73232 ? 132 ASP   B OD1   1 
ATOM   3657 O  OD2   . ASP   C 1 133 ? 25.42000  10.35000  29.78900  1.000 29.75155 ? 132 ASP   B OD2   1 
ATOM   3658 N  N     . LEU   C 1 134 ? 21.85400  10.97100  33.86700  1.000 24.04208 ? 133 LEU   B N     1 
ATOM   3659 C  CA    . LEU   C 1 134 ? 21.44100  10.78200  35.26200  1.000 24.78870 ? 133 LEU   B CA    1 
ATOM   3660 C  C     . LEU   C 1 134 ? 19.97600  10.36700  35.35100  1.000 24.55296 ? 133 LEU   B C     1 
ATOM   3661 O  O     . LEU   C 1 134 ? 19.63900  9.39800   36.03900  1.000 27.55867 ? 133 LEU   B O     1 
ATOM   3662 C  CB    . LEU   C 1 134 ? 21.68000  12.05700  36.08700  1.000 25.63846 ? 133 LEU   B CB    1 
ATOM   3663 C  CG    . LEU   C 1 134 ? 21.44900  11.85600  37.61100  1.000 24.72727 ? 133 LEU   B CG    1 
ATOM   3664 C  CD1   . LEU   C 1 134 ? 22.51600  10.92700  38.17700  1.000 30.55490 ? 133 LEU   B CD1   1 
ATOM   3665 C  CD2   . LEU   C 1 134 ? 21.40800  13.17300  38.35800  1.000 30.30930 ? 133 LEU   B CD2   1 
ATOM   3666 N  N     . ALA   C 1 135 ? 19.08300  11.09000  34.66800  1.000 21.72292 ? 134 ALA   B N     1 
ATOM   3667 C  CA    . ALA   C 1 135 ? 17.66600  10.74600  34.73000  1.000 22.31130 ? 134 ALA   B CA    1 
ATOM   3668 C  C     . ALA   C 1 135 ? 17.42700  9.34200   34.19400  1.000 26.72792 ? 134 ALA   B C     1 
ATOM   3669 O  O     . ALA   C 1 135 ? 16.64900  8.56100   34.77000  1.000 26.25455 ? 134 ALA   B O     1 
ATOM   3670 C  CB    . ALA   C 1 135 ? 16.83900  11.76200  33.94200  1.000 23.38266 ? 134 ALA   B CB    1 
ATOM   3671 N  N     . ARG   C 1 136 ? 18.10400  8.98600   33.10800  1.000 25.36359 ? 135 ARG   B N     1 
ATOM   3672 C  CA    . ARG   C 1 136 ? 17.92900  7.63700   32.59000  1.000 24.11482 ? 135 ARG   B CA    1 
ATOM   3673 C  C     . ARG   C 1 136 ? 18.36300  6.59900   33.62300  1.000 27.95618 ? 135 ARG   B C     1 
ATOM   3674 O  O     . ARG   C 1 136 ? 17.73700  5.54100   33.74800  1.000 27.88123 ? 135 ARG   B O     1 
ATOM   3675 C  CB    . ARG   C 1 136 ? 18.69100  7.45300   31.27000  1.000 25.65499 ? 135 ARG   B CB    1 
ATOM   3676 C  CG    . ARG   C 1 136 ? 18.32000  6.15700   30.50500  1.000 26.49625 ? 135 ARG   B CG    1 
ATOM   3677 C  CD    . ARG   C 1 136 ? 19.07100  5.97000   29.15900  1.000 28.57294 ? 135 ARG   B CD    1 
ATOM   3678 N  NE    . ARG   C 1 136 ? 18.93100  7.13600   28.28800  1.000 28.00515 ? 135 ARG   B NE    1 
ATOM   3679 C  CZ    . ARG   C 1 136 ? 19.88300  8.03800   28.08600  1.000 26.95014 ? 135 ARG   B CZ    1 
ATOM   3680 N  NH1   . ARG   C 1 136 ? 21.08300  7.90500   28.62200  1.000 28.67234 ? 135 ARG   B NH1   1 
ATOM   3681 N  NH2   . ARG   C 1 136 ? 19.63200  9.08300   27.29800  1.000 26.33987 ? 135 ARG   B NH2   1 
ATOM   3682 N  N     . SER   C 1 137 ? 19.42000  6.90000   34.39000  1.000 28.22435 ? 136 SER   B N     1 
ATOM   3683 C  CA    . SER   C 1 137 ? 19.90300  5.94200   35.38300  1.000 28.99019 ? 136 SER   B CA    1 
ATOM   3684 C  C     . SER   C 1 137 ? 18.94000  5.80900   36.55500  1.000 28.70403 ? 136 SER   B C     1 
ATOM   3685 O  O     . SER   C 1 137 ? 18.87400  4.74500   37.18300  1.000 31.30562 ? 136 SER   B O     1 
ATOM   3686 C  CB    . SER   C 1 137 ? 21.29700  6.33800   35.86800  1.000 30.57697 ? 136 SER   B CB    1 
ATOM   3687 O  OG    . SER   C 1 137 ? 21.25100  7.37300   36.82400  1.000 30.39090 ? 136 SER   B OG    1 
ATOM   3688 N  N     . TYR   C 1 138 ? 18.19200  6.85400   36.85500  1.000 27.33725 ? 137 TYR   B N     1 
ATOM   3689 C  CA    . TYR   C 1 138 ? 17.16400  6.82400   37.88800  1.000 27.31031 ? 137 TYR   B CA    1 
ATOM   3690 C  C     . TYR   C 1 138 ? 15.83200  6.29000   37.38300  1.000 28.95622 ? 137 TYR   B C     1 
ATOM   3691 O  O     . TYR   C 1 138 ? 14.91900  6.07200   38.20700  1.000 35.05323 ? 137 TYR   B O     1 
ATOM   3692 C  CB    . TYR   C 1 138 ? 16.88200  8.24200   38.34800  1.000 28.53907 ? 137 TYR   B CB    1 
ATOM   3693 C  CG    . TYR   C 1 138 ? 17.97300  8.95700   39.11000  1.000 26.75024 ? 137 TYR   B CG    1 
ATOM   3694 C  CD1   . TYR   C 1 138 ? 19.02800  8.27200   39.68200  1.000 33.34446 ? 137 TYR   B CD1   1 
ATOM   3695 C  CD2   . TYR   C 1 138 ? 17.90900  10.34400  39.28500  1.000 27.35742 ? 137 TYR   B CD2   1 
ATOM   3696 C  CE1   . TYR   C 1 138 ? 20.01300  8.95200   40.41500  1.000 28.70151 ? 137 TYR   B CE1   1 
ATOM   3697 C  CE2   . TYR   C 1 138 ? 18.88900  11.02600  39.98700  1.000 28.14404 ? 137 TYR   B CE2   1 
ATOM   3698 C  CZ    . TYR   C 1 138 ? 19.93000  10.33100  40.54900  1.000 29.06469 ? 137 TYR   B CZ    1 
ATOM   3699 O  OH    . TYR   C 1 138 ? 20.89300  11.00900  41.26700  1.000 34.04103 ? 137 TYR   B OH    1 
ATOM   3700 N  N     . GLY   C 1 139 ? 15.69600  6.12700   36.06800  1.000 29.77350 ? 138 GLY   B N     1 
ATOM   3701 C  CA    . GLY   C 1 139 ? 14.44600  5.75800   35.41600  1.000 27.68907 ? 138 GLY   B CA    1 
ATOM   3702 C  C     . GLY   C 1 139 ? 13.35500  6.80300   35.52300  1.000 29.08056 ? 138 GLY   B C     1 
ATOM   3703 O  O     . GLY   C 1 139 ? 12.18900  6.44900   35.75000  1.000 30.67067 ? 138 GLY   B O     1 
ATOM   3704 N  N     . ILE   C 1 140 ? 13.70200  8.08200   35.38900  1.000 24.98903 ? 139 ILE   B N     1 
ATOM   3705 C  CA    . ILE   C 1 140 ? 12.72600  9.17100   35.51800  1.000 23.54307 ? 139 ILE   B CA    1 
ATOM   3706 C  C     . ILE   C 1 140 ? 12.83300  10.11200  34.32200  1.000 21.14217 ? 139 ILE   B C     1 
ATOM   3707 O  O     . ILE   C 1 140 ? 13.86500  10.16100  33.63400  1.000 22.28360 ? 139 ILE   B O     1 
ATOM   3708 C  CB    . ILE   C 1 140 ? 12.89600  9.95600   36.84300  1.000 23.69482 ? 139 ILE   B CB    1 
ATOM   3709 C  CG1   . ILE   C 1 140 ? 14.18900  10.78000  36.83800  1.000 24.60872 ? 139 ILE   B CG1   1 
ATOM   3710 C  CG2   . ILE   C 1 140 ? 12.81300  9.02100   38.04000  1.000 23.95770 ? 139 ILE   B CG2   1 
ATOM   3711 C  CD1   . ILE   C 1 140 ? 14.42500  11.57000  38.13000  1.000 24.59585 ? 139 ILE   B CD1   1 
ATOM   3712 N  N     . PRO   C 1 141 ? 11.77600  10.87400  34.03900  1.000 22.49083 ? 140 PRO   B N     1 
ATOM   3713 C  CA    . PRO   C 1 141 ? 11.84900  11.86300  32.95900  1.000 19.11929 ? 140 PRO   B CA    1 
ATOM   3714 C  C     . PRO   C 1 141 ? 12.80100  12.99900  33.29900  1.000 18.17773 ? 140 PRO   B C     1 
ATOM   3715 O  O     . PRO   C 1 141 ? 13.03800  13.31600  34.47400  1.000 19.09920 ? 140 PRO   B O     1 
ATOM   3716 C  CB    . PRO   C 1 141 ? 10.40100  12.37100  32.82900  1.000 19.71328 ? 140 PRO   B CB    1 
ATOM   3717 C  CG    . PRO   C 1 141 ? 9.55100   11.27200  33.49200  1.000 23.21747 ? 140 PRO   B CG    1 
ATOM   3718 C  CD    . PRO   C 1 141 ? 10.42000  10.78300  34.60900  1.000 23.07674 ? 140 PRO   B CD    1 
ATOM   3719 N  N     . PHE   C 1 142 ? 13.33700  13.63100  32.24400  1.000 21.81536 ? 141 PHE   B N     1 
ATOM   3720 C  CA    . PHE   C 1 142 ? 14.14400  14.84200  32.34800  1.000 17.48760 ? 141 PHE   B CA    1 
ATOM   3721 C  C     . PHE   C 1 142 ? 13.60800  15.88500  31.38400  1.000 18.43172 ? 141 PHE   B C     1 
ATOM   3722 O  O     . PHE   C 1 142 ? 13.32000  15.57400  30.22100  1.000 19.57481 ? 141 PHE   B O     1 
ATOM   3723 C  CB    . PHE   C 1 142 ? 15.61000  14.52800  32.00200  1.000 18.63720 ? 141 PHE   B CB    1 
ATOM   3724 C  CG    . PHE   C 1 142 ? 16.47900  15.75000  31.83400  1.000 18.36362 ? 141 PHE   B CG    1 
ATOM   3725 C  CD1   . PHE   C 1 142 ? 16.63400  16.65800  32.86800  1.000 20.06737 ? 141 PHE   B CD1   1 
ATOM   3726 C  CD2   . PHE   C 1 142 ? 17.19100  15.96400  30.67100  1.000 22.35567 ? 141 PHE   B CD2   1 
ATOM   3727 C  CE1   . PHE   C 1 142 ? 17.43000  17.77500  32.70400  1.000 20.62804 ? 141 PHE   B CE1   1 
ATOM   3728 C  CE2   . PHE   C 1 142 ? 17.99900  17.09100  30.53400  1.000 21.82496 ? 141 PHE   B CE2   1 
ATOM   3729 C  CZ    . PHE   C 1 142 ? 18.12200  17.97300  31.52300  1.000 23.39161 ? 141 PHE   B CZ    1 
ATOM   3730 N  N     . ILE   C 1 143 ? 13.48900  17.12300  31.86400  1.000 16.74853 ? 142 ILE   B N     1 
ATOM   3731 C  CA    A ILE   C 1 143 ? 12.99600  18.24800  31.06600  0.500 17.49098 ? 142 ILE   B CA    1 
ATOM   3732 C  CA    B ILE   C 1 143 ? 13.04800  18.22700  31.02700  0.500 17.49579 ? 142 ILE   B CA    1 
ATOM   3733 C  C     . ILE   C 1 143 ? 13.85800  19.46900  31.36600  1.000 17.05068 ? 142 ILE   B C     1 
ATOM   3734 O  O     . ILE   C 1 143 ? 14.11500  19.76800  32.54200  1.000 18.20046 ? 142 ILE   B O     1 
ATOM   3735 C  CB    A ILE   C 1 143 ? 11.51900  18.56700  31.38500  0.500 18.50989 ? 142 ILE   B CB    1 
ATOM   3736 C  CB    B ILE   C 1 143 ? 11.54100  18.47700  31.18700  0.500 18.77522 ? 142 ILE   B CB    1 
ATOM   3737 C  CG1   A ILE   C 1 143 ? 10.60400  17.42400  30.93200  0.500 18.94421 ? 142 ILE   B CG1   1 
ATOM   3738 C  CG1   B ILE   C 1 143 ? 11.09300  19.60900  30.27100  0.500 19.19517 ? 142 ILE   B CG1   1 
ATOM   3739 C  CG2   A ILE   C 1 143 ? 11.08500  19.87300  30.71700  0.500 19.38307 ? 142 ILE   B CG2   1 
ATOM   3740 C  CG2   B ILE   C 1 143 ? 11.23500  18.79800  32.61400  0.500 18.73952 ? 142 ILE   B CG2   1 
ATOM   3741 C  CD1   A ILE   C 1 143 ? 9.18000   17.54800  31.45100  0.500 21.19784 ? 142 ILE   B CD1   1 
ATOM   3742 C  CD1   B ILE   C 1 143 ? 9.62900   19.86600  30.37900  0.500 21.75725 ? 142 ILE   B CD1   1 
ATOM   3743 N  N     . GLU   C 1 144 ? 14.28100  20.18900  30.32300  1.000 17.26247 ? 143 GLU   B N     1 
ATOM   3744 C  CA    . GLU   C 1 144 ? 14.90100  21.50500  30.48500  1.000 15.91738 ? 143 GLU   B CA    1 
ATOM   3745 C  C     . GLU   C 1 144 ? 13.82500  22.57900  30.35400  1.000 17.21426 ? 143 GLU   B C     1 
ATOM   3746 O  O     . GLU   C 1 144 ? 12.99600  22.52100  29.43300  1.000 18.93855 ? 143 GLU   B O     1 
ATOM   3747 C  CB    . GLU   C 1 144 ? 16.05100  21.75400  29.50100  1.000 19.24836 ? 143 GLU   B CB    1 
ATOM   3748 C  CG    . GLU   C 1 144 ? 17.19900  20.78200  29.71700  1.000 21.41015 ? 143 GLU   B CG    1 
ATOM   3749 C  CD    . GLU   C 1 144 ? 18.46400  21.13400  28.98800  1.000 21.23672 ? 143 GLU   B CD    1 
ATOM   3750 O  OE1   . GLU   C 1 144 ? 18.45800  22.02900  28.10400  1.000 22.73296 ? 143 GLU   B OE1   1 
ATOM   3751 O  OE2   . GLU   C 1 144 ? 19.46000  20.46800  29.29900  1.000 21.90952 ? 143 GLU   B OE2   1 
ATOM   3752 N  N     . THR   C 1 145 ? 13.83800  23.54300  31.27300  1.000 15.69181 ? 144 THR   B N     1 
ATOM   3753 C  CA    . THR   C 1 145 ? 12.80300  24.55900  31.39700  1.000 16.74809 ? 144 THR   B CA    1 
ATOM   3754 C  C     . THR   C 1 145 ? 13.44500  25.93800  31.45300  1.000 16.89649 ? 144 THR   B C     1 
ATOM   3755 O  O     . THR   C 1 145 ? 14.62800  26.08500  31.77600  1.000 17.06889 ? 144 THR   B O     1 
ATOM   3756 C  CB    . THR   C 1 145 ? 11.99700  24.38300  32.70100  1.000 15.77342 ? 144 THR   B CB    1 
ATOM   3757 O  OG1   . THR   C 1 145 ? 12.86500  24.47900  33.84000  1.000 15.48363 ? 144 THR   B OG1   1 
ATOM   3758 C  CG2   . THR   C 1 145 ? 11.31400  23.02800  32.71800  1.000 16.02560 ? 144 THR   B CG2   1 
ATOM   3759 N  N     . SER   C 1 146 ? 12.63700  26.94200  31.13800  1.000 17.37665 ? 145 SER   B N     1 
ATOM   3760 C  CA    . SER   C 1 146 ? 12.92200  28.34000  31.47700  1.000 16.84193 ? 145 SER   B CA    1 
ATOM   3761 C  C     . SER   C 1 146 ? 11.68200  28.93600  32.12800  1.000 17.20066 ? 145 SER   B C     1 
ATOM   3762 O  O     . SER   C 1 146 ? 10.65600  29.13900  31.46800  1.000 19.13555 ? 145 SER   B O     1 
ATOM   3763 C  CB    . SER   C 1 146 ? 13.28200  29.14100  30.23100  1.000 20.50771 ? 145 SER   B CB    1 
ATOM   3764 O  OG    . SER   C 1 146 ? 13.37700  30.49600  30.60000  1.000 20.03447 ? 145 SER   B OG    1 
ATOM   3765 N  N     . ALA   C 1 147 ? 11.77500  29.24100  33.42300  1.000 17.67549 ? 146 ALA   B N     1 
ATOM   3766 C  CA    . ALA   C 1 147 ? 10.71100  30.02100  34.02700  1.000 17.68100 ? 146 ALA   B CA    1 
ATOM   3767 C  C     . ALA   C 1 147 ? 10.61100  31.39300  33.38200  1.000 19.06295 ? 146 ALA   B C     1 
ATOM   3768 O  O     . ALA   C 1 147 ? 9.53000   31.97100  33.35200  1.000 24.08502 ? 146 ALA   B O     1 
ATOM   3769 C  CB    . ALA   C 1 147 ? 10.94500  30.15500  35.53400  1.000 17.51945 ? 146 ALA   B CB    1 
ATOM   3770 N  N     . LYS   C 1 148 ? 11.71600  31.90900  32.85500  1.000 18.10768 ? 147 LYS   B N     1 
ATOM   3771 C  CA    . LYS   C 1 148 ? 11.71400  33.24300  32.27600  1.000 21.78892 ? 147 LYS   B CA    1 
ATOM   3772 C  C     . LYS   C 1 148 ? 10.88300  33.28400  31.00200  1.000 25.66678 ? 147 LYS   B C     1 
ATOM   3773 O  O     . LYS   C 1 148 ? 10.04700  34.17600  30.82500  1.000 30.11957 ? 147 LYS   B O     1 
ATOM   3774 C  CB    . LYS   C 1 148 ? 13.14500  33.68400  32.04000  1.000 21.54371 ? 147 LYS   B CB    1 
ATOM   3775 C  CG    . LYS   C 1 148 ? 13.19100  35.11000  31.49100  1.000 23.77874 ? 147 LYS   B CG    1 
ATOM   3776 C  CD    . LYS   C 1 148 ? 14.59400  35.69100  31.56400  1.000 30.89992 ? 147 LYS   B CD    1 
ATOM   3777 C  CE    . LYS   C 1 148 ? 14.71800  36.99700  30.77300  1.000 33.25248 ? 147 LYS   B CE    1 
ATOM   3778 N  NZ    . LYS   C 1 148 ? 15.86700  37.77800  31.27100  1.000 44.49703 ? 147 LYS   B NZ    1 
ATOM   3779 N  N     . THR   C 1 149 ? 11.07700  32.31400  30.10800  1.000 23.42036 ? 148 THR   B N     1 
ATOM   3780 C  CA    . THR   C 1 149 ? 10.35400  32.32100  28.83400  1.000 25.16912 ? 148 THR   B CA    1 
ATOM   3781 C  C     . THR   C 1 149 ? 9.13100   31.41700  28.83600  1.000 23.23098 ? 148 THR   B C     1 
ATOM   3782 O  O     . THR   C 1 149 ? 8.37200   31.42600  27.85700  1.000 24.25449 ? 148 THR   B O     1 
ATOM   3783 C  CB    . THR   C 1 149 ? 11.25200  31.84200  27.70800  1.000 26.88473 ? 148 THR   B CB    1 
ATOM   3784 O  OG1   . THR   C 1 149 ? 11.46900  30.42700  27.87000  1.000 24.12424 ? 148 THR   B OG1   1 
ATOM   3785 C  CG2   . THR   C 1 149 ? 12.56700  32.61700  27.71600  1.000 29.83643 ? 148 THR   B CG2   1 
ATOM   3786 N  N     . ARG   C 1 150 ? 8.94900   30.63000  29.88200  1.000 21.73160 ? 149 ARG   B N     1 
ATOM   3787 C  CA    . ARG   C 1 150 ? 7.89300   29.64100  30.08600  1.000 23.23044 ? 149 ARG   B CA    1 
ATOM   3788 C  C     . ARG   C 1 150 ? 8.12900   28.32000  29.33300  1.000 21.59676 ? 149 ARG   B C     1 
ATOM   3789 O  O     . ARG   C 1 150 ? 7.31400   27.36900  29.47700  1.000 20.99740 ? 149 ARG   B O     1 
ATOM   3790 C  CB    . ARG   C 1 150 ? 6.47000   30.16800  29.85200  1.000 27.73321 ? 149 ARG   B CB    1 
ATOM   3791 C  CG    . ARG   C 1 150 ? 5.57900   29.81200  31.04400  1.000 26.60145 ? 149 ARG   B CG    1 
ATOM   3792 C  CD    . ARG   C 1 150 ? 4.20100   30.46600  30.94100  1.000 28.38382 ? 149 ARG   B CD    1 
ATOM   3793 N  NE    . ARG   C 1 150 ? 3.31700   29.89200  31.94500  1.000 32.22997 ? 149 ARG   B NE    1 
ATOM   3794 C  CZ    . ARG   C 1 150 ? 2.76200   28.69400  31.82800  1.000 30.13799 ? 149 ARG   B CZ    1 
ATOM   3795 N  NH1   . ARG   C 1 150 ? 2.97100   27.94200  30.75900  1.000 36.43671 ? 149 ARG   B NH1   1 
ATOM   3796 N  NH2   . ARG   C 1 150 ? 1.95800   28.25400  32.79200  1.000 29.96155 ? 149 ARG   B NH2   1 
ATOM   3797 N  N     . GLN   C 1 151 ? 9.21200   28.19900  28.58000  1.000 21.07717 ? 150 GLN   B N     1 
ATOM   3798 C  CA    . GLN   C 1 151 ? 9.52400   26.94900  27.88100  1.000 19.40630 ? 150 GLN   B CA    1 
ATOM   3799 C  C     . GLN   C 1 151 ? 9.55500   25.78200  28.86200  1.000 18.43626 ? 150 GLN   B C     1 
ATOM   3800 O  O     . GLN   C 1 151 ? 10.28500  25.81300  29.85400  1.000 18.12146 ? 150 GLN   B O     1 
ATOM   3801 C  CB    . GLN   C 1 151 ? 10.87200  27.06500  27.17400  1.000 20.02244 ? 150 GLN   B CB    1 
ATOM   3802 C  CG    . GLN   C 1 151 ? 11.33800  25.75200  26.49600  1.000 23.81032 ? 150 GLN   B CG    1 
ATOM   3803 C  CD    . GLN   C 1 151 ? 10.45300  25.33000  25.33400  1.000 29.43800 ? 150 GLN   B CD    1 
ATOM   3804 O  OE1   . GLN   C 1 151 ? 9.98400   26.16500  24.55100  1.000 31.79129 ? 150 GLN   B OE1   1 
ATOM   3805 N  NE2   . GLN   C 1 151 ? 10.22800  24.01800  25.20700  1.000 30.55659 ? 150 GLN   B NE2   1 
ATOM   3806 N  N     . GLY   C 1 152 ? 8.71500   24.78500  28.61300  1.000 18.85729 ? 151 GLY   B N     1 
ATOM   3807 C  CA    . GLY   C 1 152 ? 8.73800   23.55100  29.38400  1.000 17.81969 ? 151 GLY   B CA    1 
ATOM   3808 C  C     . GLY   C 1 152 ? 8.04600   23.58100  30.72700  1.000 18.69445 ? 151 GLY   B C     1 
ATOM   3809 O  O     . GLY   C 1 152 ? 8.04300   22.54400  31.40600  1.000 18.71123 ? 151 GLY   B O     1 
ATOM   3810 N  N     . VAL   C 1 153 ? 7.47800   24.71400  31.13800  1.000 17.53379 ? 152 VAL   B N     1 
ATOM   3811 C  CA    . VAL   C 1 153 ? 6.96000   24.82400  32.50400  1.000 19.40455 ? 152 VAL   B CA    1 
ATOM   3812 C  C     . VAL   C 1 153 ? 5.75200   23.91700  32.69500  1.000 19.77118 ? 152 VAL   B C     1 
ATOM   3813 O  O     . VAL   C 1 153 ? 5.72700   23.08000  33.61100  1.000 18.15898 ? 152 VAL   B O     1 
ATOM   3814 C  CB    . VAL   C 1 153 ? 6.62900   26.27900  32.87000  1.000 18.39615 ? 152 VAL   B CB    1 
ATOM   3815 C  CG1   . VAL   C 1 153 ? 5.94900   26.31000  34.24600  1.000 20.25612 ? 152 VAL   B CG1   1 
ATOM   3816 C  CG2   . VAL   C 1 153 ? 7.90200   27.15100  32.90100  1.000 19.66048 ? 152 VAL   B CG2   1 
ATOM   3817 N  N     . ASP   C 1 154 ? 4.72200   24.09200  31.85500  1.000 19.28665 ? 153 ASP   B N     1 
ATOM   3818 C  CA    . ASP   C 1 154 ? 3.57900   23.19200  31.93800  1.000 21.44897 ? 153 ASP   B CA    1 
ATOM   3819 C  C     . ASP   C 1 154 ? 4.02700   21.74700  31.76900  1.000 21.01123 ? 153 ASP   B C     1 
ATOM   3820 O  O     . ASP   C 1 154 ? 3.59000   20.86500  32.51500  1.000 20.59858 ? 153 ASP   B O     1 
ATOM   3821 C  CB    . ASP   C 1 154 ? 2.52200   23.55100  30.89700  1.000 20.77842 ? 153 ASP   B CB    1 
ATOM   3822 C  CG    . ASP   C 1 154 ? 1.83500   24.88400  31.18200  1.000 22.29069 ? 153 ASP   B CG    1 
ATOM   3823 O  OD1   . ASP   C 1 154 ? 1.81700   25.34800  32.33100  1.000 29.58729 ? 153 ASP   B OD1   1 
ATOM   3824 O  OD2   . ASP   C 1 154 ? 1.27300   25.45900  30.22200  1.000 30.68950 ? 153 ASP   B OD2   1 
ATOM   3825 N  N     A ASP   C 1 155 ? 4.94300   21.49600  30.84400  0.500 19.23039 ? 154 ASP   B N     1 
ATOM   3826 N  N     B ASP   C 1 155 ? 4.92900   21.48400  30.81500  0.500 19.25331 ? 154 ASP   B N     1 
ATOM   3827 C  CA    A ASP   C 1 155 ? 5.35800   20.12800  30.57900  0.500 20.44196 ? 154 ASP   B CA    1 
ATOM   3828 C  CA    B ASP   C 1 155 ? 5.37500   20.11200  30.56400  0.500 20.44740 ? 154 ASP   B CA    1 
ATOM   3829 C  C     A ASP   C 1 155 ? 6.00600   19.48300  31.80200  0.500 18.29146 ? 154 ASP   B C     1 
ATOM   3830 C  C     B ASP   C 1 155 ? 5.98400   19.48600  31.81600  0.500 18.29445 ? 154 ASP   B C     1 
ATOM   3831 O  O     A ASP   C 1 155 ? 5.78300   18.29700  32.07500  0.500 18.11119 ? 154 ASP   B O     1 
ATOM   3832 O  O     B ASP   C 1 155 ? 5.72400   18.31400  32.11700  0.500 18.06622 ? 154 ASP   B O     1 
ATOM   3833 C  CB    A ASP   C 1 155 ? 6.27600   20.11200  29.36100  0.500 18.71761 ? 154 ASP   B CB    1 
ATOM   3834 C  CB    B ASP   C 1 155 ? 6.36800   20.06300  29.38900  0.500 18.71906 ? 154 ASP   B CB    1 
ATOM   3835 C  CG    A ASP   C 1 155 ? 5.53500   20.46700  28.09500  0.500 25.69619 ? 154 ASP   B CG    1 
ATOM   3836 C  CG    B ASP   C 1 155 ? 6.64600   18.61900  28.88200  0.500 18.86098 ? 154 ASP   B CG    1 
ATOM   3837 O  OD1   A ASP   C 1 155 ? 4.32200   20.14800  28.02300  0.500 31.32814 ? 154 ASP   B OD1   1 
ATOM   3838 O  OD1   B ASP   C 1 155 ? 5.76400   17.75000  29.02400  0.500 20.48956 ? 154 ASP   B OD1   1 
ATOM   3839 O  OD2   A ASP   C 1 155 ? 6.14300   21.05800  27.17200  0.500 29.17240 ? 154 ASP   B OD2   1 
ATOM   3840 O  OD2   B ASP   C 1 155 ? 7.73100   18.34100  28.30600  0.500 19.12857 ? 154 ASP   B OD2   1 
ATOM   3841 N  N     . ALA   C 1 156 ? 6.79600   20.23900  32.56100  1.000 16.70785 ? 155 ALA   B N     1 
ATOM   3842 C  CA    . ALA   C 1 156 ? 7.44700   19.66000  33.73600  1.000 18.02404 ? 155 ALA   B CA    1 
ATOM   3843 C  C     . ALA   C 1 156 ? 6.42100   19.21100  34.76600  1.000 17.07836 ? 155 ALA   B C     1 
ATOM   3844 O  O     . ALA   C 1 156 ? 6.46600   18.07800  35.27100  1.000 17.14371 ? 155 ALA   B O     1 
ATOM   3845 C  CB    . ALA   C 1 156 ? 8.37500   20.69000  34.35900  1.000 19.26492 ? 155 ALA   B CB    1 
ATOM   3846 N  N     . PHE   C 1 157 ? 5.47400   20.09400  35.08100  1.000 17.13620 ? 156 PHE   B N     1 
ATOM   3847 C  CA    . PHE   C 1 157 ? 4.47000   19.73200  36.07600  1.000 16.30848 ? 156 PHE   B CA    1 
ATOM   3848 C  C     . PHE   C 1 157 ? 3.53800   18.64200  35.56600  1.000 18.02143 ? 156 PHE   B C     1 
ATOM   3849 O  O     . PHE   C 1 157 ? 3.16600   17.73200  36.32600  1.000 15.92296 ? 156 PHE   B O     1 
ATOM   3850 C  CB    . PHE   C 1 157 ? 3.69500   20.98300  36.49000  1.000 18.56967 ? 156 PHE   B CB    1 
ATOM   3851 C  CG    . PHE   C 1 157 ? 4.46700   21.88400  37.38300  1.000 15.47260 ? 156 PHE   B CG    1 
ATOM   3852 C  CD1   . PHE   C 1 157 ? 4.47500   21.68300  38.76500  1.000 16.60328 ? 156 PHE   B CD1   1 
ATOM   3853 C  CD2   . PHE   C 1 157 ? 5.21600   22.92200  36.86900  1.000 16.31336 ? 156 PHE   B CD2   1 
ATOM   3854 C  CE1   . PHE   C 1 157 ? 5.20300   22.49100  39.60500  1.000 17.76840 ? 156 PHE   B CE1   1 
ATOM   3855 C  CE2   . PHE   C 1 157 ? 5.96700   23.75700  37.72600  1.000 17.82476 ? 156 PHE   B CE2   1 
ATOM   3856 C  CZ    . PHE   C 1 157 ? 5.94500   23.55600  39.07300  1.000 15.59345 ? 156 PHE   B CZ    1 
ATOM   3857 N  N     . TYR   C 1 158 ? 3.12800   18.71900  34.30900  1.000 16.79582 ? 157 TYR   B N     1 
ATOM   3858 C  CA    . TYR   C 1 158 ? 2.20400   17.72500  33.78100  1.000 15.86852 ? 157 TYR   B CA    1 
ATOM   3859 C  C     . TYR   C 1 158 ? 2.88200   16.36300  33.64800  1.000 16.40973 ? 157 TYR   B C     1 
ATOM   3860 O  O     . TYR   C 1 158 ? 2.25300   15.33000  33.86300  1.000 17.58957 ? 157 TYR   B O     1 
ATOM   3861 C  CB    . TYR   C 1 158 ? 1.61200   18.17700  32.44300  1.000 18.38922 ? 157 TYR   B CB    1 
ATOM   3862 C  CG    . TYR   C 1 158 ? 0.70100   19.39600  32.49300  1.000 21.79665 ? 157 TYR   B CG    1 
ATOM   3863 C  CD1   . TYR   C 1 158 ? 0.48400   20.11200  33.66200  1.000 25.54381 ? 157 TYR   B CD1   1 
ATOM   3864 C  CD2   . TYR   C 1 158 ? 0.07700   19.82600  31.33600  1.000 25.21702 ? 157 TYR   B CD2   1 
ATOM   3865 C  CE1   . TYR   C 1 158 ? -0.33800  21.22900  33.67100  1.000 25.33794 ? 157 TYR   B CE1   1 
ATOM   3866 C  CE2   . TYR   C 1 158 ? -0.75900  20.92900  31.33200  1.000 23.81611 ? 157 TYR   B CE2   1 
ATOM   3867 C  CZ    . TYR   C 1 158 ? -0.95800  21.63400  32.51000  1.000 26.49840 ? 157 TYR   B CZ    1 
ATOM   3868 O  OH    . TYR   C 1 158 ? -1.79500  22.73800  32.51100  1.000 32.56915 ? 157 TYR   B OH    1 
ATOM   3869 N  N     . THR   C 1 159 ? 4.17400   16.34800  33.29500  1.000 16.21227 ? 158 THR   B N     1 
ATOM   3870 C  CA    . THR   C 1 159 ? 4.89400   15.08200  33.26200  1.000 19.04909 ? 158 THR   B CA    1 
ATOM   3871 C  C     . THR   C 1 159 ? 4.92900   14.46000  34.65700  1.000 16.38533 ? 158 THR   B C     1 
ATOM   3872 O  O     . THR   C 1 159 ? 4.78200   13.23600  34.80400  1.000 16.44757 ? 158 THR   B O     1 
ATOM   3873 C  CB    . THR   C 1 159 ? 6.30000   15.29200  32.69000  1.000 18.66564 ? 158 THR   B CB    1 
ATOM   3874 O  OG1   . THR   C 1 159 ? 6.15700   15.71300  31.31500  1.000 19.81611 ? 158 THR   B OG1   1 
ATOM   3875 C  CG2   . THR   C 1 159 ? 7.13500   14.00800  32.77500  1.000 19.08892 ? 158 THR   B CG2   1 
ATOM   3876 N  N     . LEU   C 1 160 ? 5.10300   15.28800  35.69400  1.000 15.93825 ? 159 LEU   B N     1 
ATOM   3877 C  CA    . LEU   C 1 160 ? 5.11800   14.74600  37.05200  1.000 15.76154 ? 159 LEU   B CA    1 
ATOM   3878 C  C     . LEU   C 1 160 ? 3.77300   14.12900  37.41300  1.000 15.58927 ? 159 LEU   B C     1 
ATOM   3879 O  O     . LEU   C 1 160 ? 3.72500   13.02200  37.96100  1.000 17.00789 ? 159 LEU   B O     1 
ATOM   3880 C  CB    . LEU   C 1 160 ? 5.52900   15.83300  38.04300  1.000 15.21224 ? 159 LEU   B CB    1 
ATOM   3881 C  CG    . LEU   C 1 160 ? 5.54400   15.32000  39.49900  1.000 15.32140 ? 159 LEU   B CG    1 
ATOM   3882 C  CD1   . LEU   C 1 160 ? 6.52200   14.15900  39.63300  1.000 16.94130 ? 159 LEU   B CD1   1 
ATOM   3883 C  CD2   . LEU   C 1 160 ? 5.92300   16.46400  40.40600  1.000 16.31047 ? 159 LEU   B CD2   1 
ATOM   3884 N  N     . VAL   C 1 161 ? 2.67100   14.78700  37.02800  1.000 16.23390 ? 160 VAL   B N     1 
ATOM   3885 C  CA    . VAL   C 1 161 ? 1.34500   14.19800  37.23900  1.000 17.02586 ? 160 VAL   B CA    1 
ATOM   3886 C  C     . VAL   C 1 161 ? 1.23000   12.86700  36.51800  1.000 17.33624 ? 160 VAL   B C     1 
ATOM   3887 O  O     . VAL   C 1 161 ? 0.71800   11.88400  37.07100  1.000 19.20697 ? 160 VAL   B O     1 
ATOM   3888 C  CB    . VAL   C 1 161 ? 0.23800   15.18000  36.81300  1.000 18.01718 ? 160 VAL   B CB    1 
ATOM   3889 C  CG1   . VAL   C 1 161 ? -1.15400  14.49500  36.78300  1.000 18.35955 ? 160 VAL   B CG1   1 
ATOM   3890 C  CG2   . VAL   C 1 161 ? 0.22000   16.39300  37.74800  1.000 16.62701 ? 160 VAL   B CG2   1 
ATOM   3891 N  N     . ARG   C 1 162 ? 1.69300   12.79400  35.25600  1.000 18.11044 ? 161 ARG   B N     1 
ATOM   3892 C  CA    . ARG   C 1 162 ? 1.65500   11.52800  34.52300  1.000 21.48563 ? 161 ARG   B CA    1 
ATOM   3893 C  C     . ARG   C 1 162 ? 2.49800   10.44800  35.19100  1.000 19.94165 ? 161 ARG   B C     1 
ATOM   3894 O  O     . ARG   C 1 162 ? 2.07500   9.30600   35.24800  1.000 23.13217 ? 161 ARG   B O     1 
ATOM   3895 C  CB    . ARG   C 1 162 ? 2.09300   11.75800  33.07300  1.000 20.65575 ? 161 ARG   B CB    1 
ATOM   3896 C  CG    . ARG   C 1 162 ? 1.14400   12.64800  32.26600  1.000 20.62587 ? 161 ARG   B CG    1 
ATOM   3897 C  CD    . ARG   C 1 162 ? 1.65400   12.90200  30.79900  1.000 30.91924 ? 161 ARG   B CD    1 
ATOM   3898 N  NE    . ARG   C 1 162 ? 0.87400   13.90400  30.07000  1.000 30.29546 ? 161 ARG   B NE    1 
ATOM   3899 C  CZ    . ARG   C 1 162 ? 1.30800   15.10900  29.70700  1.000 25.12577 ? 161 ARG   B CZ    1 
ATOM   3900 N  NH1   . ARG   C 1 162 ? 2.55800   15.49200  29.89200  1.000 29.70961 ? 161 ARG   B NH1   1 
ATOM   3901 N  NH2   . ARG   C 1 162 ? 0.46600   15.95000  29.12200  1.000 30.14227 ? 161 ARG   B NH2   1 
ATOM   3902 N  N     . GLU   C 1 163 ? 3.62300   10.81300  35.80300  1.000 19.47800 ? 162 GLU   B N     1 
ATOM   3903 C  CA    . GLU   C 1 163 ? 4.41800   9.85100   36.56800  1.000 21.78786 ? 162 GLU   B CA    1 
ATOM   3904 C  C     . GLU   C 1 163 ? 3.66800   9.35500   37.80400  1.000 20.84405 ? 162 GLU   B C     1 
ATOM   3905 O  O     . GLU   C 1 163 ? 3.68300   8.15200   38.11500  1.000 22.60193 ? 162 GLU   B O     1 
ATOM   3906 C  CB    . GLU   C 1 163 ? 5.75900   10.46600  36.96400  1.000 21.73639 ? 162 GLU   B CB    1 
ATOM   3907 C  CG    . GLU   C 1 163 ? 6.72400   10.68000  35.78300  1.000 22.41851 ? 162 GLU   B CG    1 
ATOM   3908 C  CD    . GLU   C 1 163 ? 7.10200   9.36700   35.12200  1.000 25.04549 ? 162 GLU   B CD    1 
ATOM   3909 O  OE1   . GLU   C 1 163 ? 7.83200   8.57500   35.76100  1.000 28.59992 ? 162 GLU   B OE1   1 
ATOM   3910 O  OE2   . GLU   C 1 163 ? 6.64200   9.11800   33.98400  1.000 28.63795 ? 162 GLU   B OE2   1 
ATOM   3911 N  N     . ILE   C 1 164 ? 3.00300   10.25600  38.52800  1.000 20.12969 ? 163 ILE   B N     1 
ATOM   3912 C  CA    . ILE   C 1 164 ? 2.16900   9.81400   39.65200  1.000 20.23950 ? 163 ILE   B CA    1 
ATOM   3913 C  C     . ILE   C 1 164 ? 1.07000   8.86900   39.18200  1.000 25.84581 ? 163 ILE   B C     1 
ATOM   3914 O  O     . ILE   C 1 164 ? 0.80100   7.83800   39.81500  1.000 27.36741 ? 163 ILE   B O     1 
ATOM   3915 C  CB    . ILE   C 1 164 ? 1.56700   11.02300  40.37500  1.000 19.29044 ? 163 ILE   B CB    1 
ATOM   3916 C  CG1   . ILE   C 1 164 ? 2.66700   11.86400  40.98600  1.000 18.30487 ? 163 ILE   B CG1   1 
ATOM   3917 C  CG2   . ILE   C 1 164 ? 0.57900   10.52900  41.45600  1.000 21.31990 ? 163 ILE   B CG2   1 
ATOM   3918 C  CD1   . ILE   C 1 164 ? 2.15500   13.17800  41.47900  1.000 17.94400 ? 163 ILE   B CD1   1 
ATOM   3919 N  N     . ARG   C 1 165 ? 0.38800   9.23900   38.09800  1.000 24.00273 ? 164 ARG   B N     1 
ATOM   3920 C  CA    . ARG   C 1 165 ? -0.72700  8.45200   37.58400  1.000 28.82610 ? 164 ARG   B CA    1 
ATOM   3921 C  C     . ARG   C 1 165 ? -0.29100  7.03400   37.25800  1.000 34.49987 ? 164 ARG   B C     1 
ATOM   3922 O  O     . ARG   C 1 165 ? -0.97600  6.07100   37.62000  1.000 31.97977 ? 164 ARG   B O     1 
ATOM   3923 C  CB    . ARG   C 1 165 ? -1.29400  9.12900   36.33600  1.000 29.08026 ? 164 ARG   B CB    1 
ATOM   3924 C  CG    . ARG   C 1 165 ? -2.32400  10.15700  36.62900  1.000 34.52160 ? 164 ARG   B CG    1 
ATOM   3925 C  CD    . ARG   C 1 165 ? -2.91900  10.82900  35.40800  1.000 36.17610 ? 164 ARG   B CD    1 
ATOM   3926 N  NE    . ARG   C 1 165 ? -3.93000  11.79500  35.82700  1.000 37.16277 ? 164 ARG   B NE    1 
ATOM   3927 C  CZ    . ARG   C 1 165 ? -4.37100  12.80300  35.08900  1.000 38.59752 ? 164 ARG   B CZ    1 
ATOM   3928 N  NH1   . ARG   C 1 165 ? -3.90700  13.02800  33.86500  1.000 37.41580 ? 164 ARG   B NH1   1 
ATOM   3929 N  NH2   . ARG   C 1 165 ? -5.31100  13.59900  35.58500  1.000 42.92207 ? 164 ARG   B NH2   1 
ATOM   3930 N  N     . LYS   C 1 166 ? 0.83500   6.88900   36.54700  1.000 29.38244 ? 165 LYS   B N     1 
ATOM   3931 C  CA    . LYS   C 1 166 ? 1.39700   5.56900   36.27100  1.000 34.50925 ? 165 LYS   B CA    1 
ATOM   3932 C  C     . LYS   C 1 166 ? 1.59900   4.80500   37.56300  1.000 29.62431 ? 165 LYS   B C     1 
ATOM   3933 O  O     . LYS   C 1 166 ? 1.24600   3.62000   37.67400  1.000 36.44191 ? 165 LYS   B O     1 
ATOM   3934 C  CB    . LYS   C 1 166 ? 2.76600   5.73600   35.62400  1.000 31.25671 ? 165 LYS   B CB    1 
ATOM   3935 C  CG    . LYS   C 1 166 ? 2.79200   6.38900   34.29500  1.000 38.58143 ? 165 LYS   B CG    1 
ATOM   3936 C  CD    . LYS   C 1 166 ? 4.23300   6.50100   33.81900  1.000 39.32775 ? 165 LYS   B CD    1 
ATOM   3937 C  CE    . LYS   C 1 166 ? 4.95500   5.16800   33.94800  1.000 36.80048 ? 165 LYS   B CE    1 
ATOM   3938 N  NZ    . LYS   C 1 166 ? 6.21100   5.10800   33.09800  1.000 47.17804 ? 165 LYS   B NZ    1 
ATOM   3939 N  N     . HIS   C 1 167 ? 2.20600   5.46400   38.54400  1.000 33.44942 ? 166 HIS   B N     1 
ATOM   3940 C  CA    . HIS   C 1 167 ? 2.57400   4.78400   39.77500  1.000 30.25899 ? 166 HIS   B CA    1 
ATOM   3941 C  C     . HIS   C 1 167 ? 1.34600   4.25700   40.50700  1.000 33.82249 ? 166 HIS   B C     1 
ATOM   3942 O  O     . HIS   C 1 167 ? 1.36800   3.14200   41.04300  1.000 35.60115 ? 166 HIS   B O     1 
ATOM   3943 C  CB    . HIS   C 1 167 ? 3.38600   5.74600   40.63900  1.000 31.62850 ? 166 HIS   B CB    1 
ATOM   3944 C  CG    . HIS   C 1 167 ? 3.83100   5.16200   41.93900  1.000 36.34995 ? 166 HIS   B CG    1 
ATOM   3945 N  ND1   . HIS   C 1 167 ? 3.12200   5.32400   43.11000  1.000 44.23283 ? 166 HIS   B ND1   1 
ATOM   3946 C  CD2   . HIS   C 1 167 ? 4.91800   4.42000   42.25600  1.000 41.00859 ? 166 HIS   B CD2   1 
ATOM   3947 C  CE1   . HIS   C 1 167 ? 3.75300   4.70500   44.09200  1.000 41.78700 ? 166 HIS   B CE1   1 
ATOM   3948 N  NE2   . HIS   C 1 167 ? 4.84700   4.15200   43.60100  1.000 42.19375 ? 166 HIS   B NE2   1 
ATOM   3949 N  N     . LYS   C 1 168 ? 0.25400   5.02200   40.51300  1.000 37.80776 ? 167 LYS   B N     1 
ATOM   3950 C  CA    . LYS   C 1 168 ? -0.91300  4.63200   41.29400  1.000 34.53723 ? 167 LYS   B CA    1 
ATOM   3951 C  C     . LYS   C 1 168 ? -1.72500  3.54200   40.62000  1.000 38.33827 ? 167 LYS   B C     1 
ATOM   3952 O  O     . LYS   C 1 168 ? -2.35400  2.73000   41.30800  1.000 37.28827 ? 167 LYS   B O     1 
ATOM   3953 C  CB    . LYS   C 1 168 ? -1.83100  5.83000   41.52700  1.000 34.75723 ? 167 LYS   B CB    1 
ATOM   3954 C  CG    . LYS   C 1 168 ? -1.28500  6.86600   42.47900  1.000 30.12462 ? 167 LYS   B CG    1 
ATOM   3955 C  CD    . LYS   C 1 168 ? -2.19700  8.06600   42.55900  1.000 28.57945 ? 167 LYS   B CD    1 
ATOM   3956 C  CE    . LYS   C 1 168 ? -3.51400  7.73500   43.27900  1.000 34.63279 ? 167 LYS   B CE    1 
ATOM   3957 N  NZ    . LYS   C 1 168 ? -4.35300  8.98400   43.41700  1.000 36.05867 ? 167 LYS   B NZ    1 
ATOM   3958 N  N     . GLU   C 1 169 ? -1.76100  3.51600   39.29400  1.000 37.80602 ? 168 GLU   B N     1 
ATOM   3959 C  CA    . GLU   C 1 169 ? -2.67600  2.61600   38.61200  1.000 44.37573 ? 168 GLU   B CA    1 
ATOM   3960 C  C     . GLU   C 1 169 ? -1.97500  1.43100   37.96600  1.000 46.26355 ? 168 GLU   B C     1 
ATOM   3961 O  O     . GLU   C 1 169 ? -2.61100  0.68400   37.20900  1.000 44.88057 ? 168 GLU   B O     1 
ATOM   3962 C  CB    . GLU   C 1 169 ? -3.58000  3.37800   37.64000  1.000 41.32465 ? 168 GLU   B CB    1 
ATOM   3963 C  CG    . GLU   C 1 169 ? -2.93900  3.80000   36.34600  1.000 45.96866 ? 168 GLU   B CG    1 
ATOM   3964 C  CD    . GLU   C 1 169 ? -3.94200  4.46000   35.42000  1.000 50.29501 ? 168 GLU   B CD    1 
ATOM   3965 O  OE1   . GLU   C 1 169 ? -4.11700  5.69200   35.53000  1.000 50.17727 ? 168 GLU   B OE1   1 
ATOM   3966 O  OE2   . GLU   C 1 169 ? -4.57200  3.73400   34.60700  1.000 48.54764 ? 168 GLU   B OE2   1 
ATOM   3967 N  N     . LYS   C 1 170 ? -0.70100  1.21000   38.28300  1.000 37.68737 ? 169 LYS   B N     1 
ATOM   3968 C  CA    . LYS   C 1 170 ? 0.02400   0.05100   37.76200  1.000 49.14735 ? 169 LYS   B CA    1 
ATOM   3969 C  C     . LYS   C 1 170 ? -0.52000  -1.22700  38.40800  1.000 51.95052 ? 169 LYS   B C     1 
ATOM   3970 O  O     . LYS   C 1 170 ? -0.91400  -1.21100  39.57300  1.000 46.24768 ? 169 LYS   B O     1 
ATOM   3971 C  CB    . LYS   C 1 170 ? 1.53300   0.19400   38.00200  1.000 44.99862 ? 169 LYS   B CB    1 
ATOM   3972 C  CG    . LYS   C 1 170 ? 1.93600   0.19600   39.46200  1.000 48.11263 ? 169 LYS   B CG    1 
ATOM   3973 C  CD    . LYS   C 1 170 ? 3.35500   0.70500   39.64100  1.000 48.43517 ? 169 LYS   B CD    1 
ATOM   3974 C  CE    . LYS   C 1 170 ? 4.37600   -0.36200  39.32400  1.000 43.30350 ? 169 LYS   B CE    1 
ATOM   3975 N  NZ    . LYS   C 1 170 ? 5.55500   0.22000   38.61800  1.000 52.20514 ? 169 LYS   B NZ    1 
ATOM   3976 O  OXT   . LYS   C 1 170 ? -0.60600  -2.29400  37.78500  1.000 50.13744 ? 169 LYS   B OXT   1 
ATOM   3977 N  N     . SER   D 2 1   ? 28.39900  56.39300  82.43900  1.000 36.23252 ? 0   SER   C N     1 
ATOM   3978 C  CA    . SER   D 2 1   ? 28.24100  55.60300  81.23000  1.000 35.98718 ? 0   SER   C CA    1 
ATOM   3979 C  C     . SER   D 2 1   ? 28.15800  54.12600  81.60500  1.000 36.24756 ? 0   SER   C C     1 
ATOM   3980 O  O     . SER   D 2 1   ? 28.51400  53.74200  82.71800  1.000 32.81555 ? 0   SER   C O     1 
ATOM   3981 C  CB    . SER   D 2 1   ? 29.43000  55.81000  80.30900  1.000 32.35856 ? 0   SER   C CB    1 
ATOM   3982 O  OG    . SER   D 2 1   ? 30.25500  54.67200  80.38900  1.000 41.13097 ? 0   SER   C OG    1 
ATOM   3983 N  N     . MET   D 2 2   ? 27.68400  53.29600  80.67700  1.000 35.77339 ? 1   MET   C N     1 
ATOM   3984 C  CA    . MET   D 2 2   ? 27.56200  51.86200  80.89900  1.000 33.92108 ? 1   MET   C CA    1 
ATOM   3985 C  C     . MET   D 2 2   ? 28.42000  51.13200  79.87900  1.000 35.67875 ? 1   MET   C C     1 
ATOM   3986 O  O     . MET   D 2 2   ? 28.58200  51.59700  78.74700  1.000 37.94021 ? 1   MET   C O     1 
ATOM   3987 C  CB    . MET   D 2 2   ? 26.10800  51.40000  80.74300  1.000 38.51730 ? 1   MET   C CB    1 
ATOM   3988 C  CG    . MET   D 2 2   ? 25.15500  51.97000  81.78500  1.000 33.18814 ? 1   MET   C CG    1 
ATOM   3989 S  SD    . MET   D 2 2   ? 25.59600  51.38100  83.43500  1.000 45.97655 ? 1   MET   C SD    1 
ATOM   3990 C  CE    . MET   D 2 2   ? 25.15800  49.64200  83.30000  1.000 45.03470 ? 1   MET   C CE    1 
ATOM   3991 N  N     . VAL   D 2 3   ? 28.97400  49.98300  80.28500  1.000 29.84630 ? 2   VAL   C N     1 
ATOM   3992 C  CA    . VAL   D 2 3   ? 29.66300  49.12800  79.32200  1.000 30.35259 ? 2   VAL   C CA    1 
ATOM   3993 C  C     . VAL   D 2 3   ? 28.71800  48.76300  78.19000  1.000 34.67758 ? 2   VAL   C C     1 
ATOM   3994 O  O     . VAL   D 2 3   ? 29.03500  48.93300  77.00600  1.000 31.78006 ? 2   VAL   C O     1 
ATOM   3995 C  CB    . VAL   D 2 3   ? 30.23100  47.86800  80.00000  1.000 32.09261 ? 2   VAL   C CB    1 
ATOM   3996 C  CG1   . VAL   D 2 3   ? 30.79800  46.92200  78.95700  1.000 31.63813 ? 2   VAL   C CG1   1 
ATOM   3997 C  CG2   . VAL   D 2 3   ? 31.30900  48.23900  80.98100  1.000 31.75979 ? 2   VAL   C CG2   1 
ATOM   3998 N  N     . ASN   D 2 4   ? 27.54200  48.25800  78.53900  1.000 30.04692 ? 3   ASN   C N     1 
ATOM   3999 C  CA    . ASN   D 2 4   ? 26.58500  47.82400  77.53100  1.000 27.68957 ? 3   ASN   C CA    1 
ATOM   4000 C  C     . ASN   D 2 4   ? 25.66100  48.98100  77.15900  1.000 30.64077 ? 3   ASN   C C     1 
ATOM   4001 O  O     . ASN   D 2 4   ? 24.86100  49.41700  78.00100  1.000 29.67848 ? 3   ASN   C O     1 
ATOM   4002 C  CB    . ASN   D 2 4   ? 25.79100  46.63900  78.03800  1.000 27.23111 ? 3   ASN   C CB    1 
ATOM   4003 C  CG    . ASN   D 2 4   ? 26.63200  45.37000  78.11500  1.000 25.59329 ? 3   ASN   C CG    1 
ATOM   4004 O  OD1   . ASN   D 2 4   ? 27.77600  45.33500  77.65700  1.000 28.86530 ? 3   ASN   C OD1   1 
ATOM   4005 N  ND2   . ASN   D 2 4   ? 26.05800  44.31400  78.66000  1.000 31.68741 ? 3   ASN   C ND2   1 
ATOM   4006 N  N     . PRO   D 2 5   ? 25.74200  49.51100  75.93500  1.000 26.27461 ? 4   PRO   C N     1 
ATOM   4007 C  CA    . PRO   D 2 5   ? 24.85200  50.60800  75.53300  1.000 27.81483 ? 4   PRO   C CA    1 
ATOM   4008 C  C     . PRO   D 2 5   ? 23.40800  50.14400  75.38300  1.000 23.32447 ? 4   PRO   C C     1 
ATOM   4009 O  O     . PRO   D 2 5   ? 23.11200  48.96600  75.19500  1.000 23.25326 ? 4   PRO   C O     1 
ATOM   4010 C  CB    . PRO   D 2 5   ? 25.41500  51.04100  74.17200  1.000 30.85065 ? 4   PRO   C CB    1 
ATOM   4011 C  CG    . PRO   D 2 5   ? 26.03500  49.80200  73.61300  1.000 32.70577 ? 4   PRO   C CG    1 
ATOM   4012 C  CD    . PRO   D 2 5   ? 26.60500  49.05900  74.82600  1.000 27.61319 ? 4   PRO   C CD    1 
ATOM   4013 N  N     . THR   D 2 6   ? 22.49000  51.10900  75.44500  1.000 25.52164 ? 5   THR   C N     1 
ATOM   4014 C  CA    . THR   D 2 6   ? 21.06600  50.86100  75.22100  1.000 21.35457 ? 5   THR   C CA    1 
ATOM   4015 C  C     . THR   D 2 6   ? 20.65000  51.63200  73.98400  1.000 23.96817 ? 5   THR   C C     1 
ATOM   4016 O  O     . THR   D 2 6   ? 20.95000  52.82000  73.87200  1.000 27.44694 ? 5   THR   C O     1 
ATOM   4017 C  CB    . THR   D 2 6   ? 20.23400  51.37100  76.41400  1.000 23.51457 ? 5   THR   C CB    1 
ATOM   4018 O  OG1   . THR   D 2 6   ? 20.70700  50.77100  77.61600  1.000 29.35430 ? 5   THR   C OG1   1 
ATOM   4019 C  CG2   . THR   D 2 6   ? 18.76500  51.02000  76.23500  1.000 25.48341 ? 5   THR   C CG2   1 
ATOM   4020 N  N     . VAL   D 2 7   ? 19.94800  50.97000  73.06700  1.000 23.36664 ? 6   VAL   C N     1 
ATOM   4021 C  CA    . VAL   D 2 7   ? 19.39000  51.64400  71.90100  1.000 22.48892 ? 6   VAL   C CA    1 
ATOM   4022 C  C     . VAL   D 2 7   ? 17.89100  51.38900  71.85900  1.000 23.54896 ? 6   VAL   C C     1 
ATOM   4023 O  O     . VAL   D 2 7   ? 17.36800  50.48400  72.52000  1.000 24.06826 ? 6   VAL   C O     1 
ATOM   4024 C  CB    . VAL   D 2 7   ? 20.06300  51.24700  70.57000  1.000 24.80325 ? 6   VAL   C CB    1 
ATOM   4025 C  CG1   . VAL   D 2 7   ? 21.54400  51.60300  70.58800  1.000 27.25268 ? 6   VAL   C CG1   1 
ATOM   4026 C  CG2   . VAL   D 2 7   ? 19.85400  49.79000  70.29100  1.000 26.03498 ? 6   VAL   C CG2   1 
ATOM   4027 N  N     . PHE   D 2 8   ? 17.19200  52.22000  71.09500  1.000 22.53196 ? 7   PHE   C N     1 
ATOM   4028 C  CA    . PHE   D 2 8   ? 15.74400  52.09200  70.97400  1.000 22.69942 ? 7   PHE   C CA    1 
ATOM   4029 C  C     . PHE   D 2 8   ? 15.32200  52.04700  69.51500  1.000 22.61714 ? 7   PHE   C C     1 
ATOM   4030 O  O     . PHE   D 2 8   ? 15.95900  52.64900  68.64400  1.000 22.16011 ? 7   PHE   C O     1 
ATOM   4031 C  CB    . PHE   D 2 8   ? 14.97200  53.25200  71.69800  1.000 22.89285 ? 7   PHE   C CB    1 
ATOM   4032 C  CG    . PHE   D 2 8   ? 15.04600  54.57900  70.99600  1.000 26.73846 ? 7   PHE   C CG    1 
ATOM   4033 C  CD1   . PHE   D 2 8   ? 16.07000  55.45700  71.27600  1.000 33.79992 ? 7   PHE   C CD1   1 
ATOM   4034 C  CD2   . PHE   D 2 8   ? 14.07800  54.95900  70.06700  1.000 27.26889 ? 7   PHE   C CD2   1 
ATOM   4035 C  CE1   . PHE   D 2 8   ? 16.13200  56.66800  70.64400  1.000 30.50829 ? 7   PHE   C CE1   1 
ATOM   4036 C  CE2   . PHE   D 2 8   ? 14.15200  56.17500  69.42200  1.000 32.16015 ? 7   PHE   C CE2   1 
ATOM   4037 C  CZ    . PHE   D 2 8   ? 15.17700  57.02400  69.71300  1.000 33.28741 ? 7   PHE   C CZ    1 
ATOM   4038 N  N     . PHE   D 2 9   ? 14.22900  51.34200  69.27200  1.000 19.43497 ? 8   PHE   C N     1 
ATOM   4039 C  CA    . PHE   D 2 9   ? 13.46000  51.46000  68.03800  1.000 20.95659 ? 8   PHE   C CA    1 
ATOM   4040 C  C     . PHE   D 2 9   ? 12.07200  51.95700  68.39600  1.000 23.88914 ? 8   PHE   C C     1 
ATOM   4041 O  O     . PHE   D 2 9   ? 11.41000  51.37500  69.26800  1.000 22.02057 ? 8   PHE   C O     1 
ATOM   4042 C  CB    . PHE   D 2 9   ? 13.22700  50.08800  67.40100  1.000 20.13392 ? 8   PHE   C CB    1 
ATOM   4043 C  CG    . PHE   D 2 9   ? 14.42100  49.46400  66.75600  1.000 19.66043 ? 8   PHE   C CG    1 
ATOM   4044 C  CD1   . PHE   D 2 9   ? 15.61800  50.13100  66.63900  1.000 22.16265 ? 8   PHE   C CD1   1 
ATOM   4045 C  CD2   . PHE   D 2 9   ? 14.32800  48.14900  66.28200  1.000 20.51713 ? 8   PHE   C CD2   1 
ATOM   4046 C  CE1   . PHE   D 2 9   ? 16.71400  49.51000  66.07700  1.000 19.42679 ? 8   PHE   C CE1   1 
ATOM   4047 C  CE2   . PHE   D 2 9   ? 15.42100  47.51700  65.69100  1.000 19.77965 ? 8   PHE   C CE2   1 
ATOM   4048 C  CZ    . PHE   D 2 9   ? 16.62300  48.22200  65.58700  1.000 20.85873 ? 8   PHE   C CZ    1 
ATOM   4049 N  N     . ASP   D 2 10  ? 11.58600  52.95800  67.66400  1.000 22.19283 ? 9   ASP   C N     1 
ATOM   4050 C  CA    . ASP   D 2 10  ? 10.16800  53.30700  67.69900  1.000 22.75680 ? 9   ASP   C CA    1 
ATOM   4051 C  C     . ASP   D 2 10  ? 9.50100   52.61000  66.51200  1.000 21.36465 ? 9   ASP   C C     1 
ATOM   4052 O  O     . ASP   D 2 10  ? 9.82000   52.89900  65.35500  1.000 23.18622 ? 9   ASP   C O     1 
ATOM   4053 C  CB    . ASP   D 2 10  ? 9.97000   54.82100  67.64500  1.000 22.21041 ? 9   ASP   C CB    1 
ATOM   4054 C  CG    . ASP   D 2 10  ? 10.30700  55.50900  68.97800  1.000 28.28861 ? 9   ASP   C CG    1 
ATOM   4055 O  OD1   . ASP   D 2 10  ? 10.02800  54.91000  70.04000  1.000 32.20395 ? 9   ASP   C OD1   1 
ATOM   4056 O  OD2   . ASP   D 2 10  ? 10.83600  56.64600  68.96000  1.000 31.35022 ? 9   ASP   C OD2   1 
ATOM   4057 N  N     . ILE   D 2 11  ? 8.63000   51.66300  66.78700  1.000 21.89527 ? 10  ILE   C N     1 
ATOM   4058 C  CA    . ILE   D 2 11  ? 8.04900   50.80400  65.76200  1.000 21.00253 ? 10  ILE   C CA    1 
ATOM   4059 C  C     . ILE   D 2 11  ? 6.74700   51.41200  65.28200  1.000 20.28754 ? 10  ILE   C C     1 
ATOM   4060 O  O     . ILE   D 2 11  ? 5.96900   51.95300  66.06600  1.000 23.68808 ? 10  ILE   C O     1 
ATOM   4061 C  CB    . ILE   D 2 11  ? 7.80500   49.39900  66.35100  1.000 19.18609 ? 10  ILE   C CB    1 
ATOM   4062 C  CG1   . ILE   D 2 11  ? 9.09800   48.82400  66.93100  1.000 21.85685 ? 10  ILE   C CG1   1 
ATOM   4063 C  CG2   . ILE   D 2 11  ? 7.26100   48.44000  65.30200  1.000 21.56278 ? 10  ILE   C CG2   1 
ATOM   4064 C  CD1   . ILE   D 2 11  ? 10.09000  48.44200  65.87700  1.000 19.98957 ? 10  ILE   C CD1   1 
ATOM   4065 N  N     . ALA   D 2 12  ? 6.48800   51.30600  63.97800  1.000 20.10900 ? 11  ALA   C N     1 
ATOM   4066 C  CA    . ALA   D 2 12  ? 5.27500   51.84900  63.39100  1.000 19.53772 ? 11  ALA   C CA    1 
ATOM   4067 C  C     . ALA   D 2 12  ? 4.57800   50.77300  62.56200  1.000 19.70267 ? 11  ALA   C C     1 
ATOM   4068 O  O     . ALA   D 2 12  ? 5.21900   49.87000  62.02200  1.000 19.21129 ? 11  ALA   C O     1 
ATOM   4069 C  CB    . ALA   D 2 12  ? 5.60800   53.06500  62.52500  1.000 21.90601 ? 11  ALA   C CB    1 
ATOM   4070 N  N     . VAL   D 2 13  ? 3.25000   50.86000  62.49100  1.000 20.50929 ? 12  VAL   C N     1 
ATOM   4071 C  CA    . VAL   D 2 13  ? 2.41700   49.96900  61.68500  1.000 22.37454 ? 12  VAL   C CA    1 
ATOM   4072 C  C     . VAL   D 2 13  ? 1.70200   50.85200  60.67200  1.000 23.23279 ? 12  VAL   C C     1 
ATOM   4073 O  O     . VAL   D 2 13  ? 0.89300   51.70900  61.04800  1.000 24.07927 ? 12  VAL   C O     1 
ATOM   4074 C  CB    . VAL   D 2 13  ? 1.39400   49.21600  62.55500  1.000 22.91212 ? 12  VAL   C CB    1 
ATOM   4075 C  CG1   . VAL   D 2 13  ? 0.52900   48.29500  61.69000  1.000 24.10724 ? 12  VAL   C CG1   1 
ATOM   4076 C  CG2   . VAL   D 2 13  ? 2.08300   48.45000  63.67600  1.000 24.88240 ? 12  VAL   C CG2   1 
ATOM   4077 N  N     . ASP   D 2 14  ? 2.01500   50.66100  59.39100  1.000 22.98761 ? 13  ASP   C N     1 
ATOM   4078 C  CA    . ASP   D 2 14  ? 1.58700   51.56700  58.32000  1.000 24.13576 ? 13  ASP   C CA    1 
ATOM   4079 C  C     . ASP   D 2 14  ? 1.78100   53.05100  58.68900  1.000 28.78098 ? 13  ASP   C C     1 
ATOM   4080 O  O     . ASP   D 2 14  ? 0.91900   53.90500  58.47900  1.000 28.95946 ? 13  ASP   C O     1 
ATOM   4081 C  CB    . ASP   D 2 14  ? 0.16500   51.24900  57.86200  1.000 30.28382 ? 13  ASP   C CB    1 
ATOM   4082 C  CG    . ASP   D 2 14  ? 0.07000   49.90700  57.12800  1.000 30.59371 ? 13  ASP   C CG    1 
ATOM   4083 O  OD1   . ASP   D 2 14  ? 1.11300   49.38700  56.67000  1.000 33.44759 ? 13  ASP   C OD1   1 
ATOM   4084 O  OD2   . ASP   D 2 14  ? -1.05300  49.37000  57.00100  1.000 37.49399 ? 13  ASP   C OD2   1 
ATOM   4085 N  N     . GLY   D 2 15  ? 2.96000   53.36200  59.22300  1.000 24.45057 ? 14  GLY   C N     1 
ATOM   4086 C  CA    . GLY   D 2 15  ? 3.31600   54.69700  59.60300  1.000 25.91545 ? 14  GLY   C CA    1 
ATOM   4087 C  C     . GLY   D 2 15  ? 2.79900   55.15400  60.95100  1.000 28.75297 ? 14  GLY   C C     1 
ATOM   4088 O  O     . GLY   D 2 15  ? 3.23100   56.21500  61.42500  1.000 31.00358 ? 14  GLY   C O     1 
ATOM   4089 N  N     . GLU   D 2 16  ? 1.90200   54.38600  61.59700  1.000 22.09128 ? 15  GLU   C N     1 
ATOM   4090 C  CA    . GLU   D 2 16  ? 1.37700   54.90000  62.86200  1.000 26.08528 ? 15  GLU   C CA    1 
ATOM   4091 C  C     . GLU   D 2 16  ? 2.13400   54.29800  64.03400  1.000 23.89688 ? 15  GLU   C C     1 
ATOM   4092 O  O     . GLU   D 2 16  ? 2.52200   53.13400  63.98100  1.000 22.24452 ? 15  GLU   C O     1 
ATOM   4093 C  CB    . GLU   D 2 16  ? -0.10200  54.55200  63.04700  1.000 26.82107 ? 15  GLU   C CB    1 
ATOM   4094 C  CG    . GLU   D 2 16  ? -1.03400  55.05600  61.95500  1.000 27.39491 ? 15  GLU   C CG    1 
ATOM   4095 C  CD    . GLU   D 2 16  ? -1.07400  56.59400  61.86100  1.000 30.32139 ? 15  GLU   C CD    1 
ATOM   4096 O  OE1   . GLU   D 2 16  ? -0.96200  57.27000  62.89000  1.000 33.38864 ? 15  GLU   C OE1   1 
ATOM   4097 O  OE2   . GLU   D 2 16  ? -1.19100  57.13600  60.74500  1.000 38.80415 ? 15  GLU   C OE2   1 
ATOM   4098 N  N     . PRO   D 2 17  ? 2.31200   55.06800  65.10800  1.000 27.82254 ? 16  PRO   C N     1 
ATOM   4099 C  CA    . PRO   D 2 17  ? 3.15300   54.62300  66.22500  1.000 29.70137 ? 16  PRO   C CA    1 
ATOM   4100 C  C     . PRO   D 2 17  ? 2.54800   53.40800  66.91400  1.000 28.99959 ? 16  PRO   C C     1 
ATOM   4101 O  O     . PRO   D 2 17  ? 1.37700   53.40900  67.29600  1.000 31.82487 ? 16  PRO   C O     1 
ATOM   4102 C  CB    . PRO   D 2 17  ? 3.16700   55.84500  67.15000  1.000 31.35311 ? 16  PRO   C CB    1 
ATOM   4103 C  CG    . PRO   D 2 17  ? 2.87900   56.97100  66.26300  1.000 37.74145 ? 16  PRO   C CG    1 
ATOM   4104 C  CD    . PRO   D 2 17  ? 1.85500   56.45100  65.30400  1.000 32.86389 ? 16  PRO   C CD    1 
ATOM   4105 N  N     . LEU   D 2 18  ? 3.34700   52.35200  67.03800  1.000 24.11003 ? 17  LEU   C N     1 
ATOM   4106 C  CA    . LEU   D 2 18  ? 2.96700   51.18400  67.82500  1.000 24.08644 ? 17  LEU   C CA    1 
ATOM   4107 C  C     . LEU   D 2 18  ? 3.53500   51.25900  69.24100  1.000 26.25651 ? 17  LEU   C C     1 
ATOM   4108 O  O     . LEU   D 2 18  ? 2.78600   51.12100  70.20900  1.000 28.16310 ? 17  LEU   C O     1 
ATOM   4109 C  CB    . LEU   D 2 18  ? 3.42300   49.90300  67.12000  1.000 23.22224 ? 17  LEU   C CB    1 
ATOM   4110 C  CG    . LEU   D 2 18  ? 3.01700   48.58400  67.78200  1.000 25.43657 ? 17  LEU   C CG    1 
ATOM   4111 C  CD1   . LEU   D 2 18  ? 1.49300   48.39500  67.68300  1.000 32.72204 ? 17  LEU   C CD1   1 
ATOM   4112 C  CD2   . LEU   D 2 18  ? 3.71400   47.49600  67.06300  1.000 23.86088 ? 17  LEU   C CD2   1 
ATOM   4113 N  N     . GLY   D 2 19  ? 4.82000   51.54500  69.36800  1.000 24.58910 ? 18  GLY   C N     1 
ATOM   4114 C  CA    . GLY   D 2 19  ? 5.46600   51.63200  70.66500  1.000 24.52782 ? 18  GLY   C CA    1 
ATOM   4115 C  C     . GLY   D 2 19  ? 6.96500   51.52600  70.51300  1.000 24.20084 ? 18  GLY   C C     1 
ATOM   4116 O  O     . GLY   D 2 19  ? 7.48800   51.28300  69.42900  1.000 24.68124 ? 18  GLY   C O     1 
ATOM   4117 N  N     . ARG   D 2 20  ? 7.64900   51.69000  71.64000  1.000 22.77507 ? 19  ARG   C N     1 
ATOM   4118 C  CA    . ARG   D 2 20  ? 9.10500   51.68500  71.66900  1.000 22.28781 ? 19  ARG   C CA    1 
ATOM   4119 C  C     . ARG   D 2 20  ? 9.63700   50.35700  72.19600  1.000 23.14305 ? 19  ARG   C C     1 
ATOM   4120 O  O     . ARG   D 2 20  ? 9.11400   49.81300  73.17000  1.000 23.43380 ? 19  ARG   C O     1 
ATOM   4121 C  CB    . ARG   D 2 20  ? 9.62100   52.82400  72.55800  1.000 26.29602 ? 19  ARG   C CB    1 
ATOM   4122 C  CG    . ARG   D 2 20  ? 11.14500  52.83000  72.78900  1.000 23.82875 ? 19  ARG   C CG    1 
ATOM   4123 C  CD    . ARG   D 2 20  ? 11.65300  54.12600  73.42000  1.000 28.12627 ? 19  ARG   C CD    1 
ATOM   4124 N  NE    . ARG   D 2 20  ? 11.49900  55.25200  72.51400  1.000 27.35219 ? 19  ARG   C NE    1 
ATOM   4125 C  CZ    . ARG   D 2 20  ? 12.08000  56.43100  72.67400  1.000 33.84088 ? 19  ARG   C CZ    1 
ATOM   4126 N  NH1   . ARG   D 2 20  ? 12.82600  56.69500  73.73600  1.000 35.44197 ? 19  ARG   C NH1   1 
ATOM   4127 N  NH2   . ARG   D 2 20  ? 11.89700  57.36900  71.74700  1.000 33.17907 ? 19  ARG   C NH2   1 
ATOM   4128 N  N     . VAL   D 2 21  ? 10.68100  49.84300  71.55000  1.000 20.37655 ? 20  VAL   C N     1 
ATOM   4129 C  CA    . VAL   D 2 21  ? 11.43000  48.68200  72.02900  1.000 20.16261 ? 20  VAL   C CA    1 
ATOM   4130 C  C     . VAL   D 2 21  ? 12.84700  49.16300  72.30700  1.000 20.41914 ? 20  VAL   C C     1 
ATOM   4131 O  O     . VAL   D 2 21  ? 13.47400  49.79000  71.44500  1.000 22.45649 ? 20  VAL   C O     1 
ATOM   4132 C  CB    . VAL   D 2 21  ? 11.43800  47.53700  70.98900  1.000 18.49513 ? 20  VAL   C CB    1 
ATOM   4133 C  CG1   . VAL   D 2 21  ? 12.19300  46.33500  71.51600  1.000 20.87978 ? 20  VAL   C CG1   1 
ATOM   4134 C  CG2   . VAL   D 2 21  ? 10.03000  47.10600  70.60100  1.000 20.38150 ? 20  VAL   C CG2   1 
ATOM   4135 N  N     . SER   D 2 22  ? 13.35700  48.88600  73.49800  1.000 22.09188 ? 21  SER   C N     1 
ATOM   4136 C  CA    . SER   D 2 22  ? 14.73500  49.22400  73.82100  1.000 22.23581 ? 21  SER   C CA    1 
ATOM   4137 C  C     . SER   D 2 22  ? 15.52500  47.93300  73.99400  1.000 22.38025 ? 21  SER   C C     1 
ATOM   4138 O  O     . SER   D 2 22  ? 14.96700  46.89600  74.35500  1.000 21.89850 ? 21  SER   C O     1 
ATOM   4139 C  CB    . SER   D 2 22  ? 14.82400  50.08600  75.08100  1.000 24.18821 ? 21  SER   C CB    1 
ATOM   4140 O  OG    . SER   D 2 22  ? 14.43700  49.37800  76.23500  1.000 27.03252 ? 21  SER   C OG    1 
ATOM   4141 N  N     . PHE   D 2 23  ? 16.82600  47.99200  73.69400  1.000 21.09944 ? 22  PHE   C N     1 
ATOM   4142 C  CA    . PHE   D 2 23  ? 17.69600  46.82000  73.71200  1.000 17.96150 ? 22  PHE   C CA    1 
ATOM   4143 C  C     . PHE   D 2 23  ? 18.95400  47.14600  74.49600  1.000 21.14409 ? 22  PHE   C C     1 
ATOM   4144 O  O     . PHE   D 2 23  ? 19.51900  48.22800  74.34400  1.000 22.71863 ? 22  PHE   C O     1 
ATOM   4145 C  CB    . PHE   D 2 23  ? 18.18000  46.51200  72.28700  1.000 21.05916 ? 22  PHE   C CB    1 
ATOM   4146 C  CG    . PHE   D 2 23  ? 17.07700  46.30900  71.29600  1.000 19.60634 ? 22  PHE   C CG    1 
ATOM   4147 C  CD1   . PHE   D 2 23  ? 16.49300  45.05700  71.15700  1.000 19.27838 ? 22  PHE   C CD1   1 
ATOM   4148 C  CD2   . PHE   D 2 23  ? 16.63500  47.36800  70.49100  1.000 20.82304 ? 22  PHE   C CD2   1 
ATOM   4149 C  CE1   . PHE   D 2 23  ? 15.47800  44.83900  70.21600  1.000 18.73769 ? 22  PHE   C CE1   1 
ATOM   4150 C  CE2   . PHE   D 2 23  ? 15.60700  47.16400  69.54100  1.000 21.82088 ? 22  PHE   C CE2   1 
ATOM   4151 C  CZ    . PHE   D 2 23  ? 15.03200  45.90100  69.41700  1.000 20.39839 ? 22  PHE   C CZ    1 
ATOM   4152 N  N     . GLU   D 2 24  ? 19.39500  46.20500  75.32900  1.000 20.02419 ? 23  GLU   C N     1 
ATOM   4153 C  CA    . GLU   D 2 24  ? 20.74500  46.22700  75.87300  1.000 20.14257 ? 23  GLU   C CA    1 
ATOM   4154 C  C     . GLU   D 2 24  ? 21.66300  45.50900  74.89600  1.000 19.69196 ? 23  GLU   C C     1 
ATOM   4155 O  O     . GLU   D 2 24  ? 21.34400  44.41600  74.42900  1.000 21.22694 ? 23  GLU   C O     1 
ATOM   4156 C  CB    . GLU   D 2 24  ? 20.77800  45.47700  77.20800  1.000 22.60053 ? 23  GLU   C CB    1 
ATOM   4157 C  CG    . GLU   D 2 24  ? 22.19600  45.36700  77.79600  1.000 23.67772 ? 23  GLU   C CG    1 
ATOM   4158 C  CD    . GLU   D 2 24  ? 22.24400  44.59200  79.09500  1.000 33.47516 ? 23  GLU   C CD    1 
ATOM   4159 O  OE1   . GLU   D 2 24  ? 21.16800  44.19600  79.59900  1.000 33.67838 ? 23  GLU   C OE1   1 
ATOM   4160 O  OE2   . GLU   D 2 24  ? 23.36600  44.39700  79.60200  1.000 31.24039 ? 23  GLU   C OE2   1 
ATOM   4161 N  N     . LEU   D 2 25  ? 22.77300  46.13700  74.54800  1.000 21.02247 ? 24  LEU   C N     1 
ATOM   4162 C  CA    . LEU   D 2 25  ? 23.71800  45.56200  73.60300  1.000 19.64913 ? 24  LEU   C CA    1 
ATOM   4163 C  C     . LEU   D 2 25  ? 24.93200  45.08400  74.38600  1.000 21.24168 ? 24  LEU   C C     1 
ATOM   4164 O  O     . LEU   D 2 25  ? 25.52700  45.85700  75.13800  1.000 23.05349 ? 24  LEU   C O     1 
ATOM   4165 C  CB    . LEU   D 2 25  ? 24.12300  46.61600  72.57100  1.000 21.48815 ? 24  LEU   C CB    1 
ATOM   4166 C  CG    . LEU   D 2 25  ? 22.96500  47.25000  71.78000  1.000 20.86018 ? 24  LEU   C CG    1 
ATOM   4167 C  CD1   . LEU   D 2 25  ? 23.50500  48.24000  70.75100  1.000 26.96603 ? 24  LEU   C CD1   1 
ATOM   4168 C  CD2   . LEU   D 2 25  ? 22.12900  46.19800  71.11700  1.000 19.44135 ? 24  LEU   C CD2   1 
ATOM   4169 N  N     . PHE   D 2 26  ? 25.31100  43.82600  74.19100  1.000 20.66008 ? 25  PHE   C N     1 
ATOM   4170 C  CA    . PHE   D 2 26  ? 26.30900  43.19200  75.05100  1.000 20.47572 ? 25  PHE   C CA    1 
ATOM   4171 C  C     . PHE   D 2 26  ? 27.72600  43.51900  74.57400  1.000 23.14930 ? 25  PHE   C C     1 
ATOM   4172 O  O     . PHE   D 2 26  ? 28.48100  42.66200  74.12500  1.000 23.81675 ? 25  PHE   C O     1 
ATOM   4173 C  CB    . PHE   D 2 26  ? 26.04900  41.69400  75.07500  1.000 23.53420 ? 25  PHE   C CB    1 
ATOM   4174 C  CG    . PHE   D 2 26  ? 24.70400  41.32000  75.64100  1.000 22.13240 ? 25  PHE   C CG    1 
ATOM   4175 C  CD1   . PHE   D 2 26  ? 24.18600  41.97300  76.74600  1.000 29.95146 ? 25  PHE   C CD1   1 
ATOM   4176 C  CD2   . PHE   D 2 26  ? 23.97300  40.30200  75.07900  1.000 22.02500 ? 25  PHE   C CD2   1 
ATOM   4177 C  CE1   . PHE   D 2 26  ? 22.94700  41.60000  77.26900  1.000 29.94386 ? 25  PHE   C CE1   1 
ATOM   4178 C  CE2   . PHE   D 2 26  ? 22.74700  39.92400  75.60500  1.000 25.52353 ? 25  PHE   C CE2   1 
ATOM   4179 C  CZ    . PHE   D 2 26  ? 22.23000  40.58600  76.66900  1.000 24.94756 ? 25  PHE   C CZ    1 
ATOM   4180 N  N     . ALA   D 2 27  ? 28.07300  44.80200  74.66200  1.000 23.35882 ? 26  ALA   C N     1 
ATOM   4181 C  CA    . ALA   D 2 27  ? 29.41700  45.21300  74.26200  1.000 24.76298 ? 26  ALA   C CA    1 
ATOM   4182 C  C     . ALA   D 2 27  ? 30.48800  44.57600  75.13700  1.000 28.71116 ? 26  ALA   C C     1 
ATOM   4183 O  O     . ALA   D 2 27  ? 31.65200  44.51500  74.73800  1.000 29.37981 ? 26  ALA   C O     1 
ATOM   4184 C  CB    . ALA   D 2 27  ? 29.53100  46.73600  74.25400  1.000 29.48593 ? 26  ALA   C CB    1 
ATOM   4185 N  N     . ASP   D 2 28  ? 30.12600  44.07700  76.31800  1.000 26.67482 ? 27  ASP   C N     1 
ATOM   4186 C  CA    . ASP   D 2 28  ? 31.13100  43.41500  77.14800  1.000 28.57891 ? 27  ASP   C CA    1 
ATOM   4187 C  C     . ASP   D 2 28  ? 31.53900  42.05200  76.60300  1.000 31.82655 ? 27  ASP   C C     1 
ATOM   4188 O  O     . ASP   D 2 28  ? 32.64300  41.58300  76.90500  1.000 40.47276 ? 27  ASP   C O     1 
ATOM   4189 C  CB    . ASP   D 2 28  ? 30.68900  43.35700  78.61200  1.000 35.43082 ? 27  ASP   C CB    1 
ATOM   4190 C  CG    . ASP   D 2 28  ? 29.31900  42.71900  78.80200  1.000 35.72659 ? 27  ASP   C CG    1 
ATOM   4191 O  OD1   . ASP   D 2 28  ? 28.72500  42.20300  77.82600  1.000 34.65137 ? 27  ASP   C OD1   1 
ATOM   4192 O  OD2   . ASP   D 2 28  ? 28.82700  42.76400  79.94900  1.000 34.23943 ? 27  ASP   C OD2   1 
ATOM   4193 N  N     . LYS   D 2 29  ? 30.70500  41.43200  75.78700  1.000 26.86690 ? 28  LYS   C N     1 
ATOM   4194 C  CA    . LYS   D 2 29  ? 30.94700  40.09900  75.24900  1.000 25.60685 ? 28  LYS   C CA    1 
ATOM   4195 C  C     . LYS   D 2 29  ? 31.23900  40.10600  73.75500  1.000 26.07910 ? 28  LYS   C C     1 
ATOM   4196 O  O     . LYS   D 2 29  ? 32.08100  39.33600  73.28400  1.000 25.91690 ? 28  LYS   C O     1 
ATOM   4197 C  CB    . LYS   D 2 29  ? 29.73700  39.19700  75.52900  1.000 30.40961 ? 28  LYS   C CB    1 
ATOM   4198 C  CG    . LYS   D 2 29  ? 29.51200  38.87200  77.02700  1.000 37.88872 ? 28  LYS   C CG    1 
ATOM   4199 C  CD    . LYS   D 2 29  ? 30.74000  38.16400  77.57400  1.000 32.38144 ? 28  LYS   C CD    1 
ATOM   4200 C  CE    . LYS   D 2 29  ? 30.79100  38.05200  79.10300  1.000 43.14910 ? 28  LYS   C CE    1 
ATOM   4201 N  NZ    . LYS   D 2 29  ? 32.10700  37.48500  79.50200  1.000 43.04374 ? 28  LYS   C NZ    1 
ATOM   4202 N  N     . VAL   D 2 30  ? 30.53700  40.94100  72.99800  1.000 27.22744 ? 29  VAL   C N     1 
ATOM   4203 C  CA    . VAL   D 2 30  ? 30.71100  41.02100  71.55100  1.000 23.68924 ? 29  VAL   C CA    1 
ATOM   4204 C  C     . VAL   D 2 30  ? 30.81500  42.49000  71.16700  1.000 23.63378 ? 29  VAL   C C     1 
ATOM   4205 O  O     . VAL   D 2 30  ? 29.87300  43.03300  70.56700  1.000 24.98664 ? 29  VAL   C O     1 
ATOM   4206 C  CB    . VAL   D 2 30  ? 29.55000  40.34200  70.80100  1.000 27.99868 ? 29  VAL   C CB    1 
ATOM   4207 C  CG1   . VAL   D 2 30  ? 29.77900  38.84100  70.67900  1.000 25.96845 ? 29  VAL   C CG1   1 
ATOM   4208 C  CG2   . VAL   D 2 30  ? 28.25400  40.60200  71.50500  1.000 27.04083 ? 29  VAL   C CG2   1 
ATOM   4209 N  N     . PRO   D 2 31  ? 31.94200  43.15400  71.44600  1.000 23.65899 ? 30  PRO   C N     1 
ATOM   4210 C  CA    . PRO   D 2 31  ? 32.01700  44.60800  71.19600  1.000 25.52941 ? 30  PRO   C CA    1 
ATOM   4211 C  C     . PRO   D 2 31  ? 31.87000  45.00100  69.73800  1.000 27.07172 ? 30  PRO   C C     1 
ATOM   4212 O  O     . PRO   D 2 31  ? 31.25000  46.03100  69.45100  1.000 26.70579 ? 30  PRO   C O     1 
ATOM   4213 C  CB    . PRO   D 2 31  ? 33.38600  45.00700  71.78000  1.000 27.84084 ? 30  PRO   C CB    1 
ATOM   4214 C  CG    . PRO   D 2 31  ? 34.17000  43.72700  71.86400  1.000 32.38666 ? 30  PRO   C CG    1 
ATOM   4215 C  CD    . PRO   D 2 31  ? 33.13100  42.66400  72.17500  1.000 25.21429 ? 30  PRO   C CD    1 
ATOM   4216 N  N     . LYS   D 2 32  ? 32.44700  44.22800  68.81400  1.000 25.98590 ? 31  LYS   C N     1 
ATOM   4217 C  CA    . LYS   D 2 32  ? 32.37900  44.59400  67.39900  1.000 25.70441 ? 31  LYS   C CA    1 
ATOM   4218 C  C     . LYS   D 2 32  ? 30.95200  44.49000  66.87600  1.000 25.10061 ? 31  LYS   C C     1 
ATOM   4219 O  O     . LYS   D 2 32  ? 30.49300  45.35900  66.12400  1.000 27.54803 ? 31  LYS   C O     1 
ATOM   4220 C  CB    . LYS   D 2 32  ? 33.32500  43.70700  66.58900  1.000 28.39518 ? 31  LYS   C CB    1 
ATOM   4221 C  CG    . LYS   D 2 32  ? 33.58000  44.16900  65.15300  1.000 36.61628 ? 31  LYS   C CG    1 
ATOM   4222 C  CD    . LYS   D 2 32  ? 34.63300  43.27800  64.49300  1.000 40.83279 ? 31  LYS   C CD    1 
ATOM   4223 C  CE    . LYS   D 2 32  ? 34.64000  43.38400  62.97500  1.000 38.17412 ? 31  LYS   C CE    1 
ATOM   4224 N  NZ    . LYS   D 2 32  ? 35.36600  42.21300  62.37600  1.000 46.12875 ? 31  LYS   C NZ    1 
ATOM   4225 N  N     . THR   D 2 33  ? 30.23500  43.44300  67.27600  1.000 22.90307 ? 32  THR   C N     1 
ATOM   4226 C  CA    . THR   D 2 33  ? 28.86500  43.25800  66.81900  1.000 23.08465 ? 32  THR   C CA    1 
ATOM   4227 C  C     . THR   D 2 33  ? 27.92600  44.26200  67.47800  1.000 23.43016 ? 32  THR   C C     1 
ATOM   4228 O  O     . THR   D 2 33  ? 27.05000  44.82500  66.81300  1.000 23.08457 ? 32  THR   C O     1 
ATOM   4229 C  CB    . THR   D 2 33  ? 28.44300  41.81300  67.09400  1.000 21.08022 ? 32  THR   C CB    1 
ATOM   4230 O  OG1   . THR   D 2 33  ? 29.44000  40.93100  66.55400  1.000 25.98529 ? 32  THR   C OG1   1 
ATOM   4231 C  CG2   . THR   D 2 33  ? 27.07500  41.49600  66.48500  1.000 20.88030 ? 32  THR   C CG2   1 
ATOM   4232 N  N     . ALA   D 2 34  ? 28.11400  44.52400  68.77800  1.000 21.80563 ? 33  ALA   C N     1 
ATOM   4233 C  CA    . ALA   D 2 34  ? 27.29700  45.52400  69.46200  1.000 22.85771 ? 33  ALA   C CA    1 
ATOM   4234 C  C     . ALA   D 2 34  ? 27.49900  46.91400  68.86300  1.000 24.77019 ? 33  ALA   C C     1 
ATOM   4235 O  O     . ALA   D 2 34  ? 26.52800  47.65000  68.68000  1.000 22.34578 ? 33  ALA   C O     1 
ATOM   4236 C  CB    . ALA   D 2 34  ? 27.60700  45.52500  70.96600  1.000 23.77022 ? 33  ALA   C CB    1 
ATOM   4237 N  N     . GLU   D 2 35  ? 28.75000  47.29200  68.57300  1.000 27.46343 ? 34  GLU   C N     1 
ATOM   4238 C  CA    . GLU   D 2 35  ? 29.03000  48.61800  68.01200  1.000 26.76405 ? 34  GLU   C CA    1 
ATOM   4239 C  C     . GLU   D 2 35  ? 28.39100  48.79600  66.63500  1.000 27.57617 ? 34  GLU   C C     1 
ATOM   4240 O  O     . GLU   D 2 35  ? 27.87200  49.87400  66.32300  1.000 26.78554 ? 34  GLU   C O     1 
ATOM   4241 C  CB    . GLU   D 2 35  ? 30.53500  48.85900  67.92000  1.000 26.12916 ? 34  GLU   C CB    1 
ATOM   4242 C  CG    . GLU   D 2 35  ? 30.92300  50.10600  67.10900  1.000 29.37919 ? 34  GLU   C CG    1 
ATOM   4243 C  CD    . GLU   D 2 35  ? 30.42300  51.39800  67.74300  1.000 36.60642 ? 34  GLU   C CD    1 
ATOM   4244 O  OE1   . GLU   D 2 35  ? 30.09800  51.40100  68.95200  1.000 33.62228 ? 34  GLU   C OE1   1 
ATOM   4245 O  OE2   . GLU   D 2 35  ? 30.39000  52.42800  67.03800  1.000 40.98522 ? 34  GLU   C OE2   1 
ATOM   4246 N  N     . ASN   D 2 36  ? 28.40600  47.74800  65.80700  1.000 24.44347 ? 35  ASN   C N     1 
ATOM   4247 C  CA    . ASN   D 2 36  ? 27.73900  47.81200  64.51100  1.000 29.07542 ? 35  ASN   C CA    1 
ATOM   4248 C  C     . ASN   D 2 36  ? 26.26000  48.12800  64.68100  1.000 25.92671 ? 35  ASN   C C     1 
ATOM   4249 O  O     . ASN   D 2 36  ? 25.73700  49.06100  64.06300  1.000 26.07299 ? 35  ASN   C O     1 
ATOM   4250 C  CB    . ASN   D 2 36  ? 27.91300  46.47300  63.80300  1.000 23.06890 ? 35  ASN   C CB    1 
ATOM   4251 C  CG    . ASN   D 2 36  ? 27.28100  46.46000  62.43900  1.000 23.49270 ? 35  ASN   C CG    1 
ATOM   4252 O  OD1   . ASN   D 2 36  ? 27.64800  47.26800  61.57000  1.000 27.83497 ? 35  ASN   C OD1   1 
ATOM   4253 N  ND2   . ASN   D 2 36  ? 26.37700  45.52400  62.21300  1.000 24.70809 ? 35  ASN   C ND2   1 
ATOM   4254 N  N     . PHE   D 2 37  ? 25.57400  47.37400  65.54600  1.000 24.83359 ? 36  PHE   C N     1 
ATOM   4255 C  CA    . PHE   D 2 37  ? 24.15300  47.63000  65.76300  1.000 23.84462 ? 36  PHE   C CA    1 
ATOM   4256 C  C     . PHE   D 2 37  ? 23.91900  49.01500  66.35600  1.000 22.61982 ? 36  PHE   C C     1 
ATOM   4257 O  O     . PHE   D 2 37  ? 22.99300  49.71400  65.94000  1.000 22.46607 ? 36  PHE   C O     1 
ATOM   4258 C  CB    . PHE   D 2 37  ? 23.55000  46.53200  66.64600  1.000 20.41429 ? 36  PHE   C CB    1 
ATOM   4259 C  CG    . PHE   D 2 37  ? 22.05300  46.52600  66.67700  1.000 17.74793 ? 36  PHE   C CG    1 
ATOM   4260 C  CD1   . PHE   D 2 37  ? 21.32800  45.75600  65.77300  1.000 19.81705 ? 36  PHE   C CD1   1 
ATOM   4261 C  CD2   . PHE   D 2 37  ? 21.36400  47.22700  67.64400  1.000 22.17052 ? 36  PHE   C CD2   1 
ATOM   4262 C  CE1   . PHE   D 2 37  ? 19.94300  45.72200  65.82200  1.000 19.29818 ? 36  PHE   C CE1   1 
ATOM   4263 C  CE2   . PHE   D 2 37  ? 19.97800  47.17800  67.71100  1.000 19.93432 ? 36  PHE   C CE2   1 
ATOM   4264 C  CZ    . PHE   D 2 37  ? 19.26300  46.42400  66.81000  1.000 20.47241 ? 36  PHE   C CZ    1 
ATOM   4265 N  N     . ARG   D 2 38  ? 24.76200  49.44200  67.29900  1.000 24.29053 ? 37  ARG   C N     1 
ATOM   4266 C  CA    . ARG   D 2 38  ? 24.57900  50.75200  67.91800  1.000 24.32087 ? 37  ARG   C CA    1 
ATOM   4267 C  C     . ARG   D 2 38  ? 24.69100  51.86600  66.88300  1.000 25.38255 ? 37  ARG   C C     1 
ATOM   4268 O  O     . ARG   D 2 38  ? 23.83900  52.76100  66.81400  1.000 25.83780 ? 37  ARG   C O     1 
ATOM   4269 C  CB    . ARG   D 2 38  ? 25.59600  50.95300  69.04600  1.000 22.85417 ? 37  ARG   C CB    1 
ATOM   4270 C  CG    . ARG   D 2 38  ? 25.42800  52.27000  69.81000  1.000 25.87643 ? 37  ARG   C CG    1 
ATOM   4271 C  CD    . ARG   D 2 38  ? 26.67600  52.64000  70.57500  1.000 28.78420 ? 37  ARG   C CD    1 
ATOM   4272 N  NE    . ARG   D 2 38  ? 27.70400  53.04900  69.61700  1.000 29.00486 ? 37  ARG   C NE    1 
ATOM   4273 C  CZ    . ARG   D 2 38  ? 27.66400  54.16700  68.90100  1.000 34.54958 ? 37  ARG   C CZ    1 
ATOM   4274 N  NH1   . ARG   D 2 38  ? 26.75000  55.10200  69.12000  1.000 32.53610 ? 37  ARG   C NH1   1 
ATOM   4275 N  NH2   . ARG   D 2 38  ? 28.55200  54.34600  67.92800  1.000 32.52606 ? 37  ARG   C NH2   1 
ATOM   4276 N  N     . ALA   D 2 39  ? 25.75000  51.81800  66.06700  1.000 25.74159 ? 38  ALA   C N     1 
ATOM   4277 C  CA    . ALA   D 2 39  ? 25.97900  52.83100  65.04200  1.000 26.93615 ? 38  ALA   C CA    1 
ATOM   4278 C  C     . ALA   D 2 39  ? 24.88700  52.81900  63.97500  1.000 25.02338 ? 38  ALA   C C     1 
ATOM   4279 O  O     . ALA   D 2 39  ? 24.48200  53.88000  63.49100  1.000 28.96235 ? 38  ALA   C O     1 
ATOM   4280 C  CB    . ALA   D 2 39  ? 27.35700  52.61700  64.42100  1.000 31.30199 ? 38  ALA   C CB    1 
ATOM   4281 N  N     . LEU   D 2 40  ? 24.41600  51.63700  63.57700  1.000 23.52892 ? 39  LEU   C N     1 
ATOM   4282 C  CA    . LEU   D 2 40  ? 23.32200  51.59800  62.60400  1.000 25.16906 ? 39  LEU   C CA    1 
ATOM   4283 C  C     . LEU   D 2 40  ? 22.03200  52.15800  63.19400  1.000 29.50611 ? 39  LEU   C C     1 
ATOM   4284 O  O     . LEU   D 2 40  ? 21.20100  52.70900  62.46200  1.000 25.05487 ? 39  LEU   C O     1 
ATOM   4285 C  CB    . LEU   D 2 40  ? 23.13100  50.17900  62.10100  1.000 23.37042 ? 39  LEU   C CB    1 
ATOM   4286 C  CG    . LEU   D 2 40  ? 24.27000  49.62500  61.27400  1.000 24.23366 ? 39  LEU   C CG    1 
ATOM   4287 C  CD1   . LEU   D 2 40  ? 23.96800  48.15800  60.99400  1.000 25.45699 ? 39  LEU   C CD1   1 
ATOM   4288 C  CD2   . LEU   D 2 40  ? 24.43800  50.43300  59.97600  1.000 27.39652 ? 39  LEU   C CD2   1 
ATOM   4289 N  N     . SER   D 2 41  ? 21.87600  52.07800  64.52000  1.000 26.48018 ? 40  SER   C N     1 
ATOM   4290 C  CA    . SER   D 2 41  ? 20.68700  52.60200  65.18000  1.000 24.59473 ? 40  SER   C CA    1 
ATOM   4291 C  C     . SER   D 2 41  ? 20.75200  54.11300  65.33400  1.000 26.75773 ? 40  SER   C C     1 
ATOM   4292 O  O     . SER   D 2 41  ? 19.71300  54.77800  65.30100  1.000 28.28630 ? 40  SER   C O     1 
ATOM   4293 C  CB    . SER   D 2 41  ? 20.51500  51.95700  66.55800  1.000 23.72530 ? 40  SER   C CB    1 
ATOM   4294 O  OG    . SER   D 2 41  ? 20.27800  50.57900  66.42500  1.000 25.10651 ? 40  SER   C OG    1 
ATOM   4295 N  N     . THR   D 2 42  ? 21.94700  54.67600  65.52200  1.000 27.71737 ? 41  THR   C N     1 
ATOM   4296 C  CA    . THR   D 2 42  ? 22.03800  56.13300  65.56000  1.000 28.28126 ? 41  THR   C CA    1 
ATOM   4297 C  C     . THR   D 2 42  ? 22.06600  56.73600  64.16200  1.000 30.86301 ? 41  THR   C C     1 
ATOM   4298 O  O     . THR   D 2 42  ? 21.68900  57.89800  63.99300  1.000 31.91300 ? 41  THR   C O     1 
ATOM   4299 C  CB    . THR   D 2 42  ? 23.29500  56.60400  66.30200  1.000 31.18404 ? 41  THR   C CB    1 
ATOM   4300 O  OG1   . THR   D 2 42  ? 24.45700  56.18700  65.57600  1.000 31.79086 ? 41  THR   C OG1   1 
ATOM   4301 C  CG2   . THR   D 2 42  ? 23.34200  56.04200  67.72700  1.000 27.45550 ? 41  THR   C CG2   1 
ATOM   4302 N  N     . GLY   D 2 43  ? 22.51500  55.97300  63.16900  1.000 28.28188 ? 42  GLY   C N     1 
ATOM   4303 C  CA    . GLY   D 2 43  ? 22.70500  56.50900  61.83000  1.000 27.40935 ? 42  GLY   C CA    1 
ATOM   4304 C  C     . GLY   D 2 43  ? 23.92900  57.37100  61.64800  1.000 37.61306 ? 42  GLY   C C     1 
ATOM   4305 O  O     . GLY   D 2 43  ? 24.01800  58.08600  60.64500  1.000 34.42762 ? 42  GLY   C O     1 
ATOM   4306 N  N     . GLU   D 2 44  ? 24.88600  57.31600  62.57900  1.000 30.88717 ? 43  GLU   C N     1 
ATOM   4307 C  CA    . GLU   D 2 44  ? 25.98700  58.27800  62.58100  1.000 32.19438 ? 43  GLU   C CA    1 
ATOM   4308 C  C     . GLU   D 2 44  ? 26.93100  58.10400  61.39400  1.000 33.60584 ? 43  GLU   C C     1 
ATOM   4309 O  O     . GLU   D 2 44  ? 27.66900  59.04400  61.06100  1.000 38.01402 ? 43  GLU   C O     1 
ATOM   4310 C  CB    . GLU   D 2 44  ? 26.71800  58.20600  63.92200  1.000 35.01168 ? 43  GLU   C CB    1 
ATOM   4311 C  CG    . GLU   D 2 44  ? 27.33600  56.85900  64.23700  1.000 34.72501 ? 43  GLU   C CG    1 
ATOM   4312 C  CD    . GLU   D 2 44  ? 27.71700  56.74000  65.70700  1.000 36.94318 ? 43  GLU   C CD    1 
ATOM   4313 O  OE1   . GLU   D 2 44  ? 26.79200  56.73100  66.54900  1.000 36.48313 ? 43  GLU   C OE1   1 
ATOM   4314 O  OE2   . GLU   D 2 44  ? 28.92400  56.67800  66.02600  1.000 38.48087 ? 43  GLU   C OE2   1 
ATOM   4315 N  N     . LYS   D 2 45  ? 26.92000  56.94000  60.74800  1.000 37.01753 ? 44  LYS   C N     1 
ATOM   4316 C  CA    . LYS   D 2 45  ? 27.72500  56.68100  59.56100  1.000 37.97765 ? 44  LYS   C CA    1 
ATOM   4317 C  C     . LYS   D 2 45  ? 27.07300  57.16800  58.27300  1.000 36.80446 ? 44  LYS   C C     1 
ATOM   4318 O  O     . LYS   D 2 45  ? 27.68100  57.02800  57.20700  1.000 37.77629 ? 44  LYS   C O     1 
ATOM   4319 C  CB    . LYS   D 2 45  ? 28.01400  55.18300  59.43000  1.000 40.71412 ? 44  LYS   C CB    1 
ATOM   4320 C  CG    . LYS   D 2 45  ? 28.84900  54.60800  60.54500  1.000 41.79756 ? 44  LYS   C CG    1 
ATOM   4321 C  CD    . LYS   D 2 45  ? 30.23100  55.22000  60.51700  1.000 48.85866 ? 44  LYS   C CD    1 
ATOM   4322 C  CE    . LYS   D 2 45  ? 31.17100  54.51900  61.49000  1.000 53.99879 ? 44  LYS   C CE    1 
ATOM   4323 N  NZ    . LYS   D 2 45  ? 32.58300  54.88600  61.18100  1.000 57.60207 ? 44  LYS   C NZ    1 
ATOM   4324 N  N     . GLY   D 2 46  ? 25.86200  57.72000  58.33200  1.000 38.39977 ? 45  GLY   C N     1 
ATOM   4325 C  CA    . GLY   D 2 46  ? 25.16500  58.16100  57.13800  1.000 39.35573 ? 45  GLY   C CA    1 
ATOM   4326 C  C     . GLY   D 2 46  ? 24.18300  57.16400  56.57000  1.000 38.39766 ? 45  GLY   C C     1 
ATOM   4327 O  O     . GLY   D 2 46  ? 23.57500  57.43400  55.52900  1.000 37.94300 ? 45  GLY   C O     1 
ATOM   4328 N  N     . PHE   D 2 47  ? 23.99400  56.03000  57.23300  1.000 32.88895 ? 46  PHE   C N     1 
ATOM   4329 C  CA    . PHE   D 2 47  ? 23.04500  55.00700  56.81800  1.000 31.56985 ? 46  PHE   C CA    1 
ATOM   4330 C  C     . PHE   D 2 47  ? 22.70700  54.20000  58.05800  1.000 32.77143 ? 46  PHE   C C     1 
ATOM   4331 O  O     . PHE   D 2 47  ? 23.46400  54.18600  59.03200  1.000 30.14822 ? 46  PHE   C O     1 
ATOM   4332 C  CB    . PHE   D 2 47  ? 23.61800  54.09700  55.72200  1.000 31.73345 ? 46  PHE   C CB    1 
ATOM   4333 C  CG    . PHE   D 2 47  ? 24.97100  53.53500  56.03300  1.000 31.59211 ? 46  PHE   C CG    1 
ATOM   4334 C  CD1   . PHE   D 2 47  ? 26.10800  54.23200  55.66700  1.000 37.15019 ? 46  PHE   C CD1   1 
ATOM   4335 C  CD2   . PHE   D 2 47  ? 25.11900  52.31600  56.69200  1.000 33.90287 ? 46  PHE   C CD2   1 
ATOM   4336 C  CE1   . PHE   D 2 47  ? 27.37100  53.73500  55.94400  1.000 41.19857 ? 46  PHE   C CE1   1 
ATOM   4337 C  CE2   . PHE   D 2 47  ? 26.39000  51.81300  56.97400  1.000 33.13616 ? 46  PHE   C CE2   1 
ATOM   4338 C  CZ    . PHE   D 2 47  ? 27.51200  52.52700  56.59900  1.000 36.64401 ? 46  PHE   C CZ    1 
ATOM   4339 N  N     . GLY   D 2 48  ? 21.55500  53.54200  58.02700  1.000 27.64634 ? 47  GLY   C N     1 
ATOM   4340 C  CA    . GLY   D 2 48  ? 21.21400  52.67200  59.13900  1.000 26.18700 ? 47  GLY   C CA    1 
ATOM   4341 C  C     . GLY   D 2 48  ? 19.76800  52.24600  59.05900  1.000 28.78519 ? 47  GLY   C C     1 
ATOM   4342 O  O     . GLY   D 2 48  ? 19.14800  52.27900  58.00000  1.000 27.14330 ? 47  GLY   C O     1 
ATOM   4343 N  N     . TYR   D 2 49  ? 19.24600  51.85800  60.21800  1.000 28.04804 ? 48  TYR   C N     1 
ATOM   4344 C  CA    . TYR   D 2 49  ? 17.97400  51.15300  60.29300  1.000 25.30015 ? 48  TYR   C CA    1 
ATOM   4345 C  C     . TYR   D 2 49  ? 16.76500  52.06500  60.13000  1.000 25.91337 ? 48  TYR   C C     1 
ATOM   4346 O  O     . TYR   D 2 49  ? 15.67800  51.56700  59.82700  1.000 24.14657 ? 48  TYR   C O     1 
ATOM   4347 C  CB    . TYR   D 2 49  ? 17.87300  50.47900  61.65100  1.000 26.22014 ? 48  TYR   C CB    1 
ATOM   4348 C  CG    . TYR   D 2 49  ? 18.82300  49.33600  61.86200  1.000 23.68708 ? 48  TYR   C CG    1 
ATOM   4349 C  CD1   . TYR   D 2 49  ? 19.00700  48.35500  60.87600  1.000 24.40065 ? 48  TYR   C CD1   1 
ATOM   4350 C  CD2   . TYR   D 2 49  ? 19.54400  49.23200  63.05100  1.000 23.14100 ? 48  TYR   C CD2   1 
ATOM   4351 C  CE1   . TYR   D 2 49  ? 19.86200  47.28100  61.08100  1.000 23.39779 ? 48  TYR   C CE1   1 
ATOM   4352 C  CE2   . TYR   D 2 49  ? 20.41700  48.15500  63.26200  1.000 23.62961 ? 48  TYR   C CE2   1 
ATOM   4353 C  CZ    . TYR   D 2 49  ? 20.57700  47.19400  62.25700  1.000 22.31135 ? 48  TYR   C CZ    1 
ATOM   4354 O  OH    . TYR   D 2 49  ? 21.43400  46.12600  62.45300  1.000 22.92076 ? 48  TYR   C OH    1 
ATOM   4355 N  N     . LYS   D 2 50  ? 16.90500  53.36900  60.35200  1.000 26.64416 ? 49  LYS   C N     1 
ATOM   4356 C  CA    . LYS   D 2 50  ? 15.73300  54.23400  60.38300  1.000 23.08488 ? 49  LYS   C CA    1 
ATOM   4357 C  C     . LYS   D 2 50  ? 15.02500  54.20800  59.03500  1.000 24.08566 ? 49  LYS   C C     1 
ATOM   4358 O  O     . LYS   D 2 50  ? 15.63800  54.50400  58.00500  1.000 26.91324 ? 49  LYS   C O     1 
ATOM   4359 C  CB    . LYS   D 2 50  ? 16.15600  55.65700  60.74700  1.000 26.53348 ? 49  LYS   C CB    1 
ATOM   4360 C  CG    . LYS   D 2 50  ? 15.02200  56.65300  60.79900  1.000 29.19209 ? 49  LYS   C CG    1 
ATOM   4361 C  CD    . LYS   D 2 50  ? 15.55900  58.08300  60.93200  1.000 43.54275 ? 49  LYS   C CD    1 
ATOM   4362 C  CE    . LYS   D 2 50  ? 14.78400  58.86200  61.96500  1.000 41.51458 ? 49  LYS   C CE    1 
ATOM   4363 N  NZ    . LYS   D 2 50  ? 13.33100  58.92000  61.60700  1.000 44.65439 ? 49  LYS   C NZ    1 
ATOM   4364 N  N     . GLY   D 2 51  ? 13.73300  53.84900  59.05500  1.000 23.26160 ? 50  GLY   C N     1 
ATOM   4365 C  CA    . GLY   D 2 51  ? 12.90600  53.71300  57.87200  1.000 22.76987 ? 50  GLY   C CA    1 
ATOM   4366 C  C     . GLY   D 2 51  ? 12.75100  52.28400  57.38700  1.000 20.53006 ? 50  GLY   C C     1 
ATOM   4367 O  O     . GLY   D 2 51  ? 11.79000  51.98200  56.66200  1.000 23.95060 ? 50  GLY   C O     1 
ATOM   4368 N  N     . SER   D 2 52  ? 13.64700  51.39100  57.78300  1.000 22.14296 ? 51  SER   C N     1 
ATOM   4369 C  CA    . SER   D 2 52  ? 13.60200  50.02700  57.29600  1.000 23.87289 ? 51  SER   C CA    1 
ATOM   4370 C  C     . SER   D 2 52  ? 12.49500  49.23800  57.98200  1.000 22.47607 ? 51  SER   C C     1 
ATOM   4371 O  O     . SER   D 2 52  ? 11.93000  49.64200  59.00100  1.000 22.72500 ? 51  SER   C O     1 
ATOM   4372 C  CB    . SER   D 2 52  ? 14.96300  49.34500  57.42100  1.000 24.42411 ? 51  SER   C CB    1 
ATOM   4373 O  OG    . SER   D 2 52  ? 15.34500  49.19000  58.76400  1.000 23.20680 ? 51  SER   C OG    1 
ATOM   4374 N  N     . CYS   D 2 53  ? 12.20700  48.07700  57.42400  1.000 22.99962 ? 52  CYS   C N     1 
ATOM   4375 C  CA    . CYS   D 2 53  ? 11.06400  47.31400  57.89900  1.000 21.35852 ? 52  CYS   C CA    1 
ATOM   4376 C  C     . CYS   D 2 53  ? 11.49100  45.98600  58.49800  1.000 17.65916 ? 52  CYS   C C     1 
ATOM   4377 O  O     . CYS   D 2 53  ? 12.60900  45.50900  58.28800  1.000 21.00990 ? 52  CYS   C O     1 
ATOM   4378 C  CB    . CYS   D 2 53  ? 10.06400  47.04900  56.76200  1.000 23.30736 ? 52  CYS   C CB    1 
ATOM   4379 S  SG    . CYS   D 2 53  ? 10.41500  45.63300  55.67500  1.000 26.39953 ? 52  CYS   C SG    1 
ATOM   4380 N  N     . PHE   D 2 54  ? 10.56800  45.40100  59.24800  1.000 17.80576 ? 53  PHE   C N     1 
ATOM   4381 C  CA    . PHE   D 2 54  ? 10.68500  44.00600  59.65600  1.000 17.47529 ? 53  PHE   C CA    1 
ATOM   4382 C  C     . PHE   D 2 54  ? 10.05100  43.17800  58.55300  1.000 18.26201 ? 53  PHE   C C     1 
ATOM   4383 O  O     . PHE   D 2 54  ? 8.81900   43.08700  58.44200  1.000 21.94449 ? 53  PHE   C O     1 
ATOM   4384 C  CB    . PHE   D 2 54  ? 9.99800   43.79800  61.00500  1.000 16.12916 ? 53  PHE   C CB    1 
ATOM   4385 C  CG    . PHE   D 2 54  ? 10.85200  44.23200  62.17300  1.000 16.72960 ? 53  PHE   C CG    1 
ATOM   4386 C  CD1   . PHE   D 2 54  ? 10.92300  45.57800  62.55200  1.000 18.98537 ? 53  PHE   C CD1   1 
ATOM   4387 C  CD2   . PHE   D 2 54  ? 11.62300  43.29200  62.86400  1.000 17.56549 ? 53  PHE   C CD2   1 
ATOM   4388 C  CE1   . PHE   D 2 54  ? 11.75200  45.95400  63.65000  1.000 21.40440 ? 53  PHE   C CE1   1 
ATOM   4389 C  CE2   . PHE   D 2 54  ? 12.42200  43.66900  63.93300  1.000 20.54474 ? 53  PHE   C CE2   1 
ATOM   4390 C  CZ    . PHE   D 2 54  ? 12.47500  44.99200  64.33300  1.000 19.28096 ? 53  PHE   C CZ    1 
ATOM   4391 N  N     . HIS   D 2 55  ? 10.89600  42.61600  57.68800  1.000 17.47634 ? 54  HIS   C N     1 
ATOM   4392 C  CA    . HIS   D 2 55  ? 10.39000  41.96300  56.48800  1.000 18.31964 ? 54  HIS   C CA    1 
ATOM   4393 C  C     . HIS   D 2 55  ? 9.91200   40.54000  56.73700  1.000 19.25264 ? 54  HIS   C C     1 
ATOM   4394 O  O     . HIS   D 2 55  ? 9.13600   40.02000  55.93400  1.000 21.38490 ? 54  HIS   C O     1 
ATOM   4395 C  CB    . HIS   D 2 55  ? 11.45900  41.98000  55.38400  1.000 19.24774 ? 54  HIS   C CB    1 
ATOM   4396 C  CG    . HIS   D 2 55  ? 12.70700  41.22500  55.73200  1.000 18.30535 ? 54  HIS   C CG    1 
ATOM   4397 N  ND1   . HIS   D 2 55  ? 13.73500  41.77700  56.46100  1.000 20.14842 ? 54  HIS   C ND1   1 
ATOM   4398 C  CD2   . HIS   D 2 55  ? 13.10900  39.97200  55.40400  1.000 20.04824 ? 54  HIS   C CD2   1 
ATOM   4399 C  CE1   . HIS   D 2 55  ? 14.70500  40.89100  56.59200  1.000 21.38446 ? 54  HIS   C CE1   1 
ATOM   4400 N  NE2   . HIS   D 2 55  ? 14.35900  39.79800  55.94700  1.000 20.90890 ? 54  HIS   C NE2   1 
ATOM   4401 N  N     . ARG   D 2 56  ? 10.31800  39.91400  57.84200  1.000 15.96009 ? 55  ARG   C N     1 
ATOM   4402 C  CA    . ARG   D 2 56  ? 9.99700   38.50600  58.07100  1.000 16.97717 ? 55  ARG   C CA    1 
ATOM   4403 C  C     . ARG   D 2 56  ? 9.62500   38.35600  59.53500  1.000 16.91057 ? 55  ARG   C C     1 
ATOM   4404 O  O     . ARG   D 2 56  ? 10.50400  38.39900  60.39500  1.000 18.45291 ? 55  ARG   C O     1 
ATOM   4405 C  CB    . ARG   D 2 56  ? 11.19400  37.62000  57.71300  1.000 17.45878 ? 55  ARG   C CB    1 
ATOM   4406 C  CG    . ARG   D 2 56  ? 10.85600  36.10800  57.70000  1.000 18.81701 ? 55  ARG   C CG    1 
ATOM   4407 C  CD    . ARG   D 2 56  ? 12.08300  35.23700  57.47500  1.000 18.65054 ? 55  ARG   C CD    1 
ATOM   4408 N  NE    . ARG   D 2 56  ? 12.67300  35.49900  56.16800  1.000 20.80107 ? 55  ARG   C NE    1 
ATOM   4409 C  CZ    . ARG   D 2 56  ? 13.92100  35.21500  55.84800  1.000 22.53428 ? 55  ARG   C CZ    1 
ATOM   4410 N  NH1   . ARG   D 2 56  ? 14.73200  34.63600  56.71100  1.000 23.74409 ? 55  ARG   C NH1   1 
ATOM   4411 N  NH2   . ARG   D 2 56  ? 14.35700  35.49400  54.61500  1.000 29.17028 ? 55  ARG   C NH2   1 
ATOM   4412 N  N     . ILE   D 2 57  ? 8.34500   38.14600  59.80800  1.000 15.65663 ? 56  ILE   C N     1 
ATOM   4413 C  CA    . ILE   D 2 57  ? 7.81800   37.97100  61.16500  1.000 15.79483 ? 56  ILE   C CA    1 
ATOM   4414 C  C     . ILE   D 2 57  ? 7.09600   36.62800  61.21200  1.000 16.19656 ? 56  ILE   C C     1 
ATOM   4415 O  O     . ILE   D 2 57  ? 6.06300   36.45100  60.56500  1.000 17.01578 ? 56  ILE   C O     1 
ATOM   4416 C  CB    . ILE   D 2 57  ? 6.87800   39.11300  61.55500  1.000 17.44099 ? 56  ILE   C CB    1 
ATOM   4417 C  CG1   . ILE   D 2 57  ? 7.65700   40.45900  61.55200  1.000 18.08859 ? 56  ILE   C CG1   1 
ATOM   4418 C  CG2   . ILE   D 2 57  ? 6.19600   38.85200  62.93900  1.000 19.13805 ? 56  ILE   C CG2   1 
ATOM   4419 C  CD1   . ILE   D 2 57  ? 6.81000   41.64000  61.94100  1.000 21.44308 ? 56  ILE   C CD1   1 
ATOM   4420 N  N     . ILE   D 2 58  ? 7.64900   35.67600  61.95900  1.000 16.45162 ? 57  ILE   C N     1 
ATOM   4421 C  CA    . ILE   D 2 58  ? 7.06500   34.33400  62.00600  1.000 17.43174 ? 57  ILE   C CA    1 
ATOM   4422 C  C     . ILE   D 2 58  ? 6.61600   34.05500  63.43500  1.000 18.82598 ? 57  ILE   C C     1 
ATOM   4423 O  O     . ILE   D 2 58  ? 7.47200   33.87500  64.31800  1.000 18.31815 ? 57  ILE   C O     1 
ATOM   4424 C  CB    . ILE   D 2 58  ? 8.01800   33.25500  61.48200  1.000 17.00980 ? 57  ILE   C CB    1 
ATOM   4425 C  CG1   . ILE   D 2 58  ? 8.39000   33.58600  60.03300  1.000 18.08521 ? 57  ILE   C CG1   1 
ATOM   4426 C  CG2   . ILE   D 2 58  ? 7.29400   31.93800  61.52400  1.000 21.12526 ? 57  ILE   C CG2   1 
ATOM   4427 C  CD1   . ILE   D 2 58  ? 9.18500   32.48900  59.36000  1.000 19.12664 ? 57  ILE   C CD1   1 
ATOM   4428 N  N     . PRO   D 2 59  ? 5.31300   34.04400  63.70400  1.000 20.08474 ? 58  PRO   C N     1 
ATOM   4429 C  CA    . PRO   D 2 59  ? 4.82600   33.86400  65.07500  1.000 21.18158 ? 58  PRO   C CA    1 
ATOM   4430 C  C     . PRO   D 2 59  ? 5.35100   32.58600  65.70500  1.000 22.06972 ? 58  PRO   C C     1 
ATOM   4431 O  O     . PRO   D 2 59  ? 5.39300   31.51400  65.08100  1.000 22.78957 ? 58  PRO   C O     1 
ATOM   4432 C  CB    . PRO   D 2 59  ? 3.29800   33.82200  64.90200  1.000 21.07464 ? 58  PRO   C CB    1 
ATOM   4433 C  CG    . PRO   D 2 59  ? 3.04500   34.65200  63.70400  1.000 21.06413 ? 58  PRO   C CG    1 
ATOM   4434 C  CD    . PRO   D 2 59  ? 4.20000   34.28000  62.77100  1.000 19.99918 ? 58  PRO   C CD    1 
ATOM   4435 N  N     . GLY   D 2 60  ? 5.79400   32.72100  66.95300  1.000 21.92328 ? 59  GLY   C N     1 
ATOM   4436 C  CA    . GLY   D 2 60  ? 6.40300   31.64300  67.68200  1.000 20.80441 ? 59  GLY   C CA    1 
ATOM   4437 C  C     . GLY   D 2 60  ? 7.88400   31.51100  67.47800  1.000 19.67723 ? 59  GLY   C C     1 
ATOM   4438 O  O     . GLY   D 2 60  ? 8.50800   30.63000  68.08800  1.000 22.85498 ? 59  GLY   C O     1 
ATOM   4439 N  N     . PHE   D 2 61  ? 8.47200   32.33500  66.60300  1.000 18.39716 ? 60  PHE   C N     1 
ATOM   4440 C  CA    . PHE   D 2 61  ? 9.90400   32.21400  66.34700  1.000 18.06155 ? 60  PHE   C CA    1 
ATOM   4441 C  C     . PHE   D 2 61  ? 10.64200  33.54600  66.48500  1.000 17.74263 ? 60  PHE   C C     1 
ATOM   4442 O  O     . PHE   D 2 61  ? 11.43000  33.73600  67.41900  1.000 17.91771 ? 60  PHE   C O     1 
ATOM   4443 C  CB    . PHE   D 2 61  ? 10.15100  31.58000  64.96100  1.000 17.98066 ? 60  PHE   C CB    1 
ATOM   4444 C  CG    . PHE   D 2 61  ? 9.72000   30.14000  64.86400  1.000 14.41587 ? 60  PHE   C CG    1 
ATOM   4445 C  CD1   . PHE   D 2 61  ? 10.58300  29.13400  65.26000  1.000 19.82284 ? 60  PHE   C CD1   1 
ATOM   4446 C  CD2   . PHE   D 2 61  ? 8.46600   29.78500  64.38200  1.000 17.97966 ? 60  PHE   C CD2   1 
ATOM   4447 C  CE1   . PHE   D 2 61  ? 10.22500  27.81500  65.17100  1.000 19.89854 ? 60  PHE   C CE1   1 
ATOM   4448 C  CE2   . PHE   D 2 61  ? 8.10800   28.44000  64.31700  1.000 21.06307 ? 60  PHE   C CE2   1 
ATOM   4449 C  CZ    . PHE   D 2 61  ? 9.00100   27.48500  64.68500  1.000 18.74338 ? 60  PHE   C CZ    1 
ATOM   4450 N  N     . MET   D 2 62  ? 10.44400  34.47400  65.55500  1.000 16.00241 ? 61  MET   C N     1 
ATOM   4451 C  CA    . MET   D 2 62  ? 11.25400  35.69000  65.59000  1.000 16.18814 ? 61  MET   C CA    1 
ATOM   4452 C  C     . MET   D 2 62  ? 10.64300  36.76100  64.70900  1.000 16.09653 ? 61  MET   C C     1 
ATOM   4453 O  O     . MET   D 2 62  ? 9.80400   36.49100  63.84400  1.000 17.15013 ? 61  MET   C O     1 
ATOM   4454 C  CB    . MET   D 2 62  ? 12.69400  35.42200  65.12000  1.000 16.71970 ? 61  MET   C CB    1 
ATOM   4455 C  CG    . MET   D 2 62  ? 12.93900  35.49800  63.59300  1.000 20.78448 ? 61  MET   C CG    1 
ATOM   4456 S  SD    . MET   D 2 62  ? 12.10200  34.14200  62.69600  1.000 19.47082 ? 61  MET   C SD    1 
ATOM   4457 C  CE    . MET   D 2 62  ? 11.91500  34.97100  61.10900  1.000 20.37420 ? 61  MET   C CE    1 
ATOM   4458 N  N     . CYS   D 2 63  ? 11.12500  37.97300  64.92600  1.000 15.47401 ? 62  CYS   C N     1 
ATOM   4459 C  CA    . CYS   D 2 63  ? 10.93300  39.12400  64.04500  1.000 15.63075 ? 62  CYS   C CA    1 
ATOM   4460 C  C     . CYS   D 2 63  ? 12.28700  39.49700  63.46200  1.000 16.13217 ? 62  CYS   C C     1 
ATOM   4461 O  O     . CYS   D 2 63  ? 13.22000  39.80500  64.21100  1.000 17.24685 ? 62  CYS   C O     1 
ATOM   4462 C  CB    . CYS   D 2 63  ? 10.37900  40.30400  64.84200  1.000 17.82321 ? 62  CYS   C CB    1 
ATOM   4463 S  SG    . CYS   D 2 63  ? 8.78500   40.01500  65.66000  1.000 20.52894 ? 62  CYS   C SG    1 
ATOM   4464 N  N     . GLN   D 2 64  ? 12.39700  39.51800  62.13500  1.000 16.01991 ? 63  GLN   C N     1 
ATOM   4465 C  CA    . GLN   D 2 64  ? 13.65700  39.77700  61.44700  1.000 13.97347 ? 63  GLN   C CA    1 
ATOM   4466 C  C     . GLN   D 2 64  ? 13.56300  41.05900  60.63000  1.000 15.99273 ? 63  GLN   C C     1 
ATOM   4467 O  O     . GLN   D 2 64  ? 12.54600  41.29900  59.97100  1.000 17.82950 ? 63  GLN   C O     1 
ATOM   4468 C  CB    . GLN   D 2 64  ? 14.06400  38.56100  60.57200  1.000 17.12356 ? 63  GLN   C CB    1 
ATOM   4469 C  CG    . GLN   D 2 64  ? 15.33700  38.72600  59.78600  1.000 15.63971 ? 63  GLN   C CG    1 
ATOM   4470 C  CD    . GLN   D 2 64  ? 15.71400  37.49400  59.01200  1.000 17.67346 ? 63  GLN   C CD    1 
ATOM   4471 O  OE1   . GLN   D 2 64  ? 15.20300  36.41600  59.30300  1.000 19.70483 ? 63  GLN   C OE1   1 
ATOM   4472 N  NE2   . GLN   D 2 64  ? 16.61000  37.63300  58.03600  1.000 19.01106 ? 63  GLN   C NE2   1 
ATOM   4473 N  N     . GLY   D 2 65  ? 14.61400  41.87700  60.69800  1.000 15.98019 ? 64  GLY   C N     1 
ATOM   4474 C  CA    . GLY   D 2 65  ? 14.67600  43.13900  59.98800  1.000 18.41984 ? 64  GLY   C CA    1 
ATOM   4475 C  C     . GLY   D 2 65  ? 16.08500  43.49000  59.56200  1.000 20.44616 ? 64  GLY   C C     1 
ATOM   4476 O  O     . GLY   D 2 65  ? 16.97600  42.63400  59.58000  1.000 18.94908 ? 64  GLY   C O     1 
ATOM   4477 N  N     . GLY   D 2 66  ? 16.28700  44.73200  59.14000  1.000 20.84894 ? 65  GLY   C N     1 
ATOM   4478 C  CA    . GLY   D 2 66  ? 17.62400  45.25300  58.95600  1.000 21.55594 ? 65  GLY   C CA    1 
ATOM   4479 C  C     . GLY   D 2 66  ? 18.08100  45.46600  57.53100  1.000 23.00588 ? 65  GLY   C C     1 
ATOM   4480 O  O     . GLY   D 2 66  ? 19.23500  45.86600  57.33400  1.000 24.24480 ? 65  GLY   C O     1 
ATOM   4481 N  N     . ASP   D 2 67  ? 17.24200  45.20500  56.52400  1.000 23.24218 ? 66  ASP   C N     1 
ATOM   4482 C  CA    . ASP   D 2 67  ? 17.63600  45.41900  55.12300  1.000 21.12924 ? 66  ASP   C CA    1 
ATOM   4483 C  C     . ASP   D 2 67  ? 17.30300  46.84500  54.73200  1.000 22.96774 ? 66  ASP   C C     1 
ATOM   4484 O  O     . ASP   D 2 67  ? 16.21300  47.13200  54.23800  1.000 25.44024 ? 66  ASP   C O     1 
ATOM   4485 C  CB    . ASP   D 2 67  ? 16.94800  44.44000  54.18400  1.000 22.45822 ? 66  ASP   C CB    1 
ATOM   4486 C  CG    . ASP   D 2 67  ? 17.35500  44.65400  52.72500  1.000 24.93475 ? 66  ASP   C CG    1 
ATOM   4487 O  OD1   . ASP   D 2 67  ? 18.11000  45.61400  52.41800  1.000 28.60992 ? 66  ASP   C OD1   1 
ATOM   4488 O  OD2   . ASP   D 2 67  ? 16.90800  43.88900  51.84600  1.000 26.85985 ? 66  ASP   C OD2   1 
ATOM   4489 N  N     . PHE   D 2 68  ? 18.28000  47.72900  54.85600  1.000 26.25131 ? 67  PHE   C N     1 
ATOM   4490 C  CA    . PHE   D 2 68  ? 18.08200  49.10300  54.45300  1.000 24.23136 ? 67  PHE   C CA    1 
ATOM   4491 C  C     . PHE   D 2 68  ? 18.72700  49.41900  53.11500  1.000 26.61183 ? 67  PHE   C C     1 
ATOM   4492 O  O     . PHE   D 2 68  ? 18.74000  50.59000  52.71000  1.000 28.82589 ? 67  PHE   C O     1 
ATOM   4493 C  CB    . PHE   D 2 68  ? 18.56900  50.06700  55.54400  1.000 26.78020 ? 67  PHE   C CB    1 
ATOM   4494 C  CG    . PHE   D 2 68  ? 20.01900  49.90400  55.91100  1.000 25.90339 ? 67  PHE   C CG    1 
ATOM   4495 C  CD1   . PHE   D 2 68  ? 21.00900  50.52900  55.15400  1.000 27.50779 ? 67  PHE   C CD1   1 
ATOM   4496 C  CD2   . PHE   D 2 68  ? 20.39800  49.16400  57.03300  1.000 30.21321 ? 67  PHE   C CD2   1 
ATOM   4497 C  CE1   . PHE   D 2 68  ? 22.33600  50.39800  55.47800  1.000 29.95748 ? 67  PHE   C CE1   1 
ATOM   4498 C  CE2   . PHE   D 2 68  ? 21.74800  49.03800  57.37000  1.000 31.64071 ? 67  PHE   C CE2   1 
ATOM   4499 C  CZ    . PHE   D 2 68  ? 22.71000  49.65900  56.59000  1.000 29.80772 ? 67  PHE   C CZ    1 
ATOM   4500 N  N     . THR   D 2 69  ? 19.28200  48.42100  52.42300  1.000 26.55678 ? 68  THR   C N     1 
ATOM   4501 C  CA    . THR   D 2 69  ? 19.99200  48.68800  51.17200  1.000 26.27330 ? 68  THR   C CA    1 
ATOM   4502 C  C     . THR   D 2 69  ? 19.24800  48.20200  49.93700  1.000 28.14179 ? 68  THR   C C     1 
ATOM   4503 O  O     . THR   D 2 69  ? 19.28300  48.87500  48.90600  1.000 31.48526 ? 68  THR   C O     1 
ATOM   4504 C  CB    . THR   D 2 69  ? 21.42300  48.12100  51.14500  1.000 32.49885 ? 68  THR   C CB    1 
ATOM   4505 O  OG1   . THR   D 2 69  ? 21.38300  46.69400  51.15700  1.000 30.93019 ? 68  THR   C OG1   1 
ATOM   4506 C  CG2   . THR   D 2 69  ? 22.26200  48.63000  52.31300  1.000 34.33688 ? 68  THR   C CG2   1 
ATOM   4507 N  N     . ARG   D 2 70  ? 18.60100  47.04100  50.00600  1.000 28.65312 ? 69  ARG   C N     1 
ATOM   4508 C  CA    . ARG   D 2 70  ? 17.80800  46.54200  48.89100  1.000 31.04919 ? 69  ARG   C CA    1 
ATOM   4509 C  C     . ARG   D 2 70  ? 16.30900  46.61800  49.14100  1.000 27.76678 ? 69  ARG   C C     1 
ATOM   4510 O  O     . ARG   D 2 70  ? 15.53500  46.50900  48.18300  1.000 31.19740 ? 69  ARG   C O     1 
ATOM   4511 C  CB    . ARG   D 2 70  ? 18.19100  45.09300  48.54900  1.000 27.98676 ? 69  ARG   C CB    1 
ATOM   4512 C  CG    . ARG   D 2 70  ? 19.64800  44.88900  48.17200  1.000 31.35422 ? 69  ARG   C CG    1 
ATOM   4513 C  CD    . ARG   D 2 70  ? 19.89100  43.44400  47.73200  1.000 38.45269 ? 69  ARG   C CD    1 
ATOM   4514 N  NE    . ARG   D 2 70  ? 21.27800  43.17200  47.37300  1.000 49.28140 ? 69  ARG   C NE    1 
ATOM   4515 C  CZ    . ARG   D 2 70  ? 21.82200  41.96200  47.37000  1.000 45.73944 ? 69  ARG   C CZ    1 
ATOM   4516 N  NH1   . ARG   D 2 70  ? 21.13300  40.89600  47.73800  1.000 43.65142 ? 69  ARG   C NH1   1 
ATOM   4517 N  NH2   . ARG   D 2 70  ? 23.08800  41.81800  46.98300  1.000 49.01409 ? 69  ARG   C NH2   1 
ATOM   4518 N  N     . HIS   D 2 71  ? 15.88200  46.78000  50.39500  1.000 27.04904 ? 70  HIS   C N     1 
ATOM   4519 C  CA    . HIS   D 2 71  ? 14.47100  46.90700  50.74500  1.000 30.49599 ? 70  HIS   C CA    1 
ATOM   4520 C  C     . HIS   D 2 71  ? 13.66400  45.69700  50.29100  1.000 32.36225 ? 70  HIS   C C     1 
ATOM   4521 O  O     . HIS   D 2 71  ? 12.48000  45.81300  49.97800  1.000 32.51483 ? 70  HIS   C O     1 
ATOM   4522 C  CB    . HIS   D 2 71  ? 13.86300  48.21100  50.21400  1.000 30.41394 ? 70  HIS   C CB    1 
ATOM   4523 C  CG    . HIS   D 2 71  ? 14.70400  49.41400  50.49300  1.000 26.53305 ? 70  HIS   C CG    1 
ATOM   4524 N  ND1   . HIS   D 2 71  ? 14.68200  50.07200  51.70500  1.000 27.02629 ? 70  HIS   C ND1   1 
ATOM   4525 C  CD2   . HIS   D 2 71  ? 15.61600  50.05700  49.73000  1.000 32.38651 ? 70  HIS   C CD2   1 
ATOM   4526 C  CE1   . HIS   D 2 71  ? 15.53800  51.07600  51.67300  1.000 30.74220 ? 70  HIS   C CE1   1 
ATOM   4527 N  NE2   . HIS   D 2 71  ? 16.11700  51.09200  50.48500  1.000 33.98474 ? 70  HIS   C NE2   1 
ATOM   4528 N  N     . ASN   D 2 72  ? 14.29800  44.52100  50.25600  1.000 28.30523 ? 71  ASN   C N     1 
ATOM   4529 C  CA    . ASN   D 2 72  ? 13.58200  43.34400  49.77700  1.000 27.91593 ? 71  ASN   C CA    1 
ATOM   4530 C  C     . ASN   D 2 72  ? 13.90800  42.10400  50.59600  1.000 27.25837 ? 71  ASN   C C     1 
ATOM   4531 O  O     . ASN   D 2 72  ? 13.64800  40.98500  50.13000  1.000 32.83536 ? 71  ASN   C O     1 
ATOM   4532 C  CB    . ASN   D 2 72  ? 13.82500  43.08700  48.26300  1.000 31.79064 ? 71  ASN   C CB    1 
ATOM   4533 C  CG    . ASN   D 2 72  ? 15.25500  42.70100  47.95400  1.000 30.60805 ? 71  ASN   C CG    1 
ATOM   4534 O  OD1   . ASN   D 2 72  ? 16.01200  42.33900  48.84900  1.000 27.67812 ? 71  ASN   C OD1   1 
ATOM   4535 N  ND2   . ASN   D 2 72  ? 15.63400  42.76900  46.68400  1.000 35.23609 ? 71  ASN   C ND2   1 
ATOM   4536 N  N     . GLY   D 2 73  ? 14.51700  42.27700  51.77500  1.000 23.73952 ? 72  GLY   C N     1 
ATOM   4537 C  CA    . GLY   D 2 73  ? 14.88600  41.19300  52.66900  1.000 25.24924 ? 72  GLY   C CA    1 
ATOM   4538 C  C     . GLY   D 2 73  ? 16.19300  40.48900  52.34500  1.000 23.74791 ? 72  GLY   C C     1 
ATOM   4539 O  O     . GLY   D 2 73  ? 16.58100  39.57200  53.08900  1.000 25.62725 ? 72  GLY   C O     1 
ATOM   4540 N  N     . THR   D 2 74  ? 16.88700  40.87800  51.27900  1.000 24.20843 ? 73  THR   C N     1 
ATOM   4541 C  CA    . THR   D 2 74  ? 18.10300  40.19600  50.86300  1.000 26.17741 ? 73  THR   C CA    1 
ATOM   4542 C  C     . THR   D 2 74  ? 19.34500  41.03700  51.10300  1.000 27.42585 ? 73  THR   C C     1 
ATOM   4543 O  O     . THR   D 2 74  ? 20.45600  40.53700  50.94000  1.000 29.11899 ? 73  THR   C O     1 
ATOM   4544 C  CB    . THR   D 2 74  ? 18.01300  39.73400  49.40900  1.000 33.54909 ? 73  THR   C CB    1 
ATOM   4545 O  OG1   . THR   D 2 74  ? 18.14200  40.85800  48.53400  1.000 28.96766 ? 73  THR   C OG1   1 
ATOM   4546 C  CG2   . THR   D 2 74  ? 16.66300  39.04600  49.16600  1.000 35.68633 ? 73  THR   C CG2   1 
ATOM   4547 N  N     . GLY   D 2 75  ? 19.18000  42.28700  51.50500  1.000 25.41708 ? 74  GLY   C N     1 
ATOM   4548 C  CA    . GLY   D 2 75  ? 20.30200  43.20200  51.55100  1.000 26.08647 ? 74  GLY   C CA    1 
ATOM   4549 C  C     . GLY   D 2 75  ? 20.76700  43.52900  52.95500  1.000 28.16229 ? 74  GLY   C C     1 
ATOM   4550 O  O     . GLY   D 2 75  ? 20.57100  42.75000  53.87600  1.000 23.92895 ? 74  GLY   C O     1 
ATOM   4551 N  N     . GLY   D 2 76  ? 21.38200  44.69000  53.13200  1.000 32.33002 ? 75  GLY   C N     1 
ATOM   4552 C  CA    . GLY   D 2 76  ? 22.00900  45.01000  54.39200  1.000 31.41720 ? 75  GLY   C CA    1 
ATOM   4553 C  C     . GLY   D 2 76  ? 23.50300  45.19900  54.26400  1.000 31.82723 ? 75  GLY   C C     1 
ATOM   4554 O  O     . GLY   D 2 76  ? 24.16300  44.67600  53.35300  1.000 32.69829 ? 75  GLY   C O     1 
ATOM   4555 N  N     . LYS   D 2 77  ? 24.04600  45.99600  55.17300  1.000 27.55424 ? 76  LYS   C N     1 
ATOM   4556 C  CA    . LYS   D 2 77  ? 25.46900  46.25500  55.17400  1.000 30.06281 ? 76  LYS   C CA    1 
ATOM   4557 C  C     . LYS   D 2 77  ? 25.87000  46.70300  56.57300  1.000 26.43785 ? 76  LYS   C C     1 
ATOM   4558 O  O     . LYS   D 2 77  ? 25.10400  47.36900  57.26500  1.000 26.68415 ? 76  LYS   C O     1 
ATOM   4559 C  CB    . LYS   D 2 77  ? 25.87500  47.25200  54.08700  1.000 34.51919 ? 76  LYS   C CB    1 
ATOM   4560 C  CG    . LYS   D 2 77  ? 25.60800  48.72700  54.36100  1.000 32.91144 ? 76  LYS   C CG    1 
ATOM   4561 C  CD    . LYS   D 2 77  ? 26.14600  49.56400  53.20100  1.000 35.44333 ? 76  LYS   C CD    1 
ATOM   4562 C  CE    . LYS   D 2 77  ? 25.86700  51.04200  53.39600  1.000 39.24544 ? 76  LYS   C CE    1 
ATOM   4563 N  NZ    . LYS   D 2 77  ? 26.48100  51.87600  52.30800  1.000 36.18686 ? 76  LYS   C NZ    1 
ATOM   4564 N  N     . SER   D 2 78  ? 27.09200  46.35400  56.95500  1.000 27.39791 ? 77  SER   C N     1 
ATOM   4565 C  CA    . SER   D 2 78  ? 27.63200  46.71900  58.25700  1.000 27.68915 ? 77  SER   C CA    1 
ATOM   4566 C  C     . SER   D 2 78  ? 28.30500  48.09600  58.18900  1.000 32.57374 ? 77  SER   C C     1 
ATOM   4567 O  O     . SER   D 2 78  ? 28.39600  48.72400  57.12900  1.000 35.36395 ? 77  SER   C O     1 
ATOM   4568 C  CB    . SER   D 2 78  ? 28.63700  45.66200  58.69600  1.000 31.90987 ? 77  SER   C CB    1 
ATOM   4569 O  OG    . SER   D 2 78  ? 29.86200  45.86000  58.00400  1.000 34.01382 ? 77  SER   C OG    1 
ATOM   4570 N  N     . ILE   D 2 79  ? 28.81200  48.57100  59.33300  1.000 28.15316 ? 78  ILE   C N     1 
ATOM   4571 C  CA    . ILE   D 2 79  ? 29.61200  49.79300  59.35400  1.000 33.64612 ? 78  ILE   C CA    1 
ATOM   4572 C  C     . ILE   D 2 79  ? 31.06600  49.53600  58.99900  1.000 32.24832 ? 78  ILE   C C     1 
ATOM   4573 O  O     . ILE   D 2 79  ? 31.87400  50.47400  58.99900  1.000 41.51302 ? 78  ILE   C O     1 
ATOM   4574 C  CB    . ILE   D 2 79  ? 29.53300  50.46400  60.74100  1.000 34.57252 ? 78  ILE   C CB    1 
ATOM   4575 C  CG1   . ILE   D 2 79  ? 30.21800  49.57700  61.78400  1.000 32.62705 ? 78  ILE   C CG1   1 
ATOM   4576 C  CG2   . ILE   D 2 79  ? 28.08900  50.77600  61.09100  1.000 33.38230 ? 78  ILE   C CG2   1 
ATOM   4577 C  CD1   . ILE   D 2 79  ? 30.37800  50.21900  63.18000  1.000 33.97577 ? 78  ILE   C CD1   1 
ATOM   4578 N  N     . TYR   D 2 80  ? 31.44000  48.28900  58.74100  1.000 35.28636 ? 79  TYR   C N     1 
ATOM   4579 C  CA    . TYR   D 2 80  ? 32.83900  47.94200  58.54200  1.000 34.90329 ? 79  TYR   C CA    1 
ATOM   4580 C  C     . TYR   D 2 80  ? 33.20400  47.86200  57.07000  1.000 45.39513 ? 79  TYR   C C     1 
ATOM   4581 O  O     . TYR   D 2 80  ? 34.20400  47.22600  56.71600  1.000 44.81399 ? 79  TYR   C O     1 
ATOM   4582 C  CB    . TYR   D 2 80  ? 33.18000  46.65500  59.29500  1.000 36.90724 ? 79  TYR   C CB    1 
ATOM   4583 C  CG    . TYR   D 2 80  ? 32.89000  46.76400  60.79000  1.000 33.28415 ? 79  TYR   C CG    1 
ATOM   4584 C  CD1   . TYR   D 2 80  ? 33.62400  47.63200  61.59800  1.000 34.79266 ? 79  TYR   C CD1   1 
ATOM   4585 C  CD2   . TYR   D 2 80  ? 31.87000  46.02700  61.38700  1.000 31.91049 ? 79  TYR   C CD2   1 
ATOM   4586 C  CE1   . TYR   D 2 80  ? 33.34700  47.74700  62.95500  1.000 30.73732 ? 79  TYR   C CE1   1 
ATOM   4587 C  CE2   . TYR   D 2 80  ? 31.59600  46.14000  62.74900  1.000 33.41733 ? 79  TYR   C CE2   1 
ATOM   4588 C  CZ    . TYR   D 2 80  ? 32.34300  46.99900  63.51700  1.000 33.76339 ? 79  TYR   C CZ    1 
ATOM   4589 O  OH    . TYR   D 2 80  ? 32.09100  47.13100  64.86000  1.000 31.87450 ? 79  TYR   C OH    1 
ATOM   4590 N  N     . GLY   D 2 81  ? 32.40900  48.50100  56.20800  1.000 39.84223 ? 80  GLY   C N     1 
ATOM   4591 C  CA    . GLY   D 2 81  ? 32.68000  48.53400  54.78300  1.000 44.33038 ? 80  GLY   C CA    1 
ATOM   4592 C  C     . GLY   D 2 81  ? 32.59100  47.19800  54.09300  1.000 43.22069 ? 80  GLY   C C     1 
ATOM   4593 O  O     . GLY   D 2 81  ? 32.87900  47.11200  52.90000  1.000 44.77961 ? 80  GLY   C O     1 
ATOM   4594 N  N     . GLU   D 2 82  ? 32.19000  46.15400  54.80800  1.000 40.16747 ? 81  GLU   C N     1 
ATOM   4595 C  CA    . GLU   D 2 82  ? 32.11300  44.80400  54.26800  1.000 44.23384 ? 81  GLU   C CA    1 
ATOM   4596 C  C     . GLU   D 2 82  ? 31.33000  43.98200  55.27700  1.000 37.88148 ? 81  GLU   C C     1 
ATOM   4597 O  O     . GLU   D 2 82  ? 31.08600  44.42800  56.40300  1.000 44.66499 ? 81  GLU   C O     1 
ATOM   4598 C  CB    . GLU   D 2 82  ? 33.51100  44.21300  54.09700  1.000 40.91801 ? 81  GLU   C CB    1 
ATOM   4599 C  CG    . GLU   D 2 82  ? 34.31600  44.19300  55.39900  1.000 47.93338 ? 81  GLU   C CG    1 
ATOM   4600 C  CD    . GLU   D 2 82  ? 35.81400  44.27600  55.16200  1.000 54.15306 ? 81  GLU   C CD    1 
ATOM   4601 O  OE1   . GLU   D 2 82  ? 36.23400  44.68000  54.05400  1.000 56.14602 ? 81  GLU   C OE1   1 
ATOM   4602 O  OE2   . GLU   D 2 82  ? 36.57600  43.93400  56.09100  1.000 61.38020 ? 81  GLU   C OE2   1 
ATOM   4603 N  N     . LYS   D 2 83  ? 30.93000  42.78100  54.86000  1.000 37.08226 ? 82  LYS   C N     1 
ATOM   4604 C  CA    . LYS   D 2 83  ? 30.40200  41.81500  55.81300  1.000 30.40346 ? 82  LYS   C CA    1 
ATOM   4605 C  C     . LYS   D 2 83  ? 31.50000  41.45200  56.80100  1.000 27.96766 ? 82  LYS   C C     1 
ATOM   4606 O  O     . LYS   D 2 83  ? 32.68700  41.50100  56.47600  1.000 32.54044 ? 82  LYS   C O     1 
ATOM   4607 C  CB    . LYS   D 2 83  ? 29.91800  40.55300  55.09800  1.000 32.96820 ? 82  LYS   C CB    1 
ATOM   4608 C  CG    . LYS   D 2 83  ? 28.70000  40.76800  54.19400  1.000 35.65033 ? 82  LYS   C CG    1 
ATOM   4609 C  CD    . LYS   D 2 83  ? 27.39900  40.95500  54.96400  1.000 39.43837 ? 82  LYS   C CD    1 
ATOM   4610 C  CE    . LYS   D 2 83  ? 26.19500  41.12800  54.02700  1.000 39.62832 ? 82  LYS   C CE    1 
ATOM   4611 N  NZ    . LYS   D 2 83  ? 26.22700  42.42500  53.32100  1.000 48.45640 ? 82  LYS   C NZ    1 
ATOM   4612 N  N     . PHE   D 2 84  ? 31.11500  41.09400  58.02400  1.000 26.78827 ? 83  PHE   C N     1 
ATOM   4613 C  CA    . PHE   D 2 84  ? 32.13400  40.87500  59.04200  1.000 28.44545 ? 83  PHE   C CA    1 
ATOM   4614 C  C     . PHE   D 2 84  ? 32.02900  39.49800  59.70100  1.000 26.74894 ? 83  PHE   C C     1 
ATOM   4615 O  O     . PHE   D 2 84  ? 31.00100  38.81100  59.64600  1.000 25.41740 ? 83  PHE   C O     1 
ATOM   4616 C  CB    . PHE   D 2 84  ? 32.23000  42.04000  60.04500  1.000 33.48602 ? 83  PHE   C CB    1 
ATOM   4617 C  CG    . PHE   D 2 84  ? 31.02500  42.21800  60.92900  1.000 29.65632 ? 83  PHE   C CG    1 
ATOM   4618 C  CD1   . PHE   D 2 84  ? 29.89600  42.86700  60.44900  1.000 30.34905 ? 83  PHE   C CD1   1 
ATOM   4619 C  CD2   . PHE   D 2 84  ? 31.03800  41.78100  62.25500  1.000 27.72086 ? 83  PHE   C CD2   1 
ATOM   4620 C  CE1   . PHE   D 2 84  ? 28.78900  43.05700  61.24400  1.000 27.93891 ? 83  PHE   C CE1   1 
ATOM   4621 C  CE2   . PHE   D 2 84  ? 29.94200  41.95500  63.08200  1.000 25.62849 ? 83  PHE   C CE2   1 
ATOM   4622 C  CZ    . PHE   D 2 84  ? 28.79700  42.59500  62.58400  1.000 26.87106 ? 83  PHE   C CZ    1 
ATOM   4623 N  N     . GLU   D 2 85  ? 33.13900  39.11100  60.32300  1.000 30.69183 ? 84  GLU   C N     1 
ATOM   4624 C  CA    . GLU   D 2 85  ? 33.31000  37.78700  60.90600  1.000 28.69728 ? 84  GLU   C CA    1 
ATOM   4625 C  C     . GLU   D 2 85  ? 32.35100  37.57000  62.07500  1.000 27.42670 ? 84  GLU   C C     1 
ATOM   4626 O  O     . GLU   D 2 85  ? 31.96600  38.51000  62.76000  1.000 27.72115 ? 84  GLU   C O     1 
ATOM   4627 C  CB    . GLU   D 2 85  ? 34.75100  37.69600  61.41400  1.000 32.06201 ? 84  GLU   C CB    1 
ATOM   4628 C  CG    . GLU   D 2 85  ? 35.28800  36.30800  61.71600  1.000 48.34600 ? 84  GLU   C CG    1 
ATOM   4629 C  CD    . GLU   D 2 85  ? 36.79900  36.22800  61.59900  1.000 48.73277 ? 84  GLU   C CD    1 
ATOM   4630 O  OE1   . GLU   D 2 85  ? 37.33000  36.47300  60.49100  1.000 49.29520 ? 84  GLU   C OE1   1 
ATOM   4631 O  OE2   . GLU   D 2 85  ? 37.46100  35.92800  62.61800  1.000 47.51888 ? 84  GLU   C OE2   1 
ATOM   4632 N  N     . ASP   D 2 86  ? 31.96500  36.30800  62.29000  1.000 25.85457 ? 85  ASP   C N     1 
ATOM   4633 C  CA    . ASP   D 2 86  ? 31.32000  35.91200  63.54400  1.000 26.68619 ? 85  ASP   C CA    1 
ATOM   4634 C  C     . ASP   D 2 86  ? 32.30000  36.13300  64.69800  1.000 25.73883 ? 85  ASP   C C     1 
ATOM   4635 O  O     . ASP   D 2 86  ? 33.33200  35.45300  64.79100  1.000 27.98804 ? 85  ASP   C O     1 
ATOM   4636 C  CB    . ASP   D 2 86  ? 30.93900  34.43600  63.47700  1.000 27.22339 ? 85  ASP   C CB    1 
ATOM   4637 C  CG    . ASP   D 2 86  ? 29.87400  34.14000  62.42700  1.000 27.41209 ? 85  ASP   C CG    1 
ATOM   4638 O  OD1   . ASP   D 2 86  ? 28.92300  34.94200  62.30600  1.000 26.52698 ? 85  ASP   C OD1   1 
ATOM   4639 O  OD2   . ASP   D 2 86  ? 29.99100  33.08500  61.73800  1.000 31.70625 ? 85  ASP   C OD2   1 
ATOM   4640 N  N     . GLU   D 2 87  ? 31.96400  37.08400  65.57800  1.000 23.35823 ? 86  GLU   C N     1 
ATOM   4641 C  CA    . GLU   D 2 87  ? 32.88100  37.52400  66.61600  1.000 28.47234 ? 86  GLU   C CA    1 
ATOM   4642 C  C     . GLU   D 2 87  ? 33.13800  36.41000  67.62300  1.000 25.28084 ? 86  GLU   C C     1 
ATOM   4643 O  O     . GLU   D 2 87  ? 34.29000  36.10000  67.95700  1.000 25.79647 ? 86  GLU   C O     1 
ATOM   4644 C  CB    . GLU   D 2 87  ? 32.25000  38.73000  67.31200  1.000 25.21420 ? 86  GLU   C CB    1 
ATOM   4645 C  CG    . GLU   D 2 87  ? 33.16900  39.41300  68.27400  1.000 26.39649 ? 86  GLU   C CG    1 
ATOM   4646 C  CD    . GLU   D 2 87  ? 32.70500  40.80200  68.63600  1.000 23.34474 ? 86  GLU   C CD    1 
ATOM   4647 O  OE1   . GLU   D 2 87  ? 31.54300  41.18600  68.33100  1.000 26.23243 ? 86  GLU   C OE1   1 
ATOM   4648 O  OE2   . GLU   D 2 87  ? 33.54500  41.50800  69.22000  1.000 27.81939 ? 86  GLU   C OE2   1 
ATOM   4649 N  N     . ASN   D 2 88  ? 32.06900  35.83800  68.16200  1.000 24.08768 ? 87  ASN   C N     1 
ATOM   4650 C  CA    . ASN   D 2 88  ? 32.14600  34.66800  69.02400  1.000 24.60468 ? 87  ASN   C CA    1 
ATOM   4651 C  C     . ASN   D 2 88  ? 30.72000  34.14200  69.14000  1.000 21.83099 ? 87  ASN   C C     1 
ATOM   4652 O  O     . ASN   D 2 88  ? 29.76000  34.77700  68.68600  1.000 22.57859 ? 87  ASN   C O     1 
ATOM   4653 C  CB    . ASN   D 2 88  ? 32.75800  34.96700  70.41400  1.000 24.18907 ? 87  ASN   C CB    1 
ATOM   4654 C  CG    . ASN   D 2 88  ? 31.95500  35.97900  71.18900  1.000 24.80946 ? 87  ASN   C CG    1 
ATOM   4655 O  OD1   . ASN   D 2 88  ? 30.77700  35.75000  71.50400  1.000 21.35577 ? 87  ASN   C OD1   1 
ATOM   4656 N  ND2   . ASN   D 2 88  ? 32.56600  37.12400  71.46300  1.000 24.68604 ? 87  ASN   C ND2   1 
ATOM   4657 N  N     . PHE   D 2 89  ? 30.59300  32.97000  69.73500  1.000 23.71569 ? 88  PHE   C N     1 
ATOM   4658 C  CA    . PHE   D 2 89  ? 29.29100  32.41100  70.05900  1.000 24.58687 ? 88  PHE   C CA    1 
ATOM   4659 C  C     . PHE   D 2 89  ? 29.14400  32.19000  71.55700  1.000 24.38746 ? 88  PHE   C C     1 
ATOM   4660 O  O     . PHE   D 2 89  ? 28.54400  31.20200  71.97000  1.000 25.80439 ? 88  PHE   C O     1 
ATOM   4661 C  CB    . PHE   D 2 89  ? 29.03500  31.10700  69.30900  1.000 24.49393 ? 88  PHE   C CB    1 
ATOM   4662 C  CG    . PHE   D 2 89  ? 29.04000  31.26300  67.82200  1.000 24.62793 ? 88  PHE   C CG    1 
ATOM   4663 C  CD1   . PHE   D 2 89  ? 28.01100  31.91900  67.17000  1.000 23.91871 ? 88  PHE   C CD1   1 
ATOM   4664 C  CD2   . PHE   D 2 89  ? 30.09300  30.76200  67.07600  1.000 26.99201 ? 88  PHE   C CD2   1 
ATOM   4665 C  CE1   . PHE   D 2 89  ? 28.01900  32.06700  65.80300  1.000 24.77291 ? 88  PHE   C CE1   1 
ATOM   4666 C  CE2   . PHE   D 2 89  ? 30.11200  30.90900  65.70900  1.000 30.19576 ? 88  PHE   C CE2   1 
ATOM   4667 C  CZ    . PHE   D 2 89  ? 29.07800  31.55900  65.07000  1.000 27.74241 ? 88  PHE   C CZ    1 
ATOM   4668 N  N     . ILE   D 2 90  ? 29.69400  33.09800  72.37000  1.000 22.41854 ? 89  ILE   C N     1 
ATOM   4669 C  CA    . ILE   D 2 90  ? 29.61600  32.93600  73.82500  1.000 20.84130 ? 89  ILE   C CA    1 
ATOM   4670 C  C     . ILE   D 2 90  ? 28.16400  32.92600  74.28300  1.000 22.85431 ? 89  ILE   C C     1 
ATOM   4671 O  O     . ILE   D 2 90  ? 27.77700  32.14100  75.16500  1.000 24.66290 ? 89  ILE   C O     1 
ATOM   4672 C  CB    . ILE   D 2 90  ? 30.42100  34.04000  74.53000  1.000 22.54874 ? 89  ILE   C CB    1 
ATOM   4673 C  CG1   . ILE   D 2 90  ? 31.92900  33.89100  74.28400  1.000 22.84515 ? 89  ILE   C CG1   1 
ATOM   4674 C  CG2   . ILE   D 2 90  ? 30.14600  34.00900  76.05400  1.000 22.46163 ? 89  ILE   C CG2   1 
ATOM   4675 C  CD1   . ILE   D 2 90  ? 32.67100  35.17600  74.56800  1.000 30.86552 ? 89  ILE   C CD1   1 
ATOM   4676 N  N     . LEU   D 2 91  ? 27.35100  33.83100  73.74100  1.000 20.85422 ? 90  LEU   C N     1 
ATOM   4677 C  CA    . LEU   D 2 91  ? 25.96500  33.96500  74.17700  1.000 19.61790 ? 90  LEU   C CA    1 
ATOM   4678 C  C     . LEU   D 2 91  ? 25.04000  33.09100  73.35100  1.000 18.28733 ? 90  LEU   C C     1 
ATOM   4679 O  O     . LEU   D 2 91  ? 25.25800  32.88500  72.14800  1.000 20.28383 ? 90  LEU   C O     1 
ATOM   4680 C  CB    . LEU   D 2 91  ? 25.50400  35.41400  74.15900  1.000 18.46087 ? 90  LEU   C CB    1 
ATOM   4681 C  CG    . LEU   D 2 91  ? 26.37100  36.26700  75.09100  1.000 19.97183 ? 90  LEU   C CG    1 
ATOM   4682 C  CD1   . LEU   D 2 91  ? 25.98100  37.70400  75.04100  1.000 24.82284 ? 90  LEU   C CD1   1 
ATOM   4683 C  CD2   . LEU   D 2 91  ? 26.28200  35.80800  76.54400  1.000 21.15966 ? 90  LEU   C CD2   1 
ATOM   4684 N  N     . LYS   D 2 92  ? 23.99500  32.58500  73.99100  1.000 21.00587 ? 91  LYS   C N     1 
ATOM   4685 C  CA    . LYS   D 2 92  ? 23.08800  31.63100  73.37700  1.000 18.86171 ? 91  LYS   C CA    1 
ATOM   4686 C  C     . LYS   D 2 92  ? 21.67700  32.20100  73.27700  1.000 21.41548 ? 91  LYS   C C     1 
ATOM   4687 O  O     . LYS   D 2 92  ? 21.33700  33.24400  73.86400  1.000 18.62431 ? 91  LYS   C O     1 
ATOM   4688 C  CB    . LYS   D 2 92  ? 23.08900  30.29600  74.13900  1.000 22.77631 ? 91  LYS   C CB    1 
ATOM   4689 C  CG    . LYS   D 2 92  ? 24.49800  29.82100  74.36700  1.000 24.68209 ? 91  LYS   C CG    1 
ATOM   4690 C  CD    . LYS   D 2 92  ? 24.58800  28.39300  74.87700  1.000 32.61631 ? 91  LYS   C CD    1 
ATOM   4691 C  CE    . LYS   D 2 92  ? 25.79100  27.69000  74.25100  1.000 41.76684 ? 91  LYS   C CE    1 
ATOM   4692 N  NZ    . LYS   D 2 92  ? 26.94000  28.62200  74.02300  1.000 45.16066 ? 91  LYS   C NZ    1 
ATOM   4693 N  N     . HIS   D 2 93  ? 20.86800  31.52100  72.45000  1.000 18.25698 ? 92  HIS   C N     1 
ATOM   4694 C  CA    . HIS   D 2 93  ? 19.50500  31.95300  72.16100  1.000 17.42111 ? 92  HIS   C CA    1 
ATOM   4695 C  C     . HIS   D 2 93  ? 18.62700  31.33600  73.23300  1.000 21.99115 ? 92  HIS   C C     1 
ATOM   4696 O  O     . HIS   D 2 93  ? 18.02900  30.28100  73.03100  1.000 25.10821 ? 92  HIS   C O     1 
ATOM   4697 C  CB    . HIS   D 2 93  ? 19.07600  31.47700  70.77100  1.000 18.52612 ? 92  HIS   C CB    1 
ATOM   4698 C  CG    . HIS   D 2 93  ? 19.91200  32.03100  69.65000  1.000 16.23677 ? 92  HIS   C CG    1 
ATOM   4699 N  ND1   . HIS   D 2 93  ? 21.11000  31.46000  69.26100  1.000 15.98868 ? 92  HIS   C ND1   1 
ATOM   4700 C  CD2   . HIS   D 2 93  ? 19.71200  33.08900  68.82800  1.000 19.36163 ? 92  HIS   C CD2   1 
ATOM   4701 C  CE1   . HIS   D 2 93  ? 21.61900  32.15500  68.25100  1.000 16.02225 ? 92  HIS   C CE1   1 
ATOM   4702 N  NE2   . HIS   D 2 93  ? 20.78900  33.14200  67.96700  1.000 16.70667 ? 92  HIS   C NE2   1 
ATOM   4703 N  N     . THR   D 2 94  ? 18.55400  31.99800  74.39300  1.000 19.74866 ? 93  THR   C N     1 
ATOM   4704 C  CA    . THR   D 2 94  ? 18.01800  31.38900  75.60200  1.000 21.82447 ? 93  THR   C CA    1 
ATOM   4705 C  C     . THR   D 2 94  ? 16.53000  31.62200  75.81600  1.000 19.73890 ? 93  THR   C C     1 
ATOM   4706 O  O     . THR   D 2 94  ? 15.94200  30.99000  76.71200  1.000 25.13044 ? 93  THR   C O     1 
ATOM   4707 C  CB    . THR   D 2 94  ? 18.80500  31.88800  76.81400  1.000 21.55399 ? 93  THR   C CB    1 
ATOM   4708 O  OG1   . THR   D 2 94  ? 18.96200  33.30300  76.72600  1.000 24.25822 ? 93  THR   C OG1   1 
ATOM   4709 C  CG2   . THR   D 2 94  ? 20.17800  31.23400  76.85000  1.000 22.15090 ? 93  THR   C CG2   1 
ATOM   4710 N  N     . GLY   D 2 95  ? 15.91000  32.50500  75.05700  1.000 20.21521 ? 94  GLY   C N     1 
ATOM   4711 C  CA    . GLY   D 2 95  ? 14.50100  32.77200  75.25100  1.000 21.33791 ? 94  GLY   C CA    1 
ATOM   4712 C  C     . GLY   D 2 95  ? 14.01700  34.01100  74.52100  1.000 20.78496 ? 94  GLY   C C     1 
ATOM   4713 O  O     . GLY   D 2 95  ? 14.74200  34.63600  73.74200  1.000 19.35748 ? 94  GLY   C O     1 
ATOM   4714 N  N     . PRO   D 2 96  ? 12.77200  34.40700  74.77800  1.000 20.69029 ? 95  PRO   C N     1 
ATOM   4715 C  CA    . PRO   D 2 96  ? 12.23600  35.62600  74.14100  1.000 21.60389 ? 95  PRO   C CA    1 
ATOM   4716 C  C     . PRO   D 2 96  ? 13.08100  36.85000  74.46400  1.000 18.44562 ? 95  PRO   C C     1 
ATOM   4717 O  O     . PRO   D 2 96  ? 13.64900  36.98100  75.55600  1.000 20.57819 ? 95  PRO   C O     1 
ATOM   4718 C  CB    . PRO   D 2 96  ? 10.83600  35.75600  74.75600  1.000 21.87893 ? 95  PRO   C CB    1 
ATOM   4719 C  CG    . PRO   D 2 96  ? 10.51900  34.36700  75.23900  1.000 28.11430 ? 95  PRO   C CG    1 
ATOM   4720 C  CD    . PRO   D 2 96  ? 11.79800  33.75600  75.67700  1.000 23.03217 ? 95  PRO   C CD    1 
ATOM   4721 N  N     . GLY   D 2 97  ? 13.18100  37.74200  73.48100  1.000 17.93665 ? 96  GLY   C N     1 
ATOM   4722 C  CA    . GLY   D 2 97  ? 13.87800  38.99300  73.62900  1.000 16.92696 ? 96  GLY   C CA    1 
ATOM   4723 C  C     . GLY   D 2 97  ? 15.31600  38.99000  73.16500  1.000 16.20579 ? 96  GLY   C C     1 
ATOM   4724 O  O     . GLY   D 2 97  ? 15.90100  40.07500  73.00200  1.000 16.69527 ? 96  GLY   C O     1 
ATOM   4725 N  N     . ILE   D 2 98  ? 15.90200  37.81400  72.95700  1.000 17.42454 ? 97  ILE   C N     1 
ATOM   4726 C  CA    . ILE   D 2 98  ? 17.28800  37.74500  72.49400  1.000 16.89356 ? 97  ILE   C CA    1 
ATOM   4727 C  C     . ILE   D 2 98  ? 17.42200  38.39600  71.12300  1.000 16.11960 ? 97  ILE   C C     1 
ATOM   4728 O  O     . ILE   D 2 98  ? 16.60300  38.16600  70.21800  1.000 16.73106 ? 97  ILE   C O     1 
ATOM   4729 C  CB    . ILE   D 2 98  ? 17.76000  36.28100  72.46100  1.000 18.19866 ? 97  ILE   C CB    1 
ATOM   4730 C  CG1   . ILE   D 2 98  ? 17.94800  35.74900  73.87400  1.000 19.07586 ? 97  ILE   C CG1   1 
ATOM   4731 C  CG2   . ILE   D 2 98  ? 19.04600  36.12800  71.65300  1.000 20.00021 ? 97  ILE   C CG2   1 
ATOM   4732 C  CD1   . ILE   D 2 98  ? 19.04000  36.45700  74.66900  1.000 23.57439 ? 97  ILE   C CD1   1 
ATOM   4733 N  N     . LEU   D 2 99  ? 18.45800  39.21800  70.96500  1.000 16.04731 ? 98  LEU   C N     1 
ATOM   4734 C  CA    . LEU   D 2 99  ? 18.77500  39.91500  69.72600  1.000 15.90940 ? 98  LEU   C CA    1 
ATOM   4735 C  C     . LEU   D 2 99  ? 20.03500  39.28900  69.13200  1.000 15.66982 ? 98  LEU   C C     1 
ATOM   4736 O  O     . LEU   D 2 99  ? 21.06400  39.18800  69.80900  1.000 16.67295 ? 98  LEU   C O     1 
ATOM   4737 C  CB    . LEU   D 2 99  ? 18.95700  41.40200  70.04200  1.000 16.66813 ? 98  LEU   C CB    1 
ATOM   4738 C  CG    . LEU   D 2 99  ? 19.43900  42.32000  68.93200  1.000 17.16481 ? 98  LEU   C CG    1 
ATOM   4739 C  CD1   . LEU   D 2 99  ? 18.36400  42.48400  67.86000  1.000 19.58547 ? 98  LEU   C CD1   1 
ATOM   4740 C  CD2   . LEU   D 2 99  ? 19.79700  43.66700  69.54100  1.000 20.08835 ? 98  LEU   C CD2   1 
ATOM   4741 N  N     . SER   D 2 100 ? 19.95000  38.84100  67.87600  1.000 14.40420 ? 99  SER   C N     1 
ATOM   4742 C  CA    . SER   D 2 100 ? 20.98200  38.03700  67.26600  1.000 16.15189 ? 99  SER   C CA    1 
ATOM   4743 C  C     . SER   D 2 100 ? 21.13300  38.43300  65.79700  1.000 15.59508 ? 99  SER   C C     1 
ATOM   4744 O  O     . SER   D 2 100 ? 20.23000  39.02200  65.18300  1.000 16.99941 ? 99  SER   C O     1 
ATOM   4745 C  CB    . SER   D 2 100 ? 20.58100  36.56000  67.42700  1.000 16.37337 ? 99  SER   C CB    1 
ATOM   4746 O  OG    . SER   D 2 100 ? 21.59400  35.73900  66.92700  1.000 16.75879 ? 99  SER   C OG    1 
ATOM   4747 N  N     . MET   D 2 101 ? 22.29000  38.13700  65.21900  1.000 16.34944 ? 100 MET   C N     1 
ATOM   4748 C  CA    . MET   D 2 101 ? 22.53500  38.52100  63.83200  1.000 15.98375 ? 100 MET   C CA    1 
ATOM   4749 C  C     . MET   D 2 101 ? 21.99700  37.47600  62.84800  1.000 17.68567 ? 100 MET   C C     1 
ATOM   4750 O  O     . MET   D 2 101 ? 22.27200  36.27800  62.99800  1.000 18.72238 ? 100 MET   C O     1 
ATOM   4751 C  CB    . MET   D 2 101 ? 24.03900  38.65900  63.61000  1.000 18.40335 ? 100 MET   C CB    1 
ATOM   4752 C  CG    . MET   D 2 101 ? 24.69800  39.90000  64.23500  1.000 19.95777 ? 100 MET   C CG    1 
ATOM   4753 S  SD    . MET   D 2 101 ? 23.89700  41.43900  63.77000  1.000 22.06996 ? 100 MET   C SD    1 
ATOM   4754 C  CE    . MET   D 2 101 ? 24.53300  41.67700  62.08300  1.000 21.08567 ? 100 MET   C CE    1 
ATOM   4755 N  N     . ALA   D 2 102 ? 21.24800  37.93100  61.83600  1.000 17.66914 ? 101 ALA   C N     1 
ATOM   4756 C  CA    . ALA   D 2 102 ? 20.93400  37.05800  60.72600  1.000 19.79257 ? 101 ALA   C CA    1 
ATOM   4757 C  C     . ALA   D 2 102 ? 22.14100  37.00700  59.80400  1.000 21.67572 ? 101 ALA   C C     1 
ATOM   4758 O  O     . ALA   D 2 102 ? 23.01600  37.87200  59.85400  1.000 22.35014 ? 101 ALA   C O     1 
ATOM   4759 C  CB    . ALA   D 2 102 ? 19.75600  37.60800  59.93300  1.000 19.21256 ? 101 ALA   C CB    1 
ATOM   4760 N  N     . ASN   D 2 103 ? 22.21600  35.96400  58.98700  1.000 21.12673 ? 102 ASN   C N     1 
ATOM   4761 C  CA    . ASN   D 2 103 ? 23.38900  35.83700  58.12700  1.000 20.13217 ? 102 ASN   C CA    1 
ATOM   4762 C  C     . ASN   D 2 103 ? 23.08200  34.85100  57.01100  1.000 23.43008 ? 102 ASN   C C     1 
ATOM   4763 O  O     . ASN   D 2 103 ? 22.01500  34.23300  56.97400  1.000 23.39901 ? 102 ASN   C O     1 
ATOM   4764 C  CB    . ASN   D 2 103 ? 24.62000  35.42400  58.96500  1.000 22.94329 ? 102 ASN   C CB    1 
ATOM   4765 C  CG    . ASN   D 2 103 ? 24.48700  34.03300  59.56800  1.000 25.16843 ? 102 ASN   C CG    1 
ATOM   4766 O  OD1   . ASN   D 2 103 ? 24.22200  33.04500  58.85100  1.000 22.87999 ? 102 ASN   C OD1   1 
ATOM   4767 N  ND2   . ASN   D 2 103 ? 24.73300  33.93400  60.89600  1.000 23.15281 ? 102 ASN   C ND2   1 
ATOM   4768 N  N     . ALA   D 2 104 ? 24.05000  34.70700  56.10000  1.000 24.25143 ? 103 ALA   C N     1 
ATOM   4769 C  CA    . ALA   D 2 104 ? 23.99200  33.80700  54.94900  1.000 29.21716 ? 103 ALA   C CA    1 
ATOM   4770 C  C     . ALA   D 2 104 ? 25.03300  32.69300  55.04600  1.000 31.05805 ? 103 ALA   C C     1 
ATOM   4771 O  O     . ALA   D 2 104 ? 25.56800  32.23400  54.02400  1.000 34.08572 ? 103 ALA   C O     1 
ATOM   4772 C  CB    . ALA   D 2 104 ? 24.19800  34.59600  53.65800  1.000 30.64001 ? 103 ALA   C CB    1 
ATOM   4773 N  N     . GLY   D 2 105 ? 25.34700  32.25200  56.26300  1.000 31.01560 ? 104 GLY   C N     1 
ATOM   4774 C  CA    . GLY   D 2 105 ? 26.42500  31.31700  56.46600  1.000 33.11837 ? 104 GLY   C CA    1 
ATOM   4775 C  C     . GLY   D 2 105 ? 27.52400  31.92100  57.31800  1.000 29.00190 ? 104 GLY   C C     1 
ATOM   4776 O  O     . GLY   D 2 105 ? 27.47500  33.10100  57.67200  1.000 27.84315 ? 104 GLY   C O     1 
ATOM   4777 N  N     . PRO   D 2 106 ? 28.53100  31.11600  57.66800  1.000 29.20250 ? 105 PRO   C N     1 
ATOM   4778 C  CA    . PRO   D 2 106 ? 29.61800  31.60900  58.52200  1.000 29.59673 ? 105 PRO   C CA    1 
ATOM   4779 C  C     . PRO   D 2 106 ? 30.21100  32.91800  58.01100  1.000 30.54539 ? 105 PRO   C C     1 
ATOM   4780 O  O     . PRO   D 2 106 ? 30.41600  33.10800  56.80800  1.000 32.55144 ? 105 PRO   C O     1 
ATOM   4781 C  CB    . PRO   D 2 106 ? 30.64300  30.47200  58.47200  1.000 32.87105 ? 105 PRO   C CB    1 
ATOM   4782 C  CG    . PRO   D 2 106 ? 29.80900  29.23300  58.21100  1.000 37.86162 ? 105 PRO   C CG    1 
ATOM   4783 C  CD    . PRO   D 2 106 ? 28.68000  29.68700  57.33400  1.000 36.82083 ? 105 PRO   C CD    1 
ATOM   4784 N  N     . ASN   D 2 107 ? 30.44800  33.83900  58.94600  1.000 32.41331 ? 106 ASN   C N     1 
ATOM   4785 C  CA    . ASN   D 2 107 ? 31.21000  35.06200  58.69500  1.000 28.75563 ? 106 ASN   C CA    1 
ATOM   4786 C  C     . ASN   D 2 107 ? 30.60000  35.91200  57.58100  1.000 29.34967 ? 106 ASN   C C     1 
ATOM   4787 O  O     . ASN   D 2 107 ? 31.28400  36.37700  56.67300  1.000 31.45649 ? 106 ASN   C O     1 
ATOM   4788 C  CB    . ASN   D 2 107 ? 32.68900  34.74500  58.43500  1.000 32.63711 ? 106 ASN   C CB    1 
ATOM   4789 C  CG    . ASN   D 2 107 ? 33.29200  33.85700  59.50900  1.000 34.16590 ? 106 ASN   C CG    1 
ATOM   4790 O  OD1   . ASN   D 2 107 ? 33.26100  34.18700  60.68900  1.000 31.00284 ? 106 ASN   C OD1   1 
ATOM   4791 N  ND2   . ASN   D 2 107 ? 33.81300  32.71100  59.10700  1.000 38.38067 ? 106 ASN   C ND2   1 
ATOM   4792 N  N     . THR   D 2 108 ? 29.29700  36.12700  57.65400  1.000 26.75189 ? 107 THR   C N     1 
ATOM   4793 C  CA    . THR   D 2 108 ? 28.60400  36.97300  56.68300  1.000 26.45187 ? 107 THR   C CA    1 
ATOM   4794 C  C     . THR   D 2 108 ? 27.70700  38.00300  57.36900  1.000 28.49448 ? 107 THR   C C     1 
ATOM   4795 O  O     . THR   D 2 108 ? 26.63300  38.33300  56.86300  1.000 28.93911 ? 107 THR   C O     1 
ATOM   4796 C  CB    . THR   D 2 108 ? 27.79300  36.14200  55.67400  1.000 31.09307 ? 107 THR   C CB    1 
ATOM   4797 O  OG1   . THR   D 2 108 ? 26.77800  35.40000  56.36400  1.000 27.91930 ? 107 THR   C OG1   1 
ATOM   4798 C  CG2   . THR   D 2 108 ? 28.66600  35.15600  54.88800  1.000 31.96044 ? 107 THR   C CG2   1 
ATOM   4799 N  N     . ASN   D 2 109 ? 28.13000  38.53000  58.51900  1.000 25.40971 ? 108 ASN   C N     1 
ATOM   4800 C  CA    . ASN   D 2 109 ? 27.31500  39.50400  59.24000  1.000 25.67876 ? 108 ASN   C CA    1 
ATOM   4801 C  C     . ASN   D 2 109 ? 27.28400  40.83900  58.51500  1.000 24.17200 ? 108 ASN   C C     1 
ATOM   4802 O  O     . ASN   D 2 109 ? 28.32000  41.34400  58.05800  1.000 26.35939 ? 108 ASN   C O     1 
ATOM   4803 C  CB    . ASN   D 2 109 ? 27.88300  39.70300  60.63200  1.000 24.46048 ? 108 ASN   C CB    1 
ATOM   4804 C  CG    . ASN   D 2 109 ? 27.80400  38.46400  61.44500  1.000 25.80290 ? 108 ASN   C CG    1 
ATOM   4805 O  OD1   . ASN   D 2 109 ? 26.71500  38.05000  61.82500  1.000 23.87533 ? 108 ASN   C OD1   1 
ATOM   4806 N  ND2   . ASN   D 2 109 ? 28.93900  37.82900  61.67800  1.000 26.60467 ? 108 ASN   C ND2   1 
ATOM   4807 N  N     . GLY   D 2 110 ? 26.09600  41.41000  58.38600  1.000 26.31010 ? 109 GLY   C N     1 
ATOM   4808 C  CA    . GLY   D 2 110 ? 25.97100  42.70700  57.75300  1.000 25.01455 ? 109 GLY   C CA    1 
ATOM   4809 C  C     . GLY   D 2 110 ? 25.17700  43.62500  58.65000  1.000 24.95122 ? 109 GLY   C C     1 
ATOM   4810 O  O     . GLY   D 2 110 ? 25.70400  44.14200  59.64300  1.000 26.37427 ? 109 GLY   C O     1 
ATOM   4811 N  N     . SER   D 2 111 ? 23.90300  43.81000  58.33500  1.000 23.57453 ? 110 SER   C N     1 
ATOM   4812 C  CA    . SER   D 2 111 ? 23.01300  44.53800  59.22700  1.000 23.28397 ? 110 SER   C CA    1 
ATOM   4813 C  C     . SER   D 2 111 ? 21.75400  43.77000  59.63100  1.000 19.48891 ? 110 SER   C C     1 
ATOM   4814 O  O     . SER   D 2 111 ? 21.07800  44.20400  60.57200  1.000 20.14231 ? 110 SER   C O     1 
ATOM   4815 C  CB    . SER   D 2 111 ? 22.62600  45.87700  58.58200  1.000 23.69741 ? 110 SER   C CB    1 
ATOM   4816 O  OG    . SER   D 2 111 ? 21.98300  45.60100  57.34700  1.000 23.12562 ? 110 SER   C OG    1 
ATOM   4817 N  N     . GLN   D 2 112 ? 21.39500  42.68600  58.95100  1.000 21.12491 ? 111 GLN   C N     1 
ATOM   4818 C  CA    . GLN   D 2 112 ? 20.13500  42.04700  59.30400  1.000 19.81106 ? 111 GLN   C CA    1 
ATOM   4819 C  C     . GLN   D 2 112 ? 20.24900  41.38700  60.67600  1.000 19.33611 ? 111 GLN   C C     1 
ATOM   4820 O  O     . GLN   D 2 112 ? 21.30900  40.86800  61.06400  1.000 19.51314 ? 111 GLN   C O     1 
ATOM   4821 C  CB    . GLN   D 2 112 ? 19.69300  41.05200  58.23200  1.000 20.17361 ? 111 GLN   C CB    1 
ATOM   4822 C  CG    . GLN   D 2 112 ? 19.11400  41.74400  57.00600  1.000 21.02922 ? 111 GLN   C CG    1 
ATOM   4823 C  CD    . GLN   D 2 112 ? 18.35400  40.77700  56.11600  1.000 21.51345 ? 111 GLN   C CD    1 
ATOM   4824 O  OE1   . GLN   D 2 112 ? 17.57400  39.97300  56.61200  1.000 21.49915 ? 111 GLN   C OE1   1 
ATOM   4825 N  NE2   . GLN   D 2 112 ? 18.59500  40.83100  54.80900  1.000 20.94396 ? 111 GLN   C NE2   1 
ATOM   4826 N  N     . PHE   D 2 113 ? 19.15100  41.43800  61.42300  1.000 17.37233 ? 112 PHE   C N     1 
ATOM   4827 C  CA    . PHE   D 2 113 ? 19.10400  40.97100  62.80400  1.000 16.64521 ? 112 PHE   C CA    1 
ATOM   4828 C  C     . PHE   D 2 113 ? 17.75300  40.32500  63.04200  1.000 15.37121 ? 112 PHE   C C     1 
ATOM   4829 O  O     . PHE   D 2 113 ? 16.82900  40.47300  62.24100  1.000 16.67855 ? 112 PHE   C O     1 
ATOM   4830 C  CB    . PHE   D 2 113 ? 19.27500  42.13600  63.79300  1.000 19.30192 ? 112 PHE   C CB    1 
ATOM   4831 C  CG    . PHE   D 2 113 ? 18.17600  43.14900  63.67600  1.000 16.44961 ? 112 PHE   C CG    1 
ATOM   4832 C  CD1   . PHE   D 2 113 ? 18.27500  44.17600  62.74700  1.000 20.09148 ? 112 PHE   C CD1   1 
ATOM   4833 C  CD2   . PHE   D 2 113 ? 17.01700  43.03500  64.43700  1.000 16.67833 ? 112 PHE   C CD2   1 
ATOM   4834 C  CE1   . PHE   D 2 113 ? 17.23900  45.06200  62.60000  1.000 20.65393 ? 112 PHE   C CE1   1 
ATOM   4835 C  CE2   . PHE   D 2 113 ? 15.97500  43.89900  64.26600  1.000 19.18176 ? 112 PHE   C CE2   1 
ATOM   4836 C  CZ    . PHE   D 2 113 ? 16.09700  44.93700  63.35300  1.000 20.67892 ? 112 PHE   C CZ    1 
ATOM   4837 N  N     . PHE   D 2 114 ? 17.63900  39.59100  64.14700  1.000 15.80557 ? 113 PHE   C N     1 
ATOM   4838 C  CA    . PHE   D 2 114 ? 16.33400  39.06000  64.52000  1.000 17.05869 ? 113 PHE   C CA    1 
ATOM   4839 C  C     . PHE   D 2 114 ? 16.14600  39.16000  66.02300  1.000 15.66605 ? 113 PHE   C C     1 
ATOM   4840 O  O     . PHE   D 2 114 ? 17.11000  39.13400  66.80400  1.000 15.63467 ? 113 PHE   C O     1 
ATOM   4841 C  CB    . PHE   D 2 114 ? 16.07400  37.62600  63.99200  1.000 17.51952 ? 113 PHE   C CB    1 
ATOM   4842 C  CG    . PHE   D 2 114 ? 17.02500  36.57400  64.49900  1.000 15.50453 ? 113 PHE   C CG    1 
ATOM   4843 C  CD1   . PHE   D 2 114 ? 18.30800  36.45800  63.96600  1.000 15.85868 ? 113 PHE   C CD1   1 
ATOM   4844 C  CD2   . PHE   D 2 114 ? 16.62600  35.67700  65.48400  1.000 16.15084 ? 113 PHE   C CD2   1 
ATOM   4845 C  CE1   . PHE   D 2 114 ? 19.19700  35.47000  64.40600  1.000 16.66257 ? 113 PHE   C CE1   1 
ATOM   4846 C  CE2   . PHE   D 2 114 ? 17.50600  34.69400  65.94500  1.000 16.43222 ? 113 PHE   C CE2   1 
ATOM   4847 C  CZ    . PHE   D 2 114 ? 18.76900  34.57100  65.39200  1.000 17.17714 ? 113 PHE   C CZ    1 
ATOM   4848 N  N     . ILE   D 2 115 ? 14.90100  39.35300  66.42100  1.000 14.97646 ? 114 ILE   C N     1 
ATOM   4849 C  CA    . ILE   D 2 115 ? 14.48600  39.34200  67.82300  1.000 14.58733 ? 114 ILE   C CA    1 
ATOM   4850 C  C     . ILE   D 2 115 ? 13.71000  38.05600  68.04800  1.000 15.82098 ? 114 ILE   C C     1 
ATOM   4851 O  O     . ILE   D 2 115 ? 12.68100  37.82600  67.39700  1.000 15.80809 ? 114 ILE   C O     1 
ATOM   4852 C  CB    . ILE   D 2 115 ? 13.61800  40.55400  68.17300  1.000 15.24964 ? 114 ILE   C CB    1 
ATOM   4853 C  CG1   . ILE   D 2 115 ? 14.25700  41.85300  67.69300  1.000 16.64801 ? 114 ILE   C CG1   1 
ATOM   4854 C  CG2   . ILE   D 2 115 ? 13.32800  40.57200  69.68200  1.000 16.05257 ? 114 ILE   C CG2   1 
ATOM   4855 C  CD1   . ILE   D 2 115 ? 13.27500  43.02500  67.74100  1.000 19.07221 ? 114 ILE   C CD1   1 
ATOM   4856 N  N     . CYS   D 2 116 ? 14.21100  37.20400  68.93100  1.000 15.96126 ? 115 CYS   C N     1 
ATOM   4857 C  CA    . CYS   D 2 116 ? 13.52300  35.95300  69.24900  1.000 16.74272 ? 115 CYS   C CA    1 
ATOM   4858 C  C     . CYS   D 2 116 ? 12.25200  36.22900  70.03500  1.000 16.54691 ? 115 CYS   C C     1 
ATOM   4859 O  O     . CYS   D 2 116 ? 12.22700  37.07000  70.93700  1.000 18.42804 ? 115 CYS   C O     1 
ATOM   4860 C  CB    . CYS   D 2 116 ? 14.43300  35.08700  70.11700  1.000 18.01428 ? 115 CYS   C CB    1 
ATOM   4861 S  SG    . CYS   D 2 116 ? 15.97300  34.61500  69.27100  1.000 20.84015 ? 115 CYS   C SG    1 
ATOM   4862 N  N     . THR   D 2 117 ? 11.18800  35.51700  69.69900  1.000 18.14739 ? 116 THR   C N     1 
ATOM   4863 C  CA    . THR   D 2 117 ? 9.98900   35.51200  70.52600  1.000 18.13756 ? 116 THR   C CA    1 
ATOM   4864 C  C     . THR   D 2 117 ? 9.83100   34.21200  71.29900  1.000 22.55334 ? 116 THR   C C     1 
ATOM   4865 O  O     . THR   D 2 117 ? 8.84800   34.04000  72.03900  1.000 22.94787 ? 116 THR   C O     1 
ATOM   4866 C  CB    . THR   D 2 117 ? 8.76000   35.82800  69.66800  1.000 21.48330 ? 116 THR   C CB    1 
ATOM   4867 O  OG1   . THR   D 2 117 ? 8.65500   34.87000  68.60000  1.000 23.01856 ? 116 THR   C OG1   1 
ATOM   4868 C  CG2   . THR   D 2 117 ? 8.88000   37.25600  69.11000  1.000 20.19235 ? 116 THR   C CG2   1 
ATOM   4869 N  N     . ALA   D 2 118 ? 10.80300  33.32100  71.19800  1.000 20.45535 ? 117 ALA   C N     1 
ATOM   4870 C  CA    . ALA   D 2 118 ? 10.83600  32.05400  71.90600  1.000 23.40827 ? 117 ALA   C CA    1 
ATOM   4871 C  C     . ALA   D 2 118 ? 12.29700  31.65200  72.00800  1.000 23.46996 ? 117 ALA   C C     1 
ATOM   4872 O  O     . ALA   D 2 118 ? 13.16800  32.21000  71.33100  1.000 21.83003 ? 117 ALA   C O     1 
ATOM   4873 C  CB    . ALA   D 2 118 ? 10.00400  31.00900  71.15300  1.000 24.81489 ? 117 ALA   C CB    1 
ATOM   4874 N  N     . LYS   D 2 119 ? 12.57200  30.64800  72.82500  1.000 22.45036 ? 118 LYS   C N     1 
ATOM   4875 C  CA    . LYS   D 2 119 ? 13.89900  30.04900  72.81600  1.000 24.51629 ? 118 LYS   C CA    1 
ATOM   4876 C  C     . LYS   D 2 119 ? 14.15600  29.39100  71.45900  1.000 22.56582 ? 118 LYS   C C     1 
ATOM   4877 O  O     . LYS   D 2 119 ? 13.33200  28.60700  70.97000  1.000 25.53488 ? 118 LYS   C O     1 
ATOM   4878 C  CB    . LYS   D 2 119 ? 13.96200  28.99700  73.92300  1.000 27.47042 ? 118 LYS   C CB    1 
ATOM   4879 C  CG    . LYS   D 2 119 ? 15.27500  28.27700  74.04600  1.000 25.65071 ? 118 LYS   C CG    1 
ATOM   4880 C  CD    . LYS   D 2 119 ? 15.20600  27.30900  75.22800  1.000 31.54213 ? 118 LYS   C CD    1 
ATOM   4881 C  CE    . LYS   D 2 119 ? 16.44300  26.44400  75.34700  1.000 41.67801 ? 118 LYS   C CE    1 
ATOM   4882 N  NZ    . LYS   D 2 119 ? 16.49000  25.75000  76.67200  1.000 39.65845 ? 118 LYS   C NZ    1 
ATOM   4883 N  N     . THR   D 2 120 ? 15.30600  29.70100  70.85000  1.000 19.51446 ? 119 THR   C N     1 
ATOM   4884 C  CA    . THR   D 2 120 ? 15.66700  29.15600  69.52600  1.000 20.86136 ? 119 THR   C CA    1 
ATOM   4885 C  C     . THR   D 2 120 ? 17.07000  28.54500  69.58700  1.000 18.85968 ? 119 THR   C C     1 
ATOM   4886 O  O     . THR   D 2 120 ? 18.00600  28.92700  68.87600  1.000 20.95584 ? 119 THR   C O     1 
ATOM   4887 C  CB    . THR   D 2 120 ? 15.59500  30.21800  68.43300  1.000 18.72116 ? 119 THR   C CB    1 
ATOM   4888 O  OG1   . THR   D 2 120 ? 16.56200  31.24700  68.70500  1.000 19.40294 ? 119 THR   C OG1   1 
ATOM   4889 C  CG2   . THR   D 2 120 ? 14.16900  30.81600  68.31300  1.000 22.14972 ? 119 THR   C CG2   1 
ATOM   4890 N  N     . GLU   D 2 121 ? 17.21100  27.54200  70.44700  1.000 21.10051 ? 120 GLU   C N     1 
ATOM   4891 C  CA    . GLU   D 2 121 ? 18.53400  27.03400  70.77700  1.000 21.76940 ? 120 GLU   C CA    1 
ATOM   4892 C  C     . GLU   D 2 121 ? 19.21600  26.32800  69.60300  1.000 25.79844 ? 120 GLU   C C     1 
ATOM   4893 O  O     . GLU   D 2 121 ? 20.44900  26.21000  69.59100  1.000 22.86207 ? 120 GLU   C O     1 
ATOM   4894 C  CB    . GLU   D 2 121 ? 18.43600  26.09700  71.98800  1.000 30.04901 ? 120 GLU   C CB    1 
ATOM   4895 C  CG    . GLU   D 2 121 ? 17.80600  24.76800  71.69800  1.000 28.16326 ? 120 GLU   C CG    1 
ATOM   4896 C  CD    . GLU   D 2 121 ? 16.29500  24.80700  71.47000  1.000 35.64960 ? 120 GLU   C CD    1 
ATOM   4897 O  OE1   . GLU   D 2 121 ? 15.61700  25.81200  71.81100  1.000 30.55559 ? 120 GLU   C OE1   1 
ATOM   4898 O  OE2   . GLU   D 2 121 ? 15.78300  23.79800  70.93800  1.000 43.12720 ? 120 GLU   C OE2   1 
ATOM   4899 N  N     . TRP   D 2 122 ? 18.44700  25.86100  68.61100  1.000 21.78026 ? 121 TRP   C N     1 
ATOM   4900 C  CA    . TRP   D 2 122 ? 19.06000  25.24600  67.44800  1.000 22.35776 ? 121 TRP   C CA    1 
ATOM   4901 C  C     . TRP   D 2 122 ? 19.88300  26.24300  66.64300  1.000 23.34596 ? 121 TRP   C C     1 
ATOM   4902 O  O     . TRP   D 2 122 ? 20.67400  25.82100  65.78700  1.000 24.83711 ? 121 TRP   C O     1 
ATOM   4903 C  CB    . TRP   D 2 122 ? 17.98200  24.61600  66.56700  1.000 23.42502 ? 121 TRP   C CB    1 
ATOM   4904 C  CG    . TRP   D 2 122 ? 17.01700  25.59300  66.01300  1.000 23.51044 ? 121 TRP   C CG    1 
ATOM   4905 C  CD1   . TRP   D 2 122 ? 17.09800  26.23200  64.82000  1.000 22.71534 ? 121 TRP   C CD1   1 
ATOM   4906 C  CD2   . TRP   D 2 122 ? 15.80800  26.04800  66.62700  1.000 20.92795 ? 121 TRP   C CD2   1 
ATOM   4907 N  NE1   . TRP   D 2 122 ? 16.01900  27.05700  64.65400  1.000 21.02747 ? 121 TRP   C NE1   1 
ATOM   4908 C  CE2   . TRP   D 2 122 ? 15.20200  26.95700  65.74700  1.000 20.91238 ? 121 TRP   C CE2   1 
ATOM   4909 C  CE3   . TRP   D 2 122 ? 15.17800  25.77500  67.84500  1.000 21.94052 ? 121 TRP   C CE3   1 
ATOM   4910 C  CZ2   . TRP   D 2 122 ? 13.99800  27.59700  66.04400  1.000 21.54963 ? 121 TRP   C CZ2   1 
ATOM   4911 C  CZ3   . TRP   D 2 122 ? 13.98200  26.39400  68.13100  1.000 24.06523 ? 121 TRP   C CZ3   1 
ATOM   4912 C  CH2   . TRP   D 2 122 ? 13.39900  27.29200  67.24700  1.000 20.89871 ? 121 TRP   C CH2   1 
ATOM   4913 N  N     . LEU   D 2 123 ? 19.72900  27.55000  66.90100  1.000 22.81301 ? 122 LEU   C N     1 
ATOM   4914 C  CA    . LEU   D 2 123 ? 20.53100  28.55600  66.20800  1.000 19.60421 ? 122 LEU   C CA    1 
ATOM   4915 C  C     . LEU   D 2 123 ? 21.85200  28.83700  66.91200  1.000 20.61265 ? 122 LEU   C C     1 
ATOM   4916 O  O     . LEU   D 2 123 ? 22.66700  29.59800  66.37800  1.000 20.47711 ? 122 LEU   C O     1 
ATOM   4917 C  CB    . LEU   D 2 123 ? 19.77700  29.87500  66.05000  1.000 21.03905 ? 122 LEU   C CB    1 
ATOM   4918 C  CG    . LEU   D 2 123 ? 18.45900  29.77100  65.27500  1.000 19.17715 ? 122 LEU   C CG    1 
ATOM   4919 C  CD1   . LEU   D 2 123 ? 17.67300  31.08000  65.31800  1.000 19.79078 ? 122 LEU   C CD1   1 
ATOM   4920 C  CD2   . LEU   D 2 123 ? 18.67800  29.32800  63.78600  1.000 22.81131 ? 122 LEU   C CD2   1 
ATOM   4921 N  N     . ASP   D 2 124 ? 22.07600  28.24100  68.08400  1.000 20.90377 ? 123 ASP   C N     1 
ATOM   4922 C  CA    . ASP   D 2 124 ? 23.30400  28.48800  68.82500  1.000 22.33098 ? 123 ASP   C CA    1 
ATOM   4923 C  C     . ASP   D 2 124 ? 24.49000  28.03400  67.98200  1.000 23.84408 ? 123 ASP   C C     1 
ATOM   4924 O  O     . ASP   D 2 124 ? 24.44900  26.97500  67.35200  1.000 25.54851 ? 123 ASP   C O     1 
ATOM   4925 C  CB    . ASP   D 2 124 ? 23.28700  27.70700  70.14700  1.000 22.35009 ? 123 ASP   C CB    1 
ATOM   4926 C  CG    . ASP   D 2 124 ? 22.30900  28.26400  71.17400  1.000 23.90700 ? 123 ASP   C CG    1 
ATOM   4927 O  OD1   . ASP   D 2 124 ? 21.76100  29.36500  70.99600  1.000 21.91376 ? 123 ASP   C OD1   1 
ATOM   4928 O  OD2   . ASP   D 2 124 ? 22.07800  27.57400  72.18500  1.000 23.36885 ? 123 ASP   C OD2   1 
ATOM   4929 N  N     . GLY   D 2 125 ? 25.56700  28.81900  68.00200  1.000 25.31377 ? 124 GLY   C N     1 
ATOM   4930 C  CA    . GLY   D 2 125 ? 26.75300  28.50900  67.22900  1.000 25.22747 ? 124 GLY   C CA    1 
ATOM   4931 C  C     . GLY   D 2 125 ? 26.64900  28.82400  65.75800  1.000 26.63027 ? 124 GLY   C C     1 
ATOM   4932 O  O     . GLY   D 2 125 ? 27.64500  28.66900  65.04000  1.000 30.60728 ? 124 GLY   C O     1 
ATOM   4933 N  N     . LYS   D 2 126 ? 25.48800  29.27200  65.28200  1.000 26.08170 ? 125 LYS   C N     1 
ATOM   4934 C  CA    . LYS   D 2 126 ? 25.31100  29.68400  63.89500  1.000 23.32225 ? 125 LYS   C CA    1 
ATOM   4935 C  C     . LYS   D 2 126 ? 24.98600  31.16400  63.74300  1.000 25.51044 ? 125 LYS   C C     1 
ATOM   4936 O  O     . LYS   D 2 126 ? 25.23300  31.72400  62.66500  1.000 28.02930 ? 125 LYS   C O     1 
ATOM   4937 C  CB    . LYS   D 2 126 ? 24.18700  28.87800  63.22000  1.000 26.10983 ? 125 LYS   C CB    1 
ATOM   4938 C  CG    . LYS   D 2 126 ? 24.42200  27.39100  63.13600  1.000 35.55814 ? 125 LYS   C CG    1 
ATOM   4939 C  CD    . LYS   D 2 126 ? 23.33200  26.73100  62.30100  1.000 39.10258 ? 125 LYS   C CD    1 
ATOM   4940 C  CE    . LYS   D 2 126 ? 23.78100  26.49900  60.84100  1.000 55.29351 ? 125 LYS   C CE    1 
ATOM   4941 N  NZ    . LYS   D 2 126 ? 24.11600  27.74000  60.05900  1.000 51.07212 ? 125 LYS   C NZ    1 
ATOM   4942 N  N     . HIS   D 2 127 ? 24.46100  31.81000  64.78100  1.000 22.44536 ? 126 HIS   C N     1 
ATOM   4943 C  CA    . HIS   D 2 127 ? 24.12500  33.22500  64.76200  1.000 19.96467 ? 126 HIS   C CA    1 
ATOM   4944 C  C     . HIS   D 2 127 ? 24.70100  33.85900  66.01300  1.000 20.69547 ? 126 HIS   C C     1 
ATOM   4945 O  O     . HIS   D 2 127 ? 24.61900  33.27400  67.10100  1.000 20.63309 ? 126 HIS   C O     1 
ATOM   4946 C  CB    . HIS   D 2 127 ? 22.61700  33.42400  64.72100  1.000 18.65027 ? 126 HIS   C CB    1 
ATOM   4947 C  CG    . HIS   D 2 127 ? 22.00300  32.84400  63.48600  1.000 19.42987 ? 126 HIS   C CG    1 
ATOM   4948 N  ND1   . HIS   D 2 127 ? 21.79300  33.58300  62.34000  1.000 20.32204 ? 126 HIS   C ND1   1 
ATOM   4949 C  CD2   . HIS   D 2 127 ? 21.63300  31.57700  63.19900  1.000 20.53515 ? 126 HIS   C CD2   1 
ATOM   4950 C  CE1   . HIS   D 2 127 ? 21.30500  32.79000  61.39900  1.000 20.02058 ? 126 HIS   C CE1   1 
ATOM   4951 N  NE2   . HIS   D 2 127 ? 21.20500  31.56700  61.88900  1.000 21.14660 ? 126 HIS   C NE2   1 
ATOM   4952 N  N     . VAL   D 2 128 ? 25.32600  35.02200  65.85100  1.000 18.75299 ? 127 VAL   C N     1 
ATOM   4953 C  CA    . VAL   D 2 128 ? 25.95300  35.72600  66.96100  1.000 19.40819 ? 127 VAL   C CA    1 
ATOM   4954 C  C     . VAL   D 2 128 ? 24.89200  36.49000  67.74900  1.000 17.52400 ? 127 VAL   C C     1 
ATOM   4955 O  O     . VAL   D 2 128 ? 24.29700  37.46000  67.25800  1.000 17.89866 ? 127 VAL   C O     1 
ATOM   4956 C  CB    . VAL   D 2 128 ? 27.06200  36.66700  66.47700  1.000 19.68067 ? 127 VAL   C CB    1 
ATOM   4957 C  CG1   . VAL   D 2 128 ? 27.60000  37.46800  67.69800  1.000 18.84761 ? 127 VAL   C CG1   1 
ATOM   4958 C  CG2   . VAL   D 2 128 ? 28.14800  35.88200  65.71200  1.000 22.29214 ? 127 VAL   C CG2   1 
ATOM   4959 N  N     . VAL   D 2 129 ? 24.69000  36.07300  69.00800  1.000 16.26944 ? 128 VAL   C N     1 
ATOM   4960 C  CA    . VAL   D 2 129 ? 23.82000  36.78700  69.93800  1.000 16.83455 ? 128 VAL   C CA    1 
ATOM   4961 C  C     . VAL   D 2 129 ? 24.57800  37.98400  70.49200  1.000 17.77190 ? 128 VAL   C C     1 
ATOM   4962 O  O     . VAL   D 2 129 ? 25.71700  37.84700  70.95000  1.000 18.17818 ? 128 VAL   C O     1 
ATOM   4963 C  CB    . VAL   D 2 129 ? 23.39200  35.84200  71.07200  1.000 17.58697 ? 128 VAL   C CB    1 
ATOM   4964 C  CG1   . VAL   D 2 129 ? 22.67000  36.59400  72.17800  1.000 17.53004 ? 128 VAL   C CG1   1 
ATOM   4965 C  CG2   . VAL   D 2 129 ? 22.50600  34.74000  70.46200  1.000 18.95061 ? 128 VAL   C CG2   1 
ATOM   4966 N  N     . PHE   D 2 130 ? 23.94000  39.16100  70.48400  1.000 17.07010 ? 129 PHE   C N     1 
ATOM   4967 C  CA    . PHE   D 2 130 ? 24.64800  40.34900  70.91900  1.000 19.60663 ? 129 PHE   C CA    1 
ATOM   4968 C  C     . PHE   D 2 130 ? 23.81000  41.31800  71.73000  1.000 17.88947 ? 129 PHE   C C     1 
ATOM   4969 O  O     . PHE   D 2 130 ? 24.32400  42.38500  72.09500  1.000 18.85229 ? 129 PHE   C O     1 
ATOM   4970 C  CB    . PHE   D 2 130 ? 25.26200  41.08300  69.71800  1.000 19.59921 ? 129 PHE   C CB    1 
ATOM   4971 C  CG    . PHE   D 2 130 ? 24.24400  41.63000  68.77300  1.000 19.15753 ? 129 PHE   C CG    1 
ATOM   4972 C  CD1   . PHE   D 2 130 ? 23.66300  40.82100  67.79100  1.000 18.33112 ? 129 PHE   C CD1   1 
ATOM   4973 C  CD2   . PHE   D 2 130 ? 23.82400  42.94700  68.88700  1.000 20.10090 ? 129 PHE   C CD2   1 
ATOM   4974 C  CE1   . PHE   D 2 130 ? 22.69000  41.33100  66.91300  1.000 17.71123 ? 129 PHE   C CE1   1 
ATOM   4975 C  CE2   . PHE   D 2 130 ? 22.89100  43.46200  68.01400  1.000 19.41254 ? 129 PHE   C CE2   1 
ATOM   4976 C  CZ    . PHE   D 2 130 ? 22.30500  42.65300  67.02200  1.000 19.14829 ? 129 PHE   C CZ    1 
ATOM   4977 N  N     . GLY   D 2 131 ? 22.55900  40.99200  72.02800  1.000 18.02216 ? 130 GLY   C N     1 
ATOM   4978 C  CA    . GLY   D 2 131 ? 21.78600  41.88800  72.86300  1.000 19.29098 ? 130 GLY   C CA    1 
ATOM   4979 C  C     . GLY   D 2 131 ? 20.48400  41.26000  73.30000  1.000 16.13192 ? 130 GLY   C C     1 
ATOM   4980 O  O     . GLY   D 2 131 ? 20.22800  40.06900  73.07700  1.000 16.66941 ? 130 GLY   C O     1 
ATOM   4981 N  N     . LYS   D 2 132 ? 19.66400  42.07100  73.96200  1.000 18.25087 ? 131 LYS   C N     1 
ATOM   4982 C  CA    . LYS   D 2 132 ? 18.38200  41.56300  74.42100  1.000 17.41899 ? 131 LYS   C CA    1 
ATOM   4983 C  C     . LYS   D 2 132 ? 17.44000  42.72700  74.66500  1.000 19.12938 ? 131 LYS   C C     1 
ATOM   4984 O  O     . LYS   D 2 132 ? 17.86200  43.78000  75.13700  1.000 20.96704 ? 131 LYS   C O     1 
ATOM   4985 C  CB    . LYS   D 2 132 ? 18.55300  40.79000  75.72500  1.000 20.95826 ? 131 LYS   C CB    1 
ATOM   4986 C  CG    . LYS   D 2 132 ? 17.39700  39.90500  76.08900  1.000 23.18780 ? 131 LYS   C CG    1 
ATOM   4987 C  CD    . LYS   D 2 132 ? 17.80100  39.10400  77.32500  1.000 27.97084 ? 131 LYS   C CD    1 
ATOM   4988 C  CE    . LYS   D 2 132 ? 16.80900  37.99500  77.65200  1.000 33.14513 ? 131 LYS   C CE    1 
ATOM   4989 N  NZ    . LYS   D 2 132 ? 15.58600  38.54200  78.26000  1.000 34.83909 ? 131 LYS   C NZ    1 
ATOM   4990 N  N     . VAL   D 2 133 ? 16.15300  42.51100  74.37700  1.000 18.26814 ? 132 VAL   C N     1 
ATOM   4991 C  CA    . VAL   D 2 133 ? 15.13500  43.50200  74.70500  1.000 17.85613 ? 132 VAL   C CA    1 
ATOM   4992 C  C     . VAL   D 2 133 ? 15.16000  43.83000  76.18600  1.000 20.98475 ? 132 VAL   C C     1 
ATOM   4993 O  O     . VAL   D 2 133 ? 15.17900  42.94400  77.05500  1.000 21.88025 ? 132 VAL   C O     1 
ATOM   4994 C  CB    . VAL   D 2 133 ? 13.75100  42.99300  74.27900  1.000 16.78834 ? 132 VAL   C CB    1 
ATOM   4995 C  CG1   . VAL   D 2 133 ? 12.68400  43.90600  74.79900  1.000 18.74570 ? 132 VAL   C CG1   1 
ATOM   4996 C  CG2   . VAL   D 2 133 ? 13.66100  42.83700  72.76500  1.000 19.85819 ? 132 VAL   C CG2   1 
ATOM   4997 N  N     . LYS   D 2 134 ? 15.15800  45.12000  76.47400  1.000 22.02520 ? 133 LYS   C N     1 
ATOM   4998 C  CA    . LYS   D 2 134 ? 15.09100  45.65000  77.82900  1.000 23.09704 ? 133 LYS   C CA    1 
ATOM   4999 C  C     . LYS   D 2 134 ? 13.63500  46.03600  78.07200  1.000 25.69804 ? 133 LYS   C C     1 
ATOM   5000 O  O     . LYS   D 2 134 ? 12.93200  45.35500  78.82700  1.000 32.86202 ? 133 LYS   C O     1 
ATOM   5001 C  CB    . LYS   D 2 134 ? 16.06500  46.83500  77.93400  1.000 27.66125 ? 133 LYS   C CB    1 
ATOM   5002 C  CG    . LYS   D 2 134 ? 16.14400  47.54300  79.26900  1.000 37.16585 ? 133 LYS   C CG    1 
ATOM   5003 C  CD    . LYS   D 2 134 ? 17.13700  48.70400  79.16100  1.000 37.83514 ? 133 LYS   C CD    1 
ATOM   5004 C  CE    . LYS   D 2 134 ? 17.17100  49.57200  80.41200  1.000 47.69375 ? 133 LYS   C CE    1 
ATOM   5005 N  NZ    . LYS   D 2 134 ? 17.82900  50.89600  80.13800  1.000 48.64556 ? 133 LYS   C NZ    1 
ATOM   5006 N  N     . GLU   D 2 135 ? 13.15500  47.10600  77.44100  1.000 27.06237 ? 134 GLU   C N     1 
ATOM   5007 C  CA    . GLU   D 2 135 ? 11.76300  47.52000  77.56600  1.000 29.16429 ? 134 GLU   C CA    1 
ATOM   5008 C  C     . GLU   D 2 135 ? 11.02900  47.21900  76.26800  1.000 22.79294 ? 134 GLU   C C     1 
ATOM   5009 O  O     . GLU   D 2 135 ? 11.62200  47.22300  75.19400  1.000 23.12969 ? 134 GLU   C O     1 
ATOM   5010 C  CB    . GLU   D 2 135 ? 11.64200  49.02100  77.85700  1.000 31.42165 ? 134 GLU   C CB    1 
ATOM   5011 C  CG    . GLU   D 2 135 ? 12.47800  49.50800  79.02100  1.000 38.78241 ? 134 GLU   C CG    1 
ATOM   5012 C  CD    . GLU   D 2 135 ? 11.85400  49.20100  80.36800  1.000 52.83981 ? 134 GLU   C CD    1 
ATOM   5013 O  OE1   . GLU   D 2 135 ? 10.88900  49.90100  80.74800  1.000 55.91717 ? 134 GLU   C OE1   1 
ATOM   5014 O  OE2   . GLU   D 2 135 ? 12.33300  48.26600  81.05000  1.000 51.62359 ? 134 GLU   C OE2   1 
ATOM   5015 N  N     . GLY   D 2 136 ? 9.72500   46.98900  76.37400  1.000 24.60217 ? 135 GLY   C N     1 
ATOM   5016 C  CA    . GLY   D 2 136 ? 8.87500   46.90100  75.21000  1.000 22.47705 ? 135 GLY   C CA    1 
ATOM   5017 C  C     . GLY   D 2 136 ? 8.71700   45.51700  74.62900  1.000 24.48750 ? 135 GLY   C C     1 
ATOM   5018 O  O     . GLY   D 2 136 ? 8.35000   45.38600  73.45500  1.000 21.54934 ? 135 GLY   C O     1 
ATOM   5019 N  N     . MET   D 2 137 ? 8.94200   44.46600  75.41600  1.000 21.41105 ? 136 MET   C N     1 
ATOM   5020 C  CA    . MET   D 2 137 ? 8.66200   43.14600  74.88700  1.000 20.71360 ? 136 MET   C CA    1 
ATOM   5021 C  C     . MET   D 2 137 ? 7.19700   43.01400  74.49400  1.000 20.63688 ? 136 MET   C C     1 
ATOM   5022 O  O     . MET   D 2 137 ? 6.88400   42.27200  73.56500  1.000 22.08675 ? 136 MET   C O     1 
ATOM   5023 C  CB    . MET   D 2 137 ? 9.07500   42.05500  75.89200  1.000 23.69021 ? 136 MET   C CB    1 
ATOM   5024 C  CG    . MET   D 2 137 ? 9.13800   40.67100  75.28500  1.000 25.00563 ? 136 MET   C CG    1 
ATOM   5025 S  SD    . MET   D 2 137 ? 10.43800  40.54100  74.00100  1.000 24.84640 ? 136 MET   C SD    1 
ATOM   5026 C  CE    . MET   D 2 137 ? 9.78900   39.15800  73.05800  1.000 25.07159 ? 136 MET   C CE    1 
ATOM   5027 N  N     . ASN   D 2 138 ? 6.28900   43.73400  75.16800  1.000 21.18731 ? 137 ASN   C N     1 
ATOM   5028 C  CA    . ASN   D 2 138 ? 4.89100   43.71000  74.74100  1.000 21.37564 ? 137 ASN   C CA    1 
ATOM   5029 C  C     . ASN   D 2 138 ? 4.72100   44.27900  73.33300  1.000 21.13588 ? 137 ASN   C C     1 
ATOM   5030 O  O     . ASN   D 2 138 ? 3.81900   43.85900  72.59900  1.000 21.25698 ? 137 ASN   C O     1 
ATOM   5031 C  CB    . ASN   D 2 138 ? 3.99800   44.43900  75.75900  1.000 26.77459 ? 137 ASN   C CB    1 
ATOM   5032 C  CG    . ASN   D 2 138 ? 4.27700   45.92300  75.82500  1.000 26.12249 ? 137 ASN   C CG    1 
ATOM   5033 O  OD1   . ASN   D 2 138 ? 5.43200   46.34200  75.85900  1.000 28.30916 ? 137 ASN   C OD1   1 
ATOM   5034 N  ND2   . ASN   D 2 138 ? 3.21300   46.73100  75.86500  1.000 34.04261 ? 137 ASN   C ND2   1 
ATOM   5035 N  N     . ILE   D 2 139 ? 5.57400   45.22400  72.93600  1.000 20.33419 ? 138 ILE   C N     1 
ATOM   5036 C  CA    . ILE   D 2 139 ? 5.50400   45.76300  71.57900  1.000 21.65347 ? 138 ILE   C CA    1 
ATOM   5037 C  C     . ILE   D 2 139 ? 5.99300   44.73300  70.56700  1.000 22.09498 ? 138 ILE   C C     1 
ATOM   5038 O  O     . ILE   D 2 139 ? 5.40500   44.59000  69.49300  1.000 20.02844 ? 138 ILE   C O     1 
ATOM   5039 C  CB    . ILE   D 2 139 ? 6.28800   47.08300  71.49100  1.000 21.02554 ? 138 ILE   C CB    1 
ATOM   5040 C  CG1   . ILE   D 2 139 ? 5.74600   48.09500  72.49800  1.000 24.49278 ? 138 ILE   C CG1   1 
ATOM   5041 C  CG2   . ILE   D 2 139 ? 6.23200   47.65000  70.10600  1.000 18.97400 ? 138 ILE   C CG2   1 
ATOM   5042 C  CD1   . ILE   D 2 139 ? 4.23700   48.43400  72.38400  1.000 22.95593 ? 138 ILE   C CD1   1 
ATOM   5043 N  N     . VAL   D 2 140 ? 7.04700   43.98000  70.90500  1.000 19.48384 ? 139 VAL   C N     1 
ATOM   5044 C  CA    . VAL   D 2 140 ? 7.47200   42.87600  70.04200  1.000 19.76622 ? 139 VAL   C CA    1 
ATOM   5045 C  C     . VAL   D 2 140 ? 6.35700   41.84800  69.91600  1.000 21.04536 ? 139 VAL   C C     1 
ATOM   5046 O  O     . VAL   D 2 140 ? 6.10100   41.33200  68.82000  1.000 19.41111 ? 139 VAL   C O     1 
ATOM   5047 C  CB    . VAL   D 2 140 ? 8.77000   42.23100  70.56800  1.000 21.71465 ? 139 VAL   C CB    1 
ATOM   5048 C  CG1   . VAL   D 2 140 ? 9.20600   41.03200  69.66000  1.000 21.25436 ? 139 VAL   C CG1   1 
ATOM   5049 C  CG2   . VAL   D 2 140 ? 9.87500   43.26100  70.69800  1.000 19.91069 ? 139 VAL   C CG2   1 
ATOM   5050 N  N     . GLU   D 2 141 ? 5.67600   41.52600  71.02700  1.000 20.50488 ? 140 GLU   C N     1 
ATOM   5051 C  CA    . GLU   D 2 141 ? 4.56700   40.57700  70.94200  1.000 22.03764 ? 140 GLU   C CA    1 
ATOM   5052 C  C     . GLU   D 2 141 ? 3.44400   41.11800  70.05300  1.000 21.34983 ? 140 GLU   C C     1 
ATOM   5053 O  O     . GLU   D 2 141 ? 2.81000   40.35700  69.30800  1.000 22.73216 ? 140 GLU   C O     1 
ATOM   5054 C  CB    . GLU   D 2 141 ? 4.06800   40.23100  72.35200  1.000 23.53719 ? 140 GLU   C CB    1 
ATOM   5055 C  CG    . GLU   D 2 141 ? 5.16100   39.53500  73.16900  1.000 23.37974 ? 140 GLU   C CG    1 
ATOM   5056 C  CD    . GLU   D 2 141 ? 4.88900   39.47300  74.66700  1.000 37.96691 ? 140 GLU   C CD    1 
ATOM   5057 O  OE1   . GLU   D 2 141 ? 3.88700   40.06100  75.11900  1.000 34.27398 ? 140 GLU   C OE1   1 
ATOM   5058 O  OE2   . GLU   D 2 141 ? 5.70700   38.86000  75.38900  1.000 30.98366 ? 140 GLU   C OE2   1 
ATOM   5059 N  N     . ALA   D 2 142 ? 3.22600   42.43700  70.07700  1.000 21.68138 ? 141 ALA   C N     1 
ATOM   5060 C  CA    . ALA   D 2 142 ? 2.22400   43.05200  69.19600  1.000 21.91165 ? 141 ALA   C CA    1 
ATOM   5061 C  C     . ALA   D 2 142 ? 2.62400   42.92800  67.72600  1.000 22.66824 ? 141 ALA   C C     1 
ATOM   5062 O  O     . ALA   D 2 142 ? 1.77400   42.66600  66.85900  1.000 26.31544 ? 141 ALA   C O     1 
ATOM   5063 C  CB    . ALA   D 2 142 ? 2.04100   44.52300  69.56300  1.000 23.03453 ? 141 ALA   C CB    1 
ATOM   5064 N  N     . MET   D 2 143 ? 3.90700   43.12500  67.42500  1.000 19.39892 ? 142 MET   C N     1 
ATOM   5065 C  CA    . MET   D 2 143 ? 4.38400   43.00100  66.04700  1.000 19.02509 ? 142 MET   C CA    1 
ATOM   5066 C  C     . MET   D 2 143 ? 4.17800   41.58800  65.53000  1.000 23.24787 ? 142 MET   C C     1 
ATOM   5067 O  O     . MET   D 2 143 ? 3.85000   41.38400  64.35600  1.000 22.57768 ? 142 MET   C O     1 
ATOM   5068 C  CB    . MET   D 2 143 ? 5.88200   43.28900  66.00800  1.000 19.87996 ? 142 MET   C CB    1 
ATOM   5069 C  CG    . MET   D 2 143 ? 6.28300   44.72400  66.31900  1.000 21.47280 ? 142 MET   C CG    1 
ATOM   5070 S  SD    . MET   D 2 143 ? 8.01900   44.88600  66.71900  1.000 24.27102 ? 142 MET   C SD    1 
ATOM   5071 C  CE    . MET   D 2 143 ? 8.68300   44.18800  65.20500  1.000 23.19845 ? 142 MET   C CE    1 
ATOM   5072 N  N     . GLU   D 2 144 ? 4.38300   40.59300  66.39700  1.000 25.60983 ? 143 GLU   C N     1 
ATOM   5073 C  CA    . GLU   D 2 144 ? 4.29100   39.19800  66.00600  1.000 28.68843 ? 143 GLU   C CA    1 
ATOM   5074 C  C     . GLU   D 2 144 ? 2.92700   38.85900  65.42100  1.000 25.65766 ? 143 GLU   C C     1 
ATOM   5075 O  O     . GLU   D 2 144 ? 2.84000   37.99400  64.54100  1.000 28.67417 ? 143 GLU   C O     1 
ATOM   5076 C  CB    . GLU   D 2 144 ? 4.62400   38.34400  67.23000  1.000 27.26304 ? 143 GLU   C CB    1 
ATOM   5077 C  CG    . GLU   D 2 144 ? 4.96500   36.88700  66.97900  1.000 33.73144 ? 143 GLU   C CG    1 
ATOM   5078 C  CD    . GLU   D 2 144 ? 5.22900   36.18100  68.28700  1.000 28.28170 ? 143 GLU   C CD    1 
ATOM   5079 O  OE1   . GLU   D 2 144 ? 4.78300   36.70700  69.32500  1.000 33.43617 ? 143 GLU   C OE1   1 
ATOM   5080 O  OE2   . GLU   D 2 144 ? 5.87700   35.11700  68.30000  1.000 34.26944 ? 143 GLU   C OE2   1 
ATOM   5081 N  N     . ARG   D 2 145 ? 1.87100   39.55300  65.83300  1.000 26.47805 ? 144 ARG   C N     1 
ATOM   5082 C  CA    . ARG   D 2 145 ? 0.54700   39.24800  65.30700  1.000 30.40011 ? 144 ARG   C CA    1 
ATOM   5083 C  C     . ARG   D 2 145 ? 0.34200   39.70600  63.86700  1.000 30.37503 ? 144 ARG   C C     1 
ATOM   5084 O  O     . ARG   D 2 145 ? -0.61800  39.27800  63.21900  1.000 29.36093 ? 144 ARG   C O     1 
ATOM   5085 C  CB    . ARG   D 2 145 ? -0.52500  39.77800  66.25700  1.000 31.63614 ? 144 ARG   C CB    1 
ATOM   5086 C  CG    . ARG   D 2 145 ? -0.11500  39.53000  67.70300  1.000 36.15764 ? 144 ARG   C CG    1 
ATOM   5087 C  CD    . ARG   D 2 145 ? -1.27300  39.63100  68.71500  1.000 43.61708 ? 144 ARG   C CD    1 
ATOM   5088 N  NE    . ARG   D 2 145 ? -0.76200  40.02200  70.02500  1.000 49.09752 ? 144 ARG   C NE    1 
ATOM   5089 C  CZ    . ARG   D 2 145 ? -0.80400  41.25800  70.50800  1.000 45.00818 ? 144 ARG   C CZ    1 
ATOM   5090 N  NH1   . ARG   D 2 145 ? -1.44800  42.22600  69.87500  1.000 40.85123 ? 144 ARG   C NH1   1 
ATOM   5091 N  NH2   . ARG   D 2 145 ? -0.18700  41.52900  71.65600  1.000 40.23924 ? 144 ARG   C NH2   1 
ATOM   5092 N  N     . PHE   D 2 146 ? 1.23300   40.54100  63.32600  1.000 25.89307 ? 145 PHE   C N     1 
ATOM   5093 C  CA    . PHE   D 2 146 ? 1.15500   40.92400  61.92200  1.000 22.86966 ? 145 PHE   C CA    1 
ATOM   5094 C  C     . PHE   D 2 146 ? 1.88900   39.95200  61.00300  1.000 21.00143 ? 145 PHE   C C     1 
ATOM   5095 O  O     . PHE   D 2 146 ? 1.87000   40.13300  59.78100  1.000 23.60802 ? 145 PHE   C O     1 
ATOM   5096 C  CB    . PHE   D 2 146 ? 1.71000   42.34000  61.70800  1.000 20.96153 ? 145 PHE   C CB    1 
ATOM   5097 C  CG    . PHE   D 2 146 ? 0.89600   43.39700  62.37600  1.000 19.76119 ? 145 PHE   C CG    1 
ATOM   5098 C  CD1   . PHE   D 2 146 ? -0.23800  43.90700  61.75900  1.000 26.61222 ? 145 PHE   C CD1   1 
ATOM   5099 C  CD2   . PHE   D 2 146 ? 1.26100   43.87900  63.62300  1.000 22.56804 ? 145 PHE   C CD2   1 
ATOM   5100 C  CE1   . PHE   D 2 146 ? -1.00900  44.88100  62.39000  1.000 27.17435 ? 145 PHE   C CE1   1 
ATOM   5101 C  CE2   . PHE   D 2 146 ? 0.50800   44.84600  64.24400  1.000 29.20686 ? 145 PHE   C CE2   1 
ATOM   5102 C  CZ    . PHE   D 2 146 ? -0.63100  45.34100  63.62600  1.000 26.46553 ? 145 PHE   C CZ    1 
ATOM   5103 N  N     . GLY   D 2 147 ? 2.52000   38.92600  61.55200  1.000 21.54706 ? 146 GLY   C N     1 
ATOM   5104 C  CA    . GLY   D 2 147 ? 3.27800   37.97700  60.76400  1.000 19.91906 ? 146 GLY   C CA    1 
ATOM   5105 C  C     . GLY   D 2 147 ? 2.44700   36.79000  60.30800  1.000 20.33532 ? 146 GLY   C C     1 
ATOM   5106 O  O     . GLY   D 2 147 ? 1.21800   36.76700  60.41500  1.000 21.95144 ? 146 GLY   C O     1 
ATOM   5107 N  N     . SER   D 2 148 ? 3.14500   35.80400  59.74900  1.000 19.07786 ? 147 SER   C N     1 
ATOM   5108 C  CA    . SER   D 2 148 ? 2.48900   34.62400  59.19100  1.000 20.99109 ? 147 SER   C CA    1 
ATOM   5109 C  C     . SER   D 2 148 ? 3.51000   33.50100  59.09800  1.000 21.03711 ? 147 SER   C C     1 
ATOM   5110 O  O     . SER   D 2 148 ? 4.70000   33.68900  59.37200  1.000 18.80174 ? 147 SER   C O     1 
ATOM   5111 C  CB    . SER   D 2 148 ? 1.92800   34.92800  57.80900  1.000 20.05107 ? 147 SER   C CB    1 
ATOM   5112 O  OG    . SER   D 2 148 ? 2.97200   35.21500  56.90800  1.000 21.10360 ? 147 SER   C OG    1 
ATOM   5113 N  N     . ARG   D 2 149 ? 3.02900   32.33000  58.66700  1.000 21.30636 ? 148 ARG   C N     1 
ATOM   5114 C  CA    . ARG   D 2 149 ? 3.86700   31.13300  58.57900  1.000 20.49039 ? 148 ARG   C CA    1 
ATOM   5115 C  C     . ARG   D 2 149 ? 5.11600   31.34800  57.72300  1.000 21.66145 ? 148 ARG   C C     1 
ATOM   5116 O  O     . ARG   D 2 149 ? 6.19700   30.84100  58.05500  1.000 22.92279 ? 148 ARG   C O     1 
ATOM   5117 C  CB    . ARG   D 2 149 ? 3.01600   29.98800  58.01100  1.000 23.41948 ? 148 ARG   C CB    1 
ATOM   5118 C  CG    . ARG   D 2 149 ? 3.76100   28.69300  57.78700  1.000 24.31818 ? 148 ARG   C CG    1 
ATOM   5119 C  CD    . ARG   D 2 149 ? 2.79700   27.51500  57.53200  1.000 24.70640 ? 148 ARG   C CD    1 
ATOM   5120 N  NE    . ARG   D 2 149 ? 3.55800   26.29500  57.30500  1.000 23.85569 ? 148 ARG   C NE    1 
ATOM   5121 C  CZ    . ARG   D 2 149 ? 4.19200   25.62600  58.26200  1.000 23.49873 ? 148 ARG   C CZ    1 
ATOM   5122 N  NH1   . ARG   D 2 149 ? 4.08000   25.97600  59.53400  1.000 26.09499 ? 148 ARG   C NH1   1 
ATOM   5123 N  NH2   . ARG   D 2 149 ? 4.97000   24.59800  57.93700  1.000 25.14746 ? 148 ARG   C NH2   1 
ATOM   5124 N  N     . ASN   D 2 150 ? 4.98800   32.06700  56.61200  1.000 20.57380 ? 149 ASN   C N     1 
ATOM   5125 C  CA    . ASN   D 2 150 ? 6.14300   32.32400  55.75400  1.000 20.10381 ? 149 ASN   C CA    1 
ATOM   5126 C  C     . ASN   D 2 150 ? 6.81700   33.65000  56.04900  1.000 21.88794 ? 149 ASN   C C     1 
ATOM   5127 O  O     . ASN   D 2 150 ? 7.67700   34.08900  55.26300  1.000 22.87963 ? 149 ASN   C O     1 
ATOM   5128 C  CB    . ASN   D 2 150 ? 5.80000   32.17300  54.26800  1.000 22.70091 ? 149 ASN   C CB    1 
ATOM   5129 C  CG    . ASN   D 2 150 ? 4.91200   33.26100  53.74800  1.000 23.25800 ? 149 ASN   C CG    1 
ATOM   5130 O  OD1   . ASN   D 2 150 ? 4.52100   34.18600  54.46200  1.000 22.51361 ? 149 ASN   C OD1   1 
ATOM   5131 N  ND2   . ASN   D 2 150 ? 4.56000   33.16000  52.45800  1.000 27.79405 ? 149 ASN   C ND2   1 
ATOM   5132 N  N     . GLY   D 2 151 ? 6.41000   34.32700  57.11800  1.000 18.09775 ? 150 GLY   C N     1 
ATOM   5133 C  CA    . GLY   D 2 151 ? 7.01200   35.58600  57.50700  1.000 17.67375 ? 150 GLY   C CA    1 
ATOM   5134 C  C     . GLY   D 2 151 ? 6.44600   36.82900  56.85700  1.000 17.95168 ? 150 GLY   C C     1 
ATOM   5135 O  O     . GLY   D 2 151 ? 6.78200   37.92000  57.30000  1.000 18.39884 ? 150 GLY   C O     1 
ATOM   5136 N  N     . LYS   D 2 152 ? 5.61600   36.71200  55.82600  1.000 18.46910 ? 151 LYS   C N     1 
ATOM   5137 C  CA    . LYS   D 2 152 ? 5.06400   37.92100  55.21900  1.000 19.14932 ? 151 LYS   C CA    1 
ATOM   5138 C  C     . LYS   D 2 152 ? 4.12300   38.61100  56.20200  1.000 20.89178 ? 151 LYS   C C     1 
ATOM   5139 O  O     . LYS   D 2 152 ? 3.38400   37.96100  56.94100  1.000 19.84452 ? 151 LYS   C O     1 
ATOM   5140 C  CB    . LYS   D 2 152 ? 4.33100   37.61800  53.91200  1.000 22.89107 ? 151 LYS   C CB    1 
ATOM   5141 C  CG    . LYS   D 2 152 ? 5.23200   37.06300  52.78200  1.000 29.62660 ? 151 LYS   C CG    1 
ATOM   5142 C  CD    . LYS   D 2 152 ? 6.38200   38.02300  52.43000  1.000 32.19053 ? 151 LYS   C CD    1 
ATOM   5143 C  CE    . LYS   D 2 152 ? 7.21200   37.52100  51.22000  1.000 39.12471 ? 151 LYS   C CE    1 
ATOM   5144 N  NZ    . LYS   D 2 152 ? 8.45300   38.34200  51.00400  1.000 40.98394 ? 151 LYS   C NZ    1 
ATOM   5145 N  N     . THR   D 2 153 ? 4.17100   39.93700  56.22300  1.000 21.30361 ? 152 THR   C N     1 
ATOM   5146 C  CA    . THR   D 2 153 ? 3.40400   40.74200  57.16400  1.000 21.99849 ? 152 THR   C CA    1 
ATOM   5147 C  C     . THR   D 2 153 ? 2.16100   41.33200  56.49000  1.000 24.20225 ? 152 THR   C C     1 
ATOM   5148 O  O     . THR   D 2 153 ? 2.14600   41.60800  55.28300  1.000 25.07348 ? 152 THR   C O     1 
ATOM   5149 C  CB    . THR   D 2 153 ? 4.27400   41.85300  57.78500  1.000 19.75972 ? 152 THR   C CB    1 
ATOM   5150 O  OG1   . THR   D 2 153 ? 4.69300   42.77200  56.77300  1.000 23.97985 ? 152 THR   C OG1   1 
ATOM   5151 C  CG2   . THR   D 2 153 ? 5.50900   41.24700  58.39100  1.000 20.51067 ? 152 THR   C CG2   1 
ATOM   5152 N  N     . SER   D 2 154 ? 1.08800   41.45200  57.28400  1.000 23.92905 ? 153 SER   C N     1 
ATOM   5153 C  CA    . SER   D 2 154 ? -0.18100  41.95400  56.77200  1.000 24.59007 ? 153 SER   C CA    1 
ATOM   5154 C  C     . SER   D 2 154 ? -0.23600  43.47600  56.69800  1.000 22.46262 ? 153 SER   C C     1 
ATOM   5155 O  O     . SER   D 2 154 ? -1.07800  44.01900  55.97500  1.000 25.16383 ? 153 SER   C O     1 
ATOM   5156 C  CB    . SER   D 2 154 ? -1.32500  41.41100  57.63000  1.000 27.97239 ? 153 SER   C CB    1 
ATOM   5157 O  OG    . SER   D 2 154 ? -1.16600  41.76800  58.99500  1.000 26.26403 ? 153 SER   C OG    1 
ATOM   5158 N  N     . LYS   D 2 155 ? 0.61900   44.16000  57.45000  1.000 23.61748 ? 154 LYS   C N     1 
ATOM   5159 C  CA    . LYS   D 2 155 ? 0.81200   45.60100  57.37700  1.000 22.11286 ? 154 LYS   C CA    1 
ATOM   5160 C  C     . LYS   D 2 155 ? 2.30800   45.82700  57.41700  1.000 20.64134 ? 154 LYS   C C     1 
ATOM   5161 O  O     . LYS   D 2 155 ? 3.05800   44.94300  57.83800  1.000 22.90907 ? 154 LYS   C O     1 
ATOM   5162 C  CB    . LYS   D 2 155 ? 0.10400   46.34000  58.53500  1.000 21.79359 ? 154 LYS   C CB    1 
ATOM   5163 C  CG    . LYS   D 2 155 ? -1.40100  46.16300  58.46800  1.000 29.19083 ? 154 LYS   C CG    1 
ATOM   5164 C  CD    . LYS   D 2 155 ? -2.15300  47.00800  59.47200  1.000 26.40564 ? 154 LYS   C CD    1 
ATOM   5165 C  CE    . LYS   D 2 155 ? -3.64400  46.97000  59.16700  1.000 31.65644 ? 154 LYS   C CE    1 
ATOM   5166 N  NZ    . LYS   D 2 155 ? -4.41000  47.82800  60.10800  1.000 37.33931 ? 154 LYS   C NZ    1 
ATOM   5167 N  N     . LYS   D 2 156 ? 2.73600   47.00600  56.97700  1.000 21.15866 ? 155 LYS   C N     1 
ATOM   5168 C  CA    . LYS   D 2 156 ? 4.15800   47.31600  56.93300  1.000 21.70095 ? 155 LYS   C CA    1 
ATOM   5169 C  C     . LYS   D 2 156 ? 4.62000   47.70900  58.32700  1.000 20.76632 ? 155 LYS   C C     1 
ATOM   5170 O  O     . LYS   D 2 156 ? 4.16700   48.72200  58.87200  1.000 22.63207 ? 155 LYS   C O     1 
ATOM   5171 C  CB    . LYS   D 2 156 ? 4.43300   48.46900  55.97100  1.000 27.65728 ? 155 LYS   C CB    1 
ATOM   5172 C  CG    . LYS   D 2 156 ? 4.24500   48.13600  54.50000  1.000 34.43137 ? 155 LYS   C CG    1 
ATOM   5173 C  CD    . LYS   D 2 156 ? 4.31600   49.39100  53.66100  1.000 36.70073 ? 155 LYS   C CD    1 
ATOM   5174 C  CE    . LYS   D 2 156 ? 3.91400   49.10700  52.23100  1.000 41.45476 ? 155 LYS   C CE    1 
ATOM   5175 N  NZ    . LYS   D 2 156 ? 3.41500   50.34700  51.58000  1.000 50.41415 ? 155 LYS   C NZ    1 
ATOM   5176 N  N     . ILE   D 2 157 ? 5.54000   46.93300  58.89000  1.000 18.76656 ? 156 ILE   C N     1 
ATOM   5177 C  CA    . ILE   D 2 157 ? 6.06300   47.15300  60.23800  1.000 20.33410 ? 156 ILE   C CA    1 
ATOM   5178 C  C     . ILE   D 2 157 ? 7.45200   47.74900  60.07500  1.000 19.81667 ? 156 ILE   C C     1 
ATOM   5179 O  O     . ILE   D 2 157 ? 8.35200   47.08700  59.54200  1.000 19.94270 ? 156 ILE   C O     1 
ATOM   5180 C  CB    . ILE   D 2 157 ? 6.12100   45.82400  61.00500  1.000 19.14452 ? 156 ILE   C CB    1 
ATOM   5181 C  CG1   . ILE   D 2 157 ? 4.76500   45.09100  60.90100  1.000 21.17709 ? 156 ILE   C CG1   1 
ATOM   5182 C  CG2   . ILE   D 2 157 ? 6.58800   46.06400  62.42800  1.000 21.01194 ? 156 ILE   C CG2   1 
ATOM   5183 C  CD1   . ILE   D 2 157 ? 3.54800   45.83500  61.49000  1.000 23.69072 ? 156 ILE   C CD1   1 
ATOM   5184 N  N     . THR   D 2 158 ? 7.64300   48.99300  60.50400  1.000 20.72995 ? 157 THR   C N     1 
ATOM   5185 C  CA    . THR   D 2 158 ? 8.90500   49.66500  60.23300  1.000 21.32127 ? 157 THR   C CA    1 
ATOM   5186 C  C     . THR   D 2 158 ? 9.50100   50.27800  61.49000  1.000 21.32148 ? 157 THR   C C     1 
ATOM   5187 O  O     . THR   D 2 158 ? 8.83700   50.45900  62.51900  1.000 20.97193 ? 157 THR   C O     1 
ATOM   5188 C  CB    . THR   D 2 158 ? 8.71000   50.77900  59.20900  1.000 25.17264 ? 157 THR   C CB    1 
ATOM   5189 O  OG1   . THR   D 2 158 ? 7.77400   51.74500  59.72200  1.000 24.37540 ? 157 THR   C OG1   1 
ATOM   5190 C  CG2   . THR   D 2 158 ? 8.19800   50.18900  57.86600  1.000 22.50376 ? 157 THR   C CG2   1 
ATOM   5191 N  N     . ILE   D 2 159 ? 10.78000  50.61600  61.37500  1.000 21.50576 ? 158 ILE   C N     1 
ATOM   5192 C  CA    . ILE   D 2 159 ? 11.49300  51.35000  62.41700  1.000 21.49049 ? 158 ILE   C CA    1 
ATOM   5193 C  C     . ILE   D 2 159 ? 11.32600  52.82400  62.08600  1.000 25.60906 ? 158 ILE   C C     1 
ATOM   5194 O  O     . ILE   D 2 159 ? 12.08300  53.38100  61.28500  1.000 28.30879 ? 158 ILE   C O     1 
ATOM   5195 C  CB    . ILE   D 2 159 ? 12.96000  50.92600  62.47800  1.000 20.43054 ? 158 ILE   C CB    1 
ATOM   5196 C  CG1   . ILE   D 2 159 ? 13.01100  49.40300  62.67700  1.000 21.66048 ? 158 ILE   C CG1   1 
ATOM   5197 C  CG2   . ILE   D 2 159 ? 13.72900  51.65500  63.59500  1.000 23.08722 ? 158 ILE   C CG2   1 
ATOM   5198 C  CD1   . ILE   D 2 159 ? 14.38400  48.79500  62.58400  1.000 22.99828 ? 158 ILE   C CD1   1 
ATOM   5199 N  N     . ALA   D 2 160 ? 10.29100  53.45100  62.65900  1.000 22.95828 ? 159 ALA   C N     1 
ATOM   5200 C  CA    . ALA   D 2 160 ? 10.01200  54.85600  62.34700  1.000 24.15881 ? 159 ALA   C CA    1 
ATOM   5201 C  C     . ALA   D 2 160 ? 11.05400  55.80400  62.91400  1.000 26.78150 ? 159 ALA   C C     1 
ATOM   5202 O  O     . ALA   D 2 160 ? 11.25500  56.88000  62.34200  1.000 27.14312 ? 159 ALA   C O     1 
ATOM   5203 C  CB    . ALA   D 2 160 ? 8.63500   55.24900  62.87300  1.000 27.34946 ? 159 ALA   C CB    1 
ATOM   5204 N  N     . ASP   D 2 161 ? 11.69800  55.44100  64.01900  1.000 24.43181 ? 160 ASP   C N     1 
ATOM   5205 C  CA    . ASP   D 2 161 ? 12.81000  56.20000  64.57600  1.000 25.79659 ? 160 ASP   C CA    1 
ATOM   5206 C  C     . ASP   D 2 161 ? 13.64800  55.22600  65.39200  1.000 22.44704 ? 160 ASP   C C     1 
ATOM   5207 O  O     . ASP   D 2 161 ? 13.17700  54.16000  65.77900  1.000 24.08365 ? 160 ASP   C O     1 
ATOM   5208 C  CB    . ASP   D 2 161 ? 12.31400  57.36200  65.44800  1.000 30.33451 ? 160 ASP   C CB    1 
ATOM   5209 C  CG    . ASP   D 2 161 ? 13.40800  58.37300  65.78200  1.000 36.35980 ? 160 ASP   C CG    1 
ATOM   5210 O  OD1   . ASP   D 2 161 ? 14.46900  58.39900  65.11000  1.000 32.63620 ? 160 ASP   C OD1   1 
ATOM   5211 O  OD2   . ASP   D 2 161 ? 13.18400  59.16800  66.71900  1.000 37.72706 ? 160 ASP   C OD2   1 
ATOM   5212 N  N     . CYS   D 2 162 ? 14.90900  55.58700  65.60200  1.000 24.69273 ? 161 CYS   C N     1 
ATOM   5213 C  CA    . CYS   D 2 162 ? 15.84200  54.74300  66.34100  1.000 23.96305 ? 161 CYS   C CA    1 
ATOM   5214 C  C     . CYS   D 2 162 ? 17.04900  55.57300  66.76700  1.000 25.04267 ? 161 CYS   C C     1 
ATOM   5215 O  O     . CYS   D 2 162 ? 17.30800  56.65500  66.23500  1.000 27.27305 ? 161 CYS   C O     1 
ATOM   5216 C  CB    . CYS   D 2 162 ? 16.25200  53.48200  65.54500  1.000 22.48841 ? 161 CYS   C CB    1 
ATOM   5217 S  SG    . CYS   D 2 162 ? 16.90400  53.72200  63.87100  1.000 26.29952 ? 161 CYS   C SG    1 
ATOM   5218 N  N     . GLY   D 2 163 ? 17.75800  55.06300  67.77000  1.000 25.91991 ? 162 GLY   C N     1 
ATOM   5219 C  CA    . GLY   D 2 163 ? 18.93500  55.76000  68.24900  1.000 26.54686 ? 162 GLY   C CA    1 
ATOM   5220 C  C     . GLY   D 2 163 ? 19.35700  55.20800  69.59300  1.000 24.89623 ? 162 GLY   C C     1 
ATOM   5221 O  O     . GLY   D 2 163 ? 18.96100  54.10100  69.98000  1.000 24.74528 ? 162 GLY   C O     1 
ATOM   5222 N  N     . GLN   D 2 164 ? 20.14900  56.01100  70.30500  1.000 25.23417 ? 163 GLN   C N     1 
ATOM   5223 C  CA    . GLN   D 2 164 ? 20.75700  55.59700  71.56000  1.000 24.94536 ? 163 GLN   C CA    1 
ATOM   5224 C  C     . GLN   D 2 164 ? 20.15500  56.34700  72.74200  1.000 27.25945 ? 163 GLN   C C     1 
ATOM   5225 O  O     . GLN   D 2 164 ? 19.93400  57.56400  72.67800  1.000 32.95694 ? 163 GLN   C O     1 
ATOM   5226 C  CB    . GLN   D 2 164 ? 22.27100  55.80200  71.51400  1.000 26.62392 ? 163 GLN   C CB    1 
ATOM   5227 C  CG    . GLN   D 2 164 ? 23.00400  55.16800  72.67700  1.000 27.99968 ? 163 GLN   C CG    1 
ATOM   5228 C  CD    . GLN   D 2 164 ? 24.49800  55.13600  72.46800  1.000 28.36295 ? 163 GLN   C CD    1 
ATOM   5229 O  OE1   . GLN   D 2 164 ? 25.00500  55.56000  71.41700  1.000 29.69817 ? 163 GLN   C OE1   1 
ATOM   5230 N  NE2   . GLN   D 2 164 ? 25.22100  54.67300  73.48100  1.000 29.21354 ? 163 GLN   C NE2   1 
ATOM   5231 N  N     . LEU   D 2 165 ? 19.90000  55.60800  73.82600  1.000 29.13034 ? 164 LEU   C N     1 
ATOM   5232 C  CA    . LEU   D 2 165 ? 19.44100  56.21300  75.06600  1.000 29.25376 ? 164 LEU   C CA    1 
ATOM   5233 C  C     . LEU   D 2 165 ? 20.62600  56.44000  75.99300  1.000 39.70260 ? 164 LEU   C C     1 
ATOM   5234 O  O     . LEU   D 2 165 ? 21.36400  55.49000  76.27500  1.000 39.40199 ? 164 LEU   C O     1 
ATOM   5235 C  CB    . LEU   D 2 165 ? 18.39900  55.31400  75.74400  1.000 29.79716 ? 164 LEU   C CB    1 
ATOM   5236 C  CG    . LEU   D 2 165 ? 17.10400  55.11900  74.94900  1.000 31.81647 ? 164 LEU   C CG    1 
ATOM   5237 C  CD1   . LEU   D 2 165 ? 16.16800  54.09700  75.59000  1.000 33.40707 ? 164 LEU   C CD1   1 
ATOM   5238 C  CD2   . LEU   D 2 165 ? 16.42100  56.45600  74.80200  1.000 35.97529 ? 164 LEU   C CD2   1 
HETATM 5239 P  PG    . GNP   E 3 .   ? 15.35900  18.42100  -2.69700  1.000 16.53243 ? 201 GNP   A PG    1 
HETATM 5240 O  O1G   . GNP   E 3 .   ? 16.83200  18.44100  -2.48500  1.000 17.79366 ? 201 GNP   A O1G   1 
HETATM 5241 O  O2G   . GNP   E 3 .   ? 14.80700  19.77400  -2.39400  1.000 18.83500 ? 201 GNP   A O2G   1 
HETATM 5242 O  O3G   . GNP   E 3 .   ? 14.76400  17.40000  -1.76100  1.000 19.62193 ? 201 GNP   A O3G   1 
HETATM 5243 N  N3B   . GNP   E 3 .   ? 15.04900  18.01100  -4.25000  1.000 16.33462 ? 201 GNP   A N3B   1 
HETATM 5244 P  PB    . GNP   E 3 .   ? 15.81100  18.56900  -5.59200  1.000 15.00199 ? 201 GNP   A PB    1 
HETATM 5245 O  O1B   . GNP   E 3 .   ? 17.30200  18.50700  -5.43100  1.000 15.21245 ? 201 GNP   A O1B   1 
HETATM 5246 O  O2B   . GNP   E 3 .   ? 15.21400  19.84000  -6.10400  1.000 15.45506 ? 201 GNP   A O2B   1 
HETATM 5247 O  O3A   . GNP   E 3 .   ? 15.45300  17.46800  -6.69700  1.000 16.72113 ? 201 GNP   A O3A   1 
HETATM 5248 P  PA    . GNP   E 3 .   ? 16.33100  16.28400  -7.32200  1.000 15.78800 ? 201 GNP   A PA    1 
HETATM 5249 O  O1A   . GNP   E 3 .   ? 16.67700  15.31000  -6.25300  1.000 16.63840 ? 201 GNP   A O1A   1 
HETATM 5250 O  O2A   . GNP   E 3 .   ? 17.44800  16.85900  -8.11600  1.000 16.96036 ? 201 GNP   A O2A   1 
HETATM 5251 O  "O5'" . GNP   E 3 .   ? 15.28000  15.63500  -8.33500  1.000 16.85371 ? 201 GNP   A "O5'" 1 
HETATM 5252 C  "C5'" . GNP   E 3 .   ? 14.08000  15.01800  -7.81700  1.000 16.74365 ? 201 GNP   A "C5'" 1 
HETATM 5253 C  "C4'" . GNP   E 3 .   ? 13.59000  13.98800  -8.80500  1.000 19.37372 ? 201 GNP   A "C4'" 1 
HETATM 5254 O  "O4'" . GNP   E 3 .   ? 13.34700  14.62800  -10.08200 1.000 18.31837 ? 201 GNP   A "O4'" 1 
HETATM 5255 C  "C3'" . GNP   E 3 .   ? 14.54700  12.82700  -9.10200  1.000 20.66441 ? 201 GNP   A "C3'" 1 
HETATM 5256 O  "O3'" . GNP   E 3 .   ? 13.81700  11.62400  -9.29800  1.000 22.28597 ? 201 GNP   A "O3'" 1 
HETATM 5257 C  "C2'" . GNP   E 3 .   ? 15.23400  13.27600  -10.39100 1.000 21.48140 ? 201 GNP   A "C2'" 1 
HETATM 5258 O  "O2'" . GNP   E 3 .   ? 15.72100  12.22000  -11.18400 1.000 22.43296 ? 201 GNP   A "O2'" 1 
HETATM 5259 C  "C1'" . GNP   E 3 .   ? 14.09400  13.99700  -11.09300 1.000 17.74615 ? 201 GNP   A "C1'" 1 
HETATM 5260 N  N9    . GNP   E 3 .   ? 14.54700  15.01700  -12.02500 1.000 18.89884 ? 201 GNP   A N9    1 
HETATM 5261 C  C8    . GNP   E 3 .   ? 15.34900  16.09100  -11.73900 1.000 18.06144 ? 201 GNP   A C8    1 
HETATM 5262 N  N7    . GNP   E 3 .   ? 15.59100  16.84100  -12.78300 1.000 16.93202 ? 201 GNP   A N7    1 
HETATM 5263 C  C5    . GNP   E 3 .   ? 14.90900  16.21800  -13.82000 1.000 18.72329 ? 201 GNP   A C5    1 
HETATM 5264 C  C6    . GNP   E 3 .   ? 14.80400  16.57300  -15.18400 1.000 22.60098 ? 201 GNP   A C6    1 
HETATM 5265 O  O6    . GNP   E 3 .   ? 15.30400  17.53900  -15.76700 1.000 21.87441 ? 201 GNP   A O6    1 
HETATM 5266 N  N1    . GNP   E 3 .   ? 14.01200  15.66500  -15.88400 1.000 22.73270 ? 201 GNP   A N1    1 
HETATM 5267 C  C2    . GNP   E 3 .   ? 13.40400  14.56100  -15.34500 1.000 21.33593 ? 201 GNP   A C2    1 
HETATM 5268 N  N2    . GNP   E 3 .   ? 12.68700  13.80600  -16.18700 1.000 25.17299 ? 201 GNP   A N2    1 
HETATM 5269 N  N3    . GNP   E 3 .   ? 13.50100  14.22000  -14.06300 1.000 21.73855 ? 201 GNP   A N3    1 
HETATM 5270 C  C4    . GNP   E 3 .   ? 14.26500  15.09200  -13.36400 1.000 18.00276 ? 201 GNP   A C4    1 
HETATM 5271 MG MG    . MG    F 4 .   ? 18.40700  18.11700  -3.72600  1.000 13.92763 ? 202 MG    A MG    1 
HETATM 5272 C  C1    . A1AOD G 5 .   ? 14.86600  15.22000  11.70600  1.000 13.04099 ? 203 A1AOD A C1    1 
HETATM 5273 C  C10   . A1AOD G 5 .   ? 11.18500  14.75900  2.00400   1.000 22.66280 ? 203 A1AOD A C10   1 
HETATM 5274 C  C11   . A1AOD G 5 .   ? 10.40000  14.30400  0.78000   1.000 22.81914 ? 203 A1AOD A C11   1 
HETATM 5275 C  C12   . A1AOD G 5 .   ? 10.73400  15.22600  -0.39200  1.000 25.75154 ? 203 A1AOD A C12   1 
HETATM 5276 C  C13   . A1AOD G 5 .   ? 8.97800   16.85000  -0.59500  1.000 32.68115 ? 203 A1AOD A C13   1 
HETATM 5277 C  C14   . A1AOD G 5 .   ? 8.17100   18.01100  -0.22400  1.000 40.18685 ? 203 A1AOD A C14   1 
HETATM 5278 C  C15   . A1AOD G 5 .   ? 7.94600   19.12200  -0.90800  1.000 38.77261 ? 203 A1AOD A C15   1 
HETATM 5279 C  C16   . A1AOD G 5 .   ? 7.00000   20.17200  -0.32200  1.000 45.28353 ? 203 A1AOD A C16   1 
HETATM 5280 C  C17   . A1AOD G 5 .   ? 6.49200   19.72900  2.11700   1.000 56.01799 ? 203 A1AOD A C17   1 
HETATM 5281 C  C18   . A1AOD G 5 .   ? 4.93700   18.82500  0.36200   1.000 43.41064 ? 203 A1AOD A C18   1 
HETATM 5282 C  C19   . A1AOD G 5 .   ? 6.13700   20.67100  -1.46800  1.000 41.16291 ? 203 A1AOD A C19   1 
HETATM 5283 C  C2    . A1AOD G 5 .   ? 14.92400  15.49200  10.21100  1.000 13.44622 ? 203 A1AOD A C2    1 
HETATM 5284 C  C20   . A1AOD G 5 .   ? 7.74600   21.31700  0.31400   1.000 43.52148 ? 203 A1AOD A C20   1 
HETATM 5285 C  C21   . A1AOD G 5 .   ? 10.79700  17.14600  1.08800   1.000 32.06868 ? 203 A1AOD A C21   1 
HETATM 5286 C  C22   . A1AOD G 5 .   ? 10.90000  16.22700  2.29500   1.000 23.56197 ? 203 A1AOD A C22   1 
HETATM 5287 C  C23   . A1AOD G 5 .   ? 12.37500  12.16300  2.72400   1.000 20.23587 ? 203 A1AOD A C23   1 
HETATM 5288 C  C24   . A1AOD G 5 .   ? 10.81200  10.75400  4.80200   1.000 15.92726 ? 203 A1AOD A C24   1 
HETATM 5289 C  C25   . A1AOD G 5 .   ? 9.77000   10.28100  3.78900   1.000 17.34388 ? 203 A1AOD A C25   1 
HETATM 5290 C  C26   . A1AOD G 5 .   ? 10.36400  10.24800  6.17100   1.000 17.60359 ? 203 A1AOD A C26   1 
HETATM 5291 C  C27   . A1AOD G 5 .   ? 12.29100  15.89300  7.42500   1.000 15.67700 ? 203 A1AOD A C27   1 
HETATM 5292 C  C28   . A1AOD G 5 .   ? 13.12900  16.56500  6.33500   1.000 17.69233 ? 203 A1AOD A C28   1 
HETATM 5293 C  C29   . A1AOD G 5 .   ? 14.15900  16.22900  4.30100   1.000 20.80342 ? 203 A1AOD A C29   1 
HETATM 5294 C  C3    . A1AOD G 5 .   ? 13.08500  13.56800  11.23400  1.000 14.63663 ? 203 A1AOD A C3    1 
HETATM 5295 C  C30   . A1AOD G 5 .   ? 15.40800  17.01400  4.68800   1.000 18.11734 ? 203 A1AOD A C30   1 
HETATM 5296 C  C31   . A1AOD G 5 .   ? 16.24900  18.65100  6.27300   1.000 13.36720 ? 203 A1AOD A C31   1 
HETATM 5297 C  C32   . A1AOD G 5 .   ? 16.64600  18.85200  7.58500   1.000 14.04981 ? 203 A1AOD A C32   1 
HETATM 5298 C  C33   . A1AOD G 5 .   ? 17.65300  19.75800  7.88400   1.000 12.66052 ? 203 A1AOD A C33   1 
HETATM 5299 C  C34   . A1AOD G 5 .   ? 18.29500  20.46200  6.87800   1.000 12.94023 ? 203 A1AOD A C34   1 
HETATM 5300 C  C35   . A1AOD G 5 .   ? 17.90800  20.24100  5.56100   1.000 14.30306 ? 203 A1AOD A C35   1 
HETATM 5301 C  C36   . A1AOD G 5 .   ? 16.90000  19.34000  5.25600   1.000 13.68896 ? 203 A1AOD A C36   1 
HETATM 5302 C  C37   . A1AOD G 5 .   ? 20.06300  22.17000  6.63500   1.000 14.88046 ? 203 A1AOD A C37   1 
HETATM 5303 C  C38   . A1AOD G 5 .   ? 19.30500  23.47700  6.53300   1.000 19.63538 ? 203 A1AOD A C38   1 
HETATM 5304 C  C39   . A1AOD G 5 .   ? 19.25000  21.12700  8.74600   1.000 15.63771 ? 203 A1AOD A C39   1 
HETATM 5305 C  C4    . A1AOD G 5 .   ? 13.46200  14.77900  12.07400  1.000 13.89155 ? 203 A1AOD A C4    1 
HETATM 5306 C  C40   . A1AOD G 5 .   ? 20.11400  21.87100  9.71100   1.000 14.50404 ? 203 A1AOD A C40   1 
HETATM 5307 C  C41   . A1AOD G 5 .   ? 21.49100  21.71800  9.83900   1.000 15.87584 ? 203 A1AOD A C41   1 
HETATM 5308 C  C42   . A1AOD G 5 .   ? 22.28600  20.78900  9.01600   1.000 15.96927 ? 203 A1AOD A C42   1 
HETATM 5309 C  C43   . A1AOD G 5 .   ? 23.62000  20.82600  7.08400   1.000 15.95196 ? 203 A1AOD A C43   1 
HETATM 5310 C  C44   . A1AOD G 5 .   ? 23.15900  19.91100  9.89800   1.000 20.11295 ? 203 A1AOD A C44   1 
HETATM 5311 C  C45   . A1AOD G 5 .   ? 21.55500  23.33000  11.52300  1.000 19.48975 ? 203 A1AOD A C45   1 
HETATM 5312 C  C46   . A1AOD G 5 .   ? 20.18900  23.51200  11.44100  1.000 17.54976 ? 203 A1AOD A C46   1 
HETATM 5313 C  C47   . A1AOD G 5 .   ? 19.46300  22.78000  10.52700  1.000 17.98419 ? 203 A1AOD A C47   1 
HETATM 5314 C  C48   . A1AOD G 5 .   ? 18.21800  20.12200  9.09600   1.000 13.53841 ? 203 A1AOD A C48   1 
HETATM 5315 C  C49   . A1AOD G 5 .   ? 17.84300  19.66800  10.48800  1.000 14.51195 ? 203 A1AOD A C49   1 
HETATM 5316 C  C5    . A1AOD G 5 .   ? 12.25400  13.97900  8.98600   1.000 14.48960 ? 203 A1AOD A C5    1 
HETATM 5317 C  C50   . A1AOD G 5 .   ? 18.54300  18.45400  11.07700  1.000 13.24389 ? 203 A1AOD A C50   1 
HETATM 5318 C  C51   . A1AOD G 5 .   ? 17.94100  18.23700  12.46000  1.000 14.42636 ? 203 A1AOD A C51   1 
HETATM 5319 C  C52   . A1AOD G 5 .   ? 20.03400  18.64300  11.22500  1.000 15.62089 ? 203 A1AOD A C52   1 
HETATM 5320 C  C53   . A1AOD G 5 .   ? 18.27100  17.22700  10.24400  1.000 14.42827 ? 203 A1AOD A C53   1 
HETATM 5321 C  C54   . A1AOD G 5 .   ? 16.33800  15.79200  9.87600   1.000 15.75287 ? 203 A1AOD A C54   1 
HETATM 5322 C  C55   . A1AOD G 5 .   ? 14.30300  17.28900  6.98500   1.000 16.55021 ? 203 A1AOD A C55   1 
HETATM 5323 C  C6    . A1AOD G 5 .   ? 12.50600  14.38700  7.56700   1.000 15.37838 ? 203 A1AOD A C6    1 
HETATM 5324 C  C7    . A1AOD G 5 .   ? 12.00900  12.72300  5.84300   1.000 16.91621 ? 203 A1AOD A C7    1 
HETATM 5325 C  C8    . A1AOD G 5 .   ? 10.97000  12.28600  4.83900   1.000 17.42188 ? 203 A1AOD A C8    1 
HETATM 5326 C  C9    . A1AOD G 5 .   ? 10.80800  14.00500  3.25800   1.000 21.46742 ? 203 A1AOD A C9    1 
HETATM 5327 F  F1    . A1AOD G 5 .   ? 12.46300  14.60200  1.76800   1.000 23.59153 ? 203 A1AOD A F1    1 
HETATM 5328 N  N1    . A1AOD G 5 .   ? 14.47300  14.32100  9.44800   1.000 14.21434 ? 203 A1AOD A N1    1 
HETATM 5329 N  N2    . A1AOD G 5 .   ? 13.25700  13.96300  9.84900   1.000 13.88360 ? 203 A1AOD A N2    1 
HETATM 5330 N  N3    . A1AOD G 5 .   ? 11.61500  13.67200  6.68100   1.000 14.37554 ? 203 A1AOD A N3    1 
HETATM 5331 N  N4    . A1AOD G 5 .   ? 11.37300  12.83900  3.54200   1.000 17.22778 ? 203 A1AOD A N4    1 
HETATM 5332 N  N5    . A1AOD G 5 .   ? 10.10800  16.46700  0.00700   1.000 25.51800 ? 203 A1AOD A N5    1 
HETATM 5333 N  N6    . A1AOD G 5 .   ? 6.03900   19.72800  0.71700   1.000 54.57215 ? 203 A1AOD A N6    1 
HETATM 5334 N  N7    . A1AOD G 5 .   ? 15.27300  17.69500  5.97300   1.000 17.61637 ? 203 A1AOD A N7    1 
HETATM 5335 N  N8    . A1AOD G 5 .   ? 19.23000  21.25900  7.41200   1.000 14.51644 ? 203 A1AOD A N8    1 
HETATM 5336 N  N9    . A1AOD G 5 .   ? 22.17200  22.45500  10.73200  1.000 18.09802 ? 203 A1AOD A N9    1 
HETATM 5337 O  O1    . A1AOD G 5 .   ? 11.14000  13.67000  9.32200   1.000 15.27272 ? 203 A1AOD A O1    1 
HETATM 5338 O  O2    . A1AOD G 5 .   ? 8.46800   16.17900  -1.45900  1.000 32.02322 ? 203 A1AOD A O2    1 
HETATM 5339 O  O3    . A1AOD G 5 .   ? 10.02000  14.50900  4.02000   1.000 21.16930 ? 203 A1AOD A O3    1 
HETATM 5340 O  O4    . A1AOD G 5 .   ? 13.12600  12.26200  5.84700   1.000 17.20327 ? 203 A1AOD A O4    1 
HETATM 5341 O  O5    . A1AOD G 5 .   ? 13.60000  15.58900  5.43000   1.000 19.18265 ? 203 A1AOD A O5    1 
HETATM 5342 O  O6    . A1AOD G 5 .   ? 23.12300  21.57500  8.18200   1.000 16.33673 ? 203 A1AOD A O6    1 
HETATM 5343 O  O7    . A1AOD G 5 .   ? 16.87900  17.02000  10.34600  1.000 14.03416 ? 203 A1AOD A O7    1 
HETATM 5344 O  O8    . A1AOD G 5 .   ? 17.04100  15.05700  9.24200   1.000 15.20608 ? 203 A1AOD A O8    1 
HETATM 5345 CL CL    . CL    H 6 .   ? 13.21600  18.82500  10.04600  1.000 21.41619 ? 204 CL    A CL    1 
HETATM 5346 P  PG    . GNP   I 3 .   ? 15.00700  29.47400  47.17600  1.000 17.54505 ? 201 GNP   B PG    1 
HETATM 5347 O  O1G   . GNP   I 3 .   ? 13.55500  29.55800  47.48000  1.000 18.87631 ? 201 GNP   B O1G   1 
HETATM 5348 O  O2G   . GNP   I 3 .   ? 15.46900  28.08500  47.42100  1.000 21.03830 ? 201 GNP   B O2G   1 
HETATM 5349 O  O3G   . GNP   I 3 .   ? 15.75000  30.43900  48.05200  1.000 20.81438 ? 201 GNP   B O3G   1 
HETATM 5350 N  N3B   . GNP   I 3 .   ? 15.22100  29.88800  45.60500  1.000 17.24652 ? 201 GNP   B N3B   1 
HETATM 5351 P  PB    . GNP   I 3 .   ? 14.38600  29.32400  44.31200  1.000 15.71213 ? 201 GNP   B PB    1 
HETATM 5352 O  O1B   . GNP   I 3 .   ? 12.90400  29.42600  44.52800  1.000 15.40864 ? 201 GNP   B O1B   1 
HETATM 5353 O  O2B   . GNP   I 3 .   ? 14.92500  28.02900  43.78700  1.000 17.24133 ? 201 GNP   B O2B   1 
HETATM 5354 O  O3A   . GNP   I 3 .   ? 14.69500  30.38200  43.15400  1.000 17.69320 ? 201 GNP   B O3A   1 
HETATM 5355 P  PA    . GNP   I 3 .   ? 13.81700  31.58100  42.56800  1.000 16.47606 ? 201 GNP   B PA    1 
HETATM 5356 O  O1A   . GNP   I 3 .   ? 13.56700  32.56800  43.65300  1.000 17.26375 ? 201 GNP   B O1A   1 
HETATM 5357 O  O2A   . GNP   I 3 .   ? 12.64700  31.00800  41.84800  1.000 17.09119 ? 201 GNP   B O2A   1 
HETATM 5358 O  "O5'" . GNP   I 3 .   ? 14.82300  32.19000  41.48800  1.000 16.44639 ? 201 GNP   B "O5'" 1 
HETATM 5359 C  "C5'" . GNP   I 3 .   ? 16.07200  32.76800  41.91700  1.000 17.28066 ? 201 GNP   B "C5'" 1 
HETATM 5360 C  "C4'" . GNP   I 3 .   ? 16.53400  33.76200  40.88000  1.000 19.51330 ? 201 GNP   B "C4'" 1 
HETATM 5361 O  "O4'" . GNP   I 3 .   ? 16.70500  33.08200  39.60900  1.000 19.99812 ? 201 GNP   B "O4'" 1 
HETATM 5362 C  "C3'" . GNP   I 3 .   ? 15.58600  34.93600  40.60300  1.000 20.94929 ? 201 GNP   B "C3'" 1 
HETATM 5363 O  "O3'" . GNP   I 3 .   ? 16.30900  36.13300  40.36000  1.000 20.92257 ? 201 GNP   B "O3'" 1 
HETATM 5364 C  "C2'" . GNP   I 3 .   ? 14.84200  34.48500  39.34500  1.000 19.87814 ? 201 GNP   B "C2'" 1 
HETATM 5365 O  "O2'" . GNP   I 3 .   ? 14.35400  35.55500  38.56900  1.000 21.40146 ? 201 GNP   B "O2'" 1 
HETATM 5366 C  "C1'" . GNP   I 3 .   ? 15.93200  33.70900  38.61500  1.000 18.57463 ? 201 GNP   B "C1'" 1 
HETATM 5367 N  N9    . GNP   I 3 .   ? 15.40000  32.69100  37.72100  1.000 17.96033 ? 201 GNP   B N9    1 
HETATM 5368 C  C8    . GNP   I 3 .   ? 14.52600  31.68900  38.05100  1.000 16.60025 ? 201 GNP   B C8    1 
HETATM 5369 N  N7    . GNP   I 3 .   ? 14.19900  30.93200  37.03500  1.000 17.14099 ? 201 GNP   B N7    1 
HETATM 5370 C  C5    . GNP   I 3 .   ? 14.90400  31.46900  35.96800  1.000 17.89417 ? 201 GNP   B C5    1 
HETATM 5371 C  C6    . GNP   I 3 .   ? 14.95000  31.06300  34.61400  1.000 21.44296 ? 201 GNP   B C6    1 
HETATM 5372 O  O6    . GNP   I 3 .   ? 14.35800  30.12300  34.07500  1.000 19.57593 ? 201 GNP   B O6    1 
HETATM 5373 N  N1    . GNP   I 3 .   ? 15.79200  31.88700  33.87000  1.000 19.18401 ? 201 GNP   B N1    1 
HETATM 5374 C  C2    . GNP   I 3 .   ? 16.49700  32.95500  34.36100  1.000 21.79389 ? 201 GNP   B C2    1 
HETATM 5375 N  N2    . GNP   I 3 .   ? 17.25600  33.62400  33.48600  1.000 20.54675 ? 201 GNP   B N2    1 
HETATM 5376 N  N3    . GNP   I 3 .   ? 16.45600  33.34100  35.63300  1.000 19.78599 ? 201 GNP   B N3    1 
HETATM 5377 C  C4    . GNP   I 3 .   ? 15.64400  32.55500  36.37700  1.000 17.48907 ? 201 GNP   B C4    1 
HETATM 5378 MG MG    . MG    J 4 .   ? 11.91700  29.82100  46.29900  1.000 14.99298 ? 202 MG    B MG    1 
HETATM 5379 C  C1    . A1AOD K 5 .   ? 15.95200  32.86000  61.71200  1.000 17.81815 ? 203 A1AOD B C1    1 
HETATM 5380 C  C10   . A1AOD K 5 .   ? 19.39500  33.28200  51.96500  1.000 26.42208 ? 203 A1AOD B C10   1 
HETATM 5381 C  C11   . A1AOD K 5 .   ? 19.61800  31.82900  52.32600  1.000 25.47225 ? 203 A1AOD B C11   1 
HETATM 5382 C  C12   . A1AOD K 5 .   ? 19.19900  30.94700  51.17300  1.000 32.97636 ? 203 A1AOD B C12   1 
HETATM 5383 C  C13   . A1AOD K 5 .   ? 20.99900  30.44200  49.66300  1.000 34.33788 ? 203 A1AOD B C13   1 
HETATM 5384 C  C14   . A1AOD K 5 .   ? 21.86800  30.82600  48.54900  1.000 35.56557 ? 203 A1AOD B C14   1 
HETATM 5385 C  C15   . A1AOD K 5 .   ? 22.08100  30.04100  47.48300  1.000 43.00832 ? 203 A1AOD B C15   1 
HETATM 5386 C  C16   . A1AOD K 5 .   ? 23.00200  30.57300  46.42000  1.000 48.29841 ? 203 A1AOD B C16   1 
HETATM 5387 C  C17   . A1AOD K 5 .   ? 24.92000  29.31700  47.16400  1.000 41.89864 ? 203 A1AOD B C17   1 
HETATM 5388 C  C18   . A1AOD K 5 .   ? 24.70200  29.93200  44.84800  1.000 49.97482 ? 203 A1AOD B C18   1 
HETATM 5389 C  C19   . A1AOD K 5 .   ? 22.16100  30.95300  45.20400  1.000 45.84499 ? 203 A1AOD B C19   1 
HETATM 5390 C  C2    . A1AOD K 5 .   ? 15.88600  32.57400  60.22500  1.000 16.70461 ? 203 A1AOD B C2    1 
HETATM 5391 C  C20   . A1AOD K 5 .   ? 23.77200  31.77200  46.95500  1.000 47.61934 ? 203 A1AOD B C20   1 
HETATM 5392 C  C21   . A1AOD K 5 .   ? 19.89000  32.65000  49.56000  1.000 26.99612 ? 203 A1AOD B C21   1 
HETATM 5393 C  C22   . A1AOD K 5 .   ? 20.17800  33.63200  50.70100  1.000 27.64696 ? 203 A1AOD B C22   1 
HETATM 5394 C  C23   . A1AOD K 5 .   ? 18.19700  35.84600  52.71800  1.000 22.59054 ? 203 A1AOD B C23   1 
HETATM 5395 C  C24   . A1AOD K 5 .   ? 19.84200  37.26200  54.72600  1.000 19.95759 ? 203 A1AOD B C24   1 
HETATM 5396 C  C25   . A1AOD K 5 .   ? 20.84100  37.70100  53.66600  1.000 20.19332 ? 203 A1AOD B C25   1 
HETATM 5397 C  C26   . A1AOD K 5 .   ? 20.39100  37.73100  56.06700  1.000 22.00956 ? 203 A1AOD B C26   1 
HETATM 5398 C  C27   . A1AOD K 5 .   ? 18.42400  32.12500  57.41100  1.000 18.47953 ? 203 A1AOD B C27   1 
HETATM 5399 C  C28   . A1AOD K 5 .   ? 17.58000  31.48500  56.30900  1.000 19.47179 ? 203 A1AOD B C28   1 
HETATM 5400 C  C29   . A1AOD K 5 .   ? 16.46200  31.87500  54.31800  1.000 20.10866 ? 203 A1AOD B C29   1 
HETATM 5401 C  C3    . A1AOD K 5 .   ? 17.79100  34.46800  61.21100  1.000 18.16912 ? 203 A1AOD B C3    1 
HETATM 5402 C  C30   . A1AOD K 5 .   ? 15.21100  31.10400  54.71900  1.000 19.79047 ? 203 A1AOD B C30   1 
HETATM 5403 C  C31   . A1AOD K 5 .   ? 14.41700  29.43100  56.31400  1.000 17.85645 ? 203 A1AOD B C31   1 
HETATM 5404 C  C32   . A1AOD K 5 .   ? 14.06400  29.23200  57.64500  1.000 16.52347 ? 203 A1AOD B C32   1 
HETATM 5405 C  C33   . A1AOD K 5 .   ? 13.07800  28.30900  57.97600  1.000 16.41418 ? 203 A1AOD B C33   1 
HETATM 5406 C  C34   . A1AOD K 5 .   ? 12.41800  27.59200  56.99200  1.000 16.92971 ? 203 A1AOD B C34   1 
HETATM 5407 C  C35   . A1AOD K 5 .   ? 12.76000  27.80600  55.66400  1.000 18.75588 ? 203 A1AOD B C35   1 
HETATM 5408 C  C36   . A1AOD K 5 .   ? 13.74600  28.72000  55.32500  1.000 17.66423 ? 203 A1AOD B C36   1 
HETATM 5409 C  C37   . A1AOD K 5 .   ? 10.65500  25.86300  56.81200  1.000 19.09356 ? 203 A1AOD B C37   1 
HETATM 5410 C  C38   . A1AOD K 5 .   ? 11.34600  24.51800  56.74900  1.000 21.08293 ? 203 A1AOD B C38   1 
HETATM 5411 C  C39   . A1AOD K 5 .   ? 11.52900  26.91500  58.88000  1.000 18.09381 ? 203 A1AOD B C39   1 
HETATM 5412 C  C4    . A1AOD K 5 .   ? 17.35400  33.30300  62.08800  1.000 19.54665 ? 203 A1AOD B C4    1 
HETATM 5413 C  C40   . A1AOD K 5 .   ? 10.70600  26.17800  59.88600  1.000 19.18898 ? 203 A1AOD B C40   1 
HETATM 5414 C  C41   . A1AOD K 5 .   ? 9.34300   26.35900  60.08600  1.000 20.24010 ? 203 A1AOD B C41   1 
HETATM 5415 C  C42   . A1AOD K 5 .   ? 8.53600   27.29700  59.28500  1.000 18.36887 ? 203 A1AOD B C42   1 
HETATM 5416 C  C43   . A1AOD K 5 .   ? 7.21700   27.28000  57.33900  1.000 19.54183 ? 203 A1AOD B C43   1 
HETATM 5417 C  C44   . A1AOD K 5 .   ? 7.65100   28.14400  60.19200  1.000 19.61595 ? 203 A1AOD B C44   1 
HETATM 5418 C  C45   . A1AOD K 5 .   ? 9.35500   24.77600  61.79100  1.000 20.03067 ? 203 A1AOD B C45   1 
HETATM 5419 C  C46   . A1AOD K 5 .   ? 10.70500  24.55400  61.64000  1.000 20.09927 ? 203 A1AOD B C46   1 
HETATM 5420 C  C47   . A1AOD K 5 .   ? 11.38100  25.26700  60.67900  1.000 17.79394 ? 203 A1AOD B C47   1 
HETATM 5421 C  C48   . A1AOD K 5 .   ? 12.55100  27.93800  59.20500  1.000 16.05904 ? 203 A1AOD B C48   1 
HETATM 5422 C  C49   . A1AOD K 5 .   ? 12.95300  28.39100  60.59300  1.000 16.49478 ? 203 A1AOD B C49   1 
HETATM 5423 C  C5    . A1AOD K 5 .   ? 18.55900  34.06000  58.93700  1.000 20.73483 ? 203 A1AOD B C5    1 
HETATM 5424 C  C50   . A1AOD K 5 .   ? 12.29500  29.61000  61.22000  1.000 16.42855 ? 203 A1AOD B C50   1 
HETATM 5425 C  C51   . A1AOD K 5 .   ? 12.94400  29.81000  62.57900  1.000 18.17092 ? 203 A1AOD B C51   1 
HETATM 5426 C  C52   . A1AOD K 5 .   ? 10.80900  29.41500  61.41400  1.000 15.61864 ? 203 A1AOD B C52   1 
HETATM 5427 C  C53   . A1AOD K 5 .   ? 12.52500  30.85400  60.39400  1.000 16.99927 ? 203 A1AOD B C53   1 
HETATM 5428 C  C54   . A1AOD K 5 .   ? 14.46200  32.29400  59.90400  1.000 15.37737 ? 203 A1AOD B C54   1 
HETATM 5429 C  C55   . A1AOD K 5 .   ? 16.41300  30.74100  56.95800  1.000 20.41963 ? 203 A1AOD B C55   1 
HETATM 5430 C  C6    . A1AOD K 5 .   ? 18.23800  33.63200  57.53400  1.000 17.37412 ? 203 A1AOD B C6    1 
HETATM 5431 C  C7    . A1AOD K 5 .   ? 18.68300  35.31800  55.82600  1.000 17.49827 ? 203 A1AOD B C7    1 
HETATM 5432 C  C8    . A1AOD K 5 .   ? 19.68600  35.73900  54.78000  1.000 20.88254 ? 203 A1AOD B C8    1 
HETATM 5433 C  C9    . A1AOD K 5 .   ? 19.86000  34.07100  53.15700  1.000 21.06368 ? 203 A1AOD B C9    1 
HETATM 5434 F  F1    . A1AOD K 5 .   ? 18.11300  33.47500  51.78100  1.000 25.92124 ? 203 A1AOD B F1    1 
HETATM 5435 N  N1    . A1AOD K 5 .   ? 16.35600  33.73500  59.46000  1.000 16.77776 ? 203 A1AOD B N1    1 
HETATM 5436 N  N2    . A1AOD K 5 .   ? 17.58400  34.07300  59.83300  1.000 18.52546 ? 203 A1AOD B N2    1 
HETATM 5437 N  N3    . A1AOD K 5 .   ? 19.08500  34.31300  56.58200  1.000 20.06249 ? 203 A1AOD B N3    1 
HETATM 5438 N  N4    . A1AOD K 5 .   ? 19.25600  35.20100  53.48600  1.000 19.24730 ? 203 A1AOD B N4    1 
HETATM 5439 N  N5    . A1AOD K 5 .   ? 20.08900  31.31100  50.09000  1.000 26.98487 ? 203 A1AOD B N5    1 
HETATM 5440 N  N6    . A1AOD K 5 .   ? 23.97400  29.53200  46.06200  1.000 53.92489 ? 203 A1AOD B N6    1 
HETATM 5441 N  N7    . A1AOD K 5 .   ? 15.38600  30.39500  55.98000  1.000 19.93687 ? 203 A1AOD B N7    1 
HETATM 5442 N  N8    . A1AOD K 5 .   ? 11.51100  26.78200  57.55200  1.000 17.26682 ? 203 A1AOD B N8    1 
HETATM 5443 N  N9    . A1AOD K 5 .   ? 8.70500   25.64200  61.02300  1.000 20.50088 ? 203 A1AOD B N9    1 
HETATM 5444 O  O1    . A1AOD K 5 .   ? 19.69000  34.38200  59.22700  1.000 19.60206 ? 203 A1AOD B O1    1 
HETATM 5445 O  O2    . A1AOD K 5 .   ? 21.12800  29.33600  50.14300  1.000 33.24746 ? 203 A1AOD B O2    1 
HETATM 5446 O  O3    . A1AOD K 5 .   ? 20.75000  33.60800  53.83000  1.000 26.65520 ? 203 A1AOD B O3    1 
HETATM 5447 O  O4    . A1AOD K 5 .   ? 17.59500  35.83700  55.92900  1.000 20.00501 ? 203 A1AOD B O4    1 
HETATM 5448 O  O5    . A1AOD K 5 .   ? 17.10200  32.47900  55.42900  1.000 20.44671 ? 203 A1AOD B O5    1 
HETATM 5449 O  O6    . A1AOD K 5 .   ? 7.72800   26.51500  58.41800  1.000 17.91998 ? 203 A1AOD B O6    1 
HETATM 5450 O  O7    . A1AOD K 5 .   ? 13.91500  31.10100  60.46500  1.000 16.70574 ? 203 A1AOD B O7    1 
HETATM 5451 O  O8    . A1AOD K 5 .   ? 13.77400  33.01400  59.22500  1.000 17.42813 ? 203 A1AOD B O8    1 
HETATM 5452 CL CL    . CL    L 6 .   ? 17.52900  29.27000  60.06000  1.000 25.37084 ? 204 CL    B CL    1 
HETATM 5453 O  O     . HOH   M 7 .   ? 7.38600   33.33700  1.75800   1.000 46.73622 ? 301 HOH   A O     1 
HETATM 5454 O  O     . HOH   M 7 .   ? 41.06700  33.76200  -16.83900 1.000 28.69164 ? 302 HOH   A O     1 
HETATM 5455 O  O     . HOH   M 7 .   ? 6.98700   39.07400  -4.74000  1.000 34.53414 ? 303 HOH   A O     1 
HETATM 5456 O  O     . HOH   M 7 .   ? 6.36600   23.60600  -3.06800  1.000 37.04802 ? 304 HOH   A O     1 
HETATM 5457 O  O     . HOH   M 7 .   ? 5.562     13.221    -16.900   1.000 39.63411 ? 305 HOH   A O     1 
HETATM 5458 O  O     . HOH   M 7 .   ? 21.97300  16.32300  -2.32700  1.000 31.86415 ? 306 HOH   A O     1 
HETATM 5459 O  O     . HOH   M 7 .   ? 23.51500  41.42500  -12.70300 1.000 38.91897 ? 307 HOH   A O     1 
HETATM 5460 O  O     . HOH   M 7 .   ? 9.184     40.312    1.560     1.000 42.52612 ? 308 HOH   A O     1 
HETATM 5461 O  O     . HOH   M 7 .   ? 6.49900   37.81900  -8.09600  1.000 39.90636 ? 309 HOH   A O     1 
HETATM 5462 O  O     . HOH   M 7 .   ? 12.66200  43.06500  -17.75500 1.000 40.13622 ? 310 HOH   A O     1 
HETATM 5463 O  O     . HOH   M 7 .   ? 8.26000   36.40900  1.61900   1.000 40.11333 ? 311 HOH   A O     1 
HETATM 5464 O  O     . HOH   M 7 .   ? 21.87800  41.76400  -10.20200 1.000 37.59314 ? 312 HOH   A O     1 
HETATM 5465 O  O     . HOH   M 7 .   ? 10.60000  24.62600  -20.55800 1.000 31.10416 ? 313 HOH   A O     1 
HETATM 5466 O  O     . HOH   M 7 .   ? 19.02500  20.06900  -3.52700  1.000 16.65649 ? 314 HOH   A O     1 
HETATM 5467 O  O     . HOH   M 7 .   ? 23.58900  17.19900  -4.53400  1.000 34.90362 ? 315 HOH   A O     1 
HETATM 5468 O  O     . HOH   M 7 .   ? 28.35100  28.68100  -3.05400  1.000 27.52088 ? 316 HOH   A O     1 
HETATM 5469 O  O     . HOH   M 7 .   ? 19.49700  10.88000  -19.18600 1.000 38.20942 ? 317 HOH   A O     1 
HETATM 5470 O  O     . HOH   M 7 .   ? 13.77800  10.75300  -12.79300 1.000 29.74187 ? 318 HOH   A O     1 
HETATM 5471 O  O     . HOH   M 7 .   ? 2.22400   18.51700  -10.88200 1.000 25.80219 ? 319 HOH   A O     1 
HETATM 5472 O  O     . HOH   M 7 .   ? 36.41800  21.16000  -14.71600 1.000 40.68425 ? 320 HOH   A O     1 
HETATM 5473 O  O     . HOH   M 7 .   ? 20.19800  38.84400  -12.25400 1.000 23.70695 ? 321 HOH   A O     1 
HETATM 5474 O  O     . HOH   M 7 .   ? 33.22300  36.85500  -7.03900  1.000 23.57006 ? 322 HOH   A O     1 
HETATM 5475 O  O     A HOH   M 7 .   ? 7.29100   20.87700  -5.03200  0.500 27.70122 ? 323 HOH   A O     1 
HETATM 5476 O  O     B HOH   M 7 .   ? 6.08000   21.98900  -4.95900  0.500 26.25835 ? 323 HOH   A O     1 
HETATM 5477 O  O     . HOH   M 7 .   ? 3.86100   35.14600  -15.09500 1.000 36.65944 ? 324 HOH   A O     1 
HETATM 5478 O  O     . HOH   M 7 .   ? 40.25100  25.85700  -16.79800 1.000 37.99273 ? 325 HOH   A O     1 
HETATM 5479 O  O     . HOH   M 7 .   ? 40.69200  31.57500  -19.59300 1.000 34.10205 ? 326 HOH   A O     1 
HETATM 5480 O  O     . HOH   M 7 .   ? 16.86000  1.81000   -3.99500  1.000 38.48714 ? 327 HOH   A O     1 
HETATM 5481 O  O     . HOH   M 7 .   ? 33.62300  18.18600  -16.57600 1.000 44.51917 ? 328 HOH   A O     1 
HETATM 5482 O  O     . HOH   M 7 .   ? 18.16100  12.37400  -9.07500  1.000 32.54678 ? 329 HOH   A O     1 
HETATM 5483 O  O     . HOH   M 7 .   ? 18.20200  13.12000  -6.19200  1.000 17.90327 ? 330 HOH   A O     1 
HETATM 5484 O  O     . HOH   M 7 .   ? 0.988     17.221    -21.792   1.000 31.50210 ? 331 HOH   A O     1 
HETATM 5485 O  O     . HOH   M 7 .   ? 16.55500  32.65400  4.09200   1.000 31.73434 ? 332 HOH   A O     1 
HETATM 5486 O  O     . HOH   M 7 .   ? 41.70000  27.59900  -17.75100 1.000 35.37180 ? 333 HOH   A O     1 
HETATM 5487 O  O     . HOH   M 7 .   ? 9.58700   23.12100  -1.12300  1.000 31.26942 ? 334 HOH   A O     1 
HETATM 5488 O  O     A HOH   M 7 .   ? 26.61500  14.11200  -4.72800  0.500 29.61949 ? 335 HOH   A O     1 
HETATM 5489 O  O     B HOH   M 7 .   ? 25.42500  12.71800  -5.31000  0.500 32.48073 ? 335 HOH   A O     1 
HETATM 5490 O  O     . HOH   M 7 .   ? 17.70100  26.15900  -22.74700 1.000 34.59040 ? 336 HOH   A O     1 
HETATM 5491 O  O     . HOH   M 7 .   ? 33.40800  38.68500  -19.62100 1.000 41.94292 ? 337 HOH   A O     1 
HETATM 5492 O  O     . HOH   M 7 .   ? 8.06200   38.59800  -21.66700 1.000 42.37052 ? 338 HOH   A O     1 
HETATM 5493 O  O     . HOH   M 7 .   ? 17.45500  8.10700   -2.40500  1.000 28.60440 ? 339 HOH   A O     1 
HETATM 5494 O  O     . HOH   M 7 .   ? 26.46000  11.89200  -7.42900  1.000 36.78365 ? 340 HOH   A O     1 
HETATM 5495 O  O     . HOH   M 7 .   ? 29.31500  37.54100  -22.31700 1.000 27.66173 ? 341 HOH   A O     1 
HETATM 5496 O  O     . HOH   M 7 .   ? 20.13900  23.00000  2.89300   1.000 16.58034 ? 342 HOH   A O     1 
HETATM 5497 O  O     . HOH   M 7 .   ? 27.78700  21.27900  2.17500   1.000 24.04141 ? 343 HOH   A O     1 
HETATM 5498 O  O     A HOH   M 7 .   ? 23.42000  36.91700  -18.34700 0.500 28.39938 ? 344 HOH   A O     1 
HETATM 5499 O  O     B HOH   M 7 .   ? 22.64800  37.04500  -19.49500 0.500 31.36543 ? 344 HOH   A O     1 
HETATM 5500 O  O     . HOH   M 7 .   ? 29.421    32.759    -24.702   1.000 22.00827 ? 345 HOH   A O     1 
HETATM 5501 O  O     . HOH   M 7 .   ? -1.69800  23.69400  -12.92500 1.000 31.21447 ? 346 HOH   A O     1 
HETATM 5502 O  O     . HOH   M 7 .   ? 25.49400  30.25100  -21.50400 1.000 25.57016 ? 347 HOH   A O     1 
HETATM 5503 O  O     . HOH   M 7 .   ? 26.25600  39.29600  -5.28800  1.000 28.51754 ? 348 HOH   A O     1 
HETATM 5504 O  O     . HOH   M 7 .   ? 14.63400  48.34100  -8.21000  1.000 50.00541 ? 349 HOH   A O     1 
HETATM 5505 O  O     . HOH   M 7 .   ? 41.37300  22.92800  -11.06600 1.000 28.11774 ? 350 HOH   A O     1 
HETATM 5506 O  O     . HOH   M 7 .   ? 22.08900  14.62900  -12.35700 1.000 19.19933 ? 351 HOH   A O     1 
HETATM 5507 O  O     . HOH   M 7 .   ? 34.89900  18.98600  -9.43700  1.000 31.55543 ? 352 HOH   A O     1 
HETATM 5508 O  O     . HOH   M 7 .   ? 4.032     16.528    -11.708   1.000 41.18327 ? 353 HOH   A O     1 
HETATM 5509 O  O     . HOH   M 7 .   ? 40.04600  37.65000  -9.50300  1.000 22.85248 ? 354 HOH   A O     1 
HETATM 5510 O  O     . HOH   M 7 .   ? 19.56800  49.28800  2.32900   1.000 36.29535 ? 355 HOH   A O     1 
HETATM 5511 O  O     . HOH   M 7 .   ? 12.05300  11.28200  -15.28600 1.000 42.72127 ? 356 HOH   A O     1 
HETATM 5512 O  O     . HOH   M 7 .   ? 10.56500  26.31900  -6.76200  1.000 19.53949 ? 357 HOH   A O     1 
HETATM 5513 O  O     . HOH   M 7 .   ? 17.61600  24.28400  3.38600   1.000 26.20190 ? 358 HOH   A O     1 
HETATM 5514 O  O     . HOH   M 7 .   ? 1.36800   32.42300  -13.90600 1.000 46.20025 ? 359 HOH   A O     1 
HETATM 5515 O  O     . HOH   M 7 .   ? 8.88400   25.74300  -1.33400  1.000 38.88651 ? 360 HOH   A O     1 
HETATM 5516 O  O     A HOH   M 7 .   ? 0.70100   19.75700  -20.74000 0.500 20.23552 ? 361 HOH   A O     1 
HETATM 5517 O  O     B HOH   M 7 .   ? -0.93900  19.92800  -22.01800 0.500 30.79524 ? 361 HOH   A O     1 
HETATM 5518 O  O     . HOH   M 7 .   ? 10.16300  40.87800  -3.43000  1.000 41.28369 ? 362 HOH   A O     1 
HETATM 5519 O  O     . HOH   M 7 .   ? 21.26500  33.52100  10.32600  1.000 21.62366 ? 363 HOH   A O     1 
HETATM 5520 O  O     . HOH   M 7 .   ? 33.92000  18.39100  -11.72700 1.000 35.90371 ? 364 HOH   A O     1 
HETATM 5521 O  O     . HOH   M 7 .   ? 18.02400  16.10100  -3.96400  1.000 16.04546 ? 365 HOH   A O     1 
HETATM 5522 O  O     . HOH   M 7 .   ? 21.59300  32.43400  -21.56300 1.000 28.01210 ? 366 HOH   A O     1 
HETATM 5523 O  O     . HOH   M 7 .   ? 13.87200  37.97300  -18.88300 1.000 29.54146 ? 367 HOH   A O     1 
HETATM 5524 O  O     . HOH   M 7 .   ? 24.36900  21.79200  -20.87900 1.000 23.62085 ? 368 HOH   A O     1 
HETATM 5525 O  O     . HOH   M 7 .   ? 11.76700  36.77300  -19.95500 1.000 33.05865 ? 369 HOH   A O     1 
HETATM 5526 O  O     . HOH   M 7 .   ? 15.23200  17.87800  0.93800   1.000 22.58428 ? 370 HOH   A O     1 
HETATM 5527 O  O     . HOH   M 7 .   ? 27.53000  18.28400  2.72500   1.000 33.07694 ? 371 HOH   A O     1 
HETATM 5528 O  O     . HOH   M 7 .   ? 12.11500  12.16400  -20.47200 1.000 29.69576 ? 372 HOH   A O     1 
HETATM 5529 O  O     . HOH   M 7 .   ? 23.93100  42.78300  2.00500   1.000 35.17392 ? 373 HOH   A O     1 
HETATM 5530 O  O     . HOH   M 7 .   ? 18.94900  34.66700  10.65800  1.000 33.87905 ? 374 HOH   A O     1 
HETATM 5531 O  O     . HOH   M 7 .   ? 32.55200  18.57500  -2.94800  1.000 34.30365 ? 375 HOH   A O     1 
HETATM 5532 O  O     . HOH   M 7 .   ? 31.24400  36.83500  -18.91100 1.000 24.12146 ? 376 HOH   A O     1 
HETATM 5533 O  O     . HOH   M 7 .   ? 8.37700   17.72700  -10.71800 1.000 21.72075 ? 377 HOH   A O     1 
HETATM 5534 O  O     . HOH   M 7 .   ? 15.884    43.758    4.274     1.000 22.12951 ? 378 HOH   A O     1 
HETATM 5535 O  O     . HOH   M 7 .   ? 44.453    36.439    -17.090   1.000 42.96717 ? 379 HOH   A O     1 
HETATM 5536 O  O     . HOH   M 7 .   ? 22.57600  16.22000  1.48300   1.000 18.81314 ? 380 HOH   A O     1 
HETATM 5537 O  O     . HOH   M 7 .   ? 39.59100  28.98900  -3.43800  1.000 21.15685 ? 381 HOH   A O     1 
HETATM 5538 O  O     . HOH   M 7 .   ? 34.24000  39.54300  -16.31900 1.000 36.68040 ? 382 HOH   A O     1 
HETATM 5539 O  O     . HOH   M 7 .   ? 35.93400  36.42800  -14.67100 1.000 31.64429 ? 383 HOH   A O     1 
HETATM 5540 O  O     . HOH   M 7 .   ? 6.36200   40.68700  -17.59300 1.000 37.99351 ? 384 HOH   A O     1 
HETATM 5541 O  O     . HOH   M 7 .   ? 9.46300   16.94100  5.36900   1.000 25.97552 ? 385 HOH   A O     1 
HETATM 5542 O  O     . HOH   M 7 .   ? 21.97000  18.24300  -24.27500 1.000 37.27131 ? 386 HOH   A O     1 
HETATM 5543 O  O     . HOH   M 7 .   ? 2.35400   17.07000  -14.18200 1.000 27.26692 ? 387 HOH   A O     1 
HETATM 5544 O  O     . HOH   M 7 .   ? 31.45400  24.75900  -2.53400  1.000 27.42157 ? 388 HOH   A O     1 
HETATM 5545 O  O     . HOH   M 7 .   ? 12.86300  7.64600   -9.12400  1.000 45.36072 ? 389 HOH   A O     1 
HETATM 5546 O  O     . HOH   M 7 .   ? 9.13000   26.56000  -19.66000 1.000 30.34666 ? 390 HOH   A O     1 
HETATM 5547 O  O     . HOH   M 7 .   ? 15.94000  25.92500  -1.50600  1.000 16.13296 ? 391 HOH   A O     1 
HETATM 5548 O  O     . HOH   M 7 .   ? 30.80900  23.27200  -16.87700 1.000 33.31476 ? 392 HOH   A O     1 
HETATM 5549 O  O     . HOH   M 7 .   ? 18.75600  47.78800  -3.59800  1.000 33.05115 ? 393 HOH   A O     1 
HETATM 5550 O  O     . HOH   M 7 .   ? 10.81200  14.09100  -12.33200 1.000 25.17378 ? 394 HOH   A O     1 
HETATM 5551 O  O     . HOH   M 7 .   ? 17.59600  40.85300  -9.14800  1.000 36.52288 ? 395 HOH   A O     1 
HETATM 5552 O  O     . HOH   M 7 .   ? 26.62300  39.08700  -2.06400  1.000 29.86984 ? 396 HOH   A O     1 
HETATM 5553 O  O     . HOH   M 7 .   ? 13.26500  28.88900  11.29100  1.000 37.22508 ? 397 HOH   A O     1 
HETATM 5554 O  O     . HOH   M 7 .   ? 33.75900  34.06000  -4.17700  1.000 25.22571 ? 398 HOH   A O     1 
HETATM 5555 O  O     . HOH   M 7 .   ? 17.30100  33.39200  -21.78500 1.000 39.88699 ? 399 HOH   A O     1 
HETATM 5556 O  O     . HOH   M 7 .   ? 4.24900   26.48000  -22.69800 1.000 30.24016 ? 400 HOH   A O     1 
HETATM 5557 O  O     . HOH   M 7 .   ? 9.80500   38.39100  -5.42400  1.000 30.49872 ? 401 HOH   A O     1 
HETATM 5558 O  O     . HOH   M 7 .   ? 6.17000   32.89600  -7.94800  1.000 25.58750 ? 402 HOH   A O     1 
HETATM 5559 O  O     . HOH   M 7 .   ? 28.55400  37.19300  -1.05600  1.000 30.43304 ? 403 HOH   A O     1 
HETATM 5560 O  O     . HOH   M 7 .   ? 36.376    40.949    -19.755   1.000 40.44118 ? 404 HOH   A O     1 
HETATM 5561 O  O     . HOH   M 7 .   ? 38.31100  35.04900  -14.74900 1.000 20.85007 ? 405 HOH   A O     1 
HETATM 5562 O  O     A HOH   M 7 .   ? 14.75900  30.69900  3.57800   0.500 22.17899 ? 406 HOH   A O     1 
HETATM 5563 O  O     B HOH   M 7 .   ? 14.60200  31.77800  5.21100   0.500 29.85922 ? 406 HOH   A O     1 
HETATM 5564 O  O     . HOH   M 7 .   ? 22.129    39.958    -20.797   1.000 39.03624 ? 407 HOH   A O     1 
HETATM 5565 O  O     . HOH   M 7 .   ? 31.60400  30.14200  -22.59800 1.000 23.03245 ? 408 HOH   A O     1 
HETATM 5566 O  O     . HOH   M 7 .   ? 35.17600  29.92000  -22.98900 1.000 30.20215 ? 409 HOH   A O     1 
HETATM 5567 O  O     . HOH   M 7 .   ? 29.43400  39.42200  -5.91700  1.000 34.08828 ? 410 HOH   A O     1 
HETATM 5568 O  O     . HOH   M 7 .   ? 1.15100   20.95800  -10.63300 1.000 24.02096 ? 411 HOH   A O     1 
HETATM 5569 O  O     . HOH   M 7 .   ? 24.94400  13.89100  -1.09900  1.000 35.08029 ? 412 HOH   A O     1 
HETATM 5570 O  O     . HOH   M 7 .   ? 26.12300  30.17700  0.79900   1.000 26.45568 ? 413 HOH   A O     1 
HETATM 5571 O  O     . HOH   M 7 .   ? 16.02000  28.61000  -22.41000 1.000 28.44072 ? 414 HOH   A O     1 
HETATM 5572 O  O     . HOH   M 7 .   ? 23.36100  12.51500  -18.93200 1.000 36.13431 ? 415 HOH   A O     1 
HETATM 5573 O  O     . HOH   M 7 .   ? 29.042    30.322    -23.480   1.000 25.36100 ? 416 HOH   A O     1 
HETATM 5574 O  O     . HOH   M 7 .   ? 11.544    40.929    0.789     1.000 37.60209 ? 417 HOH   A O     1 
HETATM 5575 O  O     . HOH   M 7 .   ? 29.83800  35.06800  4.55400   1.000 32.25381 ? 418 HOH   A O     1 
HETATM 5576 O  O     . HOH   M 7 .   ? 10.51200  41.77200  5.46800   1.000 27.85111 ? 419 HOH   A O     1 
HETATM 5577 O  O     . HOH   M 7 .   ? 32.49500  27.72700  -22.26000 1.000 31.53973 ? 420 HOH   A O     1 
HETATM 5578 O  O     . HOH   M 7 .   ? 15.36900  35.88800  -20.21400 1.000 36.23039 ? 421 HOH   A O     1 
HETATM 5579 O  O     . HOH   M 7 .   ? 8.24400   14.63500  -12.28800 1.000 31.26967 ? 422 HOH   A O     1 
HETATM 5580 O  O     . HOH   M 7 .   ? 11.05600  11.79900  -10.36800 1.000 36.34951 ? 423 HOH   A O     1 
HETATM 5581 O  O     . HOH   M 7 .   ? 8.94400   19.27900  -8.66000  1.000 33.21267 ? 424 HOH   A O     1 
HETATM 5582 O  O     . HOH   M 7 .   ? 3.90100   29.28800  -23.49700 1.000 33.48986 ? 425 HOH   A O     1 
HETATM 5583 O  O     . HOH   M 7 .   ? 24.46100  39.77600  1.76200   1.000 21.43902 ? 426 HOH   A O     1 
HETATM 5584 O  O     . HOH   M 7 .   ? 20.68700  39.31800  6.95300   1.000 27.41102 ? 427 HOH   A O     1 
HETATM 5585 O  O     . HOH   M 7 .   ? 6.07400   40.28500  -20.24700 1.000 44.45777 ? 428 HOH   A O     1 
HETATM 5586 O  O     . HOH   M 7 .   ? 22.30500  13.41800  -0.39100  1.000 40.09292 ? 429 HOH   A O     1 
HETATM 5587 O  O     . HOH   M 7 .   ? 1.32000   21.81400  -8.07400  1.000 23.14885 ? 430 HOH   A O     1 
HETATM 5588 O  O     . HOH   M 7 .   ? 9.93400   32.60500  1.37000   1.000 48.71034 ? 431 HOH   A O     1 
HETATM 5589 O  O     . HOH   M 7 .   ? 23.64400  10.09900  -17.21200 1.000 31.58088 ? 432 HOH   A O     1 
HETATM 5590 O  O     . HOH   M 7 .   ? 13.46900  19.65600  4.60800   1.000 31.61879 ? 433 HOH   A O     1 
HETATM 5591 O  O     . HOH   M 7 .   ? 23.63000  24.53200  -21.88200 1.000 23.59339 ? 434 HOH   A O     1 
HETATM 5592 O  O     . HOH   M 7 .   ? 24.10100  34.98600  -20.95200 1.000 35.66547 ? 435 HOH   A O     1 
HETATM 5593 O  O     . HOH   M 7 .   ? 8.54600   13.44700  -2.69700  1.000 44.14236 ? 436 HOH   A O     1 
HETATM 5594 O  O     . HOH   M 7 .   ? 36.51200  36.35200  -7.84500  1.000 23.37909 ? 437 HOH   A O     1 
HETATM 5595 O  O     . HOH   M 7 .   ? 37.33100  21.03900  -11.54800 1.000 33.12462 ? 438 HOH   A O     1 
HETATM 5596 O  O     . HOH   M 7 .   ? 31.85500  16.09500  -7.19000  1.000 33.81906 ? 439 HOH   A O     1 
HETATM 5597 O  O     . HOH   M 7 .   ? 14.87600  36.30900  6.32400   1.000 35.03612 ? 440 HOH   A O     1 
HETATM 5598 O  O     . HOH   M 7 .   ? 34.28600  24.90500  -18.80500 1.000 34.04468 ? 441 HOH   A O     1 
HETATM 5599 O  O     . HOH   M 7 .   ? 8.91700   24.78800  3.19500   1.000 40.92015 ? 442 HOH   A O     1 
HETATM 5600 O  O     . HOH   M 7 .   ? 43.732    31.144    -15.671   1.000 41.88002 ? 443 HOH   A O     1 
HETATM 5601 O  O     . HOH   M 7 .   ? 28.34900  16.78600  -21.67300 1.000 39.95570 ? 444 HOH   A O     1 
HETATM 5602 O  O     . HOH   M 7 .   ? 30.62200  11.02000  -9.92300  1.000 45.85675 ? 445 HOH   A O     1 
HETATM 5603 O  O     . HOH   M 7 .   ? 17.23400  44.25100  -14.37300 1.000 47.69527 ? 446 HOH   A O     1 
HETATM 5604 O  O     . HOH   M 7 .   ? 28.73800  17.89100  -0.05400  1.000 30.16515 ? 447 HOH   A O     1 
HETATM 5605 O  O     . HOH   M 7 .   ? 23.44900  40.39500  3.97100   1.000 34.68269 ? 448 HOH   A O     1 
HETATM 5606 O  O     A HOH   M 7 .   ? 34.74600  25.90900  -1.57100  0.500 24.30611 ? 449 HOH   A O     1 
HETATM 5607 O  O     B HOH   M 7 .   ? 36.72800  25.65700  -0.77000  0.500 22.45074 ? 449 HOH   A O     1 
HETATM 5608 O  O     . HOH   M 7 .   ? 29.78100  13.71000  -22.39200 1.000 45.11646 ? 450 HOH   A O     1 
HETATM 5609 O  O     . HOH   M 7 .   ? 32.94300  18.86500  -6.05500  1.000 27.43677 ? 451 HOH   A O     1 
HETATM 5610 O  O     . HOH   M 7 .   ? 17.97200  37.82800  7.81800   1.000 32.26867 ? 452 HOH   A O     1 
HETATM 5611 O  O     . HOH   M 7 .   ? 12.57700  20.36300  7.47600   1.000 27.93019 ? 453 HOH   A O     1 
HETATM 5612 O  O     . HOH   M 7 .   ? 16.28400  28.47700  12.36800  1.000 32.79710 ? 454 HOH   A O     1 
HETATM 5613 O  O     . HOH   M 7 .   ? 13.85600  30.50500  1.05800   1.000 32.43085 ? 455 HOH   A O     1 
HETATM 5614 O  O     . HOH   M 7 .   ? 19.46400  40.82100  -11.03900 1.000 38.99903 ? 456 HOH   A O     1 
HETATM 5615 O  O     . HOH   M 7 .   ? 27.20700  36.88300  7.09600   1.000 27.19191 ? 457 HOH   A O     1 
HETATM 5616 O  O     . HOH   M 7 .   ? 2.37200   32.96500  -6.47100  1.000 40.17217 ? 458 HOH   A O     1 
HETATM 5617 O  O     . HOH   M 7 .   ? 6.69000   13.86600  -0.04000  1.000 33.52198 ? 459 HOH   A O     1 
HETATM 5618 O  O     . HOH   M 7 .   ? 10.07900  14.79000  -8.07400  1.000 39.19416 ? 460 HOH   A O     1 
HETATM 5619 O  O     . HOH   M 7 .   ? 44.521    24.482    -15.120   1.000 37.20251 ? 461 HOH   A O     1 
HETATM 5620 O  O     . HOH   M 7 .   ? 18.70200  27.07500  11.59900  1.000 31.02670 ? 462 HOH   A O     1 
HETATM 5621 O  O     . HOH   M 7 .   ? 25.84700  13.73200  -20.29600 1.000 42.66430 ? 463 HOH   A O     1 
HETATM 5622 O  O     . HOH   M 7 .   ? 13.35100  19.73900  1.82800   1.000 26.81059 ? 464 HOH   A O     1 
HETATM 5623 O  O     . HOH   M 7 .   ? 11.84500  17.53500  -24.50400 1.000 41.92632 ? 465 HOH   A O     1 
HETATM 5624 O  O     . HOH   M 7 .   ? 23.734    38.824    10.135    1.000 33.68201 ? 466 HOH   A O     1 
HETATM 5625 O  O     . HOH   M 7 .   ? 9.69300   21.09700  2.79300   1.000 41.19699 ? 467 HOH   A O     1 
HETATM 5626 O  O     . HOH   M 7 .   ? -1.71100  20.84600  -19.75600 1.000 37.87150 ? 468 HOH   A O     1 
HETATM 5627 O  O     . HOH   M 7 .   ? 25.42700  28.10500  -22.93000 1.000 36.80643 ? 469 HOH   A O     1 
HETATM 5628 O  O     . HOH   M 7 .   ? 4.32600   37.58100  -14.28500 1.000 41.03439 ? 470 HOH   A O     1 
HETATM 5629 O  O     . HOH   M 7 .   ? -1.369    21.350    -11.603   1.000 24.60965 ? 471 HOH   A O     1 
HETATM 5630 O  O     . HOH   M 7 .   ? 29.72000  26.65600  -1.79600  1.000 33.27573 ? 472 HOH   A O     1 
HETATM 5631 O  O     . HOH   M 7 .   ? 33.66000  21.12100  -2.32600  1.000 39.17748 ? 473 HOH   A O     1 
HETATM 5632 O  O     . HOH   M 7 .   ? 29.54800  38.68300  -18.17300 1.000 26.75323 ? 474 HOH   A O     1 
HETATM 5633 O  O     . HOH   M 7 .   ? 2.18300   19.80500  -6.20800  1.000 34.17833 ? 475 HOH   A O     1 
HETATM 5634 O  O     . HOH   M 7 .   ? 24.75100  38.68100  -20.55900 1.000 35.95167 ? 476 HOH   A O     1 
HETATM 5635 O  O     . HOH   M 7 .   ? 33.21500  44.86600  -12.69200 1.000 29.79968 ? 477 HOH   A O     1 
HETATM 5636 O  O     A HOH   M 7 .   ? 24.19200  41.01700  -4.14200  0.500 26.90565 ? 478 HOH   A O     1 
HETATM 5637 O  O     B HOH   M 7 .   ? 22.97700  42.58100  -4.02800  0.500 30.05275 ? 478 HOH   A O     1 
HETATM 5638 O  O     . HOH   M 7 .   ? 3.95000   20.82700  -4.34500  1.000 40.87538 ? 479 HOH   A O     1 
HETATM 5639 O  O     . HOH   M 7 .   ? 24.56100  10.71900  -8.19400  1.000 43.55187 ? 480 HOH   A O     1 
HETATM 5640 O  O     . HOH   M 7 .   ? 32.795    23.062    1.263     1.000 31.96463 ? 481 HOH   A O     1 
HETATM 5641 O  O     . HOH   M 7 .   ? -2.73600  26.02800  -12.73000 1.000 43.79816 ? 482 HOH   A O     1 
HETATM 5642 O  O     . HOH   M 7 .   ? 42.558    39.363    -15.412   1.000 31.16089 ? 483 HOH   A O     1 
HETATM 5643 O  O     . HOH   M 7 .   ? 10.95100  44.96700  -19.28700 1.000 42.75522 ? 484 HOH   A O     1 
HETATM 5644 O  O     . HOH   M 7 .   ? 25.40000  37.36400  -22.39700 1.000 38.58876 ? 485 HOH   A O     1 
HETATM 5645 O  O     . HOH   M 7 .   ? -1.08800  22.93900  -7.49000  1.000 35.90222 ? 486 HOH   A O     1 
HETATM 5646 O  O     . HOH   M 7 .   ? 24.34700  7.88800   -9.23300  1.000 45.41646 ? 487 HOH   A O     1 
HETATM 5647 O  O     . HOH   M 7 .   ? 20.86900  13.59000  -5.98100  1.000 31.90405 ? 488 HOH   A O     1 
HETATM 5648 O  O     . HOH   M 7 .   ? 25.27200  10.15400  -2.76200  1.000 46.40130 ? 489 HOH   A O     1 
HETATM 5649 O  O     . HOH   M 7 .   ? 27.11800  36.88000  -24.13200 1.000 30.22788 ? 490 HOH   A O     1 
HETATM 5650 O  O     . HOH   M 7 .   ? 17.07700  30.88400  -23.84400 1.000 38.39866 ? 491 HOH   A O     1 
HETATM 5651 O  O     . HOH   M 7 .   ? 17.70600  38.33300  -20.20100 1.000 37.40195 ? 492 HOH   A O     1 
HETATM 5652 O  O     . HOH   M 7 .   ? 28.24200  30.07200  -0.70100  1.000 32.38891 ? 493 HOH   A O     1 
HETATM 5653 O  O     . HOH   M 7 .   ? 12.98300  34.86100  -21.45000 1.000 38.45886 ? 494 HOH   A O     1 
HETATM 5654 O  O     . HOH   M 7 .   ? 31.65000  40.74200  -17.51000 1.000 35.51256 ? 495 HOH   A O     1 
HETATM 5655 O  O     . HOH   M 7 .   ? 11.26700  19.14900  4.34800   1.000 36.46205 ? 496 HOH   A O     1 
HETATM 5656 O  O     . HOH   M 7 .   ? 27.16800  41.36200  0.10900   1.000 40.34916 ? 497 HOH   A O     1 
HETATM 5657 O  O     . HOH   M 7 .   ? 26.14700  41.95900  -1.80900  1.000 43.27213 ? 498 HOH   A O     1 
HETATM 5658 O  O     . HOH   M 7 .   ? 28.19200  39.25300  -20.41600 1.000 32.62025 ? 499 HOH   A O     1 
HETATM 5659 O  O     . HOH   M 7 .   ? 4.26400   34.52400  -9.09400  1.000 39.42524 ? 500 HOH   A O     1 
HETATM 5660 O  O     . HOH   M 7 .   ? 1.28600   30.92600  -24.11000 1.000 44.33177 ? 501 HOH   A O     1 
HETATM 5661 O  O     . HOH   M 7 .   ? 3.71700   34.40700  -11.85700 1.000 44.11996 ? 502 HOH   A O     1 
HETATM 5662 O  O     . HOH   M 7 .   ? 45.051    29.228    -14.994   1.000 46.05510 ? 503 HOH   A O     1 
HETATM 5663 O  O     . HOH   M 7 .   ? 18.84500  29.01600  15.53400  1.000 46.95753 ? 504 HOH   A O     1 
HETATM 5664 O  O     . HOH   M 7 .   ? 26.99900  9.91800   -4.49100  1.000 42.99291 ? 505 HOH   A O     1 
HETATM 5665 O  O     . HOH   M 7 .   ? 0.60000   33.18000  -25.63100 1.000 46.61639 ? 506 HOH   A O     1 
HETATM 5666 O  O     . HOH   N 7 .   ? 31.266    -6.074    17.679    1.000 32.17096 ? 201 HOH   D O     1 
HETATM 5667 O  O     . HOH   N 7 .   ? -5.31500  10.91200  17.68300  1.000 33.82465 ? 202 HOH   D O     1 
HETATM 5668 O  O     . HOH   N 7 .   ? 16.32700  -14.02600 10.72600  1.000 38.46991 ? 203 HOH   D O     1 
HETATM 5669 O  O     . HOH   N 7 .   ? 29.30900  7.19400   25.11800  1.000 41.31926 ? 204 HOH   D O     1 
HETATM 5670 O  O     . HOH   N 7 .   ? 17.51400  9.32300   0.84600   1.000 38.44628 ? 205 HOH   D O     1 
HETATM 5671 O  O     . HOH   N 7 .   ? 19.84400  20.87200  20.70600  1.000 33.78671 ? 206 HOH   D O     1 
HETATM 5672 O  O     . HOH   N 7 .   ? -6.194    12.997    13.371    1.000 43.09830 ? 207 HOH   D O     1 
HETATM 5673 O  O     . HOH   N 7 .   ? 7.75300   -3.79700  28.63500  1.000 40.96446 ? 208 HOH   D O     1 
HETATM 5674 O  O     . HOH   N 7 .   ? 0.44600   16.36200  4.79700   1.000 29.04329 ? 209 HOH   D O     1 
HETATM 5675 O  O     . HOH   N 7 .   ? 14.30800  14.03700  28.19600  1.000 22.19109 ? 210 HOH   D O     1 
HETATM 5676 O  O     . HOH   N 7 .   ? -1.34600  -4.80000  15.52000  1.000 32.09106 ? 211 HOH   D O     1 
HETATM 5677 O  O     . HOH   N 7 .   ? -0.14100  -9.14300  14.49900  1.000 40.73302 ? 212 HOH   D O     1 
HETATM 5678 O  O     . HOH   N 7 .   ? -2.58300  11.53700  31.66800  1.000 38.25845 ? 213 HOH   D O     1 
HETATM 5679 O  O     . HOH   N 7 .   ? 26.57000  18.75100  15.57500  1.000 37.87593 ? 214 HOH   D O     1 
HETATM 5680 O  O     . HOH   N 7 .   ? 8.97500   -0.66400  28.20400  1.000 35.21790 ? 215 HOH   D O     1 
HETATM 5681 O  O     . HOH   N 7 .   ? 7.53500   -5.72500  25.75200  1.000 24.55451 ? 216 HOH   D O     1 
HETATM 5682 O  O     . HOH   N 7 .   ? 7.92600   23.21800  18.01000  1.000 33.49423 ? 217 HOH   D O     1 
HETATM 5683 O  O     . HOH   N 7 .   ? 11.08800  7.70000   32.97300  1.000 34.55175 ? 218 HOH   D O     1 
HETATM 5684 O  O     . HOH   N 7 .   ? 16.13600  1.38100   9.69800   1.000 20.96949 ? 219 HOH   D O     1 
HETATM 5685 O  O     . HOH   N 7 .   ? 4.08800   18.66300  21.25500  1.000 34.70295 ? 220 HOH   D O     1 
HETATM 5686 O  O     . HOH   N 7 .   ? 23.47800  -6.66700  19.68900  1.000 33.21739 ? 221 HOH   D O     1 
HETATM 5687 O  O     . HOH   N 7 .   ? 5.49900   -5.55900  1.89800   1.000 40.89626 ? 222 HOH   D O     1 
HETATM 5688 O  O     . HOH   N 7 .   ? 7.39400   7.75300   9.16400   1.000 19.98625 ? 223 HOH   D O     1 
HETATM 5689 O  O     . HOH   N 7 .   ? 7.88400   22.61200  23.43100  1.000 38.41433 ? 224 HOH   D O     1 
HETATM 5690 O  O     . HOH   N 7 .   ? 20.95100  12.52300  4.56300   1.000 25.69223 ? 225 HOH   D O     1 
HETATM 5691 O  O     . HOH   N 7 .   ? 24.02800  3.54700   7.09900   1.000 19.26294 ? 226 HOH   D O     1 
HETATM 5692 O  O     . HOH   N 7 .   ? 18.22200  22.71400  21.52000  1.000 41.73121 ? 227 HOH   D O     1 
HETATM 5693 O  O     . HOH   N 7 .   ? 23.30600  11.02700  24.84000  1.000 22.74644 ? 228 HOH   D O     1 
HETATM 5694 O  O     . HOH   N 7 .   ? 1.56300   -1.72000  21.34100  1.000 27.39612 ? 229 HOH   D O     1 
HETATM 5695 O  O     . HOH   N 7 .   ? 6.34700   10.22300  5.48300   1.000 25.05511 ? 230 HOH   D O     1 
HETATM 5696 O  O     . HOH   N 7 .   ? 9.42800   9.48000   30.28800  1.000 35.13457 ? 231 HOH   D O     1 
HETATM 5697 O  O     . HOH   N 7 .   ? 1.88800   17.87100  26.34100  1.000 31.36502 ? 232 HOH   D O     1 
HETATM 5698 O  O     . HOH   N 7 .   ? -0.20100  17.30000  12.47100  1.000 21.80498 ? 233 HOH   D O     1 
HETATM 5699 O  O     . HOH   N 7 .   ? 5.18500   4.07800   14.71600  1.000 19.12984 ? 234 HOH   D O     1 
HETATM 5700 O  O     . HOH   N 7 .   ? 10.96400  19.74900  24.01400  1.000 28.50675 ? 235 HOH   D O     1 
HETATM 5701 O  O     . HOH   N 7 .   ? -1.40800  9.70900   32.36200  1.000 36.68574 ? 236 HOH   D O     1 
HETATM 5702 O  O     . HOH   N 7 .   ? 1.15800   -9.79300  18.25600  1.000 38.10093 ? 237 HOH   D O     1 
HETATM 5703 O  O     . HOH   N 7 .   ? 33.62700  -2.18100  7.88200   1.000 35.62001 ? 238 HOH   D O     1 
HETATM 5704 O  O     . HOH   N 7 .   ? 4.53900   14.00300  20.29900  1.000 16.39221 ? 239 HOH   D O     1 
HETATM 5705 O  O     . HOH   N 7 .   ? 4.84600   12.44100  13.11900  1.000 19.16918 ? 240 HOH   D O     1 
HETATM 5706 O  O     . HOH   N 7 .   ? 12.09100  -5.06500  3.05400   1.000 32.81904 ? 241 HOH   D O     1 
HETATM 5707 O  O     . HOH   N 7 .   ? -4.90900  7.47500   20.53900  1.000 34.81562 ? 242 HOH   D O     1 
HETATM 5708 O  O     . HOH   N 7 .   ? 25.44100  -3.22000  8.63200   1.000 18.08630 ? 243 HOH   D O     1 
HETATM 5709 O  O     . HOH   N 7 .   ? 16.27000  3.68000   6.19500   1.000 17.43643 ? 244 HOH   D O     1 
HETATM 5710 O  O     . HOH   N 7 .   ? 22.92700  -2.53900  25.31600  1.000 38.44746 ? 245 HOH   D O     1 
HETATM 5711 O  O     . HOH   N 7 .   ? 16.96800  0.75400   4.60800   1.000 18.47815 ? 246 HOH   D O     1 
HETATM 5712 O  O     . HOH   N 7 .   ? 23.72800  6.99100   4.42900   1.000 24.04131 ? 247 HOH   D O     1 
HETATM 5713 O  O     . HOH   N 7 .   ? 5.30800   -6.46200  11.07000  1.000 26.08257 ? 248 HOH   D O     1 
HETATM 5714 O  O     . HOH   N 7 .   ? 3.41500   16.90500  11.26600  1.000 30.44766 ? 249 HOH   D O     1 
HETATM 5715 O  O     . HOH   N 7 .   ? 28.53200  10.46900  19.88400  1.000 33.46896 ? 250 HOH   D O     1 
HETATM 5716 O  O     . HOH   N 7 .   ? 12.02900  -4.44200  -0.49500  1.000 29.82824 ? 251 HOH   D O     1 
HETATM 5717 O  O     . HOH   N 7 .   ? 7.23000   2.41100   -0.71900  1.000 36.02748 ? 252 HOH   D O     1 
HETATM 5718 O  O     . HOH   N 7 .   ? 15.00600  10.50000  4.55100   1.000 23.80933 ? 253 HOH   D O     1 
HETATM 5719 O  O     . HOH   N 7 .   ? 15.32600  10.21800  26.26500  1.000 20.51017 ? 254 HOH   D O     1 
HETATM 5720 O  O     A HOH   N 7 .   ? 19.03200  11.27600  3.82100   0.500 23.68926 ? 255 HOH   D O     1 
HETATM 5721 O  O     B HOH   N 7 .   ? 19.18400  12.35500  2.11200   0.500 24.44542 ? 255 HOH   D O     1 
HETATM 5722 O  O     . HOH   N 7 .   ? 7.52000   7.61100   2.13100   1.000 28.25185 ? 256 HOH   D O     1 
HETATM 5723 O  O     . HOH   N 7 .   ? 23.99500  19.24700  19.33900  1.000 33.78714 ? 257 HOH   D O     1 
HETATM 5724 O  O     . HOH   N 7 .   ? 12.47600  3.26800   29.92700  1.000 34.47588 ? 258 HOH   D O     1 
HETATM 5725 O  O     . HOH   N 7 .   ? 10.40000  18.47100  10.25500  1.000 27.93603 ? 259 HOH   D O     1 
HETATM 5726 O  O     . HOH   N 7 .   ? 19.924    -10.846   10.428    1.000 35.59924 ? 260 HOH   D O     1 
HETATM 5727 O  O     . HOH   N 7 .   ? 8.89900   13.69400  26.29600  1.000 31.57291 ? 261 HOH   D O     1 
HETATM 5728 O  O     . HOH   N 7 .   ? -3.34000  0.10800   16.66900  1.000 32.13746 ? 262 HOH   D O     1 
HETATM 5729 O  O     . HOH   N 7 .   ? 13.88900  -4.36500  6.35200   1.000 26.15539 ? 263 HOH   D O     1 
HETATM 5730 O  O     . HOH   N 7 .   ? 30.87000  -2.95700  19.75900  1.000 34.34482 ? 264 HOH   D O     1 
HETATM 5731 O  O     . HOH   N 7 .   ? -3.33900  9.07400   25.06800  1.000 29.02025 ? 265 HOH   D O     1 
HETATM 5732 O  O     . HOH   N 7 .   ? 2.55600   3.02400   31.71300  1.000 34.46540 ? 266 HOH   D O     1 
HETATM 5733 O  O     . HOH   N 7 .   ? 18.39200  -7.40200  25.96400  1.000 28.65246 ? 267 HOH   D O     1 
HETATM 5734 O  O     . HOH   N 7 .   ? 3.11800   12.07700  21.87600  1.000 17.49864 ? 268 HOH   D O     1 
HETATM 5735 O  O     . HOH   N 7 .   ? 21.02200  -5.25000  5.56300   1.000 21.58369 ? 269 HOH   D O     1 
HETATM 5736 O  O     . HOH   N 7 .   ? 3.12900   13.07900  9.91300   1.000 19.20689 ? 270 HOH   D O     1 
HETATM 5737 O  O     . HOH   N 7 .   ? 6.484     -11.430   3.880     1.000 38.41703 ? 271 HOH   D O     1 
HETATM 5738 O  O     . HOH   N 7 .   ? 7.17700   1.71700   31.77000  1.000 36.26899 ? 272 HOH   D O     1 
HETATM 5739 O  O     . HOH   N 7 .   ? 14.00500  19.34800  27.67500  1.000 17.11176 ? 273 HOH   D O     1 
HETATM 5740 O  O     . HOH   N 7 .   ? -3.60500  14.81900  13.17500  1.000 33.45105 ? 274 HOH   D O     1 
HETATM 5741 O  O     . HOH   N 7 .   ? 5.00500   6.57900   30.29200  1.000 35.27966 ? 275 HOH   D O     1 
HETATM 5742 O  O     . HOH   N 7 .   ? 21.55000  10.22800  3.97500   1.000 29.83998 ? 276 HOH   D O     1 
HETATM 5743 O  O     . HOH   N 7 .   ? 28.95000  13.53300  3.85200   1.000 30.20248 ? 277 HOH   D O     1 
HETATM 5744 O  O     . HOH   N 7 .   ? 24.79100  14.55100  20.07400  1.000 31.35874 ? 278 HOH   D O     1 
HETATM 5745 O  O     . HOH   N 7 .   ? 2.90700   -6.27900  23.48800  1.000 31.41303 ? 279 HOH   D O     1 
HETATM 5746 O  O     . HOH   N 7 .   ? 16.42600  7.89700   27.10300  1.000 24.01483 ? 280 HOH   D O     1 
HETATM 5747 O  O     . HOH   N 7 .   ? 26.61300  17.61800  12.39700  1.000 30.63477 ? 281 HOH   D O     1 
HETATM 5748 O  O     . HOH   N 7 .   ? -1.54000  12.75500  4.52600   1.000 33.46735 ? 282 HOH   D O     1 
HETATM 5749 O  O     . HOH   N 7 .   ? 24.35300  -6.12100  17.16300  1.000 23.91384 ? 283 HOH   D O     1 
HETATM 5750 O  O     . HOH   N 7 .   ? 12.25600  -7.14000  7.47600   1.000 34.27875 ? 284 HOH   D O     1 
HETATM 5751 O  O     . HOH   N 7 .   ? 32.49700  -2.97300  10.25600  1.000 33.63778 ? 285 HOH   D O     1 
HETATM 5752 O  O     . HOH   N 7 .   ? 4.38400   0.87700   31.67800  1.000 34.45748 ? 286 HOH   D O     1 
HETATM 5753 O  O     . HOH   N 7 .   ? 22.92000  -6.44300  8.70300   1.000 33.09695 ? 287 HOH   D O     1 
HETATM 5754 O  O     . HOH   N 7 .   ? -0.00100  0.21500   21.80100  1.000 28.77685 ? 288 HOH   D O     1 
HETATM 5755 O  O     . HOH   N 7 .   ? 24.57300  7.82800   27.36400  1.000 29.16773 ? 289 HOH   D O     1 
HETATM 5756 O  O     . HOH   N 7 .   ? 1.11100   9.33200   14.92800  1.000 20.69679 ? 290 HOH   D O     1 
HETATM 5757 O  O     . HOH   N 7 .   ? 18.16000  25.70500  25.74200  1.000 40.25099 ? 291 HOH   D O     1 
HETATM 5758 O  O     . HOH   N 7 .   ? 5.77700   -10.10800 20.54900  1.000 35.58615 ? 292 HOH   D O     1 
HETATM 5759 O  O     . HOH   N 7 .   ? 1.93500   18.97600  12.81400  1.000 22.30861 ? 293 HOH   D O     1 
HETATM 5760 O  O     . HOH   N 7 .   ? 21.30000  3.75600   27.99400  1.000 26.88702 ? 294 HOH   D O     1 
HETATM 5761 O  O     . HOH   N 7 .   ? 16.21200  -3.58600  27.92700  1.000 31.43114 ? 295 HOH   D O     1 
HETATM 5762 O  O     . HOH   N 7 .   ? 31.72100  9.52600   9.16200   1.000 39.00541 ? 296 HOH   D O     1 
HETATM 5763 O  O     . HOH   N 7 .   ? 23.98600  13.27700  23.52200  1.000 28.78247 ? 297 HOH   D O     1 
HETATM 5764 O  O     . HOH   N 7 .   ? -4.14800  10.04600  21.72800  1.000 30.24887 ? 298 HOH   D O     1 
HETATM 5765 O  O     . HOH   N 7 .   ? 15.812    -8.991    6.865     1.000 30.29290 ? 299 HOH   D O     1 
HETATM 5766 O  O     . HOH   N 7 .   ? 9.89500   10.38100  0.25300   1.000 30.22367 ? 300 HOH   D O     1 
HETATM 5767 O  O     . HOH   N 7 .   ? 5.97900   16.61900  19.44600  1.000 17.78130 ? 301 HOH   D O     1 
HETATM 5768 O  O     . HOH   N 7 .   ? 22.65600  0.27000   28.66600  1.000 37.90492 ? 302 HOH   D O     1 
HETATM 5769 O  O     . HOH   N 7 .   ? 11.36900  -6.68800  11.63400  1.000 22.67185 ? 303 HOH   D O     1 
HETATM 5770 O  O     . HOH   N 7 .   ? 24.51000  3.43700   27.71900  1.000 35.78371 ? 304 HOH   D O     1 
HETATM 5771 O  O     . HOH   N 7 .   ? 20.187    0.609     -1.056    1.000 37.90790 ? 305 HOH   D O     1 
HETATM 5772 O  O     . HOH   N 7 .   ? 7.96200   -0.39300  30.34100  1.000 40.03691 ? 306 HOH   D O     1 
HETATM 5773 O  O     . HOH   N 7 .   ? 14.62400  5.19500   29.68800  1.000 26.70008 ? 307 HOH   D O     1 
HETATM 5774 O  O     . HOH   N 7 .   ? 1.43700   21.15300  16.85500  1.000 32.52519 ? 308 HOH   D O     1 
HETATM 5775 O  O     . HOH   N 7 .   ? 2.44900   22.26800  15.24000  1.000 41.41091 ? 309 HOH   D O     1 
HETATM 5776 O  O     . HOH   N 7 .   ? 14.89700  15.50200  21.78000  1.000 22.95946 ? 310 HOH   D O     1 
HETATM 5777 O  O     . HOH   N 7 .   ? -3.35400  3.89800   25.57000  1.000 30.01575 ? 311 HOH   D O     1 
HETATM 5778 O  O     . HOH   N 7 .   ? 30.62700  16.17900  7.82000   1.000 36.16172 ? 312 HOH   D O     1 
HETATM 5779 O  O     . HOH   N 7 .   ? -0.08500  -4.63500  8.08200   1.000 42.17813 ? 313 HOH   D O     1 
HETATM 5780 O  O     . HOH   N 7 .   ? -2.91700  10.06800  7.25400   1.000 35.79174 ? 314 HOH   D O     1 
HETATM 5781 O  O     . HOH   N 7 .   ? 1.06500   0.76500   28.79600  1.000 41.11170 ? 315 HOH   D O     1 
HETATM 5782 O  O     A HOH   N 7 .   ? 28.29500  13.32100  0.87200   0.500 31.70046 ? 316 HOH   D O     1 
HETATM 5783 O  O     B HOH   N 7 .   ? 27.33400  12.82600  -0.96700  0.500 33.38861 ? 316 HOH   D O     1 
HETATM 5784 O  O     . HOH   N 7 .   ? 21.00900  18.94700  23.52800  1.000 28.37787 ? 317 HOH   D O     1 
HETATM 5785 O  O     . HOH   N 7 .   ? 8.96400   16.83100  8.20600   1.000 28.52562 ? 318 HOH   D O     1 
HETATM 5786 O  O     . HOH   N 7 .   ? 9.98700   -10.39600 18.79200  1.000 30.76091 ? 319 HOH   D O     1 
HETATM 5787 O  O     . HOH   N 7 .   ? 25.25800  -3.95200  23.59000  1.000 29.60946 ? 320 HOH   D O     1 
HETATM 5788 O  O     . HOH   N 7 .   ? 8.03600   6.03100   6.23800   1.000 25.91072 ? 321 HOH   D O     1 
HETATM 5789 O  O     A HOH   N 7 .   ? 29.20700  19.78800  5.42100   0.500 27.49725 ? 322 HOH   D O     1 
HETATM 5790 O  O     B HOH   N 7 .   ? 30.05800  20.02200  3.69800   0.500 25.89077 ? 322 HOH   D O     1 
HETATM 5791 O  O     . HOH   N 7 .   ? 12.03700  -8.87100  13.21000  1.000 28.00284 ? 323 HOH   D O     1 
HETATM 5792 O  O     . HOH   N 7 .   ? 37.83300  -0.61200  8.23600   1.000 36.77728 ? 324 HOH   D O     1 
HETATM 5793 O  O     . HOH   N 7 .   ? 30.29800  9.92400   6.83000   1.000 34.39293 ? 325 HOH   D O     1 
HETATM 5794 O  O     . HOH   N 7 .   ? 25.24700  -8.64700  12.97900  1.000 26.75082 ? 326 HOH   D O     1 
HETATM 5795 O  O     . HOH   N 7 .   ? -2.93100  16.47000  6.37300   1.000 34.37039 ? 327 HOH   D O     1 
HETATM 5796 O  O     . HOH   N 7 .   ? 27.03800  7.22200   2.08300   1.000 40.16886 ? 328 HOH   D O     1 
HETATM 5797 O  O     . HOH   N 7 .   ? 22.01100  13.60000  2.04900   1.000 32.86985 ? 329 HOH   D O     1 
HETATM 5798 O  O     . HOH   N 7 .   ? 19.87900  -2.50100  25.31800  1.000 33.55761 ? 330 HOH   D O     1 
HETATM 5799 O  O     . HOH   N 7 .   ? 10.71600  -11.02700 16.37000  1.000 38.64014 ? 331 HOH   D O     1 
HETATM 5800 O  O     . HOH   N 7 .   ? 28.52600  16.27400  4.70100   1.000 30.99505 ? 332 HOH   D O     1 
HETATM 5801 O  O     . HOH   N 7 .   ? 23.10400  -3.82400  4.34400   1.000 23.83012 ? 333 HOH   D O     1 
HETATM 5802 O  O     . HOH   N 7 .   ? 0.90400   -1.19700  30.33900  1.000 40.59133 ? 334 HOH   D O     1 
HETATM 5803 O  O     . HOH   N 7 .   ? -2.57100  -6.24800  10.11300  1.000 47.96329 ? 335 HOH   D O     1 
HETATM 5804 O  O     . HOH   N 7 .   ? 30.66300  -2.94600  14.74500  1.000 32.59328 ? 336 HOH   D O     1 
HETATM 5805 O  O     . HOH   N 7 .   ? 31.12900  12.11400  14.46100  1.000 41.80798 ? 337 HOH   D O     1 
HETATM 5806 O  O     . HOH   N 7 .   ? 17.20900  3.39000   3.48200   1.000 20.63383 ? 338 HOH   D O     1 
HETATM 5807 O  O     . HOH   N 7 .   ? 26.09400  3.50500   3.69400   1.000 36.53872 ? 339 HOH   D O     1 
HETATM 5808 O  O     . HOH   N 7 .   ? 31.86200  -3.09000  17.10700  1.000 31.30655 ? 340 HOH   D O     1 
HETATM 5809 O  O     . HOH   N 7 .   ? 27.76900  -3.75300  4.58000   1.000 36.39258 ? 341 HOH   D O     1 
HETATM 5810 O  O     . HOH   N 7 .   ? -3.51400  1.14000   19.25000  1.000 37.77900 ? 342 HOH   D O     1 
HETATM 5811 O  O     . HOH   N 7 .   ? 5.66600   -2.17200  -0.24400  1.000 43.10913 ? 343 HOH   D O     1 
HETATM 5812 O  O     . HOH   N 7 .   ? -5.68500  17.26900  9.94400   1.000 38.05156 ? 344 HOH   D O     1 
HETATM 5813 O  O     . HOH   N 7 .   ? 24.52600  -1.25400  26.77300  1.000 40.03393 ? 345 HOH   D O     1 
HETATM 5814 O  O     . HOH   N 7 .   ? 10.47300  -8.10700  9.36700   1.000 32.62143 ? 346 HOH   D O     1 
HETATM 5815 O  O     . HOH   N 7 .   ? 4.99600   1.67500   0.75000   1.000 43.01451 ? 347 HOH   D O     1 
HETATM 5816 O  O     . HOH   N 7 .   ? 13.69600  23.37900  24.85700  1.000 33.69628 ? 348 HOH   D O     1 
HETATM 5817 O  O     . HOH   N 7 .   ? -4.44200  6.44200   25.22900  1.000 41.25086 ? 349 HOH   D O     1 
HETATM 5818 O  O     . HOH   N 7 .   ? 17.25200  -14.11100 12.80600  1.000 36.34611 ? 350 HOH   D O     1 
HETATM 5819 O  O     . HOH   N 7 .   ? 27.90600  -6.37500  20.69300  1.000 41.40413 ? 351 HOH   D O     1 
HETATM 5820 O  O     . HOH   N 7 .   ? -4.38100  8.57300   31.98900  1.000 43.19526 ? 352 HOH   D O     1 
HETATM 5821 O  O     . HOH   N 7 .   ? 1.318     19.957    24.103    1.000 42.60464 ? 353 HOH   D O     1 
HETATM 5822 O  O     . HOH   N 7 .   ? 32.966    -5.150    16.203    1.000 45.87572 ? 354 HOH   D O     1 
HETATM 5823 O  O     . HOH   N 7 .   ? 10.32700  12.09000  27.75300  1.000 40.15248 ? 355 HOH   D O     1 
HETATM 5824 O  O     . HOH   N 7 .   ? 20.28300  3.70400   -2.35900  1.000 44.70705 ? 356 HOH   D O     1 
HETATM 5825 O  O     . HOH   N 7 .   ? 4.07600   -4.76400  27.50600  1.000 40.78346 ? 357 HOH   D O     1 
HETATM 5826 O  O     . HOH   N 7 .   ? 28.79600  3.03000   3.47200   1.000 39.50761 ? 358 HOH   D O     1 
HETATM 5827 O  O     . HOH   N 7 .   ? 10.73500  9.16500   -3.94400  1.000 40.71362 ? 359 HOH   D O     1 
HETATM 5828 O  O     . HOH   N 7 .   ? 23.18900  16.50800  24.18200  1.000 34.60109 ? 360 HOH   D O     1 
HETATM 5829 O  O     . HOH   N 7 .   ? 4.73700   8.53500   28.85900  1.000 43.06440 ? 361 HOH   D O     1 
HETATM 5830 O  O     . HOH   N 7 .   ? 15.22100  25.98600  24.34300  1.000 39.31951 ? 362 HOH   D O     1 
HETATM 5831 O  O     . HOH   N 7 .   ? 25.42000  -4.05600  5.98500   1.000 19.36492 ? 363 HOH   D O     1 
HETATM 5832 O  O     . HOH   N 7 .   ? 18.42900  -4.67800  26.19600  1.000 33.43358 ? 364 HOH   D O     1 
HETATM 5833 O  O     . HOH   N 7 .   ? -5.02800  9.19300   15.38500  1.000 33.50102 ? 365 HOH   D O     1 
HETATM 5834 O  O     . HOH   N 7 .   ? 8.45600   -3.32600  0.22700   1.000 39.83779 ? 366 HOH   D O     1 
HETATM 5835 O  O     A HOH   N 7 .   ? 29.16700  16.45500  11.89900  0.500 28.47743 ? 367 HOH   D O     1 
HETATM 5836 O  O     B HOH   N 7 .   ? 29.91900  16.81300  12.91300  0.500 30.33172 ? 367 HOH   D O     1 
HETATM 5837 O  O     . HOH   N 7 .   ? -0.73700  17.93600  24.37200  1.000 33.96508 ? 368 HOH   D O     1 
HETATM 5838 O  O     . HOH   N 7 .   ? 26.288    20.835    12.503    1.000 30.66608 ? 369 HOH   D O     1 
HETATM 5839 O  O     . HOH   N 7 .   ? 17.72000  26.08100  23.20200  1.000 41.40014 ? 370 HOH   D O     1 
HETATM 5840 O  O     . HOH   N 7 .   ? 6.18100   10.02600  2.89300   1.000 32.26076 ? 371 HOH   D O     1 
HETATM 5841 O  O     . HOH   N 7 .   ? 2.90600   9.27000   30.18200  1.000 43.38313 ? 372 HOH   D O     1 
HETATM 5842 O  O     . HOH   N 7 .   ? 24.857    -6.780    6.405     1.000 24.68807 ? 373 HOH   D O     1 
HETATM 5843 O  O     . HOH   N 7 .   ? -9.219    11.054    6.428     1.000 42.34524 ? 374 HOH   D O     1 
HETATM 5844 O  O     . HOH   N 7 .   ? 8.06600   -11.33500 20.13400  1.000 42.52896 ? 375 HOH   D O     1 
HETATM 5845 O  O     . HOH   N 7 .   ? 33.14900  -0.26800  16.85500  1.000 41.36764 ? 376 HOH   D O     1 
HETATM 5846 O  O     . HOH   N 7 .   ? 7.94000   -4.49700  2.42200   1.000 33.99877 ? 377 HOH   D O     1 
HETATM 5847 O  O     . HOH   N 7 .   ? 27.101    -8.234    5.640     1.000 24.73478 ? 378 HOH   D O     1 
HETATM 5848 O  O     . HOH   N 7 .   ? 0.00200   14.61300  2.78100   1.000 45.61712 ? 379 HOH   D O     1 
HETATM 5849 O  O     . HOH   N 7 .   ? 14.01500  -4.59700  29.13800  1.000 39.37059 ? 380 HOH   D O     1 
HETATM 5850 O  O     . HOH   N 7 .   ? 5.79400   -6.15300  27.72200  1.000 36.90035 ? 381 HOH   D O     1 
HETATM 5851 O  O     . HOH   N 7 .   ? 22.638    -6.645    25.055    1.000 40.79961 ? 382 HOH   D O     1 
HETATM 5852 O  O     . HOH   N 7 .   ? -5.58700  0.86900   15.59900  1.000 41.47137 ? 383 HOH   D O     1 
HETATM 5853 O  O     . HOH   N 7 .   ? 21.08700  -4.24200  26.53200  1.000 40.74914 ? 384 HOH   D O     1 
HETATM 5854 O  O     . HOH   N 7 .   ? 1.59300   -3.55300  23.65000  1.000 36.17910 ? 385 HOH   D O     1 
HETATM 5855 O  O     . HOH   N 7 .   ? -0.29100  18.90800  4.62500   1.000 37.30841 ? 386 HOH   D O     1 
HETATM 5856 O  O     . HOH   N 7 .   ? 7.55400   8.97300   -2.71800  1.000 44.53573 ? 387 HOH   D O     1 
HETATM 5857 O  O     . HOH   N 7 .   ? 1.10000   -3.34900  25.80700  1.000 45.11900 ? 388 HOH   D O     1 
HETATM 5858 O  O     . HOH   N 7 .   ? -5.21200  2.36300   24.82300  1.000 36.19394 ? 389 HOH   D O     1 
HETATM 5859 O  O     . HOH   N 7 .   ? 26.87800  14.24300  23.07300  1.000 42.66281 ? 390 HOH   D O     1 
HETATM 5860 O  O     . HOH   N 7 .   ? 9.74200   11.08400  -2.42400  1.000 44.17597 ? 391 HOH   D O     1 
HETATM 5861 O  O     . HOH   N 7 .   ? 7.22800   11.59300  0.81800   1.000 32.59349 ? 392 HOH   D O     1 
HETATM 5862 O  O     . HOH   N 7 .   ? 3.24800   21.42500  9.64100   1.000 36.30475 ? 393 HOH   D O     1 
HETATM 5863 O  O     . HOH   N 7 .   ? 31.058    16.386    2.391     1.000 45.08403 ? 394 HOH   D O     1 
HETATM 5864 O  O     . HOH   O 7 .   ? -3.31200  23.08200  30.88500  1.000 45.74503 ? 301 HOH   B O     1 
HETATM 5865 O  O     . HOH   O 7 .   ? -2.39700  16.31700  26.60100  1.000 38.69455 ? 302 HOH   B O     1 
HETATM 5866 O  O     . HOH   O 7 .   ? 3.06200   18.39400  28.68400  1.000 36.24849 ? 303 HOH   B O     1 
HETATM 5867 O  O     . HOH   O 7 .   ? 17.57400  22.74800  49.66600  1.000 38.72489 ? 304 HOH   B O     1 
HETATM 5868 O  O     . HOH   O 7 .   ? 15.85900  38.17400  33.51900  1.000 46.70285 ? 305 HOH   B O     1 
HETATM 5869 O  O     . HOH   O 7 .   ? 20.57500  15.85600  51.13200  1.000 48.11926 ? 306 HOH   B O     1 
HETATM 5870 O  O     . HOH   O 7 .   ? -14.94600 11.74900  33.86200  1.000 46.93750 ? 307 HOH   B O     1 
HETATM 5871 O  O     . HOH   O 7 .   ? 28.03500  18.77600  32.27700  1.000 37.34222 ? 308 HOH   B O     1 
HETATM 5872 O  O     . HOH   O 7 .   ? 26.58200  18.58900  46.29700  1.000 43.28052 ? 309 HOH   B O     1 
HETATM 5873 O  O     . HOH   O 7 .   ? 17.99600  2.33800   46.77800  1.000 38.81416 ? 310 HOH   B O     1 
HETATM 5874 O  O     . HOH   O 7 .   ? 4.60800   14.13800  29.60900  1.000 30.98703 ? 311 HOH   B O     1 
HETATM 5875 O  O     . HOH   O 7 .   ? 14.03400  15.23600  54.31800  1.000 31.35817 ? 312 HOH   B O     1 
HETATM 5876 O  O     . HOH   O 7 .   ? 14.06100  39.87900  33.47700  1.000 43.83863 ? 313 HOH   B O     1 
HETATM 5877 O  O     . HOH   O 7 .   ? 6.67400   30.83500  45.93600  1.000 27.87725 ? 314 HOH   B O     1 
HETATM 5878 O  O     . HOH   O 7 .   ? 27.03400  11.76400  31.09300  1.000 40.09261 ? 315 HOH   B O     1 
HETATM 5879 O  O     . HOH   O 7 .   ? -11.82300 14.81200  34.39500  1.000 34.27412 ? 316 HOH   B O     1 
HETATM 5880 O  O     . HOH   O 7 .   ? 19.08300  7.36300   43.41100  1.000 38.81231 ? 317 HOH   B O     1 
HETATM 5881 O  O     . HOH   O 7 .   ? 21.35900  21.18300  25.03900  1.000 30.56484 ? 318 HOH   B O     1 
HETATM 5882 O  O     . HOH   O 7 .   ? 22.52200  27.65700  44.07200  1.000 38.37056 ? 319 HOH   B O     1 
HETATM 5883 O  O     . HOH   O 7 .   ? 22.49500  6.70000   38.94300  1.000 38.18332 ? 320 HOH   B O     1 
HETATM 5884 O  O     . HOH   O 7 .   ? 20.05600  9.83300   44.92000  1.000 40.92078 ? 321 HOH   B O     1 
HETATM 5885 O  O     A HOH   O 7 .   ? 8.51200   31.67500  47.92100  0.500 18.78679 ? 322 HOH   B O     1 
HETATM 5886 O  O     B HOH   O 7 .   ? 9.28800   32.72400  48.05100  0.500 26.03583 ? 322 HOH   B O     1 
HETATM 5887 O  O     . HOH   O 7 .   ? 4.90000   15.85900  27.52700  1.000 30.60647 ? 323 HOH   B O     1 
HETATM 5888 O  O     . HOH   O 7 .   ? -4.96400  29.11900  41.74800  1.000 32.97922 ? 324 HOH   B O     1 
HETATM 5889 O  O     . HOH   O 7 .   ? 5.75100   6.60400   37.79900  1.000 34.12833 ? 325 HOH   B O     1 
HETATM 5890 O  O     . HOH   O 7 .   ? 7.35300   6.07400   39.98500  1.000 39.35978 ? 326 HOH   B O     1 
HETATM 5891 O  O     . HOH   O 7 .   ? 11.31800  27.85300  46.52300  1.000 17.91804 ? 327 HOH   B O     1 
HETATM 5892 O  O     . HOH   O 7 .   ? 13.03800  29.61200  25.95500  1.000 30.88565 ? 328 HOH   B O     1 
HETATM 5893 O  O     . HOH   O 7 .   ? 2.80500   26.87500  52.73200  1.000 23.97022 ? 329 HOH   B O     1 
HETATM 5894 O  O     . HOH   O 7 .   ? -3.24000  11.43600  43.83000  1.000 31.52370 ? 330 HOH   B O     1 
HETATM 5895 O  O     . HOH   O 7 .   ? 5.58300   39.55100  37.67700  1.000 41.32270 ? 331 HOH   B O     1 
HETATM 5896 O  O     . HOH   O 7 .   ? 10.71200  11.07700  60.44700  1.000 32.45553 ? 332 HOH   B O     1 
HETATM 5897 O  O     . HOH   O 7 .   ? 16.57600  17.29700  51.03100  1.000 35.55761 ? 333 HOH   B O     1 
HETATM 5898 O  O     . HOH   O 7 .   ? 17.80400  35.32200  29.49400  1.000 35.08748 ? 334 HOH   B O     1 
HETATM 5899 O  O     . HOH   O 7 .   ? 14.79000  43.14300  35.74000  1.000 49.72138 ? 335 HOH   B O     1 
HETATM 5900 O  O     . HOH   O 7 .   ? 11.02200  35.49500  52.09000  1.000 32.13986 ? 336 HOH   B O     1 
HETATM 5901 O  O     . HOH   O 7 .   ? 18.52500  22.04400  60.70000  1.000 42.07814 ? 337 HOH   B O     1 
HETATM 5902 O  O     . HOH   O 7 .   ? 10.41200  25.07200  53.08800  1.000 18.12734 ? 338 HOH   B O     1 
HETATM 5903 O  O     . HOH   O 7 .   ? 29.66900  27.90700  30.07700  1.000 36.25430 ? 339 HOH   B O     1 
HETATM 5904 O  O     . HOH   O 7 .   ? 12.14700  34.81900  43.85200  1.000 20.23828 ? 340 HOH   B O     1 
HETATM 5905 O  O     . HOH   O 7 .   ? 8.03100   31.89000  51.64900  1.000 18.84624 ? 341 HOH   B O     1 
HETATM 5906 O  O     . HOH   O 7 .   ? -9.898    10.836    41.570    1.000 28.84774 ? 342 HOH   B O     1 
HETATM 5907 O  O     . HOH   O 7 .   ? -5.910    8.083     45.395    1.000 38.30581 ? 343 HOH   B O     1 
HETATM 5908 O  O     . HOH   O 7 .   ? 3.71000   33.92400  45.59900  1.000 38.62712 ? 344 HOH   B O     1 
HETATM 5909 O  O     . HOH   O 7 .   ? 20.93600  25.65400  26.28000  1.000 40.23318 ? 345 HOH   B O     1 
HETATM 5910 O  O     . HOH   O 7 .   ? 21.45800  22.43800  53.32400  1.000 45.62901 ? 346 HOH   B O     1 
HETATM 5911 O  O     . HOH   O 7 .   ? 23.94200  24.38400  46.73300  1.000 43.06244 ? 347 HOH   B O     1 
HETATM 5912 O  O     . HOH   O 7 .   ? 21.04300  28.37500  40.86900  1.000 34.94067 ? 348 HOH   B O     1 
HETATM 5913 O  O     . HOH   O 7 .   ? -9.47800  19.05900  47.65500  1.000 24.26242 ? 349 HOH   B O     1 
HETATM 5914 O  O     . HOH   O 7 .   ? 21.83600  10.93100  27.23900  1.000 21.74512 ? 350 HOH   B O     1 
HETATM 5915 O  O     . HOH   O 7 .   ? 3.44900   8.81500   45.33900  1.000 28.09016 ? 351 HOH   B O     1 
HETATM 5916 O  O     . HOH   O 7 .   ? 12.86900  23.69200  53.60100  1.000 31.28940 ? 352 HOH   B O     1 
HETATM 5917 O  O     . HOH   O 7 .   ? 7.98800   7.82100   32.02000  1.000 40.26931 ? 353 HOH   B O     1 
HETATM 5918 O  O     . HOH   O 7 .   ? 0.51600   8.35400   33.24400  1.000 38.70611 ? 354 HOH   B O     1 
HETATM 5919 O  O     . HOH   O 7 .   ? -1.20600  23.45200  48.14300  1.000 28.42896 ? 355 HOH   B O     1 
HETATM 5920 O  O     . HOH   O 7 .   ? 12.31900  31.88300  45.96200  1.000 17.20141 ? 356 HOH   B O     1 
HETATM 5921 O  O     . HOH   O 7 .   ? 5.00800   25.94200  29.40800  1.000 22.82782 ? 357 HOH   B O     1 
HETATM 5922 O  O     . HOH   O 7 .   ? 10.468    -1.067    52.157    1.000 38.98446 ? 358 HOH   B O     1 
HETATM 5923 O  O     . HOH   O 7 .   ? 15.26800  27.95800  26.33700  1.000 33.76737 ? 359 HOH   B O     1 
HETATM 5924 O  O     . HOH   O 7 .   ? 25.37000  11.84800  34.39800  1.000 32.02656 ? 360 HOH   B O     1 
HETATM 5925 O  O     . HOH   O 7 .   ? -8.79100  13.73500  36.12800  1.000 37.93669 ? 361 HOH   B O     1 
HETATM 5926 O  O     . HOH   O 7 .   ? 1.182     0.982     42.690    1.000 41.88131 ? 362 HOH   B O     1 
HETATM 5927 O  O     . HOH   O 7 .   ? 11.72300  13.36000  60.67000  1.000 38.24305 ? 363 HOH   B O     1 
HETATM 5928 O  O     . HOH   O 7 .   ? 3.55800   35.69000  43.30100  1.000 38.39474 ? 364 HOH   B O     1 
HETATM 5929 O  O     . HOH   O 7 .   ? 5.42600   10.93900  32.34300  1.000 39.38214 ? 365 HOH   B O     1 
HETATM 5930 O  O     . HOH   O 7 .   ? 9.27400   9.18100   38.00700  1.000 22.51006 ? 366 HOH   B O     1 
HETATM 5931 O  O     . HOH   O 7 .   ? 3.01300   9.03600   53.15700  1.000 35.15034 ? 367 HOH   B O     1 
HETATM 5932 O  O     . HOH   O 7 .   ? 19.17500  33.53900  37.37900  1.000 24.18161 ? 368 HOH   B O     1 
HETATM 5933 O  O     . HOH   O 7 .   ? -6.06100  18.02100  27.79600  1.000 38.49072 ? 369 HOH   B O     1 
HETATM 5934 O  O     . HOH   O 7 .   ? 21.40100  22.02400  48.32700  1.000 40.18596 ? 370 HOH   B O     1 
HETATM 5935 O  O     . HOH   O 7 .   ? -0.03300  8.73000   45.81400  1.000 40.48853 ? 371 HOH   B O     1 
HETATM 5936 O  O     . HOH   O 7 .   ? 7.85000   33.18100  37.84800  1.000 20.91241 ? 372 HOH   B O     1 
HETATM 5937 O  O     . HOH   O 7 .   ? 15.32600  30.00700  50.74600  1.000 21.98402 ? 373 HOH   B O     1 
HETATM 5938 O  O     . HOH   O 7 .   ? 23.74600  14.81800  41.67700  1.000 28.39508 ? 374 HOH   B O     1 
HETATM 5939 O  O     . HOH   O 7 .   ? 14.550    4.307     54.397    1.000 24.11036 ? 375 HOH   B O     1 
HETATM 5940 O  O     . HOH   O 7 .   ? -5.619    4.321     32.112    1.000 39.94890 ? 376 HOH   B O     1 
HETATM 5941 O  O     . HOH   O 7 .   ? -3.75100  14.22400  46.47100  1.000 29.78217 ? 377 HOH   B O     1 
HETATM 5942 O  O     . HOH   O 7 .   ? 11.89500  7.07200   41.14100  1.000 33.11903 ? 378 HOH   B O     1 
HETATM 5943 O  O     . HOH   O 7 .   ? 22.75600  5.89900   29.56500  1.000 39.58374 ? 379 HOH   B O     1 
HETATM 5944 O  O     . HOH   O 7 .   ? 1.82500   19.51100  47.70200  1.000 27.66935 ? 380 HOH   B O     1 
HETATM 5945 O  O     . HOH   O 7 .   ? -7.958    20.294    49.238    1.000 39.74221 ? 381 HOH   B O     1 
HETATM 5946 O  O     . HOH   O 7 .   ? 11.04400  22.14200  27.46500  1.000 23.99034 ? 382 HOH   B O     1 
HETATM 5947 O  O     . HOH   O 7 .   ? 19.43000  21.36000  43.05000  1.000 19.93639 ? 383 HOH   B O     1 
HETATM 5948 O  O     . HOH   O 7 .   ? 5.44700   23.37900  28.59900  1.000 23.16934 ? 384 HOH   B O     1 
HETATM 5949 O  O     . HOH   O 7 .   ? 1.39400   11.12200  49.73200  1.000 31.80211 ? 385 HOH   B O     1 
HETATM 5950 O  O     . HOH   O 7 .   ? 21.72300  29.79200  38.63000  1.000 25.43106 ? 386 HOH   B O     1 
HETATM 5951 O  O     . HOH   O 7 .   ? 9.40800   14.54900  60.65800  1.000 26.07389 ? 387 HOH   B O     1 
HETATM 5952 O  O     . HOH   O 7 .   ? -1.23200  30.46800  47.22200  1.000 38.78125 ? 388 HOH   B O     1 
HETATM 5953 O  O     . HOH   O 7 .   ? 14.29500  21.97400  48.53900  1.000 19.18026 ? 389 HOH   B O     1 
HETATM 5954 O  O     . HOH   O 7 .   ? -4.248    22.848    48.976    1.000 37.36207 ? 390 HOH   B O     1 
HETATM 5955 O  O     . HOH   O 7 .   ? 27.35600  27.42500  27.14300  1.000 33.47946 ? 391 HOH   B O     1 
HETATM 5956 O  O     . HOH   O 7 .   ? 20.76100  31.47600  41.49100  1.000 38.02806 ? 392 HOH   B O     1 
HETATM 5957 O  O     . HOH   O 7 .   ? 14.41900  7.90400   31.98500  1.000 33.82293 ? 393 HOH   B O     1 
HETATM 5958 O  O     . HOH   O 7 .   ? 7.857     1.269     54.214    1.000 28.91757 ? 394 HOH   B O     1 
HETATM 5959 O  O     . HOH   O 7 .   ? 9.62600   -0.11400  49.42700  1.000 42.88289 ? 395 HOH   B O     1 
HETATM 5960 O  O     . HOH   O 7 .   ? 22.83200  27.04400  50.02200  1.000 39.26717 ? 396 HOH   B O     1 
HETATM 5961 O  O     . HOH   O 7 .   ? 27.66500  29.15800  34.67400  1.000 37.62829 ? 397 HOH   B O     1 
HETATM 5962 O  O     . HOH   O 7 .   ? 18.86000  35.97700  39.05200  1.000 36.97035 ? 398 HOH   B O     1 
HETATM 5963 O  O     . HOH   O 7 .   ? 14.25200  24.30200  27.47400  1.000 32.47356 ? 399 HOH   B O     1 
HETATM 5964 O  O     . HOH   O 7 .   ? 9.66000   8.78300   57.28700  1.000 30.01772 ? 400 HOH   B O     1 
HETATM 5965 O  O     . HOH   O 7 .   ? 21.90400  32.82300  36.93500  1.000 32.68646 ? 401 HOH   B O     1 
HETATM 5966 O  O     . HOH   O 7 .   ? -10.42200 11.75900  36.19800  1.000 41.81793 ? 402 HOH   B O     1 
HETATM 5967 O  O     . HOH   O 7 .   ? 15.81300  4.17600   32.09600  1.000 36.40397 ? 403 HOH   B O     1 
HETATM 5968 O  O     . HOH   O 7 .   ? 22.10600  6.60900   31.61300  1.000 37.95312 ? 404 HOH   B O     1 
HETATM 5969 O  O     . HOH   O 7 .   ? 6.92100   25.17000  26.39000  1.000 26.57052 ? 405 HOH   B O     1 
HETATM 5970 O  O     . HOH   O 7 .   ? -4.14600  29.96400  33.95800  1.000 44.46746 ? 406 HOH   B O     1 
HETATM 5971 O  O     . HOH   O 7 .   ? 5.81200   34.17500  49.35100  1.000 33.14700 ? 407 HOH   B O     1 
HETATM 5972 O  O     . HOH   O 7 .   ? 30.93900  23.22100  32.25600  1.000 46.59894 ? 408 HOH   B O     1 
HETATM 5973 O  O     . HOH   O 7 .   ? 11.27900  0.18800   46.83200  1.000 40.02706 ? 409 HOH   B O     1 
HETATM 5974 O  O     . HOH   O 7 .   ? 7.72900   29.59800  25.66700  1.000 36.06107 ? 410 HOH   B O     1 
HETATM 5975 O  O     . HOH   O 7 .   ? 6.09100   37.95500  33.29800  1.000 32.26566 ? 411 HOH   B O     1 
HETATM 5976 O  O     . HOH   O 7 .   ? -1.42500  25.14000  34.15600  1.000 39.17059 ? 412 HOH   B O     1 
HETATM 5977 O  O     . HOH   O 7 .   ? 17.81000  36.30600  34.55100  1.000 37.18553 ? 413 HOH   B O     1 
HETATM 5978 O  O     . HOH   O 7 .   ? 20.88800  24.85700  48.71800  1.000 36.62723 ? 414 HOH   B O     1 
HETATM 5979 O  O     . HOH   O 7 .   ? 1.57600   30.01800  50.70300  1.000 32.17926 ? 415 HOH   B O     1 
HETATM 5980 O  O     . HOH   O 7 .   ? 21.08000  19.82100  31.69600  1.000 32.91911 ? 416 HOH   B O     1 
HETATM 5981 O  O     . HOH   O 7 .   ? 4.184     17.824    51.329    1.000 26.52975 ? 417 HOH   B O     1 
HETATM 5982 O  O     . HOH   O 7 .   ? 10.96500  13.89000  29.55100  1.000 31.64552 ? 418 HOH   B O     1 
HETATM 5983 O  O     . HOH   O 7 .   ? 0.65800   13.07800  55.32900  1.000 34.83340 ? 419 HOH   B O     1 
HETATM 5984 O  O     . HOH   O 7 .   ? 15.66000  11.60900  56.40100  1.000 40.28315 ? 420 HOH   B O     1 
HETATM 5985 O  O     . HOH   O 7 .   ? 0.41000   22.43000  51.27800  1.000 39.51776 ? 421 HOH   B O     1 
HETATM 5986 O  O     . HOH   O 7 .   ? 12.75800  2.86000   40.26200  1.000 46.66422 ? 422 HOH   B O     1 
HETATM 5987 O  O     . HOH   O 7 .   ? 2.91900   29.61700  53.37700  1.000 32.09807 ? 423 HOH   B O     1 
HETATM 5988 O  O     . HOH   O 7 .   ? 15.72100  17.17300  53.53000  1.000 32.66009 ? 424 HOH   B O     1 
HETATM 5989 O  O     . HOH   O 7 .   ? 17.29000  28.48300  54.64400  1.000 32.24608 ? 425 HOH   B O     1 
HETATM 5990 O  O     A HOH   O 7 .   ? 9.05900   20.30000  27.08000  0.500 16.85605 ? 426 HOH   B O     1 
HETATM 5991 O  O     B HOH   O 7 .   ? 7.12000   22.13200  26.32000  0.500 24.15525 ? 426 HOH   B O     1 
HETATM 5992 O  O     A HOH   O 7 .   ? 18.03300  19.33700  60.81700  0.500 33.42459 ? 427 HOH   B O     1 
HETATM 5993 O  O     B HOH   O 7 .   ? 19.14600  19.20900  59.71100  0.500 37.25653 ? 427 HOH   B O     1 
HETATM 5994 O  O     . HOH   O 7 .   ? 5.56200   8.25700   52.25800  1.000 27.96880 ? 428 HOH   B O     1 
HETATM 5995 O  O     . HOH   O 7 .   ? 16.23300  37.17300  36.81300  1.000 32.18430 ? 429 HOH   B O     1 
HETATM 5996 O  O     . HOH   O 7 .   ? 7.44800   15.51700  27.20000  1.000 26.47771 ? 430 HOH   B O     1 
HETATM 5997 O  O     . HOH   O 7 .   ? 24.84200  17.79300  25.89900  1.000 27.05686 ? 431 HOH   B O     1 
HETATM 5998 O  O     . HOH   O 7 .   ? 17.36400  39.76400  43.20800  1.000 40.40359 ? 432 HOH   B O     1 
HETATM 5999 O  O     . HOH   O 7 .   ? -2.61100  29.26100  44.74800  1.000 23.77639 ? 433 HOH   B O     1 
HETATM 6000 O  O     . HOH   O 7 .   ? 8.44300   15.27900  29.32700  1.000 36.49001 ? 434 HOH   B O     1 
HETATM 6001 O  O     . HOH   O 7 .   ? 3.20200   9.03400   48.60600  1.000 31.52345 ? 435 HOH   B O     1 
HETATM 6002 O  O     . HOH   O 7 .   ? 24.46600  26.22200  44.27200  1.000 41.65512 ? 436 HOH   B O     1 
HETATM 6003 O  O     . HOH   O 7 .   ? -2.83300  18.44700  28.47700  1.000 40.18896 ? 437 HOH   B O     1 
HETATM 6004 O  O     . HOH   O 7 .   ? 14.01900  10.84600  30.63400  1.000 31.19873 ? 438 HOH   B O     1 
HETATM 6005 O  O     . HOH   O 7 .   ? 21.16900  31.09800  55.57000  1.000 33.02939 ? 439 HOH   B O     1 
HETATM 6006 O  O     . HOH   O 7 .   ? 17.09500  28.22000  51.76100  1.000 25.64273 ? 440 HOH   B O     1 
HETATM 6007 O  O     . HOH   O 7 .   ? 12.27300  5.13700   39.50000  1.000 46.61469 ? 441 HOH   B O     1 
HETATM 6008 O  O     . HOH   O 7 .   ? -5.44100  23.88300  32.25600  1.000 42.35624 ? 442 HOH   B O     1 
HETATM 6009 O  O     . HOH   O 7 .   ? 24.49900  20.62500  26.43200  1.000 26.78821 ? 443 HOH   B O     1 
HETATM 6010 O  O     . HOH   O 7 .   ? 24.79500  32.00000  33.20600  1.000 35.89726 ? 444 HOH   B O     1 
HETATM 6011 O  O     . HOH   O 7 .   ? -1.70300  31.79200  43.98600  1.000 32.90305 ? 445 HOH   B O     1 
HETATM 6012 O  O     . HOH   O 7 .   ? 12.25400  20.88700  61.63300  1.000 31.24342 ? 446 HOH   B O     1 
HETATM 6013 O  O     . HOH   O 7 .   ? 19.32700  29.54100  25.06900  1.000 39.41619 ? 447 HOH   B O     1 
HETATM 6014 O  O     . HOH   O 7 .   ? 18.06200  27.68700  57.48400  1.000 31.91193 ? 448 HOH   B O     1 
HETATM 6015 O  O     . HOH   O 7 .   ? 15.86900  8.61700   29.80800  1.000 29.45810 ? 449 HOH   B O     1 
HETATM 6016 O  O     . HOH   O 7 .   ? 28.57400  26.64200  37.47800  1.000 33.83080 ? 450 HOH   B O     1 
HETATM 6017 O  O     . HOH   O 7 .   ? 14.684    39.939    29.295    1.000 39.53875 ? 451 HOH   B O     1 
HETATM 6018 O  O     . HOH   O 7 .   ? 26.804    30.925    37.407    1.000 34.80866 ? 452 HOH   B O     1 
HETATM 6019 O  O     . HOH   O 7 .   ? -14.53400 21.32600  38.40300  1.000 39.84287 ? 453 HOH   B O     1 
HETATM 6020 O  O     . HOH   O 7 .   ? 8.12400   37.51200  45.51700  1.000 48.55318 ? 454 HOH   B O     1 
HETATM 6021 O  O     . HOH   O 7 .   ? 14.66800  19.40600  62.46600  1.000 35.62380 ? 455 HOH   B O     1 
HETATM 6022 O  O     . HOH   O 7 .   ? 11.03200  40.56500  46.31600  1.000 45.04587 ? 456 HOH   B O     1 
HETATM 6023 O  O     . HOH   O 7 .   ? 27.202    31.867    33.999    1.000 38.81558 ? 457 HOH   B O     1 
HETATM 6024 O  O     . HOH   O 7 .   ? -14.83900 23.72700  35.80600  1.000 41.79287 ? 458 HOH   B O     1 
HETATM 6025 O  O     . HOH   O 7 .   ? -12.338   9.058     41.258    1.000 33.58448 ? 459 HOH   B O     1 
HETATM 6026 O  O     . HOH   O 7 .   ? -5.69500  26.22500  33.94200  1.000 46.09831 ? 460 HOH   B O     1 
HETATM 6027 O  O     . HOH   O 7 .   ? 12.26400  10.05000  57.96900  1.000 34.84673 ? 461 HOH   B O     1 
HETATM 6028 O  O     . HOH   O 7 .   ? 17.97600  16.37900  54.92900  1.000 46.88563 ? 462 HOH   B O     1 
HETATM 6029 O  O     . HOH   O 7 .   ? 16.745    39.297    28.311    1.000 47.11773 ? 463 HOH   B O     1 
HETATM 6030 O  O     . HOH   O 7 .   ? 20.93000  4.36200   32.61900  1.000 37.00050 ? 464 HOH   B O     1 
HETATM 6031 O  O     . HOH   O 7 .   ? -9.40100  24.51300  34.48300  1.000 44.19782 ? 465 HOH   B O     1 
HETATM 6032 O  O     . HOH   O 7 .   ? -3.20400  27.63000  48.81300  1.000 39.95370 ? 466 HOH   B O     1 
HETATM 6033 O  O     . HOH   O 7 .   ? 0.357     2.784     44.339    1.000 42.11765 ? 467 HOH   B O     1 
HETATM 6034 O  O     . HOH   O 7 .   ? 10.02900  6.68900   39.14100  1.000 38.93218 ? 468 HOH   B O     1 
HETATM 6035 O  O     . HOH   O 7 .   ? 28.605    26.332    41.040    1.000 35.20796 ? 469 HOH   B O     1 
HETATM 6036 O  O     . HOH   O 7 .   ? 5.77900   3.82900   38.56700  1.000 44.63987 ? 470 HOH   B O     1 
HETATM 6037 O  O     . HOH   O 7 .   ? 24.64500  9.07700   35.08000  1.000 38.22758 ? 471 HOH   B O     1 
HETATM 6038 O  O     . HOH   O 7 .   ? 6.11300   27.62400  26.06900  1.000 39.76463 ? 472 HOH   B O     1 
HETATM 6039 O  O     . HOH   O 7 .   ? -10.39800 26.48200  35.83100  1.000 41.94795 ? 473 HOH   B O     1 
HETATM 6040 O  O     . HOH   O 7 .   ? 13.40100  11.30700  27.86000  1.000 27.38929 ? 474 HOH   B O     1 
HETATM 6041 O  O     . HOH   O 7 .   ? 20.29100  26.25000  61.58500  1.000 47.40155 ? 475 HOH   B O     1 
HETATM 6042 O  O     . HOH   O 7 .   ? 0.55500   21.55400  48.91200  1.000 32.60182 ? 476 HOH   B O     1 
HETATM 6043 O  O     . HOH   O 7 .   ? 7.261     4.060     54.707    1.000 26.20118 ? 477 HOH   B O     1 
HETATM 6044 O  O     . HOH   O 7 .   ? -4.098    -1.220    34.266    1.000 43.15634 ? 478 HOH   B O     1 
HETATM 6045 O  O     . HOH   O 7 .   ? 5.663     7.351     56.806    1.000 32.24183 ? 479 HOH   B O     1 
HETATM 6046 O  O     . HOH   O 7 .   ? 24.88300  7.02700   33.40300  1.000 43.53880 ? 480 HOH   B O     1 
HETATM 6047 O  O     . HOH   O 7 .   ? 7.99300   33.28800  45.91800  1.000 34.10664 ? 481 HOH   B O     1 
HETATM 6048 O  O     . HOH   O 7 .   ? 31.57800  27.08800  31.12100  1.000 38.37622 ? 482 HOH   B O     1 
HETATM 6049 O  O     . HOH   O 7 .   ? -2.250    25.234    52.084    1.000 36.59831 ? 483 HOH   B O     1 
HETATM 6050 O  O     . HOH   O 7 .   ? 12.70100  20.91600  25.69000  1.000 27.17473 ? 484 HOH   B O     1 
HETATM 6051 O  O     . HOH   O 7 .   ? 24.22400  30.58500  39.68300  1.000 38.64216 ? 485 HOH   B O     1 
HETATM 6052 O  O     . HOH   O 7 .   ? -5.933    32.198    36.211    1.000 43.11166 ? 486 HOH   B O     1 
HETATM 6053 O  O     . HOH   O 7 .   ? -12.334   8.764     35.917    1.000 42.35697 ? 487 HOH   B O     1 
HETATM 6054 O  O     . HOH   O 7 .   ? 6.87000   8.19300   30.01500  1.000 42.01300 ? 488 HOH   B O     1 
HETATM 6055 O  O     . HOH   O 7 .   ? 25.82600  6.38100   28.84600  1.000 44.27612 ? 489 HOH   B O     1 
HETATM 6056 O  O     . HOH   O 7 .   ? 25.24700  13.81700  39.95000  1.000 39.13989 ? 490 HOH   B O     1 
HETATM 6057 O  O     . HOH   O 7 .   ? -6.40900  29.30700  39.84800  1.000 43.93654 ? 491 HOH   B O     1 
HETATM 6058 O  O     . HOH   O 7 .   ? 29.030    28.336    39.290    1.000 39.68370 ? 492 HOH   B O     1 
HETATM 6059 O  O     . HOH   O 7 .   ? 8.28800   1.66200   34.30100  1.000 42.65892 ? 493 HOH   B O     1 
HETATM 6060 O  O     . HOH   O 7 .   ? 9.42200   34.40800  44.19700  1.000 31.58880 ? 494 HOH   B O     1 
HETATM 6061 O  O     . HOH   O 7 .   ? 7.25000   11.97000  29.62200  1.000 40.16429 ? 495 HOH   B O     1 
HETATM 6062 O  O     . HOH   O 7 .   ? 26.96800  16.71700  25.07000  1.000 39.92970 ? 496 HOH   B O     1 
HETATM 6063 O  O     . HOH   O 7 .   ? 28.58500  13.34100  30.30400  1.000 40.65979 ? 497 HOH   B O     1 
HETATM 6064 O  O     . HOH   O 7 .   ? 0.76000   32.95100  47.67100  1.000 43.38859 ? 498 HOH   B O     1 
HETATM 6065 O  O     . HOH   O 7 .   ? 1.874     18.197    49.987    1.000 35.48440 ? 499 HOH   B O     1 
HETATM 6066 O  O     . HOH   O 7 .   ? 21.250    35.826    29.475    1.000 40.34825 ? 500 HOH   B O     1 
HETATM 6067 O  O     . HOH   O 7 .   ? 5.10700   11.53200  30.23800  1.000 36.72826 ? 501 HOH   B O     1 
HETATM 6068 O  O     . HOH   O 7 .   ? -15.39100 19.28700  36.57000  1.000 40.65322 ? 502 HOH   B O     1 
HETATM 6069 O  O     . HOH   O 7 .   ? 23.11700  36.32700  51.03100  1.000 37.11855 ? 503 HOH   B O     1 
HETATM 6070 O  O     . HOH   O 7 .   ? 19.92300  28.87400  55.34200  1.000 37.78946 ? 504 HOH   B O     1 
HETATM 6071 O  O     . HOH   O 7 .   ? 23.76200  34.08200  50.02500  1.000 33.61205 ? 505 HOH   B O     1 
HETATM 6072 O  O     . HOH   O 7 .   ? -0.33100  31.25800  51.71700  1.000 38.65338 ? 506 HOH   B O     1 
HETATM 6073 O  O     . HOH   P 7 .   ? 36.933    44.918    51.878    1.000 43.60554 ? 201 HOH   C O     1 
HETATM 6074 O  O     . HOH   P 7 .   ? 27.506    30.145    76.316    1.000 40.51883 ? 202 HOH   C O     1 
HETATM 6075 O  O     . HOH   P 7 .   ? 30.40100  50.49900  75.76200  1.000 36.52657 ? 203 HOH   C O     1 
HETATM 6076 O  O     . HOH   P 7 .   ? 9.57600   35.51000  54.68500  1.000 35.35504 ? 204 HOH   C O     1 
HETATM 6077 O  O     . HOH   P 7 .   ? 7.35800   37.03900  75.18200  1.000 32.90040 ? 205 HOH   C O     1 
HETATM 6078 O  O     . HOH   P 7 .   ? 11.18800  27.39600  70.72700  1.000 39.19103 ? 206 HOH   C O     1 
HETATM 6079 O  O     . HOH   P 7 .   ? 16.27400  60.07800  64.68400  1.000 48.36224 ? 207 HOH   C O     1 
HETATM 6080 O  O     . HOH   P 7 .   ? -3.21000  43.22400  59.41800  1.000 38.76790 ? 208 HOH   C O     1 
HETATM 6081 O  O     . HOH   P 7 .   ? 20.57200  51.08700  48.69800  1.000 46.75592 ? 209 HOH   C O     1 
HETATM 6082 O  O     . HOH   P 7 .   ? 29.74800  49.75800  55.19800  1.000 44.25679 ? 210 HOH   C O     1 
HETATM 6083 O  O     . HOH   P 7 .   ? 23.21100  25.28100  72.52900  1.000 37.16511 ? 211 HOH   C O     1 
HETATM 6084 O  O     . HOH   P 7 .   ? 6.17600   48.70100  76.60200  1.000 34.99292 ? 212 HOH   C O     1 
HETATM 6085 O  O     . HOH   P 7 .   ? 20.22900  28.10400  73.91300  1.000 31.37229 ? 213 HOH   C O     1 
HETATM 6086 O  O     . HOH   P 7 .   ? 9.64700   53.23500  55.88500  1.000 26.66137 ? 214 HOH   C O     1 
HETATM 6087 O  O     . HOH   P 7 .   ? 1.72900   41.38900  75.71200  1.000 43.26461 ? 215 HOH   C O     1 
HETATM 6088 O  O     . HOH   P 7 .   ? 28.880    52.007    84.628    1.000 27.02062 ? 216 HOH   C O     1 
HETATM 6089 O  O     . HOH   P 7 .   ? 4.95300   35.92400  71.80600  1.000 36.46348 ? 217 HOH   C O     1 
HETATM 6090 O  O     . HOH   P 7 .   ? 25.17300  54.64500  60.95400  1.000 28.58146 ? 218 HOH   C O     1 
HETATM 6091 O  O     . HOH   P 7 .   ? 31.125    52.748    78.846    1.000 31.57801 ? 219 HOH   C O     1 
HETATM 6092 O  O     . HOH   P 7 .   ? 15.88200  37.69100  54.77200  1.000 28.60177 ? 220 HOH   C O     1 
HETATM 6093 O  O     . HOH   P 7 .   ? 23.50700  40.32900  59.07900  1.000 24.44228 ? 221 HOH   C O     1 
HETATM 6094 O  O     . HOH   P 7 .   ? 14.63900  46.66900  59.78100  1.000 23.61707 ? 222 HOH   C O     1 
HETATM 6095 O  O     . HOH   P 7 .   ? -0.70000  43.44700  67.32000  1.000 33.80221 ? 223 HOH   C O     1 
HETATM 6096 O  O     . HOH   P 7 .   ? 5.891     25.250    61.306    1.000 29.55694 ? 224 HOH   C O     1 
HETATM 6097 O  O     . HOH   P 7 .   ? 26.77500  28.95500  71.40300  1.000 42.20695 ? 225 HOH   C O     1 
HETATM 6098 O  O     . HOH   P 7 .   ? 33.643    46.157    75.360    1.000 39.14978 ? 226 HOH   C O     1 
HETATM 6099 O  O     . HOH   P 7 .   ? 23.01300  51.52600  78.71300  1.000 31.47175 ? 227 HOH   C O     1 
HETATM 6100 O  O     . HOH   P 7 .   ? 25.99900  35.73800  62.94300  1.000 24.57590 ? 228 HOH   C O     1 
HETATM 6101 O  O     . HOH   P 7 .   ? 23.14200  24.73100  67.99000  1.000 40.39550 ? 229 HOH   C O     1 
HETATM 6102 O  O     . HOH   P 7 .   ? 19.49300  54.59300  61.63400  1.000 29.87684 ? 230 HOH   C O     1 
HETATM 6103 O  O     . HOH   P 7 .   ? 16.99400  34.28300  78.25700  1.000 27.13970 ? 231 HOH   C O     1 
HETATM 6104 O  O     . HOH   P 7 .   ? 25.54900  58.09500  70.73900  1.000 42.93412 ? 232 HOH   C O     1 
HETATM 6105 O  O     . HOH   P 7 .   ? 25.61800  44.08300  64.67000  1.000 23.66303 ? 233 HOH   C O     1 
HETATM 6106 O  O     . HOH   P 7 .   ? 11.47500  36.74400  54.11100  1.000 32.83055 ? 234 HOH   C O     1 
HETATM 6107 O  O     . HOH   P 7 .   ? 7.66900   50.56700  75.30600  1.000 31.51602 ? 235 HOH   C O     1 
HETATM 6108 O  O     . HOH   P 7 .   ? 16.41900  52.52500  56.35700  1.000 29.70760 ? 236 HOH   C O     1 
HETATM 6109 O  O     . HOH   P 7 .   ? 4.22800   30.41700  62.91400  1.000 30.42157 ? 237 HOH   C O     1 
HETATM 6110 O  O     . HOH   P 7 .   ? 1.33800   43.07000  73.29400  1.000 30.10622 ? 238 HOH   C O     1 
HETATM 6111 O  O     . HOH   P 7 .   ? 32.08100  52.97800  65.01100  1.000 41.38699 ? 239 HOH   C O     1 
HETATM 6112 O  O     . HOH   P 7 .   ? 24.60500  37.62900  55.22100  1.000 31.28156 ? 240 HOH   C O     1 
HETATM 6113 O  O     . HOH   P 7 .   ? 21.46900  34.33600  76.33400  1.000 21.55180 ? 241 HOH   C O     1 
HETATM 6114 O  O     . HOH   P 7 .   ? -3.41200  50.60800  57.50500  1.000 36.52454 ? 242 HOH   C O     1 
HETATM 6115 O  O     . HOH   P 7 .   ? 13.14000  38.45100  50.96200  1.000 29.96323 ? 243 HOH   C O     1 
HETATM 6116 O  O     . HOH   P 7 .   ? 13.41000  45.79200  46.62100  1.000 45.23283 ? 244 HOH   C O     1 
HETATM 6117 O  O     . HOH   P 7 .   ? 34.44300  38.94700  74.60400  1.000 33.48494 ? 245 HOH   C O     1 
HETATM 6118 O  O     . HOH   P 7 .   ? 35.85900  40.41300  70.18400  1.000 31.81213 ? 246 HOH   C O     1 
HETATM 6119 O  O     . HOH   P 7 .   ? 13.824    30.916    78.452    1.000 38.23807 ? 247 HOH   C O     1 
HETATM 6120 O  O     . HOH   P 7 .   ? 34.11600  48.22700  66.35200  1.000 32.82185 ? 248 HOH   C O     1 
HETATM 6121 O  O     . HOH   P 7 .   ? 26.49900  34.18100  70.05900  1.000 20.21097 ? 249 HOH   C O     1 
HETATM 6122 O  O     . HOH   P 7 .   ? 14.00700  40.45200  76.92000  1.000 25.65854 ? 250 HOH   C O     1 
HETATM 6123 O  O     . HOH   P 7 .   ? 8.04000   56.27600  71.38100  1.000 40.10299 ? 251 HOH   C O     1 
HETATM 6124 O  O     . HOH   P 7 .   ? 13.53000  47.23700  54.88000  1.000 21.79841 ? 252 HOH   C O     1 
HETATM 6125 O  O     . HOH   P 7 .   ? 23.91200  59.52400  53.75500  1.000 40.75487 ? 253 HOH   C O     1 
HETATM 6126 O  O     . HOH   P 7 .   ? 31.96400  31.19600  62.15800  1.000 35.37029 ? 254 HOH   C O     1 
HETATM 6127 O  O     . HOH   P 7 .   ? 5.11200   51.31600  59.07500  1.000 23.37321 ? 255 HOH   C O     1 
HETATM 6128 O  O     . HOH   P 7 .   ? 28.47300  45.33100  54.77800  1.000 33.67718 ? 256 HOH   C O     1 
HETATM 6129 O  O     . HOH   P 7 .   ? 2.18900   37.61000  69.77300  1.000 32.65816 ? 257 HOH   C O     1 
HETATM 6130 O  O     . HOH   P 7 .   ? 6.41500   54.30900  67.48100  1.000 29.65067 ? 258 HOH   C O     1 
HETATM 6131 O  O     . HOH   P 7 .   ? 23.56300  53.84000  75.80600  1.000 26.49617 ? 259 HOH   C O     1 
HETATM 6132 O  O     . HOH   P 7 .   ? 19.52900  42.01100  79.00800  1.000 33.37504 ? 260 HOH   C O     1 
HETATM 6133 O  O     . HOH   P 7 .   ? 27.68800  35.18500  59.75000  1.000 26.49438 ? 261 HOH   C O     1 
HETATM 6134 O  O     . HOH   P 7 .   ? 30.90600  48.00800  71.41300  1.000 33.16766 ? 262 HOH   C O     1 
HETATM 6135 O  O     . HOH   P 7 .   ? 14.40000  44.50000  56.31800  1.000 20.23731 ? 263 HOH   C O     1 
HETATM 6136 O  O     . HOH   P 7 .   ? 20.29200  29.30900  60.48800  1.000 35.59553 ? 264 HOH   C O     1 
HETATM 6137 O  O     . HOH   P 7 .   ? 6.66100   44.63900  57.52500  1.000 22.03167 ? 265 HOH   C O     1 
HETATM 6138 O  O     . HOH   P 7 .   ? 27.97200  35.94500  71.63600  1.000 18.90128 ? 266 HOH   C O     1 
HETATM 6139 O  O     . HOH   P 7 .   ? 8.90000   37.70200  54.34900  1.000 31.62168 ? 267 HOH   C O     1 
HETATM 6140 O  O     . HOH   P 7 .   ? 4.888     56.799    63.628    1.000 34.45433 ? 268 HOH   C O     1 
HETATM 6141 O  O     . HOH   P 7 .   ? 14.53800  35.37900  77.70200  1.000 27.87869 ? 269 HOH   C O     1 
HETATM 6142 O  O     . HOH   P 7 .   ? 29.74600  38.74400  64.78600  1.000 24.49396 ? 270 HOH   C O     1 
HETATM 6143 O  O     . HOH   P 7 .   ? 15.57800  23.12100  77.21400  1.000 36.03218 ? 271 HOH   C O     1 
HETATM 6144 O  O     . HOH   P 7 .   ? 30.99000  56.92800  64.10000  1.000 44.44095 ? 272 HOH   C O     1 
HETATM 6145 O  O     . HOH   P 7 .   ? 24.91300  31.44000  69.24500  1.000 23.00978 ? 273 HOH   C O     1 
HETATM 6146 O  O     . HOH   P 7 .   ? 31.36200  37.65000  54.13800  1.000 36.48378 ? 274 HOH   C O     1 
HETATM 6147 O  O     . HOH   P 7 .   ? 16.76900  42.49500  79.36400  1.000 29.24557 ? 275 HOH   C O     1 
HETATM 6148 O  O     . HOH   P 7 .   ? 7.32900   36.23200  73.01800  1.000 39.81368 ? 276 HOH   C O     1 
HETATM 6149 O  O     . HOH   P 7 .   ? 23.08000  40.55600  52.04500  1.000 34.13527 ? 277 HOH   C O     1 
HETATM 6150 O  O     . HOH   P 7 .   ? 20.67100  37.79500  50.18100  1.000 34.25323 ? 278 HOH   C O     1 
HETATM 6151 O  O     . HOH   P 7 .   ? 27.48000  50.42700  50.06200  1.000 37.51248 ? 279 HOH   C O     1 
HETATM 6152 O  O     . HOH   P 7 .   ? 34.336    43.792    75.383    1.000 40.95785 ? 280 HOH   C O     1 
HETATM 6153 O  O     . HOH   P 7 .   ? 1.69400   34.60600  54.29000  1.000 27.96981 ? 281 HOH   C O     1 
HETATM 6154 O  O     . HOH   P 7 .   ? 15.28800  51.14700  78.32000  1.000 33.70419 ? 282 HOH   C O     1 
HETATM 6155 O  O     . HOH   P 7 .   ? 28.66700  29.10800  62.40000  1.000 34.22494 ? 283 HOH   C O     1 
HETATM 6156 O  O     . HOH   P 7 .   ? 7.70400   54.56400  59.21400  1.000 33.51372 ? 284 HOH   C O     1 
HETATM 6157 O  O     . HOH   P 7 .   ? 6.72400   41.18100  54.89300  1.000 28.01766 ? 285 HOH   C O     1 
HETATM 6158 O  O     . HOH   P 7 .   ? 8.27000   46.98500  78.85800  1.000 32.35033 ? 286 HOH   C O     1 
HETATM 6159 O  O     . HOH   P 7 .   ? 27.84200  31.18000  61.43300  1.000 33.01034 ? 287 HOH   C O     1 
HETATM 6160 O  O     . HOH   P 7 .   ? 0.51900   38.10000  57.31200  1.000 34.59408 ? 288 HOH   C O     1 
HETATM 6161 O  O     . HOH   P 7 .   ? 35.39900  37.66100  71.23500  1.000 31.31932 ? 289 HOH   C O     1 
HETATM 6162 O  O     . HOH   P 7 .   ? 13.14400  39.88400  47.50100  1.000 33.18167 ? 290 HOH   C O     1 
HETATM 6163 O  O     . HOH   P 7 .   ? 0.394     59.301    59.634    1.000 31.82837 ? 291 HOH   C O     1 
HETATM 6164 O  O     . HOH   P 7 .   ? 18.48700  52.53000  49.55400  1.000 35.81427 ? 292 HOH   C O     1 
HETATM 6165 O  O     . HOH   P 7 .   ? 29.19900  49.86500  71.27500  1.000 30.85139 ? 293 HOH   C O     1 
HETATM 6166 O  O     . HOH   P 7 .   ? 10.04300  44.10300  78.10600  1.000 27.39117 ? 294 HOH   C O     1 
HETATM 6167 O  O     . HOH   P 7 .   ? 8.24100   34.38500  52.39700  1.000 30.46728 ? 295 HOH   C O     1 
HETATM 6168 O  O     . HOH   P 7 .   ? 12.64300  55.44600  76.42200  1.000 33.57286 ? 296 HOH   C O     1 
HETATM 6169 O  O     . HOH   P 7 .   ? 22.66500  42.12900  56.22300  1.000 27.63510 ? 297 HOH   C O     1 
HETATM 6170 O  O     . HOH   P 7 .   ? 28.17200  54.34800  73.37400  1.000 34.14680 ? 298 HOH   C O     1 
HETATM 6171 O  O     . HOH   P 7 .   ? 2.30200   27.51000  61.35500  1.000 23.99919 ? 299 HOH   C O     1 
HETATM 6172 O  O     . HOH   P 7 .   ? 0.07600   31.89800  58.46600  1.000 33.93511 ? 300 HOH   C O     1 
HETATM 6173 O  O     . HOH   P 7 .   ? 21.94300  31.26100  58.02800  1.000 35.41411 ? 301 HOH   C O     1 
HETATM 6174 O  O     . HOH   P 7 .   ? 5.81900   52.11400  74.00700  1.000 29.84010 ? 302 HOH   C O     1 
HETATM 6175 O  O     . HOH   P 7 .   ? 6.65800   44.54100  78.06000  1.000 28.10903 ? 303 HOH   C O     1 
HETATM 6176 O  O     . HOH   P 7 .   ? 16.13800  32.68500  71.87700  1.000 22.73839 ? 304 HOH   C O     1 
HETATM 6177 O  O     . HOH   P 7 .   ? -1.10000  38.66900  59.88200  1.000 40.31024 ? 305 HOH   C O     1 
HETATM 6178 O  O     . HOH   P 7 .   ? 20.83900  58.59000  68.83300  1.000 30.41981 ? 306 HOH   C O     1 
HETATM 6179 O  O     . HOH   P 7 .   ? 14.576    57.167    56.953    1.000 33.24506 ? 307 HOH   C O     1 
HETATM 6180 O  O     . HOH   P 7 .   ? 18.63000  56.92300  63.40800  1.000 31.38732 ? 308 HOH   C O     1 
HETATM 6181 O  O     . HOH   P 7 .   ? 29.56000  57.77200  68.81200  1.000 42.97953 ? 309 HOH   C O     1 
HETATM 6182 O  O     . HOH   P 7 .   ? 30.05600  48.31200  52.65300  1.000 41.80910 ? 310 HOH   C O     1 
HETATM 6183 O  O     . HOH   P 7 .   ? 2.29000   31.98800  55.12500  1.000 32.52080 ? 311 HOH   C O     1 
HETATM 6184 O  O     . HOH   P 7 .   ? 24.21700  42.88500  50.83900  1.000 44.16726 ? 312 HOH   C O     1 
HETATM 6185 O  O     . HOH   P 7 .   ? 29.38800  26.12500  65.34700  1.000 37.72076 ? 313 HOH   C O     1 
HETATM 6186 O  O     . HOH   P 7 .   ? 13.43100  44.59400  53.52400  1.000 23.20608 ? 314 HOH   C O     1 
HETATM 6187 O  O     . HOH   P 7 .   ? 10.693    30.194    75.273    1.000 33.67577 ? 315 HOH   C O     1 
HETATM 6188 O  O     . HOH   P 7 .   ? 13.81400  59.90600  71.50400  1.000 41.39280 ? 316 HOH   C O     1 
HETATM 6189 O  O     . HOH   P 7 .   ? 27.16300  46.57000  81.23700  1.000 40.55894 ? 317 HOH   C O     1 
HETATM 6190 O  O     . HOH   P 7 .   ? 35.97700  43.99900  59.69600  1.000 46.92491 ? 318 HOH   C O     1 
HETATM 6191 O  O     . HOH   P 7 .   ? 3.77000   49.98100  76.05500  1.000 40.20161 ? 319 HOH   C O     1 
HETATM 6192 O  O     . HOH   P 7 .   ? 33.38800  51.71500  62.00900  1.000 47.18865 ? 320 HOH   C O     1 
HETATM 6193 O  O     . HOH   P 7 .   ? 25.20300  53.84700  78.43500  1.000 37.41386 ? 321 HOH   C O     1 
HETATM 6194 O  O     A HOH   P 7 .   ? 36.80900  35.60800  70.18900  0.250 27.56260 ? 322 HOH   C O     1 
HETATM 6195 O  O     C HOH   P 7 .   ? 36.48900  34.41800  68.87400  0.500 31.12528 ? 322 HOH   C O     1 
HETATM 6196 O  O     . HOH   P 7 .   ? 12.23700  39.22100  77.72900  1.000 41.17775 ? 323 HOH   C O     1 
HETATM 6197 O  O     . HOH   P 7 .   ? 24.40200  47.02400  81.54800  1.000 47.04600 ? 324 HOH   C O     1 
HETATM 6198 O  O     . HOH   P 7 .   ? 6.59500   55.03200  70.12500  1.000 41.58252 ? 325 HOH   C O     1 
HETATM 6199 O  O     . HOH   P 7 .   ? 2.58200   52.12600  55.17600  1.000 38.37739 ? 326 HOH   C O     1 
HETATM 6200 O  O     . HOH   P 7 .   ? 29.18700  43.99200  52.12700  1.000 42.90674 ? 327 HOH   C O     1 
HETATM 6201 O  O     . HOH   P 7 .   ? 19.85100  25.78200  75.80700  1.000 42.35727 ? 328 HOH   C O     1 
HETATM 6202 O  O     . HOH   P 7 .   ? 11.08700  43.91400  52.54300  1.000 33.22540 ? 329 HOH   C O     1 
HETATM 6203 O  O     . HOH   P 7 .   ? 2.85600   32.99300  68.92000  1.000 38.70330 ? 330 HOH   C O     1 
HETATM 6204 O  O     . HOH   P 7 .   ? 37.38800  34.56700  65.89600  1.000 35.07307 ? 331 HOH   C O     1 
HETATM 6205 O  O     . HOH   P 7 .   ? 35.48700  41.42200  74.72700  1.000 35.67540 ? 332 HOH   C O     1 
HETATM 6206 O  O     . HOH   P 7 .   ? 21.56500  51.03200  81.09600  1.000 42.19572 ? 333 HOH   C O     1 
HETATM 6207 O  O     . HOH   P 7 .   ? 4.766     27.273    62.850    1.000 30.48340 ? 334 HOH   C O     1 
HETATM 6208 O  O     . HOH   P 7 .   ? 34.64500  47.35400  69.18400  1.000 37.12613 ? 335 HOH   C O     1 
HETATM 6209 O  O     . HOH   P 7 .   ? 19.80400  56.32900  59.62100  1.000 36.58107 ? 336 HOH   C O     1 
HETATM 6210 O  O     . HOH   P 7 .   ? 5.09800   52.24000  56.36300  1.000 22.83014 ? 337 HOH   C O     1 
HETATM 6211 O  O     . HOH   P 7 .   ? 36.36200  49.18400  59.06900  1.000 47.86321 ? 338 HOH   C O     1 
HETATM 6212 O  O     A HOH   P 7 .   ? 1.16000   35.90000  67.15800  0.500 30.28928 ? 339 HOH   C O     1 
HETATM 6213 O  O     B HOH   P 7 .   ? 0.24900   35.60600  65.68700  0.500 30.07301 ? 339 HOH   C O     1 
HETATM 6214 O  O     . HOH   P 7 .   ? 14.39200  35.76900  80.70600  1.000 41.77601 ? 340 HOH   C O     1 
HETATM 6215 O  O     . HOH   P 7 .   ? 3.21800   56.33500  56.38200  1.000 32.55632 ? 341 HOH   C O     1 
HETATM 6216 O  O     . HOH   P 7 .   ? 2.59100   30.77400  68.20900  1.000 44.58882 ? 342 HOH   C O     1 
HETATM 6217 O  O     . HOH   P 7 .   ? 12.65000  52.97100  76.57400  1.000 39.63428 ? 343 HOH   C O     1 
HETATM 6218 O  O     . HOH   P 7 .   ? 22.49700  52.51400  52.52000  1.000 35.84069 ? 344 HOH   C O     1 
HETATM 6219 O  O     . HOH   P 7 .   ? 8.82700   37.44100  77.56700  1.000 34.26641 ? 345 HOH   C O     1 
HETATM 6220 O  O     . HOH   P 7 .   ? 35.55000  50.68000  60.79300  1.000 47.38494 ? 346 HOH   C O     1 
HETATM 6221 O  O     . HOH   P 7 .   ? -4.449    44.333    71.706    1.000 47.21203 ? 347 HOH   C O     1 
HETATM 6222 O  O     . HOH   P 7 .   ? 22.51600  51.32500  49.76700  1.000 44.72914 ? 348 HOH   C O     1 
HETATM 6223 O  O     . HOH   P 7 .   ? -0.07100  31.41000  55.82600  1.000 38.61660 ? 349 HOH   C O     1 
HETATM 6224 O  O     . HOH   P 7 .   ? -5.17800  43.24300  58.34600  1.000 44.28822 ? 350 HOH   C O     1 
HETATM 6225 O  O     . HOH   P 7 .   ? 9.83400   52.13200  76.78500  1.000 40.97639 ? 351 HOH   C O     1 
HETATM 6226 O  O     . HOH   P 7 .   ? 33.64000  49.05700  71.53500  1.000 43.54786 ? 352 HOH   C O     1 
HETATM 6227 O  O     . HOH   P 7 .   ? 6.91700   46.21400  54.76500  1.000 35.81535 ? 353 HOH   C O     1 
HETATM 6228 O  O     . HOH   P 7 .   ? 29.58200  51.59300  73.40800  1.000 36.70427 ? 354 HOH   C O     1 
HETATM 6229 O  O     . HOH   P 7 .   ? 19.75700  36.60500  48.32900  1.000 35.64535 ? 355 HOH   C O     1 
HETATM 6230 O  O     . HOH   P 7 .   ? 22.10700  28.17500  76.83500  1.000 32.55562 ? 356 HOH   C O     1 
HETATM 6231 O  O     . HOH   P 7 .   ? 8.45300   44.05300  52.73500  1.000 43.57464 ? 357 HOH   C O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . SER A 1   ? 0.44267 0.58886 0.53946 -0.13093 0.03088  0.03814  0   SER A N     
2    C CA    . SER A 1   ? 0.38583 0.54518 0.48021 -0.12541 0.04192  0.03693  0   SER A CA    
3    C C     . SER A 1   ? 0.31586 0.46935 0.40521 -0.11383 0.04207  0.03218  0   SER A C     
4    O O     . SER A 1   ? 0.33075 0.48768 0.41239 -0.10897 0.04990  0.03010  0   SER A O     
5    C CB    . SER A 1   ? 0.46897 0.66101 0.58429 -0.12311 0.04982  0.03393  0   SER A CB    
6    O OG    . SER A 1   ? 0.44090 0.64309 0.55075 -0.11966 0.06137  0.03265  0   SER A OG    
7    N N     . MET A 2   ? 0.25410 0.39897 0.34734 -0.10990 0.03342  0.02997  1   MET A N     
8    C CA    . MET A 2   ? 0.17116 0.30433 0.25750 -0.09950 0.03169  0.02617  1   MET A CA    
9    C C     . MET A 2   ? 0.17557 0.27931 0.24933 -0.10078 0.02101  0.02820  1   MET A C     
10   O O     . MET A 2   ? 0.17532 0.27380 0.25074 -0.11095 0.01496  0.03137  1   MET A O     
11   C CB    . MET A 2   ? 0.25949 0.40684 0.36243 -0.08625 0.03084  0.01975  1   MET A CB    
12   C CG    . MET A 2   ? 0.36164 0.50508 0.45996 -0.07250 0.03592  0.01416  1   MET A CG    
13   S SD    . MET A 2   ? 0.37721 0.53163 0.49391 -0.05829 0.03249  0.00930  1   MET A SD    
14   C CE    . MET A 2   ? 0.24072 0.43196 0.38177 -0.05969 0.03925  0.00880  1   MET A CE    
15   N N     . THR A 3   ? 0.17178 0.25708 0.23375 -0.09063 0.01896  0.02570  2   THR A N     
16   C CA    . THR A 3   ? 0.15452 0.21552 0.20783 -0.08759 0.00992  0.02542  2   THR A CA    
17   C C     . THR A 3   ? 0.16141 0.22039 0.21646 -0.07341 0.00906  0.01960  2   THR A C     
18   O O     . THR A 3   ? 0.17017 0.24268 0.23146 -0.06661 0.01503  0.01627  2   THR A O     
19   C CB    . THR A 3   ? 0.23423 0.27260 0.26993 -0.09114 0.00812  0.03036  2   THR A CB    
20   O OG1   . THR A 3   ? 0.23567 0.27819 0.26458 -0.08702 0.01428  0.03026  2   THR A OG1   
21   C CG2   . THR A 3   ? 0.26357 0.29628 0.29538 -0.10628 0.00680  0.03761  2   THR A CG2   
22   N N     . GLU A 4   ? 0.17032 0.21135 0.21901 -0.06902 0.00235  0.01826  3   GLU A N     
23   C CA    . GLU A 4   ? 0.15582 0.19348 0.20496 -0.05714 0.00138  0.01389  3   GLU A CA    
24   C C     . GLU A 4   ? 0.19070 0.20601 0.22748 -0.05406 -0.00304 0.01388  3   GLU A C     
25   O O     . GLU A 4   ? 0.20730 0.20975 0.23858 -0.05924 -0.00794 0.01538  3   GLU A O     
26   C CB    . GLU A 4   ? 0.15025 0.19850 0.21030 -0.05474 -0.00249 0.01177  3   GLU A CB    
27   C CG    . GLU A 4   ? 0.14802 0.19135 0.20706 -0.04337 -0.00391 0.00878  3   GLU A CG    
28   C CD    . GLU A 4   ? 0.19839 0.25708 0.26957 -0.03970 -0.00667 0.00813  3   GLU A CD    
29   O OE1   . GLU A 4   ? 0.18565 0.25995 0.26722 -0.04585 -0.00848 0.00932  3   GLU A OE1   
30   O OE2   . GLU A 4   ? 0.24225 0.29812 0.31305 -0.03075 -0.00748 0.00709  3   GLU A OE2   
31   N N     . TYR A 5   ? 0.16079 0.17170 0.19422 -0.04558 -0.00122 0.01171  4   TYR A N     
32   C CA    . TYR A 5   ? 0.17590 0.17005 0.20020 -0.04170 -0.00414 0.01170  4   TYR A CA    
33   C C     . TYR A 5   ? 0.14793 0.14124 0.17376 -0.03297 -0.00401 0.00811  4   TYR A C     
34   O O     . TYR A 5   ? 0.17619 0.17814 0.20695 -0.02893 -0.00029 0.00637  4   TYR A O     
35   C CB    . TYR A 5   ? 0.18720 0.17738 0.20463 -0.04227 -0.00226 0.01430  4   TYR A CB    
36   C CG    . TYR A 5   ? 0.21075 0.20100 0.22443 -0.05151 -0.00196 0.01936  4   TYR A CG    
37   C CD1   . TYR A 5   ? 0.23467 0.21047 0.24310 -0.05663 -0.00675 0.02316  4   TYR A CD1   
38   C CD2   . TYR A 5   ? 0.19322 0.19739 0.20832 -0.05572 0.00364  0.02023  4   TYR A CD2   
39   C CE1   . TYR A 5   ? 0.24935 0.22368 0.25367 -0.06676 -0.00636 0.02920  4   TYR A CE1   
40   C CE2   . TYR A 5   ? 0.21752 0.22320 0.22837 -0.06528 0.00493  0.02567  4   TYR A CE2   
41   C CZ    . TYR A 5   ? 0.22581 0.21662 0.23150 -0.07142 -0.00023 0.03082  4   TYR A CZ    
42   O OH    . TYR A 5   ? 0.25374 0.24521 0.25467 -0.08242 0.00138  0.03749  4   TYR A OH    
43   N N     . LYS A 6   ? 0.17360 0.15540 0.19444 -0.03012 -0.00747 0.00698  5   LYS A N     
44   C CA    . LYS A 6   ? 0.16919 0.14911 0.18937 -0.02285 -0.00672 0.00453  5   LYS A CA    
45   C C     . LYS A 6   ? 0.17078 0.14491 0.18778 -0.01948 -0.00547 0.00484  5   LYS A C     
46   O O     . LYS A 6   ? 0.18619 0.15043 0.19875 -0.01862 -0.00787 0.00525  5   LYS A O     
47   C CB    . LYS A 6   ? 0.20326 0.17626 0.21897 -0.02207 -0.01048 0.00243  5   LYS A CB    
48   C CG    . LYS A 6   ? 0.28417 0.26546 0.30359 -0.02557 -0.01344 0.00217  5   LYS A CG    
49   C CD    . LYS A 6   ? 0.35899 0.33209 0.37062 -0.02630 -0.01819 -0.00083 5   LYS A CD    
50   C CE    . LYS A 6   ? 0.38062 0.34012 0.38643 -0.03196 -0.02121 -0.00204 5   LYS A CE    
51   N NZ    . LYS A 6   ? 0.43986 0.38803 0.43559 -0.03199 -0.02514 -0.00703 5   LYS A NZ    
52   N N     . LEU A 7   ? 0.14983 0.13001 0.16974 -0.01730 -0.00208 0.00434  6   LEU A N     
53   C CA    . LEU A 7   ? 0.15925 0.13793 0.17801 -0.01528 -0.00157 0.00457  6   LEU A CA    
54   C C     . LEU A 7   ? 0.17579 0.15499 0.19673 -0.01070 0.00041  0.00264  6   LEU A C     
55   O O     . LEU A 7   ? 0.19875 0.18030 0.22162 -0.00962 0.00237  0.00177  6   LEU A O     
56   C CB    . LEU A 7   ? 0.15569 0.14089 0.17482 -0.01818 0.00075  0.00451  6   LEU A CB    
57   C CG    . LEU A 7   ? 0.16695 0.15499 0.18339 -0.02380 0.00090  0.00667  6   LEU A CG    
58   C CD1   . LEU A 7   ? 0.19701 0.19112 0.21086 -0.02603 0.00377  0.00539  6   LEU A CD1   
59   C CD2   . LEU A 7   ? 0.20876 0.18838 0.22000 -0.02617 -0.00346 0.01099  6   LEU A CD2   
60   N N     . VAL A 8   ? 0.15792 0.13533 0.17898 -0.00780 -0.00012 0.00264  7   VAL A N     
61   C CA    . VAL A 8   ? 0.15884 0.13850 0.18233 -0.00460 0.00267  0.00139  7   VAL A CA    
62   C C     . VAL A 8   ? 0.15570 0.14127 0.18380 -0.00500 0.00297  0.00164  7   VAL A C     
63   O O     . VAL A 8   ? 0.16483 0.15099 0.19360 -0.00410 -0.00014 0.00299  7   VAL A O     
64   C CB    . VAL A 8   ? 0.14935 0.12424 0.16992 -0.00043 0.00244  0.00023  7   VAL A CB    
65   C CG1   . VAL A 8   ? 0.17431 0.15342 0.19648 0.00205  0.00667  -0.00056 7   VAL A CG1   
66   C CG2   . VAL A 8   ? 0.18200 0.15105 0.19676 -0.00157 0.00053  -0.00062 7   VAL A CG2   
67   N N     . VAL A 9   ? 0.14439 0.13385 0.17568 -0.00659 0.00604  0.00075  8   VAL A N     
68   C CA    . VAL A 9   ? 0.14573 0.14204 0.18194 -0.00892 0.00578  0.00034  8   VAL A CA    
69   C C     . VAL A 9   ? 0.14167 0.14316 0.18336 -0.00676 0.00851  0.00058  8   VAL A C     
70   O O     . VAL A 9   ? 0.15665 0.15583 0.19724 -0.00698 0.01250  0.00076  8   VAL A O     
71   C CB    . VAL A 9   ? 0.15451 0.14996 0.19021 -0.01368 0.00761  -0.00170 8   VAL A CB    
72   C CG1   . VAL A 9   ? 0.17612 0.17865 0.21567 -0.01794 0.00603  -0.00302 8   VAL A CG1   
73   C CG2   . VAL A 9   ? 0.17255 0.16472 0.20322 -0.01485 0.00697  -0.00259 8   VAL A CG2   
74   N N     . VAL A 10  ? 0.12815 0.13755 0.17592 -0.00445 0.00652  0.00115  9   VAL A N     
75   C CA    . VAL A 10  ? 0.13995 0.15822 0.19525 -0.00179 0.01005  0.00109  9   VAL A CA    
76   C C     . VAL A 10  ? 0.16504 0.19759 0.23123 -0.00446 0.00800  0.00152  9   VAL A C     
77   O O     . VAL A 10  ? 0.15813 0.19267 0.22425 -0.00709 0.00262  0.00196  9   VAL A O     
78   C CB    . VAL A 10  ? 0.15287 0.16899 0.20741 0.00641  0.01055  0.00050  9   VAL A CB    
79   C CG1   . VAL A 10  ? 0.18453 0.18741 0.22773 0.00743  0.01144  -0.00053 9   VAL A CG1   
80   C CG2   . VAL A 10  ? 0.18348 0.20022 0.24122 0.01062  0.00437  0.00187  9   VAL A CG2   
81   N N     . GLY A 11  ? 0.13920 0.18292 0.21428 -0.00483 0.01248  0.00152  10  GLY A N     
82   C CA    . GLY A 11  ? 0.14802 0.20897 0.23619 -0.00844 0.01038  0.00194  10  GLY A CA    
83   C C     . GLY A 11  ? 0.13241 0.20172 0.22730 -0.01456 0.01684  0.00209  10  GLY A C     
84   O O     . GLY A 11  ? 0.15725 0.21617 0.24419 -0.01629 0.02222  0.00251  10  GLY A O     
85   N N     . ALA A 12  ? 0.12264 0.21081 0.23192 -0.01850 0.01545  0.00241  11  ALA A N     
86   C CA    . ALA A 12  ? 0.12147 0.22065 0.23960 -0.02583 0.02209  0.00328  11  ALA A CA    
87   C C     . ALA A 12  ? 0.14426 0.22903 0.25403 -0.03675 0.02384  0.00316  11  ALA A C     
88   O O     . ALA A 12  ? 0.16427 0.23475 0.26457 -0.03935 0.01948  0.00127  11  ALA A O     
89   C CB    . ALA A 12  ? 0.12509 0.25024 0.26268 -0.02865 0.01916  0.00359  11  ALA A CB    
90   N N     . CYS A 13  ? 0.15816 0.24762 0.27230 -0.04299 0.03092  0.00534  12  CYS A N     
91   C CA    . CYS A 13  ? 0.19025 0.26391 0.29726 -0.05352 0.03308  0.00619  12  CYS A CA    
92   C C     . CYS A 13  ? 0.15700 0.22981 0.26716 -0.06315 0.02649  0.00257  12  CYS A C     
93   O O     . CYS A 13  ? 0.19791 0.29097 0.32146 -0.06685 0.02255  0.00139  12  CYS A O     
94   C CB    . CYS A 13  ? 0.21264 0.29430 0.32570 -0.06082 0.04151  0.01033  12  CYS A CB    
95   S SG    . CYS A 13  ? 0.28146 0.39685 0.41895 -0.06863 0.04215  0.01035  12  CYS A SG    
96   N N     . GLY A 14  ? 0.18327 0.23376 0.28111 -0.06615 0.02505  0.00040  13  GLY A N     
97   C CA    . GLY A 14  ? 0.18767 0.23336 0.28525 -0.07641 0.02011  -0.00451 13  GLY A CA    
98   C C     . GLY A 14  ? 0.16189 0.21464 0.25830 -0.07437 0.01167  -0.00904 13  GLY A C     
99   O O     . GLY A 14  ? 0.21290 0.26465 0.30864 -0.08380 0.00725  -0.01382 13  GLY A O     
100  N N     . VAL A 15  ? 0.16452 0.22196 0.25864 -0.06310 0.00936  -0.00762 14  VAL A N     
101  C CA    . VAL A 15  ? 0.14102 0.20603 0.23323 -0.06143 0.00097  -0.00999 14  VAL A CA    
102  C C     . VAL A 15  ? 0.16156 0.20765 0.23763 -0.06197 -0.00046 -0.01447 14  VAL A C     
103  O O     . VAL A 15  ? 0.17228 0.22302 0.24381 -0.06400 -0.00692 -0.01712 14  VAL A O     
104  C CB    . VAL A 15  ? 0.15654 0.23254 0.25297 -0.04976 -0.00122 -0.00599 14  VAL A CB    
105  C CG1   . VAL A 15  ? 0.16733 0.26517 0.28146 -0.04813 0.00036  -0.00291 14  VAL A CG1   
106  C CG2   . VAL A 15  ? 0.15495 0.21540 0.24137 -0.04053 0.00316  -0.00434 14  VAL A CG2   
107  N N     . GLY A 16  ? 0.17391 0.20118 0.24202 -0.05968 0.00541  -0.01488 15  GLY A N     
108  C CA    . GLY A 16  ? 0.16926 0.18106 0.22464 -0.05886 0.00540  -0.01945 15  GLY A CA    
109  C C     . GLY A 16  ? 0.17250 0.17788 0.22164 -0.04874 0.00733  -0.01693 15  GLY A C     
110  O O     . GLY A 16  ? 0.18108 0.17965 0.22131 -0.04743 0.00689  -0.02035 15  GLY A O     
111  N N     . LYS A 17  ? 0.16537 0.17302 0.21858 -0.04246 0.00985  -0.01170 16  LYS A N     
112  C CA    . LYS A 17  ? 0.17713 0.17879 0.22465 -0.03415 0.01095  -0.00957 16  LYS A CA    
113  C C     . LYS A 17  ? 0.18159 0.16857 0.22268 -0.03335 0.01421  -0.01197 16  LYS A C     
114  O O     . LYS A 17  ? 0.18120 0.16579 0.21705 -0.03030 0.01364  -0.01352 16  LYS A O     
115  C CB    . LYS A 17  ? 0.16969 0.17451 0.22107 -0.02893 0.01347  -0.00493 16  LYS A CB    
116  C CG    . LYS A 17  ? 0.16380 0.18333 0.22307 -0.02698 0.01130  -0.00308 16  LYS A CG    
117  C CD    . LYS A 17  ? 0.16768 0.18905 0.22874 -0.02136 0.01533  -0.00023 16  LYS A CD    
118  C CE    . LYS A 17  ? 0.16268 0.18216 0.22502 -0.02526 0.02111  0.00145  16  LYS A CE    
119  N NZ    . LYS A 17  ? 0.16188 0.19372 0.23483 -0.03214 0.02221  0.00151  16  LYS A NZ    
120  N N     . SER A 18  ? 0.17439 0.15242 0.21679 -0.03591 0.01774  -0.01165 17  SER A N     
121  C CA    . SER A 18  ? 0.16408 0.12729 0.20201 -0.03335 0.02058  -0.01340 17  SER A CA    
122  C C     . SER A 18  ? 0.20132 0.15922 0.23481 -0.03665 0.02027  -0.02102 17  SER A C     
123  O O     . SER A 18  ? 0.20180 0.15467 0.23165 -0.03178 0.02193  -0.02373 17  SER A O     
124  C CB    . SER A 18  ? 0.19881 0.15064 0.23803 -0.03521 0.02400  -0.01007 17  SER A CB    
125  O OG    . SER A 18  ? 0.20060 0.15742 0.24099 -0.03174 0.02504  -0.00330 17  SER A OG    
126  N N     . ALA A 19  ? 0.18956 0.15022 0.22328 -0.04498 0.01821  -0.02501 18  ALA A N     
127  C CA    . ALA A 19  ? 0.19775 0.15218 0.22448 -0.04891 0.01800  -0.03360 18  ALA A CA    
128  C C     . ALA A 19  ? 0.21341 0.17671 0.23409 -0.04541 0.01638  -0.03532 18  ALA A C     
129  O O     . ALA A 19  ? 0.23067 0.18766 0.24456 -0.04376 0.01921  -0.04135 18  ALA A O     
130  C CB    . ALA A 19  ? 0.22867 0.18634 0.25634 -0.06002 0.01464  -0.03754 18  ALA A CB    
131  N N     . LEU A 20  ? 0.18239 0.15969 0.20533 -0.04396 0.01245  -0.02988 19  LEU A N     
132  C CA    . LEU A 20  ? 0.20132 0.18544 0.21790 -0.04138 0.01089  -0.02949 19  LEU A CA    
133  C C     . LEU A 20  ? 0.22124 0.20062 0.23737 -0.03433 0.01538  -0.02844 19  LEU A C     
134  O O     . LEU A 20  ? 0.21476 0.19455 0.22457 -0.03370 0.01775  -0.03218 19  LEU A O     
135  C CB    . LEU A 20  ? 0.20504 0.20141 0.22500 -0.04030 0.00555  -0.02287 19  LEU A CB    
136  C CG    . LEU A 20  ? 0.20396 0.21063 0.22429 -0.04640 -0.00067 -0.02337 19  LEU A CG    
137  C CD1   . LEU A 20  ? 0.21119 0.22847 0.23858 -0.04228 -0.00513 -0.01610 19  LEU A CD1   
138  C CD2   . LEU A 20  ? 0.22811 0.23658 0.23610 -0.05069 -0.00311 -0.02748 19  LEU A CD2   
139  N N     . THR A 21  ? 0.18108 0.15765 0.20391 -0.02936 0.01666  -0.02343 20  THR A N     
140  C CA    . THR A 21  ? 0.21159 0.18641 0.23578 -0.02298 0.01938  -0.02169 20  THR A CA    
141  C C     . THR A 21  ? 0.22231 0.18855 0.24573 -0.02063 0.02420  -0.02744 20  THR A C     
142  O O     . THR A 21  ? 0.21597 0.18602 0.23858 -0.01749 0.02683  -0.02953 20  THR A O     
143  C CB    . THR A 21  ? 0.20085 0.17408 0.23029 -0.01913 0.01882  -0.01566 20  THR A CB    
144  O OG1   . THR A 21  ? 0.19020 0.17085 0.22041 -0.02001 0.01525  -0.01171 20  THR A OG1   
145  C CG2   . THR A 21  ? 0.22222 0.19596 0.25369 -0.01309 0.01989  -0.01336 20  THR A CG2   
146  N N     . ILE A 22  ? 0.21045 0.16492 0.23449 -0.02231 0.02579  -0.03034 21  ILE A N     
147  C CA    . ILE A 22  ? 0.22686 0.16918 0.25053 -0.01866 0.03044  -0.03614 21  ILE A CA    
148  C C     . ILE A 22  ? 0.24503 0.18934 0.26121 -0.02116 0.03288  -0.04519 21  ILE A C     
149  O O     . ILE A 22  ? 0.24453 0.18668 0.26103 -0.01535 0.03780  -0.04993 21  ILE A O     
150  C CB    . ILE A 22  ? 0.23411 0.15983 0.25914 -0.02098 0.03117  -0.03623 21  ILE A CB    
151  C CG1   . ILE A 22  ? 0.26304 0.18737 0.29360 -0.01683 0.03006  -0.02648 21  ILE A CG1   
152  C CG2   . ILE A 22  ? 0.28386 0.19300 0.30701 -0.01761 0.03578  -0.04403 21  ILE A CG2   
153  C CD1   . ILE A 22  ? 0.33120 0.24365 0.36216 -0.02234 0.03013  -0.02353 21  ILE A CD1   
154  N N     . GLN A 23  ? 0.21588 0.16586 0.22512 -0.02937 0.02956  -0.04770 22  GLN A N     
155  C CA    . GLN A 23  ? 0.26154 0.21555 0.26036 -0.03251 0.03134  -0.05550 22  GLN A CA    
156  C C     . GLN A 23  ? 0.26185 0.22826 0.26021 -0.02807 0.03382  -0.05284 22  GLN A C     
157  O O     . GLN A 23  ? 0.28559 0.25284 0.27957 -0.02568 0.03973  -0.05953 22  GLN A O     
158  C CB    . GLN A 23  ? 0.27410 0.23446 0.26571 -0.04207 0.02528  -0.05635 22  GLN A CB    
159  C CG    . GLN A 23  ? 0.36573 0.31440 0.35253 -0.04890 0.02497  -0.06506 22  GLN A CG    
160  C CD    . GLN A 23  ? 0.32966 0.27110 0.30353 -0.05014 0.02989  -0.07768 22  GLN A CD    
161  O OE1   . GLN A 23  ? 0.35859 0.30192 0.32944 -0.04372 0.03615  -0.08078 22  GLN A OE1   
162  N NE2   . GLN A 23  ? 0.39067 0.32482 0.35724 -0.05891 0.02729  -0.08548 22  GLN A NE2   
163  N N     . LEU A 24  ? 0.23821 0.21435 0.24092 -0.02741 0.02988  -0.04359 23  LEU A N     
164  C CA    . LEU A 24  ? 0.24876 0.23571 0.25171 -0.02500 0.03199  -0.04044 23  LEU A CA    
165  C C     . LEU A 24  ? 0.22830 0.21470 0.23978 -0.01713 0.03797  -0.04244 23  LEU A C     
166  O O     . LEU A 24  ? 0.28042 0.27479 0.29056 -0.01573 0.04341  -0.04594 23  LEU A O     
167  C CB    . LEU A 24  ? 0.22924 0.22203 0.23628 -0.02528 0.02644  -0.03071 23  LEU A CB    
168  C CG    . LEU A 24  ? 0.26324 0.26592 0.26991 -0.02537 0.02762  -0.02666 23  LEU A CG    
169  C CD1   . LEU A 24  ? 0.29949 0.30774 0.29333 -0.03202 0.02685  -0.02697 23  LEU A CD1   
170  C CD2   . LEU A 24  ? 0.27077 0.27436 0.28385 -0.02372 0.02310  -0.01874 23  LEU A CD2   
171  N N     . ILE A 25  ? 0.24850 0.22735 0.26916 -0.01181 0.03698  -0.03945 24  ILE A N     
172  C CA    . ILE A 25  ? 0.27612 0.25668 0.30721 -0.00319 0.04021  -0.03845 24  ILE A CA    
173  C C     . ILE A 25  ? 0.29297 0.26463 0.32507 0.00233  0.04660  -0.04721 24  ILE A C     
174  O O     . ILE A 25  ? 0.29885 0.27848 0.33753 0.00882  0.05175  -0.04990 24  ILE A O     
175  C CB    . ILE A 25  ? 0.29284 0.26826 0.33085 0.00025  0.03570  -0.03082 24  ILE A CB    
176  C CG1   . ILE A 25  ? 0.26125 0.24423 0.29780 -0.00413 0.03017  -0.02378 24  ILE A CG1   
177  C CG2   . ILE A 25  ? 0.33147 0.30878 0.38028 0.00975  0.03765  -0.02934 24  ILE A CG2   
178  C CD1   . ILE A 25  ? 0.28646 0.28313 0.32640 -0.00401 0.02991  -0.02096 24  ILE A CD1   
179  N N     . GLN A 26  ? 0.27746 0.23225 0.30436 0.00013  0.04646  -0.05182 25  GLN A N     
180  C CA    . GLN A 26  ? 0.33004 0.26964 0.35799 0.00607  0.05173  -0.05983 25  GLN A CA    
181  C C     . GLN A 26  ? 0.32213 0.25450 0.33745 0.00041  0.05539  -0.07185 25  GLN A C     
182  O O     . GLN A 26  ? 0.35331 0.27119 0.36782 0.00544  0.06066  -0.08077 25  GLN A O     
183  C CB    . GLN A 26  ? 0.31106 0.23222 0.34292 0.00786  0.04865  -0.05516 25  GLN A CB    
184  C CG    . GLN A 26  ? 0.32944 0.25725 0.37088 0.01321  0.04466  -0.04355 25  GLN A CG    
185  C CD    . GLN A 26  ? 0.39476 0.30515 0.43805 0.01481  0.04206  -0.03740 25  GLN A CD    
186  O OE1   . GLN A 26  ? 0.46063 0.35305 0.49892 0.01044  0.04295  -0.04096 25  GLN A OE1   
187  N NE2   . GLN A 26  ? 0.40302 0.31855 0.45262 0.02021  0.03866  -0.02787 25  GLN A NE2   
188  N N     A ASN A 27  ? 0.31328 0.25441 0.31810 -0.00957 0.05227  -0.07244 26  ASN A N     
189  N N     B ASN A 27  ? 0.31311 0.25412 0.31782 -0.00957 0.05234  -0.07260 26  ASN A N     
190  C CA    A ASN A 27  ? 0.32771 0.26548 0.31782 -0.01637 0.05442  -0.08345 26  ASN A CA    
191  C CA    B ASN A 27  ? 0.32798 0.26554 0.31807 -0.01602 0.05483  -0.08390 26  ASN A CA    
192  C C     A ASN A 27  ? 0.33353 0.24874 0.31936 -0.01957 0.05414  -0.09139 26  ASN A C     
193  C C     B ASN A 27  ? 0.33373 0.24886 0.31931 -0.01970 0.05415  -0.09157 26  ASN A C     
194  O O     A ASN A 27  ? 0.37276 0.27751 0.34978 -0.01939 0.05937  -0.10391 26  ASN A O     
195  O O     B ASN A 27  ? 0.37293 0.27756 0.34926 -0.02006 0.05910  -0.10413 26  ASN A O     
196  C CB    A ASN A 27  ? 0.34053 0.28731 0.32631 -0.01179 0.06299  -0.09131 26  ASN A CB    
197  C CB    B ASN A 27  ? 0.34020 0.28543 0.32713 -0.01034 0.06390  -0.09211 26  ASN A CB    
198  C CG    A ASN A 27  ? 0.34588 0.31401 0.33861 -0.00921 0.06377  -0.08259 26  ASN A CG    
199  C CG    B ASN A 27  ? 0.36861 0.31821 0.33662 -0.01881 0.06577  -0.10124 26  ASN A CG    
200  O OD1   A ASN A 27  ? 0.47933 0.45926 0.46527 -0.01663 0.05971  -0.07698 26  ASN A OD1   
201  O OD1   B ASN A 27  ? 0.41588 0.37155 0.37469 -0.02859 0.05891  -0.09737 26  ASN A OD1   
202  N ND2   A ASN A 27  ? 0.37540 0.34830 0.38232 0.00114  0.06838  -0.08095 26  ASN A ND2   
203  N ND2   B ASN A 27  ? 0.37263 0.31968 0.33444 -0.01442 0.07510  -0.11350 26  ASN A ND2   
204  N N     . HIS A 28  ? 0.32355 0.23072 0.31500 -0.02318 0.04845  -0.08453 27  HIS A N     
205  C CA    . HIS A 28  ? 0.35109 0.23835 0.33790 -0.03027 0.04695  -0.09078 27  HIS A CA    
206  C C     . HIS A 28  ? 0.31824 0.20989 0.30918 -0.03906 0.03946  -0.08183 27  HIS A C     
207  O O     . HIS A 28  ? 0.30186 0.20793 0.29993 -0.03703 0.03636  -0.07109 27  HIS A O     
208  C CB    . HIS A 28  ? 0.40066 0.26354 0.39235 -0.02226 0.05196  -0.09461 27  HIS A CB    
209  C CG    . HIS A 28  ? 0.41943 0.27972 0.42422 -0.01494 0.05053  -0.08196 27  HIS A CG    
210  N ND1   . HIS A 28  ? 0.45621 0.30630 0.46423 -0.02082 0.04641  -0.07454 27  HIS A ND1   
211  C CD2   . HIS A 28  ? 0.45456 0.32292 0.46930 -0.00308 0.05235  -0.07511 27  HIS A CD2   
212  C CE1   . HIS A 28  ? 0.50908 0.35984 0.52633 -0.01257 0.04591  -0.06368 27  HIS A CE1   
213  N NE2   . HIS A 28  ? 0.50602 0.36785 0.52776 -0.00175 0.04879  -0.06393 27  HIS A NE2   
214  N N     . PHE A 29  ? 0.34863 0.22789 0.33519 -0.04919 0.03694  -0.08723 28  PHE A N     
215  C CA    . PHE A 29  ? 0.33419 0.21736 0.32577 -0.05921 0.03082  -0.08086 28  PHE A CA    
216  C C     . PHE A 29  ? 0.38954 0.24804 0.38292 -0.06369 0.03219  -0.08314 28  PHE A C     
217  O O     . PHE A 29  ? 0.52854 0.37229 0.51443 -0.06270 0.03364  -0.09132 28  PHE A O     
218  C CB    . PHE A 29  ? 0.35715 0.25327 0.34015 -0.07090 0.02491  -0.08655 28  PHE A CB    
219  C CG    . PHE A 29  ? 0.33475 0.23901 0.32507 -0.08165 0.01844  -0.08122 28  PHE A CG    
220  C CD1   . PHE A 29  ? 0.32722 0.25022 0.32806 -0.07929 0.01528  -0.06937 28  PHE A CD1   
221  C CD2   . PHE A 29  ? 0.35859 0.25412 0.34624 -0.09259 0.01531  -0.08702 28  PHE A CD2   
222  C CE1   . PHE A 29  ? 0.35669 0.28998 0.36644 -0.08818 0.01049  -0.06481 28  PHE A CE1   
223  C CE2   . PHE A 29  ? 0.34778 0.25510 0.34469 -0.10177 0.00953  -0.08113 28  PHE A CE2   
224  C CZ    . PHE A 29  ? 0.34915 0.27510 0.35780 -0.10102 0.00803  -0.07138 28  PHE A CZ    
225  N N     . VAL A 30  ? 0.52645 0.38443 0.52924 -0.06641 0.03052  -0.07278 29  VAL A N     
226  C CA    . VAL A 30  ? 0.51158 0.35435 0.51564 -0.07229 0.02886  -0.07027 29  VAL A CA    
227  C C     . VAL A 30  ? 0.39720 0.25594 0.40842 -0.08386 0.02424  -0.06380 29  VAL A C     
228  O O     . VAL A 30  ? 0.53647 0.41311 0.55470 -0.08312 0.02395  -0.05717 29  VAL A O     
229  C CB    . VAL A 30  ? 0.59869 0.42269 0.60657 -0.06314 0.03243  -0.06269 29  VAL A CB    
230  C CG1   . VAL A 30  ? 0.59038 0.39767 0.59291 -0.05174 0.03618  -0.07007 29  VAL A CG1   
231  C CG2   . VAL A 30  ? 0.60548 0.44057 0.62141 -0.05724 0.03405  -0.05153 29  VAL A CG2   
232  N N     . ASP A 31  ? 0.53452 0.38776 0.54490 -0.09432 0.02063  -0.06627 30  ASP A N     
233  C CA    . ASP A 31  ? 0.48957 0.35927 0.50875 -0.10575 0.01630  -0.06090 30  ASP A CA    
234  C C     . ASP A 31  ? 0.43560 0.30544 0.46407 -0.10506 0.01937  -0.04841 30  ASP A C     
235  O O     . ASP A 31  ? 0.42521 0.31442 0.46333 -0.11210 0.01755  -0.04259 30  ASP A O     
236  C CB    . ASP A 31  ? 0.52147 0.38137 0.53803 -0.11682 0.01219  -0.06685 30  ASP A CB    
237  C CG    . ASP A 31  ? 0.51952 0.38695 0.52737 -0.12132 0.00730  -0.07831 30  ASP A CG    
238  O OD1   . ASP A 31  ? 0.55723 0.44764 0.56594 -0.12146 0.00422  -0.07834 30  ASP A OD1   
239  O OD2   . ASP A 31  ? 0.72353 0.57352 0.72299 -0.12496 0.00609  -0.08712 30  ASP A OD2   
240  N N     . GLU A 32  ? 0.57901 0.42840 0.60470 -0.09682 0.02379  -0.04395 31  GLU A N     
241  C CA    . GLU A 32  ? 0.52650 0.37369 0.55785 -0.09788 0.02623  -0.03171 31  GLU A CA    
242  C C     . GLU A 32  ? 0.40174 0.26958 0.43905 -0.09307 0.02853  -0.02469 31  GLU A C     
243  O O     . GLU A 32  ? 0.46954 0.34116 0.50510 -0.08369 0.02977  -0.02686 31  GLU A O     
244  C CB    . GLU A 32  ? 0.57792 0.39732 0.60374 -0.09023 0.02883  -0.02771 31  GLU A CB    
245  C CG    . GLU A 32  ? 0.72926 0.53255 0.75552 -0.09988 0.02754  -0.02349 31  GLU A CG    
246  C CD    . GLU A 32  ? 0.66243 0.44359 0.68532 -0.09325 0.02960  -0.01361 31  GLU A CD    
247  O OE1   . GLU A 32  ? 0.72082 0.49873 0.74107 -0.08017 0.03167  -0.01017 31  GLU A OE1   
248  O OE2   . GLU A 32  ? 0.76166 0.52920 0.78515 -0.10152 0.02856  -0.00872 31  GLU A OE2   
249  N N     . TYR A 33  ? 0.37000 0.25188 0.41501 -0.10003 0.02929  -0.01669 32  TYR A N     
250  C CA    . TYR A 33  ? 0.31786 0.21973 0.36888 -0.09574 0.03223  -0.01001 32  TYR A CA    
251  C C     . TYR A 33  ? 0.31277 0.20150 0.35940 -0.08881 0.03682  -0.00026 32  TYR A C     
252  O O     . TYR A 33  ? 0.35810 0.23649 0.40304 -0.09385 0.03816  0.00637  32  TYR A O     
253  C CB    . TYR A 33  ? 0.32065 0.24836 0.38310 -0.10525 0.03149  -0.00713 32  TYR A CB    
254  C CG    . TYR A 33  ? 0.31451 0.26639 0.38417 -0.09995 0.03410  -0.00153 32  TYR A CG    
255  C CD1   . TYR A 33  ? 0.30656 0.26003 0.37064 -0.08550 0.03399  0.00022  32  TYR A CD1   
256  C CD2   . TYR A 33  ? 0.38490 0.36003 0.46688 -0.10769 0.03566  0.00190  32  TYR A CD2   
257  C CE1   . TYR A 33  ? 0.30840 0.28208 0.37689 -0.07908 0.03529  0.00454  32  TYR A CE1   
258  C CE2   . TYR A 33  ? 0.37935 0.37680 0.46710 -0.09991 0.03771  0.00623  32  TYR A CE2   
259  C CZ    . TYR A 33  ? 0.30060 0.29561 0.38056 -0.08551 0.03744  0.00718  32  TYR A CZ    
260  O OH    . TYR A 33  ? 0.32332 0.33737 0.40775 -0.07808 0.03954  0.01016  32  TYR A OH    
261  N N     . ASP A 34  ? 0.29024 0.18133 0.33354 -0.07592 0.03703  0.00132  33  ASP A N     
262  C CA    . ASP A 34  ? 0.28648 0.16940 0.32473 -0.06821 0.03968  0.01114  33  ASP A CA    
263  C C     . ASP A 34  ? 0.24657 0.15358 0.28677 -0.06225 0.03958  0.01458  33  ASP A C     
264  O O     . ASP A 34  ? 0.23371 0.14859 0.27305 -0.05313 0.03670  0.01096  33  ASP A O     
265  C CB    . ASP A 34  ? 0.34619 0.21124 0.37868 -0.05670 0.03838  0.00944  33  ASP A CB    
266  C CG    . ASP A 34  ? 0.42512 0.28263 0.45232 -0.04839 0.03931  0.02007  33  ASP A CG    
267  O OD1   . ASP A 34  ? 0.44130 0.30158 0.46640 -0.05328 0.04186  0.02889  33  ASP A OD1   
268  O OD2   . ASP A 34  ? 0.51979 0.37002 0.54493 -0.03714 0.03745  0.01965  33  ASP A OD2   
269  N N     . PRO A 35  ? 0.25604 0.17466 0.29854 -0.06729 0.04316  0.02111  34  PRO A N     
270  C CA    . PRO A 35  ? 0.24465 0.18588 0.28925 -0.06156 0.04361  0.02225  34  PRO A CA    
271  C C     . PRO A 35  ? 0.23796 0.17545 0.27397 -0.04930 0.04203  0.02476  34  PRO A C     
272  O O     . PRO A 35  ? 0.27817 0.20012 0.30623 -0.04625 0.04265  0.03078  34  PRO A O     
273  C CB    . PRO A 35  ? 0.27535 0.22571 0.32238 -0.06950 0.04969  0.02920  34  PRO A CB    
274  C CG    . PRO A 35  ? 0.33934 0.27919 0.39060 -0.08247 0.05078  0.02913  34  PRO A CG    
275  C CD    . PRO A 35  ? 0.30072 0.21353 0.34491 -0.07962 0.04752  0.02672  34  PRO A CD    
276  N N     . THR A 36  ? 0.21730 0.16878 0.25518 -0.04269 0.03924  0.02042  35  THR A N     
277  C CA    . THR A 36  ? 0.22282 0.17254 0.25374 -0.03264 0.03682  0.02157  35  THR A CA    
278  C C     . THR A 36  ? 0.20932 0.16424 0.23325 -0.03026 0.03976  0.02757  35  THR A C     
279  O O     . THR A 36  ? 0.21900 0.18703 0.24573 -0.03339 0.04371  0.02802  35  THR A O     
280  C CB    . THR A 36  ? 0.19792 0.15838 0.23248 -0.02813 0.03286  0.01507  35  THR A CB    
281  O OG1   . THR A 36  ? 0.20804 0.16289 0.24595 -0.03070 0.03065  0.00968  35  THR A OG1   
282  C CG2   . THR A 36  ? 0.19888 0.15840 0.22739 -0.01957 0.02995  0.01575  35  THR A CG2   
283  N N     . ILE A 37  ? 0.21164 0.15694 0.22645 -0.02458 0.03784  0.03203  36  ILE A N     
284  C CA    . ILE A 37  ? 0.20751 0.15853 0.21267 -0.02035 0.03830  0.03540  36  ILE A CA    
285  C C     . ILE A 37  ? 0.20903 0.16636 0.21459 -0.01353 0.03323  0.02958  36  ILE A C     
286  O O     . ILE A 37  ? 0.20861 0.17676 0.21442 -0.01223 0.03413  0.02570  36  ILE A O     
287  C CB    . ILE A 37  ? 0.22217 0.16050 0.21587 -0.01891 0.03780  0.04461  36  ILE A CB    
288  C CG1   . ILE A 37  ? 0.24628 0.17690 0.23730 -0.02711 0.04356  0.05216  36  ILE A CG1   
289  C CG2   . ILE A 37  ? 0.22010 0.16494 0.20161 -0.01436 0.03654  0.04651  36  ILE A CG2   
290  C CD1   . ILE A 37  ? 0.26801 0.21159 0.25482 -0.03180 0.05027  0.05423  36  ILE A CD1   
291  N N     . GLU A 38  ? 0.20234 0.15313 0.20900 -0.00927 0.02829  0.02874  37  GLU A N     
292  C CA    . GLU A 38  ? 0.19780 0.15476 0.20646 -0.00486 0.02374  0.02354  37  GLU A CA    
293  C C     . GLU A 38  ? 0.18446 0.13521 0.19772 -0.00172 0.02054  0.02312  37  GLU A C     
294  O O     . GLU A 38  ? 0.21648 0.15849 0.22742 0.00067  0.01981  0.02836  37  GLU A O     
295  C CB    . GLU A 38  ? 0.20676 0.16713 0.20568 -0.00138 0.02115  0.02509  37  GLU A CB    
296  C CG    . GLU A 38  ? 0.20392 0.17004 0.20468 0.00102  0.01676  0.01952  37  GLU A CG    
297  C CD    . GLU A 38  ? 0.22196 0.18912 0.21293 0.00345  0.01263  0.02068  37  GLU A CD    
298  O OE1   . GLU A 38  ? 0.21804 0.18712 0.20009 0.00319  0.01429  0.01916  37  GLU A OE1   
299  O OE2   . GLU A 38  ? 0.24716 0.21359 0.23902 0.00578  0.00781  0.02329  37  GLU A OE2   
300  N N     . ASP A 39  ? 0.19094 0.14626 0.21065 -0.00136 0.01902  0.01725  38  ASP A N     
301  C CA    . ASP A 39  ? 0.19551 0.14825 0.22017 0.00233  0.01716  0.01578  38  ASP A CA    
302  C C     . ASP A 39  ? 0.18990 0.15255 0.21735 0.00328  0.01435  0.01171  38  ASP A C     
303  O O     . ASP A 39  ? 0.19649 0.16434 0.22318 0.00030  0.01425  0.00888  38  ASP A O     
304  C CB    . ASP A 39  ? 0.20479 0.14994 0.23399 -0.00005 0.02026  0.01228  38  ASP A CB    
305  C CG    . ASP A 39  ? 0.26569 0.19711 0.29270 -0.00109 0.02258  0.01692  38  ASP A CG    
306  O OD1   . ASP A 39  ? 0.27902 0.20251 0.30553 0.00452  0.02126  0.02138  38  ASP A OD1   
307  O OD2   . ASP A 39  ? 0.30739 0.23679 0.33353 -0.00771 0.02537  0.01696  38  ASP A OD2   
308  N N     . SER A 40  ? 0.19556 0.16098 0.22723 0.00747  0.01212  0.01190  39  SER A N     
309  C CA    . SER A 40  ? 0.21030 0.18585 0.24550 0.00718  0.00977  0.00903  39  SER A CA    
310  C C     . SER A 40  ? 0.21490 0.19299 0.25820 0.00984  0.01188  0.00606  39  SER A C     
311  O O     . SER A 40  ? 0.23052 0.20383 0.27770 0.01508  0.01277  0.00760  39  SER A O     
312  C CB    . SER A 40  ? 0.22257 0.20361 0.25609 0.00924  0.00470  0.01238  39  SER A CB    
313  O OG    . SER A 40  ? 0.29841 0.27728 0.32266 0.00692  0.00341  0.01339  39  SER A OG    
314  N N     . TYR A 41  ? 0.17620 0.16142 0.22154 0.00664  0.01302  0.00194  40  TYR A N     
315  C CA    . TYR A 41  ? 0.18503 0.17455 0.23652 0.00846  0.01662  -0.00210 40  TYR A CA    
316  C C     . TYR A 41  ? 0.17272 0.17588 0.22788 0.00594  0.01543  -0.00246 40  TYR A C     
317  O O     . TYR A 41  ? 0.16125 0.16649 0.21223 0.00129  0.01203  -0.00066 40  TYR A O     
318  C CB    . TYR A 41  ? 0.21670 0.20033 0.26394 0.00472  0.02059  -0.00724 40  TYR A CB    
319  C CG    . TYR A 41  ? 0.22719 0.19728 0.27147 0.00486  0.02171  -0.00701 40  TYR A CG    
320  C CD1   . TYR A 41  ? 0.25468 0.21523 0.30197 0.00950  0.02467  -0.00888 40  TYR A CD1   
321  C CD2   . TYR A 41  ? 0.22119 0.18789 0.26056 0.00042  0.02013  -0.00477 40  TYR A CD2   
322  C CE1   . TYR A 41  ? 0.31839 0.26421 0.36263 0.00812  0.02569  -0.00805 40  TYR A CE1   
323  C CE2   . TYR A 41  ? 0.25057 0.20649 0.28828 -0.00113 0.02169  -0.00399 40  TYR A CE2   
324  C CZ    . TYR A 41  ? 0.31004 0.25462 0.34960 0.00193  0.02425  -0.00533 40  TYR A CZ    
325  O OH    . TYR A 41  ? 0.33503 0.26651 0.37245 -0.00116 0.02575  -0.00391 40  TYR A OH    
326  N N     . ARG A 42  ? 0.18061 0.19267 0.24387 0.00885  0.01876  -0.00499 41  ARG A N     
327  C CA    . ARG A 42  ? 0.17750 0.20483 0.24593 0.00530  0.01876  -0.00493 41  ARG A CA    
328  C C     . ARG A 42  ? 0.17613 0.21023 0.24804 0.00610  0.02603  -0.01028 41  ARG A C     
329  O O     . ARG A 42  ? 0.19724 0.22974 0.27491 0.01348  0.02989  -0.01348 41  ARG A O     
330  C CB    . ARG A 42  ? 0.22163 0.25928 0.30019 0.00940  0.01439  -0.00113 41  ARG A CB    
331  C CG    . ARG A 42  ? 0.19820 0.25308 0.28424 0.00450  0.01276  0.00003  41  ARG A CG    
332  C CD    . ARG A 42  ? 0.24603 0.30825 0.33925 0.00798  0.00544  0.00439  41  ARG A CD    
333  N NE    . ARG A 42  ? 0.22133 0.30479 0.32760 0.00496  0.00373  0.00534  41  ARG A NE    
334  C CZ    . ARG A 42  ? 0.19928 0.28795 0.30360 -0.00495 -0.00031 0.00656  41  ARG A CZ    
335  N NH1   . ARG A 42  ? 0.25645 0.32948 0.34601 -0.01137 -0.00281 0.00661  41  ARG A NH1   
336  N NH2   . ARG A 42  ? 0.19245 0.30243 0.31082 -0.00846 -0.00186 0.00763  41  ARG A NH2   
337  N N     . LYS A 43  ? 0.15762 0.19821 0.22498 -0.00124 0.02825  -0.01131 42  LYS A N     
338  C CA    . LYS A 43  ? 0.17006 0.21810 0.23762 -0.00151 0.03603  -0.01674 42  LYS A CA    
339  C C     . LYS A 43  ? 0.17314 0.23517 0.24044 -0.00971 0.03743  -0.01439 42  LYS A C     
340  O O     . LYS A 43  ? 0.17280 0.23049 0.23296 -0.01685 0.03250  -0.00976 42  LYS A O     
341  C CB    . LYS A 43  ? 0.24221 0.27699 0.29628 -0.00415 0.03790  -0.02100 42  LYS A CB    
342  C CG    . LYS A 43  ? 0.26513 0.30506 0.31475 -0.00491 0.04608  -0.02822 42  LYS A CG    
343  C CD    . LYS A 43  ? 0.32549 0.35355 0.35998 -0.00978 0.04557  -0.03183 42  LYS A CD    
344  C CE    . LYS A 43  ? 0.35082 0.38195 0.37792 -0.01046 0.05350  -0.04051 42  LYS A CE    
345  N NZ    . LYS A 43  ? 0.37641 0.40619 0.41250 -0.00081 0.06018  -0.04795 42  LYS A NZ    
346  N N     . GLN A 44  ? 0.15917 0.23683 0.23364 -0.00874 0.04472  -0.01762 43  GLN A N     
347  C CA    . GLN A 44  ? 0.15704 0.24882 0.23022 -0.01786 0.04804  -0.01531 43  GLN A CA    
348  C C     . GLN A 44  ? 0.20504 0.29169 0.26194 -0.02247 0.05323  -0.01886 43  GLN A C     
349  O O     . GLN A 44  ? 0.24329 0.32702 0.29719 -0.01693 0.05907  -0.02649 43  GLN A O     
350  C CB    . GLN A 44  ? 0.15166 0.26687 0.24261 -0.01434 0.05423  -0.01702 43  GLN A CB    
351  C CG    . GLN A 44  ? 0.19645 0.32945 0.28791 -0.02490 0.05922  -0.01424 43  GLN A CG    
352  C CD    . GLN A 44  ? 0.20436 0.36461 0.31727 -0.02138 0.06514  -0.01559 43  GLN A CD    
353  O OE1   . GLN A 44  ? 0.31873 0.48725 0.44715 -0.01826 0.05924  -0.01253 43  GLN A OE1   
354  N NE2   . GLN A 44  ? 0.28317 0.45906 0.39718 -0.02177 0.07673  -0.02027 43  GLN A NE2   
355  N N     . VAL A 45  ? 0.17972 0.26431 0.22518 -0.03270 0.05071  -0.01334 44  VAL A N     
356  C CA    . VAL A 45  ? 0.21602 0.29627 0.24361 -0.03842 0.05355  -0.01453 44  VAL A CA    
357  C C     . VAL A 45  ? 0.21740 0.30833 0.23989 -0.04917 0.05614  -0.00822 44  VAL A C     
358  O O     . VAL A 45  ? 0.20607 0.30445 0.23834 -0.05346 0.05427  -0.00260 44  VAL A O     
359  C CB    . VAL A 45  ? 0.23746 0.29893 0.25275 -0.03960 0.04526  -0.01214 44  VAL A CB    
360  C CG1   . VAL A 45  ? 0.26412 0.31505 0.28467 -0.03081 0.04293  -0.01723 44  VAL A CG1   
361  C CG2   . VAL A 45  ? 0.21919 0.27460 0.23484 -0.04444 0.03719  -0.00309 44  VAL A CG2   
362  N N     . VAL A 46  ? 0.20267 0.29450 0.20878 -0.05460 0.06049  -0.00900 45  VAL A N     
363  C CA    . VAL A 46  ? 0.21838 0.31597 0.21450 -0.06620 0.06203  -0.00101 45  VAL A CA    
364  C C     . VAL A 46  ? 0.27286 0.35400 0.24907 -0.07014 0.05481  0.00357  45  VAL A C     
365  O O     . VAL A 46  ? 0.30316 0.37996 0.26803 -0.06741 0.05553  -0.00244 45  VAL A O     
366  C CB    . VAL A 46  ? 0.25889 0.37581 0.25160 -0.06956 0.07480  -0.00514 45  VAL A CB    
367  C CG1   . VAL A 46  ? 0.27311 0.39516 0.25399 -0.08327 0.07638  0.00513  45  VAL A CG1   
368  C CG2   . VAL A 46  ? 0.26323 0.39940 0.27887 -0.06336 0.08220  -0.01045 45  VAL A CG2   
369  N N     . ILE A 47  ? 0.22473 0.29613 0.19735 -0.07609 0.04717  0.01381  46  ILE A N     
370  C CA    . ILE A 47  ? 0.23708 0.29340 0.19336 -0.07858 0.03904  0.01991  46  ILE A CA    
371  C C     . ILE A 47  ? 0.27577 0.33191 0.22068 -0.08999 0.03916  0.03113  46  ILE A C     
372  O O     . ILE A 47  ? 0.25410 0.30890 0.20714 -0.09496 0.03796  0.03720  46  ILE A O     
373  C CB    . ILE A 47  ? 0.25391 0.29441 0.21717 -0.07258 0.02884  0.02184  46  ILE A CB    
374  C CG1   . ILE A 47  ? 0.21842 0.25890 0.19133 -0.06271 0.02934  0.01195  46  ILE A CG1   
375  C CG2   . ILE A 47  ? 0.31513 0.34237 0.26382 -0.07423 0.02026  0.02911  46  ILE A CG2   
376  C CD1   . ILE A 47  ? 0.24149 0.27051 0.22341 -0.05704 0.02188  0.01314  46  ILE A CD1   
377  N N     . ASP A 48  ? 0.26125 0.31832 0.18625 -0.09515 0.04043  0.03415  47  ASP A N     
378  C CA    . ASP A 48  ? 0.29823 0.35328 0.20910 -0.10671 0.04035  0.04662  47  ASP A CA    
379  C C     . ASP A 48  ? 0.29205 0.36289 0.21204 -0.11471 0.05034  0.04811  47  ASP A C     
380  O O     . ASP A 48  ? 0.30814 0.37240 0.22871 -0.12082 0.04723  0.05711  47  ASP A O     
381  C CB    . ASP A 48  ? 0.32894 0.36249 0.23749 -0.10743 0.02823  0.05777  47  ASP A CB    
382  C CG    . ASP A 48  ? 0.34395 0.36571 0.24439 -0.10010 0.01842  0.05793  47  ASP A CG    
383  O OD1   . ASP A 48  ? 0.32594 0.35545 0.21787 -0.09755 0.02016  0.05112  47  ASP A OD1   
384  O OD2   . ASP A 48  ? 0.34287 0.34809 0.24634 -0.09668 0.00893  0.06409  47  ASP A OD2   
385  N N     . GLY A 49  ? 0.27739 0.36729 0.20785 -0.11071 0.06066  0.03718  48  GLY A N     
386  C CA    . GLY A 49  ? 0.29242 0.39895 0.23668 -0.11308 0.06847  0.03608  48  GLY A CA    
387  C C     . GLY A 49  ? 0.31196 0.42125 0.27961 -0.11219 0.06584  0.03652  48  GLY A C     
388  O O     . GLY A 49  ? 0.34659 0.47133 0.32746 -0.11456 0.07134  0.03618  48  GLY A O     
389  N N     . GLU A 50  ? 0.25179 0.34669 0.22457 -0.10892 0.05701  0.03738  49  GLU A N     
390  C CA    . GLU A 50  ? 0.24142 0.33614 0.23371 -0.10814 0.05238  0.03758  49  GLU A CA    
391  C C     . GLU A 50  ? 0.20746 0.30540 0.21426 -0.09420 0.05146  0.02700  49  GLU A C     
392  O O     . GLU A 50  ? 0.21985 0.30412 0.22023 -0.08572 0.04682  0.02323  49  GLU A O     
393  C CB    . GLU A 50  ? 0.28616 0.35534 0.27188 -0.11124 0.04059  0.04560  49  GLU A CB    
394  C CG    . GLU A 50  ? 0.31100 0.37131 0.28331 -0.12137 0.03933  0.05592  49  GLU A CG    
395  C CD    . GLU A 50  ? 0.46904 0.50085 0.43184 -0.12280 0.02812  0.06393  49  GLU A CD    
396  O OE1   . GLU A 50  ? 0.44764 0.46675 0.41623 -0.11787 0.02128  0.06190  49  GLU A OE1   
397  O OE2   . GLU A 50  ? 0.49850 0.52020 0.44789 -0.12841 0.02636  0.07231  49  GLU A OE2   
398  N N     . THR A 51  ? 0.20187 0.31848 0.22877 -0.09223 0.05549  0.02307  50  THR A N     
399  C CA    . THR A 51  ? 0.16164 0.28144 0.20226 -0.07877 0.05472  0.01442  50  THR A CA    
400  C C     . THR A 51  ? 0.18061 0.28477 0.22603 -0.07547 0.04355  0.01605  50  THR A C     
401  O O     . THR A 51  ? 0.19107 0.29259 0.24005 -0.08348 0.03827  0.02162  50  THR A O     
402  C CB    . THR A 51  ? 0.22777 0.37531 0.28904 -0.07663 0.06274  0.01037  50  THR A CB    
403  O OG1   . THR A 51  ? 0.26373 0.42727 0.31966 -0.08010 0.07482  0.00826  50  THR A OG1   
404  C CG2   . THR A 51  ? 0.21271 0.36170 0.28743 -0.06144 0.06162  0.00249  50  THR A CG2   
405  N N     . SER A 52  ? 0.16175 0.25532 0.20647 -0.06441 0.04044  0.01080  51  SER A N     
406  C CA    . SER A 52  ? 0.15884 0.23806 0.20593 -0.06071 0.03104  0.01177  51  SER A CA    
407  C C     . SER A 52  ? 0.17893 0.25915 0.23493 -0.04856 0.03081  0.00564  51  SER A C     
408  O O     . SER A 52  ? 0.18837 0.27087 0.24329 -0.04227 0.03642  0.00035  51  SER A O     
409  C CB    . SER A 52  ? 0.20185 0.25892 0.23305 -0.06145 0.02512  0.01483  51  SER A CB    
410  O OG    . SER A 52  ? 0.21966 0.27207 0.24214 -0.07219 0.02393  0.02204  51  SER A OG    
411  N N     . LEU A 53  ? 0.14202 0.21814 0.20466 -0.04566 0.02400  0.00640  52  LEU A N     
412  C CA    . LEU A 53  ? 0.13876 0.20963 0.20514 -0.03489 0.02209  0.00278  52  LEU A CA    
413  C C     . LEU A 53  ? 0.15929 0.20959 0.21315 -0.03355 0.01710  0.00350  52  LEU A C     
414  O O     . LEU A 53  ? 0.16316 0.20438 0.21191 -0.03810 0.01152  0.00671  52  LEU A O     
415  C CB    . LEU A 53  ? 0.16487 0.24439 0.24385 -0.03269 0.01709  0.00388  52  LEU A CB    
416  C CG    . LEU A 53  ? 0.20621 0.31015 0.30245 -0.03216 0.02094  0.00333  52  LEU A CG    
417  C CD1   . LEU A 53  ? 0.21823 0.33256 0.32684 -0.03152 0.01349  0.00545  52  LEU A CD1   
418  C CD2   . LEU A 53  ? 0.30507 0.41340 0.40660 -0.02133 0.02796  -0.00156 52  LEU A CD2   
419  N N     . LEU A 54  ? 0.14580 0.18865 0.19532 -0.02746 0.01912  0.00018  53  LEU A N     
420  C CA    . LEU A 54  ? 0.16190 0.18926 0.20332 -0.02534 0.01480  0.00068  53  LEU A CA    
421  C C     . LEU A 54  ? 0.17468 0.19863 0.22108 -0.01834 0.01255  -0.00021 53  LEU A C     
422  O O     . LEU A 54  ? 0.17382 0.20092 0.22595 -0.01267 0.01580  -0.00274 53  LEU A O     
423  C CB    . LEU A 54  ? 0.15326 0.17551 0.18690 -0.02485 0.01765  -0.00194 53  LEU A CB    
424  C CG    . LEU A 54  ? 0.17786 0.20419 0.20405 -0.03140 0.02010  -0.00078 53  LEU A CG    
425  C CD1   . LEU A 54  ? 0.23502 0.25599 0.25180 -0.03139 0.02074  -0.00347 53  LEU A CD1   
426  C CD2   . LEU A 54  ? 0.19233 0.21499 0.21375 -0.03811 0.01573  0.00557  53  LEU A CD2   
427  N N     . ASP A 55  ? 0.16172 0.17828 0.20491 -0.01849 0.00734  0.00186  54  ASP A N     
428  C CA    . ASP A 55  ? 0.15974 0.17156 0.20354 -0.01277 0.00530  0.00189  54  ASP A CA    
429  C C     . ASP A 55  ? 0.16914 0.16990 0.20542 -0.01176 0.00533  0.00145  54  ASP A C     
430  O O     . ASP A 55  ? 0.19939 0.19441 0.23022 -0.01406 0.00261  0.00232  54  ASP A O     
431  C CB    . ASP A 55  ? 0.17697 0.18959 0.22065 -0.01420 -0.00024 0.00365  54  ASP A CB    
432  C CG    . ASP A 55  ? 0.29400 0.32058 0.34717 -0.01642 -0.00132 0.00444  54  ASP A CG    
433  O OD1   . ASP A 55  ? 0.31218 0.34832 0.37454 -0.01161 0.00141  0.00408  54  ASP A OD1   
434  O OD2   . ASP A 55  ? 0.26301 0.29085 0.31513 -0.02305 -0.00483 0.00529  54  ASP A OD2   
435  N N     . ILE A 56  ? 0.15905 0.15681 0.19591 -0.00840 0.00838  -0.00000 55  ILE A N     
436  C CA    . ILE A 56  ? 0.14850 0.13969 0.18081 -0.00881 0.00890  -0.00060 55  ILE A CA    
437  C C     . ILE A 56  ? 0.18014 0.16635 0.21163 -0.00545 0.00878  0.00079  55  ILE A C     
438  O O     . ILE A 56  ? 0.19004 0.17490 0.22419 -0.00244 0.01021  0.00142  55  ILE A O     
439  C CB    . ILE A 56  ? 0.17764 0.16901 0.20991 -0.01020 0.01231  -0.00370 55  ILE A CB    
440  C CG1   . ILE A 56  ? 0.24528 0.24266 0.27576 -0.01406 0.01299  -0.00447 55  ILE A CG1   
441  C CG2   . ILE A 56  ? 0.20588 0.19348 0.23550 -0.01165 0.01170  -0.00403 55  ILE A CG2   
442  C CD1   . ILE A 56  ? 0.28651 0.28501 0.31426 -0.01593 0.01641  -0.00853 55  ILE A CD1   
443  N N     . LEU A 57  ? 0.15580 0.13911 0.18338 -0.00555 0.00741  0.00159  56  LEU A N     
444  C CA    . LEU A 57  ? 0.16277 0.14276 0.18804 -0.00340 0.00867  0.00301  56  LEU A CA    
445  C C     . LEU A 57  ? 0.15447 0.13435 0.18152 -0.00501 0.01135  0.00223  56  LEU A C     
446  O O     . LEU A 57  ? 0.16729 0.14977 0.19498 -0.00594 0.01039  0.00124  56  LEU A O     
447  C CB    . LEU A 57  ? 0.17473 0.15326 0.19436 -0.00219 0.00645  0.00323  56  LEU A CB    
448  C CG    . LEU A 57  ? 0.18090 0.15753 0.19586 -0.00030 0.00880  0.00462  56  LEU A CG    
449  C CD1   . LEU A 57  ? 0.20847 0.18364 0.22104 0.00109  0.00838  0.00802  56  LEU A CD1   
450  C CD2   . LEU A 57  ? 0.22202 0.19692 0.23041 0.00111  0.00780  0.00263  56  LEU A CD2   
451  N N     . ASP A 58  ? 0.16587 0.14264 0.19435 -0.00551 0.01415  0.00306  57  ASP A N     
452  C CA    . ASP A 58  ? 0.18650 0.16377 0.21771 -0.00891 0.01652  0.00230  57  ASP A CA    
453  C C     . ASP A 58  ? 0.18582 0.16353 0.21530 -0.00852 0.01899  0.00533  57  ASP A C     
454  O O     . ASP A 58  ? 0.18981 0.16211 0.21553 -0.00739 0.02039  0.00869  57  ASP A O     
455  C CB    . ASP A 58  ? 0.21341 0.18429 0.24626 -0.01077 0.01839  0.00087  57  ASP A CB    
456  C CG    . ASP A 58  ? 0.22879 0.19906 0.26430 -0.01630 0.02016  -0.00061 57  ASP A CG    
457  O OD1   . ASP A 58  ? 0.24244 0.22143 0.28071 -0.01875 0.01919  -0.00104 57  ASP A OD1   
458  O OD2   . ASP A 58  ? 0.24368 0.20445 0.27923 -0.01812 0.02227  -0.00127 57  ASP A OD2   
459  N N     . THR A 59  ? 0.17088 0.15578 0.20270 -0.00875 0.01958  0.00457  58  THR A N     
460  C CA    . THR A 59  ? 0.17567 0.16381 0.20574 -0.00783 0.02325  0.00653  58  THR A CA    
461  C C     . THR A 59  ? 0.18462 0.17730 0.22080 -0.01312 0.02719  0.00786  58  THR A C     
462  O O     . THR A 59  ? 0.17660 0.17165 0.21912 -0.01726 0.02586  0.00603  58  THR A O     
463  C CB    . THR A 59  ? 0.17738 0.17143 0.20780 -0.00359 0.02255  0.00420  58  THR A CB    
464  O OG1   . THR A 59  ? 0.18055 0.18317 0.22028 -0.00449 0.02152  0.00272  58  THR A OG1   
465  C CG2   . THR A 59  ? 0.17780 0.16583 0.20248 -0.00045 0.01813  0.00267  58  THR A CG2   
466  N N     . ALA A 60  ? 0.18660 0.18079 0.21991 -0.01402 0.03209  0.01112  59  ALA A N     
467  C CA    . ALA A 60  ? 0.17711 0.17848 0.21740 -0.02026 0.03674  0.01291  59  ALA A CA    
468  C C     . ALA A 60  ? 0.19424 0.21225 0.24499 -0.01894 0.03732  0.00990  59  ALA A C     
469  O O     . ALA A 60  ? 0.21597 0.23811 0.26523 -0.01200 0.03695  0.00772  59  ALA A O     
470  C CB    . ALA A 60  ? 0.20960 0.20909 0.24210 -0.02146 0.04261  0.01811  59  ALA A CB    
471  N N     . GLY A 61  ? 0.17963 0.20735 0.24153 -0.02553 0.03813  0.00979  60  GLY A N     
472  C CA    . GLY A 61  ? 0.22606 0.27315 0.30118 -0.02404 0.03805  0.00779  60  GLY A CA    
473  C C     . GLY A 61  ? 0.29648 0.35763 0.37657 -0.02352 0.04606  0.00953  60  GLY A C     
474  O O     . GLY A 61  ? 0.44811 0.52473 0.54117 -0.03001 0.04874  0.01054  60  GLY A O     
475  N N     . GLN A 62  ? 0.29708 0.35332 0.36653 -0.01760 0.05014  0.00987  61  GLN A N     
476  C CA    . GLN A 62  ? 0.33070 0.39958 0.40115 -0.01549 0.05892  0.01039  61  GLN A CA    
477  C C     . GLN A 62  ? 0.33186 0.39759 0.39524 -0.00400 0.05824  0.00571  61  GLN A C     
478  O O     . GLN A 62  ? 0.39047 0.44044 0.44356 -0.00065 0.05218  0.00430  61  GLN A O     
479  C CB    . GLN A 62  ? 0.36607 0.42547 0.42298 -0.02120 0.06456  0.01575  61  GLN A CB    
480  C CG    . GLN A 62  ? 0.34747 0.38598 0.38600 -0.01765 0.06027  0.01669  61  GLN A CG    
481  C CD    . GLN A 62  ? 0.47784 0.51566 0.50208 -0.01149 0.06451  0.01543  61  GLN A CD    
482  O OE1   . GLN A 62  ? 0.50648 0.55196 0.52607 -0.01398 0.07295  0.01815  61  GLN A OE1   
483  N NE2   . GLN A 62  ? 0.34169 0.37015 0.35776 -0.00446 0.05884  0.01116  61  GLN A NE2   
484  N N     . GLU A 63  ? 0.43311 0.51403 0.50298 0.00194  0.06457  0.00279  62  GLU A N     
485  C CA    . GLU A 63  ? 0.49703 0.57233 0.55927 0.01307  0.06459  -0.00291 62  GLU A CA    
486  C C     . GLU A 63  ? 0.48201 0.55509 0.52833 0.01477  0.07305  -0.00424 62  GLU A C     
487  O O     . GLU A 63  ? 0.53126 0.59802 0.56869 0.02337  0.07376  -0.01031 62  GLU A O     
488  C CB    . GLU A 63  ? 0.46514 0.55530 0.54473 0.02194  0.06432  -0.00693 62  GLU A CB    
489  C CG    . GLU A 63  ? 0.43512 0.52372 0.52511 0.02211  0.05382  -0.00583 62  GLU A CG    
490  C CD    . GLU A 63  ? 0.54997 0.66294 0.66316 0.02388  0.05387  -0.00524 62  GLU A CD    
491  O OE1   . GLU A 63  ? 0.55352 0.68278 0.67714 0.01504  0.05772  -0.00220 62  GLU A OE1   
492  O OE2   . GLU A 63  ? 0.52620 0.64211 0.64767 0.03395  0.04969  -0.00744 62  GLU A OE2   
493  N N     . GLU A 64  ? 0.46212 0.53882 0.50305 0.00633  0.07930  0.00130  63  GLU A N     
494  C CA    . GLU A 64  ? 0.50434 0.57589 0.52505 0.00664  0.08572  0.00146  63  GLU A CA    
495  C C     . GLU A 64  ? 0.36793 0.41698 0.36992 0.00754  0.07721  0.00147  63  GLU A C     
496  O O     . GLU A 64  ? 0.43055 0.46907 0.43624 0.00675  0.06784  0.00231  63  GLU A O     
497  C CB    . GLU A 64  ? 0.49151 0.57189 0.51045 -0.00345 0.09430  0.00923  63  GLU A CB    
498  C CG    . GLU A 64  ? 0.57050 0.65307 0.56986 -0.00298 0.10405  0.00948  63  GLU A CG    
499  C CD    . GLU A 64  ? 0.61883 0.71248 0.61780 -0.01389 0.11402  0.01830  63  GLU A CD    
500  O OE1   . GLU A 64  ? 0.60118 0.68496 0.59936 -0.02344 0.11037  0.02708  63  GLU A OE1   
501  O OE2   . GLU A 64  ? 0.66229 0.77415 0.66171 -0.01299 0.12609  0.01638  63  GLU A OE2   
502  N N     . TYR A 65  ? 0.32686 0.37049 0.30868 0.00905  0.08069  0.00021  64  TYR A N     
503  C CA    . TYR A 65  ? 0.30460 0.33060 0.26816 0.01007  0.07281  -0.00055 64  TYR A CA    
504  C C     . TYR A 65  ? 0.30285 0.32079 0.26821 0.01742  0.06623  -0.00917 64  TYR A C     
505  O O     . TYR A 65  ? 0.29029 0.29720 0.25636 0.01657  0.05671  -0.00847 64  TYR A O     
506  C CB    . TYR A 65  ? 0.29385 0.30964 0.25493 0.00338  0.06594  0.00829  64  TYR A CB    
507  C CG    . TYR A 65  ? 0.24427 0.26459 0.20078 -0.00406 0.07312  0.01744  64  TYR A CG    
508  C CD1   . TYR A 65  ? 0.27710 0.29864 0.21374 -0.00515 0.07923  0.01971  64  TYR A CD1   
509  C CD2   . TYR A 65  ? 0.23436 0.25727 0.20534 -0.01066 0.07404  0.02345  64  TYR A CD2   
510  C CE1   . TYR A 65  ? 0.26483 0.28942 0.19557 -0.01285 0.08615  0.02948  64  TYR A CE1   
511  C CE2   . TYR A 65  ? 0.21815 0.24299 0.18506 -0.01876 0.08070  0.03232  64  TYR A CE2   
512  C CZ    . TYR A 65  ? 0.25217 0.27775 0.19912 -0.01986 0.08685  0.03605  64  TYR A CZ    
513  O OH    . TYR A 65  ? 0.25149 0.27799 0.19261 -0.02870 0.09379  0.04622  64  TYR A OH    
514  N N     . SER A 66  ? 0.35523 0.37832 0.32056 0.02474  0.07211  -0.01739 65  SER A N     
515  C CA    . SER A 66  ? 0.31406 0.32784 0.28284 0.03208  0.06659  -0.02523 65  SER A CA    
516  C C     . SER A 66  ? 0.31987 0.31517 0.27125 0.03072  0.05793  -0.02795 65  SER A C     
517  O O     . SER A 66  ? 0.30089 0.28578 0.25692 0.03228  0.05006  -0.03027 65  SER A O     
518  C CB    . SER A 66  ? 0.38815 0.40893 0.35911 0.04161  0.07526  -0.03414 65  SER A CB    
519  O OG    . SER A 66  ? 0.51175 0.53206 0.46203 0.04200  0.08257  -0.03847 65  SER A OG    
520  N N     . ALA A 67  ? 0.28290 0.27468 0.21391 0.02744  0.05899  -0.02763 66  ALA A N     
521  C CA    . ALA A 67  ? 0.35860 0.33575 0.27432 0.02513  0.04963  -0.03008 66  ALA A CA    
522  C C     . ALA A 67  ? 0.31183 0.28517 0.23775 0.02030  0.03987  -0.02299 66  ALA A C     
523  O O     . ALA A 67  ? 0.29685 0.26059 0.22425 0.02002  0.03190  -0.02600 66  ALA A O     
524  C CB    . ALA A 67  ? 0.39261 0.36955 0.28449 0.02182  0.05156  -0.02925 66  ALA A CB    
525  N N     A MET A 68  ? 0.25657 0.23711 0.19008 0.01626  0.04106  -0.01376 67  MET A N     
526  N N     B MET A 68  ? 0.25659 0.23715 0.19012 0.01627  0.04110  -0.01377 67  MET A N     
527  C CA    A MET A 68  ? 0.26323 0.24062 0.20641 0.01272  0.03326  -0.00801 67  MET A CA    
528  C CA    B MET A 68  ? 0.26328 0.24081 0.20658 0.01271  0.03338  -0.00795 67  MET A CA    
529  C C     A MET A 68  ? 0.23457 0.21192 0.19492 0.01459  0.03109  -0.01031 67  MET A C     
530  C C     B MET A 68  ? 0.23448 0.21189 0.19485 0.01458  0.03113  -0.01028 67  MET A C     
531  O O     A MET A 68  ? 0.23530 0.20641 0.19880 0.01338  0.02379  -0.01074 67  MET A O     
532  O O     B MET A 68  ? 0.23573 0.20688 0.19918 0.01335  0.02381  -0.01069 67  MET A O     
533  C CB    A MET A 68  ? 0.29517 0.27725 0.24157 0.00858  0.03581  0.00143  67  MET A CB    
534  C CB    B MET A 68  ? 0.29471 0.27716 0.24130 0.00861  0.03624  0.00141  67  MET A CB    
535  C CG    A MET A 68  ? 0.21801 0.19571 0.17178 0.00614  0.02843  0.00652  67  MET A CG    
536  C CG    B MET A 68  ? 0.29728 0.27590 0.22749 0.00620  0.03333  0.00690  67  MET A CG    
537  S SD    A MET A 68  ? 0.26411 0.23556 0.20609 0.00581  0.01839  0.00699  67  MET A SD    
538  S SD    B MET A 68  ? 0.34095 0.31294 0.27129 0.00559  0.02093  0.00836  67  MET A SD    
539  C CE    A MET A 68  ? 0.35971 0.33186 0.28145 0.00472  0.02186  0.01225  67  MET A CE    
540  C CE    B MET A 68  ? 0.36164 0.33386 0.31053 0.00405  0.02054  0.01534  67  MET A CE    
541  N N     . ARG A 69  ? 0.23488 0.22064 0.20664 0.01720  0.03718  -0.01125 68  ARG A N     
542  C CA    . ARG A 69  ? 0.25056 0.23724 0.23768 0.01893  0.03404  -0.01210 68  ARG A CA    
543  C C     . ARG A 69  ? 0.21347 0.18958 0.19742 0.02335  0.02965  -0.01834 68  ARG A C     
544  O O     . ARG A 69  ? 0.22188 0.19270 0.21192 0.02216  0.02345  -0.01725 68  ARG A O     
545  C CB    . ARG A 69  ? 0.29282 0.29329 0.29407 0.02067  0.04019  -0.01127 68  ARG A CB    
546  C CG    . ARG A 69  ? 0.31852 0.32687 0.32418 0.01401  0.04353  -0.00467 68  ARG A CG    
547  C CD    . ARG A 69  ? 0.31906 0.34299 0.34152 0.01374  0.04804  -0.00388 68  ARG A CD    
548  N NE    . ARG A 69  ? 0.32879 0.35428 0.36372 0.01602  0.04214  -0.00518 68  ARG A NE    
549  C CZ    . ARG A 69  ? 0.33777 0.36197 0.37878 0.01083  0.03690  -0.00215 68  ARG A CZ    
550  N NH1   . ARG A 69  ? 0.30894 0.32814 0.34588 0.00404  0.03664  0.00161  68  ARG A NH1   
551  N NH2   . ARG A 69  ? 0.32770 0.35480 0.37809 0.01297  0.03177  -0.00297 68  ARG A NH2   
552  N N     . ASP A 70  ? 0.23385 0.20504 0.20638 0.02762  0.03276  -0.02491 69  ASP A N     
553  C CA    . ASP A 70  ? 0.24622 0.20276 0.21356 0.03083  0.02807  -0.03136 69  ASP A CA    
554  C C     . ASP A 70  ? 0.25992 0.20676 0.22115 0.02405  0.01919  -0.02956 69  ASP A C     
555  O O     . ASP A 70  ? 0.23122 0.16822 0.19562 0.02332  0.01355  -0.03048 69  ASP A O     
556  C CB    . ASP A 70  ? 0.27275 0.22352 0.22600 0.03608  0.03316  -0.04039 69  ASP A CB    
557  C CG    . ASP A 70  ? 0.28172 0.24256 0.24359 0.04493  0.04257  -0.04398 69  ASP A CG    
558  O OD1   . ASP A 70  ? 0.28451 0.25689 0.26442 0.04675  0.04373  -0.03925 69  ASP A OD1   
559  O OD2   . ASP A 70  ? 0.34096 0.29903 0.29143 0.05003  0.04868  -0.05209 69  ASP A OD2   
560  N N     . GLN A 71  ? 0.23412 0.18383 0.18639 0.01909  0.01775  -0.02672 70  GLN A N     
561  C CA    . GLN A 71  ? 0.23084 0.17570 0.18047 0.01308  0.00933  -0.02471 70  GLN A CA    
562  C C     . GLN A 71  ? 0.22049 0.16934 0.18531 0.01048  0.00640  -0.01879 70  GLN A C     
563  O O     . GLN A 71  ? 0.22345 0.16699 0.19056 0.00688  0.00055  -0.01883 70  GLN A O     
564  C CB    . GLN A 71  ? 0.24594 0.19521 0.18445 0.00971  0.00769  -0.02171 70  GLN A CB    
565  C CG    . GLN A 71  ? 0.26750 0.21427 0.20391 0.00409  -0.00177 -0.02081 70  GLN A CG    
566  C CD    . GLN A 71  ? 0.27982 0.21435 0.20893 0.00196  -0.00649 -0.02885 70  GLN A CD    
567  O OE1   . GLN A 71  ? 0.31079 0.23836 0.22500 0.00318  -0.00541 -0.03585 70  GLN A OE1   
568  N NE2   . GLN A 71  ? 0.31073 0.24193 0.24934 -0.00192 -0.01144 -0.02791 70  GLN A NE2   
569  N N     . TYR A 72  ? 0.21052 0.16864 0.18533 0.01144  0.01065  -0.01409 71  TYR A N     
570  C CA    . TYR A 72  ? 0.20432 0.16553 0.19129 0.00895  0.00823  -0.00997 71  TYR A CA    
571  C C     . TYR A 72  ? 0.19612 0.15081 0.18715 0.00997  0.00534  -0.01206 71  TYR A C     
572  O O     . TYR A 72  ? 0.22107 0.17389 0.21562 0.00606  0.00109  -0.00990 71  TYR A O     
573  C CB    . TYR A 72  ? 0.21177 0.18211 0.20801 0.00959  0.01318  -0.00661 71  TYR A CB    
574  C CG    . TYR A 72  ? 0.18790 0.16285 0.18208 0.00765  0.01645  -0.00256 71  TYR A CG    
575  C CD1   . TYR A 72  ? 0.20969 0.18197 0.19618 0.00596  0.01358  -0.00017 71  TYR A CD1   
576  C CD2   . TYR A 72  ? 0.19489 0.17688 0.19519 0.00729  0.02199  -0.00052 71  TYR A CD2   
577  C CE1   . TYR A 72  ? 0.22172 0.19577 0.20610 0.00480  0.01609  0.00496  71  TYR A CE1   
578  C CE2   . TYR A 72  ? 0.19120 0.17460 0.18936 0.00448  0.02505  0.00419  71  TYR A CE2   
579  C CZ    . TYR A 72  ? 0.18963 0.16775 0.17946 0.00375  0.02202  0.00712  71  TYR A CZ    
580  O OH    . TYR A 72  ? 0.20787 0.18495 0.19537 0.00147  0.02472  0.01309  71  TYR A OH    
581  N N     . MET A 73  ? 0.19943 0.15080 0.19004 0.01559  0.00800  -0.01584 72  MET A N     
582  C CA    . MET A 73  ? 0.20484 0.14830 0.19950 0.01816  0.00507  -0.01663 72  MET A CA    
583  C C     . MET A 73  ? 0.23940 0.16715 0.22494 0.01551  0.00003  -0.01990 72  MET A C     
584  O O     . MET A 73  ? 0.23730 0.15788 0.22546 0.01288  -0.00437 -0.01732 72  MET A O     
585  C CB    . MET A 73  ? 0.21281 0.15942 0.21269 0.02659  0.00961  -0.01924 72  MET A CB    
586  C CG    . MET A 73  ? 0.25218 0.21571 0.26388 0.02671  0.01308  -0.01509 72  MET A CG    
587  S SD    . MET A 73  ? 0.26124 0.23439 0.28249 0.03662  0.01896  -0.01811 72  MET A SD    
588  C CE    . MET A 73  ? 0.24802 0.24155 0.28301 0.03185  0.02098  -0.01237 72  MET A CE    
589  N N     . ARG A 74  ? 0.22614 0.14883 0.20015 0.01443  0.00004  -0.02488 73  ARG A N     
590  C CA    . ARG A 74  ? 0.25802 0.16585 0.22326 0.00980  -0.00564 -0.02860 73  ARG A CA    
591  C C     . ARG A 74  ? 0.23852 0.15066 0.20785 0.00083  -0.01092 -0.02336 73  ARG A C     
592  O O     . ARG A 74  ? 0.27581 0.17791 0.24505 -0.00413 -0.01542 -0.02286 73  ARG A O     
593  C CB    . ARG A 74  ? 0.26618 0.16937 0.21662 0.00966  -0.00520 -0.03574 73  ARG A CB    
594  C CG    . ARG A 74  ? 0.27817 0.17236 0.22243 0.01830  -0.00003 -0.04342 73  ARG A CG    
595  C CD    . ARG A 74  ? 0.35869 0.24327 0.28461 0.01658  -0.00095 -0.05229 73  ARG A CD    
596  N NE    . ARG A 74  ? 0.36537 0.26424 0.28439 0.01490  0.00152  -0.05054 73  ARG A NE    
597  C CZ    . ARG A 74  ? 0.32813 0.23448 0.24217 0.02088  0.00970  -0.05281 73  ARG A CZ    
598  N NH1   . ARG A 74  ? 0.37359 0.27683 0.29034 0.02981  0.01667  -0.05808 73  ARG A NH1   
599  N NH2   . ARG A 74  ? 0.34456 0.26235 0.25108 0.01805  0.01112  -0.04922 73  ARG A NH2   
600  N N     . THR A 75  ? 0.22545 0.15222 0.19888 -0.00119 -0.00998 -0.01925 74  THR A N     
601  C CA    . THR A 75  ? 0.24756 0.18156 0.22662 -0.00814 -0.01388 -0.01494 74  THR A CA    
602  C C     . THR A 75  ? 0.25705 0.19441 0.24615 -0.00951 -0.01311 -0.01004 74  THR A C     
603  O O     . THR A 75  ? 0.24351 0.18217 0.23594 -0.01589 -0.01609 -0.00764 74  THR A O     
604  C CB    . THR A 75  ? 0.23367 0.18047 0.21367 -0.00758 -0.01287 -0.01234 74  THR A CB    
605  O OG1   . THR A 75  ? 0.28762 0.23164 0.25574 -0.00778 -0.01506 -0.01613 74  THR A OG1   
606  C CG2   . THR A 75  ? 0.28819 0.24509 0.27703 -0.01241 -0.01585 -0.00811 74  THR A CG2   
607  N N     . GLY A 76  ? 0.19934 0.13954 0.19299 -0.00436 -0.00917 -0.00850 75  GLY A N     
608  C CA    . GLY A 76  ? 0.20631 0.15127 0.20736 -0.00602 -0.00884 -0.00403 75  GLY A CA    
609  C C     . GLY A 76  ? 0.19356 0.12734 0.19277 -0.00859 -0.01232 -0.00245 75  GLY A C     
610  O O     . GLY A 76  ? 0.22496 0.14575 0.21958 -0.00530 -0.01373 -0.00495 75  GLY A O     
611  N N     . GLU A 77  ? 0.19155 0.12959 0.19369 -0.01441 -0.01330 0.00183  76  GLU A N     
612  C CA    . GLU A 77  ? 0.19427 0.12187 0.19364 -0.01824 -0.01642 0.00552  76  GLU A CA    
613  C C     . GLU A 77  ? 0.20493 0.13317 0.20589 -0.01449 -0.01642 0.00953  76  GLU A C     
614  O O     . GLU A 77  ? 0.22900 0.14511 0.22644 -0.01459 -0.01976 0.01326  76  GLU A O     
615  C CB    . GLU A 77  ? 0.21799 0.15127 0.21855 -0.02798 -0.01704 0.00866  76  GLU A CB    
616  C CG    . GLU A 77  ? 0.24298 0.17539 0.24283 -0.03330 -0.01926 0.00563  76  GLU A CG    
617  C CD    . GLU A 77  ? 0.28018 0.22358 0.28489 -0.04250 -0.01896 0.00891  76  GLU A CD    
618  O OE1   . GLU A 77  ? 0.26075 0.22109 0.27252 -0.04174 -0.01599 0.00861  76  GLU A OE1   
619  O OE2   . GLU A 77  ? 0.38074 0.31559 0.38262 -0.05048 -0.02131 0.01199  76  GLU A OE2   
620  N N     . GLY A 78  ? 0.19268 0.13427 0.19844 -0.01207 -0.01350 0.00944  77  GLY A N     
621  C CA    . GLY A 78  ? 0.18929 0.13450 0.19681 -0.00944 -0.01450 0.01281  77  GLY A CA    
622  C C     . GLY A 78  ? 0.16092 0.11865 0.17447 -0.00588 -0.01117 0.00997  77  GLY A C     
623  O O     . GLY A 78  ? 0.17391 0.13744 0.18917 -0.00706 -0.00772 0.00698  77  GLY A O     
624  N N     . PHE A 79  ? 0.16758 0.12941 0.18492 -0.00169 -0.01271 0.01151  78  PHE A N     
625  C CA    . PHE A 79  ? 0.14773 0.12107 0.17222 0.00117  -0.00984 0.00890  78  PHE A CA    
626  C C     . PHE A 79  ? 0.15194 0.13513 0.17896 -0.00115 -0.01221 0.01126  78  PHE A C     
627  O O     . PHE A 79  ? 0.16676 0.14888 0.19300 0.00046  -0.01724 0.01549  78  PHE A O     
628  C CB    . PHE A 79  ? 0.16763 0.13991 0.19698 0.00932  -0.00888 0.00688  78  PHE A CB    
629  C CG    . PHE A 79  ? 0.16863 0.13043 0.19255 0.01102  -0.00686 0.00338  78  PHE A CG    
630  C CD1   . PHE A 79  ? 0.19468 0.14146 0.21241 0.01143  -0.01023 0.00391  78  PHE A CD1   
631  C CD2   . PHE A 79  ? 0.19050 0.15644 0.21388 0.01085  -0.00214 -0.00010 78  PHE A CD2   
632  C CE1   . PHE A 79  ? 0.20186 0.13884 0.21317 0.01113  -0.00926 -0.00024 78  PHE A CE1   
633  C CE2   . PHE A 79  ? 0.18083 0.13777 0.19674 0.01132  -0.00134 -0.00345 78  PHE A CE2   
634  C CZ    . PHE A 79  ? 0.21605 0.15913 0.22617 0.01129  -0.00503 -0.00418 78  PHE A CZ    
635  N N     . LEU A 80  ? 0.15755 0.14935 0.18700 -0.00487 -0.00917 0.00856  79  LEU A N     
636  C CA    . LEU A 80  ? 0.15941 0.16173 0.19223 -0.00728 -0.01149 0.00893  79  LEU A CA    
637  C C     . LEU A 80  ? 0.16808 0.17957 0.21182 -0.00322 -0.01059 0.00785  79  LEU A C     
638  O O     . LEU A 80  ? 0.16987 0.18209 0.21682 -0.00290 -0.00534 0.00507  79  LEU A O     
639  C CB    . LEU A 80  ? 0.19422 0.19923 0.22413 -0.01383 -0.00840 0.00538  79  LEU A CB    
640  C CG    . LEU A 80  ? 0.20997 0.21117 0.23043 -0.01844 -0.00805 0.00544  79  LEU A CG    
641  C CD1   . LEU A 80  ? 0.23534 0.23940 0.25402 -0.02322 -0.00475 0.00040  79  LEU A CD1   
642  C CD2   . LEU A 80  ? 0.20893 0.21085 0.22304 -0.01981 -0.01378 0.01037  79  LEU A CD2   
643  N N     . LEU A 81  ? 0.15028 0.16993 0.20006 -0.00010 -0.01559 0.01065  80  LEU A N     
644  C CA    . LEU A 81  ? 0.15769 0.19105 0.22104 0.00379  -0.01488 0.00996  80  LEU A CA    
645  C C     . LEU A 81  ? 0.15921 0.20549 0.22627 -0.00394 -0.01730 0.00903  80  LEU A C     
646  O O     . LEU A 81  ? 0.15830 0.21129 0.22512 -0.00520 -0.02452 0.01188  80  LEU A O     
647  C CB    . LEU A 81  ? 0.19017 0.22637 0.26008 0.01290  -0.01992 0.01376  80  LEU A CB    
648  C CG    . LEU A 81  ? 0.19931 0.21846 0.26313 0.02010  -0.02002 0.01497  80  LEU A CG    
649  C CD1   . LEU A 81  ? 0.22269 0.24286 0.29383 0.03033  -0.02577 0.01916  80  LEU A CD1   
650  C CD2   . LEU A 81  ? 0.24147 0.25584 0.30512 0.02252  -0.01221 0.00988  80  LEU A CD2   
651  N N     . VAL A 82  ? 0.13173 0.18110 0.20173 -0.00950 -0.01190 0.00528  81  VAL A N     
652  C CA    . VAL A 82  ? 0.14081 0.19790 0.21205 -0.01874 -0.01377 0.00288  81  VAL A CA    
653  C C     . VAL A 82  ? 0.13527 0.21104 0.22258 -0.02011 -0.01412 0.00294  81  VAL A C     
654  O O     . VAL A 82  ? 0.14617 0.22557 0.24141 -0.01763 -0.00787 0.00273  81  VAL A O     
655  C CB    . VAL A 82  ? 0.13172 0.17721 0.19546 -0.02488 -0.00798 -0.00118 81  VAL A CB    
656  C CG1   . VAL A 82  ? 0.18291 0.23231 0.24541 -0.03497 -0.01034 -0.00515 81  VAL A CG1   
657  C CG2   . VAL A 82  ? 0.17410 0.20487 0.22524 -0.02287 -0.00671 -0.00127 81  VAL A CG2   
658  N N     . PHE A 83  ? 0.13015 0.21942 0.22208 -0.02473 -0.02141 0.00333  82  PHE A N     
659  C CA    . PHE A 83  ? 0.13747 0.24645 0.24523 -0.03018 -0.02202 0.00239  82  PHE A CA    
660  C C     . PHE A 83  ? 0.14744 0.25727 0.24956 -0.04295 -0.02621 -0.00171 82  PHE A C     
661  O O     . PHE A 83  ? 0.14637 0.24333 0.23249 -0.04564 -0.02857 -0.00373 82  PHE A O     
662  C CB    . PHE A 83  ? 0.12911 0.25933 0.25292 -0.02261 -0.02804 0.00670  82  PHE A CB    
663  C CG    . PHE A 83  ? 0.13497 0.27093 0.25457 -0.02277 -0.03965 0.00965  82  PHE A CG    
664  C CD1   . PHE A 83  ? 0.15930 0.28134 0.26636 -0.01560 -0.04311 0.01346  82  PHE A CD1   
665  C CD2   . PHE A 83  ? 0.14218 0.29713 0.26913 -0.03124 -0.04743 0.00896  82  PHE A CD2   
666  C CE1   . PHE A 83  ? 0.16385 0.29024 0.26465 -0.01597 -0.05386 0.01770  82  PHE A CE1   
667  C CE2   . PHE A 83  ? 0.17302 0.33382 0.29365 -0.03169 -0.05911 0.01231  82  PHE A CE2   
668  C CZ    . PHE A 83  ? 0.13952 0.28515 0.24600 -0.02364 -0.06205 0.01723  82  PHE A CZ    
669  N N     . ALA A 84  ? 0.12659 0.25096 0.24131 -0.05151 -0.02621 -0.00362 83  ALA A N     
670  C CA    . ALA A 84  ? 0.14113 0.26637 0.25091 -0.06490 -0.03102 -0.00871 83  ALA A CA    
671  C C     . ALA A 84  ? 0.15549 0.30662 0.27712 -0.06787 -0.04189 -0.00692 83  ALA A C     
672  O O     . ALA A 84  ? 0.12912 0.30199 0.27098 -0.06442 -0.04241 -0.00325 83  ALA A O     
673  C CB    . ALA A 84  ? 0.15967 0.27877 0.27294 -0.07552 -0.02396 -0.01266 83  ALA A CB    
674  N N     . ILE A 85  ? 0.17122 0.32162 0.28044 -0.07446 -0.05053 -0.00975 84  ILE A N     
675  C CA    . ILE A 85  ? 0.15148 0.32686 0.26967 -0.07666 -0.06298 -0.00707 84  ILE A CA    
676  C C     . ILE A 85  ? 0.18046 0.37773 0.31790 -0.08816 -0.06521 -0.00962 84  ILE A C     
677  O O     . ILE A 85  ? 0.16645 0.38629 0.31623 -0.08710 -0.07424 -0.00671 84  ILE A O     
678  C CB    . ILE A 85  ? 0.18871 0.35770 0.28517 -0.08177 -0.07189 -0.00942 84  ILE A CB    
679  C CG1   . ILE A 85  ? 0.20802 0.36060 0.28957 -0.09582 -0.06836 -0.01997 84  ILE A CG1   
680  C CG2   . ILE A 85  ? 0.19827 0.35065 0.27891 -0.07040 -0.07029 -0.00464 84  ILE A CG2   
681  C CD1   . ILE A 85  ? 0.29570 0.45953 0.37747 -0.10810 -0.07665 -0.02518 84  ILE A CD1   
682  N N     . ASN A 86  ? 0.18305 0.37018 0.32260 -0.09690 -0.05603 -0.01434 85  ASN A N     
683  C CA    . ASN A 86  ? 0.17144 0.37014 0.32635 -0.10531 -0.05521 -0.01611 85  ASN A CA    
684  C C     . ASN A 86  ? 0.20982 0.41773 0.38374 -0.10132 -0.04487 -0.01187 85  ASN A C     
685  O O     . ASN A 86  ? 0.21929 0.42831 0.40201 -0.10987 -0.04005 -0.01324 85  ASN A O     
686  C CB    . ASN A 86  ? 0.19495 0.37171 0.33561 -0.11896 -0.05345 -0.02427 85  ASN A CB    
687  C CG    . ASN A 86  ? 0.22748 0.37772 0.35834 -0.12014 -0.04180 -0.02632 85  ASN A CG    
688  O OD1   . ASN A 86  ? 0.19818 0.34316 0.32626 -0.11174 -0.03645 -0.02321 85  ASN A OD1   
689  N ND2   . ASN A 86  ? 0.32346 0.45650 0.44962 -0.13039 -0.03816 -0.03118 85  ASN A ND2   
690  N N     . ASN A 87  ? 0.14817 0.36224 0.32745 -0.08847 -0.04136 -0.00657 86  ASN A N     
691  C CA    . ASN A 87  ? 0.13766 0.35986 0.33205 -0.08240 -0.03027 -0.00299 86  ASN A CA    
692  C C     . ASN A 87  ? 0.12428 0.36376 0.33067 -0.06509 -0.03306 0.00229  86  ASN A C     
693  O O     . ASN A 87  ? 0.11899 0.34062 0.31241 -0.05261 -0.03172 0.00390  86  ASN A O     
694  C CB    . ASN A 87  ? 0.16111 0.35316 0.33943 -0.08160 -0.01866 -0.00419 86  ASN A CB    
695  C CG    . ASN A 87  ? 0.18964 0.38772 0.37823 -0.07545 -0.00714 -0.00060 86  ASN A CG    
696  O OD1   . ASN A 87  ? 0.17181 0.39535 0.37920 -0.06816 -0.00627 0.00237  86  ASN A OD1   
697  N ND2   . ASN A 87  ? 0.31125 0.48595 0.48682 -0.07730 0.00196  -0.00084 86  ASN A ND2   
698  N N     . THR A 88  ? 0.12025 0.38787 0.34874 -0.06321 -0.03645 0.00414  87  THR A N     
699  C CA    . THR A 88  ? 0.14294 0.42732 0.38473 -0.04587 -0.03989 0.00880  87  THR A CA    
700  C C     . THR A 88  ? 0.12345 0.40485 0.36914 -0.03350 -0.02773 0.01057  87  THR A C     
701  O O     . THR A 88  ? 0.10964 0.38059 0.34945 -0.01801 -0.02901 0.01275  87  THR A O     
702  C CB    . THR A 88  ? 0.14934 0.46048 0.41300 -0.04542 -0.04514 0.00913  87  THR A CB    
703  O OG1   . THR A 88  ? 0.17817 0.49158 0.43569 -0.05412 -0.05849 0.00790  87  THR A OG1   
704  C CG2   . THR A 88  ? 0.16115 0.48800 0.44094 -0.02569 -0.04630 0.01312  87  THR A CG2   
705  N N     . LYS A 89  ? 0.11689 0.39890 0.36691 -0.03955 -0.01528 0.00874  88  LYS A N     
706  C CA    . LYS A 89  ? 0.12043 0.39453 0.36807 -0.02822 -0.00302 0.00906  88  LYS A CA    
707  C C     . LYS A 89  ? 0.12082 0.35830 0.34129 -0.02136 -0.00259 0.00811  88  LYS A C     
708  O O     . LYS A 89  ? 0.12696 0.35623 0.34379 -0.00706 0.00138  0.00836  88  LYS A O     
709  C CB    . LYS A 89  ? 0.15047 0.42767 0.40140 -0.03929 0.00962  0.00822  88  LYS A CB    
710  C CG    . LYS A 89  ? 0.21827 0.48761 0.46367 -0.02933 0.02264  0.00814  88  LYS A CG    
711  C CD    . LYS A 89  ? 0.26866 0.56187 0.53377 -0.01521 0.02657  0.00796  88  LYS A CD    
712  C CE    . LYS A 89  ? 0.32126 0.60743 0.57864 -0.00582 0.04033  0.00663  88  LYS A CE    
713  N NZ    . LYS A 89  ? 0.35112 0.61524 0.58830 -0.01789 0.04758  0.00721  88  LYS A NZ    
714  N N     . SER A 90  ? 0.10368 0.31883 0.30511 -0.03161 -0.00617 0.00641  89  SER A N     
715  C CA    . SER A 90  ? 0.10863 0.29245 0.28666 -0.02575 -0.00532 0.00567  89  SER A CA    
716  C C     . SER A 90  ? 0.11224 0.29262 0.28685 -0.01350 -0.01367 0.00798  89  SER A C     
717  O O     . SER A 90  ? 0.14233 0.30347 0.30469 -0.00447 -0.01103 0.00817  89  SER A O     
718  C CB    . SER A 90  ? 0.12835 0.29099 0.28867 -0.03790 -0.00656 0.00295  89  SER A CB    
719  O OG    . SER A 90  ? 0.13394 0.29890 0.29039 -0.04327 -0.01760 0.00201  89  SER A OG    
720  N N     . PHE A 91  ? 0.11498 0.31351 0.30000 -0.01366 -0.02419 0.01023  90  PHE A N     
721  C CA    . PHE A 91  ? 0.13926 0.33531 0.32213 -0.00165 -0.03280 0.01430  90  PHE A CA    
722  C C     . PHE A 91  ? 0.15938 0.36509 0.35745 0.01457  -0.02893 0.01609  90  PHE A C     
723  O O     . PHE A 91  ? 0.13371 0.32186 0.32277 0.02607  -0.02976 0.01778  90  PHE A O     
724  C CB    . PHE A 91  ? 0.14827 0.36240 0.33715 -0.00709 -0.04610 0.01692  90  PHE A CB    
725  C CG    . PHE A 91  ? 0.15273 0.36550 0.33957 0.00493  -0.05643 0.02315  90  PHE A CG    
726  C CD1   . PHE A 91  ? 0.16496 0.35136 0.32840 0.00603  -0.05923 0.02495  90  PHE A CD1   
727  C CD2   . PHE A 91  ? 0.16363 0.40133 0.37252 0.01536  -0.06288 0.02778  90  PHE A CD2   
728  C CE1   . PHE A 91  ? 0.17613 0.35819 0.33579 0.01605  -0.06846 0.03198  90  PHE A CE1   
729  C CE2   . PHE A 91  ? 0.22054 0.45376 0.42654 0.02711  -0.07289 0.03476  90  PHE A CE2   
730  C CZ    . PHE A 91  ? 0.22933 0.43311 0.40942 0.02680  -0.07563 0.03717  90  PHE A CZ    
731  N N     . GLU A 92  ? 0.13125 0.36451 0.35247 0.01542  -0.02417 0.01533  91  GLU A N     
732  C CA    . GLU A 92  ? 0.13428 0.37793 0.37053 0.03137  -0.01798 0.01530  91  GLU A CA    
733  C C     . GLU A 92  ? 0.14579 0.36442 0.36597 0.03622  -0.00631 0.01146  91  GLU A C     
734  O O     . GLU A 92  ? 0.23272 0.44748 0.45599 0.05119  -0.00252 0.01035  91  GLU A O     
735  C CB    . GLU A 92  ? 0.16358 0.44461 0.42781 0.02836  -0.01346 0.01474  91  GLU A CB    
736  C CG    . GLU A 92  ? 0.18465 0.48850 0.46329 0.02318  -0.02658 0.01734  91  GLU A CG    
737  C CD    . GLU A 92  ? 0.27992 0.60940 0.57985 0.01680  -0.02205 0.01438  91  GLU A CD    
738  O OE1   . GLU A 92  ? 0.25152 0.58218 0.55242 0.00887  -0.00955 0.01159  91  GLU A OE1   
739  O OE2   . GLU A 92  ? 0.31185 0.65998 0.62742 0.01947  -0.03121 0.01564  91  GLU A OE2   
740  N N     . ASP A 93  ? 0.15657 0.35807 0.35971 0.02422  -0.00094 0.00915  92  ASP A N     
741  C CA    . ASP A 93  ? 0.18372 0.36216 0.37015 0.02780  0.00838  0.00606  92  ASP A CA    
742  C C     . ASP A 93  ? 0.17300 0.32332 0.34104 0.03482  0.00327  0.00646  92  ASP A C     
743  O O     . ASP A 93  ? 0.18803 0.32073 0.34404 0.03999  0.00948  0.00358  92  ASP A O     
744  C CB    . ASP A 93  ? 0.23380 0.40151 0.40753 0.01343  0.01394  0.00482  92  ASP A CB    
745  C CG    . ASP A 93  ? 0.32069 0.50886 0.50750 0.00643  0.02329  0.00442  92  ASP A CG    
746  O OD1   . ASP A 93  ? 0.26476 0.47743 0.47083 0.01327  0.02754  0.00419  92  ASP A OD1   
747  O OD2   . ASP A 93  ? 0.34644 0.52592 0.52442 -0.00605 0.02674  0.00462  92  ASP A OD2   
748  N N     . ILE A 94  ? 0.15815 0.30346 0.32197 0.03333  -0.00783 0.01004  93  ILE A N     
749  C CA    . ILE A 94  ? 0.15378 0.27156 0.29801 0.03569  -0.01198 0.01119  93  ILE A CA    
750  C C     . ILE A 94  ? 0.21176 0.31730 0.35483 0.05011  -0.00979 0.01025  93  ILE A C     
751  O O     . ILE A 94  ? 0.21175 0.29386 0.33853 0.05073  -0.00707 0.00819  93  ILE A O     
752  C CB    . ILE A 94  ? 0.17149 0.28907 0.31177 0.03211  -0.02395 0.01613  93  ILE A CB    
753  C CG1   . ILE A 94  ? 0.16969 0.28911 0.30272 0.01677  -0.02515 0.01474  93  ILE A CG1   
754  C CG2   . ILE A 94  ? 0.19396 0.28569 0.31704 0.03648  -0.02821 0.01897  93  ILE A CG2   
755  C CD1   . ILE A 94  ? 0.18993 0.28701 0.30440 0.01035  -0.01961 0.01173  93  ILE A CD1   
756  N N     . HIS A 95  ? 0.18937 0.31021 0.34995 0.06189  -0.01114 0.01128  94  HIS A N     
757  C CA    . HIS A 95  ? 0.22583 0.33148 0.38473 0.07676  -0.00990 0.00982  94  HIS A CA    
758  C C     . HIS A 95  ? 0.25883 0.35319 0.40860 0.07824  0.00183  0.00250  94  HIS A C     
759  O O     . HIS A 95  ? 0.24470 0.31474 0.38157 0.08427  0.00245  -0.00005 94  HIS A O     
760  C CB    . HIS A 95  ? 0.26473 0.38994 0.44635 0.09129  -0.01314 0.01197  94  HIS A CB    
761  C CG    . HIS A 95  ? 0.33182 0.48573 0.53360 0.09453  -0.00356 0.00764  94  HIS A CG    
762  N ND1   . HIS A 95  ? 0.34164 0.49693 0.55074 0.10856  0.00553  0.00191  94  HIS A ND1   
763  C CD2   . HIS A 95  ? 0.27335 0.45594 0.48928 0.08474  -0.00100 0.00798  94  HIS A CD2   
764  C CE1   . HIS A 95  ? 0.39671 0.58269 0.62427 0.10755  0.01389  -0.00056 94  HIS A CE1   
765  N NE2   . HIS A 95  ? 0.38685 0.58965 0.61936 0.09263  0.00980  0.00349  94  HIS A NE2   
766  N N     . HIS A 96  ? 0.22980 0.34003 0.38402 0.07135  0.01064  -0.00056 95  HIS A N     
767  C CA    . HIS A 96  ? 0.21104 0.31203 0.35439 0.07205  0.02158  -0.00675 95  HIS A CA    
768  C C     . HIS A 96  ? 0.23129 0.30518 0.35088 0.06403  0.02007  -0.00735 95  HIS A C     
769  O O     . HIS A 96  ? 0.23903 0.29560 0.34543 0.06808  0.02411  -0.01210 95  HIS A O     
770  C CB    . HIS A 96  ? 0.29250 0.41652 0.44477 0.06475  0.03092  -0.00781 95  HIS A CB    
771  C CG    . HIS A 96  ? 0.39791 0.55162 0.57462 0.07296  0.03549  -0.00861 95  HIS A CG    
772  N ND1   . HIS A 96  ? 0.43514 0.59115 0.61781 0.08839  0.04175  -0.01377 95  HIS A ND1   
773  C CD2   . HIS A 96  ? 0.40648 0.59028 0.60425 0.06770  0.03514  -0.00545 95  HIS A CD2   
774  C CE1   . HIS A 96  ? 0.45810 0.64625 0.66603 0.09342  0.04537  -0.01335 95  HIS A CE1   
775  N NE2   . HIS A 96  ? 0.38763 0.59397 0.60556 0.08033  0.04110  -0.00802 95  HIS A NE2   
776  N N     . TYR A 97  ? 0.17946 0.25045 0.29365 0.05262  0.01432  -0.00316 96  TYR A N     
777  C CA    . TYR A 97  ? 0.18010 0.22883 0.27485 0.04577  0.01284  -0.00344 96  TYR A CA    
778  C C     . TYR A 97  ? 0.21608 0.24398 0.30207 0.05185  0.00695  -0.00313 96  TYR A C     
779  O O     . TYR A 97  ? 0.23575 0.24522 0.30779 0.05164  0.00847  -0.00626 96  TYR A O     
780  C CB    . TYR A 97  ? 0.21400 0.26508 0.30632 0.03372  0.00863  0.00018  96  TYR A CB    
781  C CG    . TYR A 97  ? 0.21856 0.28268 0.31536 0.02549  0.01468  -0.00027 96  TYR A CG    
782  C CD1   . TYR A 97  ? 0.22356 0.27847 0.30907 0.02069  0.02037  -0.00168 96  TYR A CD1   
783  C CD2   . TYR A 97  ? 0.22120 0.30666 0.33368 0.02205  0.01407  0.00132  96  TYR A CD2   
784  C CE1   . TYR A 97  ? 0.26301 0.32696 0.35177 0.01326  0.02576  -0.00084 96  TYR A CE1   
785  C CE2   . TYR A 97  ? 0.20387 0.29941 0.32051 0.01326  0.01976  0.00131  96  TYR A CE2   
786  C CZ    . TYR A 97  ? 0.24960 0.33264 0.35352 0.00906  0.02588  0.00055  96  TYR A CZ    
787  O OH    . TYR A 97  ? 0.28923 0.37885 0.39560 0.00010  0.03164  0.00179  96  TYR A OH    
788  N N     . ARG A 98  ? 0.19829 0.22871 0.29231 0.05707  -0.00026 0.00101  97  ARG A N     
789  C CA    . ARG A 98  ? 0.22508 0.23366 0.31074 0.06248  -0.00606 0.00269  97  ARG A CA    
790  C C     . ARG A 98  ? 0.25450 0.25081 0.33810 0.07346  -0.00112 -0.00354 97  ARG A C     
791  O O     . ARG A 98  ? 0.26646 0.23890 0.33615 0.07317  -0.00242 -0.00559 97  ARG A O     
792  C CB    . ARG A 98  ? 0.25829 0.27239 0.35263 0.06664  -0.01531 0.00985  97  ARG A CB    
793  C CG    . ARG A 98  ? 0.30258 0.29229 0.38807 0.07200  -0.02148 0.01325  97  ARG A CG    
794  C CD    . ARG A 98  ? 0.30984 0.30446 0.40032 0.07393  -0.03173 0.02244  97  ARG A CD    
795  N NE    . ARG A 98  ? 0.35146 0.32057 0.43336 0.07950  -0.03769 0.02717  97  ARG A NE    
796  C CZ    . ARG A 98  ? 0.40884 0.36912 0.49816 0.09418  -0.03924 0.02730  97  ARG A CZ    
797  N NH1   . ARG A 98  ? 0.47453 0.45209 0.58119 0.10579  -0.03456 0.02238  97  ARG A NH1   
798  N NH2   . ARG A 98  ? 0.53911 0.47234 0.61865 0.09743  -0.04526 0.03262  97  ARG A NH2   
799  N N     . GLU A 99  ? 0.22871 0.24147 0.32603 0.08275  0.00486  -0.00720 98  GLU A N     
800  C CA    . GLU A 99  ? 0.24219 0.24401 0.33712 0.09435  0.01084  -0.01479 98  GLU A CA    
801  C C     . GLU A 99  ? 0.22956 0.21872 0.30641 0.08796  0.01727  -0.02144 98  GLU A C     
802  O O     . GLU A 99  ? 0.27162 0.23855 0.33633 0.09248  0.01803  -0.02725 98  GLU A O     
803  C CB    . GLU A 99  ? 0.25244 0.28014 0.36719 0.10479  0.01789  -0.01773 98  GLU A CB    
804  C CG    . GLU A 99  ? 0.35610 0.39665 0.49092 0.11535  0.01117  -0.01223 98  GLU A CG    
805  C CD    . GLU A 99  ? 0.47141 0.54816 0.63018 0.12026  0.01723  -0.01297 98  GLU A CD    
806  O OE1   . GLU A 99  ? 0.46449 0.55338 0.62306 0.11722  0.02849  -0.01863 98  GLU A OE1   
807  O OE2   . GLU A 99  ? 0.45408 0.54850 0.63202 0.12647  0.01046  -0.00725 98  GLU A OE2   
808  N N     . GLN A 100 ? 0.21746 0.21999 0.29207 0.07755  0.02151  -0.02069 99  GLN A N     
809  C CA    . GLN A 100 ? 0.23774 0.22985 0.29484 0.07113  0.02611  -0.02527 99  GLN A CA    
810  C C     . GLN A 100 ? 0.24747 0.21574 0.28934 0.06482  0.01889  -0.02433 99  GLN A C     
811  O O     . GLN A 100 ? 0.25767 0.20992 0.28505 0.06459  0.02021  -0.03014 99  GLN A O     
812  C CB    . GLN A 100 ? 0.29401 0.30308 0.35227 0.06117  0.03051  -0.02235 99  GLN A CB    
813  C CG    . GLN A 100 ? 0.36507 0.39319 0.43023 0.06478  0.04105  -0.02554 99  GLN A CG    
814  C CD    . GLN A 100 ? 0.43792 0.45572 0.48859 0.07045  0.04807  -0.03391 99  GLN A CD    
815  O OE1   . GLN A 100 ? 0.47725 0.49639 0.53291 0.08199  0.05247  -0.03976 99  GLN A OE1   
816  N NE2   . GLN A 100 ? 0.44547 0.45290 0.47780 0.06275  0.04873  -0.03479 99  GLN A NE2   
817  N N     . ILE A 101 ? 0.21459 0.18137 0.25904 0.05879  0.01134  -0.01733 100 ILE A N     
818  C CA    . ILE A 101 ? 0.22576 0.17291 0.25745 0.05190  0.00540  -0.01594 100 ILE A CA    
819  C C     . ILE A 101 ? 0.23711 0.16178 0.26308 0.05867  0.00228  -0.01902 100 ILE A C     
820  O O     . ILE A 101 ? 0.25981 0.16667 0.27248 0.05467  0.00109  -0.02298 100 ILE A O     
821  C CB    . ILE A 101 ? 0.24925 0.20132 0.28458 0.04440  -0.00065 -0.00804 100 ILE A CB    
822  C CG1   . ILE A 101 ? 0.21614 0.18467 0.25414 0.03666  0.00244  -0.00651 100 ILE A CG1   
823  C CG2   . ILE A 101 ? 0.26487 0.19795 0.28904 0.03804  -0.00622 -0.00600 100 ILE A CG2   
824  C CD1   . ILE A 101 ? 0.22280 0.20076 0.26720 0.03193  -0.00210 -0.00055 100 ILE A CD1   
825  N N     . LYS A 102 ? 0.22548 0.14994 0.26166 0.06910  0.00046  -0.01735 101 LYS A N     
826  C CA    . LYS A 102 ? 0.25090 0.15077 0.28221 0.07716  -0.00241 -0.02018 101 LYS A CA    
827  C C     . LYS A 102 ? 0.26519 0.15429 0.28712 0.08224  0.00424  -0.03167 101 LYS A C     
828  O O     . LYS A 102 ? 0.29084 0.15382 0.30091 0.08263  0.00185  -0.03631 101 LYS A O     
829  C CB    . LYS A 102 ? 0.27871 0.18334 0.32516 0.09016  -0.00512 -0.01614 101 LYS A CB    
830  C CG    . LYS A 102 ? 0.32435 0.23192 0.37470 0.08495  -0.01415 -0.00443 101 LYS A CG    
831  C CD    . LYS A 102 ? 0.42353 0.33999 0.48971 0.09757  -0.01838 0.00098  101 LYS A CD    
832  C CE    . LYS A 102 ? 0.49385 0.39268 0.56261 0.11320  -0.01711 -0.00406 101 LYS A CE    
833  N NZ    . LYS A 102 ? 0.44145 0.35540 0.52998 0.12778  -0.02031 0.00082  101 LYS A NZ    
834  N N     . ARG A 103 ? 0.26589 0.17440 0.29285 0.08657  0.01286  -0.03665 102 ARG A N     
835  C CA    . ARG A 103 ? 0.29190 0.19183 0.30855 0.09237  0.02016  -0.04814 102 ARG A CA    
836  C C     . ARG A 103 ? 0.27449 0.16393 0.27164 0.08021  0.01942  -0.05174 102 ARG A C     
837  O O     . ARG A 103 ? 0.32767 0.19597 0.31011 0.08106  0.01946  -0.06031 102 ARG A O     
838  C CB    . ARG A 103 ? 0.33596 0.26337 0.36406 0.09902  0.03024  -0.05073 102 ARG A CB    
839  C CG    . ARG A 103 ? 0.44194 0.37046 0.45885 0.10260  0.04048  -0.06155 102 ARG A CG    
840  C CD    . ARG A 103 ? 0.48607 0.44791 0.51583 0.10212  0.04914  -0.05864 102 ARG A CD    
841  N NE    . ARG A 103 ? 0.54377 0.52192 0.59406 0.11617  0.05426  -0.06009 102 ARG A NE    
842  C CZ    . ARG A 103 ? 0.40707 0.40810 0.47975 0.11760  0.05224  -0.05214 102 ARG A CZ    
843  N NH1   . ARG A 103 ? 0.46317 0.47258 0.53959 0.10550  0.04580  -0.04268 102 ARG A NH1   
844  N NH2   . ARG A 103 ? 0.44749 0.46455 0.53966 0.13174  0.05692  -0.05441 102 ARG A NH2   
845  N N     . VAL A 104 ? 0.26736 0.17109 0.26444 0.06905  0.01818  -0.04550 103 VAL A N     
846  C CA    . VAL A 104 ? 0.27995 0.17789 0.26105 0.05856  0.01691  -0.04781 103 VAL A CA    
847  C C     . VAL A 104 ? 0.29616 0.17217 0.26911 0.05150  0.00818  -0.04699 103 VAL A C     
848  O O     . VAL A 104 ? 0.32581 0.18804 0.28377 0.04666  0.00643  -0.05332 103 VAL A O     
849  C CB    . VAL A 104 ? 0.26126 0.17965 0.24673 0.05022  0.01781  -0.04062 103 VAL A CB    
850  C CG1   . VAL A 104 ? 0.28513 0.19755 0.25753 0.03995  0.01379  -0.04056 103 VAL A CG1   
851  C CG2   . VAL A 104 ? 0.25684 0.19417 0.24609 0.05451  0.02720  -0.04227 103 VAL A CG2   
852  N N     . LYS A 105 ? 0.28586 0.15913 0.26781 0.04974  0.00244  -0.03904 104 LYS A N     
853  C CA    . LYS A 105 ? 0.30276 0.15636 0.27798 0.04176  -0.00519 -0.03677 104 LYS A CA    
854  C C     . LYS A 105 ? 0.33617 0.16333 0.30749 0.04882  -0.00755 -0.04094 104 LYS A C     
855  O O     . LYS A 105 ? 0.36087 0.16754 0.32495 0.04152  -0.01359 -0.03982 104 LYS A O     
856  C CB    . LYS A 105 ? 0.31818 0.18155 0.30190 0.03473  -0.00958 -0.02582 104 LYS A CB    
857  C CG    . LYS A 105 ? 0.30629 0.19326 0.29383 0.02888  -0.00672 -0.02286 104 LYS A CG    
858  C CD    . LYS A 105 ? 0.29639 0.19240 0.29046 0.02168  -0.01023 -0.01389 104 LYS A CD    
859  C CE    . LYS A 105 ? 0.25493 0.14226 0.24295 0.01049  -0.01513 -0.01130 104 LYS A CE    
860  N NZ    . LYS A 105 ? 0.26360 0.15281 0.24490 0.00432  -0.01503 -0.01572 104 LYS A NZ    
861  N N     . ASP A 106 ? 0.32115 0.14767 0.29727 0.06296  -0.00247 -0.04618 105 ASP A N     
862  C CA    . ASP A 106 ? 0.34055 0.14005 0.31306 0.07248  -0.00368 -0.05175 105 ASP A CA    
863  C C     . ASP A 106 ? 0.33034 0.11687 0.30786 0.06921  -0.01136 -0.04108 105 ASP A C     
864  O O     . ASP A 106 ? 0.39024 0.15554 0.36060 0.06331  -0.01454 -0.04135 105 ASP A O     
865  C CB    . ASP A 106 ? 0.35455 0.13682 0.31073 0.06734  -0.00214 -0.06293 105 ASP A CB    
866  C CG    . ASP A 106 ? 0.38962 0.15449 0.34735 0.07462  -0.00021 -0.06777 105 ASP A CG    
867  O OD1   . ASP A 106 ? 0.39563 0.16801 0.36652 0.08817  0.00430  -0.06711 105 ASP A OD1   
868  O OD2   . ASP A 106 ? 0.41066 0.15481 0.35768 0.06689  -0.00323 -0.07230 105 ASP A OD2   
869  N N     . SER A 107 ? 0.34306 0.14502 0.33288 0.07181  -0.01401 -0.03102 106 SER A N     
870  C CA    . SER A 107 ? 0.34396 0.13519 0.33516 0.06698  -0.02170 -0.01957 106 SER A CA    
871  C C     . SER A 107 ? 0.35205 0.16094 0.35841 0.07594  -0.02370 -0.01085 106 SER A C     
872  O O     . SER A 107 ? 0.37882 0.21653 0.39454 0.07634  -0.01974 -0.01049 106 SER A O     
873  C CB    . SER A 107 ? 0.37371 0.16828 0.35791 0.04958  -0.02520 -0.01441 106 SER A CB    
874  O OG    . SER A 107 ? 0.48593 0.27010 0.46945 0.04426  -0.03188 -0.00324 106 SER A OG    
875  N N     . GLU A 108 ? 0.40531 0.20289 0.41410 0.07920  -0.02849 -0.00236 107 GLU A N     
876  C CA    . GLU A 108 ? 0.41764 0.23083 0.43870 0.08572  -0.03313 0.00789  107 GLU A CA    
877  C C     . GLU A 108 ? 0.43491 0.25237 0.45144 0.07308  -0.03990 0.01874  107 GLU A C     
878  O O     . GLU A 108 ? 0.51808 0.35270 0.54291 0.07555  -0.04387 0.02710  107 GLU A O     
879  C CB    . GLU A 108 ? 0.51571 0.31671 0.54110 0.09624  -0.03478 0.01272  107 GLU A CB    
880  C CG    . GLU A 108 ? 0.55961 0.36326 0.59425 0.11062  -0.02731 0.00320  107 GLU A CG    
881  C CD    . GLU A 108 ? 0.54034 0.33800 0.58418 0.12321  -0.02926 0.00946  107 GLU A CD    
882  O OE1   . GLU A 108 ? 0.66093 0.43807 0.69695 0.11929  -0.03502 0.01812  107 GLU A OE1   
883  O OE2   . GLU A 108 ? 0.55425 0.36856 0.61372 0.13687  -0.02470 0.00615  107 GLU A OE2   
884  N N     . ASP A 109 ? 0.39114 0.19789 0.39495 0.05832  -0.04002 0.01868  108 ASP A N     
885  C CA    . ASP A 109 ? 0.43923 0.25202 0.43764 0.04479  -0.04378 0.02859  108 ASP A CA    
886  C C     . ASP A 109 ? 0.43437 0.26293 0.42976 0.03235  -0.03867 0.02351  108 ASP A C     
887  O O     . ASP A 109 ? 0.48790 0.30512 0.47447 0.02158  -0.03852 0.02206  108 ASP A O     
888  C CB    . ASP A 109 ? 0.51199 0.29818 0.49938 0.03833  -0.04844 0.03608  108 ASP A CB    
889  C CG    . ASP A 109 ? 0.66844 0.45854 0.64798 0.02275  -0.05117 0.04536  108 ASP A CG    
890  O OD1   . ASP A 109 ? 0.66049 0.47070 0.64314 0.02164  -0.05270 0.05161  108 ASP A OD1   
891  O OD2   . ASP A 109 ? 0.69333 0.47175 0.66434 0.01089  -0.04994 0.04517  108 ASP A OD2   
892  N N     . VAL A 110 ? 0.35260 0.20816 0.35640 0.03380  -0.03481 0.02117  109 VAL A N     
893  C CA    . VAL A 110 ? 0.29019 0.16143 0.29259 0.02393  -0.03036 0.01758  109 VAL A CA    
894  C C     . VAL A 110 ? 0.26464 0.15312 0.26891 0.01785  -0.03187 0.02464  109 VAL A C     
895  O O     . VAL A 110 ? 0.27682 0.17719 0.28822 0.02385  -0.03376 0.02782  109 VAL A O     
896  C CB    . VAL A 110 ? 0.27409 0.15952 0.28258 0.02953  -0.02406 0.00884  109 VAL A CB    
897  C CG1   . VAL A 110 ? 0.27324 0.17282 0.28018 0.02015  -0.02046 0.00677  109 VAL A CG1   
898  C CG2   . VAL A 110 ? 0.32378 0.19276 0.32800 0.03595  -0.02182 0.00051  109 VAL A CG2   
899  N N     . PRO A 111 ? 0.23935 0.13176 0.23802 0.00616  -0.03079 0.02633  110 PRO A N     
900  C CA    . PRO A 111 ? 0.23464 0.14371 0.23350 0.00057  -0.03091 0.03098  110 PRO A CA    
901  C C     . PRO A 111 ? 0.20350 0.13297 0.21106 0.00430  -0.02774 0.02672  110 PRO A C     
902  O O     . PRO A 111 ? 0.19940 0.13554 0.21052 0.00448  -0.02278 0.02019  110 PRO A O     
903  C CB    . PRO A 111 ? 0.22985 0.14041 0.22327 -0.01097 -0.02807 0.03062  110 PRO A CB    
904  C CG    . PRO A 111 ? 0.25818 0.14832 0.24661 -0.01346 -0.02982 0.03021  110 PRO A CG    
905  C CD    . PRO A 111 ? 0.27601 0.15785 0.26807 -0.00257 -0.02978 0.02403  110 PRO A CD    
906  N N     . MET A 112 ? 0.21012 0.14922 0.22055 0.00656  -0.03121 0.03103  111 MET A N     
907  C CA    . MET A 112 ? 0.21305 0.17110 0.23215 0.00844  -0.02917 0.02752  111 MET A CA    
908  C C     . MET A 112 ? 0.18748 0.15597 0.20405 0.00451  -0.03375 0.03260  111 MET A C     
909  O O     . MET A 112 ? 0.21383 0.17564 0.22461 0.00492  -0.03983 0.04012  111 MET A O     
910  C CB    . MET A 112 ? 0.25250 0.21505 0.28306 0.01936  -0.02952 0.02552  111 MET A CB    
911  C CG    . MET A 112 ? 0.26461 0.21694 0.29672 0.02552  -0.02521 0.01980  111 MET A CG    
912  S SD    . MET A 112 ? 0.30418 0.26680 0.35139 0.03920  -0.02430 0.01746  111 MET A SD    
913  C CE    . MET A 112 ? 0.40049 0.34300 0.44260 0.04609  -0.02008 0.01073  111 MET A CE    
914  N N     . VAL A 113 ? 0.19300 0.17710 0.21350 0.00094  -0.03129 0.02850  112 VAL A N     
915  C CA    . VAL A 113 ? 0.19905 0.19502 0.21692 -0.00337 -0.03573 0.03106  112 VAL A CA    
916  C C     . VAL A 113 ? 0.16631 0.17845 0.19674 -0.00136 -0.03536 0.02680  112 VAL A C     
917  O O     . VAL A 113 ? 0.17565 0.19014 0.21173 -0.00182 -0.02894 0.02082  112 VAL A O     
918  C CB    . VAL A 113 ? 0.18467 0.18110 0.19120 -0.01329 -0.03220 0.02900  112 VAL A CB    
919  C CG1   . VAL A 113 ? 0.21142 0.22012 0.21324 -0.01871 -0.03568 0.02874  112 VAL A CG1   
920  C CG2   . VAL A 113 ? 0.21589 0.19953 0.21105 -0.01684 -0.03234 0.03431  112 VAL A CG2   
921  N N     . LEU A 114 ? 0.17850 0.20225 0.21360 0.00046  -0.04255 0.03058  113 LEU A N     
922  C CA    . LEU A 114 ? 0.18307 0.22545 0.23128 0.00015  -0.04321 0.02709  113 LEU A CA    
923  C C     . LEU A 114 ? 0.15829 0.20714 0.19848 -0.01095 -0.04343 0.02335  113 LEU A C     
924  O O     . LEU A 114 ? 0.19009 0.23787 0.21759 -0.01564 -0.04842 0.02653  113 LEU A O     
925  C CB    . LEU A 114 ? 0.17681 0.23082 0.23522 0.00749  -0.05211 0.03316  113 LEU A CB    
926  C CG    . LEU A 114 ? 0.16684 0.24424 0.24220 0.00686  -0.05361 0.03029  113 LEU A CG    
927  C CD1   . LEU A 114 ? 0.19351 0.27389 0.28218 0.01156  -0.04478 0.02526  113 LEU A CD1   
928  C CD2   . LEU A 114 ? 0.19670 0.28792 0.28181 0.01377  -0.06408 0.03721  113 LEU A CD2   
929  N N     . VAL A 115 ? 0.17414 0.22846 0.22052 -0.01530 -0.03780 0.01655  114 VAL A N     
930  C CA    . VAL A 115 ? 0.18879 0.24526 0.22770 -0.02549 -0.03660 0.01096  114 VAL A CA    
931  C C     . VAL A 115 ? 0.14595 0.21864 0.19729 -0.02960 -0.03894 0.00792  114 VAL A C     
932  O O     . VAL A 115 ? 0.17110 0.24792 0.23535 -0.02776 -0.03400 0.00606  114 VAL A O     
933  C CB    . VAL A 115 ? 0.17831 0.22202 0.21215 -0.02774 -0.02728 0.00566  114 VAL A CB    
934  C CG1   . VAL A 115 ? 0.22058 0.26394 0.24751 -0.03660 -0.02537 -0.00101 114 VAL A CG1   
935  C CG2   . VAL A 115 ? 0.18456 0.21586 0.20802 -0.02513 -0.02565 0.00879  114 VAL A CG2   
936  N N     . GLY A 116 ? 0.17349 0.25630 0.22043 -0.03599 -0.04666 0.00770  115 GLY A N     
937  C CA    . GLY A 116 ? 0.18302 0.28218 0.24104 -0.04285 -0.04992 0.00404  115 GLY A CA    
938  C C     . GLY A 116 ? 0.20497 0.29620 0.25253 -0.05408 -0.04610 -0.00476 115 GLY A C     
939  O O     . GLY A 116 ? 0.19500 0.28386 0.22703 -0.06002 -0.05006 -0.00733 115 GLY A O     
940  N N     . ASN A 117 ? 0.17438 0.25955 0.22861 -0.05659 -0.03800 -0.00935 116 ASN A N     
941  C CA    . ASN A 117 ? 0.17460 0.24632 0.21883 -0.06500 -0.03292 -0.01766 116 ASN A CA    
942  C C     . ASN A 117 ? 0.18367 0.26474 0.23412 -0.07664 -0.03657 -0.02297 116 ASN A C     
943  O O     . ASN A 117 ? 0.19476 0.29551 0.26010 -0.07824 -0.04223 -0.01975 116 ASN A O     
944  C CB    . ASN A 117 ? 0.16865 0.22559 0.21547 -0.06068 -0.02264 -0.01826 116 ASN A CB    
945  C CG    . ASN A 117 ? 0.17743 0.21682 0.21339 -0.06587 -0.01692 -0.02589 116 ASN A CG    
946  O OD1   . ASN A 117 ? 0.20907 0.24221 0.23058 -0.06803 -0.01765 -0.03037 116 ASN A OD1   
947  N ND2   . ASN A 117 ? 0.20071 0.23172 0.24312 -0.06779 -0.01086 -0.02744 116 ASN A ND2   
948  N N     . LYS A 118 ? 0.20988 0.27652 0.24923 -0.08487 -0.03323 -0.03163 117 LYS A N     
949  C CA    . LYS A 118 ? 0.21577 0.28543 0.25692 -0.09836 -0.03653 -0.03880 117 LYS A CA    
950  C C     . LYS A 118 ? 0.23266 0.31799 0.26752 -0.10508 -0.04813 -0.04050 117 LYS A C     
951  O O     . LYS A 118 ? 0.22791 0.32697 0.27139 -0.11540 -0.05455 -0.04303 117 LYS A O     
952  C CB    . LYS A 118 ? 0.21253 0.29053 0.27369 -0.10277 -0.03418 -0.03658 117 LYS A CB    
953  C CG    . LYS A 118 ? 0.19099 0.25440 0.25642 -0.09576 -0.02328 -0.03331 117 LYS A CG    
954  C CD    . LYS A 118 ? 0.19500 0.26181 0.27501 -0.10378 -0.01946 -0.03248 117 LYS A CD    
955  C CE    . LYS A 118 ? 0.19480 0.24681 0.27542 -0.09657 -0.00948 -0.02832 117 LYS A CE    
956  N NZ    . LYS A 118 ? 0.20821 0.26294 0.30101 -0.10574 -0.00521 -0.02644 117 LYS A NZ    
957  N N     . SER A 119 ? 0.24300 0.32677 0.26199 -0.10017 -0.05114 -0.03880 118 SER A N     
958  C CA    A SER A 119 ? 0.25974 0.35849 0.26971 -0.10579 -0.06304 -0.03870 118 SER A CA    
959  C CA    B SER A 119 ? 0.25982 0.35851 0.26969 -0.10577 -0.06303 -0.03870 118 SER A CA    
960  C C     . SER A 119 ? 0.26315 0.35649 0.25962 -0.11951 -0.06568 -0.05071 118 SER A C     
961  O O     . SER A 119 ? 0.29211 0.39733 0.28356 -0.12299 -0.07512 -0.05030 118 SER A O     
962  C CB    A SER A 119 ? 0.26294 0.35853 0.25633 -0.09827 -0.06443 -0.03322 118 SER A CB    
963  C CB    B SER A 119 ? 0.26319 0.35843 0.25605 -0.09842 -0.06435 -0.03344 118 SER A CB    
964  O OG    A SER A 119 ? 0.21918 0.31810 0.22452 -0.08591 -0.06322 -0.02234 118 SER A OG    
965  O OG    B SER A 119 ? 0.37839 0.45470 0.35129 -0.10047 -0.05648 -0.04155 118 SER A OG    
966  N N     . ASP A 120 ? 0.26290 0.33427 0.25327 -0.12283 -0.05612 -0.06005 119 ASP A N     
967  C CA    . ASP A 120 ? 0.30124 0.36112 0.28111 -0.13107 -0.05614 -0.07054 119 ASP A CA    
968  C C     . ASP A 120 ? 0.32036 0.38998 0.31727 -0.13830 -0.06121 -0.07021 119 ASP A C     
969  O O     . ASP A 120 ? 0.36224 0.42695 0.35131 -0.14638 -0.06457 -0.07791 119 ASP A O     
970  C CB    . ASP A 120 ? 0.29662 0.32902 0.26862 -0.12984 -0.04408 -0.07895 119 ASP A CB    
971  C CG    . ASP A 120 ? 0.30271 0.32813 0.29339 -0.12715 -0.03706 -0.07484 119 ASP A CG    
972  O OD1   . ASP A 120 ? 0.30456 0.33474 0.30317 -0.11929 -0.03390 -0.06726 119 ASP A OD1   
973  O OD2   . ASP A 120 ? 0.32239 0.33710 0.31885 -0.13253 -0.03497 -0.07841 119 ASP A OD2   
974  N N     . LEU A 121 ? 0.28286 0.36791 0.30394 -0.13569 -0.06167 -0.06135 120 LEU A N     
975  C CA    . LEU A 121 ? 0.28508 0.37522 0.32130 -0.14373 -0.06334 -0.06258 120 LEU A CA    
976  C C     . LEU A 121 ? 0.30147 0.41822 0.34645 -0.14703 -0.07555 -0.05932 120 LEU A C     
977  O O     . LEU A 121 ? 0.32862 0.46445 0.37794 -0.13982 -0.08176 -0.05162 120 LEU A O     
978  C CB    . LEU A 121 ? 0.32845 0.42194 0.38578 -0.14063 -0.05631 -0.05580 120 LEU A CB    
979  C CG    . LEU A 121 ? 0.31117 0.37786 0.36331 -0.13884 -0.04457 -0.05833 120 LEU A CG    
980  C CD1   . LEU A 121 ? 0.30137 0.37612 0.37331 -0.13542 -0.03872 -0.04994 120 LEU A CD1   
981  C CD2   . LEU A 121 ? 0.39654 0.44166 0.44046 -0.14776 -0.04256 -0.06699 120 LEU A CD2   
982  N N     . PRO A 122 ? 0.28792 0.40576 0.33758 -0.15764 -0.07906 -0.06456 121 PRO A N     
983  C CA    . PRO A 122 ? 0.31122 0.45466 0.37009 -0.16191 -0.09116 -0.06252 121 PRO A CA    
984  C C     . PRO A 122 ? 0.28287 0.45176 0.37194 -0.16032 -0.09253 -0.05422 121 PRO A C     
985  O O     . PRO A 122 ? 0.29351 0.48326 0.39446 -0.16558 -0.10149 -0.05362 121 PRO A O     
986  C CB    . PRO A 122 ? 0.32736 0.45768 0.37622 -0.17502 -0.09347 -0.07339 121 PRO A CB    
987  C CG    . PRO A 122 ? 0.32724 0.43279 0.37776 -0.17780 -0.08195 -0.07695 121 PRO A CG    
988  C CD    . PRO A 122 ? 0.30716 0.40039 0.35098 -0.16630 -0.07292 -0.07332 121 PRO A CD    
989  N N     . SER A 123 ? 0.25999 0.42863 0.36176 -0.15284 -0.08357 -0.04803 122 SER A N     
990  C CA    . SER A 123 ? 0.26982 0.46102 0.39993 -0.15075 -0.08180 -0.04095 122 SER A CA    
991  C C     . SER A 123 ? 0.25322 0.46308 0.39440 -0.13627 -0.08281 -0.03171 122 SER A C     
992  O O     . SER A 123 ? 0.20961 0.43030 0.37004 -0.13070 -0.07616 -0.02618 122 SER A O     
993  C CB    . SER A 123 ? 0.28704 0.46302 0.42404 -0.15516 -0.06970 -0.04144 122 SER A CB    
994  O OG    . SER A 123 ? 0.26646 0.41617 0.38697 -0.15048 -0.06131 -0.04296 122 SER A OG    
995  N N     . ARG A 124 ? 0.22638 0.43966 0.35490 -0.12986 -0.09101 -0.02977 123 ARG A N     
996  C CA    . ARG A 124 ? 0.22209 0.44822 0.35832 -0.11528 -0.09254 -0.02071 123 ARG A CA    
997  C C     . ARG A 124 ? 0.20139 0.45636 0.36751 -0.10904 -0.09422 -0.01443 123 ARG A C     
998  O O     . ARG A 124 ? 0.21376 0.48689 0.39178 -0.11429 -0.10142 -0.01527 123 ARG A O     
999  C CB    . ARG A 124 ? 0.29956 0.52648 0.41772 -0.11109 -0.10337 -0.01844 123 ARG A CB    
1000 C CG    . ARG A 124 ? 0.22602 0.46454 0.35149 -0.09565 -0.10701 -0.00797 123 ARG A CG    
1001 C CD    . ARG A 124 ? 0.26752 0.50304 0.37155 -0.09265 -0.11748 -0.00452 123 ARG A CD    
1002 N NE    . ARG A 124 ? 0.29599 0.50645 0.37202 -0.09702 -0.11283 -0.00905 123 ARG A NE    
1003 C CZ    . ARG A 124 ? 0.35577 0.55368 0.42332 -0.08976 -0.10798 -0.00476 123 ARG A CZ    
1004 N NH1   . ARG A 124 ? 0.26793 0.47325 0.35214 -0.07762 -0.10665 0.00391  123 ARG A NH1   
1005 N NH2   . ARG A 124 ? 0.34766 0.52481 0.38981 -0.09463 -0.10379 -0.00984 123 ARG A NH2   
1006 N N     . THR A 125 ? 0.18956 0.44901 0.36812 -0.09744 -0.08703 -0.00861 124 THR A N     
1007 C CA    . THR A 125 ? 0.18395 0.47014 0.38955 -0.08744 -0.08772 -0.00267 124 THR A CA    
1008 C C     . THR A 125 ? 0.17286 0.46420 0.38016 -0.06975 -0.09148 0.00508  124 THR A C     
1009 O O     . THR A 125 ? 0.21004 0.52310 0.43785 -0.05938 -0.09492 0.00967  124 THR A O     
1010 C CB    . THR A 125 ? 0.21134 0.50033 0.43367 -0.08835 -0.07404 -0.00296 124 THR A CB    
1011 O OG1   . THR A 125 ? 0.18637 0.45650 0.39827 -0.08287 -0.06441 -0.00195 124 THR A OG1   
1012 C CG2   . THR A 125 ? 0.21949 0.50257 0.44212 -0.10553 -0.07046 -0.00892 124 THR A CG2   
1013 N N     . VAL A 126 ? 0.20391 0.47509 0.39073 -0.06587 -0.09098 0.00667  125 VAL A N     
1014 C CA    . VAL A 126 ? 0.19374 0.46413 0.37953 -0.04960 -0.09440 0.01482  125 VAL A CA    
1015 C C     . VAL A 126 ? 0.18860 0.45169 0.35286 -0.05063 -0.10656 0.01741  125 VAL A C     
1016 O O     . VAL A 126 ? 0.24513 0.49027 0.38605 -0.06057 -0.10620 0.01298  125 VAL A O     
1017 C CB    . VAL A 126 ? 0.21512 0.46490 0.39268 -0.04446 -0.08350 0.01541  125 VAL A CB    
1018 C CG1   . VAL A 126 ? 0.17146 0.41234 0.34624 -0.02616 -0.08525 0.02301  125 VAL A CG1   
1019 C CG2   . VAL A 126 ? 0.17943 0.43263 0.37238 -0.04608 -0.07004 0.01189  125 VAL A CG2   
1020 N N     . ASP A 127 ? 0.24036 0.51632 0.41138 -0.03996 -0.11665 0.02440  126 ASP A N     
1021 C CA    . ASP A 127 ? 0.22915 0.49815 0.37830 -0.04044 -0.12810 0.02839  126 ASP A CA    
1022 C C     . ASP A 127 ? 0.24227 0.48854 0.37195 -0.03390 -0.12630 0.03421  126 ASP A C     
1023 O O     . ASP A 127 ? 0.25781 0.49885 0.39706 -0.02173 -0.12101 0.03912  126 ASP A O     
1024 C CB    . ASP A 127 ? 0.28574 0.57338 0.44791 -0.02960 -0.13952 0.03540  126 ASP A CB    
1025 C CG    . ASP A 127 ? 0.37244 0.68352 0.55056 -0.03774 -0.14476 0.03044  126 ASP A CG    
1026 O OD1   . ASP A 127 ? 0.46681 0.77598 0.62950 -0.05163 -0.14989 0.02522  126 ASP A OD1   
1027 O OD2   . ASP A 127 ? 0.46397 0.79500 0.67003 -0.03036 -0.14324 0.03129  126 ASP A OD2   
1028 N N     . THR A 128 ? 0.26631 0.49845 0.36792 -0.04209 -0.13045 0.03348  127 THR A N     
1029 C CA    . THR A 128 ? 0.25675 0.46727 0.33797 -0.03762 -0.12918 0.03958  127 THR A CA    
1030 C C     . THR A 128 ? 0.25107 0.46056 0.33934 -0.02058 -0.13467 0.05181  127 THR A C     
1031 O O     . THR A 128 ? 0.23670 0.42775 0.32175 -0.01205 -0.12885 0.05617  127 THR A O     
1032 C CB    . THR A 128 ? 0.34987 0.54932 0.39988 -0.04859 -0.13306 0.03709  127 THR A CB    
1033 O OG1   . THR A 128 ? 0.41834 0.61111 0.45975 -0.06247 -0.12524 0.02454  127 THR A OG1   
1034 C CG2   . THR A 128 ? 0.39831 0.57758 0.42690 -0.04391 -0.13275 0.04536  127 THR A CG2   
1035 N N     . LYS A 129 ? 0.26735 0.49226 0.36383 -0.01485 -0.14468 0.05618  128 LYS A N     
1036 C CA    . LYS A 129 ? 0.30726 0.52876 0.40984 0.00228  -0.14998 0.06714  128 LYS A CA    
1037 C C     . LYS A 129 ? 0.27534 0.49611 0.40124 0.01566  -0.14159 0.06759  128 LYS A C     
1038 O O     . LYS A 129 ? 0.26478 0.46741 0.38727 0.02776  -0.14044 0.07465  128 LYS A O     
1039 C CB    . LYS A 129 ? 0.28147 0.52277 0.39233 0.00655  -0.16230 0.07056  128 LYS A CB    
1040 C CG    . LYS A 129 ? 0.41132 0.64244 0.51697 0.02181  -0.16988 0.08278  128 LYS A CG    
1041 C CD    . LYS A 129 ? 0.51885 0.72997 0.58996 0.01484  -0.17416 0.08896  128 LYS A CD    
1042 C CE    . LYS A 129 ? 0.51915 0.70597 0.58024 0.02762  -0.17456 0.10063  128 LYS A CE    
1043 N NZ    . LYS A 129 ? 0.38426 0.54940 0.44297 0.02830  -0.16268 0.09926  128 LYS A NZ    
1044 N N     . GLN A 130 ? 0.25549 0.49411 0.40409 0.01337  -0.13484 0.05970  129 GLN A N     
1045 C CA    . GLN A 130 ? 0.26992 0.50824 0.43891 0.02595  -0.12518 0.05906  129 GLN A CA    
1046 C C     . GLN A 130 ? 0.21630 0.42686 0.37101 0.02618  -0.11578 0.05894  129 GLN A C     
1047 O O     . GLN A 130 ? 0.22355 0.41974 0.38274 0.03977  -0.11018 0.06100  129 GLN A O     
1048 C CB    . GLN A 130 ? 0.22560 0.48626 0.41741 0.02028  -0.11731 0.05024  129 GLN A CB    
1049 C CG    . GLN A 130 ? 0.35796 0.64355 0.56015 0.01154  -0.12445 0.04651  129 GLN A CG    
1050 C CD    . GLN A 130 ? 0.38176 0.68288 0.60288 0.00320  -0.11424 0.03814  129 GLN A CD    
1051 O OE1   . GLN A 130 ? 0.40897 0.72077 0.63102 -0.01147 -0.11637 0.03266  129 GLN A OE1   
1052 N NE2   . GLN A 130 ? 0.33155 0.63159 0.56611 0.01227  -0.10248 0.03707  129 GLN A NE2   
1053 N N     . ALA A 131 ? 0.18996 0.38667 0.32366 0.01136  -0.11075 0.05262  130 ALA A N     
1054 C CA    . ALA A 131 ? 0.19009 0.35677 0.30701 0.01071  -0.09883 0.04884  130 ALA A CA    
1055 C C     . ALA A 131 ? 0.20199 0.34569 0.29987 0.01649  -0.10311 0.05729  130 ALA A C     
1056 O O     . ALA A 131 ? 0.21704 0.33958 0.31134 0.02385  -0.09600 0.05782  130 ALA A O     
1057 C CB    . ALA A 131 ? 0.24282 0.40324 0.34496 -0.00555 -0.09268 0.03988  130 ALA A CB    
1058 N N     . GLN A 132 ? 0.26350 0.41042 0.34739 0.01178  -0.11465 0.06388  131 GLN A N     
1059 C CA    . GLN A 132 ? 0.29291 0.41947 0.35886 0.01662  -0.11982 0.07423  131 GLN A CA    
1060 C C     . GLN A 132 ? 0.28327 0.40522 0.36457 0.03455  -0.12327 0.08226  131 GLN A C     
1061 O O     . GLN A 132 ? 0.32465 0.42057 0.39589 0.04022  -0.12015 0.08664  131 GLN A O     
1062 C CB    . GLN A 132 ? 0.34999 0.48581 0.39983 0.00914  -0.13303 0.08107  131 GLN A CB    
1063 C CG    . GLN A 132 ? 0.33637 0.47344 0.36668 -0.00824 -0.12984 0.07257  131 GLN A CG    
1064 C CD    . GLN A 132 ? 0.41875 0.56734 0.43366 -0.01500 -0.14235 0.07713  131 GLN A CD    
1065 O OE1   . GLN A 132 ? 0.39808 0.55976 0.42387 -0.00753 -0.15087 0.08155  131 GLN A OE1   
1066 N NE2   . GLN A 132 ? 0.54188 0.68284 0.53046 -0.02803 -0.14013 0.07327  131 GLN A NE2   
1067 N N     . ASP A 133 ? 0.26293 0.40981 0.36932 0.04368  -0.12956 0.08392  132 ASP A N     
1068 C CA    . ASP A 133 ? 0.30127 0.44120 0.42067 0.06237  -0.12947 0.08779  132 ASP A CA    
1069 C C     . ASP A 133 ? 0.30451 0.42893 0.43253 0.06936  -0.11732 0.08255  132 ASP A C     
1070 O O     . ASP A 133 ? 0.31411 0.41448 0.43780 0.08035  -0.11579 0.08623  132 ASP A O     
1071 C CB    . ASP A 133 ? 0.32747 0.49675 0.46992 0.07056  -0.13441 0.08598  132 ASP A CB    
1072 C CG    . ASP A 133 ? 0.36461 0.54459 0.49747 0.06744  -0.14792 0.09207  132 ASP A CG    
1073 O OD1   . ASP A 133 ? 0.40264 0.56453 0.51001 0.06211  -0.15290 0.09915  132 ASP A OD1   
1074 O OD2   . ASP A 133 ? 0.35918 0.56633 0.50997 0.06989  -0.15351 0.08964  132 ASP A OD2   
1075 N N     . LEU A 134 ? 0.24379 0.37725 0.37860 0.06198  -0.10598 0.07111  133 LEU A N     
1076 C CA    . LEU A 134 ? 0.25532 0.37275 0.39280 0.06732  -0.09252 0.06369  133 LEU A CA    
1077 C C     . LEU A 134 ? 0.24059 0.32393 0.35291 0.06251  -0.08828 0.06421  133 LEU A C     
1078 O O     . LEU A 134 ? 0.29217 0.35411 0.40264 0.07177  -0.08431 0.06426  133 LEU A O     
1079 C CB    . LEU A 134 ? 0.27310 0.40607 0.41946 0.05846  -0.08196 0.05302  133 LEU A CB    
1080 C CG    . LEU A 134 ? 0.26185 0.38197 0.41074 0.06375  -0.06832 0.04543  133 LEU A CG    
1081 C CD1   . LEU A 134 ? 0.32335 0.45156 0.49270 0.08152  -0.06751 0.04613  133 LEU A CD1   
1082 C CD2   . LEU A 134 ? 0.22753 0.36054 0.38039 0.05228  -0.05910 0.03710  133 LEU A CD2   
1083 N N     . ALA A 135 ? 0.25237 0.33072 0.34535 0.04784  -0.08908 0.06422  134 ALA A N     
1084 C CA    . ALA A 135 ? 0.25154 0.30148 0.32296 0.04259  -0.08470 0.06503  134 ALA A CA    
1085 C C     . ALA A 135 ? 0.27900 0.30898 0.34210 0.05061  -0.09246 0.07621  134 ALA A C     
1086 O O     . ALA A 135 ? 0.27895 0.28386 0.33424 0.05307  -0.08786 0.07627  134 ALA A O     
1087 C CB    . ALA A 135 ? 0.24751 0.29849 0.30105 0.02652  -0.08360 0.06285  134 ALA A CB    
1088 N N     . ARG A 136 ? 0.30176 0.34185 0.36586 0.05409  -0.10484 0.08608  135 ARG A N     
1089 C CA    . ARG A 136 ? 0.31833 0.33822 0.37479 0.06257  -0.11321 0.09849  135 ARG A CA    
1090 C C     . ARG A 136 ? 0.35816 0.36481 0.42968 0.07931  -0.10996 0.09685  135 ARG A C     
1091 O O     . ARG A 136 ? 0.38366 0.36097 0.44315 0.08256  -0.10785 0.09994  135 ARG A O     
1092 C CB    . ARG A 136 ? 0.32834 0.36421 0.38290 0.06412  -0.12575 0.10767  135 ARG A CB    
1093 C CG    . ARG A 136 ? 0.44235 0.45567 0.48204 0.07005  -0.13032 0.11817  135 ARG A CG    
1094 C CD    . ARG A 136 ? 0.46377 0.49432 0.49913 0.07046  -0.14142 0.12542  135 ARG A CD    
1095 N NE    . ARG A 136 ? 0.59148 0.62838 0.60618 0.05347  -0.14431 0.12717  135 ARG A NE    
1096 C CZ    . ARG A 136 ? 0.62731 0.64377 0.61673 0.04390  -0.14283 0.13329  135 ARG A CZ    
1097 N NH1   . ARG A 136 ? 0.68772 0.67518 0.66986 0.04773  -0.13861 0.13823  135 ARG A NH1   
1098 N NH2   . ARG A 136 ? 0.55565 0.58132 0.52642 0.02954  -0.14479 0.13360  135 ARG A NH2   
1099 N N     . SER A 137 ? 0.33664 0.36473 0.43229 0.08865  -0.10667 0.08967  136 SER A N     
1100 C CA    . SER A 137 ? 0.38911 0.40669 0.49622 0.10469  -0.10032 0.08493  136 SER A CA    
1101 C C     . SER A 137 ? 0.38691 0.37777 0.48614 0.10259  -0.09071 0.07789  136 SER A C     
1102 O O     . SER A 137 ? 0.38956 0.35864 0.48640 0.11262  -0.08619 0.07569  136 SER A O     
1103 C CB    . SER A 137 ? 0.37906 0.42895 0.51288 0.11376  -0.09731 0.07821  136 SER A CB    
1104 O OG    . SER A 137 ? 0.45195 0.51538 0.59451 0.10599  -0.08843 0.06869  136 SER A OG    
1105 N N     . TYR A 138 ? 0.30197 0.29484 0.39051 0.08733  -0.08347 0.07129  137 TYR A N     
1106 C CA    . TYR A 138 ? 0.36182 0.33419 0.43975 0.08204  -0.07310 0.06299  137 TYR A CA    
1107 C C     . TYR A 138 ? 0.30280 0.24826 0.35834 0.07235  -0.07529 0.06889  137 TYR A C     
1108 O O     . TYR A 138 ? 0.37810 0.30559 0.42480 0.06757  -0.06828 0.06303  137 TYR A O     
1109 C CB    . TYR A 138 ? 0.32650 0.31592 0.40478 0.07032  -0.06437 0.05366  137 TYR A CB    
1110 C CG    . TYR A 138 ? 0.30268 0.31681 0.40074 0.07571  -0.05846 0.04603  137 TYR A CG    
1111 C CD1   . TYR A 138 ? 0.33199 0.35143 0.44715 0.09166  -0.05782 0.04470  137 TYR A CD1   
1112 C CD2   . TYR A 138 ? 0.27219 0.30385 0.37181 0.06469  -0.05292 0.04026  137 TYR A CD2   
1113 C CE1   . TYR A 138 ? 0.34063 0.38512 0.47429 0.09559  -0.05101 0.03791  137 TYR A CE1   
1114 C CE2   . TYR A 138 ? 0.30897 0.36262 0.42589 0.06776  -0.04686 0.03425  137 TYR A CE2   
1115 C CZ    . TYR A 138 ? 0.29227 0.35371 0.42633 0.08281  -0.04578 0.03335  137 TYR A CZ    
1116 O OH    . TYR A 138 ? 0.35785 0.44376 0.50962 0.08493  -0.03858 0.02770  137 TYR A OH    
1117 N N     . GLY A 139 ? 0.33264 0.27768 0.37868 0.06803  -0.08464 0.08024  138 GLY A N     
1118 C CA    . GLY A 139 ? 0.36271 0.28646 0.38700 0.05663  -0.08619 0.08714  138 GLY A CA    
1119 C C     . GLY A 139 ? 0.36451 0.29362 0.37849 0.04081  -0.07806 0.08038  138 GLY A C     
1120 O O     . GLY A 139 ? 0.38493 0.29517 0.38644 0.03289  -0.07422 0.08056  138 GLY A O     
1121 N N     . ILE A 140 ? 0.27516 0.22956 0.29541 0.03622  -0.07523 0.07406  139 ILE A N     
1122 C CA    . ILE A 140 ? 0.28741 0.24687 0.29971 0.02323  -0.06730 0.06701  139 ILE A CA    
1123 C C     . ILE A 140 ? 0.24463 0.22331 0.25135 0.01490  -0.07081 0.06866  139 ILE A C     
1124 O O     . ILE A 140 ? 0.29621 0.28949 0.30953 0.01933  -0.07860 0.07258  139 ILE A O     
1125 C CB    . ILE A 140 ? 0.25221 0.21892 0.27632 0.02521  -0.05809 0.05499  139 ILE A CB    
1126 C CG1   . ILE A 140 ? 0.23799 0.22925 0.27839 0.02997  -0.05889 0.05124  139 ILE A CG1   
1127 C CG2   . ILE A 140 ? 0.30204 0.24963 0.32908 0.03320  -0.05490 0.05222  139 ILE A CG2   
1128 C CD1   . ILE A 140 ? 0.22233 0.22189 0.27232 0.02978  -0.04922 0.04063  139 ILE A CD1   
1129 N N     . PRO A 141 ? 0.28643 0.26636 0.28150 0.00303  -0.06522 0.06497  140 PRO A N     
1130 C CA    . PRO A 141 ? 0.26549 0.26176 0.25293 -0.00543 -0.06737 0.06416  140 PRO A CA    
1131 C C     . PRO A 141 ? 0.21690 0.23278 0.21836 -0.00464 -0.06592 0.05543  140 PRO A C     
1132 O O     . PRO A 141 ? 0.22309 0.24002 0.23721 -0.00086 -0.05951 0.04833  140 PRO A O     
1133 C CB    . PRO A 141 ? 0.29017 0.28056 0.26419 -0.01620 -0.05912 0.06044  140 PRO A CB    
1134 C CG    . PRO A 141 ? 0.30206 0.27217 0.27284 -0.01493 -0.05683 0.06485  140 PRO A CG    
1135 C CD    . PRO A 141 ? 0.29312 0.25845 0.27999 -0.00326 -0.05759 0.06238  140 PRO A CD    
1136 N N     . PHE A 142 ? 0.24013 0.27131 0.23756 -0.00967 -0.07203 0.05615  141 PHE A N     
1137 C CA    . PHE A 142 ? 0.25343 0.30253 0.26092 -0.01314 -0.07081 0.04755  141 PHE A CA    
1138 C C     . PHE A 142 ? 0.24913 0.30124 0.24083 -0.02539 -0.06823 0.04186  141 PHE A C     
1139 O O     . PHE A 142 ? 0.29026 0.34335 0.26553 -0.03056 -0.07388 0.04672  141 PHE A O     
1140 C CB    . PHE A 142 ? 0.23548 0.30282 0.25518 -0.00829 -0.08154 0.05194  141 PHE A CB    
1141 C CG    . PHE A 142 ? 0.24218 0.32898 0.27039 -0.01508 -0.08189 0.04393  141 PHE A CG    
1142 C CD1   . PHE A 142 ? 0.24032 0.32948 0.28133 -0.01581 -0.07275 0.03519  141 PHE A CD1   
1143 C CD2   . PHE A 142 ? 0.30857 0.41048 0.33092 -0.02165 -0.09174 0.04540  141 PHE A CD2   
1144 C CE1   . PHE A 142 ? 0.20630 0.31071 0.25464 -0.02367 -0.07274 0.02816  141 PHE A CE1   
1145 C CE2   . PHE A 142 ? 0.26921 0.38752 0.29919 -0.02967 -0.09231 0.03719  141 PHE A CE2   
1146 C CZ    . PHE A 142 ? 0.24666 0.36577 0.29046 -0.03075 -0.08274 0.02885  141 PHE A CZ    
1147 N N     . ILE A 143 ? 0.23258 0.28548 0.22832 -0.02967 -0.05968 0.03163  142 ILE A N     
1148 C CA    . ILE A 143 ? 0.25231 0.30604 0.23447 -0.03991 -0.05581 0.02405  142 ILE A CA    
1149 C C     . ILE A 143 ? 0.23986 0.30501 0.23198 -0.04420 -0.05595 0.01561  142 ILE A C     
1150 O O     . ILE A 143 ? 0.21632 0.28213 0.22422 -0.04071 -0.05136 0.01246  142 ILE A O     
1151 C CB    . ILE A 143 ? 0.27828 0.31882 0.25519 -0.04121 -0.04453 0.01937  142 ILE A CB    
1152 C CG1   . ILE A 143 ? 0.31669 0.34604 0.28658 -0.03826 -0.04396 0.02773  142 ILE A CG1   
1153 C CG2   . ILE A 143 ? 0.31946 0.36039 0.28269 -0.04995 -0.03966 0.01090  142 ILE A CG2   
1154 C CD1   . ILE A 143 ? 0.37203 0.40187 0.32298 -0.04357 -0.04902 0.03442  142 ILE A CD1   
1155 N N     . GLU A 144 ? 0.24361 0.31681 0.22509 -0.05281 -0.06085 0.01178  143 GLU A N     
1156 C CA    . GLU A 144 ? 0.23717 0.31818 0.22482 -0.05998 -0.06070 0.00236  143 GLU A CA    
1157 C C     . GLU A 144 ? 0.25883 0.32670 0.23696 -0.06529 -0.05021 -0.00805 143 GLU A C     
1158 O O     . GLU A 144 ? 0.31493 0.37594 0.27481 -0.06830 -0.04721 -0.01010 143 GLU A O     
1159 C CB    . GLU A 144 ? 0.28636 0.38121 0.26474 -0.06761 -0.07202 0.00228  143 GLU A CB    
1160 C CG    . GLU A 144 ? 0.35565 0.46489 0.34238 -0.06160 -0.08417 0.01366  143 GLU A CG    
1161 C CD    . GLU A 144 ? 0.47704 0.60161 0.45385 -0.06980 -0.09659 0.01372  143 GLU A CD    
1162 O OE1   . GLU A 144 ? 0.42782 0.56239 0.41010 -0.07851 -0.09877 0.00516  143 GLU A OE1   
1163 O OE2   . GLU A 144 ? 0.48689 0.61284 0.44916 -0.06847 -0.10454 0.02252  143 GLU A OE2   
1164 N N     . THR A 145 ? 0.23530 0.29982 0.22561 -0.06623 -0.04431 -0.01435 144 THR A N     
1165 C CA    . THR A 145 ? 0.22443 0.27437 0.20767 -0.06879 -0.03436 -0.02322 144 THR A CA    
1166 C C     . THR A 145 ? 0.23137 0.28033 0.21905 -0.07674 -0.03365 -0.03229 144 THR A C     
1167 O O     . THR A 145 ? 0.22940 0.28980 0.23012 -0.07986 -0.03907 -0.03092 144 THR A O     
1168 C CB    . THR A 145 ? 0.20709 0.24650 0.19882 -0.06059 -0.02564 -0.02082 144 THR A CB    
1169 O OG1   . THR A 145 ? 0.20614 0.24905 0.21571 -0.05777 -0.02518 -0.01868 144 THR A OG1   
1170 C CG2   . THR A 145 ? 0.23396 0.27248 0.22209 -0.05387 -0.02647 -0.01197 144 THR A CG2   
1171 N N     . SER A 146 ? 0.25920 0.29406 0.23695 -0.07986 -0.02640 -0.04159 145 SER A N     
1172 C CA    . SER A 146 ? 0.23882 0.26469 0.22151 -0.08585 -0.02299 -0.05002 145 SER A CA    
1173 C C     . SER A 146 ? 0.25612 0.26361 0.23620 -0.08052 -0.01215 -0.05434 145 SER A C     
1174 O O     . SER A 146 ? 0.27687 0.27749 0.24287 -0.07981 -0.00791 -0.06016 145 SER A O     
1175 C CB    . SER A 146 ? 0.26666 0.29338 0.23716 -0.09758 -0.02805 -0.05984 145 SER A CB    
1176 O OG    . SER A 146 ? 0.30392 0.31497 0.27573 -0.10319 -0.02295 -0.06932 145 SER A OG    
1177 N N     . ALA A 147 ? 0.23604 0.23712 0.22964 -0.07620 -0.00759 -0.05101 146 ALA A N     
1178 C CA    . ALA A 147 ? 0.24989 0.23350 0.24225 -0.07125 0.00134  -0.05492 146 ALA A CA    
1179 C C     . ALA A 147 ? 0.29238 0.26104 0.27556 -0.07764 0.00418  -0.06703 146 ALA A C     
1180 O O     . ALA A 147 ? 0.33450 0.28969 0.31262 -0.07253 0.01130  -0.07235 146 ALA A O     
1181 C CB    . ALA A 147 ? 0.26007 0.23918 0.26663 -0.06662 0.00459  -0.04849 146 ALA A CB    
1182 N N     . LYS A 148 ? 0.28025 0.25112 0.26145 -0.08862 -0.00138 -0.07209 147 LYS A N     
1183 C CA    . LYS A 148 ? 0.30866 0.26137 0.28085 -0.09552 0.00133  -0.08465 147 LYS A CA    
1184 C C     . LYS A 148 ? 0.38367 0.33421 0.33641 -0.09605 0.00286  -0.09449 147 LYS A C     
1185 O O     . LYS A 148 ? 0.40602 0.33821 0.35049 -0.09417 0.00990  -0.10477 147 LYS A O     
1186 C CB    . LYS A 148 ? 0.33017 0.28623 0.30706 -0.10910 -0.00555 -0.08730 147 LYS A CB    
1187 C CG    . LYS A 148 ? 0.38358 0.32325 0.35012 -0.11422 -0.00531 -0.09759 147 LYS A CG    
1188 C CD    . LYS A 148 ? 0.36913 0.31460 0.34544 -0.12419 -0.01211 -0.09533 147 LYS A CD    
1189 C CE    . LYS A 148 ? 0.42841 0.35473 0.39533 -0.12955 -0.01193 -0.10545 147 LYS A CE    
1190 N NZ    . LYS A 148 ? 0.55588 0.48833 0.53229 -0.14101 -0.01904 -0.10410 147 LYS A NZ    
1191 N N     . THR A 149 ? 0.35910 0.32772 0.30354 -0.09880 -0.00362 -0.09180 148 THR A N     
1192 C CA    . THR A 149 ? 0.39495 0.36387 0.31816 -0.10081 -0.00230 -0.10035 148 THR A CA    
1193 C C     . THR A 149 ? 0.34630 0.32091 0.26615 -0.09063 0.00361  -0.09448 148 THR A C     
1194 O O     . THR A 149 ? 0.36788 0.34386 0.27002 -0.09149 0.00690  -0.10071 148 THR A O     
1195 C CB    . THR A 149 ? 0.38029 0.36592 0.29312 -0.11098 -0.01376 -0.10005 148 THR A CB    
1196 O OG1   . THR A 149 ? 0.32032 0.32478 0.24040 -0.10628 -0.01971 -0.08543 148 THR A OG1   
1197 C CG2   . THR A 149 ? 0.36570 0.35065 0.28666 -0.11905 -0.02061 -0.10201 148 THR A CG2   
1198 N N     . ARG A 150 ? 0.30016 0.27985 0.23562 -0.08249 0.00442  -0.08251 149 ARG A N     
1199 C CA    . ARG A 150 ? 0.32631 0.31240 0.26120 -0.07412 0.00901  -0.07542 149 ARG A CA    
1200 C C     . ARG A 150 ? 0.31411 0.31635 0.24068 -0.07706 0.00145  -0.06694 149 ARG A C     
1201 O O     . ARG A 150 ? 0.32932 0.33649 0.25577 -0.07192 0.00409  -0.05956 149 ARG A O     
1202 C CB    . ARG A 150 ? 0.38013 0.35780 0.30785 -0.06900 0.02008  -0.08395 149 ARG A CB    
1203 C CG    . ARG A 150 ? 0.48366 0.46391 0.42414 -0.05902 0.02533  -0.07564 149 ARG A CG    
1204 C CD    . ARG A 150 ? 0.51172 0.48467 0.45363 -0.05153 0.03629  -0.08302 149 ARG A CD    
1205 N NE    . ARG A 150 ? 0.44183 0.41972 0.39771 -0.04284 0.03977  -0.07474 149 ARG A NE    
1206 C CZ    . ARG A 150 ? 0.51914 0.51036 0.47523 -0.04209 0.03976  -0.06665 149 ARG A CZ    
1207 N NH1   . ARG A 150 ? 0.52472 0.52519 0.46688 -0.04871 0.03700  -0.06459 149 ARG A NH1   
1208 N NH2   . ARG A 150 ? 0.50207 0.49680 0.47158 -0.03535 0.04207  -0.06030 149 ARG A NH2   
1209 N N     . GLN A 151 ? 0.32188 0.33213 0.24332 -0.08495 -0.00835 -0.06670 150 GLN A N     
1210 C CA    . GLN A 151 ? 0.35323 0.37794 0.26880 -0.08619 -0.01699 -0.05647 150 GLN A CA    
1211 C C     . GLN A 151 ? 0.31706 0.34539 0.24763 -0.07769 -0.01778 -0.04331 150 GLN A C     
1212 O O     . GLN A 151 ? 0.28548 0.31343 0.23383 -0.07423 -0.01897 -0.04000 150 GLN A O     
1213 C CB    . GLN A 151 ? 0.35444 0.38935 0.27043 -0.09406 -0.02896 -0.05642 150 GLN A CB    
1214 C CG    . GLN A 151 ? 0.39902 0.44891 0.31522 -0.09229 -0.03937 -0.04295 150 GLN A CG    
1215 C CD    . GLN A 151 ? 0.48344 0.54757 0.40790 -0.09744 -0.05192 -0.04062 150 GLN A CD    
1216 O OE1   . GLN A 151 ? 0.47819 0.54207 0.40908 -0.10406 -0.05312 -0.04892 150 GLN A OE1   
1217 N NE2   . GLN A 151 ? 0.55406 0.63099 0.47921 -0.09454 -0.06171 -0.02882 150 GLN A NE2   
1218 N N     . GLY A 152 ? 0.30258 0.33392 0.22485 -0.07508 -0.01689 -0.03600 151 GLY A N     
1219 C CA    . GLY A 152 ? 0.27328 0.30650 0.20663 -0.06833 -0.01924 -0.02372 151 GLY A CA    
1220 C C     . GLY A 152 ? 0.25521 0.28069 0.20301 -0.06118 -0.01156 -0.02310 151 GLY A C     
1221 O O     . GLY A 152 ? 0.24869 0.27418 0.20502 -0.05600 -0.01354 -0.01433 151 GLY A O     
1222 N N     . VAL A 153 ? 0.24231 0.26033 0.19299 -0.06035 -0.00345 -0.03211 152 VAL A N     
1223 C CA    . VAL A 153 ? 0.27850 0.29023 0.24338 -0.05339 0.00210  -0.03066 152 VAL A CA    
1224 C C     . VAL A 153 ? 0.23126 0.24424 0.19515 -0.04989 0.00581  -0.02488 152 VAL A C     
1225 O O     . VAL A 153 ? 0.22856 0.24079 0.20168 -0.04556 0.00417  -0.01769 152 VAL A O     
1226 C CB    . VAL A 153 ? 0.25513 0.25746 0.22305 -0.05256 0.00903  -0.04051 152 VAL A CB    
1227 C CG1   . VAL A 153 ? 0.30246 0.29957 0.28282 -0.04485 0.01428  -0.03776 152 VAL A CG1   
1228 C CG2   . VAL A 153 ? 0.27061 0.26994 0.24234 -0.05707 0.00514  -0.04467 152 VAL A CG2   
1229 N N     . ASP A 154 ? 0.26050 0.27565 0.21322 -0.05226 0.01149  -0.02861 153 ASP A N     
1230 C CA    . ASP A 154 ? 0.23922 0.25795 0.19162 -0.05106 0.01506  -0.02250 153 ASP A CA    
1231 C C     . ASP A 154 ? 0.24261 0.26297 0.19187 -0.05280 0.00725  -0.01119 153 ASP A C     
1232 O O     . ASP A 154 ? 0.24738 0.26563 0.20406 -0.05014 0.00673  -0.00446 153 ASP A O     
1233 C CB    . ASP A 154 ? 0.29467 0.31886 0.23437 -0.05460 0.02272  -0.02759 153 ASP A CB    
1234 C CG    . ASP A 154 ? 0.41750 0.43953 0.36314 -0.05018 0.03198  -0.03820 153 ASP A CG    
1235 O OD1   . ASP A 154 ? 0.42416 0.43998 0.38401 -0.04435 0.03231  -0.03956 153 ASP A OD1   
1236 O OD2   . ASP A 154 ? 0.42412 0.45044 0.35923 -0.05219 0.03915  -0.04518 153 ASP A OD2   
1237 N N     . ASP A 155 ? 0.25038 0.27351 0.18898 -0.05697 0.00037  -0.00920 154 ASP A N     
1238 C CA    . ASP A 155 ? 0.27258 0.29618 0.20734 -0.05758 -0.00800 0.00217  154 ASP A CA    
1239 C C     . ASP A 155 ? 0.27518 0.29384 0.22613 -0.05086 -0.01207 0.00738  154 ASP A C     
1240 O O     . ASP A 155 ? 0.25604 0.27003 0.20788 -0.04916 -0.01439 0.01580  154 ASP A O     
1241 C CB    . ASP A 155 ? 0.30395 0.33317 0.22729 -0.06198 -0.01602 0.00231  154 ASP A CB    
1242 C CG    . ASP A 155 ? 0.42753 0.45742 0.34352 -0.06250 -0.02502 0.01495  154 ASP A CG    
1243 O OD1   . ASP A 155 ? 0.42303 0.44742 0.33730 -0.06191 -0.02329 0.02292  154 ASP A OD1   
1244 O OD2   . ASP A 155 ? 0.45643 0.49214 0.36864 -0.06374 -0.03432 0.01720  154 ASP A OD2   
1245 N N     . ALA A 156 ? 0.22627 0.24484 0.18926 -0.04743 -0.01226 0.00218  155 ALA A N     
1246 C CA    . ALA A 156 ? 0.22433 0.23976 0.20103 -0.04107 -0.01523 0.00631  155 ALA A CA    
1247 C C     . ALA A 156 ? 0.22988 0.23844 0.21156 -0.03787 -0.01036 0.00809  155 ALA A C     
1248 O O     . ALA A 156 ? 0.20780 0.21111 0.19215 -0.03472 -0.01359 0.01445  155 ALA A O     
1249 C CB    . ALA A 156 ? 0.22738 0.24530 0.21476 -0.03970 -0.01465 0.00024  155 ALA A CB    
1250 N N     . PHE A 157 ? 0.21630 0.22455 0.19944 -0.03851 -0.00304 0.00227  156 PHE A N     
1251 C CA    . PHE A 157 ? 0.20964 0.21417 0.19890 -0.03594 0.00049  0.00370  156 PHE A CA    
1252 C C     . PHE A 157 ? 0.18717 0.19129 0.16933 -0.03998 0.00050  0.00961  156 PHE A C     
1253 O O     . PHE A 157 ? 0.18142 0.18009 0.16730 -0.03892 -0.00106 0.01401  156 PHE A O     
1254 C CB    . PHE A 157 ? 0.18817 0.19417 0.18257 -0.03448 0.00745  -0.00327 156 PHE A CB    
1255 C CG    . PHE A 157 ? 0.18736 0.19013 0.18978 -0.03062 0.00761  -0.00696 156 PHE A CG    
1256 C CD1   . PHE A 157 ? 0.18689 0.18593 0.19751 -0.02606 0.00696  -0.00475 156 PHE A CD1   
1257 C CD2   . PHE A 157 ? 0.22144 0.22426 0.22195 -0.03254 0.00827  -0.01247 156 PHE A CD2   
1258 C CE1   . PHE A 157 ? 0.19455 0.19079 0.21114 -0.02338 0.00776  -0.00692 156 PHE A CE1   
1259 C CE2   . PHE A 157 ? 0.21149 0.21044 0.21945 -0.03048 0.00865  -0.01472 156 PHE A CE2   
1260 C CZ    . PHE A 157 ? 0.19917 0.19514 0.21507 -0.02579 0.00885  -0.01140 156 PHE A CZ    
1261 N N     . TYR A 158 ? 0.21935 0.22856 0.19009 -0.04551 0.00230  0.00972  157 TYR A N     
1262 C CA    . TYR A 158 ? 0.22032 0.22976 0.18326 -0.05100 0.00324  0.01638  157 TYR A CA    
1263 C C     . TYR A 158 ? 0.22008 0.22067 0.17882 -0.05107 -0.00498 0.02606  157 TYR A C     
1264 O O     . TYR A 158 ? 0.22275 0.21717 0.18059 -0.05384 -0.00556 0.03241  157 TYR A O     
1265 C CB    . TYR A 158 ? 0.26137 0.27902 0.21057 -0.05719 0.00776  0.01447  157 TYR A CB    
1266 C CG    . TYR A 158 ? 0.28061 0.30651 0.23344 -0.05665 0.01753  0.00489  157 TYR A CG    
1267 C CD1   . TYR A 158 ? 0.30915 0.33441 0.27693 -0.05048 0.02047  -0.00069 157 TYR A CD1   
1268 C CD2   . TYR A 158 ? 0.32555 0.35966 0.26606 -0.06172 0.02382  0.00169  157 TYR A CD2   
1269 C CE1   . TYR A 158 ? 0.28799 0.31996 0.26023 -0.04825 0.02904  -0.00896 157 TYR A CE1   
1270 C CE2   . TYR A 158 ? 0.31648 0.35809 0.26121 -0.05955 0.03364  -0.00808 157 TYR A CE2   
1271 C CZ    . TYR A 158 ? 0.32969 0.36961 0.29135 -0.05222 0.03573  -0.01301 157 TYR A CZ    
1272 O OH    . TYR A 158 ? 0.41470 0.46101 0.38188 -0.04832 0.04489  -0.02207 157 TYR A OH    
1273 N N     . THR A 159 ? 0.22597 0.22584 0.18245 -0.04829 -0.01167 0.02751  158 THR A N     
1274 C CA    . THR A 159 ? 0.21267 0.20394 0.16711 -0.04590 -0.02002 0.03685  158 THR A CA    
1275 C C     . THR A 159 ? 0.20779 0.18914 0.17415 -0.03988 -0.02089 0.03719  158 THR A C     
1276 O O     . THR A 159 ? 0.22891 0.19849 0.19281 -0.03984 -0.02434 0.04427  158 THR A O     
1277 C CB    . THR A 159 ? 0.22456 0.22134 0.17816 -0.04291 -0.02722 0.03738  158 THR A CB    
1278 O OG1   . THR A 159 ? 0.27292 0.27763 0.21155 -0.04980 -0.02736 0.03725  158 THR A OG1   
1279 C CG2   . THR A 159 ? 0.27549 0.26421 0.23021 -0.03764 -0.03622 0.04701  158 THR A CG2   
1280 N N     . LEU A 160 ? 0.20384 0.18830 0.18148 -0.03548 -0.01743 0.02946  159 LEU A N     
1281 C CA    . LEU A 160 ? 0.19582 0.17162 0.18204 -0.03050 -0.01753 0.02873  159 LEU A CA    
1282 C C     . LEU A 160 ? 0.20357 0.17336 0.18763 -0.03552 -0.01484 0.03056  159 LEU A C     
1283 O O     . LEU A 160 ? 0.20986 0.16720 0.19399 -0.03450 -0.01790 0.03391  159 LEU A O     
1284 C CB    . LEU A 160 ? 0.18336 0.16459 0.17944 -0.02618 -0.01389 0.02110  159 LEU A CB    
1285 C CG    . LEU A 160 ? 0.18200 0.15536 0.18443 -0.02119 -0.01373 0.01964  159 LEU A CG    
1286 C CD1   . LEU A 160 ? 0.20248 0.16704 0.20594 -0.01527 -0.01904 0.02337  159 LEU A CD1   
1287 C CD2   . LEU A 160 ? 0.18265 0.16192 0.19254 -0.01781 -0.00996 0.01358  159 LEU A CD2   
1288 N N     . VAL A 161 ? 0.18945 0.16813 0.17182 -0.04131 -0.00916 0.02823  160 VAL A N     
1289 C CA    . VAL A 161 ? 0.20627 0.18315 0.18839 -0.04756 -0.00675 0.03069  160 VAL A CA    
1290 C C     . VAL A 161 ? 0.24651 0.21285 0.21867 -0.05321 -0.01075 0.04014  160 VAL A C     
1291 O O     . VAL A 161 ? 0.25280 0.20838 0.22550 -0.05648 -0.01260 0.04347  160 VAL A O     
1292 C CB    . VAL A 161 ? 0.20927 0.20105 0.19317 -0.05180 0.00081  0.02658  160 VAL A CB    
1293 C CG1   . VAL A 161 ? 0.24938 0.24329 0.23376 -0.06005 0.00325  0.03055  160 VAL A CG1   
1294 C CG2   . VAL A 161 ? 0.23228 0.23017 0.22710 -0.04564 0.00394  0.01860  160 VAL A CG2   
1295 N N     . ARG A 162 ? 0.23231 0.20031 0.19406 -0.05507 -0.01271 0.04500  161 ARG A N     
1296 C CA    . ARG A 162 ? 0.24069 0.19652 0.19149 -0.05997 -0.01738 0.05590  161 ARG A CA    
1297 C C     . ARG A 162 ? 0.27111 0.20832 0.22502 -0.05332 -0.02461 0.05936  161 ARG A C     
1298 O O     . ARG A 162 ? 0.31412 0.23560 0.26353 -0.05765 -0.02718 0.06613  161 ARG A O     
1299 C CB    . ARG A 162 ? 0.28537 0.24670 0.22305 -0.06207 -0.01968 0.06097  161 ARG A CB    
1300 C CG    . ARG A 162 ? 0.27743 0.25502 0.20837 -0.06947 -0.01163 0.05749  161 ARG A CG    
1301 C CD    . ARG A 162 ? 0.35158 0.33293 0.26533 -0.07328 -0.01440 0.06318  161 ARG A CD    
1302 N NE    . ARG A 162 ? 0.34711 0.34438 0.25444 -0.07884 -0.00548 0.05676  161 ARG A NE    
1303 C CZ    . ARG A 162 ? 0.33068 0.33798 0.23787 -0.07569 -0.00351 0.04709  161 ARG A CZ    
1304 N NH1   . ARG A 162 ? 0.32434 0.32961 0.23606 -0.06891 -0.01056 0.04438  161 ARG A NH1   
1305 N NH2   . ARG A 162 ? 0.30199 0.32163 0.20502 -0.07961 0.00605  0.03963  161 ARG A NH2   
1306 N N     . GLU A 163 ? 0.26640 0.20462 0.22829 -0.04304 -0.02738 0.05443  162 GLU A N     
1307 C CA    . GLU A 163 ? 0.28282 0.20513 0.24923 -0.03478 -0.03272 0.05571  162 GLU A CA    
1308 C C     . GLU A 163 ? 0.27810 0.18915 0.24857 -0.03634 -0.03062 0.05169  162 GLU A C     
1309 O O     . GLU A 163 ? 0.32071 0.21196 0.28880 -0.03464 -0.03472 0.05513  162 GLU A O     
1310 C CB    . GLU A 163 ? 0.28123 0.21191 0.25715 -0.02416 -0.03426 0.05039  162 GLU A CB    
1311 C CG    . GLU A 163 ? 0.30590 0.24600 0.27917 -0.02173 -0.03922 0.05485  162 GLU A CG    
1312 C CD    . GLU A 163 ? 0.39473 0.32150 0.36079 -0.01968 -0.04700 0.06590  162 GLU A CD    
1313 O OE1   . GLU A 163 ? 0.39932 0.31416 0.37176 -0.01036 -0.05085 0.06711  162 GLU A OE1   
1314 O OE2   . GLU A 163 ? 0.39835 0.32612 0.35174 -0.02696 -0.04901 0.07343  162 GLU A OE2   
1315 N N     . ILE A 164 ? 0.25059 0.17302 0.22675 -0.03945 -0.02494 0.04441  163 ILE A N     
1316 C CA    . ILE A 164 ? 0.28586 0.20029 0.26492 -0.04268 -0.02402 0.04085  163 ILE A CA    
1317 C C     . ILE A 164 ? 0.35243 0.25806 0.32494 -0.05424 -0.02469 0.04761  163 ILE A C     
1318 O O     . ILE A 164 ? 0.36560 0.25271 0.33596 -0.05655 -0.02801 0.04860  163 ILE A O     
1319 C CB    . ILE A 164 ? 0.24629 0.17691 0.23335 -0.04291 -0.01888 0.03298  163 ILE A CB    
1320 C CG1   . ILE A 164 ? 0.21628 0.15226 0.20912 -0.03271 -0.01812 0.02695  163 ILE A CG1   
1321 C CG2   . ILE A 164 ? 0.28485 0.20948 0.27404 -0.04805 -0.01939 0.03024  163 ILE A CG2   
1322 C CD1   . ILE A 164 ? 0.23506 0.18635 0.23425 -0.03287 -0.01325 0.02133  163 ILE A CD1   
1323 N N     . ARG A 165 ? 0.30996 0.22893 0.27907 -0.06242 -0.02084 0.05162  164 ARG A N     
1324 C CA    . ARG A 165 ? 0.35258 0.26673 0.31575 -0.07517 -0.02007 0.05899  164 ARG A CA    
1325 C C     . ARG A 165 ? 0.38440 0.27374 0.33716 -0.07579 -0.02661 0.06859  164 ARG A C     
1326 O O     . ARG A 165 ? 0.47693 0.35044 0.42673 -0.08367 -0.02849 0.07254  164 ARG A O     
1327 C CB    . ARG A 165 ? 0.30402 0.23905 0.26409 -0.08225 -0.01348 0.06125  164 ARG A CB    
1328 C CG    . ARG A 165 ? 0.38568 0.34436 0.35688 -0.08169 -0.00629 0.05228  164 ARG A CG    
1329 C CD    . ARG A 165 ? 0.33502 0.31303 0.30173 -0.08743 0.00131  0.05348  164 ARG A CD    
1330 N NE    . ARG A 165 ? 0.32010 0.31930 0.29834 -0.08553 0.00853  0.04498  164 ARG A NE    
1331 C CZ    . ARG A 165 ? 0.31124 0.32725 0.28714 -0.08668 0.01603  0.04231  164 ARG A CZ    
1332 N NH1   . ARG A 165 ? 0.29916 0.31462 0.25992 -0.09040 0.01714  0.04704  164 ARG A NH1   
1333 N NH2   . ARG A 165 ? 0.28075 0.31396 0.26906 -0.08311 0.02232  0.03435  164 ARG A NH2   
1334 N N     . LYS A 166 ? 0.40515 0.29046 0.35327 -0.06693 -0.03072 0.07217  165 LYS A N     
1335 C CA    . LYS A 166 ? 0.50606 0.36730 0.44565 -0.06454 -0.03797 0.08189  165 LYS A CA    
1336 C C     . LYS A 166 ? 0.49817 0.33701 0.44253 -0.05783 -0.04181 0.07746  165 LYS A C     
1337 O O     . LYS A 166 ? 0.59579 0.41742 0.53645 -0.05950 -0.04352 0.08013  165 LYS A O     
1338 C CB    . LYS A 166 ? 0.56504 0.43176 0.50153 -0.05508 -0.04233 0.08589  165 LYS A CB    
1339 C CG    . LYS A 166 ? 0.58820 0.46724 0.51259 -0.06298 -0.04129 0.09399  165 LYS A CG    
1340 C CD    . LYS A 166 ? 0.62948 0.52311 0.55417 -0.05425 -0.04455 0.09272  165 LYS A CD    
1341 C CE    . LYS A 166 ? 0.66673 0.54568 0.59240 -0.04273 -0.05431 0.09917  165 LYS A CE    
1342 N NZ    . LYS A 166 ? 0.65136 0.54732 0.57842 -0.03576 -0.05870 0.09888  165 LYS A NZ    
1343 N N     . HIS A 167 ? 0.48429 0.33062 0.43874 -0.04758 -0.04046 0.06659  166 HIS A N     
1344 C CA    . HIS A 167 ? 0.50581 0.33292 0.46358 -0.03972 -0.04301 0.06049  166 HIS A CA    
1345 C C     . HIS A 167 ? 0.46207 0.27651 0.41746 -0.04974 -0.04214 0.05771  166 HIS A C     
1346 O O     . HIS A 167 ? 0.48659 0.28121 0.43977 -0.04620 -0.04418 0.05591  166 HIS A O     
1347 C CB    . HIS A 167 ? 0.41233 0.25508 0.38001 -0.03056 -0.03946 0.04900  166 HIS A CB    
1348 C CG    . HIS A 167 ? 0.46065 0.28775 0.42975 -0.02574 -0.03984 0.04039  166 HIS A CG    
1349 N ND1   . HIS A 167 ? 0.61153 0.41918 0.58019 -0.01446 -0.04311 0.03930  166 HIS A ND1   
1350 C CD2   . HIS A 167 ? 0.43250 0.26109 0.40272 -0.03029 -0.03746 0.03198  166 HIS A CD2   
1351 C CE1   . HIS A 167 ? 0.58684 0.38365 0.55482 -0.01262 -0.04189 0.02960  166 HIS A CE1   
1352 N NE2   . HIS A 167 ? 0.57885 0.38841 0.54717 -0.02256 -0.03902 0.02531  166 HIS A NE2   
1353 N N     . LYS A 168 ? 0.42409 0.25408 0.38201 -0.06096 -0.03820 0.05555  167 LYS A N     
1354 C CA    . LYS A 168 ? 0.46065 0.28692 0.41902 -0.07095 -0.03710 0.05236  167 LYS A CA    
1355 C C     . LYS A 168 ? 0.56341 0.37896 0.51499 -0.07847 -0.03778 0.06116  167 LYS A C     
1356 O O     . LYS A 168 ? 0.53621 0.34725 0.48178 -0.07544 -0.03929 0.06981  167 LYS A O     
1357 C CB    . LYS A 168 ? 0.43042 0.28108 0.39581 -0.08033 -0.03278 0.04928  167 LYS A CB    
1358 C CG    . LYS A 168 ? 0.42384 0.29015 0.39720 -0.07315 -0.03089 0.04010  167 LYS A CG    
1359 C CD    . LYS A 168 ? 0.47969 0.37286 0.46082 -0.08139 -0.02593 0.03966  167 LYS A CD    
1360 C CE    . LYS A 168 ? 0.46240 0.37318 0.45270 -0.07648 -0.02401 0.03098  167 LYS A CE    
1361 N NZ    . LYS A 168 ? 0.41745 0.35075 0.41649 -0.08628 -0.02041 0.03184  167 LYS A NZ    
1362 N N     . ASN B 4   ? 0.42097 0.34598 0.40196 0.01213  0.16467  0.07933  3   ASN D N     
1363 C CA    . ASN B 4   ? 0.37500 0.30880 0.36634 0.00955  0.15172  0.07365  3   ASN D CA    
1364 C C     . ASN B 4   ? 0.37079 0.28759 0.35874 0.00860  0.14830  0.07702  3   ASN D C     
1365 O O     . ASN B 4   ? 0.42936 0.32875 0.39212 0.01874  0.14838  0.08557  3   ASN D O     
1366 C CB    . ASN B 4   ? 0.35062 0.29119 0.32259 0.02051  0.13961  0.07219  3   ASN D CB    
1367 C CG    . ASN B 4   ? 0.34185 0.30230 0.32460 0.02048  0.13849  0.06424  3   ASN D CG    
1368 O OD1   . ASN B 4   ? 0.35986 0.33368 0.36908 0.01200  0.14665  0.06041  3   ASN D OD1   
1369 N ND2   . ASN B 4   ? 0.36783 0.33051 0.33112 0.03012  0.12846  0.06127  3   ASN D ND2   
1370 N N     . PRO B 5   ? 0.32386 0.24612 0.33664 -0.00254 0.14496  0.06968  4   PRO D N     
1371 C CA    . PRO B 5   ? 0.34981 0.25510 0.35984 -0.00310 0.14211  0.07135  4   PRO D CA    
1372 C C     . PRO B 5   ? 0.32146 0.22488 0.31477 0.00740  0.12857  0.07379  4   PRO D C     
1373 O O     . PRO B 5   ? 0.31574 0.23592 0.30642 0.01200  0.11537  0.06816  4   PRO D O     
1374 C CB    . PRO B 5   ? 0.38978 0.30493 0.43049 -0.01822 0.14043  0.05984  4   PRO D CB    
1375 C CG    . PRO B 5   ? 0.40621 0.34815 0.46376 -0.02197 0.13553  0.05247  4   PRO D CG    
1376 C CD    . PRO B 5   ? 0.31871 0.26356 0.36309 -0.01437 0.14280  0.05851  4   PRO D CD    
1377 N N     . THR B 6   ? 0.35136 0.23675 0.33515 0.01204  0.12820  0.07905  5   THR D N     
1378 C CA    . THR B 6   ? 0.31302 0.19901 0.28524 0.02227  0.11364  0.07978  5   THR D CA    
1379 C C     . THR B 6   ? 0.31410 0.19423 0.30144 0.01601  0.11106  0.07417  5   THR D C     
1380 O O     . THR B 6   ? 0.34966 0.21359 0.34146 0.01129  0.12142  0.07538  5   THR D O     
1381 C CB    . THR B 6   ? 0.40790 0.27883 0.35265 0.03740  0.11530  0.09217  5   THR D CB    
1382 O OG1   . THR B 6   ? 0.44947 0.32468 0.37587 0.04415  0.11719  0.09639  5   THR D OG1   
1383 C CG2   . THR B 6   ? 0.42707 0.30172 0.36446 0.04784  0.10025  0.09288  5   THR D CG2   
1384 N N     . VAL B 7   ? 0.30529 0.19969 0.29950 0.01656  0.09603  0.06578  6   VAL D N     
1385 C CA    . VAL B 7   ? 0.31213 0.19972 0.31650 0.01262  0.09403  0.06065  6   VAL D CA    
1386 C C     . VAL B 7   ? 0.31468 0.20450 0.30940 0.02478  0.08294  0.06325  6   VAL D C     
1387 O O     . VAL B 7   ? 0.30925 0.21116 0.29432 0.03294  0.07382  0.06529  6   VAL D O     
1388 C CB    . VAL B 7   ? 0.32656 0.22960 0.35133 0.00008  0.08841  0.04697  6   VAL D CB    
1389 C CG1   . VAL B 7   ? 0.35177 0.25575 0.39035 -0.01220 0.09942  0.04397  6   VAL D CG1   
1390 C CG2   . VAL B 7   ? 0.31978 0.24363 0.34441 0.00341  0.07534  0.04246  6   VAL D CG2   
1391 N N     . PHE B 8   ? 0.32436 0.20241 0.32256 0.02588  0.08435  0.06255  7   PHE D N     
1392 C CA    . PHE B 8   ? 0.30994 0.19270 0.30375 0.03716  0.07490  0.06447  7   PHE D CA    
1393 C C     . PHE B 8   ? 0.28579 0.17313 0.29274 0.03159  0.07038  0.05423  7   PHE D C     
1394 O O     . PHE B 8   ? 0.29544 0.17307 0.31052 0.02162  0.07687  0.04778  7   PHE D O     
1395 C CB    . PHE B 8   ? 0.35629 0.21918 0.33716 0.05018  0.08176  0.07687  7   PHE D CB    
1396 C CG    . PHE B 8   ? 0.34973 0.19539 0.33621 0.04514  0.09135  0.07344  7   PHE D CG    
1397 C CD1   . PHE B 8   ? 0.35877 0.18984 0.34487 0.03708  0.10391  0.07364  7   PHE D CD1   
1398 C CD2   . PHE B 8   ? 0.34085 0.18553 0.33377 0.04787  0.08834  0.06886  7   PHE D CD2   
1399 C CE1   . PHE B 8   ? 0.37570 0.19058 0.36664 0.03201  0.11240  0.06929  7   PHE D CE1   
1400 C CE2   . PHE B 8   ? 0.36034 0.18822 0.35623 0.04339  0.09732  0.06481  7   PHE D CE2   
1401 C CZ    . PHE B 8   ? 0.36777 0.18064 0.36256 0.03527  0.10877  0.06473  7   PHE D CZ    
1402 N N     . PHE B 9   ? 0.28445 0.18642 0.29288 0.03806  0.05967  0.05250  8   PHE D N     
1403 C CA    . PHE B 9   ? 0.26179 0.16581 0.27882 0.03729  0.05707  0.04591  8   PHE D CA    
1404 C C     . PHE B 9   ? 0.26530 0.16708 0.27968 0.05131  0.05607  0.05310  8   PHE D C     
1405 O O     . PHE B 9   ? 0.27174 0.18647 0.28219 0.06013  0.04839  0.05837  8   PHE D O     
1406 C CB    . PHE B 9   ? 0.25081 0.17625 0.27434 0.03345  0.04645  0.03840  8   PHE D CB    
1407 C CG    . PHE B 9   ? 0.22583 0.15702 0.25376 0.02190  0.04539  0.03052  8   PHE D CG    
1408 C CD1   . PHE B 9   ? 0.24065 0.16219 0.27066 0.01357  0.05270  0.02819  8   PHE D CD1   
1409 C CD2   . PHE B 9   ? 0.24118 0.18871 0.27240 0.01978  0.03692  0.02551  8   PHE D CD2   
1410 C CE1   . PHE B 9   ? 0.20328 0.13559 0.24008 0.00410  0.04970  0.02041  8   PHE D CE1   
1411 C CE2   . PHE B 9   ? 0.24109 0.19545 0.27587 0.01179  0.03491  0.01925  8   PHE D CE2   
1412 C CZ    . PHE B 9   ? 0.21311 0.16198 0.25127 0.00453  0.04037  0.01659  8   PHE D CZ    
1413 N N     . ASP B 10  ? 0.26353 0.15026 0.28060 0.05383  0.06324  0.05244  9   ASP D N     
1414 C CA    . ASP B 10  ? 0.26077 0.14995 0.28018 0.06755  0.06177  0.05732  9   ASP D CA    
1415 C C     . ASP B 10  ? 0.26596 0.17060 0.29679 0.06391  0.05673  0.04808  9   ASP D C     
1416 O O     . ASP B 10  ? 0.28066 0.17588 0.31348 0.05625  0.06202  0.04009  9   ASP D O     
1417 C CB    . ASP B 10  ? 0.29594 0.16529 0.30976 0.07055  0.07157  0.05983  9   ASP D CB    
1418 C CG    . ASP B 10  ? 0.37059 0.23001 0.37179 0.07499  0.07552  0.06938  9   ASP D CG    
1419 O OD1   . ASP B 10  ? 0.36806 0.24034 0.36344 0.08300  0.06791  0.07621  9   ASP D OD1   
1420 O OD2   . ASP B 10  ? 0.43489 0.27381 0.43123 0.07050  0.08639  0.06965  9   ASP D OD2   
1421 N N     . ILE B 11  ? 0.23694 0.16507 0.27429 0.06816  0.04673  0.04845  10  ILE D N     
1422 C CA    . ILE B 11  ? 0.21573 0.15923 0.26393 0.06390  0.04303  0.04083  10  ILE D CA    
1423 C C     . ILE B 11  ? 0.20268 0.14773 0.26002 0.07419  0.04704  0.04247  10  ILE D C     
1424 O O     . ILE B 11  ? 0.23697 0.18606 0.29681 0.08695  0.04552  0.05023  10  ILE D O     
1425 C CB    . ILE B 11  ? 0.19957 0.16658 0.25261 0.06205  0.03175  0.03974  10  ILE D CB    
1426 C CG1   . ILE B 11  ? 0.22701 0.19258 0.27069 0.05398  0.02856  0.03853  10  ILE D CG1   
1427 C CG2   . ILE B 11  ? 0.21500 0.19570 0.27946 0.05707  0.03000  0.03295  10  ILE D CG2   
1428 C CD1   . ILE B 11  ? 0.24761 0.20542 0.28954 0.04270  0.03237  0.03163  10  ILE D CD1   
1429 N N     . ALA B 12  ? 0.22174 0.16490 0.28364 0.06983  0.05213  0.03534  11  ALA D N     
1430 C CA    . ALA B 12  ? 0.19693 0.14257 0.26861 0.07919  0.05781  0.03583  11  ALA D CA    
1431 C C     . ALA B 12  ? 0.20023 0.16482 0.28293 0.07447  0.05598  0.03017  11  ALA D C     
1432 O O     . ALA B 12  ? 0.20269 0.16919 0.28063 0.06328  0.05348  0.02460  11  ALA D O     
1433 C CB    . ALA B 12  ? 0.24366 0.16435 0.30573 0.07788  0.06872  0.03197  11  ALA D CB    
1434 N N     . VAL B 13  ? 0.20059 0.17950 0.29883 0.08382  0.05791  0.03237  12  VAL D N     
1435 C CA    . VAL B 13  ? 0.18396 0.18100 0.29610 0.08046  0.05930  0.02820  12  VAL D CA    
1436 C C     . VAL B 13  ? 0.21476 0.20185 0.32573 0.08494  0.07051  0.02591  12  VAL D C     
1437 O O     . VAL B 13  ? 0.21831 0.20771 0.33387 0.09421  0.07113  0.02957  12  VAL D O     
1438 C CB    . VAL B 13  ? 0.19002 0.21712 0.32324 0.08510  0.05041  0.03141  12  VAL D CB    
1439 C CG1   . VAL B 13  ? 0.24842 0.29372 0.40005 0.08160  0.05512  0.02736  12  VAL D CG1   
1440 C CG2   . VAL B 13  ? 0.22293 0.25754 0.35105 0.07823  0.03810  0.03152  12  VAL D CG2   
1441 N N     . ASP B 14  ? 0.22364 0.19938 0.32600 0.07856  0.07883  0.01955  13  ASP D N     
1442 C CA    . ASP B 14  ? 0.22579 0.18825 0.32102 0.08152  0.08953  0.01605  13  ASP D CA    
1443 C C     . ASP B 14  ? 0.24987 0.19321 0.33562 0.08747  0.09144  0.01818  13  ASP D C     
1444 O O     . ASP B 14  ? 0.27810 0.21872 0.36652 0.09511  0.09728  0.01923  13  ASP D O     
1445 C CB    . ASP B 14  ? 0.28855 0.27106 0.40126 0.08581  0.09390  0.01693  13  ASP D CB    
1446 C CG    . ASP B 14  ? 0.30646 0.29877 0.42271 0.07781  0.09752  0.01366  13  ASP D CG    
1447 O OD1   . ASP B 14  ? 0.28945 0.26950 0.39027 0.07051  0.09868  0.00976  13  ASP D OD1   
1448 O OD2   . ASP B 14  ? 0.33521 0.34751 0.46974 0.07895  0.09992  0.01495  13  ASP D OD2   
1449 N N     . GLY B 15  ? 0.28021 0.20970 0.35525 0.08366  0.08739  0.01903  14  GLY D N     
1450 C CA    . GLY B 15  ? 0.26148 0.17008 0.32636 0.08674  0.09049  0.02118  14  GLY D CA    
1451 C C     . GLY B 15  ? 0.29267 0.20910 0.36416 0.09706  0.08544  0.03110  14  GLY D C     
1452 O O     . GLY B 15  ? 0.33054 0.22841 0.39225 0.09946  0.08843  0.03448  14  GLY D O     
1453 N N     . GLU B 16  ? 0.23842 0.18171 0.32572 0.10296  0.07795  0.03536  15  GLU D N     
1454 C CA    . GLU B 16  ? 0.25049 0.20358 0.34262 0.11384  0.07121  0.04388  15  GLU D CA    
1455 C C     . GLU B 16  ? 0.23569 0.19170 0.32180 0.11084  0.06199  0.04796  15  GLU D C     
1456 O O     . GLU B 16  ? 0.21449 0.18363 0.30563 0.10367  0.05630  0.04503  15  GLU D O     
1457 C CB    . GLU B 16  ? 0.24091 0.22488 0.35452 0.12085  0.06569  0.04470  15  GLU D CB    
1458 C CG    . GLU B 16  ? 0.28093 0.26373 0.40120 0.12889  0.07397  0.04403  15  GLU D CG    
1459 C CD    . GLU B 16  ? 0.32656 0.28981 0.43634 0.13955  0.07789  0.05021  15  GLU D CD    
1460 O OE1   . GLU B 16  ? 0.32797 0.28917 0.43138 0.14494  0.07138  0.05728  15  GLU D OE1   
1461 O OE2   . GLU B 16  ? 0.35510 0.30317 0.46139 0.14241  0.08857  0.04800  15  GLU D OE2   
1462 N N     . PRO B 17  ? 0.25286 0.19679 0.32770 0.11645  0.06103  0.05503  16  PRO D N     
1463 C CA    . PRO B 17  ? 0.28098 0.22615 0.34727 0.11400  0.05366  0.05926  16  PRO D CA    
1464 C C     . PRO B 17  ? 0.25533 0.23160 0.33399 0.11733  0.04037  0.06015  16  PRO D C     
1465 O O     . PRO B 17  ? 0.28545 0.28052 0.37588 0.12680  0.03481  0.06211  16  PRO D O     
1466 C CB    . PRO B 17  ? 0.31739 0.24536 0.37012 0.12232  0.05696  0.06778  16  PRO D CB    
1467 C CG    . PRO B 17  ? 0.35334 0.26312 0.40491 0.12473  0.06832  0.06616  16  PRO D CG    
1468 C CD    . PRO B 17  ? 0.29211 0.21683 0.35920 0.12461  0.06894  0.05938  16  PRO D CD    
1469 N N     . LEU B 18  ? 0.25534 0.23752 0.33245 0.10905  0.03519  0.05780  17  LEU D N     
1470 C CA    . LEU B 18  ? 0.24664 0.25616 0.33308 0.10983  0.02229  0.05741  17  LEU D CA    
1471 C C     . LEU B 18  ? 0.26110 0.26728 0.33092 0.11379  0.01549  0.06370  17  LEU D C     
1472 O O     . LEU B 18  ? 0.29727 0.32056 0.36861 0.12203  0.00520  0.06656  17  LEU D O     
1473 C CB    . LEU B 18  ? 0.25058 0.26820 0.34460 0.09715  0.02143  0.04995  17  LEU D CB    
1474 C CG    . LEU B 18  ? 0.23195 0.27610 0.33503 0.09230  0.00858  0.04579  17  LEU D CG    
1475 C CD1   . LEU B 18  ? 0.25934 0.33070 0.38642 0.10014  0.00403  0.04538  17  LEU D CD1   
1476 C CD2   . LEU B 18  ? 0.25186 0.29467 0.35414 0.07606  0.00933  0.03742  17  LEU D CD2   
1477 N N     . GLY B 19  ? 0.25199 0.23580 0.30552 0.10808  0.02181  0.06558  18  GLY D N     
1478 C CA    . GLY B 19  ? 0.30997 0.28797 0.34536 0.11157  0.01824  0.07204  18  GLY D CA    
1479 C C     . GLY B 19  ? 0.27948 0.23714 0.30325 0.10176  0.02614  0.07174  18  GLY D C     
1480 O O     . GLY B 19  ? 0.28631 0.23696 0.31619 0.09073  0.03194  0.06475  18  GLY D O     
1481 N N     . ARG B 20  ? 0.26985 0.21991 0.27610 0.10411  0.02588  0.07783  19  ARG D N     
1482 C CA    . ARG B 20  ? 0.27092 0.20284 0.26713 0.09489  0.03439  0.07827  19  ARG D CA    
1483 C C     . ARG B 20  ? 0.28824 0.23558 0.28020 0.08779  0.02577  0.07317  19  ARG D C     
1484 O O     . ARG B 20  ? 0.31595 0.27683 0.30030 0.09558  0.01603  0.07572  19  ARG D O     
1485 C CB    . ARG B 20  ? 0.31358 0.22490 0.29296 0.09836  0.04374  0.08640  19  ARG D CB    
1486 C CG    . ARG B 20  ? 0.31234 0.20887 0.28431 0.08776  0.05293  0.08645  19  ARG D CG    
1487 C CD    . ARG B 20  ? 0.36925 0.24421 0.32842 0.08925  0.06535  0.09349  19  ARG D CD    
1488 N NE    . ARG B 20  ? 0.36206 0.22124 0.32883 0.08618  0.07457  0.09106  19  ARG D NE    
1489 C CZ    . ARG B 20  ? 0.39194 0.22958 0.35302 0.08344  0.08773  0.09406  19  ARG D CZ    
1490 N NH1   . ARG B 20  ? 0.41970 0.24873 0.36767 0.08441  0.09429  0.10081  19  ARG D NH1   
1491 N NH2   . ARG B 20  ? 0.41598 0.24010 0.38442 0.07965  0.09511  0.08970  19  ARG D NH2   
1492 N N     . VAL B 21  ? 0.25554 0.20055 0.25177 0.07371  0.02922  0.06551  20  VAL D N     
1493 C CA    . VAL B 21  ? 0.25693 0.21113 0.24802 0.06705  0.02452  0.06112  20  VAL D CA    
1494 C C     . VAL B 21  ? 0.28078 0.21815 0.26331 0.06162  0.03587  0.06432  20  VAL D C     
1495 O O     . VAL B 21  ? 0.29713 0.22268 0.28705 0.05403  0.04462  0.06210  20  VAL D O     
1496 C CB    . VAL B 21  ? 0.25136 0.21889 0.25619 0.05648  0.01923  0.05004  20  VAL D CB    
1497 C CG1   . VAL B 21  ? 0.27308 0.24826 0.27187 0.05159  0.01491  0.04586  20  VAL D CG1   
1498 C CG2   . VAL B 21  ? 0.24777 0.23061 0.26426 0.06021  0.01119  0.04705  20  VAL D CG2   
1499 N N     . SER B 22  ? 0.27515 0.21229 0.24279 0.06465  0.03609  0.06845  21  SER D N     
1500 C CA    . SER B 22  ? 0.28313 0.20742 0.24608 0.05816  0.04816  0.07078  21  SER D CA    
1501 C C     . SER B 22  ? 0.29644 0.23344 0.25931 0.05197  0.04445  0.06400  21  SER D C     
1502 O O     . SER B 22  ? 0.26286 0.21325 0.22100 0.05560  0.03362  0.06032  21  SER D O     
1503 C CB    . SER B 22  ? 0.34430 0.25131 0.28759 0.06756  0.05750  0.08368  21  SER D CB    
1504 O OG    . SER B 22  ? 0.37991 0.29528 0.30475 0.07717  0.04995  0.08704  21  SER D OG    
1505 N N     . PHE B 23  ? 0.25978 0.19294 0.22965 0.04241  0.05363  0.06154  22  PHE D N     
1506 C CA    . PHE B 23  ? 0.24508 0.19024 0.21821 0.03703  0.05155  0.05492  22  PHE D CA    
1507 C C     . PHE B 23  ? 0.27408 0.21197 0.24191 0.03488  0.06468  0.05959  22  PHE D C     
1508 O O     . PHE B 23  ? 0.30890 0.23507 0.28279 0.02993  0.07620  0.06325  22  PHE D O     
1509 C CB    . PHE B 23  ? 0.23973 0.19322 0.23299 0.02672  0.04943  0.04562  22  PHE D CB    
1510 C CG    . PHE B 23  ? 0.20916 0.16751 0.20998 0.02681  0.04022  0.04100  22  PHE D CG    
1511 C CD1   . PHE B 23  ? 0.22488 0.19507 0.22576 0.02871  0.02976  0.03617  22  PHE D CD1   
1512 C CD2   . PHE B 23  ? 0.24137 0.19115 0.24915 0.02464  0.04351  0.04111  22  PHE D CD2   
1513 C CE1   . PHE B 23  ? 0.22965 0.20431 0.23846 0.02828  0.02360  0.03254  22  PHE D CE1   
1514 C CE2   . PHE B 23  ? 0.25972 0.21406 0.27382 0.02519  0.03694  0.03695  22  PHE D CE2   
1515 C CZ    . PHE B 23  ? 0.23251 0.19989 0.24750 0.02698  0.02745  0.03324  22  PHE D CZ    
1516 N N     . GLU B 24  ? 0.27596 0.22027 0.23337 0.03794  0.06401  0.05868  23  GLU D N     
1517 C CA    . GLU B 24  ? 0.27477 0.21707 0.23232 0.03441  0.07720  0.06080  23  GLU D CA    
1518 C C     . GLU B 24  ? 0.25059 0.20748 0.23125 0.02495  0.07554  0.05109  23  GLU D C     
1519 O O     . GLU B 24  ? 0.25466 0.22245 0.23861 0.02563  0.06442  0.04397  23  GLU D O     
1520 C CB    . GLU B 24  ? 0.33826 0.28112 0.27314 0.04299  0.07748  0.06300  23  GLU D CB    
1521 C CG    . GLU B 24  ? 0.30190 0.24557 0.23875 0.03978  0.09206  0.06406  23  GLU D CG    
1522 C CD    . GLU B 24  ? 0.46399 0.40602 0.37521 0.04894  0.09415  0.06569  23  GLU D CD    
1523 O OE1   . GLU B 24  ? 0.45567 0.39684 0.34711 0.05719  0.08256  0.06485  23  GLU D OE1   
1524 O OE2   . GLU B 24  ? 0.44951 0.39167 0.36076 0.04773  0.10792  0.06733  23  GLU D OE2   
1525 N N     . LEU B 25  ? 0.24350 0.20090 0.24052 0.01634  0.08652  0.05080  24  LEU D N     
1526 C CA    . LEU B 25  ? 0.24440 0.21882 0.26420 0.00864  0.08426  0.04187  24  LEU D CA    
1527 C C     . LEU B 25  ? 0.22099 0.20308 0.24359 0.00887  0.09461  0.04264  24  LEU D C     
1528 O O     . LEU B 25  ? 0.25725 0.23114 0.27790 0.00698  0.10959  0.04916  24  LEU D O     
1529 C CB    . LEU B 25  ? 0.23830 0.21291 0.27909 -0.00239 0.08742  0.03820  24  LEU D CB    
1530 C CG    . LEU B 25  ? 0.24031 0.20436 0.27854 -0.00286 0.08089  0.03759  24  LEU D CG    
1531 C CD1   . LEU B 25  ? 0.24673 0.21000 0.30476 -0.01488 0.08482  0.03165  24  LEU D CD1   
1532 C CD2   . LEU B 25  ? 0.24372 0.21606 0.27774 0.00229  0.06545  0.03278  24  LEU D CD2   
1533 N N     . PHE B 26  ? 0.22094 0.21740 0.24811 0.01164  0.08822  0.03650  25  PHE D N     
1534 C CA    . PHE B 26  ? 0.25215 0.25596 0.27981 0.01465  0.09782  0.03689  25  PHE D CA    
1535 C C     . PHE B 26  ? 0.24471 0.26410 0.30204 0.00578  0.10654  0.03395  25  PHE D C     
1536 O O     . PHE B 26  ? 0.22761 0.26516 0.30101 0.00649  0.10377  0.02817  25  PHE D O     
1537 C CB    . PHE B 26  ? 0.25242 0.26227 0.27199 0.02228  0.08847  0.03155  25  PHE D CB    
1538 C CG    . PHE B 26  ? 0.24909 0.24690 0.24383 0.02884  0.07871  0.03210  25  PHE D CG    
1539 C CD1   . PHE B 26  ? 0.34672 0.33067 0.31913 0.03316  0.08192  0.03887  25  PHE D CD1   
1540 C CD2   . PHE B 26  ? 0.27600 0.27740 0.27082 0.03079  0.06622  0.02572  25  PHE D CD2   
1541 C CE1   . PHE B 26  ? 0.32732 0.30524 0.28013 0.03917  0.07052  0.03771  25  PHE D CE1   
1542 C CE2   . PHE B 26  ? 0.32707 0.32043 0.30335 0.03520  0.05695  0.02443  25  PHE D CE2   
1543 C CZ    . PHE B 26  ? 0.31022 0.29389 0.26692 0.03916  0.05830  0.02977  25  PHE D CZ    
1544 N N     . ALA B 27  ? 0.23518 0.24691 0.29979 -0.00218 0.11814  0.03830  26  ALA D N     
1545 C CA    . ALA B 27  ? 0.23358 0.26034 0.32860 -0.01278 0.12824  0.03503  26  ALA D CA    
1546 C C     . ALA B 27  ? 0.27086 0.30994 0.37142 -0.00888 0.14027  0.03635  26  ALA D C     
1547 O O     . ALA B 27  ? 0.25646 0.31713 0.38422 -0.01434 0.14011  0.03002  26  ALA D O     
1548 C CB    . ALA B 27  ? 0.26639 0.27717 0.36520 -0.02252 0.14007  0.03952  26  ALA D CB    
1549 N N     . ASP B 28  ? 0.24192 0.26774 0.31377 0.00171  0.14612  0.04284  27  ASP D N     
1550 C CA    . ASP B 28  ? 0.25965 0.29292 0.33007 0.00689  0.15439  0.04282  27  ASP D CA    
1551 C C     . ASP B 28  ? 0.28099 0.33627 0.36659 0.01210  0.14743  0.03514  27  ASP D C     
1552 O O     . ASP B 28  ? 0.32375 0.39374 0.42357 0.01283  0.15316  0.03264  27  ASP D O     
1553 C CB    . ASP B 28  ? 0.34512 0.35717 0.37725 0.01745  0.16027  0.05023  27  ASP D CB    
1554 C CG    . ASP B 28  ? 0.37639 0.37752 0.38090 0.02677  0.14891  0.05058  27  ASP D CG    
1555 O OD1   . ASP B 28  ? 0.34806 0.35570 0.36159 0.02512  0.13186  0.04393  27  ASP D OD1   
1556 O OD2   . ASP B 28  ? 0.48133 0.46622 0.45306 0.03533  0.15181  0.05588  27  ASP D OD2   
1557 N N     . LYS B 29  ? 0.26813 0.32352 0.34791 0.01635  0.13137  0.03078  28  LYS D N     
1558 C CA    . LYS B 29  ? 0.29729 0.36750 0.38544 0.02336  0.12258  0.02423  28  LYS D CA    
1559 C C     . LYS B 29  ? 0.23174 0.31873 0.34449 0.01824  0.10887  0.01804  28  LYS D C     
1560 O O     . LYS B 29  ? 0.21411 0.32039 0.34473 0.02254  0.10544  0.01366  28  LYS D O     
1561 C CB    . LYS B 29  ? 0.32157 0.37526 0.37882 0.03324  0.11310  0.02321  28  LYS D CB    
1562 C CG    . LYS B 29  ? 0.43443 0.47582 0.46606 0.04154  0.12434  0.02616  28  LYS D CG    
1563 C CD    . LYS B 29  ? 0.46969 0.52592 0.51587 0.04666  0.13701  0.02448  28  LYS D CD    
1564 C CE    . LYS B 29  ? 0.53253 0.57787 0.56016 0.04847  0.15121  0.02936  28  LYS D CE    
1565 N NZ    . LYS B 29  ? 0.54581 0.60511 0.58876 0.05088  0.15969  0.02694  28  LYS D NZ    
1566 N N     . VAL B 30  ? 0.21326 0.29321 0.32622 0.01025  0.10132  0.01775  29  VAL D N     
1567 C CA    . VAL B 30  ? 0.19229 0.28509 0.32191 0.00633  0.08720  0.01149  29  VAL D CA    
1568 C C     . VAL B 30  ? 0.16772 0.26324 0.31474 -0.00723 0.08999  0.00981  29  VAL D C     
1569 O O     . VAL B 30  ? 0.18904 0.27272 0.32810 -0.01136 0.08222  0.00885  29  VAL D O     
1570 C CB    . VAL B 30  ? 0.23897 0.31805 0.34753 0.01176  0.07302  0.01075  29  VAL D CB    
1571 C CG1   . VAL B 30  ? 0.26559 0.36017 0.38613 0.01558  0.06161  0.00561  29  VAL D CG1   
1572 C CG2   . VAL B 30  ? 0.29549 0.35839 0.37702 0.02141  0.07510  0.01398  29  VAL D CG2   
1573 N N     . PRO B 31  ? 0.17433 0.28441 0.34600 -0.01499 0.10194  0.00880  30  PRO D N     
1574 C CA    . PRO B 31  ? 0.18040 0.28612 0.36571 -0.02958 0.10801  0.00738  30  PRO D CA    
1575 C C     . PRO B 31  ? 0.20384 0.31808 0.40246 -0.03741 0.09364  -0.00169 30  PRO D C     
1576 O O     . PRO B 31  ? 0.19547 0.29245 0.38877 -0.04556 0.09456  -0.00209 30  PRO D O     
1577 C CB    . PRO B 31  ? 0.21204 0.33101 0.41549 -0.03497 0.11911  0.00705  30  PRO D CB    
1578 C CG    . PRO B 31  ? 0.18504 0.32581 0.39602 -0.02411 0.11646  0.00553  30  PRO D CG    
1579 C CD    . PRO B 31  ? 0.16653 0.29254 0.35191 -0.01124 0.11443  0.01010  30  PRO D CD    
1580 N N     . LYS B 32  ? 0.17100 0.31085 0.38605 -0.03459 0.08106  -0.00900 31  LYS D N     
1581 C CA    . LYS B 32  ? 0.15939 0.30850 0.38449 -0.04134 0.06694  -0.01830 31  LYS D CA    
1582 C C     . LYS B 32  ? 0.16425 0.29045 0.36073 -0.03657 0.05677  -0.01659 31  LYS D C     
1583 O O     . LYS B 32  ? 0.17040 0.28838 0.36572 -0.04461 0.05222  -0.02165 31  LYS D O     
1584 C CB    . LYS B 32  ? 0.17093 0.35299 0.41585 -0.03573 0.05508  -0.02473 31  LYS D CB    
1585 C CG    . LYS B 32  ? 0.25265 0.45202 0.51308 -0.04370 0.04114  -0.03601 31  LYS D CG    
1586 C CD    . LYS B 32  ? 0.23801 0.46929 0.51380 -0.03542 0.02963  -0.03930 31  LYS D CD    
1587 C CE    . LYS B 32  ? 0.31615 0.55968 0.59102 -0.03469 0.01030  -0.04777 31  LYS D CE    
1588 N NZ    . LYS B 32  ? 0.27854 0.54501 0.55725 -0.01917 -0.00059 -0.04596 31  LYS D NZ    
1589 N N     . THR B 33  ? 0.14183 0.25789 0.31620 -0.02389 0.05370  -0.01037 32  THR D N     
1590 C CA    . THR B 33  ? 0.14587 0.24288 0.29610 -0.01929 0.04505  -0.00860 32  THR D CA    
1591 C C     . THR B 33  ? 0.17211 0.24370 0.30740 -0.02326 0.05303  -0.00347 32  THR D C     
1592 O O     . THR B 33  ? 0.16442 0.22377 0.29110 -0.02578 0.04806  -0.00513 32  THR D O     
1593 C CB    . THR B 33  ? 0.15288 0.24710 0.28723 -0.00619 0.04077  -0.00441 32  THR D CB    
1594 O OG1   . THR B 33  ? 0.15594 0.27254 0.30449 -0.00074 0.03495  -0.00789 32  THR D OG1   
1595 C CG2   . THR B 33  ? 0.15490 0.23374 0.26933 -0.00250 0.03159  -0.00367 32  THR D CG2   
1596 N N     . ALA B 34  ? 0.17268 0.23609 0.30385 -0.02256 0.06596  0.00320  33  ALA D N     
1597 C CA    . ALA B 34  ? 0.18612 0.22547 0.30236 -0.02440 0.07450  0.00976  33  ALA D CA    
1598 C C     . ALA B 34  ? 0.20657 0.24048 0.33626 -0.03688 0.07920  0.00574  33  ALA D C     
1599 O O     . ALA B 34  ? 0.21553 0.23030 0.33340 -0.03765 0.07881  0.00746  33  ALA D O     
1600 C CB    . ALA B 34  ? 0.21234 0.24531 0.32045 -0.02051 0.08846  0.01797  33  ALA D CB    
1601 N N     . GLU B 35  ? 0.20725 0.25844 0.36303 -0.04684 0.08347  -0.00061 34  GLU D N     
1602 C CA    . GLU B 35  ? 0.20876 0.25367 0.37887 -0.06087 0.08874  -0.00638 34  GLU D CA    
1603 C C     . GLU B 35  ? 0.24682 0.29030 0.41383 -0.06306 0.07481  -0.01507 34  GLU D C     
1604 O O     . GLU B 35  ? 0.20946 0.23400 0.37323 -0.06993 0.07864  -0.01724 34  GLU D O     
1605 C CB    . GLU B 35  ? 0.20223 0.26920 0.40187 -0.07131 0.09403  -0.01289 34  GLU D CB    
1606 C CG    . GLU B 35  ? 0.21947 0.28159 0.43010 -0.08481 0.09353  -0.02197 34  GLU D CG    
1607 C CD    . GLU B 35  ? 0.30789 0.33634 0.50383 -0.08800 0.10714  -0.01531 34  GLU D CD    
1608 O OE1   . GLU B 35  ? 0.33507 0.34612 0.51283 -0.07971 0.11713  -0.00292 34  GLU D OE1   
1609 O OE2   . GLU B 35  ? 0.38361 0.40276 0.58491 -0.09778 0.10751  -0.02265 34  GLU D OE2   
1610 N N     . ASN B 36  ? 0.17348 0.23475 0.33972 -0.05654 0.05979  -0.01976 35  ASN D N     
1611 C CA    . ASN B 36  ? 0.18800 0.24678 0.34695 -0.05702 0.04741  -0.02708 35  ASN D CA    
1612 C C     . ASN B 36  ? 0.18184 0.21314 0.31686 -0.05157 0.04931  -0.02072 35  ASN D C     
1613 O O     . ASN B 36  ? 0.18617 0.20294 0.31792 -0.05718 0.05026  -0.02516 35  ASN D O     
1614 C CB    . ASN B 36  ? 0.15640 0.23625 0.31451 -0.04824 0.03297  -0.02998 35  ASN D CB    
1615 C CG    . ASN B 36  ? 0.15618 0.23316 0.30271 -0.04683 0.02094  -0.03623 35  ASN D CG    
1616 O OD1   . ASN B 36  ? 0.17668 0.25763 0.33124 -0.05597 0.01707  -0.04655 35  ASN D OD1   
1617 N ND2   . ASN B 36  ? 0.17051 0.24067 0.29783 -0.03562 0.01544  -0.03061 35  ASN D ND2   
1618 N N     . PHE B 37  ? 0.19083 0.21524 0.30989 -0.04054 0.05018  -0.01094 36  PHE D N     
1619 C CA    . PHE B 37  ? 0.16878 0.17206 0.26794 -0.03417 0.05062  -0.00490 36  PHE D CA    
1620 C C     . PHE B 37  ? 0.19138 0.17290 0.28814 -0.03852 0.06329  -0.00042 36  PHE D C     
1621 O O     . PHE B 37  ? 0.21104 0.17602 0.29919 -0.03763 0.06370  -0.00034 36  PHE D O     
1622 C CB    . PHE B 37  ? 0.20077 0.20484 0.28623 -0.02278 0.04816  0.00295  36  PHE D CB    
1623 C CG    . PHE B 37  ? 0.18017 0.17002 0.24852 -0.01537 0.04511  0.00775  36  PHE D CG    
1624 C CD1   . PHE B 37  ? 0.21613 0.19006 0.27429 -0.01171 0.05243  0.01573  36  PHE D CD1   
1625 C CD2   . PHE B 37  ? 0.19285 0.18616 0.25593 -0.01146 0.03543  0.00476  36  PHE D CD2   
1626 C CE1   . PHE B 37  ? 0.19693 0.16262 0.24279 -0.00402 0.04842  0.01973  36  PHE D CE1   
1627 C CE2   . PHE B 37  ? 0.20544 0.18908 0.25732 -0.00539 0.03357  0.00877  36  PHE D CE2   
1628 C CZ    . PHE B 37  ? 0.20188 0.17372 0.24663 -0.00160 0.03919  0.01573  36  PHE D CZ    
1629 N N     . ARG B 38  ? 0.21378 0.19379 0.31778 -0.04258 0.07511  0.00385  37  ARG D N     
1630 C CA    . ARG B 38  ? 0.21429 0.17049 0.31482 -0.04637 0.08921  0.00951  37  ARG D CA    
1631 C C     . ARG B 38  ? 0.24028 0.18757 0.35141 -0.05792 0.09079  -0.00020 37  ARG D C     
1632 O O     . ARG B 38  ? 0.26346 0.18705 0.36396 -0.05625 0.09556  0.00253  37  ARG D O     
1633 C CB    . ARG B 38  ? 0.24392 0.20195 0.35295 -0.05065 0.10319  0.01472  37  ARG D CB    
1634 C CG    . ARG B 38  ? 0.27211 0.20220 0.37135 -0.05114 0.11903  0.02386  37  ARG D CG    
1635 C CD    . ARG B 38  ? 0.27779 0.21218 0.38719 -0.05707 0.12967  0.02423  37  ARG D CD    
1636 N NE    . ARG B 38  ? 0.29005 0.23892 0.42469 -0.07122 0.12696  0.01075  37  ARG D NE    
1637 C CZ    . ARG B 38  ? 0.29541 0.23225 0.43497 -0.07954 0.12790  0.00352  37  ARG D CZ    
1638 N NH1   . ARG B 38  ? 0.34947 0.25813 0.47181 -0.07493 0.13342  0.00901  37  ARG D NH1   
1639 N NH2   . ARG B 38  ? 0.32713 0.28141 0.48913 -0.09193 0.12303  -0.00974 37  ARG D NH2   
1640 N N     . ALA B 39  ? 0.23123 0.19762 0.36350 -0.06933 0.08675  -0.01222 38  ALA D N     
1641 C CA    . ALA B 39  ? 0.23253 0.19158 0.37517 -0.08205 0.08748  -0.02419 38  ALA D CA    
1642 C C     . ALA B 39  ? 0.22283 0.17401 0.35079 -0.07696 0.07696  -0.02935 38  ALA D C     
1643 O O     . ALA B 39  ? 0.27165 0.20171 0.39633 -0.08225 0.08200  -0.03421 38  ALA D O     
1644 C CB    . ALA B 39  ? 0.26174 0.24872 0.42757 -0.09248 0.08106  -0.03648 38  ALA D CB    
1645 N N     . LEU B 40  ? 0.22833 0.19530 0.34748 -0.06699 0.06342  -0.02896 39  LEU D N     
1646 C CA    . LEU B 40  ? 0.22438 0.18320 0.32819 -0.06105 0.05563  -0.03215 39  LEU D CA    
1647 C C     . LEU B 40  ? 0.29101 0.22377 0.37926 -0.05285 0.06380  -0.02228 39  LEU D C     
1648 O O     . LEU B 40  ? 0.27896 0.19759 0.35843 -0.05114 0.06358  -0.02592 39  LEU D O     
1649 C CB    . LEU B 40  ? 0.24084 0.21947 0.33813 -0.05176 0.04223  -0.03147 39  LEU D CB    
1650 C CG    . LEU B 40  ? 0.21537 0.21951 0.32615 -0.05753 0.03240  -0.04182 39  LEU D CG    
1651 C CD1   . LEU B 40  ? 0.19666 0.21538 0.29901 -0.04651 0.02201  -0.03810 39  LEU D CD1   
1652 C CD2   . LEU B 40  ? 0.23772 0.24040 0.34981 -0.06618 0.02756  -0.05587 39  LEU D CD2   
1653 N N     . SER B 41  ? 0.24599 0.17264 0.33009 -0.04679 0.07113  -0.00991 40  SER D N     
1654 C CA    . SER B 41  ? 0.27193 0.17738 0.34139 -0.03675 0.07732  0.00060  40  SER D CA    
1655 C C     . SER B 41  ? 0.26922 0.14737 0.33916 -0.04207 0.09136  0.00150  40  SER D C     
1656 O O     . SER B 41  ? 0.31298 0.17198 0.37233 -0.03462 0.09491  0.00547  40  SER D O     
1657 C CB    . SER B 41  ? 0.25135 0.16109 0.31290 -0.02715 0.07849  0.01308  40  SER D CB    
1658 O OG    . SER B 41  ? 0.27098 0.20022 0.32942 -0.02088 0.06659  0.01274  40  SER D OG    
1659 N N     . THR B 42  ? 0.30233 0.17897 0.38468 -0.05390 0.09971  -0.00200 41  THR D N     
1660 C CA    . THR B 42  ? 0.31012 0.16649 0.38968 -0.05671 0.10944  -0.00291 41  THR D CA    
1661 C C     . THR B 42  ? 0.33038 0.18363 0.41495 -0.06577 0.10568  -0.01802 41  THR D C     
1662 O O     . THR B 42  ? 0.38421 0.21757 0.46399 -0.06665 0.11331  -0.01937 41  THR D O     
1663 C CB    . THR B 42  ? 0.37332 0.23189 0.46303 -0.06472 0.11881  -0.00162 41  THR D CB    
1664 O OG1   . THR B 42  ? 0.33892 0.22025 0.44879 -0.07812 0.11270  -0.01453 41  THR D OG1   
1665 C CG2   . THR B 42  ? 0.34399 0.20487 0.42597 -0.05567 0.12360  0.01269  41  THR D CG2   
1666 N N     . GLY B 43  ? 0.30110 0.17356 0.39414 -0.07218 0.09425  -0.02960 42  GLY D N     
1667 C CA    . GLY B 43  ? 0.34365 0.21612 0.43987 -0.08128 0.08923  -0.04543 42  GLY D CA    
1668 C C     . GLY B 43  ? 0.36313 0.23988 0.47420 -0.09525 0.09255  -0.05472 42  GLY D C     
1669 O O     . GLY B 43  ? 0.42488 0.29692 0.53628 -0.10261 0.08998  -0.06741 42  GLY D O     
1670 N N     . GLU B 44  ? 0.31788 0.20423 0.44146 -0.09922 0.09815  -0.04939 43  GLU D N     
1671 C CA    . GLU B 44  ? 0.35551 0.24145 0.49352 -0.11202 0.10456  -0.05658 43  GLU D CA    
1672 C C     . GLU B 44  ? 0.35252 0.26293 0.50672 -0.12426 0.09224  -0.07406 43  GLU D C     
1673 O O     . GLU B 44  ? 0.40055 0.30815 0.56537 -0.13582 0.09577  -0.08328 43  GLU D O     
1674 C CB    . GLU B 44  ? 0.37689 0.26628 0.52347 -0.11244 0.11507  -0.04615 43  GLU D CB    
1675 C CG    . GLU B 44  ? 0.34704 0.26713 0.50558 -0.11172 0.10723  -0.04500 43  GLU D CG    
1676 C CD    . GLU B 44  ? 0.39508 0.31398 0.55418 -0.10736 0.11880  -0.03147 43  GLU D CD    
1677 O OE1   . GLU B 44  ? 0.37857 0.27752 0.51873 -0.09599 0.12604  -0.01807 43  GLU D OE1   
1678 O OE2   . GLU B 44  ? 0.38200 0.32060 0.55971 -0.11456 0.12026  -0.03443 43  GLU D OE2   
1679 N N     . LYS B 45  ? 0.35169 0.28628 0.50768 -0.12149 0.07763  -0.07878 44  LYS D N     
1680 C CA    . LYS B 45  ? 0.37485 0.33362 0.54224 -0.13025 0.06358  -0.09517 44  LYS D CA    
1681 C C     . LYS B 45  ? 0.34570 0.29153 0.49776 -0.13108 0.05705  -0.10664 44  LYS D C     
1682 O O     . LYS B 45  ? 0.40118 0.36468 0.55846 -0.13769 0.04469  -0.12092 44  LYS D O     
1683 C CB    . LYS B 45  ? 0.34100 0.33290 0.51605 -0.12543 0.05017  -0.09536 44  LYS D CB    
1684 C CG    . LYS B 45  ? 0.32183 0.32736 0.50954 -0.12210 0.05635  -0.08348 44  LYS D CG    
1685 C CD    . LYS B 45  ? 0.37855 0.39747 0.58889 -0.13255 0.06152  -0.08686 44  LYS D CD    
1686 C CE    . LYS B 45  ? 0.42953 0.46233 0.65005 -0.12762 0.06807  -0.07509 44  LYS D CE    
1687 N NZ    . LYS B 45  ? 0.47433 0.51535 0.71566 -0.13757 0.07678  -0.07673 44  LYS D NZ    
1688 N N     . GLY B 46  ? 0.37443 0.29051 0.50700 -0.12362 0.06494  -0.10067 45  GLY D N     
1689 C CA    . GLY B 46  ? 0.38947 0.29106 0.50573 -0.12295 0.06083  -0.11079 45  GLY D CA    
1690 C C     . GLY B 46  ? 0.34780 0.25350 0.44772 -0.11232 0.05164  -0.11043 45  GLY D C     
1691 O O     . GLY B 46  ? 0.42576 0.32116 0.50970 -0.11037 0.04782  -0.11906 45  GLY D O     
1692 N N     . PHE B 47  ? 0.32867 0.24826 0.43153 -0.10535 0.04881  -0.10090 46  PHE D N     
1693 C CA    . PHE B 47  ? 0.32427 0.24557 0.41227 -0.09496 0.04225  -0.09910 46  PHE D CA    
1694 C C     . PHE B 47  ? 0.31620 0.24225 0.40500 -0.08376 0.04590  -0.08013 46  PHE D C     
1695 O O     . PHE B 47  ? 0.32712 0.25735 0.43096 -0.08833 0.05226  -0.07428 46  PHE D O     
1696 C CB    . PHE B 47  ? 0.31984 0.27035 0.40600 -0.09468 0.02456  -0.10910 46  PHE D CB    
1697 C CG    . PHE B 47  ? 0.35155 0.33296 0.46060 -0.10107 0.01742  -0.11113 46  PHE D CG    
1698 C CD1   . PHE B 47  ? 0.30463 0.30279 0.41805 -0.09132 0.01546  -0.09711 46  PHE D CD1   
1699 C CD2   . PHE B 47  ? 0.36570 0.36079 0.48850 -0.11262 0.01217  -0.12355 46  PHE D CD2   
1700 C CE1   . PHE B 47  ? 0.26787 0.29454 0.40338 -0.09591 0.01034  -0.09889 46  PHE D CE1   
1701 C CE2   . PHE B 47  ? 0.33606 0.36180 0.48106 -0.11624 0.00610  -0.12384 46  PHE D CE2   
1702 C CZ    . PHE B 47  ? 0.29260 0.33456 0.44646 -0.10922 0.00579  -0.11316 46  PHE D CZ    
1703 N N     . GLY B 48  ? 0.27589 0.20081 0.34837 -0.06961 0.04268  -0.07117 47  GLY D N     
1704 C CA    . GLY B 48  ? 0.24000 0.17103 0.31218 -0.05938 0.04406  -0.05538 47  GLY D CA    
1705 C C     . GLY B 48  ? 0.24955 0.17104 0.30567 -0.04597 0.04472  -0.04671 47  GLY D C     
1706 O O     . GLY B 48  ? 0.27607 0.19215 0.32086 -0.04313 0.04229  -0.05236 47  GLY D O     
1707 N N     . TYR B 49  ? 0.26616 0.18695 0.32198 -0.03797 0.04825  -0.03342 48  TYR D N     
1708 C CA    . TYR B 49  ? 0.23460 0.15548 0.28045 -0.02581 0.04626  -0.02524 48  TYR D CA    
1709 C C     . TYR B 49  ? 0.23377 0.13391 0.27224 -0.01998 0.05405  -0.02321 48  TYR D C     
1710 O O     . TYR B 49  ? 0.23854 0.14139 0.27087 -0.01143 0.05196  -0.02006 48  TYR D O     
1711 C CB    . TYR B 49  ? 0.24386 0.17212 0.29184 -0.01963 0.04622  -0.01346 48  TYR D CB    
1712 C CG    . TYR B 49  ? 0.19942 0.14815 0.25305 -0.02171 0.03905  -0.01392 48  TYR D CG    
1713 C CD1   . TYR B 49  ? 0.19610 0.15881 0.24731 -0.02083 0.02985  -0.01891 48  TYR D CD1   
1714 C CD2   . TYR B 49  ? 0.21301 0.16584 0.27261 -0.02287 0.04244  -0.00847 48  TYR D CD2   
1715 C CE1   . TYR B 49  ? 0.20071 0.18085 0.25672 -0.02056 0.02378  -0.01852 48  TYR D CE1   
1716 C CE2   . TYR B 49  ? 0.18925 0.16080 0.25430 -0.02318 0.03676  -0.00894 48  TYR D CE2   
1717 C CZ    . TYR B 49  ? 0.18687 0.17173 0.25082 -0.02186 0.02730  -0.01408 48  TYR D CZ    
1718 O OH    . TYR B 49  ? 0.19144 0.19332 0.26084 -0.02045 0.02243  -0.01387 48  TYR D OH    
1719 N N     . LYS B 50  ? 0.26334 0.14243 0.30320 -0.02395 0.06402  -0.02469 49  LYS D N     
1720 C CA    . LYS B 50  ? 0.27672 0.13579 0.30983 -0.01533 0.07218  -0.02064 49  LYS D CA    
1721 C C     . LYS B 50  ? 0.28141 0.13940 0.30653 -0.01288 0.07004  -0.02895 49  LYS D C     
1722 O O     . LYS B 50  ? 0.30957 0.16469 0.33164 -0.02166 0.06838  -0.04190 49  LYS D O     
1723 C CB    . LYS B 50  ? 0.33706 0.16950 0.37166 -0.02056 0.08462  -0.02181 49  LYS D CB    
1724 C CG    . LYS B 50  ? 0.33527 0.15130 0.36254 -0.00800 0.09236  -0.01360 49  LYS D CG    
1725 C CD    . LYS B 50  ? 0.42773 0.22710 0.45430 -0.01017 0.10215  -0.00951 49  LYS D CD    
1726 C CE    . LYS B 50  ? 0.52892 0.31358 0.55316 -0.01793 0.10686  -0.02159 49  LYS D CE    
1727 N NZ    . LYS B 50  ? 0.60712 0.37390 0.63144 -0.02052 0.11765  -0.01774 49  LYS D NZ    
1728 N N     . GLY B 51  ? 0.26071 0.12156 0.28254 -0.00089 0.07046  -0.02187 50  GLY D N     
1729 C CA    . GLY B 51  ? 0.29412 0.15444 0.30833 0.00321  0.07084  -0.02753 50  GLY D CA    
1730 C C     . GLY B 51  ? 0.27182 0.15407 0.28402 0.00434  0.06174  -0.02730 50  GLY D C     
1731 O O     . GLY B 51  ? 0.26767 0.15119 0.27458 0.01024  0.06381  -0.02789 50  GLY D O     
1732 N N     . SER B 52  ? 0.23947 0.13771 0.25588 -0.00048 0.05330  -0.02575 51  SER D N     
1733 C CA    . SER B 52  ? 0.23735 0.15261 0.25031 0.00045  0.04557  -0.02567 51  SER D CA    
1734 C C     . SER B 52  ? 0.23093 0.15548 0.24909 0.00855  0.04547  -0.01564 51  SER D C     
1735 O O     . SER B 52  ? 0.23679 0.15906 0.26187 0.01364  0.04867  -0.00864 51  SER D O     
1736 C CB    . SER B 52  ? 0.22940 0.15740 0.24547 -0.00660 0.03725  -0.02841 51  SER D CB    
1737 O OG    . SER B 52  ? 0.23389 0.16724 0.25970 -0.00624 0.03683  -0.02054 51  SER D OG    
1738 N N     . CYS B 53  ? 0.22416 0.15925 0.23874 0.00991  0.04171  -0.01509 52  CYS D N     
1739 C CA    . CYS B 53  ? 0.24237 0.18595 0.26381 0.01576  0.04263  -0.00775 52  CYS D CA    
1740 C C     . CYS B 53  ? 0.20245 0.15909 0.22753 0.01425  0.03557  -0.00383 52  CYS D C     
1741 O O     . CYS B 53  ? 0.22945 0.18948 0.24986 0.01031  0.03035  -0.00635 52  CYS D O     
1742 C CB    . CYS B 53  ? 0.28217 0.22383 0.29856 0.01938  0.04855  -0.00920 52  CYS D CB    
1743 S SG    . CYS B 53  ? 0.33414 0.28180 0.33997 0.01779  0.04593  -0.00987 52  CYS D SG    
1744 N N     . PHE B 54  ? 0.18077 0.14531 0.21513 0.01775  0.03518  0.00176  53  PHE D N     
1745 C CA    . PHE B 54  ? 0.19058 0.16511 0.22776 0.01637  0.03016  0.00420  53  PHE D CA    
1746 C C     . PHE B 54  ? 0.19118 0.16621 0.22552 0.01654  0.03398  0.00369  53  PHE D C     
1747 O O     . PHE B 54  ? 0.21499 0.19387 0.25769 0.01885  0.03859  0.00551  53  PHE D O     
1748 C CB    . PHE B 54  ? 0.18266 0.16548 0.23056 0.01917  0.02761  0.00852  53  PHE D CB    
1749 C CG    . PHE B 54  ? 0.17590 0.15782 0.22229 0.01921  0.02388  0.01041  53  PHE D CG    
1750 C CD1   . PHE B 54  ? 0.19676 0.17078 0.24238 0.02200  0.02705  0.01237  53  PHE D CD1   
1751 C CD2   . PHE B 54  ? 0.17524 0.16185 0.21948 0.01663  0.01884  0.01045  53  PHE D CD2   
1752 C CE1   . PHE B 54  ? 0.22812 0.19958 0.27082 0.02185  0.02577  0.01519  53  PHE D CE1   
1753 C CE2   . PHE B 54  ? 0.19073 0.17638 0.23248 0.01695  0.01724  0.01247  53  PHE D CE2   
1754 C CZ    . PHE B 54  ? 0.20493 0.18319 0.24578 0.01933  0.02098  0.01517  53  PHE D CZ    
1755 N N     . HIS B 55  ? 0.19586 0.16759 0.21857 0.01468  0.03260  0.00162  54  HIS D N     
1756 C CA    . HIS B 55  ? 0.20764 0.17605 0.22242 0.01578  0.03786  0.00215  54  HIS D CA    
1757 C C     . HIS B 55  ? 0.18589 0.15822 0.20595 0.01471  0.03873  0.00635  54  HIS D C     
1758 O O     . HIS B 55  ? 0.22292 0.19225 0.24080 0.01521  0.04618  0.00829  54  HIS D O     
1759 C CB    . HIS B 55  ? 0.23429 0.19691 0.23094 0.01599  0.03548  -0.00141 54  HIS D CB    
1760 C CG    . HIS B 55  ? 0.22880 0.19587 0.22263 0.01509  0.02735  -0.00092 54  HIS D CG    
1761 N ND1   . HIS B 55  ? 0.23014 0.20224 0.23005 0.01261  0.02110  -0.00341 54  HIS D ND1   
1762 C CD2   . HIS B 55  ? 0.24953 0.21627 0.23587 0.01718  0.02579  0.00248  54  HIS D CD2   
1763 C CE1   . HIS B 55  ? 0.24080 0.21773 0.23823 0.01351  0.01564  -0.00219 54  HIS D CE1   
1764 N NE2   . HIS B 55  ? 0.25263 0.22561 0.24121 0.01683  0.01803  0.00150  54  HIS D NE2   
1765 N N     . ARG B 56  ? 0.17360 0.15109 0.20033 0.01286  0.03268  0.00749  55  ARG D N     
1766 C CA    . ARG B 56  ? 0.17964 0.15750 0.20990 0.01084  0.03363  0.00988  55  ARG D CA    
1767 C C     . ARG B 56  ? 0.14597 0.13270 0.19057 0.00873  0.02892  0.00921  55  ARG D C     
1768 O O     . ARG B 56  ? 0.16547 0.15408 0.20839 0.00919  0.02258  0.00837  55  ARG D O     
1769 C CB    . ARG B 56  ? 0.18661 0.15835 0.20349 0.01219  0.03058  0.01092  55  ARG D CB    
1770 C CG    . ARG B 56  ? 0.20654 0.17307 0.22470 0.01050  0.03377  0.01372  55  ARG D CG    
1771 C CD    . ARG B 56  ? 0.21909 0.17900 0.22454 0.01422  0.03054  0.01569  55  ARG D CD    
1772 N NE    . ARG B 56  ? 0.22721 0.18124 0.21595 0.01904  0.03261  0.01791  55  ARG D NE    
1773 C CZ    . ARG B 56  ? 0.26336 0.21775 0.24026 0.02439  0.02680  0.01827  55  ARG D CZ    
1774 N NH1   . ARG B 56  ? 0.29516 0.25445 0.27637 0.02578  0.02052  0.01747  55  ARG D NH1   
1775 N NH2   . ARG B 56  ? 0.35853 0.30895 0.31841 0.02916  0.02757  0.01942  55  ARG D NH2   
1776 N N     . ILE B 57  ? 0.14165 0.13507 0.20031 0.00665  0.03201  0.00917  56  ILE D N     
1777 C CA    . ILE B 57  ? 0.14878 0.15324 0.22083 0.00499  0.02609  0.00737  56  ILE D CA    
1778 C C     . ILE B 57  ? 0.14855 0.15431 0.23008 -0.00104 0.02904  0.00581  56  ILE D C     
1779 O O     . ILE B 57  ? 0.14643 0.15481 0.23791 -0.00339 0.03671  0.00638  56  ILE D O     
1780 C CB    . ILE B 57  ? 0.15274 0.16826 0.23667 0.00876  0.02524  0.00769  56  ILE D CB    
1781 C CG1   . ILE B 57  ? 0.17935 0.18864 0.25286 0.01380  0.02415  0.00918  56  ILE D CG1   
1782 C CG2   . ILE B 57  ? 0.16377 0.19313 0.26033 0.00790  0.01756  0.00558  56  ILE D CG2   
1783 C CD1   . ILE B 57  ? 0.18812 0.20444 0.27140 0.01953  0.02470  0.01079  56  ILE D CD1   
1784 N N     . ILE B 58  ? 0.14522 0.14776 0.22368 -0.00386 0.02433  0.00352  57  ILE D N     
1785 C CA    . ILE B 58  ? 0.14574 0.14513 0.23197 -0.01088 0.02789  0.00094  57  ILE D CA    
1786 C C     . ILE B 58  ? 0.13164 0.14272 0.22865 -0.01428 0.01904  -0.00526 57  ILE D C     
1787 O O     . ILE B 58  ? 0.16053 0.16827 0.24709 -0.01226 0.01247  -0.00712 57  ILE D O     
1788 C CB    . ILE B 58  ? 0.17902 0.15970 0.24975 -0.01086 0.03206  0.00315  57  ILE D CB    
1789 C CG1   . ILE B 58  ? 0.17883 0.14980 0.23633 -0.00620 0.03931  0.00918  57  ILE D CG1   
1790 C CG2   . ILE B 58  ? 0.19764 0.17185 0.27727 -0.01897 0.03721  0.00013  57  ILE D CG2   
1791 C CD1   . ILE B 58  ? 0.21522 0.16863 0.25641 -0.00366 0.04304  0.01286  57  ILE D CD1   
1792 N N     . PRO B 59  ? 0.15950 0.18569 0.27702 -0.01889 0.01849  -0.00892 58  PRO D N     
1793 C CA    . PRO B 59  ? 0.18262 0.22364 0.31003 -0.02134 0.00772  -0.01590 58  PRO D CA    
1794 C C     . PRO B 59  ? 0.18048 0.21002 0.30063 -0.02729 0.00557  -0.02192 58  PRO D C     
1795 O O     . PRO B 59  ? 0.19195 0.20692 0.31208 -0.03352 0.01404  -0.02250 58  PRO D O     
1796 C CB    . PRO B 59  ? 0.20045 0.26067 0.35519 -0.02668 0.00952  -0.01919 58  PRO D CB    
1797 C CG    . PRO B 59  ? 0.20323 0.26144 0.35971 -0.02229 0.02007  -0.01190 58  PRO D CG    
1798 C CD    . PRO B 59  ? 0.16454 0.19784 0.29732 -0.02054 0.02732  -0.00673 58  PRO D CD    
1799 N N     . GLY B 60  ? 0.20199 0.23609 0.31391 -0.02441 -0.00484 -0.02598 59  GLY D N     
1800 C CA    . GLY B 60  ? 0.19295 0.21525 0.29464 -0.02824 -0.00726 -0.03254 59  GLY D CA    
1801 C C     . GLY B 60  ? 0.17486 0.17840 0.25490 -0.02212 -0.00352 -0.02760 59  GLY D C     
1802 O O     . GLY B 60  ? 0.23471 0.22707 0.30438 -0.02322 -0.00457 -0.03256 59  GLY D O     
1803 N N     . PHE B 61  ? 0.15960 0.15990 0.23341 -0.01579 0.00092  -0.01890 60  PHE D N     
1804 C CA    . PHE B 61  ? 0.17234 0.15909 0.22938 -0.01005 0.00376  -0.01465 60  PHE D CA    
1805 C C     . PHE B 61  ? 0.17912 0.17213 0.22921 -0.00271 0.00093  -0.00957 60  PHE D C     
1806 O O     . PHE B 61  ? 0.17890 0.17176 0.21957 0.00098  -0.00257 -0.01038 60  PHE D O     
1807 C CB    . PHE B 61  ? 0.18130 0.15388 0.23549 -0.01044 0.01307  -0.00989 60  PHE D CB    
1808 C CG    . PHE B 61  ? 0.16791 0.12719 0.22511 -0.01713 0.01856  -0.01373 60  PHE D CG    
1809 C CD1   . PHE B 61  ? 0.20622 0.15029 0.25231 -0.01546 0.01966  -0.01608 60  PHE D CD1   
1810 C CD2   . PHE B 61  ? 0.20094 0.16193 0.27313 -0.02530 0.02392  -0.01534 60  PHE D CD2   
1811 C CE1   . PHE B 61  ? 0.24238 0.16998 0.29011 -0.02155 0.02615  -0.01959 60  PHE D CE1   
1812 C CE2   . PHE B 61  ? 0.22072 0.16648 0.29618 -0.03275 0.03086  -0.01886 60  PHE D CE2   
1813 C CZ    . PHE B 61  ? 0.20979 0.13714 0.27200 -0.03090 0.03188  -0.02115 60  PHE D CZ    
1814 N N     . MET B 62  ? 0.15784 0.15426 0.21149 -0.00079 0.00384  -0.00460 61  MET D N     
1815 C CA    . MET B 62  ? 0.16128 0.15977 0.20838 0.00468  0.00279  -0.00057 61  MET D CA    
1816 C C     . MET B 62  ? 0.16181 0.16393 0.21438 0.00585  0.00573  0.00268  61  MET D C     
1817 O O     . MET B 62  ? 0.17122 0.17328 0.23064 0.00341  0.01011  0.00291  61  MET D O     
1818 C CB    . MET B 62  ? 0.19498 0.18526 0.23186 0.00743  0.00502  0.00136  61  MET D CB    
1819 C CG    . MET B 62  ? 0.23044 0.21599 0.26517 0.00822  0.00947  0.00449  61  MET D CG    
1820 S SD    . MET B 62  ? 0.21605 0.19185 0.25176 0.00502  0.01529  0.00483  61  MET D SD    
1821 C CE    . MET B 62  ? 0.19787 0.17323 0.23004 0.00708  0.01949  0.00853  61  MET D CE    
1822 N N     . CYS B 63  ? 0.15527 0.15855 0.20388 0.00961  0.00486  0.00517  62  CYS D N     
1823 C CA    . CYS B 63  ? 0.14723 0.14973 0.19751 0.01136  0.00847  0.00749  62  CYS D CA    
1824 C C     . CYS B 63  ? 0.17573 0.17190 0.21741 0.01168  0.00998  0.00792  62  CYS D C     
1825 O O     . CYS B 63  ? 0.17125 0.16745 0.20941 0.01251  0.00832  0.00836  62  CYS D O     
1826 C CB    . CYS B 63  ? 0.18735 0.19488 0.24124 0.01539  0.00669  0.00965  62  CYS D CB    
1827 S SG    . CYS B 63  ? 0.21111 0.23280 0.27844 0.01660  0.00217  0.00851  62  CYS D SG    
1828 N N     . GLN B 64  ? 0.15793 0.14987 0.19641 0.01108  0.01321  0.00747  63  GLN D N     
1829 C CA    . GLN B 64  ? 0.14649 0.13566 0.17783 0.01106  0.01278  0.00626  63  GLN D CA    
1830 C C     . GLN B 64  ? 0.15139 0.13723 0.18105 0.01075  0.01552  0.00457  63  GLN D C     
1831 O O     . GLN B 64  ? 0.17629 0.15931 0.20585 0.01158  0.01952  0.00463  63  GLN D O     
1832 C CB    . GLN B 64  ? 0.16788 0.15412 0.19249 0.01195  0.01284  0.00657  63  GLN D CB    
1833 C CG    . GLN B 64  ? 0.16449 0.15199 0.18234 0.01334  0.01011  0.00495  63  GLN D CG    
1834 C CD    . GLN B 64  ? 0.19562 0.17987 0.20492 0.01699  0.00965  0.00697  63  GLN D CD    
1835 O OE1   . GLN B 64  ? 0.20442 0.18338 0.21343 0.01768  0.01207  0.00958  63  GLN D OE1   
1836 N NE2   . GLN B 64  ? 0.19030 0.17692 0.19206 0.01954  0.00657  0.00560  63  GLN D NE2   
1837 N N     . GLY B 65  ? 0.14936 0.13506 0.17846 0.00913  0.01441  0.00246  64  GLY D N     
1838 C CA    . GLY B 65  ? 0.17610 0.15622 0.20287 0.00750  0.01710  -0.00116 64  GLY D CA    
1839 C C     . GLY B 65  ? 0.17832 0.16098 0.20421 0.00372  0.01421  -0.00603 64  GLY D C     
1840 O O     . GLY B 65  ? 0.18167 0.17231 0.20840 0.00379  0.00986  -0.00614 64  GLY D O     
1841 N N     . GLY B 66  ? 0.21067 0.18692 0.23612 0.00038  0.01683  -0.01079 65  GLY D N     
1842 C CA    . GLY B 66  ? 0.21019 0.19007 0.23954 -0.00551 0.01456  -0.01680 65  GLY D CA    
1843 C C     . GLY B 66  ? 0.20703 0.18887 0.22915 -0.00784 0.01033  -0.02525 65  GLY D C     
1844 O O     . GLY B 66  ? 0.21053 0.19911 0.23875 -0.01374 0.00694  -0.03184 65  GLY D O     
1845 N N     . ASP B 67  ? 0.20811 0.18501 0.21746 -0.00368 0.01063  -0.02584 66  ASP D N     
1846 C CA    . ASP B 67  ? 0.21114 0.18903 0.20913 -0.00499 0.00610  -0.03452 66  ASP D CA    
1847 C C     . ASP B 67  ? 0.23327 0.19774 0.22856 -0.00971 0.01135  -0.04241 66  ASP D C     
1848 O O     . ASP B 67  ? 0.25552 0.20823 0.24090 -0.00602 0.01751  -0.04215 66  ASP D O     
1849 C CB    . ASP B 67  ? 0.23451 0.21050 0.21604 0.00226  0.00580  -0.03126 66  ASP D CB    
1850 C CG    . ASP B 67  ? 0.24495 0.22153 0.20973 0.00272  0.00052  -0.03984 66  ASP D CG    
1851 O OD1   . ASP B 67  ? 0.26818 0.24738 0.23561 -0.00384 -0.00375 -0.05032 66  ASP D OD1   
1852 O OD2   . ASP B 67  ? 0.26667 0.23966 0.21404 0.00930  0.00132  -0.03689 66  ASP D OD2   
1853 N N     . PHE B 68  ? 0.21497 0.18085 0.21926 -0.01809 0.00968  -0.05023 67  PHE D N     
1854 C CA    . PHE B 68  ? 0.24600 0.19653 0.24738 -0.02395 0.01489  -0.05971 67  PHE D CA    
1855 C C     . PHE B 68  ? 0.28478 0.23874 0.27494 -0.02831 0.00741  -0.07376 67  PHE D C     
1856 O O     . PHE B 68  ? 0.31284 0.25256 0.29861 -0.03397 0.01142  -0.08405 67  PHE D O     
1857 C CB    . PHE B 68  ? 0.29060 0.23454 0.30854 -0.03177 0.02089  -0.05997 67  PHE D CB    
1858 C CG    . PHE B 68  ? 0.24064 0.20185 0.27379 -0.03932 0.01485  -0.06320 67  PHE D CG    
1859 C CD1   . PHE B 68  ? 0.27762 0.24615 0.31469 -0.04880 0.00884  -0.07710 67  PHE D CD1   
1860 C CD2   . PHE B 68  ? 0.24544 0.21714 0.28994 -0.03695 0.01522  -0.05313 67  PHE D CD2   
1861 C CE1   . PHE B 68  ? 0.25696 0.24550 0.31223 -0.05583 0.00339  -0.08057 67  PHE D CE1   
1862 C CE2   . PHE B 68  ? 0.25522 0.24387 0.31547 -0.04344 0.01136  -0.05626 67  PHE D CE2   
1863 C CZ    . PHE B 68  ? 0.25293 0.25147 0.32010 -0.05265 0.00541  -0.06956 67  PHE D CZ    
1864 N N     . THR B 69  ? 0.28312 0.25480 0.26726 -0.02516 -0.00355 -0.07485 68  THR D N     
1865 C CA    . THR B 69  ? 0.28624 0.26389 0.25746 -0.02783 -0.01290 -0.08842 68  THR D CA    
1866 C C     . THR B 69  ? 0.32538 0.29527 0.26868 -0.01842 -0.01283 -0.08786 68  THR D C     
1867 O O     . THR B 69  ? 0.35875 0.32165 0.28605 -0.02067 -0.01477 -0.10003 68  THR D O     
1868 C CB    . THR B 69  ? 0.29403 0.29832 0.27517 -0.02960 -0.02669 -0.09204 68  THR D CB    
1869 O OG1   . THR B 69  ? 0.31082 0.32495 0.28518 -0.01792 -0.03056 -0.07993 68  THR D OG1   
1870 C CG2   . THR B 69  ? 0.31105 0.32428 0.32120 -0.03953 -0.02493 -0.09283 68  THR D CG2   
1871 N N     . ARG B 70  ? 0.32321 0.29363 0.25934 -0.00835 -0.01015 -0.07469 69  ARG D N     
1872 C CA    . ARG B 70  ? 0.33693 0.29840 0.24662 0.00047  -0.00720 -0.07259 69  ARG D CA    
1873 C C     . ARG B 70  ? 0.32020 0.26542 0.22915 0.00452  0.00748  -0.06405 69  ARG D C     
1874 O O     . ARG B 70  ? 0.36509 0.29982 0.25345 0.01033  0.01362  -0.06401 69  ARG D O     
1875 C CB    . ARG B 70  ? 0.36295 0.33649 0.26221 0.00961  -0.01446 -0.06407 69  ARG D CB    
1876 C CG    . ARG B 70  ? 0.38819 0.38175 0.28721 0.00892  -0.03039 -0.07156 69  ARG D CG    
1877 C CD    . ARG B 70  ? 0.48014 0.47275 0.35572 0.00863  -0.03759 -0.08555 69  ARG D CD    
1878 N NE    . ARG B 70  ? 0.54449 0.51702 0.39204 0.01496  -0.02783 -0.08409 69  ARG D NE    
1879 C CZ    . ARG B 70  ? 0.52421 0.49167 0.34948 0.02669  -0.02453 -0.07328 69  ARG D CZ    
1880 N NH1   . ARG B 70  ? 0.61354 0.59164 0.44102 0.03400  -0.02953 -0.06192 69  ARG D NH1   
1881 N NH2   . ARG B 70  ? 0.63868 0.58828 0.43848 0.03144  -0.01444 -0.07367 69  ARG D NH2   
1882 N N     . HIS B 71  ? 0.29392 0.23815 0.22447 0.00219  0.01320  -0.05702 70  HIS D N     
1883 C CA    . HIS B 71  ? 0.32026 0.25319 0.25496 0.00599  0.02567  -0.04983 70  HIS D CA    
1884 C C     . HIS B 71  ? 0.33309 0.26669 0.25797 0.01373  0.03006  -0.04053 70  HIS D C     
1885 O O     . HIS B 71  ? 0.36964 0.29419 0.29046 0.01768  0.04081  -0.03794 70  HIS D O     
1886 C CB    . HIS B 71  ? 0.34757 0.26349 0.27461 0.00500  0.03410  -0.05839 70  HIS D CB    
1887 C CG    . HIS B 71  ? 0.33283 0.24388 0.26581 -0.00394 0.03090  -0.06973 70  HIS D CG    
1888 N ND1   . HIS B 71  ? 0.31515 0.22148 0.26740 -0.00801 0.03512  -0.06712 70  HIS D ND1   
1889 C CD2   . HIS B 71  ? 0.33269 0.24256 0.25518 -0.01011 0.02427  -0.08395 70  HIS D CD2   
1890 C CE1   . HIS B 71  ? 0.30892 0.20950 0.26345 -0.01712 0.03296  -0.07870 70  HIS D CE1   
1891 N NE2   . HIS B 71  ? 0.36959 0.27330 0.30760 -0.01928 0.02577  -0.09008 70  HIS D NE2   
1892 N N     . ASN B 72  ? 0.32363 0.26724 0.24497 0.01615  0.02293  -0.03549 71  ASN D N     
1893 C CA    . ASN B 72  ? 0.33816 0.27889 0.24894 0.02280  0.02875  -0.02636 71  ASN D CA    
1894 C C     . ASN B 72  ? 0.30873 0.25802 0.23018 0.02395  0.02488  -0.01729 71  ASN D C     
1895 O O     . ASN B 72  ? 0.36188 0.30745 0.27335 0.02895  0.02895  -0.00982 71  ASN D O     
1896 C CB    . ASN B 72  ? 0.36676 0.30190 0.24746 0.02840  0.02789  -0.02948 71  ASN D CB    
1897 C CG    . ASN B 72  ? 0.35042 0.29640 0.22185 0.02970  0.01336  -0.03325 71  ASN D CG    
1898 O OD1   . ASN B 72  ? 0.31924 0.27737 0.20778 0.02718  0.00541  -0.03155 71  ASN D OD1   
1899 N ND2   . ASN B 72  ? 0.47622 0.41915 0.31987 0.03468  0.00966  -0.03834 71  ASN D ND2   
1900 N N     . GLY B 73  ? 0.25950 0.21816 0.19888 0.01975  0.01822  -0.01783 72  GLY D N     
1901 C CA    . GLY B 73  ? 0.26204 0.22762 0.21101 0.02096  0.01490  -0.01080 72  GLY D CA    
1902 C C     . GLY B 73  ? 0.29112 0.26550 0.23301 0.02444  0.00488  -0.01129 72  GLY D C     
1903 O O     . GLY B 73  ? 0.31569 0.29483 0.26520 0.02640  0.00258  -0.00592 72  GLY D O     
1904 N N     . THR B 74  ? 0.29382 0.27113 0.22113 0.02606  -0.00144 -0.01802 73  THR D N     
1905 C CA    . THR B 74  ? 0.27863 0.26764 0.19897 0.03134  -0.01244 -0.01858 73  THR D CA    
1906 C C     . THR B 74  ? 0.29122 0.29666 0.22609 0.02531  -0.02257 -0.02836 73  THR D C     
1907 O O     . THR B 74  ? 0.31242 0.33294 0.24935 0.02948  -0.03238 -0.02876 73  THR D O     
1908 C CB    . THR B 74  ? 0.31870 0.30234 0.20957 0.03926  -0.01435 -0.01897 73  THR D CB    
1909 O OG1   . THR B 74  ? 0.33677 0.31959 0.21892 0.03479  -0.01681 -0.03083 73  THR D OG1   
1910 C CG2   . THR B 74  ? 0.37960 0.34544 0.25578 0.04464  -0.00143 -0.00863 73  THR D CG2   
1911 N N     . GLY B 75  ? 0.25362 0.25658 0.19977 0.01594  -0.01970 -0.03593 74  GLY D N     
1912 C CA    . GLY B 75  ? 0.26645 0.28269 0.22554 0.00834  -0.02753 -0.04666 74  GLY D CA    
1913 C C     . GLY B 75  ? 0.24866 0.26997 0.23340 0.00123  -0.02445 -0.04547 74  GLY D C     
1914 O O     . GLY B 75  ? 0.24167 0.26295 0.23450 0.00435  -0.02064 -0.03609 74  GLY D O     
1915 N N     . GLY B 76  ? 0.28501 0.30934 0.28139 -0.00872 -0.02542 -0.05553 75  GLY D N     
1916 C CA    . GLY B 76  ? 0.28024 0.30967 0.29987 -0.01615 -0.02190 -0.05519 75  GLY D CA    
1917 C C     . GLY B 76  ? 0.26183 0.31441 0.29744 -0.02129 -0.03115 -0.06336 75  GLY D C     
1918 O O     . GLY B 76  ? 0.27500 0.34322 0.30468 -0.01652 -0.04228 -0.06726 75  GLY D O     
1919 N N     . LYS B 77  ? 0.24023 0.29563 0.29691 -0.03079 -0.02601 -0.06567 76  LYS D N     
1920 C CA    . LYS B 77  ? 0.24950 0.32914 0.32744 -0.03751 -0.03276 -0.07379 76  LYS D CA    
1921 C C     . LYS B 77  ? 0.20446 0.28353 0.30389 -0.04454 -0.02224 -0.06967 76  LYS D C     
1922 O O     . LYS B 77  ? 0.23044 0.28785 0.32660 -0.04698 -0.01083 -0.06443 76  LYS D O     
1923 C CB    . LYS B 77  ? 0.32593 0.41082 0.40470 -0.04730 -0.03991 -0.09033 76  LYS D CB    
1924 C CG    . LYS B 77  ? 0.32882 0.39367 0.41261 -0.06045 -0.02985 -0.09771 76  LYS D CG    
1925 C CD    . LYS B 77  ? 0.31644 0.39021 0.40187 -0.07049 -0.03927 -0.11647 76  LYS D CD    
1926 C CE    . LYS B 77  ? 0.41397 0.46203 0.49894 -0.08290 -0.02899 -0.12560 76  LYS D CE    
1927 N NZ    . LYS B 77  ? 0.42375 0.48069 0.51110 -0.09440 -0.03872 -0.14627 76  LYS D NZ    
1928 N N     . SER B 78  ? 0.17404 0.27755 0.29428 -0.04587 -0.02577 -0.07086 77  SER D N     
1929 C CA    . SER B 78  ? 0.18579 0.29115 0.32651 -0.05226 -0.01484 -0.06702 77  SER D CA    
1930 C C     . SER B 78  ? 0.22282 0.33231 0.38389 -0.06897 -0.01159 -0.07924 77  SER D C     
1931 O O     . SER B 78  ? 0.23255 0.34807 0.39369 -0.07543 -0.02034 -0.09231 77  SER D O     
1932 C CB    . SER B 78  ? 0.14617 0.27563 0.30039 -0.04471 -0.01796 -0.06194 77  SER D CB    
1933 O OG    . SER B 78  ? 0.18890 0.34839 0.36531 -0.04988 -0.02680 -0.07240 77  SER D OG    
1934 N N     . ILE B 79  ? 0.19047 0.29533 0.36790 -0.07637 0.00189  -0.07521 78  ILE D N     
1935 C CA    . ILE B 79  ? 0.20505 0.31459 0.40674 -0.09365 0.00786  -0.08581 78  ILE D CA    
1936 C C     . ILE B 79  ? 0.21200 0.35634 0.43569 -0.09597 -0.00167 -0.09282 78  ILE D C     
1937 O O     . ILE B 79  ? 0.26805 0.41468 0.50439 -0.10710 0.00063  -0.09982 78  ILE D O     
1938 C CB    . ILE B 79  ? 0.24197 0.33125 0.44952 -0.09912 0.02747  -0.07655 78  ILE D CB    
1939 C CG1   . ILE B 79  ? 0.21646 0.32254 0.43654 -0.09320 0.03304  -0.06676 78  ILE D CG1   
1940 C CG2   . ILE B 79  ? 0.21529 0.26852 0.39666 -0.09307 0.03594  -0.06694 78  ILE D CG2   
1941 C CD1   . ILE B 79  ? 0.23906 0.32687 0.46096 -0.09714 0.05167  -0.05730 78  ILE D CD1   
1942 N N     . TYR B 80  ? 0.17089 0.34044 0.39725 -0.08416 -0.01235 -0.09012 79  TYR D N     
1943 C CA    . TYR B 80  ? 0.17284 0.37466 0.41784 -0.08226 -0.02109 -0.09331 79  TYR D CA    
1944 C C     . TYR B 80  ? 0.22393 0.44308 0.46041 -0.07678 -0.04070 -0.10208 79  TYR D C     
1945 O O     . TYR B 80  ? 0.31969 0.56494 0.57130 -0.07632 -0.04935 -0.10621 79  TYR D O     
1946 C CB    . TYR B 80  ? 0.21605 0.43258 0.46870 -0.06989 -0.01786 -0.08213 79  TYR D CB    
1947 C CG    . TYR B 80  ? 0.16573 0.36436 0.42060 -0.07200 0.00112  -0.07202 79  TYR D CG    
1948 C CD1   . TYR B 80  ? 0.23109 0.42486 0.50033 -0.08346 0.01427  -0.07155 79  TYR D CD1   
1949 C CD2   . TYR B 80  ? 0.16956 0.35143 0.40493 -0.06048 0.00575  -0.06089 79  TYR D CD2   
1950 C CE1   . TYR B 80  ? 0.17588 0.35115 0.44175 -0.08355 0.03175  -0.06104 79  TYR D CE1   
1951 C CE2   . TYR B 80  ? 0.20587 0.36936 0.43718 -0.06064 0.02197  -0.05089 79  TYR D CE2   
1952 C CZ    . TYR B 80  ? 0.19524 0.35811 0.44503 -0.07286 0.03554  -0.05182 79  TYR D CZ    
1953 O OH    . TYR B 80  ? 0.20948 0.35322 0.45172 -0.07145 0.05211  -0.04092 79  TYR D OH    
1954 N N     . GLY B 81  ? 0.31449 0.51970 0.52589 -0.07153 -0.04759 -0.10415 80  GLY D N     
1955 C CA    . GLY B 81  ? 0.28165 0.50008 0.47727 -0.06230 -0.06536 -0.10929 80  GLY D CA    
1956 C C     . GLY B 81  ? 0.29877 0.49817 0.46424 -0.05008 -0.06681 -0.10219 80  GLY D C     
1957 O O     . GLY B 81  ? 0.27717 0.44922 0.43252 -0.04929 -0.05306 -0.09183 80  GLY D O     
1958 N N     . GLU B 82  ? 0.33346 0.53992 0.47802 -0.03853 -0.08087 -0.10349 81  GLU D N     
1959 C CA    . GLU B 82  ? 0.37428 0.55506 0.48541 -0.02525 -0.07788 -0.09149 81  GLU D CA    
1960 C C     . GLU B 82  ? 0.36275 0.53869 0.47505 -0.01431 -0.06976 -0.07543 81  GLU D C     
1961 O O     . GLU B 82  ? 0.35282 0.50219 0.44685 -0.01011 -0.06055 -0.06577 81  GLU D O     
1962 C CB    . GLU B 82  ? 0.35739 0.54420 0.44297 -0.01411 -0.09257 -0.09450 81  GLU D CB    
1963 C CG    . GLU B 82  ? 0.55287 0.73178 0.62423 -0.02341 -0.09781 -0.10943 81  GLU D CG    
1964 C CD    . GLU B 82  ? 0.60974 0.79047 0.64870 -0.01038 -0.11069 -0.11065 81  GLU D CD    
1965 O OE1   . GLU B 82  ? 0.55759 0.74017 0.58276 0.00627  -0.11333 -0.09768 81  GLU D OE1   
1966 O OE2   . GLU B 82  ? 0.61650 0.79258 0.64170 -0.01652 -0.11602 -0.12304 81  GLU D OE2   
1967 N N     . LYS B 83  ? 0.34461 0.54615 0.47913 -0.00988 -0.07261 -0.07329 82  LYS D N     
1968 C CA    . LYS B 83  ? 0.25404 0.44986 0.38779 0.00121  -0.06490 -0.05947 82  LYS D CA    
1969 C C     . LYS B 83  ? 0.24156 0.46030 0.40789 -0.00212 -0.06033 -0.06002 82  LYS D C     
1970 O O     . LYS B 83  ? 0.28256 0.53135 0.47343 -0.00762 -0.06792 -0.06989 82  LYS D O     
1971 C CB    . LYS B 83  ? 0.28098 0.48017 0.39623 0.01974  -0.07366 -0.05190 82  LYS D CB    
1972 C CG    . LYS B 83  ? 0.37212 0.54987 0.45378 0.02499  -0.07708 -0.04993 82  LYS D CG    
1973 C CD    . LYS B 83  ? 0.41140 0.55594 0.47746 0.02291  -0.06351 -0.04181 82  LYS D CD    
1974 C CE    . LYS B 83  ? 0.48857 0.61342 0.52784 0.02263  -0.06411 -0.04330 82  LYS D CE    
1975 N NZ    . LYS B 83  ? 0.48440 0.59530 0.52762 0.00849  -0.05638 -0.04954 82  LYS D NZ    
1976 N N     . PHE B 84  ? 0.17440 0.38030 0.34104 0.00166  -0.04792 -0.04983 83  PHE D N     
1977 C CA    . PHE B 84  ? 0.17992 0.40501 0.37356 0.00122  -0.04116 -0.04851 83  PHE D CA    
1978 C C     . PHE B 84  ? 0.14936 0.36792 0.33387 0.01684  -0.03654 -0.03712 83  PHE D C     
1979 O O     . PHE B 84  ? 0.15681 0.35003 0.31527 0.02402  -0.03476 -0.02980 83  PHE D O     
1980 C CB    . PHE B 84  ? 0.18291 0.40152 0.39295 -0.01504 -0.02732 -0.05122 83  PHE D CB    
1981 C CG    . PHE B 84  ? 0.18793 0.37187 0.37761 -0.01627 -0.01444 -0.04252 83  PHE D CG    
1982 C CD1   . PHE B 84  ? 0.16066 0.32006 0.33062 -0.02124 -0.01432 -0.04331 83  PHE D CD1   
1983 C CD2   . PHE B 84  ? 0.14839 0.32676 0.34079 -0.01303 -0.00228 -0.03474 83  PHE D CD2   
1984 C CE1   . PHE B 84  ? 0.16941 0.30100 0.32327 -0.02157 -0.00396 -0.03571 83  PHE D CE1   
1985 C CE2   . PHE B 84  ? 0.18025 0.32958 0.35361 -0.01366 0.00770  -0.02752 83  PHE D CE2   
1986 C CZ    . PHE B 84  ? 0.18222 0.30949 0.33763 -0.01782 0.00627  -0.02787 83  PHE D CZ    
1987 N N     . GLU B 85  ? 0.16287 0.40436 0.37060 0.02149  -0.03347 -0.03636 84  GLU D N     
1988 C CA    . GLU B 85  ? 0.15362 0.39043 0.35370 0.03766  -0.02966 -0.02717 84  GLU D CA    
1989 C C     . GLU B 85  ? 0.16740 0.37373 0.35125 0.03639  -0.01546 -0.02016 84  GLU D C     
1990 O O     . GLU B 85  ? 0.16167 0.35725 0.34724 0.02413  -0.00659 -0.02131 84  GLU D O     
1991 C CB    . GLU B 85  ? 0.16119 0.42706 0.38897 0.04282  -0.02821 -0.02758 84  GLU D CB    
1992 C CG    . GLU B 85  ? 0.25660 0.54234 0.48913 0.04875  -0.04320 -0.02970 84  GLU D CG    
1993 C CD    . GLU B 85  ? 0.44546 0.75540 0.70410 0.05277  -0.04134 -0.02858 84  GLU D CD    
1994 O OE1   . GLU B 85  ? 0.45259 0.76666 0.72899 0.04743  -0.02789 -0.02759 84  GLU D OE1   
1995 O OE2   . GLU B 85  ? 0.48699 0.81199 0.74782 0.06189  -0.05301 -0.02832 84  GLU D OE2   
1996 N N     . ASP B 86  ? 0.14375 0.33592 0.31127 0.04997  -0.01340 -0.01295 85  ASP D N     
1997 C CA    . ASP B 86  ? 0.15759 0.32485 0.31095 0.05016  -0.00134 -0.00786 85  ASP D CA    
1998 C C     . ASP B 86  ? 0.14958 0.33067 0.32304 0.04838  0.01002  -0.00844 85  ASP D C     
1999 O O     . ASP B 86  ? 0.16181 0.36163 0.35025 0.05839  0.01137  -0.00792 85  ASP D O     
2000 C CB    . ASP B 86  ? 0.14562 0.29533 0.27914 0.06422  -0.00187 -0.00200 85  ASP D CB    
2001 C CG    . ASP B 86  ? 0.17531 0.30748 0.28716 0.06524  -0.00970 -0.00011 85  ASP D CG    
2002 O OD1   . ASP B 86  ? 0.19143 0.31024 0.29400 0.05466  -0.00944 -0.00153 85  ASP D OD1   
2003 O OD2   . ASP B 86  ? 0.18325 0.31444 0.28722 0.07780  -0.01485 0.00354  85  ASP D OD2   
2004 N N     . GLU B 87  ? 0.15097 0.32145 0.32340 0.03681  0.01939  -0.00866 86  GLU D N     
2005 C CA    . GLU B 87  ? 0.15840 0.34151 0.34988 0.03267  0.03197  -0.00902 86  GLU D CA    
2006 C C     . GLU B 87  ? 0.15449 0.33120 0.33845 0.04451  0.04148  -0.00468 86  GLU D C     
2007 O O     . GLU B 87  ? 0.15429 0.35225 0.35875 0.05000  0.04740  -0.00528 86  GLU D O     
2008 C CB    . GLU B 87  ? 0.15974 0.32753 0.34636 0.01891  0.04047  -0.00853 86  GLU D CB    
2009 C CG    . GLU B 87  ? 0.14499 0.32288 0.34991 0.01289  0.05564  -0.00795 86  GLU D CG    
2010 C CD    . GLU B 87  ? 0.17161 0.33374 0.37262 -0.00068 0.06354  -0.00693 86  GLU D CD    
2011 O OE1   . GLU B 87  ? 0.17350 0.31432 0.35381 -0.00289 0.05760  -0.00582 86  GLU D OE1   
2012 O OE2   . GLU B 87  ? 0.21578 0.38698 0.43562 -0.00876 0.07639  -0.00700 86  GLU D OE2   
2013 N N     . ASN B 88  ? 0.14975 0.29779 0.30532 0.04795  0.04371  -0.00118 87  ASN D N     
2014 C CA    . ASN B 88  ? 0.16561 0.30275 0.30882 0.05930  0.05133  0.00116  87  ASN D CA    
2015 C C     . ASN B 88  ? 0.16851 0.27568 0.28169 0.06082  0.04733  0.00254  87  ASN D C     
2016 O O     . ASN B 88  ? 0.16319 0.26043 0.26755 0.05314  0.04072  0.00255  87  ASN D O     
2017 C CB    . ASN B 88  ? 0.18738 0.32657 0.33482 0.05735  0.06724  0.00226  87  ASN D CB    
2018 C CG    . ASN B 88  ? 0.18772 0.30769 0.31828 0.04710  0.07244  0.00439  87  ASN D CG    
2019 O OD1   . ASN B 88  ? 0.18321 0.28020 0.28821 0.04823  0.06928  0.00544  87  ASN D OD1   
2020 N ND2   . ASN B 88  ? 0.20725 0.33700 0.35296 0.03777  0.08165  0.00525  87  ASN D ND2   
2021 N N     . PHE B 89  ? 0.20527 0.29869 0.30436 0.07064  0.05169  0.00290  88  PHE D N     
2022 C CA    . PHE B 89  ? 0.21822 0.28423 0.29127 0.07082  0.04917  0.00254  88  PHE D CA    
2023 C C     . PHE B 89  ? 0.21801 0.27006 0.27469 0.07180  0.05905  0.00127  88  PHE D C     
2024 O O     . PHE B 89  ? 0.27539 0.30819 0.31368 0.07646  0.05969  -0.00120 88  PHE D O     
2025 C CB    . PHE B 89  ? 0.21169 0.26790 0.27822 0.08028  0.04379  0.00282  88  PHE D CB    
2026 C CG    . PHE B 89  ? 0.18362 0.25074 0.25964 0.08011  0.03341  0.00470  88  PHE D CG    
2027 C CD1   . PHE B 89  ? 0.19959 0.26044 0.26932 0.07052  0.02636  0.00483  88  PHE D CD1   
2028 C CD2   . PHE B 89  ? 0.20826 0.29314 0.29888 0.09057  0.03053  0.00624  88  PHE D CD2   
2029 C CE1   . PHE B 89  ? 0.20748 0.27712 0.28232 0.07085  0.01742  0.00596  88  PHE D CE1   
2030 C CE2   . PHE B 89  ? 0.24454 0.33974 0.34022 0.09099  0.01997  0.00756  88  PHE D CE2   
2031 C CZ    . PHE B 89  ? 0.20877 0.29562 0.29549 0.08109  0.01386  0.00718  88  PHE D CZ    
2032 N N     . ILE B 90  ? 0.19499 0.25587 0.25735 0.06729  0.06751  0.00262  89  ILE D N     
2033 C CA    . ILE B 90  ? 0.23602 0.28448 0.27996 0.06956  0.07777  0.00210  89  ILE D CA    
2034 C C     . ILE B 90  ? 0.23334 0.26008 0.25129 0.06569  0.07187  0.00064  89  ILE D C     
2035 O O     . ILE B 90  ? 0.27373 0.28489 0.27107 0.07054  0.07417  -0.00315 89  ILE D O     
2036 C CB    . ILE B 90  ? 0.23526 0.29645 0.29017 0.06508  0.08945  0.00552  89  ILE D CB    
2037 C CG1   . ILE B 90  ? 0.25379 0.33974 0.33746 0.06954  0.09623  0.00545  89  ILE D CG1   
2038 C CG2   . ILE B 90  ? 0.31790 0.36293 0.34676 0.06749  0.09979  0.00630  89  ILE D CG2   
2039 C CD1   . ILE B 90  ? 0.30110 0.40288 0.40318 0.06217  0.10834  0.00846  89  ILE D CD1   
2040 N N     . LEU B 91  ? 0.21311 0.23937 0.23232 0.05724  0.06406  0.00268  90  LEU D N     
2041 C CA    . LEU B 91  ? 0.21285 0.22345 0.21179 0.05387  0.05790  0.00161  90  LEU D CA    
2042 C C     . LEU B 91  ? 0.21141 0.21382 0.20824 0.05336  0.04761  -0.00186 90  LEU D C     
2043 O O     . LEU B 91  ? 0.20715 0.21585 0.21772 0.05407  0.04393  -0.00121 90  LEU D O     
2044 C CB    . LEU B 91  ? 0.22930 0.24280 0.23073 0.04654  0.05731  0.00643  90  LEU D CB    
2045 C CG    . LEU B 91  ? 0.26780 0.28710 0.27205 0.04673  0.07047  0.01066  90  LEU D CG    
2046 C CD1   . LEU B 91  ? 0.35320 0.37259 0.36159 0.03951  0.07156  0.01586  90  LEU D CD1   
2047 C CD2   . LEU B 91  ? 0.29397 0.30208 0.27359 0.05346  0.07816  0.01006  90  LEU D CD2   
2048 N N     . LYS B 92  ? 0.25147 0.23985 0.23033 0.05257  0.04354  -0.00582 91  LYS D N     
2049 C CA    . LYS B 92  ? 0.24228 0.22009 0.21809 0.05123  0.03649  -0.01010 91  LYS D CA    
2050 C C     . LYS B 92  ? 0.23967 0.21550 0.21237 0.04395  0.02802  -0.01034 91  LYS D C     
2051 O O     . LYS B 92  ? 0.24699 0.22662 0.21474 0.04184  0.02701  -0.00784 91  LYS D O     
2052 C CB    . LYS B 92  ? 0.25657 0.21939 0.21669 0.05602  0.03967  -0.01735 91  LYS D CB    
2053 C CG    . LYS B 92  ? 0.33654 0.30032 0.29748 0.06522  0.04990  -0.01756 91  LYS D CG    
2054 C CD    . LYS B 92  ? 0.35199 0.32343 0.33124 0.06998  0.05094  -0.01368 91  LYS D CD    
2055 C CE    . LYS B 92  ? 0.33664 0.31008 0.31788 0.08094  0.06148  -0.01444 91  LYS D CE    
2056 N NZ    . LYS B 92  ? 0.55565 0.50703 0.52004 0.08654  0.06532  -0.02150 91  LYS D NZ    
2057 N N     . HIS B 93  ? 0.23457 0.20420 0.21095 0.04087  0.02284  -0.01262 92  HIS D N     
2058 C CA    . HIS B 93  ? 0.22407 0.19394 0.20198 0.03413  0.01558  -0.01316 92  HIS D CA    
2059 C C     . HIS B 93  ? 0.24365 0.20572 0.20895 0.03199  0.01167  -0.02087 92  HIS D C     
2060 O O     . HIS B 93  ? 0.32294 0.27580 0.28859 0.02845  0.00960  -0.02656 92  HIS D O     
2061 C CB    . HIS B 93  ? 0.20512 0.17210 0.19310 0.03152  0.01377  -0.01183 92  HIS D CB    
2062 C CG    . HIS B 93  ? 0.18023 0.15602 0.17887 0.03371  0.01529  -0.00577 92  HIS D CG    
2063 N ND1   . HIS B 93  ? 0.18451 0.16214 0.18623 0.04029  0.01924  -0.00428 92  HIS D ND1   
2064 C CD2   . HIS B 93  ? 0.19671 0.18096 0.20352 0.03055  0.01291  -0.00189 92  HIS D CD2   
2065 C CE1   . HIS B 93  ? 0.16016 0.14887 0.17208 0.04053  0.01782  -0.00025 92  HIS D CE1   
2066 N NE2   . HIS B 93  ? 0.17237 0.16395 0.18649 0.03419  0.01437  0.00083  92  HIS D NE2   
2067 N N     . THR B 94  ? 0.22260 0.18781 0.17576 0.03409  0.01095  -0.02143 93  THR D N     
2068 C CA    . THR B 94  ? 0.25469 0.21316 0.19161 0.03396  0.00715  -0.03036 93  THR D CA    
2069 C C     . THR B 94  ? 0.22088 0.18532 0.15883 0.02849  -0.00355 -0.03409 93  THR D C     
2070 O O     . THR B 94  ? 0.26627 0.22699 0.19375 0.02650  -0.00907 -0.04385 93  THR D O     
2071 C CB    . THR B 94  ? 0.26606 0.22478 0.18515 0.04067  0.01186  -0.02895 93  THR D CB    
2072 O OG1   . THR B 94  ? 0.26332 0.23182 0.18599 0.04196  0.01314  -0.01904 93  THR D OG1   
2073 C CG2   . THR B 94  ? 0.27956 0.23174 0.19623 0.04653  0.02287  -0.02926 93  THR D CG2   
2074 N N     . GLY B 95  ? 0.21458 0.18924 0.16447 0.02658  -0.00674 -0.02741 94  GLY D N     
2075 C CA    . GLY B 95  ? 0.23353 0.21653 0.18862 0.02232  -0.01645 -0.03085 94  GLY D CA    
2076 C C     . GLY B 95  ? 0.22415 0.21725 0.19142 0.02277  -0.01741 -0.02179 94  GLY D C     
2077 O O     . GLY B 95  ? 0.22727 0.21930 0.19945 0.02458  -0.01077 -0.01409 94  GLY D O     
2078 N N     . PRO B 96  ? 0.20568 0.20941 0.17921 0.02106  -0.02588 -0.02357 95  PRO D N     
2079 C CA    . PRO B 96  ? 0.20395 0.21618 0.18912 0.02258  -0.02628 -0.01553 95  PRO D CA    
2080 C C     . PRO B 96  ? 0.20866 0.21854 0.18338 0.02985  -0.02147 -0.00601 95  PRO D C     
2081 O O     . PRO B 96  ? 0.23781 0.24554 0.19449 0.03549  -0.02191 -0.00508 95  PRO D O     
2082 C CB    . PRO B 96  ? 0.22123 0.24760 0.21206 0.02211  -0.03722 -0.02010 95  PRO D CB    
2083 C CG    . PRO B 96  ? 0.25361 0.27877 0.24149 0.01623  -0.04250 -0.03262 95  PRO D CG    
2084 C CD    . PRO B 96  ? 0.23208 0.24130 0.20292 0.01785  -0.03559 -0.03422 95  PRO D CD    
2085 N N     . GLY B 97  ? 0.19748 0.20627 0.18258 0.02936  -0.01588 0.00079  96  GLY D N     
2086 C CA    . GLY B 97  ? 0.20004 0.20470 0.17952 0.03397  -0.00963 0.00948  96  GLY D CA    
2087 C C     . GLY B 97  ? 0.20757 0.20545 0.18757 0.03192  -0.00038 0.01129  96  GLY D C     
2088 O O     . GLY B 97  ? 0.20410 0.19849 0.18430 0.03302  0.00618  0.01753  96  GLY D O     
2089 N N     . ILE B 98  ? 0.19525 0.19148 0.17712 0.02902  0.00062  0.00587  97  ILE D N     
2090 C CA    . ILE B 98  ? 0.20083 0.19493 0.18658 0.02822  0.00822  0.00737  97  ILE D CA    
2091 C C     . ILE B 98  ? 0.17814 0.17439 0.17807 0.02450  0.00986  0.00987  97  ILE D C     
2092 O O     . ILE B 98  ? 0.17322 0.17054 0.18029 0.02192  0.00592  0.00812  97  ILE D O     
2093 C CB    . ILE B 98  ? 0.20439 0.19566 0.18867 0.02808  0.00820  0.00128  97  ILE D CB    
2094 C CG1   . ILE B 98  ? 0.27460 0.26176 0.24206 0.03219  0.00891  -0.00210 97  ILE D CG1   
2095 C CG2   . ILE B 98  ? 0.24683 0.23993 0.24092 0.02793  0.01364  0.00251  97  ILE D CG2   
2096 C CD1   . ILE B 98  ? 0.28615 0.27305 0.24686 0.03621  0.01774  0.00255  97  ILE D CD1   
2097 N N     . LEU B 99  ? 0.17209 0.16902 0.17613 0.02370  0.01629  0.01317  98  LEU D N     
2098 C CA    . LEU B 99  ? 0.17066 0.16975 0.18679 0.01955  0.01791  0.01377  98  LEU D CA    
2099 C C     . LEU B 99  ? 0.14961 0.15492 0.17361 0.01856  0.01968  0.01113  98  LEU D C     
2100 O O     . LEU B 99  ? 0.16440 0.17270 0.18849 0.02006  0.02486  0.01172  98  LEU D O     
2101 C CB    . LEU B 99  ? 0.17677 0.17184 0.19324 0.01840  0.02390  0.01860  98  LEU D CB    
2102 C CG    . LEU B 99  ? 0.15657 0.15217 0.18497 0.01269  0.02667  0.01753  98  LEU D CG    
2103 C CD1   . LEU B 99  ? 0.18709 0.18064 0.21766 0.01186  0.02166  0.01569  98  LEU D CD1   
2104 C CD2   . LEU B 99  ? 0.21247 0.20039 0.23984 0.01132  0.03506  0.02237  98  LEU D CD2   
2105 N N     . SER B 100 ? 0.14662 0.15443 0.17637 0.01732  0.01559  0.00859  99  SER D N     
2106 C CA    . SER B 100 ? 0.12720 0.14178 0.16270 0.01907  0.01509  0.00656  99  SER D CA    
2107 C C     . SER B 100 ? 0.15256 0.17161 0.19463 0.01661  0.01154  0.00496  99  SER D C     
2108 O O     . SER B 100 ? 0.15051 0.16444 0.19035 0.01398  0.00985  0.00495  99  SER D O     
2109 C CB    . SER B 100 ? 0.14711 0.15576 0.17504 0.02334  0.01295  0.00528  99  SER D CB    
2110 O OG    . SER B 100 ? 0.16707 0.18008 0.19868 0.02763  0.01287  0.00453  99  SER D OG    
2111 N N     . MET B 101 ? 0.13853 0.16837 0.18852 0.01820  0.01027  0.00324  100 MET D N     
2112 C CA    . MET B 101 ? 0.14114 0.17688 0.19507 0.01639  0.00549  0.00067  100 MET D CA    
2113 C C     . MET B 101 ? 0.16257 0.19277 0.20700 0.02158  0.00126  0.00176  100 MET D C     
2114 O O     . MET B 101 ? 0.17022 0.19851 0.21115 0.02791  0.00128  0.00362  100 MET D O     
2115 C CB    . MET B 101 ? 0.14340 0.19660 0.21099 0.01637  0.00401  -0.00227 100 MET D CB    
2116 C CG    . MET B 101 ? 0.14448 0.20390 0.22455 0.00926  0.00974  -0.00385 100 MET D CG    
2117 S SD    . MET B 101 ? 0.17827 0.22758 0.25709 -0.00018 0.01101  -0.00630 100 MET D SD    
2118 C CE    . MET B 101 ? 0.20236 0.26497 0.28860 -0.00365 0.00247  -0.01436 100 MET D CE    
2119 N N     . ALA B 102 ? 0.15491 0.18046 0.19416 0.01924  -0.00087 0.00087  101 ALA D N     
2120 C CA    . ALA B 102 ? 0.16485 0.18556 0.19412 0.02410  -0.00364 0.00243  101 ALA D CA    
2121 C C     . ALA B 102 ? 0.16386 0.19793 0.19529 0.02830  -0.00969 0.00044  101 ALA D C     
2122 O O     . ALA B 102 ? 0.17063 0.21843 0.21352 0.02444  -0.01209 -0.00403 101 ALA D O     
2123 C CB    . ALA B 102 ? 0.16448 0.17643 0.18704 0.02043  -0.00239 0.00191  101 ALA D CB    
2124 N N     . ASN B 103 ? 0.16663 0.19750 0.18806 0.03657  -0.01204 0.00386  102 ASN D N     
2125 C CA    . ASN B 103 ? 0.17289 0.21905 0.19556 0.04270  -0.01963 0.00234  102 ASN D CA    
2126 C C     . ASN B 103 ? 0.21728 0.25366 0.22158 0.05213  -0.02127 0.00763  102 ASN D C     
2127 O O     . ASN B 103 ? 0.21098 0.22839 0.20430 0.05278  -0.01491 0.01242  102 ASN D O     
2128 C CB    . ASN B 103 ? 0.16911 0.23027 0.20660 0.04711  -0.02044 0.00222  102 ASN D CB    
2129 C CG    . ASN B 103 ? 0.20452 0.25302 0.23631 0.05514  -0.01511 0.00818  102 ASN D CG    
2130 O OD1   . ASN B 103 ? 0.20488 0.24135 0.22284 0.06296  -0.01495 0.01317  102 ASN D OD1   
2131 N ND2   . ASN B 103 ? 0.17125 0.22034 0.21214 0.05310  -0.00974 0.00746  102 ASN D ND2   
2132 N N     . ALA B 104 ? 0.20500 0.25518 0.20622 0.05949  -0.02979 0.00673  103 ALA D N     
2133 C CA    . ALA B 104 ? 0.22861 0.27012 0.20945 0.07135  -0.03181 0.01325  103 ALA D CA    
2134 C C     . ALA B 104 ? 0.27052 0.31946 0.25409 0.08481  -0.03478 0.01834  103 ALA D C     
2135 O O     . ALA B 104 ? 0.32420 0.37698 0.29492 0.09709  -0.04108 0.02235  103 ALA D O     
2136 C CB    . ALA B 104 ? 0.28732 0.33786 0.25695 0.07202  -0.04042 0.00869  103 ALA D CB    
2137 N N     . GLY B 105 ? 0.24086 0.29116 0.23944 0.08415  -0.02993 0.01861  104 GLY D N     
2138 C CA    . GLY B 105 ? 0.26519 0.32401 0.26934 0.09742  -0.03170 0.02253  104 GLY D CA    
2139 C C     . GLY B 105 ? 0.23975 0.32486 0.26997 0.09418  -0.03446 0.01622  104 GLY D C     
2140 O O     . GLY B 105 ? 0.20908 0.30295 0.25168 0.08086  -0.03420 0.00930  104 GLY D O     
2141 N N     . PRO B 106 ? 0.23332 0.33009 0.27261 0.10668  -0.03550 0.01906  105 PRO D N     
2142 C CA    . PRO B 106 ? 0.24776 0.37005 0.31414 0.10391  -0.03541 0.01362  105 PRO D CA    
2143 C C     . PRO B 106 ? 0.19535 0.34626 0.27853 0.09467  -0.04484 0.00493  105 PRO D C     
2144 O O     . PRO B 106 ? 0.21630 0.37917 0.29380 0.09905  -0.05612 0.00341  105 PRO D O     
2145 C CB    . PRO B 106 ? 0.28059 0.40932 0.35022 0.11989  -0.03609 0.01867  105 PRO D CB    
2146 C CG    . PRO B 106 ? 0.28889 0.38328 0.33231 0.12770  -0.02989 0.02706  105 PRO D CG    
2147 C CD    . PRO B 106 ? 0.24168 0.32504 0.26669 0.12386  -0.03396 0.02813  105 PRO D CD    
2148 N N     . ASN B 107 ? 0.15907 0.31913 0.26143 0.08148  -0.03962 -0.00109 106 ASN D N     
2149 C CA    . ASN B 107 ? 0.15300 0.34065 0.27748 0.07093  -0.04580 -0.01041 106 ASN D CA    
2150 C C     . ASN B 107 ? 0.16775 0.35099 0.27986 0.06237  -0.05352 -0.01577 106 ASN D C     
2151 O O     . ASN B 107 ? 0.20366 0.41024 0.32445 0.06125  -0.06504 -0.02293 106 ASN D O     
2152 C CB    . ASN B 107 ? 0.15822 0.37969 0.30438 0.08025  -0.05372 -0.01244 106 ASN D CB    
2153 C CG    . ASN B 107 ? 0.19202 0.41231 0.34796 0.08784  -0.04349 -0.00700 106 ASN D CG    
2154 O OD1   . ASN B 107 ? 0.20483 0.42493 0.37298 0.08098  -0.03259 -0.00848 106 ASN D OD1   
2155 N ND2   . ASN B 107 ? 0.26024 0.47705 0.40842 0.10236  -0.04576 -0.00063 106 ASN D ND2   
2156 N N     . THR B 108 ? 0.17007 0.32419 0.26201 0.05671  -0.04732 -0.01305 107 THR D N     
2157 C CA    . THR B 108 ? 0.18505 0.33201 0.26385 0.04928  -0.05221 -0.01801 107 THR D CA    
2158 C C     . THR B 108 ? 0.19428 0.32350 0.27303 0.03512  -0.04279 -0.02021 107 THR D C     
2159 O O     . THR B 108 ? 0.24424 0.35589 0.30598 0.03174  -0.04179 -0.02042 107 THR D O     
2160 C CB    . THR B 108 ? 0.22096 0.35028 0.27091 0.05983  -0.05514 -0.01158 107 THR D CB    
2161 O OG1   . THR B 108 ? 0.20791 0.31041 0.24568 0.06157  -0.04423 -0.00339 107 THR D OG1   
2162 C CG2   . THR B 108 ? 0.21691 0.36263 0.26253 0.07628  -0.06566 -0.00831 107 THR D CG2   
2163 N N     . ASN B 109 ? 0.18267 0.31710 0.28022 0.02754  -0.03552 -0.02172 108 ASN D N     
2164 C CA    . ASN B 109 ? 0.17261 0.29052 0.26957 0.01605  -0.02661 -0.02260 108 ASN D CA    
2165 C C     . ASN B 109 ? 0.15891 0.27942 0.25909 0.00505  -0.03016 -0.03176 108 ASN D C     
2166 O O     . ASN B 109 ? 0.16551 0.30771 0.28180 0.00056  -0.03659 -0.03994 108 ASN D O     
2167 C CB    . ASN B 109 ? 0.17305 0.29608 0.28716 0.01207  -0.01739 -0.02117 108 ASN D CB    
2168 C CG    . ASN B 109 ? 0.15028 0.26758 0.25878 0.02233  -0.01295 -0.01375 108 ASN D CG    
2169 O OD1   . ASN B 109 ? 0.17740 0.27372 0.26927 0.02460  -0.00904 -0.00884 108 ASN D OD1   
2170 N ND2   . ASN B 109 ? 0.17440 0.31095 0.29770 0.02870  -0.01350 -0.01367 108 ASN D ND2   
2171 N N     . GLY B 110 ? 0.15054 0.24941 0.23639 0.00069  -0.02590 -0.03121 109 GLY D N     
2172 C CA    . GLY B 110 ? 0.17259 0.26857 0.25966 -0.00974 -0.02694 -0.04023 109 GLY D CA    
2173 C C     . GLY B 110 ? 0.18475 0.26121 0.27244 -0.01704 -0.01539 -0.03774 109 GLY D C     
2174 O O     . GLY B 110 ? 0.17868 0.25825 0.28194 -0.02330 -0.00861 -0.03760 109 GLY D O     
2175 N N     . SER B 111 ? 0.16570 0.22232 0.23646 -0.01551 -0.01250 -0.03534 110 SER D N     
2176 C CA    . SER B 111 ? 0.15364 0.19154 0.22263 -0.01895 -0.00248 -0.03129 110 SER D CA    
2177 C C     . SER B 111 ? 0.15506 0.18104 0.21115 -0.01086 0.00025  -0.02230 110 SER D C     
2178 O O     . SER B 111 ? 0.16557 0.18076 0.22158 -0.01114 0.00705  -0.01730 110 SER D O     
2179 C CB    . SER B 111 ? 0.18306 0.20856 0.24850 -0.02623 -0.00011 -0.03878 110 SER D CB    
2180 O OG    . SER B 111 ? 0.20020 0.22152 0.24919 -0.02158 -0.00516 -0.04133 110 SER D OG    
2181 N N     . GLN B 112 ? 0.17085 0.19792 0.21588 -0.00381 -0.00460 -0.02023 111 GLN D N     
2182 C CA    . GLN B 112 ? 0.16024 0.17619 0.19642 0.00141  -0.00103 -0.01313 111 GLN D CA    
2183 C C     . GLN B 112 ? 0.14447 0.16236 0.18609 0.00381  0.00141  -0.00759 111 GLN D C     
2184 O O     . GLN B 112 ? 0.15678 0.18525 0.20489 0.00537  -0.00051 -0.00762 111 GLN D O     
2185 C CB    . GLN B 112 ? 0.15028 0.16422 0.17341 0.00762  -0.00430 -0.01143 111 GLN D CB    
2186 C CG    . GLN B 112 ? 0.18465 0.19227 0.19708 0.00639  -0.00453 -0.01614 111 GLN D CG    
2187 C CD    . GLN B 112 ? 0.19096 0.19170 0.18832 0.01281  -0.00363 -0.01193 111 GLN D CD    
2188 O OE1   . GLN B 112 ? 0.21249 0.20725 0.20993 0.01520  0.00077  -0.00572 111 GLN D OE1   
2189 N NE2   . GLN B 112 ? 0.19195 0.19331 0.17583 0.01542  -0.00748 -0.01547 111 GLN D NE2   
2190 N N     . PHE B 113 ? 0.15287 0.16128 0.19152 0.00475  0.00552  -0.00335 112 PHE D N     
2191 C CA    . PHE B 113 ? 0.15632 0.16477 0.19683 0.00673  0.00764  0.00069  112 PHE D CA    
2192 C C     . PHE B 113 ? 0.14907 0.15057 0.18375 0.00951  0.00789  0.00364  112 PHE D C     
2193 O O     . PHE B 113 ? 0.15033 0.14727 0.18233 0.00933  0.00841  0.00337  112 PHE D O     
2194 C CB    . PHE B 113 ? 0.15611 0.16185 0.20126 0.00341  0.01268  0.00191  112 PHE D CB    
2195 C CG    . PHE B 113 ? 0.16018 0.15581 0.20254 0.00267  0.01548  0.00309  112 PHE D CG    
2196 C CD1   . PHE B 113 ? 0.18283 0.17404 0.22678 -0.00139 0.01706  -0.00098 112 PHE D CD1   
2197 C CD2   . PHE B 113 ? 0.17446 0.16560 0.21276 0.00672  0.01612  0.00757  112 PHE D CD2   
2198 C CE1   . PHE B 113 ? 0.19964 0.18006 0.24074 -0.00038 0.02074  0.00027  112 PHE D CE1   
2199 C CE2   . PHE B 113 ? 0.19372 0.17766 0.23118 0.00813  0.01849  0.00920  112 PHE D CE2   
2200 C CZ    . PHE B 113 ? 0.21639 0.19388 0.25507 0.00500  0.02160  0.00588  112 PHE D CZ    
2201 N N     . PHE B 114 ? 0.13633 0.13770 0.16993 0.01163  0.00803  0.00571  113 PHE D N     
2202 C CA    . PHE B 114 ? 0.15033 0.14789 0.18161 0.01267  0.00739  0.00684  113 PHE D CA    
2203 C C     . PHE B 114 ? 0.14449 0.14256 0.17394 0.01405  0.00729  0.00817  113 PHE D C     
2204 O O     . PHE B 114 ? 0.15928 0.15889 0.18683 0.01508  0.00879  0.00859  113 PHE D O     
2205 C CB    . PHE B 114 ? 0.15517 0.14990 0.18371 0.01374  0.00639  0.00616  113 PHE D CB    
2206 C CG    . PHE B 114 ? 0.14526 0.13984 0.17108 0.01640  0.00592  0.00561  113 PHE D CG    
2207 C CD1   . PHE B 114 ? 0.14393 0.14292 0.17033 0.01891  0.00549  0.00564  113 PHE D CD1   
2208 C CD2   . PHE B 114 ? 0.15427 0.14505 0.17750 0.01673  0.00567  0.00418  113 PHE D CD2   
2209 C CE1   . PHE B 114 ? 0.15629 0.15549 0.18126 0.02330  0.00599  0.00551  113 PHE D CE1   
2210 C CE2   . PHE B 114 ? 0.16659 0.15447 0.18605 0.02004  0.00659  0.00309  113 PHE D CE2   
2211 C CZ    . PHE B 114 ? 0.16326 0.15516 0.18386 0.02401  0.00733  0.00438  113 PHE D CZ    
2212 N N     . ILE B 115 ? 0.16168 0.15966 0.19160 0.01468  0.00565  0.00882  114 ILE D N     
2213 C CA    . ILE B 115 ? 0.16455 0.16420 0.19014 0.01723  0.00338  0.00964  114 ILE D CA    
2214 C C     . ILE B 115 ? 0.15180 0.15329 0.17797 0.01603  -0.00070 0.00561  114 ILE D C     
2215 O O     . ILE B 115 ? 0.16109 0.16492 0.19471 0.01388  -0.00173 0.00435  114 ILE D O     
2216 C CB    . ILE B 115 ? 0.17045 0.17100 0.19734 0.02001  0.00324  0.01322  114 ILE D CB    
2217 C CG1   . ILE B 115 ? 0.18156 0.17626 0.20918 0.01961  0.00897  0.01631  114 ILE D CG1   
2218 C CG2   . ILE B 115 ? 0.19018 0.19306 0.20872 0.02435  -0.00020 0.01455  114 ILE D CG2   
2219 C CD1   . ILE B 115 ? 0.21304 0.20480 0.24219 0.02343  0.01053  0.02025  114 ILE D CD1   
2220 N N     . CYS B 116 ? 0.17840 0.17818 0.19744 0.01683  -0.00192 0.00292  115 CYS D N     
2221 C CA    . CYS B 116 ? 0.17282 0.17187 0.19224 0.01427  -0.00531 -0.00268 115 CYS D CA    
2222 C C     . CYS B 116 ? 0.17844 0.18600 0.20081 0.01418  -0.01157 -0.00471 115 CYS D C     
2223 O O     . CYS B 116 ? 0.20336 0.21501 0.21939 0.01884  -0.01416 -0.00201 115 CYS D O     
2224 C CB    . CYS B 116 ? 0.20433 0.19773 0.21318 0.01597  -0.00464 -0.00614 115 CYS D CB    
2225 S SG    . CYS B 116 ? 0.24838 0.23574 0.25671 0.01812  0.00174  -0.00396 115 CYS D SG    
2226 N N     . THR B 117 ? 0.18465 0.19544 0.21721 0.00913  -0.01375 -0.00929 116 THR D N     
2227 C CA    . THR B 117 ? 0.19669 0.21941 0.23505 0.00819  -0.02144 -0.01370 116 THR D CA    
2228 C C     . THR B 117 ? 0.22445 0.24467 0.26037 0.00298  -0.02513 -0.02320 116 THR D C     
2229 O O     . THR B 117 ? 0.23458 0.26595 0.27933 -0.00075 -0.03207 -0.02972 116 THR D O     
2230 C CB    . THR B 117 ? 0.18678 0.21930 0.24326 0.00591  -0.02093 -0.01239 116 THR D CB    
2231 O OG1   . THR B 117 ? 0.19884 0.22443 0.26369 -0.00108 -0.01470 -0.01449 116 THR D OG1   
2232 C CG2   . THR B 117 ? 0.20382 0.23599 0.25981 0.01186  -0.01699 -0.00410 116 THR D CG2   
2233 N N     . ALA B 118 ? 0.20154 0.20768 0.22671 0.00274  -0.02051 -0.02473 117 ALA D N     
2234 C CA    . ALA B 118 ? 0.20768 0.20563 0.22794 -0.00184 -0.02171 -0.03422 117 ALA D CA    
2235 C C     . ALA B 118 ? 0.20900 0.19346 0.21341 0.00330  -0.01625 -0.03284 117 ALA D C     
2236 O O     . ALA B 118 ? 0.23043 0.21356 0.23250 0.00838  -0.01135 -0.02494 117 ALA D O     
2237 C CB    . ALA B 118 ? 0.25324 0.24481 0.28743 -0.01062 -0.01741 -0.03796 117 ALA D CB    
2238 N N     . LYS B 119 ? 0.23146 0.20646 0.22638 0.00168  -0.01679 -0.04152 118 LYS D N     
2239 C CA    . LYS B 119 ? 0.23134 0.19204 0.21410 0.00672  -0.00966 -0.04103 118 LYS D CA    
2240 C C     . LYS B 119 ? 0.28850 0.23799 0.27969 0.00532  -0.00218 -0.03727 118 LYS D C     
2241 O O     . LYS B 119 ? 0.32283 0.26587 0.32236 -0.00185 -0.00125 -0.04127 118 LYS D O     
2242 C CB    . LYS B 119 ? 0.29116 0.24252 0.26044 0.00537  -0.01178 -0.05279 118 LYS D CB    
2243 C CG    . LYS B 119 ? 0.33431 0.26933 0.29063 0.01145  -0.00340 -0.05401 118 LYS D CG    
2244 C CD    . LYS B 119 ? 0.34647 0.27005 0.28746 0.00972  -0.00520 -0.06751 118 LYS D CD    
2245 C CE    . LYS B 119 ? 0.36237 0.27248 0.31091 -0.00046 -0.00519 -0.07778 118 LYS D CE    
2246 N NZ    . LYS B 119 ? 0.38708 0.28119 0.31838 -0.00144 -0.00480 -0.09203 118 LYS D NZ    
2247 N N     . THR B 120 ? 0.23438 0.18277 0.22415 0.01211  0.00313  -0.02924 119 THR D N     
2248 C CA    . THR B 120 ? 0.24828 0.18829 0.24346 0.01343  0.00891  -0.02389 119 THR D CA    
2249 C C     . THR B 120 ? 0.26237 0.19406 0.24988 0.02204  0.01444  -0.02218 119 THR D C     
2250 O O     . THR B 120 ? 0.23987 0.17760 0.23031 0.02797  0.01633  -0.01526 119 THR D O     
2251 C CB    . THR B 120 ? 0.24460 0.19518 0.24850 0.01364  0.00835  -0.01586 119 THR D CB    
2252 O OG1   . THR B 120 ? 0.21423 0.17565 0.21654 0.01872  0.00748  -0.01176 119 THR D OG1   
2253 C CG2   . THR B 120 ? 0.24074 0.20006 0.25380 0.00672  0.00423  -0.01718 119 THR D CG2   
2254 N N     . GLU B 121 ? 0.27977 0.19800 0.25839 0.02280  0.01698  -0.02936 120 GLU D N     
2255 C CA    . GLU B 121 ? 0.30308 0.21502 0.27420 0.03236  0.02272  -0.02878 120 GLU D CA    
2256 C C     . GLU B 121 ? 0.25562 0.15943 0.23015 0.03937  0.02815  -0.02199 120 GLU D C     
2257 O O     . GLU B 121 ? 0.28433 0.19187 0.25846 0.04913  0.03162  -0.01843 120 GLU D O     
2258 C CB    . GLU B 121 ? 0.36224 0.25964 0.32056 0.03183  0.02465  -0.03948 120 GLU D CB    
2259 C CG    . GLU B 121 ? 0.39300 0.26769 0.34989 0.02671  0.02806  -0.04587 120 GLU D CG    
2260 C CD    . GLU B 121 ? 0.44729 0.32326 0.41420 0.01398  0.02338  -0.04885 120 GLU D CD    
2261 O OE1   . GLU B 121 ? 0.39999 0.29409 0.37230 0.00830  0.01529  -0.05004 120 GLU D OE1   
2262 O OE2   . GLU B 121 ? 0.58625 0.44400 0.55634 0.01005  0.02902  -0.04965 120 GLU D OE2   
2263 N N     . TRP B 122 ? 0.25102 0.14558 0.22933 0.03546  0.02912  -0.01923 121 TRP D N     
2264 C CA    . TRP B 122 ? 0.26144 0.14772 0.23936 0.04402  0.03380  -0.01125 121 TRP D CA    
2265 C C     . TRP B 122 ? 0.24877 0.15557 0.23292 0.05011  0.03001  -0.00327 121 TRP D C     
2266 O O     . TRP B 122 ? 0.30004 0.20517 0.28321 0.05987  0.03187  0.00314  121 TRP D O     
2267 C CB    . TRP B 122 ? 0.28562 0.15527 0.26368 0.03814  0.03743  -0.00928 121 TRP D CB    
2268 C CG    . TRP B 122 ? 0.24871 0.13224 0.23520 0.02909  0.03277  -0.00754 121 TRP D CG    
2269 C CD1   . TRP B 122 ? 0.26481 0.15782 0.25365 0.03165  0.03132  0.00035  121 TRP D CD1   
2270 C CD2   . TRP B 122 ? 0.24924 0.13955 0.24261 0.01733  0.02885  -0.01447 121 TRP D CD2   
2271 N NE1   . TRP B 122 ? 0.25449 0.15769 0.25098 0.02258  0.02832  -0.00089 121 TRP D NE1   
2272 C CE2   . TRP B 122 ? 0.25397 0.15688 0.25475 0.01400  0.02654  -0.00951 121 TRP D CE2   
2273 C CE3   . TRP B 122 ? 0.27560 0.16318 0.26926 0.00983  0.02656  -0.02504 121 TRP D CE3   
2274 C CZ2   . TRP B 122 ? 0.23606 0.15022 0.24666 0.00458  0.02251  -0.01379 121 TRP D CZ2   
2275 C CZ3   . TRP B 122 ? 0.26363 0.16458 0.26681 0.00030  0.02078  -0.02948 121 TRP D CZ3   
2276 C CH2   . TRP B 122 ? 0.25088 0.16486 0.26347 -0.00190 0.01926  -0.02349 121 TRP D CH2   
2277 N N     . LEU B 123 ? 0.21920 0.14487 0.20955 0.04476  0.02450  -0.00374 122 LEU D N     
2278 C CA    . LEU B 123 ? 0.22008 0.16484 0.21748 0.04837  0.02105  0.00147  122 LEU D CA    
2279 C C     . LEU B 123 ? 0.22912 0.18593 0.23012 0.05488  0.02236  0.00090  122 LEU D C     
2280 O O     . LEU B 123 ? 0.21690 0.19067 0.22660 0.05802  0.02006  0.00416  122 LEU D O     
2281 C CB    . LEU B 123 ? 0.20911 0.16542 0.21171 0.03969  0.01649  0.00117  122 LEU D CB    
2282 C CG    . LEU B 123 ? 0.21523 0.16356 0.21745 0.03336  0.01621  0.00199  122 LEU D CG    
2283 C CD1   . LEU B 123 ? 0.22129 0.18151 0.22939 0.02668  0.01240  0.00148  122 LEU D CD1   
2284 C CD2   . LEU B 123 ? 0.25165 0.19486 0.25063 0.03902  0.01780  0.00801  122 LEU D CD2   
2285 N N     . ASP B 124 ? 0.22539 0.17434 0.22039 0.05663  0.02649  -0.00389 123 ASP D N     
2286 C CA    . ASP B 124 ? 0.22601 0.18594 0.22430 0.06308  0.03021  -0.00431 123 ASP D CA    
2287 C C     . ASP B 124 ? 0.23540 0.20259 0.24159 0.07432  0.03171  0.00040  123 ASP D C     
2288 O O     . ASP B 124 ? 0.26173 0.21499 0.26301 0.08098  0.03325  0.00252  123 ASP D O     
2289 C CB    . ASP B 124 ? 0.22995 0.17582 0.21623 0.06491  0.03565  -0.01085 123 ASP D CB    
2290 C CG    . ASP B 124 ? 0.25253 0.19685 0.23037 0.05597  0.03279  -0.01595 123 ASP D CG    
2291 O OD1   . ASP B 124 ? 0.25317 0.20865 0.23602 0.04955  0.02785  -0.01334 123 ASP D OD1   
2292 O OD2   . ASP B 124 ? 0.29740 0.22850 0.26241 0.05638  0.03543  -0.02300 123 ASP D OD2   
2293 N N     . GLY B 125 ? 0.21704 0.20647 0.23622 0.07673  0.03147  0.00222  124 GLY D N     
2294 C CA    . GLY B 125 ? 0.22971 0.23251 0.25995 0.08766  0.03100  0.00597  124 GLY D CA    
2295 C C     . GLY B 125 ? 0.21501 0.22607 0.24954 0.08796  0.02282  0.01014  124 GLY D C     
2296 O O     . GLY B 125 ? 0.25691 0.28287 0.30083 0.09774  0.02002  0.01313  124 GLY D O     
2297 N N     . LYS B 126 ? 0.21167 0.21554 0.23979 0.07842  0.01868  0.01017  125 LYS D N     
2298 C CA    . LYS B 126 ? 0.21196 0.22306 0.24120 0.07850  0.01160  0.01340  125 LYS D CA    
2299 C C     . LYS B 126 ? 0.17543 0.19853 0.21099 0.06700  0.00743  0.01094  125 LYS D C     
2300 O O     . LYS B 126 ? 0.23313 0.26742 0.27192 0.06679  0.00118  0.01163  125 LYS D O     
2301 C CB    . LYS B 126 ? 0.23915 0.22658 0.25279 0.07969  0.01263  0.01677  125 LYS D CB    
2302 C CG    . LYS B 126 ? 0.40870 0.38306 0.41566 0.09367  0.01674  0.02093  125 LYS D CG    
2303 C CD    . LYS B 126 ? 0.54181 0.48787 0.53332 0.09391  0.02120  0.02442  125 LYS D CD    
2304 C CE    . LYS B 126 ? 0.49479 0.42455 0.47942 0.10834  0.02711  0.02857  125 LYS D CE    
2305 N NZ    . LYS B 126 ? 0.66621 0.57151 0.63604 0.10929  0.03107  0.03442  125 LYS D NZ    
2306 N N     . HIS B 127 ? 0.16896 0.18830 0.20424 0.05814  0.01060  0.00803  126 HIS D N     
2307 C CA    . HIS B 127 ? 0.16194 0.18957 0.20278 0.04836  0.00849  0.00635  126 HIS D CA    
2308 C C     . HIS B 127 ? 0.17340 0.20860 0.22139 0.04543  0.01369  0.00467  126 HIS D C     
2309 O O     . HIS B 127 ? 0.18516 0.21177 0.22645 0.04791  0.01875  0.00405  126 HIS D O     
2310 C CB    . HIS B 127 ? 0.16195 0.17439 0.19270 0.04186  0.00826  0.00627  126 HIS D CB    
2311 C CG    . HIS B 127 ? 0.17755 0.18189 0.20124 0.04381  0.00561  0.00857  126 HIS D CG    
2312 N ND1   . HIS B 127 ? 0.17953 0.18898 0.20350 0.04092  0.00173  0.00886  126 HIS D ND1   
2313 C CD2   . HIS B 127 ? 0.20307 0.19312 0.21787 0.04913  0.00756  0.01099  126 HIS D CD2   
2314 C CE1   . HIS B 127 ? 0.19080 0.19002 0.20493 0.04489  0.00152  0.01201  126 HIS D CE1   
2315 N NE2   . HIS B 127 ? 0.21511 0.20208 0.22420 0.04980  0.00538  0.01387  126 HIS D NE2   
2316 N N     . VAL B 128 ? 0.14534 0.19513 0.20570 0.03995  0.01335  0.00359  127 VAL D N     
2317 C CA    . VAL B 128 ? 0.14904 0.20576 0.21708 0.03687  0.02054  0.00320  127 VAL D CA    
2318 C C     . VAL B 128 ? 0.12225 0.16591 0.17981 0.03054  0.02337  0.00431  127 VAL D C     
2319 O O     . VAL B 128 ? 0.13380 0.17557 0.19221 0.02425  0.02085  0.00431  127 VAL D O     
2320 C CB    . VAL B 128 ? 0.13851 0.21621 0.22701 0.03256  0.02039  0.00115  127 VAL D CB    
2321 C CG1   . VAL B 128 ? 0.16016 0.24185 0.25631 0.02783  0.03087  0.00184  127 VAL D CG1   
2322 C CG2   . VAL B 128 ? 0.15204 0.24728 0.25253 0.04105  0.01621  0.00012  127 VAL D CG2   
2323 N N     . VAL B 129 ? 0.14088 0.17558 0.18754 0.03334  0.02842  0.00503  128 VAL D N     
2324 C CA    . VAL B 129 ? 0.14795 0.17271 0.18333 0.02987  0.03079  0.00674  128 VAL D CA    
2325 C C     . VAL B 129 ? 0.15249 0.18336 0.19525 0.02612  0.03883  0.00934  128 VAL D C     
2326 O O     . VAL B 129 ? 0.17062 0.20999 0.22079 0.02824  0.04617  0.00949  128 VAL D O     
2327 C CB    . VAL B 129 ? 0.15825 0.17230 0.17711 0.03486  0.03253  0.00538  128 VAL D CB    
2328 C CG1   . VAL B 129 ? 0.22461 0.23170 0.23052 0.03336  0.03454  0.00770  128 VAL D CG1   
2329 C CG2   . VAL B 129 ? 0.18108 0.18618 0.19379 0.03639  0.02593  0.00221  128 VAL D CG2   
2330 N N     . PHE B 130 ? 0.14557 0.17124 0.18705 0.02069  0.03891  0.01169  129 PHE D N     
2331 C CA    . PHE B 130 ? 0.18043 0.20819 0.22912 0.01608  0.04831  0.01468  129 PHE D CA    
2332 C C     . PHE B 130 ? 0.19205 0.20542 0.22654 0.01564  0.05198  0.02010  129 PHE D C     
2333 O O     . PHE B 130 ? 0.21195 0.22241 0.25047 0.01166  0.06141  0.02386  129 PHE D O     
2334 C CB    . PHE B 130 ? 0.17873 0.21718 0.24766 0.00854  0.04699  0.01150  129 PHE D CB    
2335 C CG    . PHE B 130 ? 0.17060 0.20184 0.23678 0.00506  0.03980  0.01021  129 PHE D CG    
2336 C CD1   . PHE B 130 ? 0.14717 0.18006 0.21090 0.00767  0.02998  0.00711  129 PHE D CD1   
2337 C CD2   . PHE B 130 ? 0.17805 0.19863 0.24271 0.00002  0.04450  0.01276  129 PHE D CD2   
2338 C CE1   . PHE B 130 ? 0.16389 0.18977 0.22405 0.00513  0.02522  0.00613  129 PHE D CE1   
2339 C CE2   . PHE B 130 ? 0.18502 0.19831 0.24694 -0.00199 0.03921  0.01132  129 PHE D CE2   
2340 C CZ    . PHE B 130 ? 0.17065 0.18748 0.23045 0.00048  0.02965  0.00777  129 PHE D CZ    
2341 N N     . GLY B 131 ? 0.18188 0.18643 0.20065 0.01987  0.04545  0.02092  130 GLY D N     
2342 C CA    . GLY B 131 ? 0.22827 0.22141 0.23298 0.02208  0.04827  0.02695  130 GLY D CA    
2343 C C     . GLY B 131 ? 0.20144 0.19087 0.19082 0.02772  0.03916  0.02588  130 GLY D C     
2344 O O     . GLY B 131 ? 0.19255 0.18597 0.18272 0.02840  0.03233  0.02020  130 GLY D O     
2345 N N     . LYS B 132 ? 0.21047 0.19229 0.18707 0.03170  0.03886  0.03130  131 LYS D N     
2346 C CA    . LYS B 132 ? 0.23099 0.21344 0.19728 0.03628  0.02824  0.02933  131 LYS D CA    
2347 C C     . LYS B 132 ? 0.24033 0.21735 0.20136 0.04028  0.02732  0.03616  131 LYS D C     
2348 O O     . LYS B 132 ? 0.25141 0.21961 0.20863 0.04150  0.03655  0.04358  131 LYS D O     
2349 C CB    . LYS B 132 ? 0.26835 0.25020 0.21605 0.04173  0.02662  0.02685  131 LYS D CB    
2350 C CG    . LYS B 132 ? 0.34386 0.31803 0.27207 0.04815  0.03412  0.03447  131 LYS D CG    
2351 C CD    . LYS B 132 ? 0.36102 0.33428 0.26818 0.05367  0.03225  0.03014  131 LYS D CD    
2352 C CE    . LYS B 132 ? 0.42481 0.38919 0.30799 0.06112  0.04187  0.03790  131 LYS D CE    
2353 N NZ    . LYS B 132 ? 0.48689 0.45030 0.34884 0.06607  0.03960  0.03113  131 LYS D NZ    
2354 N N     . VAL B 133 ? 0.24128 0.22345 0.20309 0.04263  0.01690  0.03378  132 VAL D N     
2355 C CA    . VAL B 133 ? 0.23752 0.21715 0.19494 0.04907  0.01452  0.04026  132 VAL D CA    
2356 C C     . VAL B 133 ? 0.28513 0.25903 0.21924 0.05841  0.01636  0.04714  132 VAL D C     
2357 O O     . VAL B 133 ? 0.27320 0.25118 0.19333 0.06140  0.01142  0.04328  132 VAL D O     
2358 C CB    . VAL B 133 ? 0.21876 0.20999 0.18464 0.04972  0.00250  0.03499  132 VAL D CB    
2359 C CG1   . VAL B 133 ? 0.23526 0.22754 0.19645 0.05932  -0.00134 0.04192  132 VAL D CG1   
2360 C CG2   . VAL B 133 ? 0.20968 0.20338 0.19530 0.04191  0.00322  0.03049  132 VAL D CG2   
2361 N N     . LYS B 134 ? 0.27424 0.23656 0.20199 0.06353  0.02415  0.05741  133 LYS D N     
2362 C CA    . LYS B 134 ? 0.33630 0.29009 0.23900 0.07459  0.02721  0.06688  133 LYS D CA    
2363 C C     . LYS B 134 ? 0.34521 0.30471 0.24197 0.08561  0.01602  0.07065  133 LYS D C     
2364 O O     . LYS B 134 ? 0.42347 0.39124 0.30363 0.09360  0.00586  0.06948  133 LYS D O     
2365 C CB    . LYS B 134 ? 0.38915 0.32438 0.29003 0.07323  0.04453  0.07670  133 LYS D CB    
2366 C CG    . LYS B 134 ? 0.49032 0.41174 0.36296 0.08448  0.05233  0.08884  133 LYS D CG    
2367 C CD    . LYS B 134 ? 0.48896 0.39061 0.36364 0.07998  0.07223  0.09758  133 LYS D CD    
2368 C CE    . LYS B 134 ? 0.51910 0.42463 0.40510 0.06820  0.08157  0.09137  133 LYS D CE    
2369 N NZ    . LYS B 134 ? 0.64178 0.53170 0.51233 0.07030  0.09949  0.10120  133 LYS D NZ    
2370 N N     . GLU B 135 ? 0.34022 0.29573 0.24996 0.08687  0.01792  0.07492  134 GLU D N     
2371 C CA    . GLU B 135 ? 0.33422 0.29714 0.24327 0.09836  0.00821  0.07896  134 GLU D CA    
2372 C C     . GLU B 135 ? 0.31564 0.29014 0.25194 0.09156  0.00297  0.07110  134 GLU D C     
2373 O O     . GLU B 135 ? 0.31179 0.28077 0.26251 0.08059  0.01021  0.06677  134 GLU D O     
2374 C CB    . GLU B 135 ? 0.37626 0.31941 0.27347 0.10911  0.01862  0.09358  134 GLU D CB    
2375 C CG    . GLU B 135 ? 0.51913 0.44961 0.39119 0.11320  0.02686  0.10020  134 GLU D CG    
2376 C CD    . GLU B 135 ? 0.74004 0.67800 0.59537 0.12624  0.01727  0.10332  134 GLU D CD    
2377 O OE1   . GLU B 135 ? 0.77601 0.73256 0.62521 0.12942  0.00228  0.09673  134 GLU D OE1   
2378 O OE2   . GLU B 135 ? 0.80679 0.73213 0.65556 0.13315  0.02448  0.11171  134 GLU D OE2   
2379 N N     . GLY B 136 ? 0.32908 0.32123 0.27209 0.09825  -0.00981 0.06885  135 GLY D N     
2380 C CA    . GLY B 136 ? 0.30414 0.30713 0.27241 0.09367  -0.01286 0.06309  135 GLY D CA    
2381 C C     . GLY B 136 ? 0.27027 0.28842 0.25347 0.08169  -0.01967 0.05023  135 GLY D C     
2382 O O     . GLY B 136 ? 0.23270 0.25369 0.23480 0.07483  -0.01720 0.04576  135 GLY D O     
2383 N N     . MET B 137 ? 0.24186 0.26780 0.21568 0.07906  -0.02719 0.04396  136 MET D N     
2384 C CA    . MET B 137 ? 0.21776 0.25542 0.20613 0.06798  -0.03276 0.03196  136 MET D CA    
2385 C C     . MET B 137 ? 0.22958 0.28670 0.23940 0.06866  -0.04099 0.02803  136 MET D C     
2386 O O     . MET B 137 ? 0.21061 0.27321 0.23831 0.05891  -0.04026 0.02087  136 MET D O     
2387 C CB    . MET B 137 ? 0.24125 0.28170 0.21434 0.06599  -0.03912 0.02513  136 MET D CB    
2388 C CG    . MET B 137 ? 0.24562 0.29075 0.23136 0.05375  -0.04130 0.01336  136 MET D CG    
2389 S SD    . MET B 137 ? 0.24611 0.27553 0.23818 0.04443  -0.02799 0.01361  136 MET D SD    
2390 C CE    . MET B 137 ? 0.23533 0.27241 0.24817 0.03363  -0.03094 0.00356  136 MET D CE    
2391 N N     . ASN B 138 ? 0.23147 0.29871 0.24030 0.08093  -0.04747 0.03369  137 ASN D N     
2392 C CA    . ASN B 138 ? 0.23705 0.32640 0.26963 0.08317  -0.05487 0.03062  137 ASN D CA    
2393 C C     . ASN B 138 ? 0.20823 0.29122 0.25880 0.08026  -0.04382 0.03313  137 ASN D C     
2394 O O     . ASN B 138 ? 0.21037 0.30909 0.28427 0.07573  -0.04566 0.02751  137 ASN D O     
2395 C CB    . ASN B 138 ? 0.26770 0.37154 0.29433 0.09952  -0.06557 0.03668  137 ASN D CB    
2396 C CG    . ASN B 138 ? 0.33316 0.41844 0.34567 0.11311  -0.05653 0.05139  137 ASN D CG    
2397 O OD1   . ASN B 138 ? 0.36893 0.42935 0.36379 0.11125  -0.04529 0.05691  137 ASN D OD1   
2398 N ND2   . ASN B 138 ? 0.34684 0.44074 0.36850 0.12279  -0.05923 0.05612  137 ASN D ND2   
2399 N N     . ILE B 139 ? 0.20995 0.26973 0.24984 0.08181  -0.03168 0.04053  138 ILE D N     
2400 C CA    . ILE B 139 ? 0.20689 0.25752 0.25953 0.07804  -0.02092 0.04107  138 ILE D CA    
2401 C C     . ILE B 139 ? 0.20886 0.25832 0.26918 0.06343  -0.01784 0.03233  138 ILE D C     
2402 O O     . ILE B 139 ? 0.17488 0.22916 0.25123 0.05930  -0.01418 0.02897  138 ILE D O     
2403 C CB    . ILE B 139 ? 0.21116 0.23655 0.24954 0.08235  -0.00951 0.04958  138 ILE D CB    
2404 C CG1   . ILE B 139 ? 0.29136 0.31326 0.31907 0.09853  -0.01065 0.06039  138 ILE D CG1   
2405 C CG2   . ILE B 139 ? 0.23538 0.25033 0.28446 0.07899  0.00088  0.04860  138 ILE D CG2   
2406 C CD1   . ILE B 139 ? 0.30678 0.34766 0.34933 0.10977  -0.01734 0.06227  138 ILE D CD1   
2407 N N     . VAL B 140 ? 0.18610 0.22884 0.23418 0.05661  -0.01861 0.02909  139 VAL D N     
2408 C CA    . VAL B 140 ? 0.18984 0.23069 0.24334 0.04484  -0.01617 0.02185  139 VAL D CA    
2409 C C     . VAL B 140 ? 0.16697 0.22536 0.23705 0.04012  -0.02247 0.01473  139 VAL D C     
2410 O O     . VAL B 140 ? 0.16501 0.22332 0.24660 0.03327  -0.01758 0.01138  139 VAL D O     
2411 C CB    . VAL B 140 ? 0.17764 0.20842 0.21563 0.04052  -0.01528 0.02025  139 VAL D CB    
2412 C CG1   . VAL B 140 ? 0.22211 0.25020 0.26540 0.03063  -0.01272 0.01390  139 VAL D CG1   
2413 C CG2   . VAL B 140 ? 0.20509 0.22055 0.23184 0.04353  -0.00741 0.02694  139 VAL D CG2   
2414 N N     . GLU B 141 ? 0.18586 0.25947 0.25714 0.04352  -0.03305 0.01212  140 GLU D N     
2415 C CA    . GLU B 141 ? 0.18404 0.27655 0.27451 0.03753  -0.03949 0.00390  140 GLU D CA    
2416 C C     . GLU B 141 ? 0.16438 0.26891 0.27748 0.03960  -0.03585 0.00564  140 GLU D C     
2417 O O     . GLU B 141 ? 0.19404 0.30618 0.32536 0.03105  -0.03295 0.00019  140 GLU D O     
2418 C CB    . GLU B 141 ? 0.21558 0.32437 0.30205 0.04179  -0.05348 -0.00018 140 GLU D CB    
2419 C CG    . GLU B 141 ? 0.20141 0.29799 0.26483 0.03890  -0.05601 -0.00389 140 GLU D CG    
2420 C CD    . GLU B 141 ? 0.32081 0.42895 0.37090 0.04635  -0.06902 -0.00610 140 GLU D CD    
2421 O OE1   . GLU B 141 ? 0.33733 0.46242 0.39273 0.05640  -0.07707 -0.00254 140 GLU D OE1   
2422 O OE2   . GLU B 141 ? 0.34096 0.44065 0.37326 0.04328  -0.07110 -0.01133 140 GLU D OE2   
2423 N N     . ALA B 142 ? 0.14759 0.25144 0.25919 0.05119  -0.03385 0.01376  141 ALA D N     
2424 C CA    . ALA B 142 ? 0.13907 0.25280 0.27150 0.05483  -0.02852 0.01566  141 ALA D CA    
2425 C C     . ALA B 142 ? 0.12740 0.22527 0.26112 0.04738  -0.01520 0.01518  141 ALA D C     
2426 O O     . ALA B 142 ? 0.16080 0.26819 0.31358 0.04489  -0.00975 0.01311  141 ALA D O     
2427 C CB    . ALA B 142 ? 0.18540 0.29812 0.31361 0.07061  -0.02833 0.02491  141 ALA D CB    
2428 N N     . MET B 143 ? 0.15562 0.23088 0.26966 0.04468  -0.00966 0.01719  142 MET D N     
2429 C CA    . MET B 143 ? 0.18239 0.24390 0.29475 0.03816  0.00086  0.01592  142 MET D CA    
2430 C C     . MET B 143 ? 0.20789 0.27559 0.33062 0.02787  0.00208  0.00999  142 MET D C     
2431 O O     . MET B 143 ? 0.18045 0.24457 0.30881 0.02478  0.01107  0.00952  142 MET D O     
2432 C CB    . MET B 143 ? 0.18863 0.22953 0.28045 0.03624  0.00403  0.01761  142 MET D CB    
2433 C CG    . MET B 143 ? 0.22559 0.25604 0.30839 0.04478  0.00658  0.02366  142 MET D CG    
2434 S SD    . MET B 143 ? 0.26451 0.27650 0.32746 0.04118  0.00858  0.02501  142 MET D SD    
2435 C CE    . MET B 143 ? 0.25693 0.26147 0.31996 0.03212  0.01455  0.01949  142 MET D CE    
2436 N N     . GLU B 144 ? 0.24876 0.32450 0.37344 0.02269  -0.00591 0.00532  143 GLU D N     
2437 C CA    . GLU B 144 ? 0.27549 0.35394 0.41070 0.01215  -0.00323 -0.00035 143 GLU D CA    
2438 C C     . GLU B 144 ? 0.32932 0.42367 0.48973 0.00992  0.00182  -0.00190 143 GLU D C     
2439 O O     . GLU B 144 ? 0.27114 0.36068 0.43766 0.00187  0.01032  -0.00377 143 GLU D O     
2440 C CB    . GLU B 144 ? 0.28321 0.36716 0.41749 0.00676  -0.01268 -0.00679 143 GLU D CB    
2441 C CG    . GLU B 144 ? 0.28013 0.34766 0.39102 0.00743  -0.01477 -0.00612 143 GLU D CG    
2442 C CD    . GLU B 144 ? 0.31284 0.38153 0.42099 0.00119  -0.02156 -0.01396 143 GLU D CD    
2443 O OE1   . GLU B 144 ? 0.30836 0.39075 0.41789 0.00372  -0.03194 -0.01765 143 GLU D OE1   
2444 O OE2   . GLU B 144 ? 0.32783 0.38290 0.43097 -0.00541 -0.01663 -0.01663 143 GLU D OE2   
2445 N N     . ARG B 145 ? 0.25828 0.37238 0.43456 0.01733  -0.00261 -0.00082 144 ARG D N     
2446 C CA    . ARG B 145 ? 0.31037 0.44279 0.51431 0.01571  0.00319  -0.00239 144 ARG D CA    
2447 C C     . ARG B 145 ? 0.30526 0.42331 0.50633 0.01545  0.01909  0.00136  144 ARG D C     
2448 O O     . ARG B 145 ? 0.30414 0.43180 0.52501 0.01075  0.02802  -0.00022 144 ARG D O     
2449 C CB    . ARG B 145 ? 0.31513 0.47153 0.53540 0.02725  -0.00446 -0.00051 144 ARG D CB    
2450 C CG    . ARG B 145 ? 0.35375 0.53470 0.60756 0.02689  0.00105  -0.00240 144 ARG D CG    
2451 C CD    . ARG B 145 ? 0.26626 0.47340 0.53714 0.04074  -0.00787 -0.00001 144 ARG D CD    
2452 N NE    . ARG B 145 ? 0.27851 0.47145 0.53403 0.05590  -0.00354 0.00893  144 ARG D NE    
2453 C CZ    . ARG B 145 ? 0.36415 0.55532 0.62435 0.06293  0.00763  0.01212  144 ARG D CZ    
2454 N NH1   . ARG B 145 ? 0.37623 0.57779 0.65401 0.05635  0.01703  0.00850  144 ARG D NH1   
2455 N NH2   . ARG B 145 ? 0.39856 0.57448 0.64272 0.07637  0.01001  0.01868  144 ARG D NH2   
2456 N N     . PHE B 146 ? 0.20153 0.29701 0.37812 0.01994  0.02319  0.00568  145 PHE D N     
2457 C CA    . PHE B 146 ? 0.23997 0.32144 0.40953 0.02103  0.03660  0.00818  145 PHE D CA    
2458 C C     . PHE B 146 ? 0.24614 0.30997 0.40057 0.01254  0.04263  0.00734  145 PHE D C     
2459 O O     . PHE B 146 ? 0.25210 0.30401 0.39755 0.01327  0.05353  0.00907  145 PHE D O     
2460 C CB    . PHE B 146 ? 0.25587 0.32376 0.40907 0.03061  0.03756  0.01192  145 PHE D CB    
2461 C CG    . PHE B 146 ? 0.22979 0.31150 0.39576 0.04146  0.03346  0.01464  145 PHE D CG    
2462 C CD1   . PHE B 146 ? 0.21979 0.31189 0.40305 0.04782  0.04149  0.01576  145 PHE D CD1   
2463 C CD2   . PHE B 146 ? 0.19648 0.28028 0.35598 0.04648  0.02233  0.01675  145 PHE D CD2   
2464 C CE1   . PHE B 146 ? 0.21751 0.32282 0.41283 0.06013  0.03746  0.01921  145 PHE D CE1   
2465 C CE2   . PHE B 146 ? 0.20942 0.30438 0.37770 0.05843  0.01843  0.02073  145 PHE D CE2   
2466 C CZ    . PHE B 146 ? 0.19796 0.30396 0.38467 0.06568  0.02550  0.02207  145 PHE D CZ    
2467 N N     . GLY B 147 ? 0.20870 0.26986 0.35845 0.00582  0.03596  0.00483  146 GLY D N     
2468 C CA    . GLY B 147 ? 0.20624 0.24992 0.34109 -0.00018 0.04120  0.00510  146 GLY D CA    
2469 C C     . GLY B 147 ? 0.21456 0.26118 0.36415 -0.00891 0.04940  0.00347  146 GLY D C     
2470 O O     . GLY B 147 ? 0.24047 0.30458 0.41470 -0.01138 0.05271  0.00158  146 GLY D O     
2471 N N     . SER B 148 ? 0.18793 0.21678 0.32284 -0.01337 0.05359  0.00457  147 SER D N     
2472 C CA    . SER B 148 ? 0.18682 0.21092 0.33083 -0.02155 0.06504  0.00478  147 SER D CA    
2473 C C     . SER B 148 ? 0.16124 0.16425 0.28622 -0.02432 0.06520  0.00592  147 SER D C     
2474 O O     . SER B 148 ? 0.17766 0.17252 0.28389 -0.01909 0.05717  0.00671  147 SER D O     
2475 C CB    . SER B 148 ? 0.19994 0.21864 0.34119 -0.01894 0.08025  0.00976  147 SER D CB    
2476 O OG    . SER B 148 ? 0.21858 0.21742 0.32947 -0.01251 0.08231  0.01429  147 SER D OG    
2477 N N     . ARG B 149 ? 0.20793 0.20146 0.33886 -0.03232 0.07605  0.00650  148 ARG D N     
2478 C CA    . ARG B 149 ? 0.24291 0.21497 0.35794 -0.03444 0.07726  0.00770  148 ARG D CA    
2479 C C     . ARG B 149 ? 0.21194 0.16595 0.29616 -0.02436 0.07841  0.01495  148 ARG D C     
2480 O O     . ARG B 149 ? 0.24596 0.18856 0.31541 -0.02131 0.07285  0.01540  148 ARG D O     
2481 C CB    . ARG B 149 ? 0.27095 0.23330 0.39829 -0.04488 0.09166  0.00801  148 ARG D CB    
2482 C CG    . ARG B 149 ? 0.38598 0.32844 0.50413 -0.04880 0.09167  0.00661  148 ARG D CG    
2483 C CD    . ARG B 149 ? 0.43085 0.37279 0.57256 -0.06356 0.09801  -0.00040 148 ARG D CD    
2484 N NE    . ARG B 149 ? 0.41621 0.33112 0.53934 -0.06330 0.10063  0.00064  148 ARG D NE    
2485 C CZ    . ARG B 149 ? 0.38032 0.27202 0.48065 -0.05643 0.11159  0.01049  148 ARG D CZ    
2486 N NH1   . ARG B 149 ? 0.35830 0.25029 0.45279 -0.05175 0.12096  0.01810  148 ARG D NH1   
2487 N NH2   . ARG B 149 ? 0.37479 0.24320 0.45656 -0.05274 0.11267  0.01260  148 ARG D NH2   
2488 N N     . ASN B 150 ? 0.22308 0.17512 0.29744 -0.01875 0.08550  0.02001  149 ASN D N     
2489 C CA    . ASN B 150 ? 0.25885 0.19741 0.30423 -0.00915 0.08440  0.02526  149 ASN D CA    
2490 C C     . ASN B 150 ? 0.27134 0.22077 0.31138 -0.00300 0.07282  0.02238  149 ASN D C     
2491 O O     . ASN B 150 ? 0.30178 0.24415 0.32075 0.00403  0.07106  0.02481  149 ASN D O     
2492 C CB    . ASN B 150 ? 0.30619 0.23147 0.33631 -0.00587 0.09898  0.03220  149 ASN D CB    
2493 C CG    . ASN B 150 ? 0.33003 0.26704 0.36897 -0.00519 0.10519  0.03104  149 ASN D CG    
2494 O OD1   . ASN B 150 ? 0.29912 0.25394 0.35447 -0.00559 0.09768  0.02568  149 ASN D OD1   
2495 N ND2   . ASN B 150 ? 0.35629 0.28173 0.38256 -0.00288 0.12036  0.03680  149 ASN D ND2   
2496 N N     . GLY B 151 ? 0.20098 0.16717 0.25937 -0.00544 0.06518  0.01719  150 GLY D N     
2497 C CA    . GLY B 151 ? 0.20043 0.17428 0.25475 -0.00034 0.05550  0.01495  150 GLY D CA    
2498 C C     . GLY B 151 ? 0.20722 0.18540 0.26180 0.00347  0.05970  0.01493  150 GLY D C     
2499 O O     . GLY B 151 ? 0.18774 0.17146 0.24263 0.00668  0.05312  0.01274  150 GLY D O     
2500 N N     . LYS B 152 ? 0.22386 0.19826 0.27822 0.00339  0.07184  0.01735  151 LYS D N     
2501 C CA    . LYS B 152 ? 0.24627 0.22371 0.30068 0.00781  0.07737  0.01658  151 LYS D CA    
2502 C C     . LYS B 152 ? 0.22116 0.21635 0.30071 0.00767  0.07431  0.01399  151 LYS D C     
2503 O O     . LYS B 152 ? 0.21287 0.22030 0.31372 0.00270  0.07345  0.01312  151 LYS D O     
2504 C CB    . LYS B 152 ? 0.28749 0.25702 0.33599 0.00811  0.09308  0.02011  151 LYS D CB    
2505 C CG    . LYS B 152 ? 0.34302 0.29455 0.36060 0.01191  0.09484  0.02321  151 LYS D CG    
2506 C CD    . LYS B 152 ? 0.45397 0.40290 0.45406 0.01735  0.08559  0.01919  151 LYS D CD    
2507 C CE    . LYS B 152 ? 0.56741 0.50202 0.53614 0.02232  0.08583  0.02124  151 LYS D CE    
2508 N NZ    . LYS B 152 ? 0.54695 0.48301 0.50419 0.02481  0.07251  0.01581  151 LYS D NZ    
2509 N N     . THR B 153 ? 0.24655 0.24287 0.32329 0.01352  0.07211  0.01239  152 THR D N     
2510 C CA    . THR B 153 ? 0.23426 0.24593 0.33190 0.01644  0.06880  0.01141  152 THR D CA    
2511 C C     . THR B 153 ? 0.23001 0.24800 0.34015 0.02059  0.08063  0.01193  152 THR D C     
2512 O O     . THR B 153 ? 0.33125 0.33723 0.42684 0.02340  0.09071  0.01204  152 THR D O     
2513 C CB    . THR B 153 ? 0.25214 0.26004 0.34148 0.02098  0.05982  0.01042  152 THR D CB    
2514 O OG1   . THR B 153 ? 0.27758 0.27122 0.34965 0.02471  0.06489  0.00896  152 THR D OG1   
2515 C CG2   . THR B 153 ? 0.24743 0.25177 0.32743 0.01714  0.04953  0.01000  152 THR D CG2   
2516 N N     . SER B 154 ? 0.24071 0.27889 0.37774 0.02171  0.07895  0.01183  153 SER D N     
2517 C CA    . SER B 154 ? 0.23443 0.28393 0.38997 0.02625  0.09038  0.01243  153 SER D CA    
2518 C C     . SER B 154 ? 0.23816 0.28346 0.38955 0.03734  0.09208  0.01268  153 SER D C     
2519 O O     . SER B 154 ? 0.24951 0.29734 0.40859 0.04294  0.10440  0.01299  153 SER D O     
2520 C CB    . SER B 154 ? 0.33642 0.41338 0.52644 0.02278  0.08741  0.01146  153 SER D CB    
2521 O OG    . SER B 154 ? 0.27933 0.36826 0.47671 0.02578  0.07185  0.01061  153 SER D OG    
2522 N N     . LYS B 155 ? 0.26317 0.30045 0.40245 0.04061  0.08158  0.01264  154 LYS D N     
2523 C CA    . LYS B 155 ? 0.25278 0.27850 0.38314 0.04988  0.08379  0.01277  154 LYS D CA    
2524 C C     . LYS B 155 ? 0.22460 0.23073 0.32978 0.04633  0.07707  0.01104  154 LYS D C     
2525 O O     . LYS B 155 ? 0.23505 0.24168 0.33433 0.03911  0.06894  0.01082  154 LYS D O     
2526 C CB    . LYS B 155 ? 0.24382 0.28524 0.39391 0.05889  0.07794  0.01594  154 LYS D CB    
2527 C CG    . LYS B 155 ? 0.25154 0.31598 0.42786 0.06202  0.08219  0.01667  154 LYS D CG    
2528 C CD    . LYS B 155 ? 0.30791 0.38369 0.49488 0.07290  0.07581  0.01949  154 LYS D CD    
2529 C CE    . LYS B 155 ? 0.36927 0.46718 0.57898 0.07533  0.07983  0.01873  154 LYS D CE    
2530 N NZ    . LYS B 155 ? 0.36083 0.47143 0.58094 0.08773  0.07335  0.02130  154 LYS D NZ    
2531 N N     . LYS B 156 ? 0.23460 0.22357 0.32616 0.05098  0.08091  0.00918  155 LYS D N     
2532 C CA    . LYS B 156 ? 0.25557 0.22769 0.32641 0.04625  0.07556  0.00616  155 LYS D CA    
2533 C C     . LYS B 156 ? 0.22171 0.19588 0.29678 0.04751  0.06622  0.00953  155 LYS D C     
2534 O O     . LYS B 156 ? 0.20655 0.17928 0.28842 0.05571  0.06796  0.01270  155 LYS D O     
2535 C CB    . LYS B 156 ? 0.30332 0.25475 0.35733 0.04841  0.08362  0.00075  155 LYS D CB    
2536 C CG    . LYS B 156 ? 0.41443 0.35485 0.44928 0.04028  0.07727  -0.00418 155 LYS D CG    
2537 C CD    . LYS B 156 ? 0.38853 0.31184 0.40348 0.03944  0.08348  -0.01215 155 LYS D CD    
2538 C CE    . LYS B 156 ? 0.37154 0.28812 0.37288 0.03158  0.07470  -0.01767 155 LYS D CE    
2539 N NZ    . LYS B 156 ? 0.59032 0.49223 0.57101 0.03040  0.07899  -0.02727 155 LYS D NZ    
2540 N N     . ILE B 157 ? 0.19624 0.17276 0.26605 0.04065  0.05740  0.00952  156 ILE D N     
2541 C CA    . ILE B 157 ? 0.18508 0.16388 0.25660 0.04148  0.04937  0.01305  156 ILE D CA    
2542 C C     . ILE B 157 ? 0.21733 0.17931 0.27383 0.03708  0.04912  0.01018  156 ILE D C     
2543 O O     . ILE B 157 ? 0.21953 0.17931 0.26713 0.03003  0.04664  0.00615  156 ILE D O     
2544 C CB    . ILE B 157 ? 0.17652 0.17020 0.25380 0.03700  0.04061  0.01429  156 ILE D CB    
2545 C CG1   . ILE B 157 ? 0.18161 0.19291 0.27624 0.03785  0.04128  0.01480  156 ILE D CG1   
2546 C CG2   . ILE B 157 ? 0.19130 0.18654 0.26738 0.03947  0.03352  0.01796  156 ILE D CG2   
2547 C CD1   . ILE B 157 ? 0.23442 0.25716 0.34520 0.04737  0.04253  0.01802  156 ILE D CD1   
2548 N N     . THR B 158 ? 0.21066 0.16024 0.26494 0.04134  0.05254  0.01199  157 THR D N     
2549 C CA    . THR B 158 ? 0.21592 0.14882 0.25900 0.03530  0.05438  0.00764  157 THR D CA    
2550 C C     . THR B 158 ? 0.24082 0.16824 0.28345 0.03599  0.05285  0.01292  157 THR D C     
2551 O O     . THR B 158 ? 0.23741 0.16913 0.28479 0.04415  0.05172  0.02054  157 THR D O     
2552 C CB    . THR B 158 ? 0.26949 0.18418 0.30636 0.03671  0.06371  0.00230  157 THR D CB    
2553 O OG1   . THR B 158 ? 0.27588 0.18443 0.31881 0.04735  0.06971  0.00816  157 THR D OG1   
2554 C CG2   . THR B 158 ? 0.28586 0.20434 0.31852 0.03568  0.06615  -0.00320 157 THR D CG2   
2555 N N     . ILE B 159 ? 0.22598 0.14423 0.26257 0.02757  0.05318  0.00869  158 ILE D N     
2556 C CA    . ILE B 159 ? 0.23538 0.14329 0.27044 0.02679  0.05585  0.01314  158 ILE D CA    
2557 C C     . ILE B 159 ? 0.26026 0.14471 0.29221 0.02859  0.06632  0.01171  158 ILE D C     
2558 O O     . ILE B 159 ? 0.30613 0.17892 0.33491 0.01995  0.06995  0.00282  158 ILE D O     
2559 C CB    . ILE B 159 ? 0.23789 0.14988 0.27215 0.01626  0.05232  0.00909  158 ILE D CB    
2560 C CG1   . ILE B 159 ? 0.21982 0.15213 0.25599 0.01586  0.04312  0.00991  158 ILE D CG1   
2561 C CG2   . ILE B 159 ? 0.27766 0.17864 0.31112 0.01492  0.05764  0.01437  158 ILE D CG2   
2562 C CD1   . ILE B 159 ? 0.24672 0.18578 0.28344 0.00738  0.03938  0.00552  158 ILE D CD1   
2563 N N     . ALA B 160 ? 0.24745 0.12525 0.28046 0.04057  0.07088  0.01970  159 ALA D N     
2564 C CA    . ALA B 160 ? 0.30829 0.16268 0.33759 0.04423  0.08160  0.01906  159 ALA D CA    
2565 C C     . ALA B 160 ? 0.32367 0.16111 0.34777 0.03726  0.08719  0.02005  159 ALA D C     
2566 O O     . ALA B 160 ? 0.38308 0.20380 0.40355 0.03169  0.09421  0.01370  159 ALA D O     
2567 C CB    . ALA B 160 ? 0.29157 0.15218 0.32322 0.05863  0.08170  0.02826  159 ALA D CB    
2568 N N     . ASP B 161 ? 0.29765 0.13942 0.32133 0.03723  0.08484  0.02766  160 ASP D N     
2569 C CA    . ASP B 161 ? 0.30981 0.13797 0.33015 0.02962  0.09146  0.02893  160 ASP D CA    
2570 C C     . ASP B 161 ? 0.29540 0.13476 0.31781 0.02520  0.08689  0.03214  160 ASP D C     
2571 O O     . ASP B 161 ? 0.28585 0.14460 0.30870 0.03112  0.07765  0.03595  160 ASP D O     
2572 C CB    . ASP B 161 ? 0.37928 0.19578 0.39218 0.03977  0.09790  0.03960  160 ASP D CB    
2573 C CG    . ASP B 161 ? 0.49309 0.29010 0.50316 0.03099  0.10870  0.03848  160 ASP D CG    
2574 O OD1   . ASP B 161 ? 0.39400 0.18819 0.40999 0.01622  0.11057  0.02798  160 ASP D OD1   
2575 O OD2   . ASP B 161 ? 0.45968 0.24509 0.46220 0.03909  0.11528  0.04793  160 ASP D OD2   
2576 N N     . CYS B 162 ? 0.31211 0.14464 0.33631 0.01384  0.09234  0.02941  161 CYS D N     
2577 C CA    . CYS B 162 ? 0.29204 0.13670 0.31836 0.00941  0.08953  0.03247  161 CYS D CA    
2578 C C     . CYS B 162 ? 0.30844 0.14144 0.33696 -0.00027 0.09996  0.03214  161 CYS D C     
2579 O O     . CYS B 162 ? 0.34144 0.16188 0.37258 -0.00698 0.10618  0.02536  161 CYS D O     
2580 C CB    . CYS B 162 ? 0.29043 0.16086 0.32401 0.00222  0.07754  0.02258  161 CYS D CB    
2581 S SG    . CYS B 162 ? 0.29891 0.16829 0.34030 -0.01146 0.07656  0.00577  161 CYS D SG    
2582 N N     . GLY B 163 ? 0.31183 0.15084 0.33895 -0.00064 0.10179  0.03895  162 GLY D N     
2583 C CA    . GLY B 163 ? 0.29568 0.12671 0.32528 -0.00840 0.11242  0.03956  162 GLY D CA    
2584 C C     . GLY B 163 ? 0.29463 0.13345 0.31902 -0.00509 0.11432  0.04868  162 GLY D C     
2585 O O     . GLY B 163 ? 0.31301 0.16426 0.33266 0.00143  0.10656  0.05295  162 GLY D O     
2586 N N     . GLN B 164 ? 0.34428 0.17507 0.36929 -0.00981 0.12535  0.05101  163 GLN D N     
2587 C CA    . GLN B 164 ? 0.32423 0.16083 0.34365 -0.00742 0.12970  0.05869  163 GLN D CA    
2588 C C     . GLN B 164 ? 0.36956 0.18891 0.36924 0.00534  0.13717  0.07119  163 GLN D C     
2589 O O     . GLN B 164 ? 0.44818 0.24954 0.44652 0.00493  0.14565  0.07188  163 GLN D O     
2590 C CB    . GLN B 164 ? 0.37030 0.21275 0.40730 -0.02258 0.13746  0.05136  163 GLN D CB    
2591 C CG    . GLN B 164 ? 0.36893 0.21771 0.40100 -0.02015 0.14372  0.05867  163 GLN D CG    
2592 C CD    . GLN B 164 ? 0.39736 0.25995 0.45136 -0.03464 0.14884  0.05039  163 GLN D CD    
2593 O OE1   . GLN B 164 ? 0.36852 0.23667 0.44175 -0.04719 0.14699  0.03867  163 GLN D OE1   
2594 N NE2   . GLN B 164 ? 0.34325 0.21311 0.39425 -0.03235 0.15462  0.05590  163 GLN D NE2   
2595 N N     . LEU B 165 ? 0.39843 0.22330 0.38188 0.01697  0.13381  0.08059  164 LEU D N     
2596 C CA    . LEU B 165 ? 0.43448 0.24610 0.39688 0.03019  0.13957  0.09255  164 LEU D CA    
2597 C C     . LEU B 165 ? 0.50085 0.30765 0.46007 0.02641  0.15220  0.09637  164 LEU D C     
2598 O O     . LEU B 165 ? 0.50056 0.32047 0.46996 0.01769  0.15307  0.09177  164 LEU D O     
2599 C CB    . LEU B 165 ? 0.51712 0.33946 0.46231 0.04529  0.12698  0.09901  164 LEU D CB    
2600 C CG    . LEU B 165 ? 0.47109 0.30068 0.42115 0.05002  0.11422  0.09552  164 LEU D CG    
2601 C CD1   . LEU B 165 ? 0.51606 0.36001 0.45183 0.06360  0.10079  0.10041  164 LEU D CD1   
2602 C CD2   . LEU B 165 ? 0.50453 0.31830 0.45391 0.05455  0.11897  0.09744  164 LEU D CD2   
2603 N N     . SER C 1   ? 0.41695 0.64944 0.55989 -0.17353 0.02264  -0.16220 0   SER B N     
2604 C CA    . SER C 1   ? 0.35070 0.57671 0.50051 -0.16535 0.02675  -0.15332 0   SER B CA    
2605 C C     . SER C 1   ? 0.30426 0.50991 0.44648 -0.14865 0.01892  -0.13846 0   SER B C     
2606 O O     . SER C 1   ? 0.38865 0.58902 0.52192 -0.14247 0.00925  -0.13528 0   SER B O     
2607 C CB    . SER C 1   ? 0.40633 0.60021 0.54466 -0.18053 0.04776  -0.15532 0   SER B CB    
2608 O OG    . SER C 1   ? 0.48863 0.63566 0.60555 -0.17749 0.05472  -0.14413 0   SER B OG    
2609 N N     . MET C 2   ? 0.28744 0.48190 0.43250 -0.14222 0.02378  -0.13011 1   MET B N     
2610 C CA    . MET C 2   ? 0.25694 0.43239 0.39539 -0.12840 0.01831  -0.11723 1   MET B CA    
2611 C C     . MET C 2   ? 0.22834 0.35560 0.34465 -0.13528 0.03223  -0.11153 1   MET B C     
2612 O O     . MET C 2   ? 0.26372 0.37037 0.36968 -0.14862 0.04742  -0.11563 1   MET B O     
2613 C CB    . MET C 2   ? 0.25324 0.44508 0.40737 -0.11583 0.01539  -0.11117 1   MET B CB    
2614 C CG    . MET C 2   ? 0.23754 0.47259 0.41161 -0.10386 0.00208  -0.11398 1   MET B CG    
2615 S SD    . MET C 2   ? 0.31228 0.55593 0.49921 -0.08550 -0.00062 -0.10457 1   MET B SD    
2616 C CE    . MET C 2   ? 0.35775 0.57647 0.53077 -0.07324 -0.00878 -0.09246 1   MET B CE    
2617 N N     . THR C 3   ? 0.21358 0.32217 0.32138 -0.12477 0.02720  -0.10157 2   THR B N     
2618 C CA    . THR C 3   ? 0.24891 0.31308 0.33667 -0.12578 0.03883  -0.09323 2   THR B CA    
2619 C C     . THR C 3   ? 0.25400 0.31665 0.34380 -0.10770 0.03292  -0.08001 2   THR B C     
2620 O O     . THR C 3   ? 0.22532 0.31715 0.33020 -0.09608 0.02017  -0.07849 2   THR B O     
2621 C CB    . THR C 3   ? 0.26930 0.30554 0.33679 -0.12674 0.03891  -0.09243 2   THR B CB    
2622 O OG1   . THR C 3   ? 0.29866 0.35714 0.37169 -0.11659 0.02218  -0.09215 2   THR B OG1   
2623 C CG2   . THR C 3   ? 0.34947 0.37280 0.40520 -0.14134 0.04967  -0.10167 2   THR B CG2   
2624 N N     . GLU C 4   ? 0.23059 0.25734 0.30175 -0.10260 0.04189  -0.06921 3   GLU B N     
2625 C CA    . GLU C 4   ? 0.20980 0.23205 0.27837 -0.08513 0.03692  -0.05628 3   GLU B CA    
2626 C C     . GLU C 4   ? 0.21642 0.20035 0.26034 -0.07767 0.04183  -0.04539 3   GLU B C     
2627 O O     . GLU C 4   ? 0.27028 0.22604 0.29836 -0.08615 0.05442  -0.04624 3   GLU B O     
2628 C CB    . GLU C 4   ? 0.20204 0.23506 0.28107 -0.08767 0.04374  -0.05711 3   GLU B CB    
2629 C CG    . GLU C 4   ? 0.21113 0.23713 0.28499 -0.07197 0.04031  -0.04537 3   GLU B CG    
2630 C CD    . GLU C 4   ? 0.22468 0.26962 0.31278 -0.07236 0.04400  -0.04807 3   GLU B CD    
2631 O OE1   . GLU C 4   ? 0.21955 0.28168 0.32110 -0.08512 0.05102  -0.05829 3   GLU B OE1   
2632 O OE2   . GLU C 4   ? 0.23150 0.27581 0.31803 -0.06024 0.04005  -0.04098 3   GLU B OE2   
2633 N N     . TYR C 5   ? 0.20622 0.18901 0.24639 -0.06181 0.03259  -0.03561 4   TYR B N     
2634 C CA    . TYR C 5   ? 0.22186 0.17674 0.24227 -0.05261 0.03499  -0.02605 4   TYR B CA    
2635 C C     . TYR C 5   ? 0.23758 0.19489 0.25706 -0.03964 0.03024  -0.01645 4   TYR B C     
2636 O O     . TYR C 5   ? 0.21451 0.19274 0.24646 -0.03434 0.02081  -0.01621 4   TYR B O     
2637 C CB    . TYR C 5   ? 0.24367 0.19742 0.25989 -0.04841 0.02801  -0.02645 4   TYR B CB    
2638 C CG    . TYR C 5   ? 0.24759 0.20096 0.26411 -0.06213 0.03178  -0.03754 4   TYR B CG    
2639 C CD1   . TYR C 5   ? 0.28362 0.20709 0.28385 -0.07003 0.04481  -0.03996 4   TYR B CD1   
2640 C CD2   . TYR C 5   ? 0.22795 0.21072 0.26001 -0.06779 0.02294  -0.04640 4   TYR B CD2   
2641 C CE1   . TYR C 5   ? 0.29726 0.21919 0.29692 -0.08614 0.04989  -0.05257 4   TYR B CE1   
2642 C CE2   . TYR C 5   ? 0.24796 0.23452 0.28089 -0.08256 0.02602  -0.05872 4   TYR B CE2   
2643 C CZ    . TYR C 5   ? 0.26909 0.22482 0.28597 -0.09305 0.03992  -0.06251 4   TYR B CZ    
2644 O OH    . TYR C 5   ? 0.30626 0.26510 0.32323 -0.11023 0.04385  -0.07665 4   TYR B OH    
2645 N N     . LYS C 6   ? 0.24428 0.17938 0.24722 -0.03398 0.03663  -0.00867 5   LYS B N     
2646 C CA    . LYS C 6   ? 0.24091 0.17837 0.24022 -0.02215 0.03184  -0.00033 5   LYS B CA    
2647 C C     . LYS C 6   ? 0.22546 0.15831 0.21748 -0.01160 0.02622  0.00506  5   LYS B C     
2648 O O     . LYS C 6   ? 0.24920 0.16162 0.22607 -0.00724 0.03184  0.00892  5   LYS B O     
2649 C CB    . LYS C 6   ? 0.29177 0.21122 0.27610 -0.02140 0.04150  0.00480  5   LYS B CB    
2650 C CG    . LYS C 6   ? 0.36697 0.29200 0.35849 -0.03260 0.04895  -0.00088 5   LYS B CG    
2651 C CD    . LYS C 6   ? 0.47314 0.38108 0.44759 -0.03109 0.05822  0.00511  5   LYS B CD    
2652 C CE    . LYS C 6   ? 0.59714 0.47266 0.55106 -0.03706 0.07240  0.00692  5   LYS B CE    
2653 N NZ    . LYS C 6   ? 0.61390 0.49130 0.57747 -0.05548 0.08215  -0.00380 5   LYS B NZ    
2654 N N     . LEU C 7   ? 0.19882 0.14962 0.20080 -0.00717 0.01629  0.00528  6   LEU B N     
2655 C CA    . LEU C 7   ? 0.20515 0.15671 0.20339 0.00087  0.01138  0.00883  6   LEU B CA    
2656 C C     . LEU C 7   ? 0.23470 0.19464 0.23223 0.00855  0.00711  0.01407  6   LEU B C     
2657 O O     . LEU C 7   ? 0.23495 0.20502 0.23923 0.00664  0.00432  0.01309  6   LEU B O     
2658 C CB    . LEU C 7   ? 0.20814 0.17267 0.21573 -0.00163 0.00442  0.00476  6   LEU B CB    
2659 C CG    . LEU C 7   ? 0.19808 0.16247 0.20902 -0.01057 0.00594  -0.00251 6   LEU B CG    
2660 C CD1   . LEU C 7   ? 0.23284 0.21013 0.24895 -0.01027 -0.00224 -0.00488 6   LEU B CD1   
2661 C CD2   . LEU C 7   ? 0.23326 0.17671 0.23178 -0.01324 0.01457  -0.00408 6   LEU B CD2   
2662 N N     . VAL C 8   ? 0.19572 0.15290 0.18534 0.01728  0.00680  0.01867  7   VAL B N     
2663 C CA    . VAL C 8   ? 0.20166 0.17072 0.19066 0.02370  0.00245  0.02223  7   VAL B CA    
2664 C C     . VAL C 8   ? 0.20516 0.18661 0.19879 0.02765  -0.00217 0.02210  7   VAL B C     
2665 O O     . VAL C 8   ? 0.21729 0.19244 0.20684 0.03224  0.00031  0.02286  7   VAL B O     
2666 C CB    . VAL C 8   ? 0.22122 0.17976 0.19571 0.03204  0.00654  0.02804  7   VAL B CB    
2667 C CG1   . VAL C 8   ? 0.23110 0.20742 0.20540 0.03824  0.00048  0.03032  7   VAL B CG1   
2668 C CG2   . VAL C 8   ? 0.24705 0.19063 0.21504 0.02603  0.01354  0.02792  7   VAL B CG2   
2669 N N     . VAL C 9   ? 0.17915 0.17667 0.18027 0.02516  -0.00742 0.02052  8   VAL B N     
2670 C CA    . VAL C 9   ? 0.18787 0.19861 0.19406 0.02595  -0.01038 0.01939  8   VAL B CA    
2671 C C     . VAL C 9   ? 0.17892 0.20633 0.18496 0.03170  -0.01297 0.02067  8   VAL B C     
2672 O O     . VAL C 9   ? 0.17808 0.21266 0.18442 0.02884  -0.01536 0.01962  8   VAL B O     
2673 C CB    . VAL C 9   ? 0.17070 0.18536 0.18341 0.01743  -0.01300 0.01612  8   VAL B CB    
2674 C CG1   . VAL C 9   ? 0.18702 0.21110 0.20244 0.01626  -0.01362 0.01496  8   VAL B CG1   
2675 C CG2   . VAL C 9   ? 0.18466 0.18820 0.19818 0.01337  -0.01245 0.01464  8   VAL B CG2   
2676 N N     . VAL C 10  ? 0.17310 0.20858 0.17864 0.04038  -0.01256 0.02222  9   VAL B N     
2677 C CA    . VAL C 10  ? 0.16057 0.21779 0.16744 0.04812  -0.01602 0.02300  9   VAL B CA    
2678 C C     . VAL C 10  ? 0.15901 0.23729 0.17600 0.04802  -0.01668 0.01953  9   VAL B C     
2679 O O     . VAL C 10  ? 0.18004 0.25117 0.19900 0.04516  -0.01331 0.01822  9   VAL B O     
2680 C CB    . VAL C 10  ? 0.18984 0.23926 0.18492 0.06335  -0.01452 0.02927  9   VAL B CB    
2681 C CG1   . VAL C 10  ? 0.24802 0.27452 0.23132 0.06141  -0.01162 0.03253  9   VAL B CG1   
2682 C CG2   . VAL C 10  ? 0.22697 0.26529 0.21877 0.07273  -0.00947 0.03130  9   VAL B CG2   
2683 N N     . GLY C 11  ? 0.15123 0.25749 0.17426 0.05071  -0.02080 0.01738  10  GLY B N     
2684 C CA    . GLY C 11  ? 0.17730 0.30935 0.21230 0.04904  -0.02059 0.01265  10  GLY B CA    
2685 C C     . GLY C 11  ? 0.15086 0.31230 0.19458 0.04037  -0.02490 0.00638  10  GLY B C     
2686 O O     . GLY C 11  ? 0.18273 0.33932 0.22187 0.03400  -0.02758 0.00542  10  GLY B O     
2687 N N     . ALA C 12  ? 0.15429 0.34586 0.21043 0.03885  -0.02459 0.00105  11  ALA B N     
2688 C CA    . ALA C 12  ? 0.12706 0.35203 0.19309 0.02873  -0.02820 -0.00716 11  ALA B CA    
2689 C C     . ALA C 12  ? 0.14988 0.36085 0.21372 0.00783  -0.02551 -0.01235 11  ALA B C     
2690 O O     . ALA C 12  ? 0.14801 0.32870 0.20544 0.00149  -0.02081 -0.00982 11  ALA B O     
2691 C CB    . ALA C 12  ? 0.16051 0.42111 0.24213 0.02947  -0.02642 -0.01289 11  ALA B CB    
2692 N N     . CYS C 13  ? 0.15067 0.38531 0.21927 -0.00217 -0.02852 -0.02016 12  CYS B N     
2693 C CA    . CYS C 13  ? 0.18581 0.40584 0.25064 -0.02238 -0.02459 -0.02629 12  CYS B CA    
2694 C C     . CYS C 13  ? 0.16510 0.37501 0.23249 -0.03565 -0.01589 -0.02900 12  CYS B C     
2695 O O     . CYS C 13  ? 0.19605 0.43049 0.27441 -0.03593 -0.01340 -0.03216 12  CYS B O     
2696 C CB    . CYS C 13  ? 0.20310 0.45478 0.27335 -0.03301 -0.02823 -0.03680 12  CYS B CB    
2697 S SG    . CYS C 13  ? 0.29407 0.58499 0.37845 -0.03672 -0.02582 -0.04517 12  CYS B SG    
2698 N N     . GLY C 14  ? 0.16177 0.33625 0.21816 -0.04464 -0.01112 -0.02724 13  GLY B N     
2699 C CA    . GLY C 14  ? 0.17289 0.33251 0.22629 -0.05770 -0.00226 -0.02895 13  GLY B CA    
2700 C C     . GLY C 14  ? 0.17608 0.32434 0.22779 -0.04966 0.00075  -0.02223 13  GLY B C     
2701 O O     . GLY C 14  ? 0.20975 0.34708 0.25695 -0.06025 0.00836  -0.02340 13  GLY B O     
2702 N N     . VAL C 15  ? 0.17248 0.31954 0.22481 -0.03268 -0.00401 -0.01570 14  VAL B N     
2703 C CA    . VAL C 15  ? 0.14998 0.28789 0.20006 -0.02588 -0.00066 -0.01116 14  VAL B CA    
2704 C C     . VAL C 15  ? 0.19650 0.29747 0.23250 -0.02784 0.00106  -0.00575 14  VAL B C     
2705 O O     . VAL C 15  ? 0.18895 0.28043 0.21993 -0.02672 0.00466  -0.00337 14  VAL B O     
2706 C CB    . VAL C 15  ? 0.15861 0.30579 0.21251 -0.00776 -0.00459 -0.00718 14  VAL B CB    
2707 C CG1   . VAL C 15  ? 0.15691 0.34343 0.22445 -0.00212 -0.00675 -0.01172 14  VAL B CG1   
2708 C CG2   . VAL C 15  ? 0.17188 0.29979 0.21831 0.00120  -0.00979 -0.00166 14  VAL B CG2   
2709 N N     . GLY C 16  ? 0.18378 0.26726 0.21378 -0.02948 -0.00174 -0.00428 15  GLY B N     
2710 C CA    . GLY C 16  ? 0.16171 0.21527 0.18027 -0.02876 -0.00142 0.00059  15  GLY B CA    
2711 C C     . GLY C 16  ? 0.16753 0.21066 0.18495 -0.01812 -0.00680 0.00480  15  GLY B C     
2712 O O     . GLY C 16  ? 0.19184 0.21713 0.20245 -0.01535 -0.00749 0.00838  15  GLY B O     
2713 N N     . LYS C 17  ? 0.16714 0.22133 0.19003 -0.01236 -0.01033 0.00432  16  LYS B N     
2714 C CA    . LYS C 17  ? 0.16604 0.20896 0.18693 -0.00451 -0.01336 0.00775  16  LYS B CA    
2715 C C     . LYS C 17  ? 0.17245 0.19749 0.18883 -0.00760 -0.01365 0.00832  16  LYS B C     
2716 O O     . LYS C 17  ? 0.17702 0.19121 0.19152 -0.00365 -0.01486 0.01075  16  LYS B O     
2717 C CB    . LYS C 17  ? 0.16600 0.22138 0.18965 0.00038  -0.01581 0.00728  16  LYS B CB    
2718 C CG    . LYS C 17  ? 0.17126 0.24499 0.19879 0.00794  -0.01631 0.00773  16  LYS B CG    
2719 C CD    . LYS C 17  ? 0.19013 0.27414 0.21645 0.01570  -0.01950 0.00897  16  LYS B CD    
2720 C CE    . LYS C 17  ? 0.15285 0.25157 0.18103 0.00853  -0.02200 0.00413  16  LYS B CE    
2721 N NZ    . LYS C 17  ? 0.15642 0.28000 0.19306 0.00208  -0.02196 -0.00166 16  LYS B NZ    
2722 N N     . SER C 18  ? 0.17195 0.19555 0.18690 -0.01423 -0.01236 0.00528  17  SER B N     
2723 C CA    . SER C 18  ? 0.17813 0.18388 0.18830 -0.01486 -0.01177 0.00570  17  SER B CA    
2724 C C     . SER C 18  ? 0.19825 0.18829 0.20130 -0.01507 -0.01032 0.00874  17  SER B C     
2725 O O     . SER C 18  ? 0.21099 0.19029 0.21194 -0.00914 -0.01235 0.01140  17  SER B O     
2726 C CB    . SER C 18  ? 0.19678 0.20132 0.20448 -0.02245 -0.00923 0.00076  17  SER B CB    
2727 O OG    . SER C 18  ? 0.19208 0.21119 0.20385 -0.02070 -0.01166 -0.00153 17  SER B OG    
2728 N N     . ALA C 19  ? 0.20464 0.19520 0.20363 -0.02124 -0.00686 0.00841  18  ALA B N     
2729 C CA    . ALA C 19  ? 0.19502 0.16773 0.18275 -0.02099 -0.00493 0.01236  18  ALA B CA    
2730 C C     . ALA C 19  ? 0.20737 0.18134 0.19554 -0.01228 -0.00971 0.01595  18  ALA B C     
2731 O O     . ALA C 19  ? 0.22896 0.19022 0.20967 -0.00714 -0.01193 0.01944  18  ALA B O     
2732 C CB    . ALA C 19  ? 0.23242 0.20510 0.21432 -0.03102 0.00161  0.01099  18  ALA B CB    
2733 N N     . LEU C 20  ? 0.18107 0.17037 0.17722 -0.00993 -0.01140 0.01469  19  LEU B N     
2734 C CA    . LEU C 20  ? 0.19584 0.18471 0.19125 -0.00403 -0.01481 0.01622  19  LEU B CA    
2735 C C     . LEU C 20  ? 0.20251 0.18902 0.20212 0.00099  -0.01909 0.01629  19  LEU B C     
2736 O O     . LEU C 20  ? 0.21166 0.19448 0.20804 0.00461  -0.02259 0.01740  19  LEU B O     
2737 C CB    . LEU C 20  ? 0.19815 0.19921 0.19942 -0.00224 -0.01383 0.01441  19  LEU B CB    
2738 C CG    . LEU C 20  ? 0.19737 0.20413 0.19574 -0.00510 -0.00953 0.01371  19  LEU B CG    
2739 C CD1   . LEU C 20  ? 0.24199 0.26063 0.24711 -0.00009 -0.00848 0.01208  19  LEU B CD1   
2740 C CD2   . LEU C 20  ? 0.23036 0.22698 0.21737 -0.00534 -0.00929 0.01536  19  LEU B CD2   
2741 N N     . THR C 21  ? 0.20545 0.19616 0.21214 0.00103  -0.01874 0.01457  20  THR B N     
2742 C CA    . THR C 21  ? 0.21076 0.20163 0.22295 0.00471  -0.02101 0.01368  20  THR B CA    
2743 C C     . THR C 21  ? 0.21001 0.19219 0.21902 0.00792  -0.02259 0.01493  20  THR B C     
2744 O O     . THR C 21  ? 0.20696 0.19198 0.21916 0.01279  -0.02618 0.01474  20  THR B O     
2745 C CB    . THR C 21  ? 0.19588 0.19146 0.21291 0.00366  -0.01900 0.01189  20  THR B CB    
2746 O OG1   . THR C 21  ? 0.22656 0.22895 0.24444 0.00394  -0.01781 0.01201  20  THR B OG1   
2747 C CG2   . THR C 21  ? 0.23561 0.23182 0.25845 0.00628  -0.01943 0.01036  20  THR B CG2   
2748 N N     . ILE C 22  ? 0.20065 0.17219 0.20257 0.00548  -0.01959 0.01590  21  ILE B N     
2749 C CA    . ILE C 22  ? 0.23330 0.19094 0.22869 0.01064  -0.01972 0.01801  21  ILE B CA    
2750 C C     . ILE C 22  ? 0.23672 0.18881 0.22306 0.01610  -0.02329 0.02238  21  ILE B C     
2751 O O     . ILE C 22  ? 0.26979 0.21856 0.25432 0.02538  -0.02690 0.02446  21  ILE B O     
2752 C CB    . ILE C 22  ? 0.24034 0.18314 0.22736 0.00479  -0.01359 0.01713  21  ILE B CB    
2753 C CG1   . ILE C 22  ? 0.23672 0.18640 0.23176 0.00185  -0.01175 0.01216  21  ILE B CG1   
2754 C CG2   . ILE C 22  ? 0.29734 0.21840 0.27237 0.01135  -0.01203 0.02064  21  ILE B CG2   
2755 C CD1   . ILE C 22  ? 0.31303 0.25596 0.30226 -0.00793 -0.00610 0.00826  21  ILE B CD1   
2756 N N     . GLN C 23  ? 0.22183 0.17410 0.20158 0.01156  -0.02247 0.02377  22  GLN B N     
2757 C CA    . GLN C 23  ? 0.25057 0.19926 0.21989 0.01666  -0.02638 0.02750  22  GLN B CA    
2758 C C     . GLN C 23  ? 0.26776 0.23308 0.24703 0.02228  -0.03366 0.02498  22  GLN B C     
2759 O O     . GLN C 23  ? 0.27993 0.24605 0.25491 0.03077  -0.03934 0.02711  22  GLN B O     
2760 C CB    . GLN C 23  ? 0.28260 0.23050 0.24376 0.00997  -0.02305 0.02811  22  GLN B CB    
2761 C CG    . GLN C 23  ? 0.35391 0.28317 0.29895 0.00551  -0.01655 0.03181  22  GLN B CG    
2762 C CD    . GLN C 23  ? 0.36926 0.28023 0.29428 0.01327  -0.01849 0.03863  22  GLN B CD    
2763 O OE1   . GLN C 23  ? 0.34433 0.25816 0.26934 0.02448  -0.02617 0.04063  22  GLN B OE1   
2764 N NE2   . GLN C 23  ? 0.40206 0.29505 0.30928 0.00751  -0.01113 0.04217  22  GLN B NE2   
2765 N N     . LEU C 24  ? 0.24209 0.22093 0.23380 0.01763  -0.03326 0.02016  23  LEU B N     
2766 C CA    . LEU C 24  ? 0.22169 0.21520 0.22255 0.01940  -0.03812 0.01608  23  LEU B CA    
2767 C C     . LEU C 24  ? 0.23765 0.23822 0.24745 0.02621  -0.04157 0.01503  23  LEU B C     
2768 O O     . LEU C 24  ? 0.26270 0.27501 0.27506 0.03152  -0.04795 0.01354  23  LEU B O     
2769 C CB    . LEU C 24  ? 0.24301 0.24275 0.25256 0.01302  -0.03437 0.01179  23  LEU B CB    
2770 C CG    . LEU C 24  ? 0.28053 0.29262 0.29876 0.01142  -0.03688 0.00617  23  LEU B CG    
2771 C CD1   . LEU C 24  ? 0.30899 0.32194 0.31900 0.00894  -0.03889 0.00419  23  LEU B CD1   
2772 C CD2   . LEU C 24  ? 0.30632 0.31855 0.33185 0.00665  -0.03119 0.00338  23  LEU B CD2   
2773 N N     . ILE C 25  ? 0.24298 0.23912 0.25812 0.02640  -0.03746 0.01492  24  ILE B N     
2774 C CA    . ILE C 25  ? 0.25748 0.26238 0.28378 0.03233  -0.03867 0.01242  24  ILE B CA    
2775 C C     . ILE C 25  ? 0.30456 0.30037 0.32326 0.04380  -0.04123 0.01677  24  ILE B C     
2776 O O     . ILE C 25  ? 0.32411 0.33328 0.35031 0.05307  -0.04624 0.01546  24  ILE B O     
2777 C CB    . ILE C 25  ? 0.28846 0.29159 0.32160 0.02770  -0.03229 0.00984  24  ILE B CB    
2778 C CG1   . ILE C 25  ? 0.25528 0.26427 0.29271 0.01899  -0.02939 0.00702  24  ILE B CG1   
2779 C CG2   . ILE C 25  ? 0.26599 0.27679 0.30964 0.03465  -0.03190 0.00702  24  ILE B CG2   
2780 C CD1   . ILE C 25  ? 0.31011 0.33448 0.35882 0.01662  -0.03018 0.00183  24  ILE B CD1   
2781 N N     . GLN C 26  ? 0.29315 0.26612 0.29631 0.04365  -0.03731 0.02179  25  GLN B N     
2782 C CA    . GLN C 26  ? 0.32875 0.28403 0.32081 0.05442  -0.03654 0.02645  25  GLN B CA    
2783 C C     . GLN C 26  ? 0.35271 0.29131 0.32395 0.05881  -0.03832 0.03366  25  GLN B C     
2784 O O     . GLN C 26  ? 0.38618 0.30625 0.34396 0.07000  -0.03773 0.03910  25  GLN B O     
2785 C CB    . GLN C 26  ? 0.34034 0.27745 0.32884 0.04956  -0.02786 0.02523  25  GLN B CB    
2786 C CG    . GLN C 26  ? 0.33187 0.28381 0.33759 0.04655  -0.02570 0.01862  25  GLN B CG    
2787 C CD    . GLN C 26  ? 0.31389 0.24868 0.31387 0.04110  -0.01757 0.01629  25  GLN B CD    
2788 O OE1   . GLN C 26  ? 0.39861 0.31028 0.38286 0.03848  -0.01306 0.01884  25  GLN B OE1   
2789 N NE2   . GLN C 26  ? 0.37253 0.31793 0.38366 0.03813  -0.01497 0.01082  25  GLN B NE2   
2790 N N     . ASN C 27  ? 0.34584 0.28856 0.31209 0.05110  -0.03965 0.03409  26  ASN B N     
2791 C CA    . ASN C 27  ? 0.35251 0.28133 0.29747 0.05447  -0.04114 0.04068  26  ASN B CA    
2792 C C     . ASN C 27  ? 0.36160 0.25696 0.28545 0.05328  -0.03246 0.04665  26  ASN B C     
2793 O O     . ASN C 27  ? 0.41336 0.28932 0.31634 0.06300  -0.03307 0.05420  26  ASN B O     
2794 C CB    . ASN C 27  ? 0.37614 0.31635 0.31797 0.06930  -0.05142 0.04336  26  ASN B CB    
2795 C CG    . ASN C 27  ? 0.46122 0.43045 0.41541 0.06515  -0.05875 0.03717  26  ASN B CG    
2796 O OD1   . ASN C 27  ? 0.57367 0.56672 0.54835 0.06561  -0.06262 0.03054  26  ASN B OD1   
2797 N ND2   . ASN C 27  ? 0.55364 0.51984 0.49473 0.05948  -0.05917 0.03839  26  ASN B ND2   
2798 N N     . HIS C 28  ? 0.36060 0.24842 0.28803 0.04091  -0.02392 0.04311  27  HIS B N     
2799 C CA    . HIS C 28  ? 0.39292 0.25038 0.29996 0.03434  -0.01397 0.04673  27  HIS B CA    
2800 C C     . HIS C 28  ? 0.33354 0.19906 0.24898 0.01672  -0.00742 0.04058  27  HIS B C     
2801 O O     . HIS C 28  ? 0.32322 0.21270 0.25848 0.01283  -0.01039 0.03465  27  HIS B O     
2802 C CB    . HIS C 28  ? 0.47102 0.30227 0.36826 0.04148  -0.00886 0.04891  27  HIS B CB    
2803 C CG    . HIS C 28  ? 0.46237 0.30512 0.37852 0.03936  -0.00798 0.04156  27  HIS B CG    
2804 N ND1   . HIS C 28  ? 0.51855 0.35364 0.43583 0.02530  0.00058  0.03577  27  HIS B ND1   
2805 C CD2   . HIS C 28  ? 0.46733 0.33121 0.40203 0.04830  -0.01434 0.03823  27  HIS B CD2   
2806 C CE1   . HIS C 28  ? 0.48535 0.33398 0.41863 0.02687  -0.00085 0.03002  27  HIS B CE1   
2807 N NE2   . HIS C 28  ? 0.54265 0.40780 0.48673 0.04055  -0.00906 0.03158  27  HIS B NE2   
2808 N N     . PHE C 29  ? 0.42986 0.27585 0.32908 0.00649  0.00178  0.04218  28  PHE B N     
2809 C CA    . PHE C 29  ? 0.39330 0.25052 0.30038 -0.01023 0.00822  0.03584  28  PHE B CA    
2810 C C     . PHE C 29  ? 0.45387 0.29742 0.35928 -0.02001 0.01657  0.03096  28  PHE B C     
2811 O O     . PHE C 29  ? 0.48205 0.29294 0.36738 -0.02099 0.02425  0.03415  28  PHE B O     
2812 C CB    . PHE C 29  ? 0.39759 0.24795 0.29042 -0.01828 0.01429  0.03847  28  PHE B CB    
2813 C CG    . PHE C 29  ? 0.36166 0.22640 0.26368 -0.03530 0.02187  0.03115  28  PHE B CG    
2814 C CD1   . PHE C 29  ? 0.32670 0.22496 0.25185 -0.03706 0.01706  0.02497  28  PHE B CD1   
2815 C CD2   . PHE C 29  ? 0.41282 0.25825 0.29983 -0.04907 0.03413  0.03034  28  PHE B CD2   
2816 C CE1   . PHE C 29  ? 0.30918 0.22539 0.24385 -0.05017 0.02287  0.01823  28  PHE B CE1   
2817 C CE2   . PHE C 29  ? 0.39385 0.25841 0.29182 -0.06529 0.04086  0.02220  28  PHE B CE2   
2818 C CZ    . PHE C 29  ? 0.31974 0.22236 0.24268 -0.06474 0.03436  0.01615  28  PHE B CZ    
2819 N N     . VAL C 30  ? 0.45546 0.32265 0.37973 -0.02739 0.01548  0.02308  29  VAL B N     
2820 C CA    . VAL C 30  ? 0.45822 0.31954 0.38288 -0.03902 0.02240  0.01594  29  VAL B CA    
2821 C C     . VAL C 30  ? 0.45601 0.32248 0.37839 -0.05728 0.03088  0.01090  29  VAL B C     
2822 O O     . VAL C 30  ? 0.45284 0.35005 0.39026 -0.06170 0.02801  0.00722  29  VAL B O     
2823 C CB    . VAL C 30  ? 0.49541 0.38104 0.43920 -0.03671 0.01625  0.01019  29  VAL B CB    
2824 C CG1   . VAL C 30  ? 0.49682 0.37505 0.44203 -0.02109 0.01091  0.01377  29  VAL B CG1   
2825 C CG2   . VAL C 30  ? 0.49616 0.41515 0.45673 -0.03584 0.00966  0.00909  29  VAL B CG2   
2826 N N     . ASP C 31  ? 0.48138 0.31733 0.38456 -0.06774 0.04227  0.01042  30  ASP B N     
2827 C CA    . ASP C 31  ? 0.42505 0.26481 0.32529 -0.08794 0.05265  0.00442  30  ASP B CA    
2828 C C     . ASP C 31  ? 0.47994 0.34151 0.39424 -0.10337 0.05494  -0.00837 30  ASP B C     
2829 O O     . ASP C 31  ? 0.43449 0.32483 0.36079 -0.11672 0.05741  -0.01564 30  ASP B O     
2830 C CB    . ASP C 31  ? 0.58406 0.37824 0.45487 -0.09489 0.06594  0.00881  30  ASP B CB    
2831 C CG    . ASP C 31  ? 0.67922 0.48041 0.54732 -0.11431 0.07690  0.00318  30  ASP B CG    
2832 O OD1   . ASP C 31  ? 0.64069 0.45186 0.50841 -0.11427 0.07711  0.00758  30  ASP B OD1   
2833 O OD2   . ASP C 31  ? 0.76639 0.56693 0.63365 -0.12779 0.08467  -0.00661 30  ASP B OD2   
2834 N N     . GLU C 32  ? 0.51778 0.36748 0.43023 -0.10177 0.05445  -0.01193 31  GLU B N     
2835 C CA    . GLU C 32  ? 0.46697 0.33735 0.39019 -0.11614 0.05572  -0.02466 31  GLU B CA    
2836 C C     . GLU C 32  ? 0.39906 0.31360 0.34609 -0.10710 0.04259  -0.02629 31  GLU B C     
2837 O O     . GLU C 32  ? 0.46708 0.38596 0.41965 -0.08933 0.03376  -0.01832 31  GLU B O     
2838 C CB    . GLU C 32  ? 0.57489 0.41344 0.48459 -0.11686 0.06078  -0.02802 31  GLU B CB    
2839 C CG    . GLU C 32  ? 0.73861 0.56532 0.64781 -0.09382 0.05287  -0.01946 31  GLU B CG    
2840 C CD    . GLU C 32  ? 0.95642 0.74535 0.84917 -0.09164 0.06008  -0.02149 31  GLU B CD    
2841 O OE1   . GLU C 32  ? 0.90602 0.68093 0.78785 -0.10547 0.07012  -0.02909 31  GLU B OE1   
2842 O OE2   . GLU C 32  ? 0.96628 0.74782 0.86002 -0.07259 0.05454  -0.01546 31  GLU B OE2   
2843 N N     . TYR C 33  ? 0.40099 0.34819 0.36082 -0.11992 0.04196  -0.03691 32  TYR B N     
2844 C CA    . TYR C 33  ? 0.35029 0.33785 0.32939 -0.11071 0.03013  -0.03830 32  TYR B CA    
2845 C C     . TYR C 33  ? 0.30706 0.29352 0.28492 -0.10995 0.02707  -0.04361 32  TYR B C     
2846 O O     . TYR C 33  ? 0.34729 0.33692 0.32214 -0.12597 0.03186  -0.05468 32  TYR B O     
2847 C CB    . TYR C 33  ? 0.32476 0.35402 0.31913 -0.12098 0.02945  -0.04588 32  TYR B CB    
2848 C CG    . TYR C 33  ? 0.28830 0.35937 0.30007 -0.11037 0.01796  -0.04695 32  TYR B CG    
2849 C CD1   . TYR C 33  ? 0.23772 0.30626 0.25057 -0.09213 0.00940  -0.03940 32  TYR B CD1   
2850 C CD2   . TYR C 33  ? 0.32335 0.43686 0.34977 -0.11830 0.01632  -0.05554 32  TYR B CD2   
2851 C CE1   . TYR C 33  ? 0.26681 0.36761 0.29095 -0.08184 0.00041  -0.03918 32  TYR B CE1   
2852 C CE2   . TYR C 33  ? 0.31148 0.46146 0.35102 -0.10580 0.00577  -0.05533 32  TYR B CE2   
2853 C CZ    . TYR C 33  ? 0.27298 0.41359 0.30947 -0.08727 -0.00184 -0.04648 32  TYR B CZ    
2854 O OH    . TYR C 33  ? 0.25298 0.42412 0.29819 -0.07423 -0.01090 -0.04508 32  TYR B OH    
2855 N N     . ASP C 34  ? 0.25761 0.23912 0.23687 -0.09292 0.02019  -0.03664 33  ASP B N     
2856 C CA    . ASP C 34  ? 0.28083 0.26322 0.25900 -0.09010 0.01725  -0.04078 33  ASP B CA    
2857 C C     . ASP C 34  ? 0.26711 0.28289 0.25832 -0.07939 0.00700  -0.03824 33  ASP B C     
2858 O O     . ASP C 34  ? 0.22819 0.24112 0.22277 -0.06479 0.00262  -0.02940 33  ASP B O     
2859 C CB    . ASP C 34  ? 0.33562 0.28451 0.30449 -0.07826 0.01924  -0.03439 33  ASP B CB    
2860 C CG    . ASP C 34  ? 0.41829 0.36703 0.38599 -0.07393 0.01748  -0.03825 33  ASP B CG    
2861 O OD1   . ASP C 34  ? 0.38294 0.34865 0.35099 -0.08358 0.01677  -0.04737 33  ASP B OD1   
2862 O OD2   . ASP C 34  ? 0.46655 0.40078 0.43335 -0.06054 0.01661  -0.03237 33  ASP B OD2   
2863 N N     . PRO C 35  ? 0.23687 0.28435 0.23443 -0.08600 0.00318  -0.04587 34  PRO B N     
2864 C CA    . PRO C 35  ? 0.23041 0.30724 0.23722 -0.07339 -0.00617 -0.04188 34  PRO B CA    
2865 C C     . PRO C 35  ? 0.21974 0.28483 0.22195 -0.06007 -0.00944 -0.03596 34  PRO B C     
2866 O O     . PRO C 35  ? 0.25623 0.30694 0.25010 -0.06297 -0.00687 -0.03986 34  PRO B O     
2867 C CB    . PRO C 35  ? 0.27872 0.39002 0.28984 -0.08362 -0.00946 -0.05270 34  PRO B CB    
2868 C CG    . PRO C 35  ? 0.31068 0.41708 0.32065 -0.10403 -0.00087 -0.06209 34  PRO B CG    
2869 C CD    . PRO C 35  ? 0.29067 0.34985 0.28688 -0.10562 0.00757  -0.05869 34  PRO B CD    
2870 N N     . THR C 36  ? 0.18934 0.26011 0.19641 -0.04619 -0.01391 -0.02723 35  THR B N     
2871 C CA    . THR C 36  ? 0.20004 0.25862 0.20319 -0.03517 -0.01515 -0.02150 35  THR B CA    
2872 C C     . THR C 36  ? 0.20830 0.28269 0.20655 -0.03192 -0.01922 -0.02343 35  THR B C     
2873 O O     . THR C 36  ? 0.18568 0.28613 0.18621 -0.03042 -0.02436 -0.02484 35  THR B O     
2874 C CB    . THR C 36  ? 0.18189 0.23795 0.19000 -0.02386 -0.01689 -0.01252 35  THR B CB    
2875 O OG1   . THR C 36  ? 0.18888 0.23009 0.19890 -0.02636 -0.01369 -0.01063 35  THR B OG1   
2876 C CG2   . THR C 36  ? 0.20186 0.24634 0.20664 -0.01476 -0.01672 -0.00750 35  THR B CG2   
2877 N N     . ILE C 37  ? 0.19879 0.25828 0.18957 -0.02990 -0.01678 -0.02347 36  ILE B N     
2878 C CA    . ILE C 37  ? 0.18781 0.25588 0.17042 -0.02389 -0.01951 -0.02226 36  ILE B CA    
2879 C C     . ILE C 37  ? 0.18893 0.24692 0.17235 -0.01208 -0.01877 -0.01239 36  ILE B C     
2880 O O     . ILE C 37  ? 0.21221 0.28067 0.19387 -0.00346 -0.02239 -0.00674 36  ILE B O     
2881 C CB    . ILE C 37  ? 0.20127 0.25854 0.17398 -0.02994 -0.01541 -0.02907 36  ILE B CB    
2882 C CG1   . ILE C 37  ? 0.26347 0.33165 0.23313 -0.04351 -0.01586 -0.04047 36  ILE B CG1   
2883 C CG2   . ILE C 37  ? 0.19629 0.25749 0.15769 -0.02241 -0.01670 -0.02584 36  ILE B CG2   
2884 C CD1   . ILE C 37  ? 0.33176 0.43035 0.29810 -0.04291 -0.02344 -0.04299 36  ILE B CD1   
2885 N N     . GLU C 38  ? 0.19554 0.23350 0.18170 -0.01147 -0.01374 -0.01071 37  GLU B N     
2886 C CA    . GLU C 38  ? 0.18388 0.21283 0.17302 -0.00384 -0.01204 -0.00358 37  GLU B CA    
2887 C C     . GLU C 38  ? 0.18335 0.19736 0.17912 -0.00531 -0.00788 -0.00480 37  GLU B C     
2888 O O     . GLU C 38  ? 0.22561 0.23252 0.21917 -0.00844 -0.00441 -0.00965 37  GLU B O     
2889 C CB    . GLU C 38  ? 0.20927 0.23630 0.18791 0.00110  -0.01000 -0.00047 37  GLU B CB    
2890 C CG    . GLU C 38  ? 0.20723 0.22366 0.18699 0.00653  -0.00652 0.00592  37  GLU B CG    
2891 C CD    . GLU C 38  ? 0.21719 0.22511 0.18555 0.00825  -0.00078 0.00797  37  GLU B CD    
2892 O OE1   . GLU C 38  ? 0.24430 0.25316 0.19878 0.01376  -0.00152 0.01268  37  GLU B OE1   
2893 O OE2   . GLU C 38  ? 0.25503 0.25576 0.22770 0.00454  0.00494  0.00474  37  GLU B OE2   
2894 N N     . ASP C 39  ? 0.19245 0.20245 0.19558 -0.00207 -0.00825 -0.00083 38  ASP B N     
2895 C CA    . ASP C 39  ? 0.22205 0.22271 0.23193 -0.00117 -0.00581 -0.00171 38  ASP B CA    
2896 C C     . ASP C 39  ? 0.21777 0.21836 0.23337 0.00233  -0.00533 0.00177  38  ASP B C     
2897 O O     . ASP C 39  ? 0.20920 0.21218 0.22339 0.00374  -0.00700 0.00527  38  ASP B O     
2898 C CB    . ASP C 39  ? 0.22757 0.22290 0.23961 -0.00296 -0.00735 -0.00247 38  ASP B CB    
2899 C CG    . ASP C 39  ? 0.25922 0.24851 0.26483 -0.00856 -0.00504 -0.00774 38  ASP B CG    
2900 O OD1   . ASP C 39  ? 0.30497 0.28453 0.30917 -0.00735 -0.00118 -0.01084 38  ASP B OD1   
2901 O OD2   . ASP C 39  ? 0.29664 0.29185 0.29879 -0.01454 -0.00641 -0.00968 38  ASP B OD2   
2902 N N     . SER C 40  ? 0.20812 0.20680 0.23028 0.00349  -0.00233 -0.00020 39  SER B N     
2903 C CA    . SER C 40  ? 0.20971 0.21081 0.23856 0.00395  -0.00081 0.00055  39  SER B CA    
2904 C C     . SER C 40  ? 0.19530 0.20001 0.23492 0.00655  -0.00308 -0.00151 39  SER B C     
2905 O O     . SER C 40  ? 0.23230 0.23607 0.27466 0.00955  -0.00229 -0.00399 39  SER B O     
2906 C CB    . SER C 40  ? 0.22572 0.22670 0.25316 0.00202  0.00609  -0.00118 39  SER B CB    
2907 O OG    . SER C 40  ? 0.29773 0.29387 0.31194 0.00155  0.00796  0.00233  39  SER B OG    
2908 N N     . TYR C 41  ? 0.17076 0.17948 0.21535 0.00635  -0.00580 -0.00076 40  TYR B N     
2909 C CA    . TYR C 41  ? 0.16760 0.18312 0.22106 0.01009  -0.00984 -0.00233 40  TYR B CA    
2910 C C     . TYR C 41  ? 0.17253 0.19901 0.23518 0.00655  -0.00886 -0.00582 40  TYR B C     
2911 O O     . TYR C 41  ? 0.18207 0.20470 0.24086 0.00070  -0.00493 -0.00577 40  TYR B O     
2912 C CB    . TYR C 41  ? 0.21208 0.22244 0.25955 0.01212  -0.01549 0.00127  40  TYR B CB    
2913 C CG    . TYR C 41  ? 0.19553 0.19502 0.23373 0.01239  -0.01512 0.00348  40  TYR B CG    
2914 C CD1   . TYR C 41  ? 0.23014 0.22702 0.26131 0.00803  -0.01394 0.00489  40  TYR B CD1   
2915 C CD2   . TYR C 41  ? 0.26510 0.25725 0.30118 0.01710  -0.01547 0.00359  40  TYR B CD2   
2916 C CE1   . TYR C 41  ? 0.22195 0.21262 0.24614 0.00562  -0.01317 0.00473  40  TYR B CE1   
2917 C CE2   . TYR C 41  ? 0.31194 0.29137 0.33817 0.01464  -0.01331 0.00415  40  TYR B CE2   
2918 C CZ    . TYR C 41  ? 0.31460 0.29516 0.33598 0.00755  -0.01223 0.00395  40  TYR B CZ    
2919 O OH    . TYR C 41  ? 0.34330 0.31459 0.35636 0.00269  -0.00973 0.00253  40  TYR B OH    
2920 N N     . ARG C 42  ? 0.16637 0.20648 0.24042 0.01030  -0.01222 -0.00921 41  ARG B N     
2921 C CA    . ARG C 42  ? 0.14201 0.19835 0.22782 0.00512  -0.01125 -0.01514 41  ARG B CA    
2922 C C     . ARG C 42  ? 0.16790 0.23941 0.26135 0.01169  -0.01998 -0.01672 41  ARG B C     
2923 O O     . ARG C 42  ? 0.18997 0.26527 0.28663 0.02212  -0.02330 -0.01547 41  ARG B O     
2924 C CB    . ARG C 42  ? 0.17751 0.24374 0.27369 0.00268  -0.00376 -0.02028 41  ARG B CB    
2925 C CG    . ARG C 42  ? 0.16563 0.25059 0.27548 -0.00571 -0.00029 -0.02815 41  ARG B CG    
2926 C CD    . ARG C 42  ? 0.17954 0.26982 0.29607 -0.00935 0.00995  -0.03231 41  ARG B CD    
2927 N NE    . ARG C 42  ? 0.18461 0.29939 0.31905 -0.01736 0.01430  -0.04186 41  ARG B NE    
2928 C CZ    . ARG C 42  ? 0.15683 0.26967 0.29026 -0.03205 0.02215  -0.04630 41  ARG B CZ    
2929 N NH1   . ARG C 42  ? 0.21960 0.30559 0.33392 -0.03782 0.02540  -0.04103 41  ARG B NH1   
2930 N NH2   . ARG C 42  ? 0.17332 0.31148 0.32504 -0.04109 0.02773  -0.05669 41  ARG B NH2   
2931 N N     . LYS C 43  ? 0.15534 0.23426 0.24973 0.00650  -0.02348 -0.01949 42  LYS B N     
2932 C CA    . LYS C 43  ? 0.15720 0.25223 0.25603 0.01306  -0.03317 -0.02090 42  LYS B CA    
2933 C C     . LYS C 43  ? 0.14707 0.25885 0.25299 0.00279  -0.03424 -0.02910 42  LYS B C     
2934 O O     . LYS C 43  ? 0.17295 0.27199 0.27169 -0.00811 -0.02849 -0.03049 42  LYS B O     
2935 C CB    . LYS C 43  ? 0.25105 0.32876 0.33312 0.01862  -0.03840 -0.01325 42  LYS B CB    
2936 C CG    . LYS C 43  ? 0.30831 0.39654 0.38845 0.02855  -0.04842 -0.01180 42  LYS B CG    
2937 C CD    . LYS C 43  ? 0.36203 0.42761 0.42221 0.03084  -0.05005 -0.00390 42  LYS B CD    
2938 C CE    . LYS C 43  ? 0.38804 0.46007 0.44000 0.03823  -0.05931 -0.00190 42  LYS B CE    
2939 N NZ    . LYS C 43  ? 0.45518 0.53335 0.50938 0.05326  -0.06429 0.00114  42  LYS B NZ    
2940 N N     . GLN C 44  ? 0.14295 0.28271 0.26137 0.00707  -0.04187 -0.03463 43  GLN B N     
2941 C CA    . GLN C 44  ? 0.12941 0.28975 0.25474 -0.00341 -0.04469 -0.04433 43  GLN B CA    
2942 C C     . GLN C 44  ? 0.21787 0.37368 0.32872 0.00083  -0.05407 -0.04104 43  GLN B C     
2943 O O     . GLN C 44  ? 0.21893 0.37565 0.32405 0.01547  -0.06241 -0.03440 43  GLN B O     
2944 C CB    . GLN C 44  ? 0.13415 0.33443 0.28273 -0.00131 -0.04882 -0.05370 43  GLN B CB    
2945 C CG    . GLN C 44  ? 0.15646 0.38215 0.31324 -0.01438 -0.05205 -0.06590 43  GLN B CG    
2946 C CD    . GLN C 44  ? 0.19674 0.45418 0.37030 -0.01231 -0.05335 -0.07233 43  GLN B CD    
2947 O OE1   . GLN C 44  ? 0.24136 0.50621 0.42797 -0.01718 -0.04431 -0.07650 43  GLN B OE1   
2948 N NE2   . GLN C 44  ? 0.25703 0.53264 0.42893 -0.00489 -0.06406 -0.07299 43  GLN B NE2   
2949 N N     . VAL C 45  ? 0.15623 0.30400 0.25878 -0.01180 -0.05140 -0.04549 44  VAL B N     
2950 C CA    . VAL C 45  ? 0.20701 0.34984 0.29415 -0.01018 -0.05856 -0.04394 44  VAL B CA    
2951 C C     . VAL C 45  ? 0.19808 0.35948 0.28956 -0.02426 -0.05982 -0.05712 44  VAL B C     
2952 O O     . VAL C 45  ? 0.21426 0.38360 0.31739 -0.03792 -0.05222 -0.06660 44  VAL B O     
2953 C CB    . VAL C 45  ? 0.24303 0.35082 0.31114 -0.01134 -0.05213 -0.03596 44  VAL B CB    
2954 C CG1   . VAL C 45  ? 0.26963 0.36117 0.33427 -0.00082 -0.05006 -0.02519 44  VAL B CG1   
2955 C CG2   . VAL C 45  ? 0.26341 0.35666 0.33019 -0.02561 -0.04057 -0.04122 44  VAL B CG2   
2956 N N     . VAL C 46  ? 0.20336 0.37029 0.28335 -0.02225 -0.06861 -0.05833 45  VAL B N     
2957 C CA    . VAL C 46  ? 0.21768 0.39619 0.29610 -0.03748 -0.06902 -0.07147 45  VAL B CA    
2958 C C     . VAL C 46  ? 0.29219 0.43831 0.34736 -0.04131 -0.06402 -0.06813 45  VAL B C     
2959 O O     . VAL C 46  ? 0.36723 0.50173 0.40737 -0.02986 -0.06904 -0.05854 45  VAL B O     
2960 C CB    . VAL C 46  ? 0.29164 0.50290 0.37380 -0.03249 -0.08170 -0.07617 45  VAL B CB    
2961 C CG1   . VAL C 46  ? 0.32636 0.54160 0.40337 -0.04949 -0.07890 -0.08865 45  VAL B CG1   
2962 C CG2   . VAL C 46  ? 0.29273 0.52885 0.39571 -0.02570 -0.08307 -0.07638 45  VAL B CG2   
2963 N N     . ILE C 47  ? 0.28736 0.41705 0.33872 -0.05696 -0.05272 -0.07584 46  ILE B N     
2964 C CA    . ILE C 47  ? 0.28941 0.38741 0.31980 -0.05986 -0.04581 -0.07369 46  ILE B CA    
2965 C C     . ILE C 47  ? 0.33397 0.43514 0.35952 -0.07739 -0.04243 -0.08932 46  ILE B C     
2966 O O     . ILE C 47  ? 0.32084 0.42063 0.35434 -0.09189 -0.03318 -0.09866 46  ILE B O     
2967 C CB    . ILE C 47  ? 0.25672 0.32224 0.28270 -0.05872 -0.03281 -0.06583 46  ILE B CB    
2968 C CG1   . ILE C 47  ? 0.22103 0.28369 0.25130 -0.04369 -0.03552 -0.05209 46  ILE B CG1   
2969 C CG2   . ILE C 47  ? 0.31301 0.34926 0.31888 -0.06029 -0.02536 -0.06500 46  ILE B CG2   
2970 C CD1   . ILE C 47  ? 0.25915 0.29969 0.28974 -0.04371 -0.02420 -0.04652 46  ILE B CD1   
2971 N N     . ASP C 48  ? 0.36567 0.46838 0.37600 -0.07731 -0.04847 -0.09260 47  ASP B N     
2972 C CA    . ASP C 48  ? 0.43467 0.54057 0.43757 -0.09473 -0.04592 -0.10906 47  ASP B CA    
2973 C C     . ASP C 48  ? 0.38036 0.51440 0.40218 -0.10270 -0.04715 -0.11713 47  ASP B C     
2974 O O     . ASP C 48  ? 0.43363 0.55874 0.45618 -0.11770 -0.03581 -0.12628 47  ASP B O     
2975 C CB    . ASP C 48  ? 0.42474 0.48931 0.41243 -0.10417 -0.02882 -0.11181 47  ASP B CB    
2976 C CG    . ASP C 48  ? 0.47512 0.51009 0.44703 -0.08957 -0.02487 -0.09789 47  ASP B CG    
2977 O OD1   . ASP C 48  ? 0.47211 0.51651 0.43863 -0.07729 -0.03482 -0.08996 47  ASP B OD1   
2978 O OD2   . ASP C 48  ? 0.42395 0.42665 0.38850 -0.09002 -0.01136 -0.09482 47  ASP B OD2   
2979 N N     . GLY C 49  ? 0.34323 0.51003 0.37917 -0.09131 -0.05986 -0.11298 48  GLY B N     
2980 C CA    . GLY C 49  ? 0.33031 0.52835 0.38469 -0.09592 -0.06207 -0.12020 48  GLY B CA    
2981 C C     . GLY C 49  ? 0.34725 0.54571 0.41913 -0.10387 -0.05086 -0.12280 48  GLY B C     
2982 O O     . GLY C 49  ? 0.46285 0.68604 0.54912 -0.11104 -0.04965 -0.13117 48  GLY B O     
2983 N N     . GLU C 50  ? 0.34531 0.51765 0.41543 -0.10319 -0.04215 -0.11633 49  GLU B N     
2984 C CA    . GLU C 50  ? 0.31777 0.48507 0.40027 -0.11057 -0.03005 -0.11750 49  GLU B CA    
2985 C C     . GLU C 50  ? 0.26661 0.43947 0.36011 -0.09587 -0.03463 -0.10677 49  GLU B C     
2986 O O     . GLU C 50  ? 0.29028 0.44729 0.37476 -0.08636 -0.03822 -0.09827 49  GLU B O     
2987 C CB    . GLU C 50  ? 0.39431 0.51932 0.46094 -0.12317 -0.01313 -0.11897 49  GLU B CB    
2988 C CG    . GLU C 50  ? 0.42704 0.54437 0.48251 -0.13820 -0.00619 -0.13030 49  GLU B CG    
2989 C CD    . GLU C 50  ? 0.64381 0.71352 0.67818 -0.14626 0.01030  -0.12980 49  GLU B CD    
2990 O OE1   . GLU C 50  ? 0.64945 0.69222 0.67847 -0.14080 0.01726  -0.12068 49  GLU B OE1   
2991 O OE2   . GLU C 50  ? 0.70237 0.76104 0.72462 -0.15704 0.01659  -0.13828 49  GLU B OE2   
2992 N N     . THR C 51  ? 0.28127 0.47733 0.39390 -0.09409 -0.03398 -0.10800 50  THR B N     
2993 C CA    . THR C 51  ? 0.23213 0.43514 0.35616 -0.07974 -0.03744 -0.09887 50  THR B CA    
2994 C C     . THR C 51  ? 0.21529 0.38969 0.33676 -0.08620 -0.02370 -0.09549 50  THR B C     
2995 O O     . THR C 51  ? 0.23346 0.39480 0.35291 -0.10110 -0.01007 -0.10121 50  THR B O     
2996 C CB    . THR C 51  ? 0.24576 0.48270 0.38996 -0.07614 -0.03975 -0.10287 50  THR B CB    
2997 O OG1   . THR C 51  ? 0.30420 0.56752 0.44974 -0.06996 -0.05220 -0.10607 50  THR B OG1   
2998 C CG2   . THR C 51  ? 0.23645 0.47807 0.39034 -0.05985 -0.04278 -0.09356 50  THR B CG2   
2999 N N     . SER C 52  ? 0.21141 0.36695 0.32543 -0.07108 -0.02549 -0.08183 51  SER B N     
3000 C CA    . SER C 52  ? 0.17220 0.29430 0.27664 -0.07159 -0.01293 -0.07378 51  SER B CA    
3001 C C     . SER C 52  ? 0.19541 0.31848 0.30472 -0.05572 -0.01605 -0.06317 51  SER B C     
3002 O O     . SER C 52  ? 0.22190 0.35420 0.33176 -0.04143 -0.02711 -0.05734 51  SER B O     
3003 C CB    . SER C 52  ? 0.24993 0.33527 0.33086 -0.06948 -0.00931 -0.06635 51  SER B CB    
3004 O OG    . SER C 52  ? 0.30270 0.37681 0.37500 -0.08494 -0.00220 -0.07596 51  SER B OG    
3005 N N     . LEU C 53  ? 0.17767 0.28774 0.28745 -0.05867 -0.00524 -0.06063 52  LEU B N     
3006 C CA    . LEU C 53  ? 0.15631 0.25791 0.26456 -0.04564 -0.00558 -0.05046 52  LEU B CA    
3007 C C     . LEU C 53  ? 0.19102 0.25825 0.27838 -0.04188 -0.00167 -0.04041 52  LEU B C     
3008 O O     . LEU C 53  ? 0.19515 0.24114 0.27127 -0.05030 0.00814  -0.04070 52  LEU B O     
3009 C CB    . LEU C 53  ? 0.17894 0.28904 0.29885 -0.05001 0.00354  -0.05383 52  LEU B CB    
3010 C CG    . LEU C 53  ? 0.23183 0.38156 0.37655 -0.05286 0.00110  -0.06470 52  LEU B CG    
3011 C CD1   . LEU C 53  ? 0.20674 0.36152 0.36095 -0.06043 0.01390  -0.06897 52  LEU B CD1   
3012 C CD2   . LEU C 53  ? 0.26797 0.43790 0.42178 -0.03491 -0.01202 -0.06128 52  LEU B CD2   
3013 N N     . LEU C 54  ? 0.15671 0.21860 0.23817 -0.02920 -0.00901 -0.03195 53  LEU B N     
3014 C CA    . LEU C 54  ? 0.17779 0.21469 0.24319 -0.02449 -0.00636 -0.02313 53  LEU B CA    
3015 C C     . LEU C 54  ? 0.18932 0.22262 0.25516 -0.01873 -0.00387 -0.01805 53  LEU B C     
3016 O O     . LEU C 54  ? 0.17863 0.22271 0.25162 -0.01160 -0.00908 -0.01702 53  LEU B O     
3017 C CB    . LEU C 54  ? 0.17174 0.20483 0.22909 -0.01718 -0.01431 -0.01835 53  LEU B CB    
3018 C CG    . LEU C 54  ? 0.17622 0.21494 0.23172 -0.02197 -0.01803 -0.02392 53  LEU B CG    
3019 C CD1   . LEU C 54  ? 0.21339 0.24555 0.25798 -0.01524 -0.02383 -0.01865 53  LEU B CD1   
3020 C CD2   . LEU C 54  ? 0.24026 0.26696 0.29018 -0.03313 -0.00922 -0.02950 53  LEU B CD2   
3021 N N     . ASP C 55  ? 0.17341 0.19006 0.22948 -0.02111 0.00429  -0.01490 54  ASP B N     
3022 C CA    . ASP C 55  ? 0.17263 0.18388 0.22452 -0.01593 0.00637  -0.00995 54  ASP B CA    
3023 C C     . ASP C 55  ? 0.20811 0.20611 0.24668 -0.00995 0.00402  -0.00290 54  ASP B C     
3024 O O     . ASP C 55  ? 0.26297 0.24704 0.29061 -0.01079 0.00840  -0.00046 54  ASP B O     
3025 C CB    . ASP C 55  ? 0.19600 0.19915 0.24364 -0.02217 0.01719  -0.01100 54  ASP B CB    
3026 C CG    . ASP C 55  ? 0.25753 0.27648 0.31997 -0.03059 0.02168  -0.01957 54  ASP B CG    
3027 O OD1   . ASP C 55  ? 0.24220 0.28035 0.31889 -0.02675 0.01761  -0.02278 54  ASP B OD1   
3028 O OD2   . ASP C 55  ? 0.27765 0.28915 0.33684 -0.04099 0.03015  -0.02337 54  ASP B OD2   
3029 N N     . ILE C 56  ? 0.17835 0.18045 0.21746 -0.00388 -0.00199 -0.00005 55  ILE B N     
3030 C CA    . ILE C 56  ? 0.18339 0.17940 0.21344 0.00041  -0.00470 0.00482  55  ILE B CA    
3031 C C     . ILE C 56  ? 0.18346 0.17859 0.20850 0.00313  -0.00392 0.00743  55  ILE B C     
3032 O O     . ILE C 56  ? 0.20625 0.20585 0.23558 0.00334  -0.00497 0.00564  55  ILE B O     
3033 C CB    . ILE C 56  ? 0.22284 0.22367 0.25538 0.00251  -0.01124 0.00502  55  ILE B CB    
3034 C CG1   . ILE C 56  ? 0.27652 0.27958 0.31160 -0.00040 -0.01261 0.00174  55  ILE B CG1   
3035 C CG2   . ILE C 56  ? 0.24214 0.24019 0.26742 0.00525  -0.01260 0.00877  55  ILE B CG2   
3036 C CD1   . ILE C 56  ? 0.35443 0.36321 0.39096 0.00207  -0.01913 0.00172  55  ILE B CD1   
3037 N N     . LEU C 57  ? 0.17221 0.16171 0.18729 0.00588  -0.00197 0.01117  56  LEU B N     
3038 C CA    . LEU C 57  ? 0.17364 0.16620 0.18245 0.00878  -0.00291 0.01320  56  LEU B CA    
3039 C C     . LEU C 57  ? 0.17516 0.17550 0.18422 0.01123  -0.00806 0.01423  56  LEU B C     
3040 O O     . LEU C 57  ? 0.20725 0.20697 0.21362 0.01494  -0.00839 0.01662  56  LEU B O     
3041 C CB    . LEU C 57  ? 0.22635 0.21034 0.22250 0.01220  0.00183  0.01720  56  LEU B CB    
3042 C CG    . LEU C 57  ? 0.22075 0.21129 0.20854 0.01601  -0.00048 0.01901  56  LEU B CG    
3043 C CD1   . LEU C 57  ? 0.27070 0.26454 0.26096 0.01116  0.00061  0.01477  56  LEU B CD1   
3044 C CD2   . LEU C 57  ? 0.26738 0.24802 0.23934 0.02231  0.00336  0.02474  56  LEU B CD2   
3045 N N     . ASP C 58  ? 0.19390 0.20069 0.20601 0.00853  -0.01081 0.01167  57  ASP B N     
3046 C CA    . ASP C 58  ? 0.20266 0.21829 0.21553 0.00754  -0.01411 0.01100  57  ASP B CA    
3047 C C     . ASP C 58  ? 0.21369 0.23964 0.22139 0.00849  -0.01538 0.01035  57  ASP B C     
3048 O O     . ASP C 58  ? 0.22004 0.24573 0.22501 0.00526  -0.01469 0.00743  57  ASP B O     
3049 C CB    . ASP C 58  ? 0.23587 0.24807 0.25209 0.00248  -0.01460 0.00800  57  ASP B CB    
3050 C CG    . ASP C 58  ? 0.27804 0.29622 0.29411 -0.00162 -0.01571 0.00658  57  ASP B CG    
3051 O OD1   . ASP C 58  ? 0.25188 0.28009 0.26882 0.00021  -0.01672 0.00774  57  ASP B OD1   
3052 O OD2   . ASP C 58  ? 0.26525 0.27700 0.27979 -0.00670 -0.01446 0.00400  57  ASP B OD2   
3053 N N     . THR C 59  ? 0.19163 0.22772 0.19725 0.01399  -0.01731 0.01276  58  THR B N     
3054 C CA    . THR C 59  ? 0.20000 0.25064 0.20021 0.01748  -0.02019 0.01261  58  THR B CA    
3055 C C     . THR C 59  ? 0.20298 0.27420 0.20924 0.01173  -0.02367 0.00710  58  THR B C     
3056 O O     . THR C 59  ? 0.19850 0.27196 0.21197 0.00673  -0.02294 0.00499  58  THR B O     
3057 C CB    . THR C 59  ? 0.21587 0.26748 0.20927 0.02973  -0.02044 0.01878  58  THR B CB    
3058 O OG1   . THR C 59  ? 0.21616 0.27746 0.21648 0.03328  -0.02161 0.01903  58  THR B OG1   
3059 C CG2   . THR C 59  ? 0.22932 0.25691 0.21514 0.03271  -0.01468 0.02340  58  THR B CG2   
3060 N N     . ALA C 60  ? 0.19274 0.27951 0.19493 0.01127  -0.02695 0.00414  59  ALA B N     
3061 C CA    . ALA C 60  ? 0.20837 0.32059 0.21680 0.00493  -0.03038 -0.00260 59  ALA B CA    
3062 C C     . ALA C 60  ? 0.22280 0.35640 0.23716 0.01452  -0.03358 -0.00008 59  ALA B C     
3063 O O     . ALA C 60  ? 0.25367 0.38599 0.26190 0.02879  -0.03501 0.00686  59  ALA B O     
3064 C CB    . ALA C 60  ? 0.21842 0.34425 0.21962 0.00191  -0.03387 -0.00758 59  ALA B CB    
3065 N N     . GLY C 61  ? 0.16433 0.31768 0.18960 0.00672  -0.03379 -0.00620 60  GLY B N     
3066 C CA    . GLY C 61  ? 0.19045 0.37084 0.22458 0.01526  -0.03634 -0.00589 60  GLY B CA    
3067 C C     . GLY C 61  ? 0.30310 0.51983 0.33920 0.01912  -0.04360 -0.01024 60  GLY B C     
3068 O O     . GLY C 61  ? 0.46430 0.71128 0.51246 0.00957  -0.04478 -0.01915 60  GLY B O     
3069 N N     . GLN C 62  ? 0.29126 0.50536 0.31510 0.03080  -0.04783 -0.00499 61  GLN B N     
3070 C CA    . GLN C 62  ? 0.39574 0.63453 0.41562 0.03840  -0.05367 -0.00652 61  GLN B CA    
3071 C C     . GLN C 62  ? 0.31054 0.53145 0.31542 0.05894  -0.05392 0.00535  61  GLN B C     
3072 O O     . GLN C 62  ? 0.36293 0.55520 0.35724 0.06253  -0.05117 0.01255  61  GLN B O     
3073 C CB    . GLN C 62  ? 0.39067 0.63270 0.40307 0.02609  -0.05624 -0.01344 61  GLN B CB    
3074 C CG    . GLN C 62  ? 0.31033 0.51780 0.30808 0.02467  -0.05309 -0.00858 61  GLN B CG    
3075 C CD    . GLN C 62  ? 0.48558 0.68953 0.46443 0.03731  -0.05673 -0.00225 61  GLN B CD    
3076 O OE1   . GLN C 62  ? 0.46530 0.68890 0.43972 0.03616  -0.06128 -0.00717 61  GLN B OE1   
3077 N NE2   . GLN C 62  ? 0.38043 0.55185 0.34751 0.04712  -0.05155 0.00825  61  GLN B NE2   
3078 N N     . GLU C 63  ? 0.41646 0.65257 0.41935 0.07217  -0.05616 0.00733  62  GLU B N     
3079 C CA    . GLU C 63  ? 0.48774 0.70256 0.47335 0.09101  -0.05486 0.01847  62  GLU B CA    
3080 C C     . GLU C 63  ? 0.49207 0.71002 0.46182 0.09587  -0.05910 0.02016  62  GLU B C     
3081 O O     . GLU C 63  ? 0.45398 0.65634 0.40760 0.11178  -0.05784 0.02909  62  GLU B O     
3082 C CB    . GLU C 63  ? 0.48709 0.70626 0.47664 0.10607  -0.05261 0.02210  62  GLU B CB    
3083 C CG    . GLU C 63  ? 0.47930 0.68280 0.47755 0.10346  -0.04670 0.02321  62  GLU B CG    
3084 C CD    . GLU C 63  ? 0.56037 0.76319 0.55949 0.11877  -0.04315 0.02677  62  GLU B CD    
3085 O OE1   . GLU C 63  ? 0.53795 0.77234 0.54911 0.12112  -0.04550 0.02130  62  GLU B OE1   
3086 O OE2   . GLU C 63  ? 0.52549 0.69548 0.51257 0.12785  -0.03724 0.03442  62  GLU B OE2   
3087 N N     . GLU C 64  ? 0.41067 0.64622 0.38299 0.08189  -0.06326 0.01144  63  GLU B N     
3088 C CA    . GLU C 64  ? 0.51534 0.74938 0.47025 0.08390  -0.06664 0.01261  63  GLU B CA    
3089 C C     . GLU C 64  ? 0.38368 0.58016 0.32005 0.08442  -0.06181 0.02044  63  GLU B C     
3090 O O     . GLU C 64  ? 0.44534 0.62046 0.38445 0.08125  -0.05663 0.02346  63  GLU B O     
3091 C CB    . GLU C 64  ? 0.49671 0.75579 0.45848 0.06614  -0.07073 -0.00043 63  GLU B CB    
3092 C CG    . GLU C 64  ? 0.51844 0.81096 0.50217 0.05695  -0.07216 -0.01109 63  GLU B CG    
3093 C CD    . GLU C 64  ? 0.62321 0.94548 0.60972 0.07044  -0.07701 -0.01104 63  GLU B CD    
3094 O OE1   . GLU C 64  ? 0.65615 0.97395 0.64201 0.08785  -0.07592 -0.00270 63  GLU B OE1   
3095 O OE2   . GLU C 64  ? 0.58289 0.93309 0.57166 0.06366  -0.08162 -0.01990 63  GLU B OE2   
3096 N N     . TYR C 65  ? 0.46213 0.65157 0.37870 0.08826  -0.06312 0.02351  64  TYR B N     
3097 C CA    . TYR C 65  ? 0.37881 0.53370 0.27435 0.08858  -0.05707 0.03069  64  TYR B CA    
3098 C C     . TYR C 65  ? 0.40945 0.53187 0.29667 0.10130  -0.04939 0.04268  64  TYR B C     
3099 O O     . TYR C 65  ? 0.38936 0.48698 0.27526 0.09674  -0.04252 0.04572  64  TYR B O     
3100 C CB    . TYR C 65  ? 0.37349 0.52369 0.27257 0.07101  -0.05478 0.02328  64  TYR B CB    
3101 C CG    . TYR C 65  ? 0.30679 0.48422 0.21129 0.05708  -0.06045 0.01002  64  TYR B CG    
3102 C CD1   . TYR C 65  ? 0.30508 0.48671 0.19274 0.05788  -0.06299 0.00864  64  TYR B CD1   
3103 C CD2   . TYR C 65  ? 0.25953 0.45532 0.18505 0.04204  -0.06197 -0.00140 64  TYR B CD2   
3104 C CE1   . TYR C 65  ? 0.26914 0.47379 0.16086 0.04413  -0.06731 -0.00452 64  TYR B CE1   
3105 C CE2   . TYR C 65  ? 0.23556 0.45158 0.16519 0.02722  -0.06484 -0.01453 64  TYR B CE2   
3106 C CZ    . TYR C 65  ? 0.24040 0.46102 0.15355 0.02815  -0.06756 -0.01644 64  TYR B CZ    
3107 O OH    . TYR C 65  ? 0.27269 0.51107 0.18733 0.01354  -0.06976 -0.02970 64  TYR B OH    
3108 N N     . SER C 66  ? 0.48824 0.61065 0.36859 0.11732  -0.05005 0.04890  65  SER B N     
3109 C CA    . SER C 66  ? 0.42449 0.51691 0.29763 0.12908  -0.04202 0.05825  65  SER B CA    
3110 C C     . SER C 66  ? 0.40784 0.45814 0.25926 0.12707  -0.03186 0.06584  65  SER B C     
3111 O O     . SER C 66  ? 0.47051 0.49343 0.32170 0.12627  -0.02327 0.06953  65  SER B O     
3112 C CB    . SER C 66  ? 0.50285 0.60347 0.36921 0.14764  -0.04435 0.06285  65  SER B CB    
3113 O OG    . SER C 66  ? 0.59298 0.69941 0.44240 0.15259  -0.04848 0.06493  65  SER B OG    
3114 N N     . ALA C 67  ? 0.40496 0.45068 0.23898 0.12387  -0.03192 0.06683  66  ALA B N     
3115 C CA    . ALA C 67  ? 0.41439 0.42146 0.22715 0.11981  -0.02044 0.07305  66  ALA B CA    
3116 C C     . ALA C 67  ? 0.49501 0.49018 0.31732 0.10566  -0.01430 0.06970  66  ALA B C     
3117 O O     . ALA C 67  ? 0.45180 0.41450 0.26826 0.10324  -0.00298 0.07429  66  ALA B O     
3118 C CB    . ALA C 67  ? 0.53437 0.54243 0.32697 0.11793  -0.02154 0.07345  66  ALA B CB    
3119 N N     . MET C 68  ? 0.40700 0.42831 0.24546 0.09484  -0.02093 0.06032  67  MET B N     
3120 C CA    . MET C 68  ? 0.38598 0.39797 0.24625 0.07766  -0.01449 0.05269  67  MET B CA    
3121 C C     . MET C 68  ? 0.35139 0.35685 0.22662 0.08037  -0.01277 0.05435  67  MET B C     
3122 O O     . MET C 68  ? 0.38835 0.37081 0.26852 0.07290  -0.00379 0.05421  67  MET B O     
3123 C CB    . MET C 68  ? 0.33542 0.37360 0.21411 0.06404  -0.02072 0.04025  67  MET B CB    
3124 C CG    . MET C 68  ? 0.31710 0.34337 0.21384 0.04903  -0.01396 0.03363  67  MET B CG    
3125 S SD    . MET C 68  ? 0.44784 0.44655 0.33029 0.04258  -0.00140 0.03497  67  MET B SD    
3126 C CE    . MET C 68  ? 0.46223 0.47543 0.32723 0.04246  -0.00592 0.03147  67  MET B CE    
3127 N N     . ARG C 69  ? 0.34450 0.37274 0.22824 0.09016  -0.02120 0.05462  68  ARG B N     
3128 C CA    . ARG C 69  ? 0.33851 0.36132 0.23642 0.09168  -0.01892 0.05485  68  ARG B CA    
3129 C C     . ARG C 69  ? 0.37395 0.36171 0.25419 0.10216  -0.00955 0.06460  68  ARG B C     
3130 O O     . ARG C 69  ? 0.34636 0.31692 0.23494 0.09631  -0.00304 0.06310  68  ARG B O     
3131 C CB    . ARG C 69  ? 0.38297 0.44011 0.29581 0.09872  -0.02850 0.05170  68  ARG B CB    
3132 C CG    . ARG C 69  ? 0.32861 0.41518 0.25976 0.08374  -0.03491 0.04033  68  ARG B CG    
3133 C CD    . ARG C 69  ? 0.42780 0.55090 0.37420 0.08845  -0.04294 0.03606  68  ARG B CD    
3134 N NE    . ARG C 69  ? 0.41459 0.53204 0.37276 0.09126  -0.03927 0.03708  68  ARG B NE    
3135 C CZ    . ARG C 69  ? 0.39937 0.51060 0.37216 0.07712  -0.03552 0.03146  68  ARG B CZ    
3136 N NH1   . ARG C 69  ? 0.34400 0.45140 0.32184 0.06054  -0.03448 0.02515  68  ARG B NH1   
3137 N NH2   . ARG C 69  ? 0.34829 0.45580 0.32896 0.08089  -0.03242 0.03241  68  ARG B NH2   
3138 N N     . ASP C 70  ? 0.41213 0.38847 0.27146 0.11327  -0.00745 0.07116  69  ASP B N     
3139 C CA    . ASP C 70  ? 0.42593 0.36442 0.26893 0.11823  0.00427  0.07739  69  ASP B CA    
3140 C C     . ASP C 70  ? 0.43774 0.34538 0.27413 0.10425  0.01577  0.07790  69  ASP B C     
3141 O O     . ASP C 70  ? 0.38354 0.26553 0.21908 0.10060  0.02516  0.07816  69  ASP B O     
3142 C CB    . ASP C 70  ? 0.43553 0.36594 0.25680 0.13081  0.00534  0.08341  69  ASP B CB    
3143 C CG    . ASP C 70  ? 0.46577 0.42354 0.29277 0.14643  -0.00370 0.08332  69  ASP B CG    
3144 O OD1   . ASP C 70  ? 0.47265 0.45298 0.32039 0.14688  -0.00893 0.07838  69  ASP B OD1   
3145 O OD2   . ASP C 70  ? 0.50891 0.46573 0.31900 0.15794  -0.00495 0.08811  69  ASP B OD2   
3146 N N     . GLN C 71  ? 0.40845 0.32132 0.24346 0.09369  0.01583  0.07529  70  GLN B N     
3147 C CA    . GLN C 71  ? 0.35917 0.25105 0.19728 0.07640  0.02745  0.07097  70  GLN B CA    
3148 C C     . GLN C 71  ? 0.39317 0.29367 0.25948 0.06431  0.02669  0.06193  70  GLN B C     
3149 O O     . GLN C 71  ? 0.35109 0.23129 0.21940 0.05473  0.03646  0.05974  70  GLN B O     
3150 C CB    . GLN C 71  ? 0.39524 0.29523 0.23084 0.06680  0.02825  0.06698  70  GLN B CB    
3151 C CG    . GLN C 71  ? 0.40998 0.28936 0.24642 0.05134  0.04183  0.06335  70  GLN B CG    
3152 C CD    . GLN C 71  ? 0.46014 0.30060 0.27074 0.05392  0.05585  0.07177  70  GLN B CD    
3153 O OE1   . GLN C 71  ? 0.48989 0.31511 0.27262 0.06501  0.05828  0.08085  70  GLN B OE1   
3154 N NE2   . GLN C 71  ? 0.45750 0.28225 0.27753 0.04320  0.06489  0.06776  70  GLN B NE2   
3155 N N     . TYR C 72  ? 0.31158 0.24215 0.19864 0.06395  0.01551  0.05627  71  TYR B N     
3156 C CA    . TYR C 72  ? 0.28749 0.22456 0.19739 0.05452  0.01446  0.04914  71  TYR B CA    
3157 C C     . TYR C 72  ? 0.32732 0.24389 0.23237 0.05917  0.02024  0.05232  71  TYR B C     
3158 O O     . TYR C 72  ? 0.33645 0.24380 0.25092 0.04864  0.02520  0.04732  71  TYR B O     
3159 C CB    . TYR C 72  ? 0.28457 0.25204 0.21173 0.05587  0.00322  0.04466  71  TYR B CB    
3160 C CG    . TYR C 72  ? 0.28300 0.27160 0.21799 0.04891  -0.00275 0.03883  71  TYR B CG    
3161 C CD1   . TYR C 72  ? 0.31838 0.30069 0.25035 0.04046  0.00158  0.03600  71  TYR B CD1   
3162 C CD2   . TYR C 72  ? 0.27402 0.28853 0.21921 0.05009  -0.01151 0.03518  71  TYR B CD2   
3163 C CE1   . TYR C 72  ? 0.29759 0.29628 0.23526 0.03442  -0.00290 0.02979  71  TYR B CE1   
3164 C CE2   . TYR C 72  ? 0.26167 0.29233 0.21238 0.04213  -0.01569 0.02865  71  TYR B CE2   
3165 C CZ    . TYR C 72  ? 0.27039 0.29147 0.21691 0.03464  -0.01137 0.02597  71  TYR B CZ    
3166 O OH    . TYR C 72  ? 0.24542 0.27929 0.19553 0.02682  -0.01439 0.01864  71  TYR B OH    
3167 N N     . MET C 73  ? 0.34369 0.25396 0.23366 0.07569  0.01950  0.06005  72  MET B N     
3168 C CA    . MET C 73  ? 0.34832 0.23722 0.23204 0.08199  0.02565  0.06269  72  MET B CA    
3169 C C     . MET C 73  ? 0.36241 0.21087 0.22555 0.07754  0.04013  0.06613  72  MET B C     
3170 O O     . MET C 73  ? 0.38213 0.21160 0.24633 0.07110  0.04762  0.06270  72  MET B O     
3171 C CB    . MET C 73  ? 0.32891 0.22739 0.20547 0.10284  0.02013  0.06894  72  MET B CB    
3172 C CG    . MET C 73  ? 0.37268 0.31014 0.27316 0.10285  0.00860  0.06308  72  MET B CG    
3173 S SD    . MET C 73  ? 0.38265 0.34588 0.28368 0.12130  0.00151  0.06495  72  MET B SD    
3174 C CE    . MET C 73  ? 0.35757 0.36321 0.28715 0.11513  -0.00897 0.05702  72  MET B CE    
3175 N N     . ARG C 74  ? 0.36388 0.19907 0.20816 0.07840  0.04500  0.07157  73  ARG B N     
3176 C CA    . ARG C 74  ? 0.39636 0.19747 0.22435 0.06937  0.05981  0.07174  73  ARG B CA    
3177 C C     . ARG C 74  ? 0.41967 0.21821 0.26353 0.04773  0.06625  0.06261  73  ARG B C     
3178 O O     . ARG C 74  ? 0.43491 0.20778 0.27333 0.03833  0.07782  0.05957  73  ARG B O     
3179 C CB    . ARG C 74  ? 0.45791 0.25571 0.26783 0.07284  0.06148  0.07682  73  ARG B CB    
3180 C CG    . ARG C 74  ? 0.64677 0.41352 0.43755 0.06574  0.07585  0.07755  73  ARG B CG    
3181 C CD    . ARG C 74  ? 0.58275 0.35063 0.35379 0.07561  0.07377  0.08423  73  ARG B CD    
3182 N NE    . ARG C 74  ? 0.56270 0.34478 0.32847 0.09647  0.06285  0.08970  73  ARG B NE    
3183 C CZ    . ARG C 74  ? 0.51407 0.32374 0.28014 0.10591  0.05064  0.09215  73  ARG B CZ    
3184 N NH1   . ARG C 74  ? 0.52751 0.35186 0.29560 0.09755  0.04748  0.09032  73  ARG B NH1   
3185 N NH2   . ARG C 74  ? 0.50814 0.33217 0.27201 0.12376  0.04201  0.09552  73  ARG B NH2   
3186 N N     . THR C 75  ? 0.35865 0.18808 0.22444 0.03861  0.05841  0.05566  74  THR B N     
3187 C CA    . THR C 75  ? 0.36419 0.20213 0.25003 0.01975  0.06184  0.04512  74  THR B CA    
3188 C C     . THR C 75  ? 0.33926 0.18866 0.24535 0.01473  0.05682  0.03774  74  THR B C     
3189 O O     . THR C 75  ? 0.35355 0.19939 0.26855 0.00062  0.06288  0.03002  74  THR B O     
3190 C CB    . THR C 75  ? 0.36049 0.22526 0.26012 0.01530  0.05550  0.04112  74  THR B CB    
3191 O OG1   . THR C 75  ? 0.40892 0.26202 0.28805 0.01773  0.06164  0.04672  74  THR B OG1   
3192 C CG2   . THR C 75  ? 0.42345 0.30110 0.34532 -0.00071 0.05806  0.03052  74  THR B CG2   
3193 N N     . GLY C 76  ? 0.30445 0.16887 0.21739 0.02531  0.04630  0.03935  75  GLY B N     
3194 C CA    . GLY C 76  ? 0.28919 0.16474 0.21904 0.02067  0.04157  0.03270  75  GLY B CA    
3195 C C     . GLY C 76  ? 0.31503 0.16395 0.23450 0.01768  0.05107  0.03115  75  GLY B C     
3196 O O     . GLY C 76  ? 0.34468 0.16631 0.24255 0.02659  0.05881  0.03776  75  GLY B O     
3197 N N     . GLU C 77  ? 0.28071 0.13655 0.21412 0.00510  0.05086  0.02195  76  GLU B N     
3198 C CA    . GLU C 77  ? 0.31140 0.14456 0.23631 -0.00051 0.05933  0.01767  76  GLU B CA    
3199 C C     . GLU C 77  ? 0.30161 0.13925 0.22872 0.00792  0.05360  0.01724  76  GLU B C     
3200 O O     . GLU C 77  ? 0.33436 0.14629 0.24713 0.00982  0.06186  0.01664  76  GLU B O     
3201 C CB    . GLU C 77  ? 0.32764 0.16843 0.26558 -0.02009 0.06242  0.00619  76  GLU B CB    
3202 C CG    . GLU C 77  ? 0.37467 0.20639 0.30861 -0.03117 0.07278  0.00477  76  GLU B CG    
3203 C CD    . GLU C 77  ? 0.45768 0.30574 0.40908 -0.05023 0.07470  -0.00812 76  GLU B CD    
3204 O OE1   . GLU C 77  ? 0.37290 0.25446 0.34629 -0.05174 0.06436  -0.01232 76  GLU B OE1   
3205 O OE2   . GLU C 77  ? 0.56334 0.39121 0.50626 -0.06373 0.08682  -0.01465 76  GLU B OE2   
3206 N N     . GLY C 78  ? 0.26317 0.13023 0.20642 0.01185  0.04143  0.01688  77  GLY B N     
3207 C CA    . GLY C 78  ? 0.26754 0.14156 0.21339 0.01907  0.03668  0.01636  77  GLY B CA    
3208 C C     . GLY C 78  ? 0.25390 0.15534 0.21117 0.02690  0.02593  0.02002  77  GLY B C     
3209 O O     . GLY C 78  ? 0.23203 0.14850 0.19808 0.02322  0.02099  0.02023  77  GLY B O     
3210 N N     . PHE C 79  ? 0.25155 0.15919 0.20833 0.03725  0.02345  0.02212  78  PHE B N     
3211 C CA    . PHE C 79  ? 0.21875 0.15180 0.18459 0.04449  0.01524  0.02515  78  PHE B CA    
3212 C C     . PHE C 79  ? 0.21824 0.16579 0.19285 0.04339  0.01158  0.02140  78  PHE B C     
3213 O O     . PHE C 79  ? 0.24088 0.17793 0.20973 0.04664  0.01622  0.01964  78  PHE B O     
3214 C CB    . PHE C 79  ? 0.24086 0.17163 0.19657 0.06070  0.01662  0.03237  78  PHE B CB    
3215 C CG    . PHE C 79  ? 0.25642 0.17057 0.19933 0.06232  0.02078  0.03720  78  PHE B CG    
3216 C CD1   . PHE C 79  ? 0.28832 0.16946 0.21465 0.06211  0.03136  0.03869  78  PHE B CD1   
3217 C CD2   . PHE C 79  ? 0.24433 0.17362 0.19021 0.06184  0.01539  0.03936  78  PHE B CD2   
3218 C CE1   . PHE C 79  ? 0.32203 0.18526 0.23457 0.06138  0.03701  0.04314  78  PHE B CE1   
3219 C CE2   . PHE C 79  ? 0.26167 0.17490 0.19392 0.06209  0.02014  0.04361  78  PHE B CE2   
3220 C CZ    . PHE C 79  ? 0.30737 0.18763 0.22272 0.06206  0.03111  0.04603  78  PHE B CZ    
3221 N N     . LEU C 80  ? 0.19995 0.16835 0.18633 0.03796  0.00460  0.01983  79  LEU B N     
3222 C CA    . LEU C 80  ? 0.19296 0.17609 0.18566 0.03766  0.00203  0.01765  79  LEU B CA    
3223 C C     . LEU C 80  ? 0.22474 0.22650 0.22141 0.04676  0.00007  0.02033  79  LEU B C     
3224 O O     . LEU C 80  ? 0.20995 0.22291 0.21003 0.04666  -0.00385 0.02191  79  LEU B O     
3225 C CB    . LEU C 80  ? 0.21871 0.21176 0.21909 0.02755  -0.00309 0.01515  79  LEU B CB    
3226 C CG    . LEU C 80  ? 0.20708 0.19083 0.20626 0.01951  -0.00366 0.01174  79  LEU B CG    
3227 C CD1   . LEU C 80  ? 0.23353 0.22767 0.23759 0.01431  -0.00867 0.01127  79  LEU B CD1   
3228 C CD2   . LEU C 80  ? 0.24176 0.21458 0.23356 0.01931  0.00045  0.00840  79  LEU B CD2   
3229 N N     . LEU C 81  ? 0.19442 0.20117 0.19066 0.05492  0.00296  0.02004  80  LEU B N     
3230 C CA    . LEU C 81  ? 0.20144 0.23254 0.20424 0.06459  0.00095  0.02125  80  LEU B CA    
3231 C C     . LEU C 81  ? 0.19753 0.24859 0.21098 0.05580  -0.00029 0.01660  80  LEU B C     
3232 O O     . LEU C 81  ? 0.20683 0.25565 0.21946 0.05567  0.00399  0.01410  80  LEU B O     
3233 C CB    . LEU C 81  ? 0.23659 0.26161 0.23282 0.08077  0.00622  0.02348  80  LEU B CB    
3234 C CG    . LEU C 81  ? 0.28100 0.27646 0.26091 0.09050  0.01114  0.02854  80  LEU B CG    
3235 C CD1   . LEU C 81  ? 0.37329 0.36489 0.34643 0.11031  0.01657  0.03125  80  LEU B CD1   
3236 C CD2   . LEU C 81  ? 0.29863 0.29281 0.27404 0.09146  0.00730  0.03332  80  LEU B CD2   
3237 N N     . VAL C 82  ? 0.16506 0.23298 0.18633 0.04746  -0.00482 0.01502  81  VAL B N     
3238 C CA    . VAL C 82  ? 0.15098 0.22982 0.17842 0.03581  -0.00417 0.01091  81  VAL B CA    
3239 C C     . VAL C 82  ? 0.16732 0.27845 0.20622 0.03725  -0.00418 0.00751  81  VAL B C     
3240 O O     . VAL C 82  ? 0.16086 0.29024 0.20498 0.04061  -0.00848 0.00724  81  VAL B O     
3241 C CB    . VAL C 82  ? 0.14800 0.21850 0.17428 0.02348  -0.00713 0.01042  81  VAL B CB    
3242 C CG1   . VAL C 82  ? 0.17064 0.24266 0.19738 0.01208  -0.00458 0.00764  81  VAL B CG1   
3243 C CG2   . VAL C 82  ? 0.17995 0.22558 0.19830 0.02341  -0.00793 0.01294  81  VAL B CG2   
3244 N N     . PHE C 83  ? 0.13996 0.26066 0.18282 0.03405  0.00083  0.00411  82  PHE B N     
3245 C CA    . PHE C 83  ? 0.14217 0.29645 0.19821 0.02978  0.00219  -0.00127 82  PHE B CA    
3246 C C     . PHE C 83  ? 0.14628 0.29504 0.20022 0.01292  0.00733  -0.00448 82  PHE B C     
3247 O O     . PHE C 83  ? 0.15848 0.27957 0.20041 0.00878  0.00876  -0.00167 82  PHE B O     
3248 C CB    . PHE C 83  ? 0.14049 0.31689 0.20442 0.04450  0.00513  -0.00263 82  PHE B CB    
3249 C CG    . PHE C 83  ? 0.15331 0.31642 0.21161 0.04643  0.01292  -0.00327 82  PHE B CG    
3250 C CD1   . PHE C 83  ? 0.19398 0.32692 0.23906 0.05548  0.01444  0.00074  82  PHE B CD1   
3251 C CD2   . PHE C 83  ? 0.15053 0.33081 0.21546 0.03755  0.01971  -0.00879 82  PHE B CD2   
3252 C CE1   . PHE C 83  ? 0.17984 0.30028 0.21791 0.05650  0.02175  -0.00118 82  PHE B CE1   
3253 C CE2   . PHE C 83  ? 0.16699 0.33454 0.22450 0.03927  0.02714  -0.00967 82  PHE B CE2   
3254 C CZ    . PHE C 83  ? 0.19209 0.33025 0.23609 0.04911  0.02779  -0.00614 82  PHE B CZ    
3255 N N     . ALA C 84  ? 0.14209 0.31697 0.20644 0.00277  0.01025  -0.01049 83  ALA B N     
3256 C CA    . ALA C 84  ? 0.16394 0.33135 0.22352 -0.01346 0.01769  -0.01322 83  ALA B CA    
3257 C C     . ALA C 84  ? 0.15741 0.34624 0.22451 -0.01235 0.02566  -0.01755 83  ALA B C     
3258 O O     . ALA C 84  ? 0.16891 0.39387 0.25253 -0.00628 0.02546  -0.02232 83  ALA B O     
3259 C CB    . ALA C 84  ? 0.16294 0.34032 0.22668 -0.03003 0.01837  -0.01832 83  ALA B CB    
3260 N N     . ILE C 85  ? 0.16651 0.33524 0.22130 -0.01756 0.03264  -0.01619 84  ILE B N     
3261 C CA    . ILE C 85  ? 0.19370 0.37962 0.25332 -0.01581 0.04169  -0.02034 84  ILE B CA    
3262 C C     . ILE C 85  ? 0.18625 0.40691 0.26083 -0.02917 0.04912  -0.02872 84  ILE B C     
3263 O O     . ILE C 85  ? 0.19206 0.43622 0.27586 -0.02645 0.05676  -0.03360 84  ILE B O     
3264 C CB    . ILE C 85  ? 0.22240 0.37777 0.26204 -0.01846 0.04752  -0.01715 84  ILE B CB    
3265 C CG1   . ILE C 85  ? 0.25948 0.39439 0.28474 -0.03653 0.05164  -0.01559 84  ILE B CG1   
3266 C CG2   . ILE C 85  ? 0.22003 0.34837 0.24817 -0.00556 0.04071  -0.01154 84  ILE B CG2   
3267 C CD1   . ILE C 85  ? 0.31353 0.42534 0.31836 -0.03996 0.05863  -0.01317 84  ILE B CD1   
3268 N N     . ASN C 86  ? 0.17816 0.40312 0.25552 -0.04433 0.04809  -0.03160 85  ASN B N     
3269 C CA    . ASN C 86  ? 0.21121 0.47067 0.30358 -0.06054 0.05546  -0.04152 85  ASN B CA    
3270 C C     . ASN C 86  ? 0.21147 0.51036 0.32464 -0.05681 0.04696  -0.04739 85  ASN B C     
3271 O O     . ASN C 86  ? 0.21712 0.52922 0.33484 -0.07017 0.04797  -0.05501 85  ASN B O     
3272 C CB    . ASN C 86  ? 0.21498 0.44699 0.29161 -0.08360 0.06300  -0.04196 85  ASN B CB    
3273 C CG    . ASN C 86  ? 0.20356 0.41319 0.27228 -0.08628 0.05450  -0.03867 85  ASN B CG    
3274 O OD1   . ASN C 86  ? 0.21515 0.41943 0.28457 -0.07050 0.04337  -0.03356 85  ASN B OD1   
3275 N ND2   . ASN C 86  ? 0.27663 0.47180 0.33682 -0.10654 0.06107  -0.04202 85  ASN B ND2   
3276 N N     . ASN C 87  ? 0.15888 0.45983 0.27470 -0.03613 0.03594  -0.04225 86  ASN B N     
3277 C CA    . ASN C 87  ? 0.20609 0.53241 0.33243 -0.02958 0.02539  -0.04518 86  ASN B CA    
3278 C C     . ASN C 87  ? 0.14740 0.48737 0.27926 -0.00326 0.01997  -0.04128 86  ASN B C     
3279 O O     . ASN C 87  ? 0.15267 0.47613 0.27801 0.01261  0.01504  -0.03344 86  ASN B O     
3280 C CB    . ASN C 87  ? 0.19770 0.50181 0.31466 -0.03338 0.01850  -0.04107 86  ASN B CB    
3281 C CG    . ASN C 87  ? 0.22698 0.54950 0.34823 -0.02640 0.00767  -0.04302 86  ASN B CG    
3282 O OD1   . ASN C 87  ? 0.18442 0.53164 0.31262 -0.01340 0.00333  -0.04474 86  ASN B OD1   
3283 N ND2   . ASN C 87  ? 0.27592 0.58237 0.38972 -0.03409 0.00345  -0.04204 86  ASN B ND2   
3284 N N     . THR C 88  ? 0.18716 0.55442 0.32943 0.00128  0.02190  -0.04670 87  THR B N     
3285 C CA    . THR C 88  ? 0.17685 0.55289 0.32197 0.02656  0.01850  -0.04277 87  THR B CA    
3286 C C     . THR C 88  ? 0.18252 0.55823 0.32285 0.04197  0.00665  -0.03755 87  THR B C     
3287 O O     . THR C 88  ? 0.15894 0.51884 0.29144 0.06261  0.00411  -0.02976 87  THR B O     
3288 C CB    . THR C 88  ? 0.20397 0.61309 0.36260 0.02754  0.02247  -0.05031 87  THR B CB    
3289 O OG1   . THR C 88  ? 0.27904 0.68282 0.43861 0.01564  0.03500  -0.05368 87  THR B OG1   
3290 C CG2   . THR C 88  ? 0.30709 0.72414 0.46732 0.05470  0.01860  -0.04597 87  THR B CG2   
3291 N N     . LYS C 89  ? 0.16064 0.55072 0.30278 0.03169  0.00047  -0.04197 88  LYS B N     
3292 C CA    . LYS C 89  ? 0.22182 0.61089 0.35664 0.04531  -0.00972 -0.03709 88  LYS B CA    
3293 C C     . LYS C 89  ? 0.17527 0.52725 0.29617 0.05243  -0.01180 -0.02724 88  LYS B C     
3294 O O     . LYS C 89  ? 0.16911 0.50883 0.28025 0.07160  -0.01628 -0.01959 88  LYS B O     
3295 C CB    . LYS C 89  ? 0.22367 0.63244 0.36106 0.03046  -0.01448 -0.04477 88  LYS B CB    
3296 C CG    . LYS C 89  ? 0.24382 0.65006 0.37136 0.04234  -0.02405 -0.03998 88  LYS B CG    
3297 C CD    . LYS C 89  ? 0.34870 0.77019 0.47535 0.06687  -0.02847 -0.03580 88  LYS B CD    
3298 C CE    . LYS C 89  ? 0.35456 0.78610 0.47327 0.07388  -0.03730 -0.03476 88  LYS B CE    
3299 N NZ    . LYS C 89  ? 0.40508 0.80322 0.50833 0.07427  -0.04016 -0.02721 88  LYS B NZ    
3300 N N     . SER C 90  ? 0.13361 0.46590 0.25212 0.03722  -0.00777 -0.02713 89  SER B N     
3301 C CA    . SER C 90  ? 0.14385 0.44387 0.25055 0.04378  -0.00995 -0.01847 89  SER B CA    
3302 C C     . SER C 90  ? 0.17207 0.45342 0.27222 0.06353  -0.00661 -0.01138 89  SER B C     
3303 O O     . SER C 90  ? 0.15883 0.41307 0.24583 0.07504  -0.00941 -0.00359 89  SER B O     
3304 C CB    . SER C 90  ? 0.16271 0.43714 0.26312 0.02295  -0.00597 -0.01943 89  SER B CB    
3305 O OG    . SER C 90  ? 0.14416 0.40145 0.24089 0.01657  0.00313  -0.01951 89  SER B OG    
3306 N N     . PHE C 91  ? 0.16478 0.45558 0.27124 0.06640  0.00071  -0.01448 90  PHE B N     
3307 C CA    . PHE C 91  ? 0.16081 0.43068 0.25872 0.08490  0.00520  -0.00907 90  PHE B CA    
3308 C C     . PHE C 91  ? 0.18167 0.45322 0.27404 0.10495  0.00066  -0.00497 90  PHE B C     
3309 O O     . PHE C 91  ? 0.19095 0.43273 0.26857 0.11979  0.00159  0.00222  90  PHE B O     
3310 C CB    . PHE C 91  ? 0.16006 0.43770 0.26431 0.08126  0.01571  -0.01431 90  PHE B CB    
3311 C CG    . PHE C 91  ? 0.16982 0.42448 0.26374 0.09953  0.02179  -0.01062 90  PHE B CG    
3312 C CD1   . PHE C 91  ? 0.19548 0.40256 0.26925 0.09682  0.02448  -0.00609 90  PHE B CD1   
3313 C CD2   . PHE C 91  ? 0.19959 0.46715 0.29751 0.11299  0.02392  -0.01213 90  PHE B CD2   
3314 C CE1   . PHE C 91  ? 0.21776 0.40169 0.28040 0.11158  0.03136  -0.00444 90  PHE B CE1   
3315 C CE2   . PHE C 91  ? 0.23111 0.47392 0.31780 0.12875  0.03065  -0.00951 90  PHE B CE2   
3316 C CZ    . PHE C 91  ? 0.23496 0.43873 0.30504 0.12976  0.03554  -0.00622 90  PHE B CZ    
3317 N N     . GLU C 92  ? 0.18713 0.49231 0.28958 0.10488  -0.00351 -0.00974 91  GLU B N     
3318 C CA    . GLU C 92  ? 0.23395 0.54461 0.33044 0.12443  -0.00815 -0.00572 91  GLU B CA    
3319 C C     . GLU C 92  ? 0.26410 0.55353 0.34474 0.12996  -0.01457 0.00164  91  GLU B C     
3320 O O     . GLU C 92  ? 0.33907 0.61566 0.40671 0.14815  -0.01583 0.00824  91  GLU B O     
3321 C CB    . GLU C 92  ? 0.26936 0.62518 0.38104 0.12129  -0.01179 -0.01370 91  GLU B CB    
3322 C CG    . GLU C 92  ? 0.26019 0.63796 0.38769 0.11484  -0.00423 -0.02149 91  GLU B CG    
3323 C CD    . GLU C 92  ? 0.31157 0.73589 0.45507 0.11006  -0.00720 -0.03065 91  GLU B CD    
3324 O OE1   . GLU C 92  ? 0.42170 0.86239 0.56668 0.10046  -0.01389 -0.03428 91  GLU B OE1   
3325 O OE2   . GLU C 92  ? 0.43727 0.88192 0.59172 0.11541  -0.00229 -0.03492 91  GLU B OE2   
3326 N N     . ASP C 93  ? 0.22173 0.50573 0.30208 0.11424  -0.01765 0.00060  92  ASP B N     
3327 C CA    . ASP C 93  ? 0.24528 0.50863 0.31095 0.11695  -0.02272 0.00684  92  ASP B CA    
3328 C C     . ASP C 93  ? 0.29847 0.51763 0.34745 0.12534  -0.01833 0.01549  92  ASP B C     
3329 O O     . ASP C 93  ? 0.28870 0.48703 0.32247 0.13107  -0.02059 0.02175  92  ASP B O     
3330 C CB    . ASP C 93  ? 0.25187 0.52127 0.32278 0.09652  -0.02620 0.00223  92  ASP B CB    
3331 C CG    . ASP C 93  ? 0.34537 0.65180 0.42623 0.08737  -0.03116 -0.00616 92  ASP B CG    
3332 O OD1   . ASP C 93  ? 0.35630 0.68606 0.44005 0.09842  -0.03334 -0.00768 92  ASP B OD1   
3333 O OD2   . ASP C 93  ? 0.39675 0.70835 0.48174 0.06897  -0.03252 -0.01168 92  ASP B OD2   
3334 N N     . ILE C 94  ? 0.22732 0.43123 0.27786 0.12478  -0.01123 0.01521  93  ILE B N     
3335 C CA    . ILE C 94  ? 0.24288 0.40419 0.27806 0.12831  -0.00629 0.02128  93  ILE B CA    
3336 C C     . ILE C 94  ? 0.33310 0.46787 0.34882 0.14481  -0.00424 0.02863  93  ILE B C     
3337 O O     . ILE C 94  ? 0.32538 0.42923 0.32549 0.14486  -0.00332 0.03418  93  ILE B O     
3338 C CB    . ILE C 94  ? 0.26437 0.41730 0.30377 0.12614  0.00189  0.01805  93  ILE B CB    
3339 C CG1   . ILE C 94  ? 0.21437 0.37233 0.26180 0.10158  0.00136  0.01214  93  ILE B CG1   
3340 C CG2   . ILE C 94  ? 0.26765 0.37349 0.28735 0.13126  0.00861  0.02270  93  ILE B CG2   
3341 C CD1   . ILE C 94  ? 0.21158 0.33983 0.24841 0.08782  -0.00105 0.01462  93  ILE B CD1   
3342 N N     . HIS C 95  ? 0.28204 0.42788 0.29772 0.15855  -0.00260 0.02869  94  HIS B N     
3343 C CA    . HIS C 95  ? 0.30495 0.42247 0.30005 0.17480  0.00105  0.03597  94  HIS B CA    
3344 C C     . HIS C 95  ? 0.37384 0.48736 0.35713 0.17723  -0.00439 0.04120  94  HIS B C     
3345 O O     . HIS C 95  ? 0.40282 0.48069 0.36521 0.18368  0.00023  0.04789  94  HIS B O     
3346 C CB    . HIS C 95  ? 0.39764 0.52983 0.39528 0.19066  0.00353  0.03518  94  HIS B CB    
3347 C CG    . HIS C 95  ? 0.48558 0.65732 0.49157 0.19800  -0.00448 0.03390  94  HIS B CG    
3348 N ND1   . HIS C 95  ? 0.53038 0.74703 0.55908 0.18871  -0.00968 0.02562  94  HIS B ND1   
3349 C CD2   . HIS C 95  ? 0.49960 0.67294 0.49326 0.21354  -0.00763 0.03929  94  HIS B CD2   
3350 C CE1   . HIS C 95  ? 0.47032 0.71590 0.50122 0.19783  -0.01615 0.02528  94  HIS B CE1   
3351 N NE2   . HIS C 95  ? 0.54753 0.76829 0.55733 0.21404  -0.01545 0.03385  94  HIS B NE2   
3352 N N     . HIS C 96  ? 0.33108 0.47849 0.32619 0.17016  -0.01303 0.03754  95  HIS B N     
3353 C CA    . HIS C 96  ? 0.34010 0.48391 0.32305 0.17226  -0.01781 0.04183  95  HIS B CA    
3354 C C     . HIS C 96  ? 0.35461 0.46657 0.32750 0.16110  -0.01573 0.04500  95  HIS B C     
3355 O O     . HIS C 96  ? 0.38673 0.47438 0.34076 0.16645  -0.01398 0.05135  95  HIS B O     
3356 C CB    . HIS C 96  ? 0.36259 0.55104 0.35981 0.16703  -0.02701 0.03567  95  HIS B CB    
3357 C CG    . HIS C 96  ? 0.55753 0.77841 0.56255 0.17971  -0.02937 0.03294  95  HIS B CG    
3358 N ND1   . HIS C 96  ? 0.59388 0.85707 0.62064 0.17105  -0.03313 0.02346  95  HIS B ND1   
3359 C CD2   . HIS C 96  ? 0.57409 0.79145 0.56769 0.20049  -0.02799 0.03822  95  HIS B CD2   
3360 C CE1   . HIS C 96  ? 0.50693 0.79373 0.53679 0.18610  -0.03452 0.02273  95  HIS B CE1   
3361 N NE2   . HIS C 96  ? 0.60726 0.86708 0.61711 0.20512  -0.03183 0.03194  95  HIS B NE2   
3362 N N     . TYR C 97  ? 0.30932 0.42102 0.29383 0.14596  -0.01537 0.04073  96  TYR B N     
3363 C CA    . TYR C 97  ? 0.29320 0.37430 0.26855 0.13655  -0.01281 0.04368  96  TYR B CA    
3364 C C     . TYR C 97  ? 0.36589 0.40346 0.32249 0.14312  -0.00311 0.04918  96  TYR B C     
3365 O O     . TYR C 97  ? 0.35856 0.36839 0.29905 0.14164  0.00021  0.05388  96  TYR B O     
3366 C CB    . TYR C 97  ? 0.29643 0.38544 0.28716 0.12123  -0.01404 0.03839  96  TYR B CB    
3367 C CG    . TYR C 97  ? 0.32333 0.44774 0.32889 0.11011  -0.02203 0.03246  96  TYR B CG    
3368 C CD1   . TYR C 97  ? 0.28165 0.40428 0.28278 0.10205  -0.02626 0.03293  96  TYR B CD1   
3369 C CD2   . TYR C 97  ? 0.29522 0.45385 0.31830 0.10607  -0.02406 0.02537  96  TYR B CD2   
3370 C CE1   . TYR C 97  ? 0.27834 0.43038 0.29100 0.09012  -0.03226 0.02591  96  TYR B CE1   
3371 C CE2   . TYR C 97  ? 0.26138 0.44951 0.29635 0.09311  -0.02951 0.01844  96  TYR B CE2   
3372 C CZ    . TYR C 97  ? 0.34784 0.53195 0.37725 0.08508  -0.03375 0.01851  96  TYR B CZ    
3373 O OH    . TYR C 97  ? 0.29428 0.50470 0.33365 0.07055  -0.03795 0.01019  96  TYR B OH    
3374 N N     . ARG C 98  ? 0.34976 0.37987 0.30732 0.14896  0.00267  0.04783  97  ARG B N     
3375 C CA    . ARG C 98  ? 0.36764 0.35505 0.30575 0.15368  0.01304  0.05153  97  ARG B CA    
3376 C C     . ARG C 98  ? 0.43498 0.40703 0.35302 0.16641  0.01550  0.05829  97  ARG B C     
3377 O O     . ARG C 98  ? 0.42349 0.35868 0.32253 0.16433  0.02304  0.06213  97  ARG B O     
3378 C CB    . ARG C 98  ? 0.37680 0.36014 0.31837 0.15837  0.01903  0.04801  97  ARG B CB    
3379 C CG    . ARG C 98  ? 0.42336 0.36140 0.34345 0.16148  0.03065  0.05032  97  ARG B CG    
3380 C CD    . ARG C 98  ? 0.42053 0.35427 0.34406 0.16414  0.03679  0.04536  97  ARG B CD    
3381 N NE    . ARG C 98  ? 0.47147 0.36725 0.37356 0.17081  0.04770  0.04745  97  ARG B NE    
3382 C CZ    . ARG C 98  ? 0.62490 0.48192 0.51283 0.16005  0.05686  0.04529  97  ARG B CZ    
3383 N NH1   . ARG C 98  ? 0.60844 0.45957 0.50165 0.14307  0.05601  0.04110  97  ARG B NH1   
3384 N NH2   . ARG C 98  ? 0.64893 0.47286 0.51672 0.16592  0.06739  0.04677  97  ARG B NH2   
3385 N N     . GLU C 99  ? 0.37818 0.37810 0.29934 0.17938  0.00986  0.05946  98  GLU B N     
3386 C CA    . GLU C 99  ? 0.40096 0.38642 0.30121 0.19416  0.01218  0.06646  98  GLU B CA    
3387 C C     . GLU C 99  ? 0.37727 0.35147 0.26630 0.18796  0.01054  0.07012  98  GLU B C     
3388 O O     . GLU C 99  ? 0.42216 0.36310 0.28802 0.19330  0.01781  0.07613  98  GLU B O     
3389 C CB    . GLU C 99  ? 0.41241 0.43483 0.31996 0.20966  0.00532  0.06621  98  GLU B CB    
3390 C CG    . GLU C 99  ? 0.57875 0.59661 0.48307 0.22496  0.01099  0.06692  98  GLU B CG    
3391 C CD    . GLU C 99  ? 0.66155 0.72567 0.58051 0.23719  0.00304  0.06425  98  GLU B CD    
3392 O OE1   . GLU C 99  ? 0.69351 0.79139 0.62330 0.23298  -0.00654 0.06159  98  GLU B OE1   
3393 O OE2   . GLU C 99  ? 0.62638 0.69398 0.54624 0.25035  0.00661  0.06406  98  GLU B OE2   
3394 N N     . GLN C 100 ? 0.37742 0.37813 0.28142 0.17656  0.00191  0.06635  99  GLN B N     
3395 C CA    . GLN C 100 ? 0.38685 0.37742 0.28096 0.16946  0.00062  0.06914  99  GLN B CA    
3396 C C     . GLN C 100 ? 0.39615 0.34358 0.27694 0.15961  0.01088  0.07137  99  GLN B C     
3397 O O     . GLN C 100 ? 0.40028 0.32299 0.26167 0.16017  0.01597  0.07633  99  GLN B O     
3398 C CB    . GLN C 100 ? 0.40589 0.43053 0.31893 0.15717  -0.00934 0.06341  99  GLN B CB    
3399 C CG    . GLN C 100 ? 0.41586 0.47882 0.33527 0.16431  -0.01863 0.06132  99  GLN B CG    
3400 C CD    . GLN C 100 ? 0.58907 0.63958 0.48633 0.17597  -0.01807 0.06817  99  GLN B CD    
3401 O OE1   . GLN C 100 ? 0.60711 0.63788 0.49130 0.17007  -0.01604 0.07139  99  GLN B OE1   
3402 N NE2   . GLN C 100 ? 0.55979 0.62018 0.45128 0.19326  -0.01910 0.07081  99  GLN B NE2   
3403 N N     . ILE C 101 ? 0.37616 0.31432 0.26663 0.14981  0.01462  0.06720  100 ILE B N     
3404 C CA    . ILE C 101 ? 0.36281 0.26344 0.24281 0.13795  0.02431  0.06744  100 ILE B CA    
3405 C C     . ILE C 101 ? 0.38431 0.24782 0.24111 0.14502  0.03611  0.07131  100 ILE B C     
3406 O O     . ILE C 101 ? 0.41369 0.24771 0.25357 0.13898  0.04429  0.07380  100 ILE B O     
3407 C CB    . ILE C 101 ? 0.39742 0.29952 0.29330 0.12698  0.02483  0.06123  100 ILE B CB    
3408 C CG1   . ILE C 101 ? 0.32765 0.26189 0.24329 0.11904  0.01449  0.05799  100 ILE B CG1   
3409 C CG2   . ILE C 101 ? 0.43109 0.29463 0.31632 0.11442  0.03597  0.05957  100 ILE B CG2   
3410 C CD1   . ILE C 101 ? 0.31660 0.26178 0.25040 0.10955  0.01331  0.05065  100 ILE B CD1   
3411 N N     . LYS C 102 ? 0.38431 0.24854 0.23890 0.15790  0.03806  0.07170  101 LYS B N     
3412 C CA    . LYS C 102 ? 0.44423 0.27239 0.27434 0.16666  0.04969  0.07580  101 LYS B CA    
3413 C C     . LYS C 102 ? 0.45766 0.27681 0.26782 0.17660  0.05066  0.08311  101 LYS B C     
3414 O O     . LYS C 102 ? 0.49579 0.27690 0.28247 0.17630  0.06227  0.08643  101 LYS B O     
3415 C CB    . LYS C 102 ? 0.44257 0.27661 0.27373 0.18153  0.05078  0.07557  101 LYS B CB    
3416 C CG    . LYS C 102 ? 0.47010 0.30598 0.31640 0.17225  0.05247  0.06818  101 LYS B CG    
3417 C CD    . LYS C 102 ? 0.58205 0.43477 0.43517 0.18700  0.05135  0.06702  101 LYS B CD    
3418 C CE    . LYS C 102 ? 0.59118 0.42396 0.42237 0.20515  0.05811  0.07321  101 LYS B CE    
3419 N NZ    . LYS C 102 ? 0.56421 0.42117 0.40374 0.22246  0.05509  0.07293  101 LYS B NZ    
3420 N N     . ARG C 103 ? 0.44394 0.29765 0.26193 0.18571  0.03914  0.08516  102 ARG B N     
3421 C CA    . ARG C 103 ? 0.47343 0.32173 0.27200 0.19694  0.03877  0.09204  102 ARG B CA    
3422 C C     . ARG C 103 ? 0.47494 0.30224 0.26327 0.18284  0.04324  0.09323  102 ARG B C     
3423 O O     . ARG C 103 ? 0.51296 0.30846 0.27611 0.18660  0.05233  0.09858  102 ARG B O     
3424 C CB    . ARG C 103 ? 0.50155 0.39708 0.31412 0.20701  0.02435  0.09169  102 ARG B CB    
3425 C CG    . ARG C 103 ? 0.60450 0.50167 0.39852 0.22055  0.02152  0.09829  102 ARG B CG    
3426 C CD    . ARG C 103 ? 0.65320 0.60253 0.46487 0.22600  0.00637  0.09524  102 ARG B CD    
3427 N NE    . ARG C 103 ? 0.73101 0.71170 0.56014 0.23537  0.00116  0.09134  102 ARG B NE    
3428 C CZ    . ARG C 103 ? 0.67842 0.67029 0.50043 0.25625  -0.00051 0.09477  102 ARG B CZ    
3429 N NH1   . ARG C 103 ? 0.63152 0.60226 0.42673 0.27225  0.00304  0.10316  102 ARG B NH1   
3430 N NH2   . ARG C 103 ? 0.63940 0.66430 0.48090 0.26184  -0.00543 0.08979  102 ARG B NH2   
3431 N N     . VAL C 104 ? 0.43667 0.28058 0.24330 0.16676  0.03778  0.08828  103 VAL B N     
3432 C CA    . VAL C 104 ? 0.46736 0.29708 0.26676 0.15321  0.04120  0.08892  103 VAL B CA    
3433 C C     . VAL C 104 ? 0.45466 0.24239 0.24156 0.14068  0.05634  0.08762  103 VAL B C     
3434 O O     . VAL C 104 ? 0.52204 0.28452 0.29048 0.13560  0.06496  0.09038  103 VAL B O     
3435 C CB    . VAL C 104 ? 0.44606 0.30627 0.26822 0.14074  0.03127  0.08389  103 VAL B CB    
3436 C CG1   . VAL C 104 ? 0.49920 0.34002 0.31485 0.12465  0.03786  0.08354  103 VAL B CG1   
3437 C CG2   . VAL C 104 ? 0.44548 0.34480 0.27511 0.14992  0.01788  0.08430  103 VAL B CG2   
3438 N N     . LYS C 105 ? 0.47227 0.25376 0.26971 0.13360  0.05995  0.08229  104 LYS B N     
3439 C CA    . LYS C 105 ? 0.54114 0.28567 0.32786 0.12025  0.07439  0.07892  104 LYS B CA    
3440 C C     . LYS C 105 ? 0.54771 0.26042 0.31075 0.13103  0.08558  0.08212  104 LYS B C     
3441 O O     . LYS C 105 ? 0.56213 0.24179 0.31250 0.11949  0.09913  0.07890  104 LYS B O     
3442 C CB    . LYS C 105 ? 0.56153 0.31328 0.36900 0.10535  0.07330  0.07075  104 LYS B CB    
3443 C CG    . LYS C 105 ? 0.51294 0.29246 0.34031 0.09599  0.06338  0.06866  104 LYS B CG    
3444 C CD    . LYS C 105 ? 0.47987 0.26905 0.32788 0.08370  0.06072  0.06125  104 LYS B CD    
3445 C CE    . LYS C 105 ? 0.42352 0.19185 0.27158 0.06226  0.07089  0.05467  104 LYS B CE    
3446 N NZ    . LYS C 105 ? 0.43370 0.20137 0.27916 0.05266  0.07341  0.05590  104 LYS B NZ    
3447 N N     . ASP C 106 ? 0.52626 0.24817 0.28189 0.15258  0.08091  0.08807  105 ASP B N     
3448 C CA    . ASP C 106 ? 0.57592 0.26648 0.30612 0.16601  0.09167  0.09255  105 ASP B CA    
3449 C C     . ASP C 106 ? 0.58642 0.25262 0.31476 0.15746  0.10234  0.08673  105 ASP B C     
3450 O O     . ASP C 106 ? 0.62514 0.25201 0.33167 0.15171  0.11720  0.08628  105 ASP B O     
3451 C CB    . ASP C 106 ? 0.61802 0.27703 0.31995 0.16708  0.10161  0.09817  105 ASP B CB    
3452 C CG    . ASP C 106 ? 0.67402 0.30110 0.34708 0.18459  0.11200  0.10426  105 ASP B CG    
3453 O OD1   . ASP C 106 ? 0.67744 0.32146 0.35347 0.20389  0.10545  0.10741  105 ASP B OD1   
3454 O OD2   . ASP C 106 ? 0.71648 0.30174 0.36395 0.17904  0.12734  0.10546  105 ASP B OD2   
3455 N N     . SER C 107 ? 0.57314 0.26308 0.32406 0.15571  0.09508  0.08154  106 SER B N     
3456 C CA    . SER C 107 ? 0.58977 0.25992 0.34083 0.14591  0.10392  0.07480  106 SER B CA    
3457 C C     . SER C 107 ? 0.55971 0.25858 0.33137 0.15329  0.09488  0.07181  106 SER B C     
3458 O O     . SER C 107 ? 0.55100 0.28786 0.34477 0.15495  0.08161  0.07123  106 SER B O     
3459 C CB    . SER C 107 ? 0.67002 0.33305 0.43032 0.11983  0.10776  0.06657  106 SER B CB    
3460 O OG    . SER C 107 ? 0.68761 0.34031 0.45251 0.10970  0.11320  0.05849  106 SER B OG    
3461 N N     . GLU C 108 ? 0.60590 0.28508 0.36971 0.15588  0.10330  0.06902  107 GLU B N     
3462 C CA    . GLU C 108 ? 0.59292 0.29316 0.37424 0.16013  0.09795  0.06454  107 GLU B CA    
3463 C C     . GLU C 108 ? 0.59159 0.29120 0.38692 0.13909  0.09886  0.05444  107 GLU B C     
3464 O O     . GLU C 108 ? 0.73019 0.44686 0.54006 0.14076  0.09477  0.04974  107 GLU B O     
3465 C CB    . GLU C 108 ? 0.68564 0.36441 0.45006 0.17525  0.10701  0.06659  107 GLU B CB    
3466 C CG    . GLU C 108 ? 0.68942 0.37405 0.44205 0.19990  0.10473  0.07610  107 GLU B CG    
3467 C CD    . GLU C 108 ? 0.82409 0.49552 0.56582 0.21669  0.11156  0.07748  107 GLU B CD    
3468 O OE1   . GLU C 108 ? 0.91960 0.56174 0.65263 0.20776  0.12267  0.07213  107 GLU B OE1   
3469 O OE2   . GLU C 108 ? 0.82765 0.51931 0.56987 0.23862  0.10577  0.08330  107 GLU B OE2   
3470 N N     . ASP C 109 ? 0.58823 0.26908 0.37896 0.11944  0.10468  0.05031  108 ASP B N     
3471 C CA    . ASP C 109 ? 0.61688 0.29540 0.41848 0.09838  0.10636  0.03961  108 ASP B CA    
3472 C C     . ASP C 109 ? 0.62176 0.31683 0.43785 0.08406  0.09948  0.03781  108 ASP B C     
3473 O O     . ASP C 109 ? 0.69655 0.37498 0.50599 0.06827  0.10646  0.03468  108 ASP B O     
3474 C CB    . ASP C 109 ? 0.75301 0.39265 0.53470 0.08584  0.12200  0.03392  108 ASP B CB    
3475 C CG    . ASP C 109 ? 0.80181 0.44191 0.59424 0.06258  0.12337  0.02115  108 ASP B CG    
3476 O OD1   . ASP C 109 ? 0.78377 0.44949 0.59591 0.06043  0.11339  0.01679  108 ASP B OD1   
3477 O OD2   . ASP C 109 ? 0.86984 0.48547 0.65013 0.04630  0.13472  0.01495  108 ASP B OD2   
3478 N N     . VAL C 110 ? 0.50473 0.23335 0.34071 0.08934  0.08649  0.03942  109 VAL B N     
3479 C CA    . VAL C 110 ? 0.44761 0.19342 0.29824 0.07763  0.07929  0.03813  109 VAL B CA    
3480 C C     . VAL C 110 ? 0.42267 0.18464 0.29162 0.06907  0.07345  0.03020  109 VAL B C     
3481 O O     . VAL C 110 ? 0.40655 0.18427 0.28291 0.08017  0.06873  0.03015  109 VAL B O     
3482 C CB    . VAL C 110 ? 0.43584 0.20742 0.29239 0.09082  0.06898  0.04672  109 VAL B CB    
3483 C CG1   . VAL C 110 ? 0.39807 0.18433 0.26798 0.07853  0.06284  0.04540  109 VAL B CG1   
3484 C CG2   . VAL C 110 ? 0.47403 0.23065 0.31003 0.10233  0.07396  0.05461  109 VAL B CG2   
3485 N N     . PRO C 111 ? 0.39607 0.15968 0.27378 0.04917  0.07313  0.02263  110 PRO B N     
3486 C CA    . PRO C 111 ? 0.35515 0.14855 0.25299 0.03893  0.06386  0.01400  110 PRO B CA    
3487 C C     . PRO C 111 ? 0.31880 0.15023 0.23423 0.04757  0.05057  0.01823  110 PRO B C     
3488 O O     . PRO C 111 ? 0.30956 0.15701 0.23231 0.04775  0.04448  0.02253  110 PRO B O     
3489 C CB    . PRO C 111 ? 0.37175 0.16964 0.27775 0.01749  0.06368  0.00629  110 PRO B CB    
3490 C CG    . PRO C 111 ? 0.38773 0.14756 0.27387 0.01231  0.07824  0.00690  110 PRO B CG    
3491 C CD    . PRO C 111 ? 0.43483 0.18010 0.30577 0.03296  0.08098  0.01990  110 PRO B CD    
3492 N N     . MET C 112 ? 0.33419 0.17943 0.25562 0.05326  0.04720  0.01599  111 MET B N     
3493 C CA    . MET C 112 ? 0.29028 0.17057 0.22798 0.05830  0.03660  0.01812  111 MET B CA    
3494 C C     . MET C 112 ? 0.27414 0.16580 0.21817 0.05357  0.03474  0.01163  111 MET B C     
3495 O O     . MET C 112 ? 0.30653 0.17932 0.24037 0.05297  0.04207  0.00685  111 MET B O     
3496 C CB    . MET C 112 ? 0.34976 0.23880 0.28556 0.07831  0.03582  0.02558  111 MET B CB    
3497 C CG    . MET C 112 ? 0.39653 0.26947 0.31883 0.08928  0.03905  0.03387  111 MET B CG    
3498 S SD    . MET C 112 ? 0.47999 0.36820 0.40005 0.11618  0.03678  0.04169  111 MET B SD    
3499 C CE    . MET C 112 ? 0.52033 0.38237 0.41799 0.12193  0.04229  0.04920  111 MET B CE    
3500 N N     . VAL C 113 ? 0.24401 0.16427 0.20244 0.05026  0.02597  0.01147  112 VAL B N     
3501 C CA    . VAL C 113 ? 0.25412 0.18718 0.21716 0.04663  0.02416  0.00694  112 VAL B CA    
3502 C C     . VAL C 113 ? 0.25812 0.21838 0.23243 0.05352  0.01968  0.01024  112 VAL B C     
3503 O O     . VAL C 113 ? 0.23746 0.21166 0.21963 0.05255  0.01397  0.01352  112 VAL B O     
3504 C CB    . VAL C 113 ? 0.25760 0.19521 0.22441 0.03155  0.01878  0.00238  112 VAL B CB    
3505 C CG1   . VAL C 113 ? 0.24761 0.19812 0.21606 0.02871  0.01661  -0.00043 112 VAL B CG1   
3506 C CG2   . VAL C 113 ? 0.28685 0.20312 0.24443 0.02314  0.02334  -0.00327 112 VAL B CG2   
3507 N N     . LEU C 114 ? 0.25038 0.21893 0.22545 0.06001  0.02321  0.00843  113 LEU B N     
3508 C CA    . LEU C 114 ? 0.23278 0.23106 0.22032 0.06367  0.02032  0.00928  113 LEU B CA    
3509 C C     . LEU C 114 ? 0.20659 0.21496 0.19839 0.04957  0.01709  0.00623  113 LEU B C     
3510 O O     . LEU C 114 ? 0.22751 0.22480 0.21147 0.04372  0.01972  0.00260  113 LEU B O     
3511 C CB    . LEU C 114 ? 0.25386 0.25797 0.24098 0.07720  0.02708  0.00793  113 LEU B CB    
3512 C CG    . LEU C 114 ? 0.22617 0.26640 0.22871 0.08115  0.02531  0.00725  113 LEU B CG    
3513 C CD1   . LEU C 114 ? 0.23593 0.29474 0.24685 0.08791  0.01874  0.01165  113 LEU B CD1   
3514 C CD2   . LEU C 114 ? 0.27521 0.32114 0.27776 0.09452  0.03332  0.00458  113 LEU B CD2   
3515 N N     . VAL C 115 ? 0.18559 0.21178 0.18695 0.04400  0.01170  0.00772  114 VAL B N     
3516 C CA    . VAL C 115 ? 0.17792 0.20865 0.18017 0.03151  0.00948  0.00629  114 VAL B CA    
3517 C C     . VAL C 115 ? 0.18393 0.23962 0.19596 0.02970  0.01112  0.00487  114 VAL B C     
3518 O O     . VAL C 115 ? 0.18126 0.25416 0.20288 0.03144  0.00827  0.00549  114 VAL B O     
3519 C CB    . VAL C 115 ? 0.18223 0.20698 0.18518 0.02444  0.00326  0.00843  114 VAL B CB    
3520 C CG1   . VAL C 115 ? 0.22331 0.24890 0.22426 0.01431  0.00177  0.00812  114 VAL B CG1   
3521 C CG2   . VAL C 115 ? 0.21234 0.21761 0.20846 0.02419  0.00220  0.00837  114 VAL B CG2   
3522 N N     . GLY C 116 ? 0.19042 0.24912 0.19939 0.02475  0.01612  0.00217  115 GLY B N     
3523 C CA    . GLY C 116 ? 0.18190 0.26313 0.19935 0.01840  0.01948  -0.00034 115 GLY B CA    
3524 C C     . GLY C 116 ? 0.16005 0.23096 0.17035 0.00452  0.01855  0.00081  115 GLY B C     
3525 O O     . GLY C 116 ? 0.19379 0.24956 0.19112 -0.00011 0.02111  0.00133  115 GLY B O     
3526 N N     . ASN C 117 ? 0.17400 0.25097 0.19021 -0.00143 0.01514  0.00131  116 ASN B N     
3527 C CA    . ASN C 117 ? 0.16596 0.22761 0.17331 -0.01246 0.01458  0.00319  116 ASN B CA    
3528 C C     . ASN C 117 ? 0.16776 0.23891 0.17526 -0.02466 0.02233  0.00009  116 ASN B C     
3529 O O     . ASN C 117 ? 0.17689 0.27333 0.19594 -0.02552 0.02713  -0.00470 116 ASN B O     
3530 C CB    . ASN C 117 ? 0.17873 0.23700 0.19003 -0.01277 0.00818  0.00465  116 ASN B CB    
3531 C CG    . ASN C 117 ? 0.17757 0.21467 0.17776 -0.02014 0.00742  0.00739  116 ASN B CG    
3532 O OD1   . ASN C 117 ? 0.20587 0.22541 0.19373 -0.01925 0.00699  0.01054  116 ASN B OD1   
3533 N ND2   . ASN C 117 ? 0.18274 0.22133 0.18608 -0.02670 0.00722  0.00591  116 ASN B ND2   
3534 N N     . LYS C 118 ? 0.19581 0.24595 0.18970 -0.03390 0.02413  0.00280  117 LYS B N     
3535 C CA    . LYS C 118 ? 0.21186 0.25975 0.19909 -0.04806 0.03348  0.00097  117 LYS B CA    
3536 C C     . LYS C 118 ? 0.25461 0.30143 0.23247 -0.05018 0.04168  0.00067  117 LYS B C     
3537 O O     . LYS C 118 ? 0.27175 0.32942 0.25088 -0.06146 0.05184  -0.00345 117 LYS B O     
3538 C CB    . LYS C 118 ? 0.21009 0.28380 0.21345 -0.05764 0.03686  -0.00604 117 LYS B CB    
3539 C CG    . LYS C 118 ? 0.18761 0.26380 0.19877 -0.05533 0.02880  -0.00659 117 LYS B CG    
3540 C CD    . LYS C 118 ? 0.19540 0.29151 0.21660 -0.06948 0.03292  -0.01450 117 LYS B CD    
3541 C CE    . LYS C 118 ? 0.22670 0.32610 0.25396 -0.06536 0.02426  -0.01526 117 LYS B CE    
3542 N NZ    . LYS C 118 ? 0.22001 0.33625 0.25419 -0.08112 0.02792  -0.02422 117 LYS B NZ    
3543 N N     . SER C 119 ? 0.24614 0.27879 0.21279 -0.04104 0.03811  0.00439  118 SER B N     
3544 C CA    . SER C 119 ? 0.27353 0.30346 0.22843 -0.04214 0.04558  0.00375  118 SER B CA    
3545 C C     . SER C 119 ? 0.30831 0.31914 0.24247 -0.05430 0.05432  0.00677  118 SER B C     
3546 O O     . SER C 119 ? 0.36683 0.37745 0.29067 -0.05795 0.06313  0.00556  118 SER B O     
3547 C CB    . SER C 119 ? 0.26342 0.28098 0.20862 -0.03126 0.03921  0.00587  118 SER B CB    
3548 O OG    . SER C 119 ? 0.36492 0.35861 0.29321 -0.03044 0.03270  0.01173  118 SER B OG    
3549 N N     . ASP C 120 ? 0.31440 0.30724 0.24052 -0.06028 0.05331  0.01064  119 ASP B N     
3550 C CA    . ASP C 120 ? 0.35026 0.31688 0.25172 -0.07115 0.06270  0.01506  119 ASP B CA    
3551 C C     . ASP C 120 ? 0.38687 0.36708 0.29571 -0.08829 0.07649  0.00861  119 ASP B C     
3552 O O     . ASP C 120 ? 0.44083 0.39892 0.32810 -0.09977 0.08779  0.01138  119 ASP B O     
3553 C CB    . ASP C 120 ? 0.39087 0.33093 0.28105 -0.06904 0.05688  0.02136  119 ASP B CB    
3554 C CG    . ASP C 120 ? 0.34857 0.30097 0.25899 -0.07254 0.05401  0.01674  119 ASP B CG    
3555 O OD1   . ASP C 120 ? 0.30708 0.27798 0.23623 -0.06307 0.04424  0.01440  119 ASP B OD1   
3556 O OD2   . ASP C 120 ? 0.39198 0.33525 0.29806 -0.08583 0.06266  0.01481  119 ASP B OD2   
3557 N N     . LEU C 121 ? 0.34993 0.36544 0.28681 -0.09030 0.07613  0.00018  120 LEU B N     
3558 C CA    . LEU C 121 ? 0.35283 0.38774 0.30046 -0.10841 0.08826  -0.00808 120 LEU B CA    
3559 C C     . LEU C 121 ? 0.52117 0.57471 0.47057 -0.11412 0.10050  -0.01286 120 LEU B C     
3560 O O     . LEU C 121 ? 0.53421 0.58076 0.47343 -0.10331 0.09915  -0.00909 120 LEU B O     
3561 C CB    . LEU C 121 ? 0.35913 0.42821 0.33585 -0.10649 0.08087  -0.01534 120 LEU B CB    
3562 C CG    . LEU C 121 ? 0.31902 0.37121 0.29355 -0.10722 0.07332  -0.01324 120 LEU B CG    
3563 C CD1   . LEU C 121 ? 0.39919 0.48870 0.40056 -0.10639 0.06697  -0.02126 120 LEU B CD1   
3564 C CD2   . LEU C 121 ? 0.37316 0.39476 0.32774 -0.12511 0.08429  -0.01261 120 LEU B CD2   
3565 N N     . PRO C 122 ? 0.43038 0.50215 0.38793 -0.13287 0.11391  -0.02109 121 PRO B N     
3566 C CA    . PRO C 122 ? 0.46194 0.55576 0.42702 -0.13450 0.12241  -0.02716 121 PRO B CA    
3567 C C     . PRO C 122 ? 0.50229 0.64865 0.50170 -0.12683 0.11966  -0.03683 121 PRO B C     
3568 O O     . PRO C 122 ? 0.55765 0.71684 0.55989 -0.11755 0.12308  -0.03779 121 PRO B O     
3569 C CB    . PRO C 122 ? 0.42986 0.51018 0.38673 -0.15262 0.13148  -0.03127 121 PRO B CB    
3570 C CG    . PRO C 122 ? 0.48423 0.56191 0.44775 -0.15864 0.12552  -0.03380 121 PRO B CG    
3571 C CD    . PRO C 122 ? 0.41749 0.47557 0.37237 -0.14676 0.11574  -0.02422 121 PRO B CD    
3572 N N     . SER C 123 ? 0.52363 0.69942 0.54698 -0.12947 0.11364  -0.04428 122 SER B N     
3573 C CA    . SER C 123 ? 0.51858 0.74454 0.57264 -0.12159 0.11030  -0.05351 122 SER B CA    
3574 C C     . SER C 123 ? 0.46609 0.71137 0.53429 -0.09948 0.09980  -0.05087 122 SER B C     
3575 O O     . SER C 123 ? 0.38728 0.65930 0.47465 -0.09228 0.08965  -0.05434 122 SER B O     
3576 C CB    . SER C 123 ? 0.37939 0.62654 0.44775 -0.13343 0.10766  -0.06269 122 SER B CB    
3577 O OG    . SER C 123 ? 0.49179 0.70832 0.54061 -0.15383 0.11686  -0.06368 122 SER B OG    
3578 N N     . ARG C 124 ? 0.34877 0.57632 0.40348 -0.08912 0.10210  -0.04464 123 ARG B N     
3579 C CA    . ARG C 124 ? 0.32077 0.55993 0.38648 -0.06535 0.09126  -0.04253 123 ARG B CA    
3580 C C     . ARG C 124 ? 0.28552 0.57337 0.37977 -0.05703 0.09054  -0.05084 123 ARG B C     
3581 O O     . ARG C 124 ? 0.25881 0.56156 0.35889 -0.06237 0.09850  -0.05644 123 ARG B O     
3582 C CB    . ARG C 124 ? 0.38437 0.59803 0.43216 -0.05348 0.09366  -0.03763 123 ARG B CB    
3583 C CG    . ARG C 124 ? 0.41318 0.63568 0.47054 -0.02940 0.08578  -0.03662 123 ARG B CG    
3584 C CD    . ARG C 124 ? 0.38124 0.58085 0.42106 -0.02068 0.09078  -0.03476 123 ARG B CD    
3585 N NE    . ARG C 124 ? 0.41500 0.57091 0.42780 -0.02592 0.08654  -0.02747 123 ARG B NE    
3586 C CZ    . ARG C 124 ? 0.29847 0.43084 0.30320 -0.01666 0.07533  -0.02193 123 ARG B CZ    
3587 N NH1   . ARG C 124 ? 0.29149 0.43368 0.30994 -0.00237 0.06768  -0.02163 123 ARG B NH1   
3588 N NH2   . ARG C 124 ? 0.28686 0.38578 0.26848 -0.02168 0.07204  -0.01659 123 ARG B NH2   
3589 N N     . THR C 125 ? 0.22156 0.52750 0.33017 -0.04253 0.07851  -0.05028 124 THR B N     
3590 C CA    . THR C 125 ? 0.26525 0.60626 0.39407 -0.02717 0.07343  -0.05462 124 THR B CA    
3591 C C     . THR C 125 ? 0.19797 0.53654 0.32732 -0.00044 0.06824  -0.04949 124 THR B C     
3592 O O     . THR C 125 ? 0.27613 0.63661 0.41746 0.01498  0.06650  -0.05168 124 THR B O     
3593 C CB    . THR C 125 ? 0.20185 0.56598 0.34334 -0.03208 0.06346  -0.05884 124 THR B CB    
3594 O OG1   . THR C 125 ? 0.23123 0.57845 0.36593 -0.02981 0.05425  -0.05317 124 THR B OG1   
3595 C CG2   . THR C 125 ? 0.27457 0.64102 0.41496 -0.05800 0.07055  -0.06602 124 THR B CG2   
3596 N N     . VAL C 126 ? 0.21145 0.51818 0.32494 0.00545  0.06560  -0.04232 125 VAL B N     
3597 C CA    . VAL C 126 ? 0.19723 0.48711 0.30416 0.02915  0.06108  -0.03676 125 VAL B CA    
3598 C C     . VAL C 126 ? 0.23049 0.48542 0.31683 0.02861  0.06917  -0.03485 125 VAL B C     
3599 O O     . VAL C 126 ? 0.24218 0.46198 0.30905 0.01647  0.06821  -0.03067 125 VAL B O     
3600 C CB    . VAL C 126 ? 0.20569 0.47177 0.30423 0.03468  0.04852  -0.02925 125 VAL B CB    
3601 C CG1   . VAL C 126 ? 0.23584 0.48379 0.32681 0.05764  0.04586  -0.02410 125 VAL B CG1   
3602 C CG2   . VAL C 126 ? 0.23080 0.53018 0.34627 0.03139  0.04061  -0.03198 125 VAL B CG2   
3603 N N     . ASP C 127 ? 0.20483 0.46998 0.29464 0.04284  0.07688  -0.03823 126 ASP B N     
3604 C CA    . ASP C 127 ? 0.22374 0.45811 0.29310 0.04184  0.08534  -0.03819 126 ASP B CA    
3605 C C     . ASP C 127 ? 0.22439 0.41532 0.27359 0.04956  0.07831  -0.03162 126 ASP B C     
3606 O O     . ASP C 127 ? 0.23322 0.42111 0.28616 0.06449  0.07129  -0.02811 126 ASP B O     
3607 C CB    . ASP C 127 ? 0.23902 0.49358 0.31649 0.05690  0.09639  -0.04439 126 ASP B CB    
3608 C CG    . ASP C 127 ? 0.32090 0.61359 0.41757 0.04754  0.10347  -0.05124 126 ASP B CG    
3609 O OD1   . ASP C 127 ? 0.38252 0.68341 0.48129 0.02613  0.10490  -0.05284 126 ASP B OD1   
3610 O OD2   . ASP C 127 ? 0.37224 0.67957 0.47937 0.06099  0.10724  -0.05436 126 ASP B OD2   
3611 N N     . THR C 128 ? 0.24699 0.40513 0.27379 0.03939  0.08084  -0.03040 127 THR B N     
3612 C CA    . THR C 128 ? 0.24512 0.36549 0.25339 0.04472  0.07562  -0.02671 127 THR B CA    
3613 C C     . THR C 128 ? 0.25891 0.37386 0.26704 0.06502  0.07989  -0.02877 127 THR B C     
3614 O O     . THR C 128 ? 0.24510 0.33963 0.24787 0.07403  0.07429  -0.02516 127 THR B O     
3615 C CB    . THR C 128 ? 0.29348 0.38818 0.27841 0.03194  0.07916  -0.02740 127 THR B CB    
3616 O OG1   . THR C 128 ? 0.28536 0.38047 0.26729 0.01546  0.07600  -0.02411 127 THR B OG1   
3617 C CG2   . THR C 128 ? 0.28517 0.34554 0.25206 0.03438  0.07346  -0.02570 127 THR B CG2   
3618 N N     . LYS C 129 ? 0.26130 0.39242 0.27400 0.07249  0.09118  -0.03471 128 LYS B N     
3619 C CA    . LYS C 129 ? 0.26943 0.39261 0.28017 0.09380  0.09705  -0.03681 128 LYS B CA    
3620 C C     . LYS C 129 ? 0.28103 0.41659 0.30583 0.11138  0.08990  -0.03194 128 LYS B C     
3621 O O     . LYS C 129 ? 0.27128 0.37959 0.28511 0.12527  0.08939  -0.02895 128 LYS B O     
3622 C CB    . LYS C 129 ? 0.29556 0.44170 0.31334 0.10060  0.11066  -0.04435 128 LYS B CB    
3623 C CG    . LYS C 129 ? 0.30886 0.45038 0.32839 0.12545  0.11583  -0.04569 128 LYS B CG    
3624 C CD    . LYS C 129 ? 0.31308 0.46824 0.33821 0.12800  0.12757  -0.05335 128 LYS B CD    
3625 C CE    . LYS C 129 ? 0.36649 0.53238 0.40619 0.14868  0.12674  -0.05283 128 LYS B CE    
3626 N NZ    . LYS C 129 ? 0.38612 0.51202 0.40872 0.16388  0.12483  -0.04888 128 LYS B NZ    
3627 N N     . GLN C 130 ? 0.24527 0.42069 0.29234 0.11021  0.08473  -0.03132 129 GLN B N     
3628 C CA    . GLN C 130 ? 0.27988 0.47022 0.33878 0.12784  0.07692  -0.02668 129 GLN B CA    
3629 C C     . GLN C 130 ? 0.24298 0.40098 0.28852 0.12621  0.06753  -0.01920 129 GLN B C     
3630 O O     . GLN C 130 ? 0.26479 0.40811 0.30457 0.14406  0.06525  -0.01420 129 GLN B O     
3631 C CB    . GLN C 130 ? 0.31393 0.54970 0.39689 0.12037  0.07046  -0.02849 129 GLN B CB    
3632 C CG    . GLN C 130 ? 0.34106 0.58700 0.43101 0.13454  0.05933  -0.02322 129 GLN B CG    
3633 C CD    . GLN C 130 ? 0.42828 0.71796 0.53899 0.12555  0.05229  -0.02645 129 GLN B CD    
3634 O OE1   . GLN C 130 ? 0.38218 0.68876 0.50098 0.10535  0.05428  -0.03135 129 GLN B OE1   
3635 N NE2   . GLN C 130 ? 0.46771 0.77384 0.58436 0.13972  0.04462  -0.02405 129 GLN B NE2   
3636 N N     . ALA C 131 ? 0.20648 0.35182 0.24604 0.10467  0.06223  -0.01799 130 ALA B N     
3637 C CA    . ALA C 131 ? 0.20942 0.32647 0.23803 0.10132  0.05376  -0.01184 130 ALA B CA    
3638 C C     . ALA C 131 ? 0.25321 0.32681 0.26025 0.10487  0.05825  -0.01141 130 ALA B C     
3639 O O     . ALA C 131 ? 0.24585 0.29670 0.24429 0.11241  0.05552  -0.00682 130 ALA B O     
3640 C CB    . ALA C 131 ? 0.24750 0.36420 0.27625 0.07931  0.04746  -0.01110 130 ALA B CB    
3641 N N     . GLN C 132 ? 0.24104 0.30223 0.23770 0.09882  0.06622  -0.01692 131 GLN B N     
3642 C CA    . GLN C 132 ? 0.26595 0.28722 0.24153 0.09993  0.07112  -0.01885 131 GLN B CA    
3643 C C     . GLN C 132 ? 0.28549 0.29362 0.25647 0.12242  0.07824  -0.01808 131 GLN B C     
3644 O O     . GLN C 132 ? 0.30768 0.28073 0.26304 0.12568  0.07994  -0.01654 131 GLN B O     
3645 C CB    . GLN C 132 ? 0.28032 0.29420 0.24442 0.08865  0.07788  -0.02576 131 GLN B CB    
3646 C CG    . GLN C 132 ? 0.28890 0.26443 0.23065 0.08741  0.08340  -0.03039 131 GLN B CG    
3647 C CD    . GLN C 132 ? 0.31753 0.27292 0.25047 0.07356  0.07470  -0.02867 131 GLN B CD    
3648 O OE1   . GLN C 132 ? 0.37800 0.31161 0.30547 0.07765  0.07407  -0.02685 131 GLN B OE1   
3649 N NE2   . GLN C 132 ? 0.28689 0.25007 0.21850 0.05769  0.06822  -0.02877 131 GLN B NE2   
3650 N N     . ASP C 133 ? 0.28212 0.31782 0.26597 0.13836  0.08342  -0.01943 132 ASP B N     
3651 C CA    . ASP C 133 ? 0.30693 0.33266 0.28774 0.16000  0.08750  -0.01700 132 ASP B CA    
3652 C C     . ASP C 133 ? 0.30741 0.32370 0.28640 0.16688  0.07856  -0.00780 132 ASP B C     
3653 O O     . ASP C 133 ? 0.36595 0.34780 0.32833 0.17429  0.08130  -0.00424 132 ASP B O     
3654 C CB    . ASP C 133 ? 0.30992 0.37530 0.31052 0.16912  0.08862  -0.01935 132 ASP B CB    
3655 C CG    . ASP C 133 ? 0.34146 0.40778 0.33952 0.16596  0.10025  -0.02826 132 ASP B CG    
3656 O OD1   . ASP C 133 ? 0.37339 0.40547 0.35083 0.15847  0.10731  -0.03249 132 ASP B OD1   
3657 O OD2   . ASP C 133 ? 0.33752 0.43921 0.35369 0.17001  0.10242  -0.03169 132 ASP B OD2   
3658 N N     . LEU C 134 ? 0.29097 0.33719 0.28533 0.16317  0.06859  -0.00413 133 LEU B N     
3659 C CA    . LEU C 134 ? 0.30456 0.34226 0.29503 0.16796  0.06012  0.00431  133 LEU B CA    
3660 C C     . LEU C 134 ? 0.32356 0.31575 0.29359 0.16076  0.06255  0.00631  133 LEU B C     
3661 O O     . LEU C 134 ? 0.37617 0.33978 0.33115 0.16709  0.06353  0.01176  133 LEU B O     
3662 C CB    . LEU C 134 ? 0.29583 0.37296 0.30535 0.16155  0.04928  0.00594  133 LEU B CB    
3663 C CG    . LEU C 134 ? 0.28745 0.36009 0.29198 0.16729  0.04042  0.01417  133 LEU B CG    
3664 C CD1   . LEU C 134 ? 0.35958 0.43953 0.36184 0.18491  0.03978  0.01764  133 LEU B CD1   
3665 C CD2   . LEU C 134 ? 0.34253 0.44684 0.36224 0.15684  0.03040  0.01427  133 LEU B CD2   
3666 N N     . ALA C 135 ? 0.29045 0.27590 0.25902 0.14032  0.06145  0.00188  134 ALA B N     
3667 C CA    . ALA C 135 ? 0.31595 0.26367 0.26811 0.12792  0.06171  0.00217  134 ALA B CA    
3668 C C     . ALA C 135 ? 0.39255 0.29940 0.32358 0.13503  0.07399  -0.00098 134 ALA B C     
3669 O O     . ALA C 135 ? 0.40314 0.27581 0.31861 0.13580  0.07746  0.00178  134 ALA B O     
3670 C CB    . ALA C 135 ? 0.32695 0.27949 0.28200 0.10414  0.05664  -0.00261 134 ALA B CB    
3671 N N     . ARG C 136 ? 0.37568 0.28357 0.30445 0.13976  0.08218  -0.00729 135 ARG B N     
3672 C CA    . ARG C 136 ? 0.37913 0.24905 0.28807 0.14249  0.09263  -0.01079 135 ARG B CA    
3673 C C     . ARG C 136 ? 0.43377 0.29161 0.33683 0.15745  0.09299  -0.00209 135 ARG B C     
3674 O O     . ARG C 136 ? 0.45200 0.27160 0.33575 0.15492  0.09935  -0.00144 135 ARG B O     
3675 C CB    . ARG C 136 ? 0.39633 0.27336 0.30508 0.14410  0.10034  -0.01895 135 ARG B CB    
3676 C CG    . ARG C 136 ? 0.42768 0.26435 0.31471 0.14057  0.11067  -0.02497 135 ARG B CG    
3677 C CD    . ARG C 136 ? 0.45220 0.29556 0.33788 0.14171  0.11867  -0.03378 135 ARG B CD    
3678 N NE    . ARG C 136 ? 0.43638 0.30091 0.32677 0.12898  0.11723  -0.04015 135 ARG B NE    
3679 C CZ    . ARG C 136 ? 0.40413 0.30790 0.31196 0.13345  0.11591  -0.03977 135 ARG B CZ    
3680 N NH1   . ARG C 136 ? 0.41139 0.34147 0.33656 0.14975  0.11491  -0.03520 135 ARG B NH1   
3681 N NH2   . ARG C 136 ? 0.39047 0.31040 0.29993 0.11650  0.11267  -0.04349 135 ARG B NH2   
3682 N N     . SER C 137 ? 0.42111 0.31205 0.33924 0.17192  0.08643  0.00430  136 SER B N     
3683 C CA    . SER C 137 ? 0.43694 0.31808 0.34647 0.18773  0.08647  0.01277  136 SER B CA    
3684 C C     . SER C 137 ? 0.44421 0.30435 0.34206 0.18296  0.08316  0.01991  136 SER B C     
3685 O O     . SER C 137 ? 0.49224 0.32523 0.37200 0.19102  0.08793  0.02571  136 SER B O     
3686 C CB    . SER C 137 ? 0.43572 0.36169 0.36437 0.20303  0.07943  0.01601  136 SER B CB    
3687 O OG    . SER C 137 ? 0.41914 0.37427 0.36130 0.19945  0.06805  0.01996  136 SER B OG    
3688 N N     . TYR C 138 ? 0.42027 0.29153 0.32689 0.17017  0.07620  0.01951  137 TYR B N     
3689 C CA    . TYR C 138 ? 0.42957 0.28171 0.32638 0.16291  0.07386  0.02480  137 TYR B CA    
3690 C C     . TYR C 138 ? 0.46944 0.28087 0.34989 0.14629  0.08216  0.01963  137 TYR B C     
3691 O O     . TYR C 138 ? 0.55650 0.34836 0.42700 0.13889  0.08282  0.02315  137 TYR B O     
3692 C CB    . TYR C 138 ? 0.42925 0.31139 0.34372 0.15522  0.06309  0.02545  137 TYR B CB    
3693 C CG    . TYR C 138 ? 0.38635 0.31206 0.31798 0.16575  0.05305  0.02965  137 TYR B CG    
3694 C CD1   . TYR C 138 ? 0.46782 0.40270 0.39642 0.18255  0.05254  0.03436  137 TYR B CD1   
3695 C CD2   . TYR C 138 ? 0.37709 0.33509 0.32727 0.15768  0.04405  0.02823  137 TYR B CD2   
3696 C CE1   . TYR C 138 ? 0.38955 0.36701 0.33396 0.18987  0.04273  0.03640  137 TYR B CE1   
3697 C CE2   . TYR C 138 ? 0.36808 0.36729 0.33398 0.16341  0.03505  0.03004  137 TYR B CE2   
3698 C CZ    . TYR C 138 ? 0.37724 0.38666 0.34043 0.17874  0.03421  0.03353  137 TYR B CZ    
3699 O OH    . TYR C 138 ? 0.42126 0.47268 0.39947 0.18268  0.02511  0.03367  137 TYR B OH    
3700 N N     . GLY C 139 ? 0.48392 0.28540 0.36194 0.13871  0.08836  0.01035  138 GLY B N     
3701 C CA    . GLY C 139 ? 0.47223 0.24246 0.33737 0.11942  0.09484  0.00226  138 GLY B CA    
3702 C C     . GLY C 139 ? 0.48497 0.26205 0.35791 0.10291  0.08841  -0.00099 138 GLY B C     
3703 O O     . GLY C 139 ? 0.51584 0.27005 0.37946 0.08793  0.09138  -0.00361 138 GLY B O     
3704 N N     . ILE C 140 ? 0.41434 0.22860 0.30653 0.10204  0.07827  -0.00063 139 ILE B N     
3705 C CA    . ILE C 140 ? 0.38580 0.21866 0.29007 0.08279  0.06763  -0.00185 139 ILE B CA    
3706 C C     . ILE C 140 ? 0.34329 0.20176 0.25825 0.07209  0.06175  -0.00804 139 ILE B C     
3707 O O     . ILE C 140 ? 0.35260 0.22367 0.27041 0.08041  0.06425  -0.00962 139 ILE B O     
3708 C CB    . ILE C 140 ? 0.37623 0.23128 0.29279 0.08832  0.05850  0.00728  139 ILE B CB    
3709 C CG1   . ILE C 140 ? 0.36967 0.26263 0.30271 0.09902  0.05208  0.01012  139 ILE B CG1   
3710 C CG2   . ILE C 140 ? 0.39333 0.22156 0.29539 0.10014  0.06452  0.01464  139 ILE B CG2   
3711 C CD1   . ILE C 140 ? 0.35782 0.27455 0.30216 0.10332  0.04296  0.01729  139 ILE B CD1   
3712 N N     . PRO C 141 ? 0.35596 0.22260 0.27599 0.05436  0.05444  -0.01145 140 PRO B N     
3713 C CA    . PRO C 141 ? 0.30357 0.19244 0.23044 0.04560  0.04834  -0.01531 140 PRO B CA    
3714 C C     . PRO C 141 ? 0.27606 0.19609 0.21851 0.05162  0.04196  -0.00937 140 PRO B C     
3715 O O     . PRO C 141 ? 0.28150 0.21150 0.23267 0.05786  0.03816  -0.00296 140 PRO B O     
3716 C CB    . PRO C 141 ? 0.31034 0.20009 0.23859 0.02867  0.04129  -0.01874 140 PRO B CB    
3717 C CG    . PRO C 141 ? 0.36692 0.22931 0.28593 0.02532  0.04779  -0.02082 140 PRO B CG    
3718 C CD    . PRO C 141 ? 0.36824 0.22250 0.28607 0.04188  0.05269  -0.01253 140 PRO B CD    
3719 N N     . PHE C 142 ? 0.31645 0.25155 0.26089 0.04820  0.04140  -0.01227 141 PHE B N     
3720 C CA    . PHE C 142 ? 0.24764 0.21133 0.20547 0.04846  0.03669  -0.00871 141 PHE B CA    
3721 C C     . PHE C 142 ? 0.25866 0.22794 0.21372 0.03483  0.03186  -0.01067 141 PHE B C     
3722 O O     . PHE C 142 ? 0.28061 0.23976 0.22339 0.02973  0.03474  -0.01592 141 PHE B O     
3723 C CB    . PHE C 142 ? 0.25647 0.23351 0.21815 0.05998  0.04397  -0.00989 141 PHE B CB    
3724 C CG    . PHE C 142 ? 0.23886 0.24573 0.21315 0.05608  0.04170  -0.00898 141 PHE B CG    
3725 C CD1   . PHE C 142 ? 0.24979 0.27538 0.23730 0.05440  0.03485  -0.00465 141 PHE B CD1   
3726 C CD2   . PHE C 142 ? 0.28738 0.30280 0.25923 0.05329  0.04790  -0.01325 141 PHE B CD2   
3727 C CE1   . PHE C 142 ? 0.24516 0.29569 0.24293 0.04813  0.03447  -0.00525 141 PHE B CE1   
3728 C CE2   . PHE C 142 ? 0.26858 0.30966 0.25101 0.04737  0.04787  -0.01296 141 PHE B CE2   
3729 C CZ    . PHE C 142 ? 0.27856 0.33641 0.27381 0.04428  0.04154  -0.00937 141 PHE B CZ    
3730 N N     . ILE C 143 ? 0.22942 0.21328 0.19366 0.02966  0.02486  -0.00643 142 ILE B N     
3731 C CA    A ILE C 143 ? 0.23941 0.22609 0.19908 0.01915  0.02022  -0.00618 142 ILE B CA    
3732 C CA    B ILE C 143 ? 0.23949 0.22632 0.19895 0.01932  0.02061  -0.00632 142 ILE B CA    
3733 C C     . ILE C 143 ? 0.22468 0.22956 0.19361 0.01710  0.01965  -0.00266 142 ILE B C     
3734 O O     . ILE C 143 ? 0.23190 0.24694 0.21269 0.01981  0.01710  0.00011  142 ILE B O     
3735 C CB    A ILE C 143 ? 0.25531 0.23421 0.21377 0.01317  0.01211  -0.00519 142 ILE B CB    
3736 C CB    B ILE C 143 ? 0.25968 0.23747 0.21623 0.01295  0.01279  -0.00593 142 ILE B CB    
3737 C CG1   A ILE C 143 ? 0.26922 0.23235 0.21822 0.01098  0.01328  -0.01095 142 ILE B CG1   
3738 C CG1   B ILE C 143 ? 0.26688 0.24665 0.21580 0.00586  0.00796  -0.00467 142 ILE B CG1   
3739 C CG2   A ILE C 143 ? 0.26680 0.24926 0.22041 0.00627  0.00662  -0.00290 142 ILE B CG2   
3740 C CG2   B ILE C 143 ? 0.25379 0.23606 0.22217 0.01487  0.00860  -0.00181 142 ILE B CG2   
3741 C CD1   A ILE C 143 ? 0.29753 0.25808 0.24981 0.00552  0.00646  -0.01140 142 ILE B CD1   
3742 C CD1   B ILE C 143 ? 0.30087 0.27697 0.24883 0.00204  -0.00033 -0.00476 142 ILE B CD1   
3743 N N     . GLU C 144 ? 0.22872 0.23663 0.19054 0.01108  0.02259  -0.00323 143 GLU B N     
3744 C CA    . GLU C 144 ? 0.20604 0.22583 0.17292 0.00484  0.02318  -0.00055 143 GLU B CA    
3745 C C     . GLU C 144 ? 0.22933 0.23706 0.18767 -0.00182 0.01654  0.00349  143 GLU B C     
3746 O O     . GLU C 144 ? 0.26017 0.25519 0.20422 -0.00327 0.01384  0.00360  143 GLU B O     
3747 C CB    . GLU C 144 ? 0.24660 0.27519 0.20956 0.00121  0.03247  -0.00307 143 GLU B CB    
3748 C CG    . GLU C 144 ? 0.26445 0.30994 0.23910 0.01015  0.03919  -0.00728 143 GLU B CG    
3749 C CD    . GLU C 144 ? 0.25593 0.31814 0.23283 0.00609  0.04922  -0.01074 143 GLU B CD    
3750 O OE1   . GLU C 144 ? 0.28128 0.33668 0.24579 -0.00481 0.05281  -0.00986 143 GLU B OE1   
3751 O OE2   . GLU C 144 ? 0.25336 0.33543 0.24366 0.01480  0.05407  -0.01427 143 GLU B OE2   
3752 N N     . THR C 145 ? 0.20581 0.21820 0.17220 -0.00493 0.01385  0.00633  144 THR B N     
3753 C CA    . THR C 145 ? 0.22531 0.22562 0.18542 -0.00823 0.00786  0.01042  144 THR B CA    
3754 C C     . THR C 145 ? 0.22814 0.22802 0.18582 -0.01623 0.01216  0.01250  144 THR B C     
3755 O O     . THR C 145 ? 0.22241 0.23699 0.18913 -0.02038 0.01825  0.00967  144 THR B O     
3756 C CB    . THR C 145 ? 0.20881 0.21036 0.18014 -0.00438 0.00135  0.01106  144 THR B CB    
3757 O OG1   . THR C 145 ? 0.19598 0.21161 0.18071 -0.00434 0.00330  0.01001  144 THR B OG1   
3758 C CG2   . THR C 145 ? 0.21259 0.21128 0.18503 0.00118  -0.00106 0.00855  144 THR B CG2   
3759 N N     . SER C 146 ? 0.24406 0.22709 0.18908 -0.01820 0.00928  0.01703  145 SER B N     
3760 C CA    . SER C 146 ? 0.24142 0.21613 0.18237 -0.02544 0.01302  0.01943  145 SER B CA    
3761 C C     . SER C 146 ? 0.25025 0.21307 0.19023 -0.02083 0.00566  0.02287  145 SER B C     
3762 O O     . SER C 146 ? 0.28325 0.23305 0.21077 -0.01520 0.00060  0.02698  145 SER B O     
3763 C CB    . SER C 146 ? 0.30029 0.25900 0.21992 -0.03148 0.02019  0.02281  145 SER B CB    
3764 O OG    . SER C 146 ? 0.30158 0.24544 0.21421 -0.03837 0.02447  0.02540  145 SER B OG    
3765 N N     . ALA C 147 ? 0.24984 0.21901 0.20274 -0.02261 0.00497  0.02077  146 ALA B N     
3766 C CA    . ALA C 147 ? 0.25503 0.21118 0.20558 -0.01909 0.00050  0.02355  146 ALA B CA    
3767 C C     . ALA C 147 ? 0.28740 0.21881 0.21810 -0.02209 0.00505  0.02846  146 ALA B C     
3768 O O     . ALA C 147 ? 0.35858 0.27521 0.28134 -0.01467 0.00070  0.03273  146 ALA B O     
3769 C CB    . ALA C 147 ? 0.24470 0.21104 0.20993 -0.02178 0.00037  0.01962  146 ALA B CB    
3770 N N     . LYS C 148 ? 0.27993 0.20627 0.20181 -0.03233 0.01452  0.02795  147 LYS B N     
3771 C CA    . LYS C 148 ? 0.34388 0.24097 0.24303 -0.03662 0.02148  0.03306  147 LYS B CA    
3772 C C     . LYS C 148 ? 0.40561 0.28586 0.28375 -0.02670 0.01752  0.04082  147 LYS B C     
3773 O O     . LYS C 148 ? 0.47529 0.33184 0.33728 -0.01943 0.01582  0.04726  147 LYS B O     
3774 C CB    . LYS C 148 ? 0.34148 0.23971 0.23737 -0.05256 0.03416  0.02926  147 LYS B CB    
3775 C CG    . LYS C 148 ? 0.39095 0.25275 0.25979 -0.05922 0.04416  0.03457  147 LYS B CG    
3776 C CD    . LYS C 148 ? 0.48042 0.34440 0.34924 -0.07929 0.05850  0.02827  147 LYS B CD    
3777 C CE    . LYS C 148 ? 0.53487 0.35725 0.37132 -0.08751 0.07144  0.03427  147 LYS B CE    
3778 N NZ    . LYS C 148 ? 0.67650 0.49859 0.51560 -0.10958 0.08558  0.02584  147 LYS B NZ    
3779 N N     . THR C 149 ? 0.37337 0.26599 0.25051 -0.02502 0.01567  0.04007  148 THR B N     
3780 C CA    . THR C 149 ? 0.40721 0.28671 0.26239 -0.01652 0.01136  0.04646  148 THR B CA    
3781 C C     . THR C 149 ? 0.37461 0.26886 0.23921 -0.00458 -0.00204 0.04536  148 THR B C     
3782 O O     . THR C 149 ? 0.39519 0.28321 0.24316 0.00358  -0.00813 0.04969  148 THR B O     
3783 C CB    . THR C 149 ? 0.43165 0.31400 0.27584 -0.02290 0.01827  0.04539  148 THR B CB    
3784 O OG1   . THR C 149 ? 0.38108 0.29027 0.24527 -0.02212 0.01466  0.03803  148 THR B OG1   
3785 C CG2   . THR C 149 ? 0.47371 0.34753 0.31241 -0.03766 0.03321  0.04428  148 THR B CG2   
3786 N N     . ARG C 150 ? 0.34073 0.25483 0.23014 -0.00417 -0.00626 0.03931  149 ARG B N     
3787 C CA    . ARG C 150 ? 0.35013 0.28022 0.25230 0.00323  -0.01642 0.03597  149 ARG B CA    
3788 C C     . ARG C 150 ? 0.32499 0.26761 0.22797 0.00160  -0.01718 0.03109  149 ARG B C     
3789 O O     . ARG C 150 ? 0.30995 0.26489 0.22297 0.00494  -0.02389 0.02667  149 ARG B O     
3790 C CB    . ARG C 150 ? 0.41113 0.33622 0.30639 0.01436  -0.02574 0.04019  149 ARG B CB    
3791 C CG    . ARG C 150 ? 0.38467 0.32397 0.30210 0.01808  -0.03139 0.03609  149 ARG B CG    
3792 C CD    . ARG C 150 ? 0.40867 0.34692 0.32287 0.03017  -0.03978 0.03958  149 ARG B CD    
3793 N NE    . ARG C 150 ? 0.44375 0.40036 0.38049 0.03208  -0.04438 0.03392  149 ARG B NE    
3794 C CZ    . ARG C 150 ? 0.40689 0.38316 0.35505 0.03019  -0.04922 0.02745  149 ARG B CZ    
3795 N NH1   . ARG C 150 ? 0.48822 0.46864 0.42757 0.02711  -0.05090 0.02529  149 ARG B NH1   
3796 N NH2   . ARG C 150 ? 0.39351 0.38410 0.36079 0.03050  -0.05136 0.02246  149 ARG B NH2   
3797 N N     . GLN C 151 ? 0.32271 0.26232 0.21582 -0.00429 -0.00928 0.03070  150 GLN B N     
3798 C CA    . GLN C 151 ? 0.29849 0.24764 0.19122 -0.00548 -0.00814 0.02526  150 GLN B CA    
3799 C C     . GLN C 151 ? 0.27395 0.23778 0.18877 -0.00491 -0.00904 0.01893  150 GLN B C     
3800 O O     . GLN C 151 ? 0.26315 0.23333 0.19205 -0.00699 -0.00478 0.01797  150 GLN B O     
3801 C CB    . GLN C 151 ? 0.31055 0.25668 0.19353 -0.01225 0.00306  0.02502  150 GLN B CB    
3802 C CG    . GLN C 151 ? 0.35559 0.31068 0.23842 -0.01271 0.00642  0.01850  150 GLN B CG    
3803 C CD    . GLN C 151 ? 0.43470 0.38456 0.29925 -0.00960 0.00024  0.01765  150 GLN B CD    
3804 O OE1   . GLN C 151 ? 0.47520 0.41357 0.31915 -0.00801 -0.00293 0.02344  150 GLN B OE1   
3805 N NE2   . GLN C 151 ? 0.44451 0.40189 0.31461 -0.00859 -0.00123 0.01017  150 GLN B NE2   
3806 N N     . GLY C 152 ? 0.27723 0.24573 0.19353 -0.00228 -0.01459 0.01455  151 GLY B N     
3807 C CA    . GLY C 152 ? 0.25645 0.23261 0.18801 -0.00197 -0.01339 0.00886  151 GLY B CA    
3808 C C     . GLY C 152 ? 0.26075 0.24128 0.20827 -0.00008 -0.01743 0.00916  151 GLY B C     
3809 O O     . GLY C 152 ? 0.25681 0.24020 0.21393 0.00036  -0.01551 0.00540  151 GLY B O     
3810 N N     . VAL C 153 ? 0.24623 0.22502 0.19495 0.00155  -0.02177 0.01361  152 VAL B N     
3811 C CA    . VAL C 153 ? 0.26358 0.24655 0.22716 0.00300  -0.02381 0.01359  152 VAL B CA    
3812 C C     . VAL C 153 ? 0.26383 0.25292 0.23447 0.00357  -0.02838 0.00880  152 VAL B C     
3813 O O     . VAL C 153 ? 0.23940 0.23064 0.21992 0.00248  -0.02567 0.00598  152 VAL B O     
3814 C CB    . VAL C 153 ? 0.25330 0.23058 0.21509 0.00508  -0.02597 0.01864  152 VAL B CB    
3815 C CG1   . VAL C 153 ? 0.27030 0.25265 0.24670 0.00673  -0.02788 0.01739  152 VAL B CG1   
3816 C CG2   . VAL C 153 ? 0.27356 0.24381 0.22964 0.00086  -0.01906 0.02168  152 VAL B CG2   
3817 N N     . ASP C 154 ? 0.25842 0.25104 0.22335 0.00509  -0.03512 0.00766  153 ASP B N     
3818 C CA    . ASP C 154 ? 0.27992 0.28234 0.25270 0.00287  -0.03884 0.00089  153 ASP B CA    
3819 C C     . ASP C 154 ? 0.27628 0.27459 0.24746 -0.00273 -0.03283 -0.00520 153 ASP B C     
3820 O O     . ASP C 154 ? 0.26796 0.26678 0.24791 -0.00626 -0.02997 -0.00969 153 ASP B O     
3821 C CB    . ASP C 154 ? 0.27037 0.28243 0.23669 0.00551  -0.04798 -0.00062 153 ASP B CB    
3822 C CG    . ASP C 154 ? 0.28752 0.30308 0.25634 0.01399  -0.05393 0.00517  153 ASP B CG    
3823 O OD1   . ASP C 154 ? 0.37707 0.39052 0.35658 0.01567  -0.05127 0.00749  153 ASP B OD1   
3824 O OD2   . ASP C 154 ? 0.39593 0.41591 0.35423 0.02005  -0.06139 0.00728  153 ASP B OD2   
3825 N N     A ASP C 155 ? 0.26016 0.25170 0.21881 -0.00335 -0.02923 -0.00520 154 ASP B N     
3826 N N     B ASP C 155 ? 0.26051 0.25211 0.21892 -0.00342 -0.02931 -0.00533 154 ASP B N     
3827 C CA    A ASP C 155 ? 0.27903 0.26386 0.23381 -0.00705 -0.02264 -0.01140 154 ASP B CA    
3828 C CA    B ASP C 155 ? 0.27923 0.26389 0.23380 -0.00707 -0.02252 -0.01147 154 ASP B CA    
3829 C C     A ASP C 155 ? 0.25096 0.22942 0.21462 -0.00519 -0.01530 -0.01020 154 ASP B C     
3830 C C     B ASP C 155 ? 0.25090 0.22946 0.21475 -0.00523 -0.01539 -0.01022 154 ASP B C     
3831 O O     A ASP C 155 ? 0.25124 0.22197 0.21493 -0.00781 -0.01045 -0.01526 154 ASP B O     
3832 O O     B ASP C 155 ? 0.25037 0.22146 0.21461 -0.00795 -0.01071 -0.01526 154 ASP B O     
3833 C CB    A ASP C 155 ? 0.26402 0.24368 0.20349 -0.00678 -0.01933 -0.01143 154 ASP B CB    
3834 C CB    B ASP C 155 ? 0.26420 0.24327 0.20377 -0.00668 -0.01861 -0.01142 154 ASP B CB    
3835 C CG    A ASP C 155 ? 0.35522 0.33960 0.28152 -0.00854 -0.02664 -0.01357 154 ASP B CG    
3836 C CG    B ASP C 155 ? 0.27142 0.24152 0.20368 -0.00992 -0.01159 -0.01947 154 ASP B CG    
3837 O OD1   A ASP C 155 ? 0.42250 0.41553 0.35230 -0.01167 -0.03306 -0.01917 154 ASP B OD1   
3838 O OD1   B ASP C 155 ? 0.29206 0.26021 0.22624 -0.01504 -0.01192 -0.02646 154 ASP B OD1   
3839 O OD2   A ASP C 155 ? 0.40520 0.38608 0.31715 -0.00700 -0.02591 -0.00999 154 ASP B OD2   
3840 O OD2   B ASP C 155 ? 0.27955 0.24383 0.20342 -0.00796 -0.00466 -0.01971 154 ASP B OD2   
3841 N N     . ALA C 156 ? 0.22821 0.20888 0.19773 -0.00083 -0.01413 -0.00377 155 ALA B N     
3842 C CA    . ALA C 156 ? 0.24357 0.22126 0.22001 0.00274  -0.00867 -0.00214 155 ALA B CA    
3843 C C     . ALA C 156 ? 0.23002 0.20546 0.21341 0.00086  -0.00926 -0.00358 155 ALA B C     
3844 O O     . ALA C 156 ? 0.23487 0.20005 0.21647 0.00147  -0.00335 -0.00539 155 ALA B O     
3845 C CB    . ALA C 156 ? 0.25489 0.24017 0.23692 0.00587  -0.00884 0.00343  155 ALA B CB    
3846 N N     . PHE C 157 ? 0.22588 0.20928 0.21594 -0.00103 -0.01528 -0.00271 156 PHE B N     
3847 C CA    . PHE C 157 ? 0.21271 0.19645 0.21049 -0.00371 -0.01471 -0.00472 156 PHE B CA    
3848 C C     . PHE C 157 ? 0.23626 0.21671 0.23176 -0.01100 -0.01279 -0.01262 156 PHE B C     
3849 O O     . PHE C 157 ? 0.21228 0.18407 0.20866 -0.01460 -0.00665 -0.01507 156 PHE B O     
3850 C CB    . PHE C 157 ? 0.23490 0.22953 0.24114 -0.00271 -0.02087 -0.00265 156 PHE B CB    
3851 C CG    . PHE C 157 ? 0.19489 0.18945 0.20355 0.00160  -0.02037 0.00313  156 PHE B CG    
3852 C CD1   . PHE C 157 ? 0.20814 0.20116 0.22156 0.00235  -0.01704 0.00438  156 PHE B CD1   
3853 C CD2   . PHE C 157 ? 0.20676 0.20194 0.21114 0.00374  -0.02235 0.00678  156 PHE B CD2   
3854 C CE1   . PHE C 157 ? 0.22179 0.21672 0.23660 0.00512  -0.01699 0.00816  156 PHE B CE1   
3855 C CE2   . PHE C 157 ? 0.22498 0.22072 0.23156 0.00508  -0.02103 0.01021  156 PHE B CE2   
3856 C CZ    . PHE C 157 ? 0.19440 0.19145 0.20664 0.00574  -0.01907 0.01040  156 PHE B CZ    
3857 N N     . TYR C 158 ? 0.22017 0.20679 0.21121 -0.01422 -0.01743 -0.01710 157 TYR B N     
3858 C CA    . TYR C 158 ? 0.20896 0.19578 0.19819 -0.02351 -0.01610 -0.02683 157 TYR B CA    
3859 C C     . TYR C 158 ? 0.22666 0.19228 0.20455 -0.02608 -0.00586 -0.03021 157 TYR B C     
3860 O O     . TYR C 158 ? 0.24517 0.20166 0.22150 -0.03460 0.00033  -0.03721 157 TYR B O     
3861 C CB    . TYR C 158 ? 0.23722 0.23873 0.22276 -0.02551 -0.02502 -0.03120 157 TYR B CB    
3862 C CG    . TYR C 158 ? 0.27028 0.29219 0.26571 -0.02135 -0.03517 -0.02879 157 TYR B CG    
3863 C CD1   . TYR C 158 ? 0.31266 0.33806 0.31983 -0.01679 -0.03529 -0.02353 157 TYR B CD1   
3864 C CD2   . TYR C 158 ? 0.31007 0.34706 0.30101 -0.02058 -0.04455 -0.03179 157 TYR B CD2   
3865 C CE1   . TYR C 158 ? 0.30201 0.34374 0.31698 -0.01096 -0.04356 -0.02146 157 TYR B CE1   
3866 C CE2   . TYR C 158 ? 0.28390 0.33876 0.28225 -0.01354 -0.05395 -0.02890 157 TYR B CE2   
3867 C CZ    . TYR C 158 ? 0.31328 0.36946 0.32407 -0.00837 -0.05288 -0.02372 157 TYR B CZ    
3868 O OH    . TYR C 158 ? 0.38271 0.45459 0.40017 0.00058  -0.06120 -0.02093 157 TYR B OH    
3869 N N     . THR C 159 ? 0.22988 0.18675 0.19936 -0.01875 -0.00285 -0.02567 158 THR B N     
3870 C CA    . THR C 159 ? 0.27649 0.21210 0.23518 -0.01748 0.00765  -0.02790 158 THR B CA    
3871 C C     . THR C 159 ? 0.24668 0.16862 0.20727 -0.01475 0.01472  -0.02426 158 THR B C     
3872 O O     . THR C 159 ? 0.25782 0.15821 0.20891 -0.01817 0.02420  -0.02845 158 THR B O     
3873 C CB    . THR C 159 ? 0.27406 0.20852 0.22663 -0.00844 0.00947  -0.02366 158 THR B CB    
3874 O OG1   . THR C 159 ? 0.28811 0.23074 0.23407 -0.01254 0.00462  -0.02770 158 THR B OG1   
3875 C CG2   . THR C 159 ? 0.28998 0.20295 0.23236 -0.00292 0.02082  -0.02493 158 THR B CG2   
3876 N N     . LEU C 160 ? 0.23453 0.16630 0.20474 -0.00897 0.01096  -0.01662 159 LEU B N     
3877 C CA    . LEU C 160 ? 0.23675 0.15607 0.20605 -0.00580 0.01711  -0.01249 159 LEU B CA    
3878 C C     . LEU C 160 ? 0.23688 0.14881 0.20663 -0.01770 0.02142  -0.01873 159 LEU B C     
3879 O O     . LEU C 160 ? 0.26619 0.15457 0.22546 -0.01905 0.03173  -0.01916 159 LEU B O     
3880 C CB    . LEU C 160 ? 0.22190 0.15559 0.20051 0.00119  0.01160  -0.00466 159 LEU B CB    
3881 C CG    . LEU C 160 ? 0.22837 0.15030 0.20347 0.00521  0.01721  0.00017  159 LEU B CG    
3882 C CD1   . LEU C 160 ? 0.26030 0.16182 0.22157 0.01491  0.02534  0.00337  159 LEU B CD1   
3883 C CD2   . LEU C 160 ? 0.23259 0.17095 0.21618 0.01045  0.01104  0.00598  159 LEU B CD2   
3884 N N     . VAL C 161 ? 0.23487 0.16632 0.21563 -0.02649 0.01444  -0.02420 160 VAL B N     
3885 C CA    . VAL C 161 ? 0.24391 0.17483 0.22817 -0.03998 0.01868  -0.03264 160 VAL B CA    
3886 C C     . VAL C 161 ? 0.25908 0.16956 0.23006 -0.04927 0.02761  -0.04147 160 VAL B C     
3887 O O     . VAL C 161 ? 0.29125 0.18261 0.25592 -0.05824 0.03858  -0.04559 160 VAL B O     
3888 C CB    . VAL C 161 ? 0.24096 0.20252 0.24109 -0.04516 0.00811  -0.03760 160 VAL B CB    
3889 C CG1   . VAL C 161 ? 0.24099 0.20929 0.24731 -0.06127 0.01215  -0.04958 160 VAL B CG1   
3890 C CG2   . VAL C 161 ? 0.21507 0.19024 0.22644 -0.03689 0.00261  -0.02971 160 VAL B CG2   
3891 N N     . ARG C 162 ? 0.27075 0.18229 0.23507 -0.04837 0.02444  -0.04515 161 ARG B N     
3892 C CA    . ARG C 162 ? 0.32581 0.21537 0.27518 -0.05725 0.03380  -0.05468 161 ARG B CA    
3893 C C     . ARG C 162 ? 0.32394 0.17669 0.25707 -0.05031 0.04769  -0.04970 161 ARG B C     
3894 O O     . ARG C 162 ? 0.37689 0.20400 0.29803 -0.06044 0.05960  -0.05676 161 ARG B O     
3895 C CB    . ARG C 162 ? 0.31432 0.21255 0.25795 -0.05581 0.02767  -0.05873 161 ARG B CB    
3896 C CG    . ARG C 162 ? 0.29930 0.23064 0.25375 -0.06248 0.01432  -0.06451 161 ARG B CG    
3897 C CD    . ARG C 162 ? 0.43113 0.36858 0.37508 -0.05997 0.00854  -0.06716 161 ARG B CD    
3898 N NE    . ARG C 162 ? 0.41044 0.37892 0.36173 -0.06153 -0.00562 -0.06930 161 ARG B NE    
3899 C CZ    . ARG C 162 ? 0.34024 0.32188 0.29254 -0.05062 -0.01480 -0.06034 161 ARG B CZ    
3900 N NH1   . ARG C 162 ? 0.40354 0.37381 0.35148 -0.03972 -0.01154 -0.05029 161 ARG B NH1   
3901 N NH2   . ARG C 162 ? 0.39374 0.40079 0.35073 -0.05064 -0.02714 -0.06183 161 ARG B NH2   
3902 N N     . GLU C 163 ? 0.31914 0.16930 0.25164 -0.03325 0.04665  -0.03762 162 GLU B N     
3903 C CA    . GLU C 163 ? 0.36408 0.18244 0.28133 -0.02269 0.05835  -0.03112 162 GLU B CA    
3904 C C     . GLU C 163 ? 0.35904 0.16056 0.27238 -0.02859 0.06643  -0.02924 162 GLU B C     
3905 O O     . GLU C 163 ? 0.39966 0.16483 0.29428 -0.02974 0.08040  -0.02992 162 GLU B O     
3906 C CB    . GLU C 163 ? 0.35880 0.18754 0.27955 -0.00317 0.05319  -0.01959 162 GLU B CB    
3907 C CG    . GLU C 163 ? 0.36462 0.20248 0.28471 0.00364  0.05011  -0.02117 162 GLU B CG    
3908 C CD    . GLU C 163 ? 0.41434 0.22150 0.31578 0.00544  0.06234  -0.02662 162 GLU B CD    
3909 O OE1   . GLU C 163 ? 0.47084 0.25499 0.36084 0.01899  0.07114  -0.02058 162 GLU B OE1   
3910 O OE2   . GLU C 163 ? 0.46207 0.26723 0.35881 -0.00611 0.06327  -0.03711 162 GLU B OE2   
3911 N N     . ILE C 164 ? 0.33717 0.16178 0.26589 -0.03230 0.05928  -0.02682 163 ILE B N     
3912 C CA    . ILE C 164 ? 0.34439 0.15502 0.26959 -0.04043 0.06801  -0.02642 163 ILE B CA    
3913 C C     . ILE C 164 ? 0.42222 0.21800 0.34181 -0.06119 0.07824  -0.03967 163 ILE B C     
3914 O O     . ILE C 164 ? 0.45686 0.22217 0.36081 -0.06639 0.09235  -0.03952 163 ILE B O     
3915 C CB    . ILE C 164 ? 0.31564 0.15723 0.26008 -0.04169 0.05858  -0.02370 163 ILE B CB    
3916 C CG1   . ILE C 164 ? 0.29878 0.15085 0.24587 -0.02365 0.05074  -0.01179 163 ILE B CG1   
3917 C CG2   . ILE C 164 ? 0.34678 0.17546 0.28782 -0.05281 0.06926  -0.02521 163 ILE B CG2   
3918 C CD1   . ILE C 164 ? 0.27825 0.16007 0.24347 -0.02469 0.04102  -0.01052 163 ILE B CD1   
3919 N N     . ARG C 165 ? 0.38612 0.20737 0.31851 -0.07307 0.07052  -0.05100 164 ARG B N     
3920 C CA    . ARG C 165 ? 0.44938 0.26577 0.38011 -0.09534 0.07822  -0.06630 164 ARG B CA    
3921 C C     . ARG C 165 ? 0.53987 0.32293 0.44804 -0.09424 0.09099  -0.06675 164 ARG B C     
3922 O O     . ARG C 165 ? 0.51472 0.28513 0.41524 -0.10447 0.10238  -0.07018 164 ARG B O     
3923 C CB    . ARG C 165 ? 0.43478 0.28898 0.38116 -0.10287 0.06453  -0.07673 164 ARG B CB    
3924 C CG    . ARG C 165 ? 0.48208 0.37686 0.45272 -0.10750 0.05393  -0.07894 164 ARG B CG    
3925 C CD    . ARG C 165 ? 0.48600 0.41856 0.46997 -0.11206 0.03953  -0.08809 164 ARG B CD    
3926 N NE    . ARG C 165 ? 0.47816 0.44839 0.48547 -0.11344 0.03049  -0.08927 164 ARG B NE    
3927 C CZ    . ARG C 165 ? 0.47938 0.48650 0.50065 -0.10892 0.01497  -0.09128 164 ARG B CZ    
3928 N NH1   . ARG C 165 ? 0.46528 0.47762 0.47873 -0.10389 0.00615  -0.09211 164 ARG B NH1   
3929 N NH2   . ARG C 165 ? 0.51675 0.55531 0.55878 -0.10853 0.00877  -0.09231 164 ARG B NH2   
3930 N N     . LYS C 166 ? 0.48348 0.25245 0.38047 -0.08210 0.09012  -0.06402 165 LYS B N     
3931 C CA    . LYS C 166 ? 0.56639 0.30301 0.44180 -0.07784 0.10254  -0.06313 165 LYS B CA    
3932 C C     . LYS C 166 ? 0.51832 0.22774 0.37953 -0.06991 0.11418  -0.05246 165 LYS B C     
3933 O O     . LYS C 166 ? 0.61754 0.30377 0.46332 -0.07707 0.12732  -0.05521 165 LYS B O     
3934 C CB    . LYS C 166 ? 0.53014 0.25909 0.39838 -0.06019 0.09940  -0.05839 165 LYS B CB    
3935 C CG    . LYS C 166 ? 0.61357 0.36353 0.48881 -0.06528 0.08962  -0.06804 165 LYS B CG    
3936 C CD    . LYS C 166 ? 0.62895 0.36961 0.49572 -0.04602 0.08940  -0.06236 165 LYS B CD    
3937 C CE    . LYS C 166 ? 0.61359 0.32262 0.46204 -0.03576 0.10267  -0.05738 165 LYS B CE    
3938 N NZ    . LYS C 166 ? 0.74851 0.45386 0.59018 -0.02061 0.10330  -0.05638 165 LYS B NZ    
3939 N N     . HIS C 167 ? 0.56516 0.27651 0.42925 -0.05455 0.10972  -0.04016 166 HIS B N     
3940 C CA    . HIS C 167 ? 0.53820 0.22550 0.38601 -0.04326 0.11889  -0.02871 166 HIS B CA    
3941 C C     . HIS C 167 ? 0.58661 0.26749 0.43100 -0.05984 0.12854  -0.03292 166 HIS B C     
3942 O O     . HIS C 167 ? 0.62596 0.27752 0.44920 -0.05827 0.14181  -0.02973 166 HIS B O     
3943 C CB    . HIS C 167 ? 0.54964 0.24830 0.40380 -0.02483 0.10975  -0.01602 166 HIS B CB    
3944 C CG    . HIS C 167 ? 0.62143 0.30099 0.45871 -0.01123 0.11640  -0.00396 166 HIS B CG    
3945 N ND1   . HIS C 167 ? 0.72134 0.40125 0.55805 -0.01665 0.11908  -0.00075 166 HIS B ND1   
3946 C CD2   . HIS C 167 ? 0.69244 0.35360 0.51210 0.00814  0.12065  0.00521  166 HIS B CD2   
3947 C CE1   . HIS C 167 ? 0.70308 0.36398 0.52066 -0.00137 0.12450  0.00988  166 HIS B CE1   
3948 N NE2   . HIS C 167 ? 0.71506 0.36548 0.52263 0.01418  0.12507  0.01373  166 HIS B NE2   
3949 N N     . LYS C 168 ? 0.62117 0.32970 0.48565 -0.07572 0.12279  -0.04077 167 LYS B N     
3950 C CA    . LYS C 168 ? 0.58030 0.28775 0.44421 -0.09057 0.13195  -0.04499 167 LYS B CA    
3951 C C     . LYS C 168 ? 0.63418 0.33205 0.49045 -0.10876 0.14306  -0.05770 167 LYS B C     
3952 O O     . LYS C 168 ? 0.63093 0.31118 0.47468 -0.11744 0.15664  -0.05935 167 LYS B O     
3953 C CB    . LYS C 168 ? 0.56172 0.30676 0.45213 -0.10039 0.12211  -0.04973 167 LYS B CB    
3954 C CG    . LYS C 168 ? 0.49853 0.25102 0.39505 -0.08624 0.11449  -0.03775 167 LYS B CG    
3955 C CD    . LYS C 168 ? 0.45725 0.24778 0.38086 -0.09611 0.10513  -0.04361 167 LYS B CD    
3956 C CE    . LYS C 168 ? 0.52991 0.32799 0.45798 -0.11148 0.11423  -0.05022 167 LYS B CE    
3957 N NZ    . LYS C 168 ? 0.52469 0.36404 0.48133 -0.11763 0.10449  -0.05518 167 LYS B NZ    
3958 N N     . GLU C 169 ? 0.62149 0.33091 0.48405 -0.11561 0.13806  -0.06745 168 GLU B N     
3959 C CA    . GLU C 169 ? 0.70661 0.41419 0.56527 -0.13542 0.14713  -0.08137 168 GLU B CA    
3960 C C     . GLU C 169 ? 0.75032 0.42275 0.58473 -0.13203 0.15789  -0.08177 168 GLU B C     
3961 O O     . GLU C 169 ? 0.73513 0.40506 0.56507 -0.14854 0.16508  -0.09414 168 GLU B O     
3962 C CB    . GLU C 169 ? 0.64478 0.39654 0.52883 -0.14969 0.13444  -0.09479 168 GLU B CB    
3963 C CG    . GLU C 169 ? 0.69843 0.46168 0.58649 -0.14436 0.12273  -0.09783 168 GLU B CG    
3964 C CD    . GLU C 169 ? 0.73100 0.53883 0.64115 -0.15799 0.11026  -0.11111 168 GLU B CD    
3965 O OE1   . GLU C 169 ? 0.71225 0.55188 0.64238 -0.15348 0.09612  -0.10915 168 GLU B OE1   
3966 O OE2   . GLU C 169 ? 0.70875 0.52028 0.61556 -0.17268 0.11477  -0.12339 168 GLU B OE2   
3967 N N     . LYS C 170 ? 0.65579 0.30189 0.47427 -0.11083 0.15979  -0.06878 169 LYS B N     
3968 C CA    . LYS C 170 ? 0.82054 0.43175 0.61508 -0.10491 0.17105  -0.06799 169 LYS B CA    
3969 C C     . LYS C 170 ? 0.87505 0.45229 0.64654 -0.11416 0.19076  -0.06936 169 LYS B C     
3970 O O     . LYS C 170 ? 0.80567 0.37775 0.57378 -0.11426 0.19555  -0.06408 169 LYS B O     
3971 C CB    . LYS C 170 ? 0.77550 0.37297 0.56128 -0.07751 0.16715  -0.05348 169 LYS B CB    
3972 C CG    . LYS C 170 ? 0.82254 0.40666 0.59886 -0.06201 0.17002  -0.03910 169 LYS B CG    
3973 C CD    . LYS C 170 ? 0.82520 0.41287 0.60225 -0.03544 0.16074  -0.02631 169 LYS B CD    
3974 C CE    . LYS C 170 ? 0.77766 0.33519 0.53249 -0.02020 0.16987  -0.02156 169 LYS B CE    
3975 N NZ    . LYS C 170 ? 0.88177 0.45538 0.64641 -0.00309 0.15905  -0.01825 169 LYS B NZ    
3976 O OXT   . LYS C 170 ? 0.86573 0.41899 0.62027 -0.12254 0.20310  -0.07635 169 LYS B OXT   
3998 N N     . ASN D 4   ? 0.39375 0.39085 0.35704 -0.04326 -0.14958 -0.01421 3   ASN C N     
3999 C CA    . ASN D 4   ? 0.36374 0.36181 0.32653 -0.04347 -0.13241 -0.00672 3   ASN C CA    
4000 C C     . ASN D 4   ? 0.41158 0.38410 0.36853 -0.04901 -0.13651 -0.00637 3   ASN C C     
4001 O O     . ASN D 4   ? 0.41385 0.36244 0.35135 -0.03770 -0.14145 -0.01459 3   ASN C O     
4002 C CB    . ASN D 4   ? 0.36438 0.36066 0.30962 -0.02569 -0.11912 -0.00842 3   ASN C CB    
4003 C CG    . ASN D 4   ? 0.33332 0.35353 0.28558 -0.02043 -0.11388 -0.00667 3   ASN C CG    
4004 O OD1   . ASN D 4   ? 0.36047 0.40337 0.33291 -0.02946 -0.11810 -0.00456 3   ASN C OD1   
4005 N ND2   . ASN D 4   ? 0.41714 0.43319 0.35364 -0.00594 -0.10469 -0.00706 3   ASN C ND2   
4006 N N     . PRO D 5   ? 0.34980 0.32674 0.32178 -0.06505 -0.13515 0.00273  4   PRO C N     
4007 C CA    . PRO D 5   ? 0.38035 0.33050 0.34599 -0.06954 -0.14049 0.00375  4   PRO C CA    
4008 C C     . PRO D 5   ? 0.33157 0.27208 0.28257 -0.05601 -0.12709 0.00242  4   PRO C C     
4009 O O     . PRO D 5   ? 0.32555 0.28224 0.27573 -0.04849 -0.11173 0.00455  4   PRO C O     
4010 C CB    . PRO D 5   ? 0.40786 0.37110 0.39322 -0.09050 -0.13981 0.01675  4   PRO C CB    
4011 C CG    . PRO D 5   ? 0.41512 0.41472 0.41283 -0.09077 -0.12499 0.02205  4   PRO C CG    
4012 C CD    . PRO D 5   ? 0.34904 0.35725 0.34289 -0.07818 -0.12757 0.01280  4   PRO C CD    
4013 N N     . THR D 6   ? 0.37192 0.28529 0.31249 -0.05307 -0.13421 -0.00142 5   THR C N     
4014 C CA    . THR D 6   ? 0.32535 0.23074 0.25529 -0.04158 -0.12321 -0.00284 5   THR C CA    
4015 C C     . THR D 6   ? 0.35954 0.25498 0.29617 -0.05279 -0.12554 0.00505  5   THR C C     
4016 O O     . THR D 6   ? 0.40955 0.28549 0.34783 -0.06226 -0.14147 0.00577  5   THR C O     
4017 C CB    . THR D 6   ? 0.36662 0.24989 0.27693 -0.02477 -0.13008 -0.01598 5   THR C CB    
4018 O OG1   . THR D 6   ? 0.44119 0.33187 0.34227 -0.01486 -0.13007 -0.02267 5   THR C OG1   
4019 C CG2   . THR D 6   ? 0.39471 0.27644 0.29710 -0.01255 -0.11719 -0.01754 5   THR C CG2   
4020 N N     . VAL D 7   ? 0.34717 0.25391 0.28675 -0.05169 -0.11111 0.01104  6   VAL C N     
4021 C CA    . VAL D 7   ? 0.33852 0.23503 0.28093 -0.05953 -0.11297 0.01823  6   VAL C CA    
4022 C C     . VAL D 7   ? 0.35702 0.24695 0.29079 -0.04496 -0.10492 0.01318  6   VAL C C     
4023 O O     . VAL D 7   ? 0.36194 0.26168 0.29086 -0.03213 -0.09420 0.00729  6   VAL C O     
4024 C CB    . VAL D 7   ? 0.35586 0.27468 0.31187 -0.07480 -0.10532 0.03153  6   VAL C CB    
4025 C CG1   . VAL D 7   ? 0.37952 0.30878 0.34718 -0.09052 -0.11343 0.03708  6   VAL C CG1   
4026 C CG2   . VAL D 7   ? 0.36215 0.30601 0.32105 -0.06744 -0.08763 0.03174  6   VAL C CG2   
4027 N N     . PHE D 8   ? 0.35024 0.22342 0.28246 -0.04731 -0.11095 0.01603  7   PHE C N     
4028 C CA    . PHE D 8   ? 0.35571 0.22426 0.28251 -0.03378 -0.10504 0.01087  7   PHE C CA    
4029 C C     . PHE D 8   ? 0.35132 0.22420 0.28383 -0.04103 -0.10085 0.02058  7   PHE C C     
4030 O O     . PHE D 8   ? 0.34612 0.21392 0.28194 -0.05569 -0.10783 0.03082  7   PHE C O     
4031 C CB    . PHE D 8   ? 0.37141 0.21147 0.28695 -0.02191 -0.11917 -0.00020 7   PHE C CB    
4032 C CG    . PHE D 8   ? 0.42947 0.24248 0.34399 -0.03092 -0.13649 0.00456  7   PHE C CG    
4033 C CD1   . PHE D 8   ? 0.52485 0.32034 0.43905 -0.04214 -0.15264 0.00634  7   PHE C CD1   
4034 C CD2   . PHE D 8   ? 0.43950 0.24319 0.35340 -0.02842 -0.13799 0.00761  7   PHE C CD2   
4035 C CE1   . PHE D 8   ? 0.49289 0.26048 0.40581 -0.05184 -0.16953 0.01235  7   PHE C CE1   
4036 C CE2   . PHE D 8   ? 0.51175 0.28743 0.42276 -0.03678 -0.15506 0.01352  7   PHE C CE2   
4037 C CZ    . PHE D 8   ? 0.53258 0.28930 0.44289 -0.04901 -0.17067 0.01648  7   PHE C CZ    
4038 N N     . PHE D 9   ? 0.30745 0.19024 0.24075 -0.03094 -0.08981 0.01760  8   PHE C N     
4039 C CA    . PHE D 9   ? 0.32626 0.20810 0.26189 -0.03256 -0.08880 0.02287  8   PHE C CA    
4040 C C     . PHE D 9   ? 0.36938 0.23788 0.30042 -0.01720 -0.09285 0.01313  8   PHE C C     
4041 O O     . PHE D 9   ? 0.34251 0.22070 0.27348 -0.00465 -0.08457 0.00420  8   PHE C O     
4042 C CB    . PHE D 9   ? 0.30465 0.21248 0.24787 -0.03238 -0.07277 0.02575  8   PHE C CB    
4043 C CG    . PHE D 9   ? 0.29081 0.21667 0.23953 -0.04487 -0.06714 0.03455  8   PHE C CG    
4044 C CD1   . PHE D 9   ? 0.32343 0.24610 0.27255 -0.05772 -0.07489 0.04150  8   PHE C CD1   
4045 C CD2   . PHE D 9   ? 0.29235 0.24013 0.24708 -0.04314 -0.05410 0.03509  8   PHE C CD2   
4046 C CE1   . PHE D 9   ? 0.27900 0.22415 0.23497 -0.06778 -0.06838 0.04863  8   PHE C CE1   
4047 C CE2   . PHE D 9   ? 0.27500 0.24186 0.23467 -0.05178 -0.04877 0.04113  8   PHE C CE2   
4048 C CZ    . PHE D 9   ? 0.28817 0.25566 0.24871 -0.06383 -0.05535 0.04794  8   PHE C CZ    
4049 N N     . ASP D 10  ? 0.35552 0.20447 0.28324 -0.01787 -0.10466 0.01557  9   ASP C N     
4050 C CA    . ASP D 10  ? 0.36552 0.20724 0.29190 -0.00245 -0.10758 0.00679  9   ASP C CA    
4051 C C     . ASP D 10  ? 0.34003 0.19803 0.27370 -0.00392 -0.09897 0.01219  9   ASP C C     
4052 O O     . ASP D 10  ? 0.36541 0.21808 0.29748 -0.01455 -0.10371 0.02277  9   ASP C O     
4053 C CB    . ASP D 10  ? 0.37287 0.18058 0.29045 0.00038  -0.12810 0.00469  9   ASP C CB    
4054 C CG    . ASP D 10  ? 0.45824 0.24862 0.36798 0.00755  -0.13818 -0.00598 9   ASP C CG    
4055 O OD1   . ASP D 10  ? 0.50284 0.30850 0.41227 0.01908  -0.12854 -0.01618 9   ASP C OD1   
4056 O OD2   . ASP D 10  ? 0.50909 0.26990 0.41217 0.00156  -0.15635 -0.00396 9   ASP C OD2   
4057 N N     . ILE D 11  ? 0.33729 0.21598 0.27865 0.00563  -0.08641 0.00568  10  ILE C N     
4058 C CA    . ILE D 11  ? 0.31715 0.21365 0.26720 0.00391  -0.07791 0.00927  10  ILE C CA    
4059 C C     . ILE D 11  ? 0.30979 0.19927 0.26177 0.01457  -0.08564 0.00420  10  ILE C C     
4060 O O     . ILE D 11  ? 0.35481 0.23863 0.30660 0.02804  -0.08983 -0.00599 10  ILE C O     
4061 C CB    . ILE D 11  ? 0.28264 0.20431 0.24203 0.00698  -0.06134 0.00554  10  ILE C CB    
4062 C CG1   . ILE D 11  ? 0.31565 0.24264 0.27217 -0.00106 -0.05544 0.00948  10  ILE C CG1   
4063 C CG2   . ILE D 11  ? 0.30383 0.24235 0.27310 0.00442  -0.05414 0.00823  10  ILE C CG2   
4064 C CD1   . ILE D 11  ? 0.28979 0.22273 0.24699 -0.01419 -0.05417 0.01927  10  ILE C CD1   
4065 N N     . ALA D 12  ? 0.30630 0.19794 0.25981 0.00995  -0.08781 0.01051  11  ALA C N     
4066 C CA    . ALA D 12  ? 0.30034 0.18605 0.25596 0.02013  -0.09659 0.00624  11  ALA C CA    
4067 C C     . ALA D 12  ? 0.29081 0.19988 0.25793 0.02023  -0.08788 0.00602  11  ALA C C     
4068 O O     . ALA D 12  ? 0.27996 0.20174 0.24824 0.01008  -0.07947 0.01228  11  ALA C O     
4069 C CB    . ALA D 12  ? 0.34411 0.20184 0.28638 0.01497  -0.11348 0.01488  11  ALA C CB    
4070 N N     . VAL D 13  ? 0.29563 0.21132 0.27231 0.03265  -0.09068 -0.00249 12  VAL C N     
4071 C CA    . VAL D 13  ? 0.30811 0.24434 0.29768 0.03375  -0.08591 -0.00434 12  VAL C CA    
4072 C C     . VAL D 13  ? 0.32488 0.24789 0.30997 0.04019  -0.10148 -0.00415 12  VAL C C     
4073 O O     . VAL D 13  ? 0.33783 0.25236 0.32471 0.05329  -0.11077 -0.01180 12  VAL C O     
4074 C CB    . VAL D 13  ? 0.30036 0.26108 0.30911 0.04229  -0.07515 -0.01460 12  VAL C CB    
4075 C CG1   . VAL D 13  ? 0.30343 0.28453 0.32800 0.04171  -0.07222 -0.01662 12  VAL C CG1   
4076 C CG2   . VAL D 13  ? 0.32192 0.29183 0.33167 0.03715  -0.06117 -0.01380 12  VAL C CG2   
4077 N N     . ASP D 14  ? 0.32488 0.24596 0.30259 0.03226  -0.10500 0.00424  13  ASP C N     
4078 C CA    . ASP D 14  ? 0.34870 0.25250 0.31585 0.03621  -0.12120 0.00812  13  ASP C CA    
4079 C C     . ASP D 14  ? 0.42277 0.29453 0.37624 0.04030  -0.13590 0.01050  13  ASP C C     
4080 O O     . ASP D 14  ? 0.43023 0.28799 0.38210 0.05244  -0.15019 0.00605  13  ASP C O     
4081 C CB    . ASP D 14  ? 0.41628 0.33586 0.39850 0.04800  -0.12488 -0.00150 13  ASP C CB    
4082 C CG    . ASP D 14  ? 0.40908 0.35281 0.40054 0.04175  -0.11572 -0.00173 13  ASP C CG    
4083 O OD1   . ASP D 14  ? 0.44835 0.39296 0.42954 0.02979  -0.10947 0.00668  13  ASP C OD1   
4084 O OD2   . ASP D 14  ? 0.48404 0.44664 0.49392 0.04916  -0.11554 -0.01105 13  ASP C OD2   
4085 N N     . GLY D 15  ? 0.37550 0.23434 0.31917 0.03002  -0.13384 0.01739  14  GLY C N     
4086 C CA    . GLY D 15  ? 0.40922 0.23540 0.34006 0.03096  -0.14841 0.02024  14  GLY C CA    
4087 C C     . GLY D 15  ? 0.44479 0.26578 0.38191 0.04534  -0.15091 0.00598  14  GLY C C     
4088 O O     . GLY D 15  ? 0.48655 0.27869 0.41275 0.04590  -0.16336 0.00668  14  GLY C O     
4089 N N     . GLU D 16  ? 0.34557 0.19409 0.29971 0.05667  -0.13966 -0.00685 15  GLU C N     
4090 C CA    . GLU D 16  ? 0.39584 0.24164 0.35365 0.07216  -0.14196 -0.02070 15  GLU C CA    
4091 C C     . GLU D 16  ? 0.36382 0.22128 0.32288 0.06685  -0.12778 -0.02248 15  GLU C C     
4092 O O     . GLU D 16  ? 0.33309 0.21296 0.29914 0.05661  -0.11226 -0.01770 15  GLU C O     
4093 C CB    . GLU D 16  ? 0.39050 0.26209 0.36649 0.08910  -0.13799 -0.03404 15  GLU C CB    
4094 C CG    . GLU D 16  ? 0.39931 0.26439 0.37718 0.09771  -0.15229 -0.03501 15  GLU C CG    
4095 C CD    . GLU D 16  ? 0.45404 0.28237 0.41567 0.10464  -0.17228 -0.03677 15  GLU C CD    
4096 O OE1   . GLU D 16  ? 0.49832 0.31557 0.45473 0.11149  -0.17520 -0.04529 15  GLU C OE1   
4097 O OE2   . GLU D 16  ? 0.56963 0.38249 0.52226 0.09969  -0.18222 -0.03010 15  GLU C OE2   
4098 N N     . PRO D 17  ? 0.42127 0.26297 0.37289 0.07521  -0.13413 -0.03032 16  PRO C N     
4099 C CA    . PRO D 17  ? 0.44373 0.29220 0.39259 0.07024  -0.12352 -0.03138 16  PRO C CA    
4100 C C     . PRO D 17  ? 0.41779 0.30317 0.38089 0.07523  -0.10359 -0.03748 16  PRO C C     
4101 O O     . PRO D 17  ? 0.44494 0.34646 0.41779 0.09049  -0.10092 -0.04833 16  PRO C O     
4102 C CB    . PRO D 17  ? 0.47717 0.29956 0.41455 0.08287  -0.13824 -0.04184 16  PRO C CB    
4103 C CG    . PRO D 17  ? 0.57047 0.36264 0.50089 0.08586  -0.15870 -0.03952 16  PRO C CG    
4104 C CD    . PRO D 17  ? 0.49780 0.31030 0.44058 0.08972  -0.15409 -0.03853 16  PRO C CD    
4105 N N     . LEU D 18  ? 0.35046 0.25005 0.31556 0.06192  -0.08983 -0.02977 17  LEU C N     
4106 C CA    . LEU D 18  ? 0.33660 0.26618 0.31239 0.06416  -0.07160 -0.03310 17  LEU C CA    
4107 C C     . LEU D 18  ? 0.36805 0.29574 0.33384 0.06821  -0.06754 -0.03769 17  LEU C C     
4108 O O     . LEU D 18  ? 0.38575 0.32971 0.35461 0.08069  -0.06007 -0.04663 17  LEU C O     
4109 C CB    . LEU D 18  ? 0.31804 0.26278 0.30152 0.04921  -0.06029 -0.02289 17  LEU C CB    
4110 C CG    . LEU D 18  ? 0.33281 0.30538 0.32829 0.04888  -0.04266 -0.02380 17  LEU C CG    
4111 C CD1   . LEU D 18  ? 0.41232 0.40591 0.42506 0.05857  -0.03903 -0.03080 17  LEU C CD1   
4112 C CD2   . LEU D 18  ? 0.30976 0.28815 0.30870 0.03473  -0.03617 -0.01452 17  LEU C CD2   
4113 N N     . GLY D 19  ? 0.35716 0.26631 0.31080 0.05853  -0.07321 -0.03209 18  GLY C N     
4114 C CA    . GLY D 19  ? 0.36118 0.26677 0.30399 0.06192  -0.07164 -0.03655 18  GLY C CA    
4115 C C     . GLY D 19  ? 0.36307 0.25721 0.29924 0.04624  -0.07462 -0.02708 18  GLY C C     
4116 O O     . GLY D 19  ? 0.36813 0.26113 0.30851 0.03288  -0.07528 -0.01679 18  GLY C O     
4117 N N     . ARG D 20  ? 0.35039 0.23881 0.27615 0.04884  -0.07618 -0.03131 19  ARG C N     
4118 C CA    . ARG D 20  ? 0.34895 0.22818 0.26971 0.03532  -0.08059 -0.02417 19  ARG C CA    
4119 C C     . ARG D 20  ? 0.35187 0.25262 0.27484 0.03113  -0.06532 -0.02001 19  ARG C C     
4120 O O     . ARG D 20  ? 0.35217 0.26598 0.27223 0.04128  -0.05558 -0.02544 19  ARG C O     
4121 C CB    . ARG D 20  ? 0.41213 0.26733 0.31967 0.04057  -0.09632 -0.03230 19  ARG C CB    
4122 C CG    . ARG D 20  ? 0.38416 0.23281 0.28841 0.02708  -0.10165 -0.02645 19  ARG C CG    
4123 C CD    . ARG D 20  ? 0.45187 0.27158 0.34522 0.02948  -0.12178 -0.03398 19  ARG C CD    
4124 N NE    . ARG D 20  ? 0.45033 0.24451 0.34442 0.02434  -0.13768 -0.03083 19  ARG C NE    
4125 C CZ    . ARG D 20  ? 0.54472 0.30865 0.43244 0.02013  -0.15808 -0.03292 19  ARG C CZ    
4126 N NH1   . ARG D 20  ? 0.57014 0.32590 0.45059 0.02169  -0.16611 -0.04030 19  ARG C NH1   
4127 N NH2   . ARG D 20  ? 0.54421 0.28406 0.43238 0.01412  -0.17195 -0.02728 19  ARG C NH2   
4128 N N     . VAL D 21  ? 0.31395 0.21877 0.24149 0.01663  -0.06351 -0.01005 20  VAL C N     
4129 C CA    . VAL D 21  ? 0.30571 0.22620 0.23418 0.01263  -0.05290 -0.00619 20  VAL C CA    
4130 C C     . VAL D 21  ? 0.31380 0.22461 0.23742 0.00440  -0.06295 -0.00413 20  VAL C C     
4131 O O     . VAL D 21  ? 0.34114 0.24370 0.26840 -0.00690 -0.07172 0.00175  20  VAL C O     
4132 C CB    . VAL D 21  ? 0.27507 0.21242 0.21524 0.00447  -0.04220 0.00203  20  VAL C CB    
4133 C CG1   . VAL D 21  ? 0.30083 0.25120 0.24131 0.00227  -0.03312 0.00515  20  VAL C CG1   
4134 C CG2   . VAL D 21  ? 0.29323 0.24001 0.24117 0.01063  -0.03443 0.00004  20  VAL C CG2   
4135 N N     . SER D 22  ? 0.33700 0.24978 0.25261 0.00942  -0.06209 -0.00829 21  SER C N     
4136 C CA    . SER D 22  ? 0.34141 0.24862 0.25483 0.00163  -0.07180 -0.00698 21  SER C CA    
4137 C C     . SER D 22  ? 0.33559 0.26187 0.25289 -0.00174 -0.06177 -0.00187 21  SER C C     
4138 O O     . SER D 22  ? 0.32623 0.26380 0.24201 0.00521  -0.04939 -0.00168 21  SER C O     
4139 C CB    . SER D 22  ? 0.37619 0.26721 0.27564 0.01119  -0.08337 -0.01765 21  SER C CB    
4140 O OG    . SER D 22  ? 0.41258 0.31297 0.30156 0.02413  -0.07426 -0.02305 21  SER C OG    
4141 N N     . PHE D 23  ? 0.31594 0.24627 0.23947 -0.01285 -0.06762 0.00279  22  PHE C N     
4142 C CA    . PHE D 23  ? 0.26812 0.21715 0.19719 -0.01557 -0.06018 0.00709  22  PHE C CA    
4143 C C     . PHE D 23  ? 0.30927 0.25765 0.23646 -0.01818 -0.07075 0.00462  22  PHE C C     
4144 O O     . PHE D 23  ? 0.33130 0.27030 0.26160 -0.02672 -0.08355 0.00448  22  PHE C O     
4145 C CB    . PHE D 23  ? 0.29805 0.26088 0.24123 -0.02750 -0.05643 0.01550  22  PHE C CB    
4146 C CG    . PHE D 23  ? 0.27838 0.24181 0.22476 -0.02697 -0.04898 0.01807  22  PHE C CG    
4147 C CD1   . PHE D 23  ? 0.26994 0.24403 0.21852 -0.02124 -0.03681 0.01844  22  PHE C CD1   
4148 C CD2   . PHE D 23  ? 0.29734 0.24926 0.24458 -0.03251 -0.05566 0.02034  22  PHE C CD2   
4149 C CE1   . PHE D 23  ? 0.26105 0.23674 0.21416 -0.02108 -0.03126 0.01997  22  PHE C CE1   
4150 C CE2   . PHE D 23  ? 0.30854 0.26193 0.25862 -0.03117 -0.04992 0.02226  22  PHE C CE2   
4151 C CZ    . PHE D 23  ? 0.28503 0.25133 0.23869 -0.02544 -0.03780 0.02145  22  PHE C CZ    
4152 N N     . GLU D 24  ? 0.29363 0.25113 0.21607 -0.01131 -0.06651 0.00312  23  GLU C N     
4153 C CA    . GLU D 24  ? 0.29229 0.25597 0.21706 -0.01441 -0.07552 0.00182  23  GLU C CA    
4154 C C     . GLU D 24  ? 0.27356 0.25937 0.21527 -0.02350 -0.07075 0.00878  23  GLU C C     
4155 O O     . GLU D 24  ? 0.28867 0.28477 0.23308 -0.02006 -0.05901 0.01206  23  GLU C O     
4156 C CB    . GLU D 24  ? 0.32848 0.29189 0.23835 -0.00105 -0.07351 -0.00261 23  GLU C CB    
4157 C CG    . GLU D 24  ? 0.33844 0.31017 0.25103 -0.00248 -0.08353 -0.00456 23  GLU C CG    
4158 C CD    . GLU D 24  ? 0.46883 0.43909 0.36398 0.01143  -0.08234 -0.00783 23  GLU C CD    
4159 O OE1   . GLU D 24  ? 0.47881 0.44179 0.35902 0.02125  -0.07312 -0.00788 23  GLU C OE1   
4160 O OE2   . GLU D 24  ? 0.43751 0.41521 0.33427 0.01215  -0.09087 -0.00978 23  GLU C OE2   
4161 N N     . LEU D 25  ? 0.28369 0.27756 0.23751 -0.03522 -0.08009 0.01080  24  LEU C N     
4162 C CA    . LEU D 25  ? 0.25192 0.27181 0.22284 -0.04354 -0.07550 0.01674  24  LEU C CA    
4163 C C     . LEU D 25  ? 0.26580 0.30014 0.24115 -0.04038 -0.08119 0.01333  24  LEU C C     
4164 O O     . LEU D 25  ? 0.29093 0.31916 0.26583 -0.04333 -0.09431 0.00946  24  LEU C O     
4165 C CB    . LEU D 25  ? 0.26973 0.29350 0.25322 -0.06067 -0.08083 0.02340  24  LEU C CB    
4166 C CG    . LEU D 25  ? 0.26926 0.27601 0.24732 -0.06384 -0.07832 0.02706  24  LEU C CG    
4167 C CD1   . LEU D 25  ? 0.34154 0.35231 0.33073 -0.08202 -0.08413 0.03617  24  LEU C CD1   
4168 C CD2   . LEU D 25  ? 0.24960 0.26356 0.22552 -0.05629 -0.06384 0.02833  24  LEU C CD2   
4169 N N     . PHE D 26  ? 0.25078 0.30345 0.23076 -0.03390 -0.07297 0.01403  25  PHE C N     
4170 C CA    . PHE D 26  ? 0.24430 0.30824 0.22544 -0.02651 -0.07839 0.00989  25  PHE C CA    
4171 C C     . PHE D 26  ? 0.26160 0.35321 0.26476 -0.03756 -0.08492 0.01125  25  PHE C C     
4172 O O     . PHE D 26  ? 0.25745 0.37465 0.27283 -0.03490 -0.08059 0.01159  25  PHE C O     
4173 C CB    . PHE D 26  ? 0.28351 0.35143 0.25925 -0.01364 -0.06838 0.00992  25  PHE C CB    
4174 C CG    . PHE D 26  ? 0.28026 0.32428 0.23639 -0.00439 -0.06173 0.00997  25  PHE C CG    
4175 C CD1   . PHE D 26  ? 0.39140 0.41572 0.33089 -0.00004 -0.06715 0.00663  25  PHE C CD1   
4176 C CD2   . PHE D 26  ? 0.27961 0.32267 0.23457 0.00009  -0.05039 0.01293  25  PHE C CD2   
4177 C CE1   . PHE D 26  ? 0.40235 0.41030 0.32508 0.00840  -0.05930 0.00730  25  PHE C CE1   
4178 C CE2   . PHE D 26  ? 0.33507 0.35974 0.27497 0.00682  -0.04378 0.01414  25  PHE C CE2   
4179 C CZ    . PHE D 26  ? 0.33804 0.34728 0.26258 0.01057  -0.04726 0.01187  25  PHE C CZ    
4180 N N     . ALA D 27  ? 0.26389 0.35064 0.27300 -0.05031 -0.09602 0.01189  26  ALA C N     
4181 C CA    . ALA D 27  ? 0.26456 0.37930 0.29702 -0.06365 -0.10278 0.01443  26  ALA C CA    
4182 C C     . ALA D 27  ? 0.30686 0.43889 0.34514 -0.05493 -0.11003 0.00795  26  ALA C C     
4183 O O     . ALA D 27  ? 0.29695 0.46167 0.35767 -0.06227 -0.11235 0.00929  26  ALA C O     
4184 C CB    . ALA D 27  ? 0.32728 0.42838 0.36467 -0.08040 -0.11539 0.01711  26  ALA C CB    
4185 N N     . ASP D 28  ? 0.29406 0.40693 0.31253 -0.03891 -0.11348 0.00128  27  ASP C N     
4186 C CA    . ASP D 28  ? 0.31205 0.43993 0.33389 -0.02896 -0.12137 -0.00457 27  ASP C CA    
4187 C C     . ASP D 28  ? 0.34230 0.49445 0.37252 -0.01941 -0.11140 -0.00373 27  ASP C C     
4188 O O     . ASP D 28  ? 0.43999 0.61536 0.48243 -0.01427 -0.11808 -0.00775 27  ASP C O     
4189 C CB    . ASP D 28  ? 0.41683 0.51693 0.41245 -0.01487 -0.12937 -0.01112 27  ASP C CB    
4190 C CG    . ASP D 28  ? 0.43681 0.51267 0.40796 -0.00319 -0.11696 -0.00909 27  ASP C CG    
4191 O OD1   . ASP D 28  ? 0.42069 0.50014 0.39576 -0.00482 -0.10320 -0.00359 27  ASP C OD1   
4192 O OD2   . ASP D 28  ? 0.43295 0.48716 0.38084 0.00738  -0.12138 -0.01315 27  ASP C OD2   
4193 N N     . LYS D 29  ? 0.28263 0.43047 0.30772 -0.01651 -0.09710 0.00040  28  LYS C N     
4194 C CA    . LYS D 29  ? 0.25927 0.42426 0.28941 -0.00567 -0.08858 -0.00020 28  LYS C CA    
4195 C C     . LYS D 29  ? 0.24918 0.44270 0.29900 -0.01510 -0.07926 0.00353  28  LYS C C     
4196 O O     . LYS D 29  ? 0.23252 0.45556 0.29664 -0.00908 -0.07709 0.00070  28  LYS C O     
4197 C CB    . LYS D 29  ? 0.33715 0.47369 0.34459 0.00676  -0.08036 0.00080  28  LYS C CB    
4198 C CG    . LYS D 29  ? 0.44722 0.55984 0.43254 0.01927  -0.08745 -0.00176 28  LYS C CG    
4199 C CD    . LYS D 29  ? 0.36965 0.49941 0.36129 0.02985  -0.09682 -0.00650 28  LYS C CD    
4200 C CE    . LYS D 29  ? 0.51970 0.62990 0.48987 0.04100  -0.10722 -0.00909 28  LYS C CE    
4201 N NZ    . LYS D 29  ? 0.50816 0.63895 0.48836 0.05041  -0.11832 -0.01424 28  LYS C NZ    
4202 N N     . VAL D 30  ? 0.26662 0.45203 0.31587 -0.02828 -0.07386 0.00950  29  VAL C N     
4203 C CA    . VAL D 30  ? 0.20855 0.41929 0.27224 -0.03767 -0.06450 0.01441  29  VAL C CA    
4204 C C     . VAL D 30  ? 0.20479 0.41645 0.27673 -0.05838 -0.06866 0.02166  29  VAL C C     
4205 O O     . VAL D 30  ? 0.23076 0.42452 0.29410 -0.06544 -0.06397 0.02714  29  VAL C O     
4206 C CB    . VAL D 30  ? 0.27213 0.46838 0.32331 -0.03118 -0.05265 0.01565  29  VAL C CB    
4207 C CG1   . VAL D 30  ? 0.24294 0.44967 0.29407 -0.01410 -0.04817 0.00958  29  VAL C CG1   
4208 C CG2   . VAL D 30  ? 0.28019 0.43656 0.31068 -0.02847 -0.05345 0.01621  29  VAL C CG2   
4209 N N     . PRO D 31  ? 0.19245 0.42454 0.28194 -0.06899 -0.07821 0.02231  30  PRO C N     
4210 C CA    . PRO D 31  ? 0.21577 0.44198 0.31226 -0.09021 -0.08493 0.03007  30  PRO C CA    
4211 C C     . PRO D 31  ? 0.23050 0.46660 0.33150 -0.10190 -0.07298 0.04001  30  PRO C C     
4212 O O     . PRO D 31  ? 0.23637 0.44831 0.33001 -0.11350 -0.07542 0.04681  30  PRO C O     
4213 C CB    . PRO D 31  ? 0.23422 0.47567 0.34793 -0.09433 -0.09388 0.02664  30  PRO C CB    
4214 C CG    . PRO D 31  ? 0.27839 0.55073 0.40143 -0.07927 -0.08982 0.01982  30  PRO C CG    
4215 C CD    . PRO D 31  ? 0.19989 0.45573 0.30240 -0.06177 -0.08617 0.01550  30  PRO C CD    
4216 N N     . LYS D 32  ? 0.20240 0.47187 0.31308 -0.09767 -0.06097 0.04056  31  LYS C N     
4217 C CA    . LYS D 32  ? 0.19520 0.47527 0.30618 -0.10742 -0.04980 0.05011  31  LYS C CA    
4218 C C     . LYS D 32  ? 0.20048 0.45883 0.29440 -0.10546 -0.04489 0.05295  31  LYS C C     
4219 O O     . LYS D 32  ? 0.23814 0.48318 0.32538 -0.11692 -0.04310 0.06225  31  LYS C O     
4220 C CB    . LYS D 32  ? 0.21209 0.53276 0.33404 -0.10009 -0.03889 0.04759  31  LYS C CB    
4221 C CG    . LYS D 32  ? 0.31066 0.64803 0.43256 -0.11045 -0.02875 0.05757  31  LYS C CG    
4222 C CD    . LYS D 32  ? 0.34669 0.72574 0.47903 -0.10130 -0.01967 0.05275  31  LYS C CD    
4223 C CE    . LYS D 32  ? 0.30950 0.70572 0.43523 -0.10560 -0.00853 0.06013  31  LYS C CE    
4224 N NZ    . LYS D 32  ? 0.39661 0.82898 0.52710 -0.09036 -0.00005 0.05122  31  LYS C NZ    
4225 N N     . THR D 33  ? 0.17853 0.42848 0.26320 -0.08934 -0.04299 0.04479  32  THR C N     
4226 C CA    . THR D 33  ? 0.19609 0.41859 0.26243 -0.08369 -0.03690 0.04533  32  THR C CA    
4227 C C     . THR D 33  ? 0.21850 0.39997 0.27178 -0.08893 -0.04526 0.04746  32  THR C C     
4228 O O     . THR D 33  ? 0.22253 0.38745 0.26713 -0.09466 -0.04322 0.05311  32  THR C O     
4229 C CB    . THR D 33  ? 0.17513 0.39264 0.23318 -0.06300 -0.03163 0.03544  32  THR C CB    
4230 O OG1   . THR D 33  ? 0.22020 0.47591 0.29121 -0.05636 -0.02638 0.03153  32  THR C OG1   
4231 C CG2   . THR D 33  ? 0.18496 0.38029 0.22810 -0.05782 -0.02487 0.03564  32  THR C CG2   
4232 N N     . ALA D 34  ? 0.20398 0.36941 0.25513 -0.08599 -0.05562 0.04227  33  ALA C N     
4233 C CA    . ALA D 34  ? 0.23391 0.36219 0.27239 -0.08909 -0.06474 0.04222  33  ALA C CA    
4234 C C     . ALA D 34  ? 0.25731 0.38166 0.30218 -0.10911 -0.07165 0.05201  33  ALA C C     
4235 O O     . ALA D 34  ? 0.23984 0.33600 0.27320 -0.11185 -0.07452 0.05475  33  ALA C O     
4236 C CB    . ALA D 34  ? 0.25114 0.36684 0.28519 -0.08124 -0.07524 0.03386  33  ALA C CB    
4237 N N     . GLU D 35  ? 0.27587 0.42803 0.33959 -0.12328 -0.07507 0.05767  34  GLU C N     
4238 C CA    . GLU D 35  ? 0.27014 0.41095 0.33581 -0.13859 -0.07883 0.06748  34  GLU C CA    
4239 C C     . GLU D 35  ? 0.28312 0.42339 0.34126 -0.14328 -0.06942 0.07730  34  GLU C C     
4240 O O     . GLU D 35  ? 0.28486 0.39850 0.33437 -0.15110 -0.07544 0.08405  34  GLU C O     
4241 C CB    . GLU D 35  ? 0.24687 0.41517 0.33076 -0.14692 -0.07910 0.07041  34  GLU C CB    
4242 C CG    . GLU D 35  ? 0.28873 0.45221 0.37533 -0.16368 -0.08104 0.08312  34  GLU C CG    
4243 C CD    . GLU D 35  ? 0.39727 0.51833 0.47528 -0.16990 -0.09654 0.08395  34  GLU C CD    
4244 O OE1   . GLU D 35  ? 0.36811 0.46817 0.44122 -0.16200 -0.10671 0.07323  34  GLU C OE1   
4245 O OE2   . GLU D 35  ? 0.45782 0.56651 0.53292 -0.18166 -0.09949 0.09490  34  GLU C OE2   
4246 N N     . ASN D 36  ? 0.23359 0.40173 0.29342 -0.13681 -0.05591 0.07725  35  ASN C N     
4247 C CA    . ASN D 36  ? 0.29569 0.46332 0.34573 -0.13854 -0.04764 0.08466  35  ASN C CA    
4248 C C     . ASN D 36  ? 0.27278 0.40427 0.30805 -0.13576 -0.05234 0.08371  35  ASN C C     
4249 O O     . ASN D 36  ? 0.28448 0.39569 0.31049 -0.14234 -0.05591 0.09146  35  ASN C O     
4250 C CB    . ASN D 36  ? 0.20766 0.40836 0.26050 -0.12781 -0.03403 0.08039  35  ASN C CB    
4251 C CG    . ASN D 36  ? 0.21624 0.41847 0.25790 -0.12773 -0.02624 0.08617  35  ASN C CG    
4252 O OD1   . ASN D 36  ? 0.27069 0.47673 0.31018 -0.13767 -0.02632 0.09594  35  ASN C OD1   
4253 N ND2   . ASN D 36  ? 0.23428 0.43528 0.26923 -0.11638 -0.02001 0.08012  35  ASN C ND2   
4254 N N     . PHE D 37  ? 0.26520 0.38381 0.29455 -0.12096 -0.05215 0.07247  36  PHE C N     
4255 C CA    . PHE D 37  ? 0.26985 0.35293 0.28321 -0.11266 -0.05464 0.06884  36  PHE C CA    
4256 C C     . PHE D 37  ? 0.26644 0.31776 0.27525 -0.12084 -0.06952 0.07096  36  PHE C C     
4257 O O     . PHE D 37  ? 0.27576 0.30314 0.27471 -0.12225 -0.07335 0.07435  36  PHE C O     
4258 C CB    . PHE D 37  ? 0.23086 0.30701 0.23777 -0.09362 -0.04999 0.05664  36  PHE C CB    
4259 C CG    . PHE D 37  ? 0.21008 0.26037 0.20389 -0.08421 -0.04851 0.05300  36  PHE C CG    
4260 C CD1   . PHE D 37  ? 0.23506 0.29186 0.22604 -0.07825 -0.03888 0.05285  36  PHE C CD1   
4261 C CD2   . PHE D 37  ? 0.27856 0.30024 0.26358 -0.07990 -0.05696 0.04827  36  PHE C CD2   
4262 C CE1   . PHE D 37  ? 0.23825 0.27464 0.22035 -0.06996 -0.03786 0.04912  36  PHE C CE1   
4263 C CE2   . PHE D 37  ? 0.25965 0.26278 0.23499 -0.07011 -0.05472 0.04411  36  PHE C CE2   
4264 C CZ    . PHE D 37  ? 0.26389 0.27498 0.23899 -0.06579 -0.04514 0.04491  36  PHE C CZ    
4265 N N     . ARG D 38  ? 0.28564 0.33573 0.30156 -0.12572 -0.07952 0.06835  37  ARG C N     
4266 C CA    . ARG D 38  ? 0.29854 0.31586 0.30968 -0.13237 -0.09605 0.06826  37  ARG C CA    
4267 C C     . ARG D 38  ? 0.31507 0.32380 0.32555 -0.14528 -0.09894 0.08117  37  ARG C C     
4268 O O     . ARG D 38  ? 0.33532 0.31189 0.33451 -0.14456 -0.10753 0.08220  37  ARG C O     
4269 C CB    . ARG D 38  ? 0.27629 0.29657 0.29549 -0.13397 -0.10600 0.06231  37  ARG C CB    
4270 C CG    . ARG D 38  ? 0.32931 0.31286 0.34101 -0.13494 -0.12242 0.05874  37  ARG C CG    
4271 C CD    . ARG D 38  ? 0.36005 0.35077 0.38284 -0.13968 -0.13076 0.05599  37  ARG C CD    
4272 N NE    . ARG D 38  ? 0.35081 0.36291 0.38833 -0.15534 -0.12675 0.06888  37  ARG C NE    
4273 C CZ    . ARG D 38  ? 0.42683 0.42343 0.46247 -0.16623 -0.13158 0.07947  37  ARG C CZ    
4274 N NH1   . ARG D 38  ? 0.41893 0.37664 0.44065 -0.16306 -0.14283 0.07781  37  ARG C NH1   
4275 N NH2   . ARG D 38  ? 0.38909 0.41055 0.43621 -0.17944 -0.12538 0.09178  37  ARG C NH2   
4276 N N     . ALA D 39  ? 0.30627 0.34441 0.32739 -0.15476 -0.09187 0.09038  38  ALA C N     
4277 C CA    . ALA D 39  ? 0.32335 0.35759 0.34252 -0.16638 -0.09416 0.10333  38  ALA C CA    
4278 C C     . ALA D 39  ? 0.30626 0.33201 0.31250 -0.16326 -0.08928 0.10814  38  ALA C C     
4279 O O     . ALA D 39  ? 0.36642 0.36950 0.36452 -0.16846 -0.09768 0.11509  38  ALA C O     
4280 C CB    . ALA D 39  ? 0.36107 0.43384 0.39442 -0.17573 -0.08618 0.11063  38  ALA C CB    
4281 N N     . LEU D 40  ? 0.28187 0.32569 0.28643 -0.15446 -0.07670 0.10422  39  LEU C N     
4282 C CA    . LEU D 40  ? 0.30966 0.34449 0.30216 -0.15032 -0.07292 0.10724  39  LEU C CA    
4283 C C     . LEU D 40  ? 0.38176 0.37623 0.36311 -0.14381 -0.08340 0.10198  39  LEU C C     
4284 O O     . LEU D 40  ? 0.33441 0.31191 0.30564 -0.14289 -0.08678 0.10607  39  LEU C O     
4285 C CB    . LEU D 40  ? 0.27726 0.33969 0.27102 -0.14148 -0.05791 0.10296  39  LEU C CB    
4286 C CG    . LEU D 40  ? 0.27202 0.37466 0.27409 -0.14462 -0.04743 0.10684  39  LEU C CG    
4287 C CD1   . LEU D 40  ? 0.28012 0.40463 0.28249 -0.13227 -0.03492 0.09900  39  LEU C CD1   
4288 C CD2   . LEU D 40  ? 0.31274 0.41897 0.30924 -0.15347 -0.04788 0.11839  39  LEU C CD2   
4289 N N     . SER D 41  ? 0.34811 0.32711 0.33091 -0.13843 -0.08983 0.09197  40  SER C N     
4290 C CA    . SER D 41  ? 0.34020 0.28227 0.31203 -0.12927 -0.09994 0.08417  40  SER C CA    
4291 C C     . SER D 41  ? 0.37899 0.29177 0.34591 -0.13418 -0.11631 0.08734  40  SER C C     
4292 O O     . SER D 41  ? 0.41152 0.29540 0.36783 -0.12740 -0.12477 0.08464  40  SER C O     
4293 C CB    . SER D 41  ? 0.32976 0.27077 0.30093 -0.11338 -0.09828 0.06859  40  SER C CB    
4294 O OG    . SER D 41  ? 0.33873 0.30360 0.31160 -0.10247 -0.08253 0.06391  40  SER C OG    
4295 N N     . THR D 42  ? 0.38608 0.30597 0.36108 -0.14454 -0.12144 0.09227  41  THR C N     
4296 C CA    . THR D 42  ? 0.40376 0.29624 0.37456 -0.15001 -0.13733 0.09656  41  THR C CA    
4297 C C     . THR D 42  ? 0.43621 0.33232 0.40413 -0.15996 -0.13678 0.11074  41  THR C C     
4298 O O     . THR D 42  ? 0.46119 0.32960 0.42177 -0.16183 -0.15031 0.11400  41  THR C O     
4299 C CB    . THR D 42  ? 0.43585 0.33191 0.41708 -0.15847 -0.14469 0.09686  41  THR C CB    
4300 O OG1   . THR D 42  ? 0.42711 0.35982 0.42098 -0.17085 -0.13402 0.10712  41  THR C OG1   
4301 C CG2   . THR D 42  ? 0.38900 0.28222 0.37196 -0.14803 -0.14667 0.08169  41  THR C CG2   
4302 N N     . GLY D 43  ? 0.39056 0.32056 0.36346 -0.16543 -0.12211 0.11831  42  GLY C N     
4303 C CA    . GLY D 43  ? 0.37784 0.31561 0.34798 -0.17555 -0.12085 0.13168  42  GLY C CA    
4304 C C     . GLY D 43  ? 0.50217 0.44653 0.48043 -0.19166 -0.12663 0.14269  42  GLY C C     
4305 O O     . GLY D 43  ? 0.46366 0.40648 0.43796 -0.20127 -0.12930 0.15457  42  GLY C O     
4306 N N     . GLU D 44  ? 0.41043 0.36265 0.40050 -0.19540 -0.12872 0.13932  43  GLU C N     
4307 C CA    . GLU D 44  ? 0.42383 0.37658 0.42283 -0.21105 -0.13717 0.14890  43  GLU C CA    
4308 C C     . GLU D 44  ? 0.42684 0.41658 0.43345 -0.22397 -0.12566 0.16238  43  GLU C C     
4309 O O     . GLU D 44  ? 0.48133 0.46995 0.49308 -0.23920 -0.13252 0.17402  43  GLU C O     
4310 C CB    . GLU D 44  ? 0.45596 0.40799 0.46634 -0.21033 -0.14266 0.13988  43  GLU C CB    
4311 C CG    . GLU D 44  ? 0.43625 0.42515 0.45799 -0.20550 -0.12798 0.13310  43  GLU C CG    
4312 C CD    . GLU D 44  ? 0.46448 0.44560 0.49360 -0.20040 -0.13549 0.12053  43  GLU C CD    
4313 O OE1   . GLU D 44  ? 0.47133 0.42472 0.49015 -0.18787 -0.14239 0.10918  43  GLU C OE1   
4314 O OE2   . GLU D 44  ? 0.47139 0.47436 0.51634 -0.20828 -0.13505 0.12126  43  GLU C OE2   
4315 N N     . LYS D 45  ? 0.45901 0.48124 0.46625 -0.21796 -0.10882 0.16085  44  LYS C N     
4316 C CA    . LYS D 45  ? 0.45704 0.51653 0.46941 -0.22693 -0.09682 0.17171  44  LYS C CA    
4317 C C     . LYS D 45  ? 0.44918 0.50112 0.44810 -0.23034 -0.09658 0.18192  44  LYS C C     
4318 O O     . LYS D 45  ? 0.45091 0.53256 0.45186 -0.23771 -0.08692 0.19159  44  LYS C O     
4319 C CB    . LYS D 45  ? 0.47699 0.57479 0.49518 -0.21665 -0.07982 0.16367  44  LYS C CB    
4320 C CG    . LYS D 45  ? 0.48064 0.59361 0.51387 -0.21414 -0.07841 0.15471  44  LYS C CG    
4321 C CD    . LYS D 45  ? 0.55863 0.69054 0.60724 -0.22979 -0.08062 0.16358  44  LYS C CD    
4322 C CE    . LYS D 45  ? 0.61044 0.76497 0.67629 -0.22656 -0.07773 0.15397  44  LYS C CE    
4323 N NZ    . LYS D 45  ? 0.64024 0.82499 0.72339 -0.24122 -0.07573 0.16280  44  LYS C NZ    
4324 N N     . GLY D 46  ? 0.48647 0.50081 0.47174 -0.22446 -0.10684 0.17955  45  GLY C N     
4325 C CA    . GLY D 46  ? 0.50602 0.51123 0.47810 -0.22636 -0.10741 0.18814  45  GLY C CA    
4326 C C     . GLY D 46  ? 0.49436 0.50731 0.45726 -0.21203 -0.09672 0.18081  45  GLY C C     
4327 O O     . GLY D 46  ? 0.49440 0.50138 0.44588 -0.21228 -0.09629 0.18714  45  GLY C O     
4328 N N     . PHE D 47  ? 0.41923 0.44385 0.38655 -0.19965 -0.08876 0.16784  46  PHE C N     
4329 C CA    . PHE D 47  ? 0.40287 0.43372 0.36293 -0.18571 -0.07926 0.15979  46  PHE C CA    
4330 C C     . PHE D 47  ? 0.41813 0.44403 0.38300 -0.17419 -0.07805 0.14575  46  PHE C C     
4331 O O     . PHE D 47  ? 0.38031 0.40990 0.35528 -0.17703 -0.08037 0.14271  46  PHE C O     
4332 C CB    . PHE D 47  ? 0.39056 0.46278 0.35238 -0.18527 -0.06337 0.16279  46  PHE C CB    
4333 C CG    . PHE D 47  ? 0.37226 0.47938 0.34872 -0.18922 -0.05536 0.16213  46  PHE C CG    
4334 C CD1   . PHE D 47  ? 0.43518 0.55779 0.41857 -0.20407 -0.05623 0.17403  46  PHE C CD1   
4335 C CD2   . PHE D 47  ? 0.39321 0.51795 0.37700 -0.17822 -0.04727 0.14991  46  PHE C CD2   
4336 C CE1   . PHE D 47  ? 0.47032 0.62663 0.46840 -0.20734 -0.04906 0.17313  46  PHE C CE1   
4337 C CE2   . PHE D 47  ? 0.36808 0.52522 0.36573 -0.18080 -0.04073 0.14870  46  PHE C CE2   
4338 C CZ    . PHE D 47  ? 0.40459 0.57801 0.40970 -0.19505 -0.04158 0.15995  46  PHE C CZ    
4339 N N     . GLY D 48  ? 0.35867 0.37561 0.31616 -0.16144 -0.07471 0.13761  47  GLY C N     
4340 C CA    . GLY D 48  ? 0.33957 0.35423 0.30118 -0.15099 -0.07189 0.12546  47  GLY C CA    
4341 C C     . GLY D 48  ? 0.38143 0.37884 0.33343 -0.13851 -0.07121 0.11873  47  GLY C C     
4342 O O     . GLY D 48  ? 0.36362 0.36057 0.30713 -0.13631 -0.06937 0.12218  47  GLY C O     
4343 N N     . TYR D 49  ? 0.37640 0.35958 0.32973 -0.13030 -0.07310 0.10924  48  TYR C N     
4344 C CA    . TYR D 49  ? 0.34697 0.32055 0.29376 -0.11741 -0.06974 0.10216  48  TYR C CA    
4345 C C     . TYR D 49  ? 0.36932 0.30963 0.30564 -0.11217 -0.08133 0.10185  48  TYR C C     
4346 O O     . TYR D 49  ? 0.34943 0.28696 0.28107 -0.10058 -0.07854 0.09635  48  TYR C O     
4347 C CB    . TYR D 49  ? 0.35666 0.32947 0.31011 -0.10646 -0.06716 0.08850  48  TYR C CB    
4348 C CG    . TYR D 49  ? 0.31064 0.31534 0.27402 -0.10567 -0.05564 0.08502  48  TYR C CG    
4349 C CD1   . TYR D 49  ? 0.31010 0.34246 0.27455 -0.10368 -0.04414 0.08615  48  TYR C CD1   
4350 C CD2   . TYR D 49  ? 0.30060 0.30724 0.27140 -0.10539 -0.05756 0.07953  48  TYR C CD2   
4351 C CE1   . TYR D 49  ? 0.28512 0.34533 0.25855 -0.10045 -0.03498 0.08134  48  TYR C CE1   
4352 C CE2   . TYR D 49  ? 0.29425 0.32947 0.27410 -0.10285 -0.04831 0.07578  48  TYR C CE2   
4353 C CZ    . TYR D 49  ? 0.26819 0.32984 0.24970 -0.10029 -0.03717 0.07674  48  TYR C CZ    
4354 O OH    . TYR D 49  ? 0.26404 0.35257 0.25428 -0.09572 -0.02947 0.07177  48  TYR C OH    
4355 N N     . LYS D 50  ? 0.38705 0.30404 0.32127 -0.11787 -0.09478 0.10485  49  LYS C N     
4356 C CA    . LYS D 50  ? 0.35600 0.23997 0.28115 -0.10990 -0.10730 0.10159  49  LYS C CA    
4357 C C     . LYS D 50  ? 0.37015 0.25737 0.28762 -0.10757 -0.10510 0.10654  49  LYS C C     
4358 O O     . LYS D 50  ? 0.40235 0.30211 0.31812 -0.11784 -0.10288 0.11664  49  LYS C O     
4359 C CB    . LYS D 50  ? 0.40796 0.26835 0.33184 -0.11709 -0.12290 0.10428  49  LYS C CB    
4360 C CG    . LYS D 50  ? 0.45606 0.28231 0.37080 -0.10775 -0.13755 0.09948  49  LYS C CG    
4361 C CD    . LYS D 50  ? 0.64564 0.45060 0.55818 -0.11664 -0.15353 0.10422  49  LYS C CD    
4362 C CE    . LYS D 50  ? 0.63246 0.40472 0.54018 -0.10357 -0.16880 0.09167  49  LYS C CE    
4363 N NZ    . LYS D 50  ? 0.67927 0.43754 0.57985 -0.08842 -0.17181 0.08471  49  LYS C NZ    
4364 N N     . GLY D 51  ? 0.36473 0.24156 0.27754 -0.09335 -0.10614 0.09930  50  GLY C N     
4365 C CA    . GLY D 51  ? 0.36011 0.23945 0.26559 -0.08829 -0.10532 0.10171  50  GLY C CA    
4366 C C     . GLY D 51  ? 0.32199 0.22941 0.22865 -0.08351 -0.09195 0.09971  50  GLY C C     
4367 O O     . GLY D 51  ? 0.36668 0.27496 0.26837 -0.07476 -0.09272 0.09714  50  GLY C O     
4368 N N     . SER D 52  ? 0.33144 0.26329 0.24660 -0.08723 -0.08018 0.09774  51  SER C N     
4369 C CA    . SER D 52  ? 0.34235 0.30303 0.26169 -0.08110 -0.06703 0.09156  51  SER C CA    
4370 C C     . SER D 52  ? 0.32212 0.28173 0.25014 -0.06550 -0.06401 0.07570  51  SER C C     
4371 O O     . SER D 52  ? 0.32957 0.27226 0.26161 -0.05918 -0.06908 0.06879  51  SER C O     
4372 C CB    . SER D 52  ? 0.33803 0.32588 0.26410 -0.08887 -0.05632 0.09399  51  SER C CB    
4373 O OG    . SER D 52  ? 0.32008 0.30530 0.25637 -0.08717 -0.05534 0.08681  51  SER C OG    
4374 N N     . CYS D 53  ? 0.32117 0.30041 0.25230 -0.05944 -0.05559 0.06980  52  CYS C N     
4375 C CA    . CYS D 53  ? 0.29728 0.27649 0.23775 -0.04691 -0.05322 0.05681  52  CYS C CA    
4376 C C     . CYS D 53  ? 0.24106 0.23809 0.19182 -0.04406 -0.04206 0.04935  52  CYS C C     
4377 O O     . CYS D 53  ? 0.27843 0.29126 0.22860 -0.04935 -0.03606 0.05255  52  CYS C O     
4378 C CB    . CYS D 53  ? 0.32222 0.30411 0.25924 -0.04086 -0.05627 0.05441  52  CYS C CB    
4379 S SG    . CYS D 53  ? 0.35275 0.36127 0.28904 -0.03950 -0.04749 0.05105  52  CYS C SG    
4380 N N     . PHE D 54  ? 0.24041 0.23524 0.20089 -0.03539 -0.03968 0.03970  53  PHE C N     
4381 C CA    . PHE D 54  ? 0.22862 0.23704 0.19832 -0.03177 -0.03055 0.03289  53  PHE C CA    
4382 C C     . PHE D 54  ? 0.23484 0.25259 0.20645 -0.02796 -0.03011 0.02850  53  PHE C C     
4383 O O     . PHE D 54  ? 0.28071 0.29457 0.25852 -0.02258 -0.03320 0.02326  53  PHE C O     
4384 C CB    . PHE D 54  ? 0.21081 0.21281 0.18922 -0.02602 -0.02798 0.02675  53  PHE C CB    
4385 C CG    . PHE D 54  ? 0.22118 0.21762 0.19685 -0.02844 -0.02719 0.02886  53  PHE C CG    
4386 C CD1   . PHE D 54  ? 0.25703 0.23811 0.22621 -0.03019 -0.03520 0.03183  53  PHE C CD1   
4387 C CD2   . PHE D 54  ? 0.22784 0.23287 0.20670 -0.02849 -0.02020 0.02746  53  PHE C CD2   
4388 C CE1   . PHE D 54  ? 0.29035 0.26598 0.25694 -0.03225 -0.03605 0.03243  53  PHE C CE1   
4389 C CE2   . PHE D 54  ? 0.26802 0.26870 0.24388 -0.03003 -0.02070 0.02873  53  PHE C CE2   
4390 C CZ    . PHE D 54  ? 0.25867 0.24524 0.22867 -0.03201 -0.02858 0.03076  53  PHE C CZ    
4391 N N     . HIS D 55  ? 0.22199 0.25366 0.18837 -0.03024 -0.02708 0.03000  54  HIS C N     
4392 C CA    . HIS D 55  ? 0.23068 0.27040 0.19498 -0.02607 -0.02876 0.02537  54  HIS C CA    
4393 C C     . HIS D 55  ? 0.23704 0.28108 0.21339 -0.02015 -0.02545 0.01487  54  HIS C C     
4394 O O     . HIS D 55  ? 0.26267 0.30890 0.24096 -0.01594 -0.02930 0.00874  54  HIS C O     
4395 C CB    . HIS D 55  ? 0.24163 0.29650 0.19320 -0.02947 -0.02700 0.03056  54  HIS C CB    
4396 C CG    . HIS D 55  ? 0.22375 0.29362 0.17815 -0.03019 -0.01931 0.02922  54  HIS C CG    
4397 N ND1   . HIS D 55  ? 0.24613 0.31818 0.20123 -0.03696 -0.01643 0.03618  54  HIS C ND1   
4398 C CD2   . HIS D 55  ? 0.24047 0.32403 0.19724 -0.02405 -0.01536 0.02092  54  HIS C CD2   
4399 C CE1   . HIS D 55  ? 0.25514 0.34348 0.21389 -0.03465 -0.01049 0.03239  54  HIS C CE1   
4400 N NE2   . HIS D 55  ? 0.24682 0.34172 0.20591 -0.02634 -0.00979 0.02310  54  HIS C NE2   
4401 N N     . ARG D 56  ? 0.19289 0.23639 0.17713 -0.02001 -0.01974 0.01299  55  ARG C N     
4402 C CA    . ARG D 56  ? 0.20187 0.24681 0.19638 -0.01580 -0.01736 0.00493  55  ARG C CA    
4403 C C     . ARG D 56  ? 0.20067 0.23715 0.20470 -0.01636 -0.01341 0.00564  55  ARG C C     
4404 O O     . ARG D 56  ? 0.22128 0.25719 0.22266 -0.01764 -0.00945 0.00897  55  ARG C O     
4405 C CB    . ARG D 56  ? 0.20577 0.26156 0.19603 -0.01354 -0.01435 0.00217  55  ARG C CB    
4406 C CG    . ARG D 56  ? 0.22084 0.27425 0.21987 -0.00830 -0.01509 -0.00714 55  ARG C CG    
4407 C CD    . ARG D 56  ? 0.21702 0.27978 0.21183 -0.00345 -0.01317 -0.01135 55  ARG C CD    
4408 N NE    . ARG D 56  ? 0.24278 0.32158 0.22599 -0.00093 -0.01423 -0.01283 55  ARG C NE    
4409 C CZ    . ARG D 56  ? 0.26130 0.35630 0.23861 0.00273  -0.01106 -0.01433 55  ARG C CZ    
4410 N NH1   . ARG D 56  ? 0.27471 0.37042 0.25704 0.00516  -0.00811 -0.01544 55  ARG C NH1   
4411 N NH2   . ARG D 56  ? 0.34330 0.45596 0.30908 0.00480  -0.01093 -0.01486 55  ARG C NH2   
4412 N N     . ILE D 57  ? 0.18251 0.21473 0.19764 -0.01523 -0.01440 0.00251  56  ILE C N     
4413 C CA    . ILE D 57  ? 0.18282 0.21047 0.20684 -0.01558 -0.00944 0.00366  56  ILE C CA    
4414 C C     . ILE D 57  ? 0.18324 0.21123 0.22093 -0.01587 -0.00836 -0.00063 56  ILE C C     
4415 O O     . ILE D 57  ? 0.18942 0.22019 0.23691 -0.01580 -0.01257 -0.00490 56  ILE C O     
4416 C CB    . ILE D 57  ? 0.20363 0.22897 0.23008 -0.01437 -0.01109 0.00476  56  ILE C CB    
4417 C CG1   . ILE D 57  ? 0.21836 0.23821 0.23071 -0.01509 -0.01436 0.00954  56  ILE C CG1   
4418 C CG2   . ILE D 57  ? 0.22190 0.24751 0.25776 -0.01358 -0.00449 0.00520  56  ILE C CG2   
4419 C CD1   . ILE D 57  ? 0.26268 0.27659 0.27547 -0.01187 -0.01824 0.00929  56  ILE C CD1   
4420 N N     . ILE D 58  ? 0.18744 0.21157 0.22607 -0.01653 -0.00404 0.00071  57  ILE C N     
4421 C CA    . ILE D 58  ? 0.19697 0.21737 0.24799 -0.01828 -0.00446 -0.00202 57  ILE C CA    
4422 C C     . ILE D 58  ? 0.21358 0.23082 0.27090 -0.02139 0.00275  0.00410  57  ILE C C     
4423 O O     . ILE D 58  ? 0.21175 0.22396 0.26029 -0.02041 0.00676  0.00850  57  ILE C O     
4424 C CB    . ILE D 58  ? 0.19466 0.21070 0.24093 -0.01549 -0.00778 -0.00621 57  ILE C CB    
4425 C CG1   . ILE D 58  ? 0.20840 0.23192 0.24683 -0.01167 -0.01366 -0.01228 57  ILE C CG1   
4426 C CG2   . ILE D 58  ? 0.24508 0.25273 0.30485 -0.01818 -0.01065 -0.00894 57  ILE C CG2   
4427 C CD1   . ILE D 58  ? 0.22335 0.24564 0.25773 -0.00640 -0.01779 -0.01944 57  ILE C CD1   
4428 N N     . PRO D 59  ? 0.22298 0.24527 0.29488 -0.02477 0.00468  0.00478  58  PRO C N     
4429 C CA    . PRO D 59  ? 0.23474 0.25853 0.31153 -0.02775 0.01328  0.01168  58  PRO C CA    
4430 C C     . PRO D 59  ? 0.25030 0.26272 0.32553 -0.03094 0.01548  0.01667  58  PRO C C     
4431 O O     . PRO D 59  ? 0.26005 0.26428 0.34157 -0.03337 0.00977  0.01387  58  PRO C O     
4432 C CB    . PRO D 59  ? 0.22262 0.25804 0.32009 -0.03172 0.01367  0.01016  58  PRO C CB    
4433 C CG    . PRO D 59  ? 0.22083 0.26106 0.31845 -0.02759 0.00568  0.00274  58  PRO C CG    
4434 C CD    . PRO D 59  ? 0.21504 0.24513 0.29971 -0.02547 -0.00080 -0.00072 58  PRO C CD    
4435 N N     . GLY D 60  ? 0.25266 0.26272 0.31760 -0.02983 0.02242  0.02360  59  GLY C N     
4436 C CA    . GLY D 60  ? 0.24460 0.24199 0.30388 -0.03140 0.02396  0.02972  59  GLY C CA    
4437 C C     . GLY D 60  ? 0.23816 0.22677 0.28272 -0.02524 0.01909  0.02698  59  GLY C C     
4438 O O     . GLY D 60  ? 0.28445 0.26120 0.32274 -0.02447 0.01875  0.03137  59  GLY C O     
4439 N N     . PHE D 61  ? 0.22157 0.21650 0.26094 -0.02092 0.01489  0.02028  60  PHE C N     
4440 C CA    . PHE D 61  ? 0.22193 0.21423 0.25009 -0.01549 0.01098  0.01752  60  PHE C CA    
4441 C C     . PHE D 61  ? 0.21860 0.21918 0.23636 -0.01297 0.01181  0.01756  60  PHE C C     
4442 O O     . PHE D 61  ? 0.22463 0.22320 0.23297 -0.01064 0.01347  0.02099  60  PHE C O     
4443 C CB    . PHE D 61  ? 0.21952 0.21189 0.25177 -0.01323 0.00375  0.00922  60  PHE C CB    
4444 C CG    . PHE D 61  ? 0.17590 0.15508 0.21675 -0.01479 -0.00023 0.00798  60  PHE C CG    
4445 C CD1   . PHE D 61  ? 0.25029 0.21725 0.28564 -0.01047 -0.00331 0.00841  60  PHE C CD1   
4446 C CD2   . PHE D 61  ? 0.21670 0.19457 0.27187 -0.02053 -0.00242 0.00619  60  PHE C CD2   
4447 C CE1   . PHE D 61  ? 0.25443 0.20478 0.29684 -0.01197 -0.00905 0.00747  60  PHE C CE1   
4448 C CE2   . PHE D 61  ? 0.25780 0.22072 0.32179 -0.02346 -0.00782 0.00545  60  PHE C CE2   
4449 C CZ    . PHE D 61  ? 0.23585 0.18371 0.29261 -0.01912 -0.01145 0.00608  60  PHE C CZ    
4450 N N     . MET D 62  ? 0.19354 0.20214 0.21234 -0.01367 0.00935  0.01405  61  MET C N     
4451 C CA    . MET D 62  ? 0.19732 0.21104 0.20671 -0.01299 0.00828  0.01502  61  MET C CA    
4452 C C     . MET D 62  ? 0.19423 0.21241 0.20496 -0.01487 0.00536  0.01346  61  MET C C     
4453 O O     . MET D 62  ? 0.20453 0.22451 0.22259 -0.01545 0.00330  0.01020  61  MET C O     
4454 C CB    . MET D 62  ? 0.20397 0.22338 0.20791 -0.01074 0.00563  0.01328  61  MET C CB    
4455 C CG    . MET D 62  ? 0.25195 0.28128 0.25648 -0.01068 0.00218  0.00898  61  MET C CG    
4456 S SD    . MET D 62  ? 0.23383 0.25914 0.24684 -0.00812 -0.00061 0.00206  61  MET C SD    
4457 C CE    . MET D 62  ? 0.24259 0.27938 0.25216 -0.00900 -0.00425 -0.00089 61  MET C CE    
4458 N N     . CYS D 63  ? 0.18879 0.20729 0.19187 -0.01574 0.00366  0.01579  62  CYS C N     
4459 C CA    . CYS D 63  ? 0.19124 0.21112 0.19154 -0.01783 -0.00119 0.01611  62  CYS C CA    
4460 C C     . CYS D 63  ? 0.19781 0.22413 0.19101 -0.02091 -0.00358 0.01868  62  CYS C C     
4461 O O     . CYS D 63  ? 0.21334 0.23957 0.20240 -0.02211 -0.00345 0.02114  62  CYS C O     
4462 C CB    . CYS D 63  ? 0.22246 0.23491 0.21983 -0.01686 -0.00274 0.01724  62  CYS C CB    
4463 S SG    . CYS D 63  ? 0.25374 0.26568 0.26058 -0.01258 0.00194  0.01447  62  CYS C SG    
4464 N N     . GLN D 64  ? 0.19438 0.22817 0.18613 -0.02238 -0.00590 0.01831  63  GLN C N     
4465 C CA    . GLN D 64  ? 0.16636 0.21211 0.15246 -0.02583 -0.00644 0.02148  63  GLN C CA    
4466 C C     . GLN D 64  ? 0.19458 0.23919 0.17388 -0.03152 -0.01116 0.02735  63  GLN C C     
4467 O O     . GLN D 64  ? 0.21990 0.25924 0.19830 -0.03012 -0.01440 0.02628  63  GLN C O     
4468 C CB    . GLN D 64  ? 0.20151 0.26009 0.18901 -0.02147 -0.00437 0.01616  63  GLN C CB    
4469 C CG    . GLN D 64  ? 0.17805 0.25555 0.16063 -0.02361 -0.00323 0.01858  63  GLN C CG    
4470 C CD    . GLN D 64  ? 0.19928 0.28980 0.18243 -0.01615 -0.00165 0.01079  63  GLN C CD    
4471 O OE1   . GLN D 64  ? 0.22629 0.30792 0.21449 -0.00993 -0.00229 0.00385  63  GLN C OE1   
4472 N NE2   . GLN D 64  ? 0.21092 0.32263 0.18878 -0.01659 0.00011  0.01188  63  GLN C NE2   
4473 N N     . GLY D 65  ? 0.19441 0.24327 0.16950 -0.03832 -0.01248 0.03400  64  GLY C N     
4474 C CA    . GLY D 65  ? 0.22896 0.27419 0.19671 -0.04589 -0.01783 0.04217  64  GLY C CA    
4475 C C     . GLY D 65  ? 0.24983 0.31163 0.21540 -0.05463 -0.01646 0.04977  64  GLY C C     
4476 O O     . GLY D 65  ? 0.22310 0.30371 0.19317 -0.05262 -0.01085 0.04685  64  GLY C O     
4477 N N     . GLY D 66  ? 0.25900 0.31480 0.21837 -0.06437 -0.02197 0.05980  65  GLY C N     
4478 C CA    . GLY D 66  ? 0.26272 0.33344 0.22286 -0.07583 -0.02133 0.06904  65  GLY C CA    
4479 C C     . GLY D 66  ? 0.27726 0.36674 0.23011 -0.08283 -0.01863 0.07828  65  GLY C C     
4480 O O     . GLY D 66  ? 0.28622 0.39335 0.24162 -0.09375 -0.01668 0.08716  65  GLY C O     
4481 N N     . ASP D 67  ? 0.28349 0.37217 0.22744 -0.07716 -0.01837 0.07675  66  ASP C N     
4482 C CA    . ASP D 67  ? 0.25417 0.36138 0.18727 -0.08277 -0.01565 0.08599  66  ASP C CA    
4483 C C     . ASP D 67  ? 0.28716 0.37281 0.21270 -0.09191 -0.02457 0.09738  66  ASP C C     
4484 O O     . ASP D 67  ? 0.32770 0.39597 0.24294 -0.08779 -0.03061 0.09797  66  ASP C O     
4485 C CB    . ASP D 67  ? 0.27025 0.38638 0.19669 -0.07060 -0.01266 0.07690  66  ASP C CB    
4486 C CG    . ASP D 67  ? 0.29915 0.43415 0.21410 -0.07346 -0.00966 0.08390  66  ASP C CG    
4487 O OD1   . ASP D 67  ? 0.34422 0.48225 0.26058 -0.08421 -0.00997 0.09455  66  ASP C OD1   
4488 O OD2   . ASP D 67  ? 0.32308 0.46806 0.22941 -0.06378 -0.00788 0.07693  66  ASP C OD2   
4489 N N     . PHE D 68  ? 0.32606 0.41397 0.25740 -0.10348 -0.02639 0.10556  67  PHE C N     
4490 C CA    . PHE D 68  ? 0.30962 0.37650 0.23456 -0.11224 -0.03570 0.11585  67  PHE C CA    
4491 C C     . PHE D 68  ? 0.33520 0.42125 0.25467 -0.11852 -0.03173 0.12491  67  PHE C C     
4492 O O     . PHE D 68  ? 0.37012 0.44095 0.28418 -0.12757 -0.03905 0.13534  67  PHE C O     
4493 C CB    . PHE D 68  ? 0.34512 0.39441 0.27800 -0.12152 -0.04410 0.11933  67  PHE C CB    
4494 C CG    . PHE D 68  ? 0.32145 0.39596 0.26680 -0.12905 -0.03904 0.12100  67  PHE C CG    
4495 C CD1   . PHE D 68  ? 0.33591 0.42644 0.28282 -0.14026 -0.03828 0.13135  67  PHE C CD1   
4496 C CD2   . PHE D 68  ? 0.37014 0.45226 0.32557 -0.12506 -0.03568 0.11287  67  PHE C CD2   
4497 C CE1   . PHE D 68  ? 0.35466 0.46986 0.31373 -0.14669 -0.03435 0.13296  67  PHE C CE1   
4498 C CE2   . PHE D 68  ? 0.37636 0.48223 0.34362 -0.13112 -0.03225 0.11411  67  PHE C CE2   
4499 C CZ    . PHE D 68  ? 0.34680 0.46954 0.31622 -0.14171 -0.03176 0.12392  67  PHE C CZ    
4500 N N     . THR D 69  ? 0.32337 0.44215 0.24351 -0.11352 -0.02077 0.12114  68  THR C N     
4501 C CA    . THR D 69  ? 0.31433 0.45488 0.22906 -0.11897 -0.01589 0.12978  68  THR C CA    
4502 C C     . THR D 69  ? 0.34174 0.48692 0.24060 -0.10927 -0.01287 0.12750  68  THR C C     
4503 O O     . THR D 69  ? 0.38783 0.53302 0.27544 -0.11431 -0.01377 0.13759  68  THR C O     
4504 C CB    . THR D 69  ? 0.37655 0.55503 0.30323 -0.12127 -0.00648 0.12866  68  THR C CB    
4505 O OG1   . THR D 69  ? 0.34937 0.54755 0.27829 -0.10710 0.00129  0.11498  68  THR C OG1   
4506 C CG2   . THR D 69  ? 0.39571 0.57163 0.33730 -0.13108 -0.01042 0.13130  68  THR C CG2   
4507 N N     . ARG D 70  ? 0.34756 0.49676 0.24437 -0.09547 -0.00991 0.11450  69  ARG C N     
4508 C CA    . ARG D 70  ? 0.38249 0.53382 0.26342 -0.08494 -0.00945 0.11023  69  ARG C CA    
4509 C C     . ARG D 70  ? 0.35351 0.47460 0.22690 -0.07813 -0.01928 0.10591  69  ARG C C     
4510 O O     . ARG D 70  ? 0.40317 0.52029 0.26190 -0.07088 -0.02260 0.10436  69  ARG C O     
4511 C CB    . ARG D 70  ? 0.33316 0.51429 0.21592 -0.07266 -0.00056 0.09695  69  ARG C CB    
4512 C CG    . ARG D 70  ? 0.36176 0.57758 0.25198 -0.07603 0.00885  0.09922  69  ARG C CG    
4513 C CD    . ARG D 70  ? 0.44302 0.68499 0.33302 -0.06055 0.01551  0.08395  69  ARG C CD    
4514 N NE    . ARG D 70  ? 0.56559 0.84336 0.46352 -0.06126 0.02387  0.08446  69  ARG C NE    
4515 C CZ    . ARG D 70  ? 0.51058 0.81246 0.41485 -0.04858 0.02893  0.07071  69  ARG C CZ    
4516 N NH1   . ARG D 70  ? 0.48730 0.78003 0.39122 -0.03512 0.02658  0.05553  69  ARG C NH1   
4517 N NH2   . ARG D 70  ? 0.53847 0.87425 0.44959 -0.04904 0.03559  0.07197  69  ARG C NH2   
4518 N N     . HIS D 71  ? 0.34789 0.44904 0.23082 -0.07939 -0.02460 0.10330  70  HIS C N     
4519 C CA    . HIS D 71  ? 0.40196 0.47618 0.28058 -0.07287 -0.03484 0.09912  70  HIS C CA    
4520 C C     . HIS D 71  ? 0.42400 0.50798 0.29764 -0.05950 -0.03472 0.08650  70  HIS C C     
4521 O O     . HIS D 71  ? 0.43307 0.50132 0.30102 -0.05285 -0.04380 0.08300  70  HIS C O     
4522 C CB    . HIS D 71  ? 0.41287 0.46184 0.28089 -0.07675 -0.04513 0.10909  70  HIS C CB    
4523 C CG    . HIS D 71  ? 0.36533 0.40537 0.23744 -0.09059 -0.04690 0.12104  70  HIS C CG    
4524 N ND1   . HIS D 71  ? 0.37543 0.39426 0.25718 -0.09539 -0.05349 0.12145  70  HIS C ND1   
4525 C CD2   . HIS D 71  ? 0.43730 0.48776 0.30548 -0.10076 -0.04381 0.13241  70  HIS C CD2   
4526 C CE1   . HIS D 71  ? 0.42291 0.43841 0.30675 -0.10813 -0.05561 0.13188  70  HIS C CE1   
4527 N NE2   . HIS D 71  ? 0.45995 0.49499 0.33632 -0.11232 -0.04965 0.13944  70  HIS C NE2   
4528 N N     . ASN D 72  ? 0.36250 0.47215 0.24082 -0.05434 -0.02560 0.07752  71  ASN C N     
4529 C CA    . ASN D 72  ? 0.35559 0.47096 0.23412 -0.04028 -0.02633 0.06159  71  ASN C CA    
4530 C C     . ASN D 72  ? 0.33879 0.46252 0.23439 -0.03343 -0.02026 0.04753  71  ASN C C     
4531 O O     . ASN D 72  ? 0.40646 0.53882 0.30232 -0.02257 -0.02000 0.03426  71  ASN C O     
4532 C CB    . ASN D 72  ? 0.40414 0.53935 0.26442 -0.03566 -0.02423 0.06197  71  ASN C CB    
4533 C CG    . ASN D 72  ? 0.37877 0.54190 0.24229 -0.03692 -0.01222 0.06237  71  ASN C CG    
4534 O OD1   . ASN D 72  ? 0.33397 0.50653 0.21114 -0.03922 -0.00652 0.06016  71  ASN C OD1   
4535 N ND2   . ASN D 72  ? 0.43663 0.61436 0.28781 -0.03471 -0.00888 0.06491  71  ASN C ND2   
4536 N N     . GLY D 73  ? 0.29102 0.41148 0.19950 -0.03932 -0.01653 0.05025  72  GLY C N     
4537 C CA    . GLY D 73  ? 0.30354 0.42899 0.22683 -0.03346 -0.01167 0.03919  72  GLY C CA    
4538 C C     . GLY D 73  ? 0.27479 0.42987 0.19765 -0.03096 -0.00345 0.03657  72  GLY C C     
4539 O O     . GLY D 73  ? 0.29370 0.45197 0.22806 -0.02512 -0.00055 0.02754  72  GLY C O     
4540 N N     . THR D 74  ? 0.27737 0.45523 0.18721 -0.03461 0.00037  0.04436  73  THR C N     
4541 C CA    . THR D 74  ? 0.29105 0.50219 0.20138 -0.03014 0.00877  0.04037  73  THR C CA    
4542 C C     . THR D 74  ? 0.29930 0.52355 0.21920 -0.04228 0.01358  0.05242  73  THR C C     
4543 O O     . THR D 74  ? 0.30933 0.56040 0.23666 -0.03875 0.01959  0.04863  73  THR C O     
4544 C CB    . THR D 74  ? 0.38370 0.60889 0.28212 -0.02057 0.00949  0.03411  73  THR C CB    
4545 O OG1   . THR D 74  ? 0.32833 0.55445 0.21786 -0.02993 0.00982  0.04815  73  THR C OG1   
4546 C CG2   . THR D 74  ? 0.41913 0.62749 0.30930 -0.01000 0.00120  0.02195  73  THR C CG2   
4547 N N     . GLY D 75  ? 0.27983 0.48540 0.20050 -0.05575 0.00937  0.06564  74  GLY C N     
4548 C CA    . GLY D 75  ? 0.28206 0.49858 0.21052 -0.06844 0.01128  0.07718  74  GLY C CA    
4549 C C     . GLY D 75  ? 0.30657 0.51468 0.24879 -0.07570 0.00921  0.07939  74  GLY C C     
4550 O O     . GLY D 75  ? 0.25245 0.45654 0.20020 -0.06883 0.00988  0.07048  74  GLY C O     
4551 N N     . GLY D 76  ? 0.35902 0.56347 0.30590 -0.08955 0.00593  0.09115  75  GLY C N     
4552 C CA    . GLY D 76  ? 0.34469 0.54463 0.30439 -0.09622 0.00317  0.09249  75  GLY C CA    
4553 C C     . GLY D 76  ? 0.33671 0.56570 0.30688 -0.10308 0.00661  0.09693  75  GLY C C     
4554 O O     . GLY D 76  ? 0.33770 0.59690 0.30778 -0.09875 0.01356  0.09517  75  GLY C O     
4555 N N     . LYS D 77  ? 0.28276 0.50261 0.26157 -0.11375 0.00094  0.10265  76  LYS C N     
4556 C CA    . LYS D 77  ? 0.30212 0.54825 0.29188 -0.12151 0.00294  0.10745  76  LYS C CA    
4557 C C     . LYS D 77  ? 0.25725 0.48981 0.25745 -0.12791 -0.00386 0.10771  76  LYS C C     
4558 O O     . LYS D 77  ? 0.27276 0.47196 0.26916 -0.13168 -0.01229 0.10952  76  LYS C O     
4559 C CB    . LYS D 77  ? 0.35763 0.61120 0.34274 -0.13362 0.00247  0.12097  76  LYS C CB    
4560 C CG    . LYS D 77  ? 0.34853 0.57118 0.33077 -0.14827 -0.00839 0.13288  76  LYS C CG    
4561 C CD    . LYS D 77  ? 0.37773 0.61308 0.35588 -0.16010 -0.00730 0.14685  76  LYS C CD    
4562 C CE    . LYS D 77  ? 0.43810 0.64059 0.41245 -0.17422 -0.01943 0.15877  76  LYS C CE    
4563 N NZ    . LYS D 77  ? 0.39616 0.61159 0.36718 -0.18749 -0.01831 0.17412  76  LYS C NZ    
4564 N N     . SER D 78  ? 0.25625 0.51540 0.26934 -0.12843 -0.00070 0.10541  77  SER C N     
4565 C CA    . SER D 78  ? 0.25907 0.50972 0.28327 -0.13402 -0.00714 0.10487  77  SER C CA    
4566 C C     . SER D 78  ? 0.32137 0.56687 0.34942 -0.15145 -0.01408 0.11773  77  SER C C     
4567 O O     . SER D 78  ? 0.35683 0.60748 0.37937 -0.15941 -0.01308 0.12778  77  SER C O     
4568 C CB    . SER D 78  ? 0.29768 0.57989 0.33486 -0.12527 -0.00125 0.09550  77  SER C CB    
4569 O OG    . SER D 78  ? 0.31095 0.62567 0.35575 -0.13140 0.00305  0.10096  77  SER C OG    
4570 N N     . ILE D 79  ? 0.26538 0.50089 0.30343 -0.15762 -0.02173 0.11745  78  ILE C N     
4571 C CA    . ILE D 79  ? 0.33355 0.56662 0.37823 -0.17414 -0.02879 0.12855  78  ILE C CA    
4572 C C     . ILE D 79  ? 0.29691 0.57210 0.35628 -0.17858 -0.02177 0.13094  78  ILE C C     
4573 O O     . ILE D 79  ? 0.41018 0.68895 0.47818 -0.19335 -0.02654 0.14047  78  ILE C O     
4574 C CB    . ILE D 79  ? 0.35386 0.55657 0.40316 -0.17849 -0.04168 0.12600  78  ILE C CB    
4575 C CG1   . ILE D 79  ? 0.31869 0.53919 0.38181 -0.17075 -0.03983 0.11468  78  ILE C CG1   
4576 C CG2   . ILE D 79  ? 0.35735 0.51903 0.39199 -0.17352 -0.04900 0.12328  78  ILE C CG2   
4577 C CD1   . ILE D 79  ? 0.34173 0.53779 0.41140 -0.17498 -0.05329 0.11090  78  ILE C CD1   
4578 N N     . TYR D 80  ? 0.32342 0.63048 0.38682 -0.16583 -0.01128 0.12190  79  TYR C N     
4579 C CA    . TYR D 80  ? 0.29959 0.64818 0.37840 -0.16730 -0.00501 0.12152  79  TYR C CA    
4580 C C     . TYR D 80  ? 0.42392 0.80254 0.49835 -0.16902 0.00448  0.12826  79  TYR C C     
4581 O O     . TYR D 80  ? 0.40008 0.81822 0.48442 -0.16448 0.01236  0.12467  79  TYR C O     
4582 C CB    . TYR D 80  ? 0.31630 0.68199 0.40402 -0.15112 -0.00142 0.10617  79  TYR C CB    
4583 C CG    . TYR D 80  ? 0.27787 0.61622 0.37055 -0.14998 -0.01136 0.09996  79  TYR C CG    
4584 C CD1   . TYR D 80  ? 0.29435 0.62740 0.40021 -0.16228 -0.02041 0.10373  79  TYR C CD1   
4585 C CD2   . TYR D 80  ? 0.27006 0.58799 0.35440 -0.13696 -0.01241 0.09032  79  TYR C CD2   
4586 C CE1   . TYR D 80  ? 0.25036 0.55821 0.35931 -0.16022 -0.03082 0.09692  79  TYR C CE1   
4587 C CE2   . TYR D 80  ? 0.29582 0.59024 0.38365 -0.13575 -0.02194 0.08478  79  TYR C CE2   
4588 C CZ    . TYR D 80  ? 0.29805 0.58749 0.39732 -0.14678 -0.03138 0.08763  79  TYR C CZ    
4589 O OH    . TYR D 80  ? 0.28131 0.54743 0.38234 -0.14450 -0.04231 0.08091  79  TYR C OH    
4590 N N     . GLY D 81  ? 0.36438 0.72539 0.42406 -0.17479 0.00337  0.13751  80  GLY C N     
4591 C CA    . GLY D 81  ? 0.41439 0.80168 0.46828 -0.17734 0.01153  0.14508  80  GLY C CA    
4592 C C     . GLY D 81  ? 0.39321 0.80703 0.44195 -0.15903 0.02181  0.13349  80  GLY C C     
4593 O O     . GLY D 81  ? 0.40597 0.84561 0.44985 -0.15903 0.02917  0.13802  80  GLY C O     
4594 N N     . GLU D 82  ? 0.35648 0.76400 0.40570 -0.14315 0.02199  0.11855  81  GLU C N     
4595 C CA    . GLU D 82  ? 0.40200 0.83161 0.44707 -0.12408 0.02982  0.10543  81  GLU C CA    
4596 C C     . GLU D 82  ? 0.32978 0.73595 0.37359 -0.11092 0.02638  0.09234  81  GLU C C     
4597 O O     . GLU D 82  ? 0.42267 0.80345 0.47095 -0.11664 0.01928  0.09345  81  GLU C O     
4598 C CB    . GLU D 82  ? 0.34064 0.81510 0.39896 -0.11934 0.03637  0.10070  81  GLU C CB    
4599 C CG    . GLU D 82  ? 0.42274 0.89995 0.49857 -0.12145 0.03223  0.09675  81  GLU C CG    
4600 C CD    . GLU D 82  ? 0.48201 1.00171 0.57384 -0.12661 0.03698  0.09958  81  GLU C CD    
4601 O OE1   . GLU D 82  ? 0.50005 1.04359 0.58965 -0.13401 0.04278  0.10895  81  GLU C OE1   
4602 O OE2   . GLU D 82  ? 0.56478 1.09527 0.67212 -0.12315 0.03491  0.09246  81  GLU C OE2   
4603 N N     . LYS D 83  ? 0.31894 0.73355 0.35647 -0.09315 0.03104  0.07990  82  LYS C N     
4604 C CA    . LYS D 83  ? 0.23895 0.63841 0.27783 -0.07940 0.02890  0.06672  82  LYS C CA    
4605 C C     . LYS D 83  ? 0.19721 0.61329 0.25214 -0.07644 0.02779  0.06094  82  LYS C C     
4606 O O     . LYS D 83  ? 0.24145 0.68935 0.30559 -0.07864 0.03106  0.06239  82  LYS C O     
4607 C CB    . LYS D 83  ? 0.27156 0.67923 0.30186 -0.06042 0.03330  0.05380  82  LYS C CB    
4608 C CG    . LYS D 83  ? 0.31693 0.70607 0.33155 -0.06090 0.03366  0.05709  82  LYS C CG    
4609 C CD    . LYS D 83  ? 0.37983 0.72962 0.38902 -0.06270 0.02862  0.05733  82  LYS C CD    
4610 C CE    . LYS D 83  ? 0.39309 0.72577 0.38683 -0.06198 0.02863  0.05961  82  LYS C CE    
4611 N NZ    . LYS D 83  ? 0.50782 0.83701 0.49629 -0.07744 0.02717  0.07478  82  LYS C NZ    
4612 N N     . PHE D 84  ? 0.18766 0.58348 0.24670 -0.07136 0.02300  0.05446  83  PHE C N     
4613 C CA    . PHE D 84  ? 0.19905 0.60789 0.27386 -0.06939 0.02012  0.04971  83  PHE C CA    
4614 C C     . PHE D 84  ? 0.17667 0.58565 0.25402 -0.04912 0.01931  0.03413  83  PHE C C     
4615 O O     . PHE D 84  ? 0.16874 0.56037 0.23664 -0.03871 0.01974  0.02784  83  PHE C O     
4616 C CB    . PHE D 84  ? 0.26703 0.65616 0.34913 -0.08593 0.01222  0.05887  83  PHE C CB    
4617 C CG    . PHE D 84  ? 0.23342 0.58454 0.30884 -0.08655 0.00589  0.05842  83  PHE C CG    
4618 C CD1   . PHE D 84  ? 0.25542 0.58059 0.31712 -0.09375 0.00512  0.06588  83  PHE C CD1   
4619 C CD2   . PHE D 84  ? 0.20950 0.55135 0.29241 -0.07979 -0.00031 0.05069  83  PHE C CD2   
4620 C CE1   . PHE D 84  ? 0.23788 0.52983 0.29384 -0.09430 -0.00055 0.06529  83  PHE C CE1   
4621 C CE2   . PHE D 84  ? 0.19585 0.50538 0.27254 -0.08043 -0.00646 0.05038  83  PHE C CE2   
4622 C CZ    . PHE D 84  ? 0.22422 0.50891 0.28784 -0.08796 -0.00611 0.05755  83  PHE C CZ    
4623 N N     . GLU D 85  ? 0.21545 0.64414 0.30656 -0.04352 0.01734  0.02806  84  GLU C N     
4624 C CA    . GLU D 85  ? 0.18809 0.61973 0.28255 -0.02284 0.01507  0.01316  84  GLU C CA    
4625 C C     . GLU D 85  ? 0.18368 0.58254 0.27587 -0.01897 0.00814  0.01062  84  GLU C C     
4626 O O     . GLU D 85  ? 0.19337 0.57327 0.28663 -0.03276 0.00334  0.01907  84  GLU C O     
4627 C CB    . GLU D 85  ? 0.21648 0.67438 0.32736 -0.02086 0.01265  0.00956  84  GLU C CB    
4628 C CG    . GLU D 85  ? 0.41795 0.88671 0.53227 0.00204  0.01038  -0.00616 84  GLU C CG    
4629 C CD    . GLU D 85  ? 0.40568 0.91137 0.53458 0.00405  0.01141  -0.00943 84  GLU C CD    
4630 O OE1   . GLU D 85  ? 0.40341 0.93707 0.53252 -0.00058 0.01879  -0.00610 84  GLU C OE1   
4631 O OE2   . GLU D 85  ? 0.38581 0.89358 0.52611 0.01046  0.00438  -0.01515 84  GLU C OE2   
4632 N N     . ASP D 86  ? 0.16759 0.55885 0.25592 0.00056  0.00654  -0.00134 85  ASP C N     
4633 C CA    . ASP D 86  ? 0.18694 0.55205 0.27497 0.00752  -0.00168 -0.00464 85  ASP C CA    
4634 C C     . ASP D 86  ? 0.16955 0.53980 0.26860 0.00650  -0.00971 -0.00514 85  ASP C C     
4635 O O     . ASP D 86  ? 0.18962 0.57811 0.29569 0.01816  -0.01114 -0.01324 85  ASP C O     
4636 C CB    . ASP D 86  ? 0.20058 0.55297 0.28082 0.02970  -0.00314 -0.01722 85  ASP C CB    
4637 C CG    . ASP D 86  ? 0.21223 0.55037 0.27894 0.03161  0.00260  -0.01842 85  ASP C CG    
4638 O OD1   . ASP D 86  ? 0.21152 0.52709 0.26929 0.01802  0.00450  -0.00931 85  ASP C OD1   
4639 O OD2   . ASP D 86  ? 0.26360 0.61250 0.32859 0.04803  0.00385  -0.02968 85  ASP C OD2   
4640 N N     . GLU D 87  ? 0.14567 0.49724 0.24459 -0.00676 -0.01594 0.00266  86  GLU C N     
4641 C CA    . GLU D 87  ? 0.20529 0.56200 0.31453 -0.01068 -0.02465 0.00289  86  GLU C CA    
4642 C C     . GLU D 87  ? 0.16798 0.51709 0.27549 0.00930  -0.03288 -0.00721 86  GLU C C     
4643 O O     . GLU D 87  ? 0.16523 0.53191 0.28301 0.01583  -0.03646 -0.01263 86  GLU C O     
4644 C CB    . GLU D 87  ? 0.17547 0.50394 0.27861 -0.02691 -0.03078 0.01164  86  GLU C CB    
4645 C CG    . GLU D 87  ? 0.18453 0.51927 0.29915 -0.03424 -0.04110 0.01233  86  GLU C CG    
4646 C CD    . GLU D 87  ? 0.15454 0.46693 0.26552 -0.05299 -0.04718 0.02099  86  GLU C CD    
4647 O OE1   . GLU D 87  ? 0.20608 0.48917 0.30147 -0.05746 -0.04360 0.02573  86  GLU C OE1   
4648 O OE2   . GLU D 87  ? 0.20669 0.52259 0.32772 -0.06112 -0.05509 0.02174  86  GLU C OE2   
4649 N N     . ASN D 88  ? 0.17396 0.48001 0.26125 0.01801  -0.03447 -0.00860 87  ASN C N     
4650 C CA    . ASN D 88  ? 0.18886 0.47765 0.26836 0.03711  -0.04129 -0.01609 87  ASN C CA    
4651 C C     . ASN D 88  ? 0.17535 0.42046 0.23367 0.04113  -0.03840 -0.01426 87  ASN C C     
4652 O O     . ASN D 88  ? 0.19188 0.42260 0.24340 0.02960  -0.03239 -0.00821 87  ASN C O     
4653 C CB    . ASN D 88  ? 0.18520 0.46822 0.26565 0.03801  -0.05287 -0.01623 87  ASN C CB    
4654 C CG    . ASN D 88  ? 0.20801 0.45927 0.27536 0.02520  -0.05542 -0.00876 87  ASN C CG    
4655 O OD1   . ASN D 88  ? 0.18271 0.39778 0.23092 0.02744  -0.05284 -0.00608 87  ASN C OD1   
4656 N ND2   . ASN D 88  ? 0.19792 0.46357 0.27647 0.01143  -0.06069 -0.00567 87  ASN C ND2   
4657 N N     . PHE D 89  ? 0.20914 0.43391 0.25804 0.05729  -0.04330 -0.01909 88  PHE C N     
4658 C CA    . PHE D 89  ? 0.24023 0.42340 0.27056 0.06006  -0.04174 -0.01602 88  PHE C CA    
4659 C C     . PHE D 89  ? 0.25171 0.40672 0.26818 0.06506  -0.04931 -0.01283 88  PHE C C     
4660 O O     . PHE D 89  ? 0.28334 0.41018 0.28694 0.07409  -0.05095 -0.01210 88  PHE C O     
4661 C CB    . PHE D 89  ? 0.24153 0.41913 0.27000 0.07341  -0.04049 -0.02281 88  PHE C CB    
4662 C CG    . PHE D 89  ? 0.23173 0.43474 0.26928 0.07017  -0.03278 -0.02652 88  PHE C CG    
4663 C CD1   . PHE D 89  ? 0.22736 0.42122 0.26023 0.05728  -0.02534 -0.02088 88  PHE C CD1   
4664 C CD2   . PHE D 89  ? 0.24576 0.48392 0.29589 0.08123  -0.03321 -0.03604 88  PHE C CD2   
4665 C CE1   . PHE D 89  ? 0.22867 0.44558 0.26700 0.05487  -0.01877 -0.02367 88  PHE C CE1   
4666 C CE2   . PHE D 89  ? 0.27581 0.53978 0.33171 0.07909  -0.02542 -0.03931 88  PHE C CE2   
4667 C CZ    . PHE D 89  ? 0.25088 0.50334 0.29987 0.06564  -0.01835 -0.03266 88  PHE C CZ    
4668 N N     . ILE D 90  ? 0.22375 0.38592 0.24213 0.05894  -0.05454 -0.01059 89  ILE C N     
4669 C CA    . ILE D 90  ? 0.21720 0.35485 0.21982 0.06486  -0.06228 -0.00809 89  ILE C CA    
4670 C C     . ILE D 90  ? 0.26133 0.36277 0.24426 0.06100  -0.05681 -0.00094 89  ILE C C     
4671 O O     . ILE D 90  ? 0.29812 0.37424 0.26472 0.06966  -0.05955 0.00215  89  ILE C O     
4672 C CB    . ILE D 90  ? 0.23195 0.38435 0.24046 0.05798  -0.06985 -0.00837 89  ILE C CB    
4673 C CG1   . ILE D 90  ? 0.21594 0.40649 0.24558 0.06338  -0.07662 -0.01541 89  ILE C CG1   
4674 C CG2   . ILE D 90  ? 0.24736 0.37156 0.23452 0.06375  -0.07724 -0.00565 89  ILE C CG2   
4675 C CD1   . ILE D 90  ? 0.30624 0.51758 0.34893 0.05051  -0.08251 -0.01511 89  ILE C CD1   
4676 N N     . LEU D 91  ? 0.23627 0.33573 0.22037 0.04783  -0.04936 0.00249  90  LEU C N     
4677 C CA    . LEU D 91  ? 0.23544 0.30618 0.20377 0.04389  -0.04384 0.00849  90  LEU C CA    
4678 C C     . LEU D 91  ? 0.22226 0.28210 0.19047 0.04517  -0.03651 0.00956  90  LEU C C     
4679 O O     . LEU D 91  ? 0.23799 0.31410 0.21861 0.04445  -0.03378 0.00550  90  LEU C O     
4680 C CB    . LEU D 91  ? 0.22069 0.29163 0.18911 0.03107  -0.04184 0.01071  90  LEU C CB    
4681 C CG    . LEU D 91  ? 0.23811 0.31522 0.20551 0.02978  -0.05148 0.00884  90  LEU C CG    
4682 C CD1   . LEU D 91  ? 0.30033 0.37464 0.26818 0.01767  -0.05205 0.01003  90  LEU C CD1   
4683 C CD2   . LEU D 91  ? 0.26613 0.32378 0.21406 0.04013  -0.05657 0.00988  90  LEU C CD2   
4684 N N     . LYS D 92  ? 0.27011 0.30368 0.22434 0.04672  -0.03346 0.01504  91  LYS C N     
4685 C CA    . LYS D 92  ? 0.24748 0.26727 0.20192 0.04758  -0.02853 0.01651  91  LYS C CA    
4686 C C     . LYS D 92  ? 0.28448 0.29350 0.23571 0.03772  -0.02032 0.02139  91  LYS C C     
4687 O O     . LYS D 92  ? 0.25135 0.25953 0.19676 0.03244  -0.01859 0.02384  91  LYS C O     
4688 C CB    . LYS D 92  ? 0.30783 0.30610 0.25146 0.05762  -0.03290 0.01988  91  LYS C CB    
4689 C CG    . LYS D 92  ? 0.32758 0.33655 0.27368 0.06936  -0.04263 0.01436  91  LYS C CG    
4690 C CD    . LYS D 92  ? 0.43890 0.42494 0.37543 0.08089  -0.04917 0.01678  91  LYS C CD    
4691 C CE    . LYS D 92  ? 0.54592 0.54730 0.49373 0.09385  -0.05761 0.00643  91  LYS C CE    
4692 N NZ    . LYS D 92  ? 0.57274 0.60965 0.53351 0.09379  -0.05953 -0.00065 91  LYS C NZ    
4693 N N     . HIS D 93  ? 0.24509 0.24709 0.20150 0.03607  -0.01636 0.02128  92  HIS C N     
4694 C CA    . HIS D 93  ? 0.23640 0.23175 0.19377 0.02739  -0.00914 0.02463  92  HIS C CA    
4695 C C     . HIS D 93  ? 0.30486 0.27942 0.25128 0.02768  -0.00611 0.03279  92  HIS C C     
4696 O O     . HIS D 93  ? 0.34812 0.30939 0.29649 0.02764  -0.00530 0.03547  92  HIS C O     
4697 C CB    . HIS D 93  ? 0.24546 0.24435 0.21410 0.02560  -0.00772 0.02011  92  HIS C CB    
4698 C CG    . HIS D 93  ? 0.20576 0.22779 0.18338 0.02526  -0.00921 0.01336  92  HIS C CG    
4699 N ND1   . HIS D 93  ? 0.19674 0.23201 0.17875 0.03350  -0.01397 0.00728  92  HIS C ND1   
4700 C CD2   . HIS D 93  ? 0.23923 0.27454 0.22188 0.01775  -0.00637 0.01251  92  HIS C CD2   
4701 C CE1   . HIS D 93  ? 0.18674 0.24553 0.17650 0.03018  -0.01257 0.00352  92  HIS C CE1   
4702 N NE2   . HIS D 93  ? 0.19600 0.25337 0.18541 0.02011  -0.00833 0.00736  92  HIS C NE2   
4703 N N     . THR D 94  ? 0.28136 0.25330 0.21570 0.02773  -0.00480 0.03697  93  THR C N     
4704 C CA    . THR D 94  ? 0.31789 0.27350 0.23785 0.02978  -0.00213 0.04586  93  THR C CA    
4705 C C     . THR D 94  ? 0.29289 0.24486 0.21224 0.02275  0.00756  0.05156  93  THR C C     
4706 O O     . THR D 94  ? 0.36841 0.30896 0.27746 0.02259  0.01179  0.06083  93  THR C O     
4707 C CB    . THR D 94  ? 0.31943 0.27566 0.22386 0.03594  -0.00660 0.04654  93  THR C CB    
4708 O OG1   . THR D 94  ? 0.34854 0.31782 0.25535 0.03299  -0.00726 0.04065  93  THR C OG1   
4709 C CG2   . THR D 94  ? 0.32675 0.28385 0.23103 0.04453  -0.01657 0.04324  93  THR C CG2   
4710 N N     . GLY D 95  ? 0.29196 0.25437 0.22176 0.01716  0.01111  0.04700  94  GLY C N     
4711 C CA    . GLY D 95  ? 0.30548 0.26829 0.23698 0.01192  0.01979  0.05099  94  GLY C CA    
4712 C C     . GLY D 95  ? 0.29169 0.26600 0.23204 0.00848  0.02092  0.04442  94  GLY C C     
4713 O O     . GLY D 95  ? 0.26966 0.25059 0.21525 0.00818  0.01533  0.03810  94  GLY C O     
4714 N N     . PRO D 96  ? 0.28877 0.26650 0.23087 0.00592  0.02807  0.04636  95  PRO C N     
4715 C CA    . PRO D 96  ? 0.29508 0.28138 0.24439 0.00427  0.02773  0.03997  95  PRO C CA    
4716 C C     . PRO D 96  ? 0.25792 0.24513 0.19781 0.00806  0.02119  0.03464  95  PRO C C     
4717 O O     . PRO D 96  ? 0.29087 0.27458 0.21643 0.01315  0.01947  0.03549  95  PRO C O     
4718 C CB    . PRO D 96  ? 0.29664 0.28800 0.24666 0.00395  0.03670  0.04310  95  PRO C CB    
4719 C CG    . PRO D 96  ? 0.37738 0.36358 0.32726 0.00092  0.04238  0.05259  95  PRO C CG    
4720 C CD    . PRO D 96  ? 0.32067 0.29598 0.25847 0.00458  0.03674  0.05507  95  PRO C CD    
4721 N N     . GLY D 97  ? 0.24762 0.23855 0.19534 0.00502  0.01642  0.02950  96  GLY C N     
4722 C CA    . GLY D 97  ? 0.23713 0.22710 0.17892 0.00594  0.00883  0.02509  96  GLY C CA    
4723 C C     . GLY D 97  ? 0.22620 0.21934 0.17021 0.00323  0.00174  0.02432  96  GLY C C     
4724 O O     . GLY D 97  ? 0.23246 0.22592 0.17596 0.00055  -0.00544 0.02162  96  GLY C O     
4725 N N     . ILE D 98  ? 0.23964 0.23553 0.18688 0.00390  0.00294  0.02653  97  ILE C N     
4726 C CA    . ILE D 98  ? 0.22872 0.23297 0.18019 0.00272  -0.00303 0.02492  97  ILE C CA    
4727 C C     . ILE D 98  ? 0.21237 0.22587 0.17423 -0.00419 -0.00484 0.02343  97  ILE C C     
4728 O O     . ILE D 98  ? 0.21790 0.23196 0.18584 -0.00633 -0.00111 0.02348  97  ILE C O     
4729 C CB    . ILE D 98  ? 0.24452 0.24926 0.19769 0.00720  -0.00187 0.02617  97  ILE C CB    
4730 C CG1   . ILE D 98  ? 0.26316 0.25842 0.20322 0.01379  -0.00238 0.02921  97  ILE C CG1   
4731 C CG2   . ILE D 98  ? 0.25965 0.27896 0.22131 0.00698  -0.00658 0.02294  97  ILE C CG2   
4732 C CD1   . ILE D 98  ? 0.32133 0.32009 0.25430 0.01646  -0.00993 0.02682  97  ILE C CD1   
4733 N N     . LEU D 99  ? 0.20820 0.22949 0.17203 -0.00830 -0.01105 0.02271  98  LEU C N     
4734 C CA    . LEU D 99  ? 0.20035 0.23190 0.17224 -0.01634 -0.01299 0.02365  98  LEU C CA    
4735 C C     . LEU D 99  ? 0.18818 0.23918 0.16803 -0.01661 -0.01340 0.02312  98  LEU C C     
4736 O O     . LEU D 99  ? 0.19851 0.25603 0.17896 -0.01458 -0.01742 0.02208  98  LEU C O     
4737 C CB    . LEU D 99  ? 0.21301 0.23837 0.18193 -0.02240 -0.02029 0.02447  98  LEU C CB    
4738 C CG    . LEU D 99  ? 0.21430 0.24804 0.18984 -0.03315 -0.02404 0.02820  98  LEU C CG    
4739 C CD1   . LEU D 99  ? 0.24619 0.27591 0.22206 -0.03503 -0.02063 0.02992  98  LEU C CD1   
4740 C CD2   . LEU D 99  ? 0.25584 0.27916 0.22827 -0.03892 -0.03398 0.02878  98  LEU C CD2   
4741 N N     . SER D 100 ? 0.16654 0.22839 0.15236 -0.01773 -0.00963 0.02283  99  SER C N     
4742 C CA    . SER D 100 ? 0.17964 0.26170 0.17236 -0.01447 -0.00868 0.02029  99  SER C CA    
4743 C C     . SER D 100 ? 0.16530 0.26440 0.16284 -0.02071 -0.00641 0.02188  99  SER C C     
4744 O O     . SER D 100 ? 0.18683 0.27780 0.18127 -0.02566 -0.00548 0.02454  99  SER C O     
4745 C CB    . SER D 100 ? 0.18568 0.25965 0.17679 -0.00404 -0.00618 0.01617  99  SER C CB    
4746 O OG    . SER D 100 ? 0.18264 0.27453 0.17959 0.00212  -0.00674 0.01171  99  SER C OG    
4747 N N     . MET D 101 ? 0.16394 0.28867 0.16859 -0.01996 -0.00560 0.02042  100 MET C N     
4748 C CA    . MET D 101 ? 0.15160 0.29673 0.15898 -0.02591 -0.00235 0.02302  100 MET C CA    
4749 C C     . MET D 101 ? 0.17307 0.32095 0.17795 -0.01711 0.00151  0.01686  100 MET C C     
4750 O O     . MET D 101 ? 0.18473 0.33510 0.19153 -0.00568 0.00153  0.00929  100 MET C O     
4751 C CB    . MET D 101 ? 0.16811 0.34563 0.18550 -0.02883 -0.00202 0.02397  100 MET C CB    
4752 C CG    . MET D 101 ? 0.18525 0.36531 0.20774 -0.04159 -0.00706 0.03118  100 MET C CG    
4753 S SD    . MET D 101 ? 0.22010 0.38251 0.23595 -0.05713 -0.00959 0.04159  100 MET C SD    
4754 C CE    . MET D 101 ? 0.19481 0.39185 0.21450 -0.06561 -0.00299 0.04849  100 MET C CE    
4755 N N     . ALA D 102 ? 0.17512 0.32111 0.17512 -0.02185 0.00320  0.01964  101 ALA C N     
4756 C CA    . ALA D 102 ? 0.20025 0.35410 0.19768 -0.01405 0.00569  0.01311  101 ALA C CA    
4757 C C     . ALA D 102 ? 0.21130 0.40071 0.21156 -0.01329 0.00947  0.01243  101 ALA C C     
4758 O O     . ALA D 102 ? 0.21244 0.41962 0.21714 -0.02281 0.01063  0.01995  101 ALA C O     
4759 C CB    . ALA D 102 ? 0.19927 0.34105 0.18967 -0.01878 0.00522  0.01619  101 ALA C CB    
4760 N N     . ASN D 103 ? 0.20103 0.40218 0.19951 -0.00168 0.01104  0.00289  102 ASN C N     
4761 C CA    . ASN D 103 ? 0.17467 0.41452 0.17574 0.00156  0.01572  0.00071  102 ASN C CA    
4762 C C     . ASN D 103 ? 0.21642 0.46336 0.21046 0.01475  0.01635  -0.01064 102 ASN C C     
4763 O O     . ASN D 103 ? 0.22643 0.44690 0.21573 0.02035  0.01200  -0.01671 102 ASN C O     
4764 C CB    . ASN D 103 ? 0.20090 0.45735 0.21349 0.00687  0.01514  -0.00282 102 ASN C CB    
4765 C CG    . ASN D 103 ? 0.23445 0.47385 0.24798 0.02314  0.01024  -0.01493 102 ASN C CG    
4766 O OD1   . ASN D 103 ? 0.20701 0.44613 0.21619 0.03567  0.00923  -0.02555 102 ASN C OD1   
4767 N ND2   . ASN D 103 ? 0.21220 0.43691 0.23060 0.02347  0.00606  -0.01349 102 ASN C ND2   
4768 N N     . ALA D 104 ? 0.21413 0.49915 0.20817 0.01978  0.02156  -0.01393 103 ALA C N     
4769 C CA    . ALA D 104 ? 0.27506 0.57407 0.26099 0.03450  0.02225  -0.02654 103 ALA C CA    
4770 C C     . ALA D 104 ? 0.28873 0.60948 0.28185 0.05205  0.02176  -0.04045 103 ALA C C     
4771 O O     . ALA D 104 ? 0.32135 0.66287 0.31089 0.06153  0.02174  -0.04768 103 ALA C O     
4772 C CB    . ALA D 104 ? 0.28763 0.61128 0.26527 0.02727  0.02754  -0.01880 103 ALA C CB    
4773 N N     . GLY D 105 ? 0.28976 0.59578 0.29291 0.05551  0.01705  -0.04261 104 GLY C N     
4774 C CA    . GLY D 105 ? 0.30683 0.63351 0.31801 0.07200  0.01533  -0.05457 104 GLY C CA    
4775 C C     . GLY D 105 ? 0.24413 0.58941 0.26840 0.06403  0.01699  -0.04640 104 GLY C C     
4776 O O     . GLY D 105 ? 0.22766 0.57479 0.25546 0.04595  0.02057  -0.03218 104 GLY C O     
4777 N N     . PRO D 106 ? 0.24107 0.59677 0.27171 0.07722  0.01255  -0.05566 105 PRO C N     
4778 C CA    . PRO D 106 ? 0.23662 0.60843 0.27949 0.07077  0.01245  -0.04962 105 PRO C CA    
4779 C C     . PRO D 106 ? 0.23918 0.63668 0.28473 0.05158  0.01928  -0.03599 105 PRO C C     
4780 O O     . PRO D 106 ? 0.26026 0.67700 0.29954 0.04980  0.02363  -0.03492 105 PRO C O     
4781 C CB    . PRO D 106 ? 0.27325 0.65750 0.31820 0.08976  0.00735  -0.06372 105 PRO C CB    
4782 C CG    . PRO D 106 ? 0.34872 0.70568 0.38417 0.10707  0.00087  -0.07695 105 PRO C CG    
4783 C CD    . PRO D 106 ? 0.34129 0.69043 0.36730 0.09900  0.00563  -0.07278 105 PRO C CD    
4784 N N     . ASN D 107 ? 0.26054 0.65577 0.31525 0.03706  0.01882  -0.02510 106 ASN C N     
4785 C CA    . ASN D 107 ? 0.20552 0.62148 0.26558 0.01871  0.02262  -0.01230 106 ASN C CA    
4786 C C     . ASN D 107 ? 0.21672 0.63216 0.26627 0.00573  0.02759  -0.00191 106 ASN C C     
4787 O O     . ASN D 107 ? 0.23527 0.67552 0.28441 -0.00046 0.03165  0.00339  106 ASN C O     
4788 C CB    . ASN D 107 ? 0.24024 0.69098 0.30885 0.02494  0.02374  -0.01756 106 ASN C CB    
4789 C CG    . ASN D 107 ? 0.25719 0.70607 0.33488 0.03955  0.01731  -0.02850 106 ASN C CG    
4790 O OD1   . ASN D 107 ? 0.21943 0.65393 0.30461 0.03435  0.01242  -0.02471 106 ASN C OD1   
4791 N ND2   . ASN D 107 ? 0.30709 0.76831 0.38289 0.05879  0.01578  -0.04246 106 ASN C ND2   
4792 N N     . THR D 108 ? 0.19609 0.58317 0.23719 0.00179  0.02689  0.00142  107 THR C N     
4793 C CA    . THR D 108 ? 0.19803 0.57892 0.22810 -0.01008 0.02976  0.01157  107 THR C CA    
4794 C C     . THR D 108 ? 0.23441 0.58568 0.26258 -0.02565 0.02701  0.02309  107 THR C C     
4795 O O     . THR D 108 ? 0.25004 0.58269 0.26683 -0.02955 0.02731  0.02710  107 THR C O     
4796 C CB    . THR D 108 ? 0.26244 0.63912 0.27984 0.00315  0.03117  0.00217  107 THR C CB    
4797 O OG1   . THR D 108 ? 0.23200 0.58186 0.24695 0.01256  0.02833  -0.00621 107 THR C OG1   
4798 C CG2   . THR D 108 ? 0.26393 0.66885 0.28157 0.01936  0.03235  -0.01002 107 THR C CG2   
4799 N N     . ASN D 109 ? 0.19364 0.53948 0.23234 -0.03402 0.02317  0.02785  108 ASN C N     
4800 C CA    . ASN D 109 ? 0.20747 0.52399 0.24422 -0.04763 0.01879  0.03738  108 ASN C CA    
4801 C C     . ASN D 109 ? 0.19222 0.50355 0.22265 -0.06449 0.01791  0.05124  108 ASN C C     
4802 O O     . ASN D 109 ? 0.21120 0.54378 0.24656 -0.07171 0.01898  0.05692  108 ASN C O     
4803 C CB    . ASN D 109 ? 0.18866 0.50237 0.23836 -0.05092 0.01286  0.03733  108 ASN C CB    
4804 C CG    . ASN D 109 ? 0.20971 0.51123 0.25946 -0.03256 0.00975  0.02421  108 ASN C CG    
4805 O OD1   . ASN D 109 ? 0.20051 0.46732 0.23932 -0.02587 0.00717  0.02042  108 ASN C OD1   
4806 N ND2   . ASN D 109 ? 0.20602 0.53661 0.26823 -0.02401 0.00979  0.01749  108 ASN C ND2   
4807 N N     . GLY D 110 ? 0.23230 0.51539 0.25198 -0.07027 0.01555  0.05678  109 GLY C N     
4808 C CA    . GLY D 110 ? 0.22142 0.49435 0.23467 -0.08486 0.01245  0.06967  109 GLY C CA    
4809 C C     . GLY D 110 ? 0.23339 0.47063 0.24402 -0.09407 0.00441  0.07543  109 GLY C C     
4810 O O     . GLY D 110 ? 0.25035 0.48200 0.26975 -0.10111 -0.00114 0.07765  109 GLY C O     
4811 N N     . SER D 111 ? 0.22821 0.44087 0.22665 -0.09287 0.00280  0.07670  110 SER C N     
4812 C CA    . SER D 111 ? 0.23756 0.41485 0.23227 -0.09794 -0.00509 0.07960  110 SER C CA    
4813 C C     . SER D 111 ? 0.19984 0.35247 0.18818 -0.08264 -0.00579 0.06799  110 SER C C     
4814 O O     . SER D 111 ? 0.21821 0.34225 0.20486 -0.08165 -0.01228 0.06603  110 SER C O     
4815 C CB    . SER D 111 ? 0.25217 0.41003 0.23819 -0.10859 -0.01196 0.09037  110 SER C CB    
4816 O OG    . SER D 111 ? 0.24719 0.40886 0.22262 -0.10348 -0.00794 0.09057  110 SER C OG    
4817 N N     . GLN D 112 ? 0.21825 0.38117 0.20323 -0.07111 0.00010  0.06028  111 GLN C N     
4818 C CA    . GLN D 112 ? 0.21093 0.34983 0.19196 -0.05978 -0.00146 0.05118  111 GLN C CA    
4819 C C     . GLN D 112 ? 0.20568 0.33539 0.19362 -0.05242 -0.00230 0.04348  111 GLN C C     
4820 O O     . GLN D 112 ? 0.19956 0.34705 0.19480 -0.05003 -0.00027 0.04074  111 GLN C O     
4821 C CB    . GLN D 112 ? 0.21368 0.36297 0.18986 -0.05002 0.00281  0.04428  111 GLN C CB    
4822 C CG    . GLN D 112 ? 0.22858 0.37686 0.19357 -0.05511 0.00156  0.05119  111 GLN C CG    
4823 C CD    . GLN D 112 ? 0.23595 0.38630 0.19517 -0.04379 0.00279  0.04188  111 GLN C CD    
4824 O OE1   . GLN D 112 ? 0.23941 0.37464 0.20282 -0.03506 0.00109  0.03230  111 GLN C OE1   
4825 N NE2   . GLN D 112 ? 0.22553 0.39526 0.17498 -0.04421 0.00544  0.04478  111 GLN C NE2   
4826 N N     . PHE D 113 ? 0.19056 0.29370 0.17581 -0.04853 -0.00545 0.04042  112 PHE C N     
4827 C CA    . PHE D 113 ? 0.18432 0.27555 0.17257 -0.04249 -0.00636 0.03532  112 PHE C CA    
4828 C C     . PHE D 113 ? 0.17477 0.24833 0.16093 -0.03461 -0.00516 0.02991  112 PHE C C     
4829 O O     . PHE D 113 ? 0.19385 0.26240 0.17746 -0.03475 -0.00545 0.02996  112 PHE C O     
4830 C CB    . PHE D 113 ? 0.22293 0.30041 0.21005 -0.04918 -0.01253 0.03957  112 PHE C CB    
4831 C CG    . PHE D 113 ? 0.19589 0.25230 0.17682 -0.05235 -0.01712 0.04243  112 PHE C CG    
4832 C CD1   . PHE D 113 ? 0.24289 0.29973 0.22077 -0.06218 -0.02090 0.05044  112 PHE C CD1   
4833 C CD2   . PHE D 113 ? 0.20598 0.24363 0.18409 -0.04494 -0.01755 0.03748  112 PHE C CD2   
4834 C CE1   . PHE D 113 ? 0.25909 0.29490 0.23077 -0.06308 -0.02662 0.05236  112 PHE C CE1   
4835 C CE2   . PHE D 113 ? 0.24456 0.26590 0.21836 -0.04543 -0.02195 0.03846  112 PHE C CE2   
4836 C CZ    . PHE D 113 ? 0.26555 0.28432 0.23583 -0.05395 -0.02744 0.04551  112 PHE C CZ    
4837 N N     . PHE D 114 ? 0.18258 0.24778 0.17017 -0.02811 -0.00408 0.02585  113 PHE C N     
4838 C CA    . PHE D 114 ? 0.20371 0.25340 0.19104 -0.02301 -0.00242 0.02271  113 PHE C CA    
4839 C C     . PHE D 114 ? 0.19124 0.22817 0.17583 -0.02051 -0.00260 0.02299  113 PHE C C     
4840 O O     . PHE D 114 ? 0.19044 0.23021 0.17340 -0.01964 -0.00404 0.02344  113 PHE C O     
4841 C CB    . PHE D 114 ? 0.20719 0.26011 0.19836 -0.01663 0.00033  0.01735  113 PHE C CB    
4842 C CG    . PHE D 114 ? 0.17953 0.23741 0.17217 -0.01065 0.00100  0.01445  113 PHE C CG    
4843 C CD1   . PHE D 114 ? 0.17700 0.25439 0.17117 -0.00947 0.00060  0.01299  113 PHE C CD1   
4844 C CD2   . PHE D 114 ? 0.19230 0.23646 0.18490 -0.00586 0.00187  0.01358  113 PHE C CD2   
4845 C CE1   . PHE D 114 ? 0.18470 0.26746 0.18095 -0.00178 -0.00011 0.00902  113 PHE C CE1   
4846 C CE2   . PHE D 114 ? 0.19537 0.24107 0.18792 0.00074  0.00071  0.01126  113 PHE C CE2   
4847 C CZ    . PHE D 114 ? 0.19784 0.26227 0.19255 0.00377  -0.00085 0.00804  113 PHE C CZ    
4848 N N     . ILE D 115 ? 0.18681 0.21167 0.17056 -0.01897 -0.00146 0.02250  114 ILE C N     
4849 C CA    . ILE D 115 ? 0.18663 0.20143 0.16619 -0.01510 0.00018  0.02246  114 ILE C CA    
4850 C C     . ILE D 115 ? 0.20182 0.21390 0.18540 -0.01143 0.00571  0.02181  114 ILE C C     
4851 O O     . ILE D 115 ? 0.19949 0.21147 0.18967 -0.01229 0.00734  0.02059  114 ILE C O     
4852 C CB    . ILE D 115 ? 0.19906 0.20511 0.17525 -0.01523 -0.00223 0.02207  114 ILE C CB    
4853 C CG1   . ILE D 115 ? 0.21823 0.22282 0.19150 -0.02084 -0.00978 0.02373  114 ILE C CG1   
4854 C CG2   . ILE D 115 ? 0.21384 0.21300 0.18309 -0.00968 -0.00004 0.02120  114 ILE C CG2   
4855 C CD1   . ILE D 115 ? 0.25372 0.24678 0.22415 -0.01972 -0.01434 0.02235  114 ILE C CD1   
4856 N N     . CYS D 116 ? 0.20569 0.21500 0.18577 -0.00789 0.00747  0.02305  115 CYS C N     
4857 C CA    . CYS D 116 ? 0.21651 0.21994 0.19970 -0.00600 0.01183  0.02457  115 CYS C CA    
4858 C C     . CYS D 116 ? 0.21548 0.21495 0.19828 -0.00626 0.01697  0.02701  115 CYS C C     
4859 O O     . CYS D 116 ? 0.24249 0.24073 0.21695 -0.00402 0.01744  0.02750  115 CYS C O     
4860 C CB    . CYS D 116 ? 0.23633 0.23521 0.21292 -0.00166 0.01116  0.02673  115 CYS C CB    
4861 S SG    . CYS D 116 ? 0.26804 0.27650 0.24730 0.00127  0.00549  0.02239  115 CYS C SG    
4862 N N     . THR D 117 ? 0.23268 0.23167 0.22517 -0.00865 0.02045  0.02785  116 THR C N     
4863 C CA    . THR D 117 ? 0.23155 0.23138 0.22622 -0.00924 0.02712  0.03127  116 THR C CA    
4864 C C     . THR D 117 ? 0.28985 0.28322 0.28386 -0.01066 0.03171  0.03816  116 THR C C     
4865 O O     . THR D 117 ? 0.29301 0.28962 0.28929 -0.01255 0.03889  0.04315  116 THR C O     
4866 C CB    . THR D 117 ? 0.26694 0.27386 0.27546 -0.01212 0.02756  0.02805  116 THR C CB    
4867 O OG1   . THR D 117 ? 0.28337 0.28869 0.30254 -0.01573 0.02445  0.02633  116 THR C OG1   
4868 C CG2   . THR D 117 ? 0.25068 0.26049 0.25605 -0.00999 0.02233  0.02306  116 THR C CG2   
4869 N N     . ALA D 118 ? 0.26736 0.25222 0.25763 -0.00942 0.02763  0.03909  117 ALA C N     
4870 C CA    . ALA D 118 ? 0.30956 0.28311 0.29673 -0.01025 0.02932  0.04642  117 ALA C CA    
4871 C C     . ALA D 118 ? 0.31595 0.28249 0.29331 -0.00417 0.02272  0.04485  117 ALA C C     
4872 O O     . ALA D 118 ? 0.29283 0.26636 0.27025 -0.00111 0.01776  0.03795  117 ALA C O     
4873 C CB    . ALA D 118 ? 0.32390 0.29243 0.32653 -0.01654 0.02852  0.04718  117 ALA C CB    
4874 N N     . LYS D 119 ? 0.30993 0.26353 0.27955 -0.00255 0.02233  0.05180  118 LYS C N     
4875 C CA    . LYS D 119 ? 0.34067 0.28711 0.30373 0.00457  0.01448  0.04938  118 LYS C CA    
4876 C C     . LYS D 119 ? 0.31232 0.25773 0.28735 0.00557  0.00812  0.04142  118 LYS C C     
4877 O O     . LYS D 119 ? 0.34963 0.28640 0.33418 0.00085  0.00767  0.04230  118 LYS C O     
4878 C CB    . LYS D 119 ? 0.38764 0.31652 0.33958 0.00609  0.01424  0.05960  118 LYS C CB    
4879 C CG    . LYS D 119 ? 0.37020 0.28965 0.31476 0.01528  0.00489  0.05743  118 LYS C CG    
4880 C CD    . LYS D 119 ? 0.45617 0.35535 0.38694 0.01630  0.00435  0.06978  118 LYS C CD    
4881 C CE    . LYS D 119 ? 0.59116 0.47754 0.51487 0.02696  -0.00692 0.06763  118 LYS C CE    
4882 N NZ    . LYS D 119 ? 0.57821 0.44521 0.48341 0.02902  -0.00797 0.08098  118 LYS C NZ    
4883 N N     . THR D 120 ? 0.27033 0.22596 0.24517 0.01179  0.00289  0.03328  119 THR C N     
4884 C CA    . THR D 120 ? 0.28322 0.24240 0.26701 0.01515  -0.00272 0.02406  119 THR C CA    
4885 C C     . THR D 120 ? 0.25921 0.21885 0.23852 0.02589  -0.00987 0.01944  119 THR C C     
4886 O O     . THR D 120 ? 0.27874 0.25656 0.26093 0.03063  -0.01214 0.01177  119 THR C O     
4887 C CB    . THR D 120 ? 0.24762 0.22598 0.23772 0.01212  -0.00087 0.01786  119 THR C CB    
4888 O OG1   . THR D 120 ? 0.25312 0.24597 0.23813 0.01359  -0.00053 0.01742  119 THR C OG1   
4889 C CG2   . THR D 120 ? 0.28924 0.26746 0.28489 0.00341  0.00459  0.02105  119 THR C CG2   
4890 N N     . GLU D 121 ? 0.29639 0.23648 0.26886 0.02996  -0.01368 0.02470  120 GLU C N     
4891 C CA    . GLU D 121 ? 0.30688 0.24663 0.27362 0.04161  -0.02119 0.02128  120 GLU C CA    
4892 C C     . GLU D 121 ? 0.35342 0.29894 0.32786 0.05110  -0.02848 0.00889  120 GLU C C     
4893 O O     . GLU D 121 ? 0.31259 0.26980 0.28626 0.06177  -0.03368 0.00269  120 GLU C O     
4894 C CB    . GLU D 121 ? 0.42423 0.33798 0.37951 0.04398  -0.02462 0.03124  120 GLU C CB    
4895 C CG    . GLU D 121 ? 0.40782 0.29602 0.36623 0.04327  -0.02989 0.03305  120 GLU C CG    
4896 C CD    . GLU D 121 ? 0.50210 0.38414 0.46828 0.02938  -0.02298 0.03901  120 GLU C CD    
4897 O OE1   . GLU D 121 ? 0.43327 0.32813 0.39957 0.02094  -0.01305 0.04410  120 GLU C OE1   
4898 O OE2   . GLU D 121 ? 0.60046 0.46457 0.57361 0.02752  -0.02872 0.03774  120 GLU C OE2   
4899 N N     . TRP D 122 ? 0.30194 0.24152 0.28409 0.04837  -0.02943 0.00410  121 TRP C N     
4900 C CA    . TRP D 122 ? 0.30504 0.25192 0.29253 0.05896  -0.03633 -0.00950 121 TRP C CA    
4901 C C     . TRP D 122 ? 0.30457 0.28660 0.29587 0.06138  -0.03223 -0.01689 121 TRP C C     
4902 O O     . TRP D 122 ? 0.31784 0.31373 0.31212 0.07255  -0.03675 -0.02846 121 TRP C O     
4903 C CB    . TRP D 122 ? 0.32111 0.25381 0.31513 0.05491  -0.03910 -0.01359 121 TRP C CB    
4904 C CG    . TRP D 122 ? 0.31611 0.26150 0.31568 0.04305  -0.03102 -0.01162 121 TRP C CG    
4905 C CD1   . TRP D 122 ? 0.29740 0.26512 0.30056 0.04367  -0.02894 -0.01988 121 TRP C CD1   
4906 C CD2   . TRP D 122 ? 0.28540 0.22276 0.28701 0.02967  -0.02429 -0.00056 121 TRP C CD2   
4907 N NE1   . TRP D 122 ? 0.27359 0.24479 0.28056 0.03192  -0.02272 -0.01472 121 TRP C NE1   
4908 C CE2   . TRP D 122 ? 0.27774 0.23180 0.28504 0.02367  -0.01967 -0.00371 121 TRP C CE2   
4909 C CE3   . TRP D 122 ? 0.30523 0.22460 0.30381 0.02275  -0.02143 0.01200  121 TRP C CE3   
4910 C CZ2   . TRP D 122 ? 0.28447 0.23808 0.29624 0.01237  -0.01321 0.00370  121 TRP C CZ2   
4911 C CZ3   . TRP D 122 ? 0.32978 0.25162 0.33297 0.01098  -0.01349 0.01954  121 TRP C CZ3   
4912 C CH2   . TRP D 122 ? 0.28156 0.22038 0.29211 0.00646  -0.00983 0.01472  121 TRP C CH2   
4913 N N     . LEU D 123 ? 0.29294 0.28988 0.28397 0.05137  -0.02417 -0.01037 122 LEU C N     
4914 C CA    . LEU D 123 ? 0.24046 0.26922 0.23519 0.05092  -0.02063 -0.01449 122 LEU C CA    
4915 C C     . LEU D 123 ? 0.24843 0.29232 0.24243 0.05633  -0.02255 -0.01418 122 LEU C C     
4916 O O     . LEU D 123 ? 0.23537 0.30807 0.23459 0.05533  -0.02017 -0.01694 122 LEU C O     
4917 C CB    . LEU D 123 ? 0.25618 0.29173 0.25148 0.03757  -0.01342 -0.00815 122 LEU C CB    
4918 C CG    . LEU D 123 ? 0.23503 0.26067 0.23295 0.03193  -0.01181 -0.00896 122 LEU C CG    
4919 C CD1   . LEU D 123 ? 0.24163 0.27088 0.23944 0.02047  -0.00607 -0.00232 122 LEU C CD1   
4920 C CD2   . LEU D 123 ? 0.27564 0.31438 0.27671 0.03830  -0.01450 -0.01988 122 LEU C CD2   
4921 N N     . ASP D 124 ? 0.26018 0.28605 0.24803 0.06144  -0.02720 -0.01025 123 ASP C N     
4922 C CA    . ASP D 124 ? 0.27390 0.31342 0.26115 0.06724  -0.03073 -0.01043 123 ASP C CA    
4923 C C     . ASP D 124 ? 0.28166 0.34665 0.27765 0.07950  -0.03483 -0.02206 123 ASP C C     
4924 O O     . ASP D 124 ? 0.30540 0.36304 0.30228 0.08971  -0.03930 -0.03006 123 ASP C O     
4925 C CB    . ASP D 124 ? 0.28675 0.29925 0.26320 0.07303  -0.03659 -0.00459 123 ASP C CB    
4926 C CG    . ASP D 124 ? 0.31579 0.31030 0.28226 0.06230  -0.03145 0.00719  123 ASP C CG    
4927 O OD1   . ASP D 124 ? 0.28688 0.29038 0.25536 0.05154  -0.02456 0.00988  123 ASP C OD1   
4928 O OD2   . ASP D 124 ? 0.32051 0.29141 0.27599 0.06544  -0.03462 0.01399  123 ASP C OD2   
4929 N N     . GLY D 125 ? 0.28767 0.38340 0.29074 0.07895  -0.03400 -0.02351 124 GLY C N     
4930 C CA    . GLY D 125 ? 0.27226 0.40042 0.28586 0.09009  -0.03617 -0.03416 124 GLY C CA    
4931 C C     . GLY D 125 ? 0.27993 0.43227 0.29964 0.08699  -0.02943 -0.03926 124 GLY C C     
4932 O O     . GLY D 125 ? 0.31616 0.50201 0.34477 0.09575  -0.02918 -0.04792 124 GLY C O     
4933 N N     . LYS D 126 ? 0.27907 0.41790 0.29402 0.07553  -0.02393 -0.03427 125 LYS C N     
4934 C CA    . LYS D 126 ? 0.23606 0.39631 0.25377 0.07161  -0.01780 -0.03749 125 LYS C CA    
4935 C C     . LYS D 126 ? 0.26043 0.43014 0.27871 0.05365  -0.01092 -0.02707 125 LYS C C     
4936 O O     . LYS D 126 ? 0.28258 0.47864 0.30376 0.04935  -0.00570 -0.02748 125 LYS C O     
4937 C CB    . LYS D 126 ? 0.28133 0.41776 0.29296 0.07517  -0.01947 -0.04246 125 LYS C CB    
4938 C CG    . LYS D 126 ? 0.40565 0.52924 0.41615 0.09294  -0.02810 -0.05406 125 LYS C CG    
4939 C CD    . LYS D 126 ? 0.45874 0.56194 0.46504 0.09442  -0.03065 -0.05979 125 LYS C CD    
4940 C CE    . LYS D 126 ? 0.65425 0.78555 0.66110 0.10500  -0.02999 -0.07319 125 LYS C CE    
4941 N NZ    . LYS D 126 ? 0.58789 0.75635 0.59626 0.09573  -0.01969 -0.06885 125 LYS C NZ    
4942 N N     . HIS D 127 ? 0.22980 0.37878 0.24424 0.04389  -0.01128 -0.01786 126 HIS C N     
4943 C CA    . HIS D 127 ? 0.19740 0.34964 0.21153 0.02822  -0.00728 -0.00877 126 HIS C CA    
4944 C C     . HIS D 127 ? 0.20685 0.35738 0.22210 0.02397  -0.01068 -0.00366 126 HIS C C     
4945 O O     . HIS D 127 ? 0.21426 0.34531 0.22439 0.03041  -0.01489 -0.00390 126 HIS C O     
4946 C CB    . HIS D 127 ? 0.19231 0.31725 0.19906 0.02189  -0.00539 -0.00470 126 HIS C CB    
4947 C CG    . HIS D 127 ? 0.20227 0.32798 0.20799 0.02562  -0.00379 -0.01036 126 HIS C CG    
4948 N ND1   . HIS D 127 ? 0.20883 0.34937 0.21395 0.01892  -0.00007 -0.00874 126 HIS C ND1   
4949 C CD2   . HIS D 127 ? 0.22075 0.33422 0.22527 0.03595  -0.00682 -0.01815 126 HIS C CD2   
4950 C CE1   . HIS D 127 ? 0.20632 0.34514 0.20923 0.02587  -0.00064 -0.01620 126 HIS C CE1   
4951 N NE2   . HIS D 127 ? 0.22600 0.34812 0.22936 0.03608  -0.00514 -0.02257 126 HIS C NE2   
4952 N N     . VAL D 128 ? 0.17341 0.34426 0.19486 0.01317  -0.00975 0.00110  127 VAL C N     
4953 C CA    . VAL D 128 ? 0.18087 0.35192 0.20463 0.00833  -0.01482 0.00472  127 VAL C CA    
4954 C C     . VAL D 128 ? 0.17060 0.31140 0.18384 0.00095  -0.01600 0.01051  127 VAL C C     
4955 O O     . VAL D 128 ? 0.17720 0.31394 0.18893 -0.00974 -0.01391 0.01542  127 VAL C O     
4956 C CB    . VAL D 128 ? 0.16882 0.37338 0.20557 -0.00189 -0.01469 0.00777  127 VAL C CB    
4957 C CG1   . VAL D 128 ? 0.15905 0.35895 0.19812 -0.00800 -0.02239 0.01082  127 VAL C CG1   
4958 C CG2   . VAL D 128 ? 0.18591 0.42685 0.23423 0.00727  -0.01234 0.00098  127 VAL C CG2   
4959 N N     . VAL D 129 ? 0.16427 0.28460 0.16930 0.00759  -0.01986 0.00992  128 VAL C N     
4960 C CA    . VAL D 129 ? 0.18315 0.27904 0.17745 0.00308  -0.02110 0.01405  128 VAL C CA    
4961 C C     . VAL D 129 ? 0.19159 0.29475 0.18891 -0.00470 -0.02759 0.01569  128 VAL C C     
4962 O O     . VAL D 129 ? 0.18991 0.30761 0.19317 -0.00170 -0.03315 0.01325  128 VAL C O     
4963 C CB    . VAL D 129 ? 0.20368 0.27811 0.18643 0.01330  -0.02216 0.01370  128 VAL C CB    
4964 C CG1   . VAL D 129 ? 0.21354 0.26843 0.18409 0.01070  -0.02326 0.01698  128 VAL C CG1   
4965 C CG2   . VAL D 129 ? 0.22490 0.28877 0.20636 0.01795  -0.01686 0.01302  128 VAL C CG2   
4966 N N     . PHE D 130 ? 0.18769 0.27953 0.18137 -0.01419 -0.02843 0.01918  129 PHE C N     
4967 C CA    . PHE D 130 ? 0.21727 0.31306 0.21463 -0.02290 -0.03659 0.02043  129 PHE C CA    
4968 C C     . PHE D 130 ? 0.20809 0.27822 0.19341 -0.02507 -0.04104 0.02078  129 PHE C C     
4969 O O     . PHE D 130 ? 0.22002 0.28874 0.20754 -0.03255 -0.04994 0.02098  129 PHE C O     
4970 C CB    . PHE D 130 ? 0.20534 0.32301 0.21633 -0.03594 -0.03608 0.02480  129 PHE C CB    
4971 C CG    . PHE D 130 ? 0.20436 0.31206 0.21148 -0.04259 -0.03157 0.02925  129 PHE C CG    
4972 C CD1   . PHE D 130 ? 0.19254 0.30502 0.19894 -0.03802 -0.02306 0.02875  129 PHE C CD1   
4973 C CD2   . PHE D 130 ? 0.22314 0.31422 0.22638 -0.05219 -0.03749 0.03302  129 PHE C CD2   
4974 C CE1   . PHE D 130 ? 0.18916 0.29241 0.19138 -0.04330 -0.02016 0.03246  129 PHE C CE1   
4975 C CE2   . PHE D 130 ? 0.21912 0.30018 0.21828 -0.05709 -0.03479 0.03712  129 PHE C CE2   
4976 C CZ    . PHE D 130 ? 0.21370 0.30159 0.21226 -0.05264 -0.02587 0.03703  129 PHE C CZ    
4977 N N     . GLY D 131 ? 0.22001 0.27106 0.19369 -0.01865 -0.03581 0.02031  130 GLY C N     
4978 C CA    . GLY D 131 ? 0.24696 0.27711 0.20890 -0.01797 -0.03981 0.01890  130 GLY C CA    
4979 C C     . GLY D 131 ? 0.21528 0.23140 0.16625 -0.00932 -0.03202 0.01851  130 GLY C C     
4980 O O     . GLY D 131 ? 0.22060 0.24003 0.17273 -0.00457 -0.02481 0.01989  130 GLY C O     
4981 N N     . LYS D 132 ? 0.25067 0.25139 0.19139 -0.00712 -0.03414 0.01632  131 LYS C N     
4982 C CA    . LYS D 132 ? 0.24601 0.23788 0.17796 0.00032  -0.02578 0.01642  131 LYS C CA    
4983 C C     . LYS D 132 ? 0.27373 0.25366 0.19944 0.00142  -0.02839 0.01295  131 LYS C C     
4984 O O     . LYS D 132 ? 0.30120 0.27357 0.22188 0.00080  -0.03849 0.00893  131 LYS C O     
4985 C CB    . LYS D 132 ? 0.29626 0.28479 0.21526 0.00961  -0.02437 0.01633  131 LYS C CB    
4986 C CG    . LYS D 132 ? 0.32794 0.31230 0.24079 0.01496  -0.01360 0.01976  131 LYS C CG    
4987 C CD    . LYS D 132 ? 0.39446 0.37535 0.29296 0.02292  -0.01339 0.02199  131 LYS C CD    
4988 C CE    . LYS D 132 ? 0.46276 0.44017 0.35644 0.02579  -0.00241 0.02862  131 LYS C CE    
4989 N NZ    . LYS D 132 ? 0.48768 0.46320 0.37284 0.02882  0.00390  0.02808  131 LYS C NZ    
4990 N N     . VAL D 133 ? 0.26308 0.24128 0.18974 0.00384  -0.02029 0.01367  132 VAL C N     
4991 C CA    . VAL D 133 ? 0.26294 0.23189 0.18362 0.00828  -0.02206 0.00902  132 VAL C CA    
4992 C C     . VAL D 133 ? 0.31028 0.27270 0.21434 0.01790  -0.02502 0.00389  132 VAL C C     
4993 O O     . VAL D 133 ? 0.32327 0.28946 0.21862 0.02364  -0.01876 0.00597  132 VAL C O     
4994 C CB    . VAL D 133 ? 0.24598 0.21944 0.17246 0.01039  -0.01168 0.01055  132 VAL C CB    
4995 C CG1   . VAL D 133 ? 0.27470 0.24258 0.19497 0.01811  -0.01262 0.00451  132 VAL C CG1   
4996 C CG2   . VAL D 133 ? 0.27852 0.25678 0.21921 0.00212  -0.01105 0.01384  132 VAL C CG2   
4997 N N     . LYS D 134 ? 0.32924 0.28029 0.22733 0.02012  -0.03560 -0.00286 133 LYS C N     
4998 C CA    . LYS D 134 ? 0.35130 0.29460 0.23168 0.03114  -0.04061 -0.01060 133 LYS C CA    
4999 C C     . LYS D 134 ? 0.38601 0.32873 0.26167 0.04085  -0.03490 -0.01563 133 LYS C C     
5000 O O     . LYS D 134 ? 0.47627 0.42836 0.34398 0.04895  -0.02355 -0.01478 133 LYS C O     
5001 C CB    . LYS D 134 ? 0.41423 0.34413 0.29264 0.02730  -0.05827 -0.01618 133 LYS C CB    
5002 C CG    . LYS D 134 ? 0.54463 0.46339 0.40411 0.03887  -0.06781 -0.02668 133 LYS C CG    
5003 C CD    . LYS D 134 ? 0.55717 0.46090 0.41949 0.03148  -0.08728 -0.03128 133 LYS C CD    
5004 C CE    . LYS D 134 ? 0.69347 0.58199 0.53669 0.04368  -0.10037 -0.04440 133 LYS C CE    
5005 N NZ    . LYS D 134 ? 0.71054 0.57893 0.55883 0.03539  -0.12118 -0.04933 133 LYS C NZ    
5006 N N     . GLU D 135 ? 0.40480 0.33783 0.28561 0.04025  -0.04253 -0.02029 134 GLU C N     
5007 C CA    . GLU D 135 ? 0.43141 0.36613 0.31057 0.05070  -0.03824 -0.02631 134 GLU C CA    
5008 C C     . GLU D 135 ? 0.34247 0.28427 0.23929 0.04375  -0.03199 -0.02053 134 GLU C C     
5009 O O     . GLU D 135 ? 0.34448 0.28281 0.25153 0.03190  -0.03624 -0.01455 134 GLU C O     
5010 C CB    . GLU D 135 ? 0.46928 0.38487 0.33973 0.05853  -0.05408 -0.03795 134 GLU C CB    
5011 C CG    . GLU D 135 ? 0.57196 0.47646 0.42514 0.06469  -0.06496 -0.04566 134 GLU C CG    
5012 C CD    . GLU D 135 ? 0.75246 0.66731 0.58790 0.08137  -0.05648 -0.05251 134 GLU C CD    
5013 O OE1   . GLU D 135 ? 0.79424 0.70763 0.62273 0.09528  -0.05783 -0.06303 134 GLU C OE1   
5014 O OE2   . GLU D 135 ? 0.73625 0.66134 0.56387 0.08130  -0.04868 -0.04730 134 GLU C OE2   
5015 N N     . GLY D 136 ? 0.36027 0.31390 0.26060 0.05156  -0.02218 -0.02271 135 GLY C N     
5016 C CA    . GLY D 136 ? 0.32601 0.28545 0.24257 0.04749  -0.01905 -0.02004 135 GLY C CA    
5017 C C     . GLY D 136 ? 0.34212 0.31685 0.27144 0.03872  -0.00651 -0.01050 135 GLY C C     
5018 O O     . GLY D 136 ? 0.29967 0.27676 0.24234 0.03254  -0.00671 -0.00757 135 GLY C O     
5019 N N     . MET D 137 ? 0.30169 0.28546 0.22637 0.03857  0.00341  -0.00572 136 MET C N     
5020 C CA    . MET D 137 ? 0.28488 0.28004 0.22210 0.03091  0.01380  0.00261  136 MET C CA    
5021 C C     . MET D 137 ? 0.27470 0.28337 0.22603 0.03284  0.02091  0.00148  136 MET C C     
5022 O O     . MET D 137 ? 0.28634 0.30048 0.25237 0.02517  0.02409  0.00595  136 MET C O     
5023 C CB    . MET D 137 ? 0.32416 0.32358 0.25237 0.03104  0.02215  0.00887  136 MET C CB    
5024 C CG    . MET D 137 ? 0.33554 0.33933 0.27523 0.02196  0.02859  0.01756  136 MET C CG    
5025 S SD    . MET D 137 ? 0.33414 0.32949 0.28042 0.01316  0.01899  0.01871  136 MET C SD    
5026 C CE    . MET D 137 ? 0.32903 0.33116 0.29242 0.00609  0.02607  0.02413  136 MET C CE    
5027 N N     . ASN D 138 ? 0.28057 0.29603 0.22842 0.04381  0.02261  -0.00559 137 ASN C N     
5028 C CA    . ASN D 138 ? 0.27207 0.30373 0.23637 0.04631  0.02819  -0.00784 137 ASN C CA    
5029 C C     . ASN D 138 ? 0.26777 0.29159 0.24370 0.04274  0.01794  -0.01043 137 ASN C C     
5030 O O     . ASN D 138 ? 0.25945 0.29549 0.25273 0.03978  0.02151  -0.00942 137 ASN C O     
5031 C CB    . ASN D 138 ? 0.33862 0.38207 0.29662 0.06120  0.03168  -0.01655 137 ASN C CB    
5032 C CG    . ASN D 138 ? 0.34023 0.36596 0.28635 0.07159  0.01683  -0.02783 137 ASN C CG    
5033 O OD1   . ASN D 138 ? 0.37900 0.38401 0.31261 0.06867  0.00659  -0.02790 137 ASN C OD1   
5034 N ND2   . ASN D 138 ? 0.43622 0.47014 0.38711 0.08404  0.01470  -0.03779 137 ASN C ND2   
5035 N N     . ILE D 139 ? 0.26745 0.27114 0.23401 0.04229  0.00468  -0.01307 138 ILE C N     
5036 C CA    . ILE D 139 ? 0.28457 0.27935 0.25881 0.03791  -0.00521 -0.01315 138 ILE C CA    
5037 C C     . ILE D 139 ? 0.28630 0.28404 0.26916 0.02524  -0.00215 -0.00485 138 ILE C C     
5038 O O     . ILE D 139 ? 0.25485 0.25688 0.24926 0.02234  -0.00378 -0.00433 138 ILE C O     
5039 C CB    . ILE D 139 ? 0.28865 0.26026 0.24996 0.03933  -0.02040 -0.01640 138 ILE C CB    
5040 C CG1   . ILE D 139 ? 0.33733 0.30399 0.28930 0.05427  -0.02527 -0.02713 138 ILE C CG1   
5041 C CG2   . ILE D 139 ? 0.26431 0.22579 0.23082 0.03407  -0.03043 -0.01412 138 ILE C CG2   
5042 C CD1   . ILE D 139 ? 0.31030 0.28939 0.27253 0.06606  -0.02378 -0.03480 138 ILE C CD1   
5043 N N     . VAL D 140 ? 0.25571 0.25185 0.23274 0.01910  0.00160  0.00061  139 VAL C N     
5044 C CA    . VAL D 140 ? 0.25520 0.25565 0.24018 0.00971  0.00492  0.00666  139 VAL C CA    
5045 C C     . VAL D 140 ? 0.26177 0.27648 0.26138 0.00886  0.01394  0.00772  139 VAL C C     
5046 O O     . VAL D 140 ? 0.23640 0.25438 0.24675 0.00377  0.01276  0.00870  139 VAL C O     
5047 C CB    . VAL D 140 ? 0.28383 0.28096 0.26027 0.00590  0.00674  0.01103  139 VAL C CB    
5048 C CG1   . VAL D 140 ? 0.27381 0.27543 0.25833 -0.00137 0.00936  0.01540  139 VAL C CG1   
5049 C CG2   . VAL D 140 ? 0.26859 0.25407 0.23385 0.00512  -0.00296 0.01000  139 VAL C CG2   
5050 N N     . GLU D 141 ? 0.25148 0.27582 0.25179 0.01336  0.02283  0.00776  140 GLU C N     
5051 C CA    . GLU D 141 ? 0.26022 0.29992 0.27719 0.01037  0.03143  0.01008  140 GLU C CA    
5052 C C     . GLU D 141 ? 0.24378 0.29179 0.27562 0.01275  0.02727  0.00445  140 GLU C C     
5053 O O     . GLU D 141 ? 0.25306 0.30932 0.30133 0.00702  0.02861  0.00565  140 GLU C O     
5054 C CB    . GLU D 141 ? 0.27648 0.32772 0.29011 0.01416  0.04274  0.01281  140 GLU C CB    
5055 C CG    . GLU D 141 ? 0.28265 0.32454 0.28114 0.01168  0.04584  0.01946  140 GLU C CG    
5056 C CD    . GLU D 141 ? 0.46846 0.51873 0.45537 0.01759  0.05528  0.02209  140 GLU C CD    
5057 O OE1   . GLU D 141 ? 0.41566 0.48087 0.40572 0.02472  0.06003  0.01762  140 GLU C OE1   
5058 O OE2   . GLU D 141 ? 0.38704 0.42969 0.36051 0.01629  0.05748  0.02819  140 GLU C OE2   
5059 N N     . ALA D 142 ? 0.25134 0.29517 0.27728 0.02154  0.02019  -0.00226 141 ALA C N     
5060 C CA    . ALA D 142 ? 0.24838 0.29759 0.28658 0.02560  0.01373  -0.00801 141 ALA C CA    
5061 C C     . ALA D 142 ? 0.26040 0.29994 0.30095 0.01845  0.00504  -0.00602 141 ALA C C     
5062 O O     . ALA D 142 ? 0.29866 0.34717 0.35404 0.01734  0.00280  -0.00804 141 ALA C O     
5063 C CB    . ALA D 142 ? 0.26855 0.30984 0.29682 0.03774  0.00559  -0.01573 141 ALA C CB    
5064 N N     . MET D 143 ? 0.22913 0.25263 0.25531 0.01387  -0.00004 -0.00234 142 MET C N     
5065 C CA    . MET D 143 ? 0.22661 0.24393 0.25233 0.00749  -0.00685 0.00016  142 MET C CA    
5066 C C     . MET D 143 ? 0.27267 0.30003 0.31061 0.00124  -0.00144 0.00187  142 MET C C     
5067 O O     . MET D 143 ? 0.26147 0.29085 0.30553 -0.00079 -0.00657 0.00046  142 MET C O     
5068 C CB    . MET D 143 ? 0.24685 0.25139 0.25711 0.00266  -0.01022 0.00476  142 MET C CB    
5069 C CG    . MET D 143 ? 0.27615 0.26588 0.27384 0.00605  -0.01900 0.00390  142 MET C CG    
5070 S SD    . MET D 143 ? 0.31924 0.29948 0.30347 -0.00072 -0.02071 0.00915  142 MET C SD    
5071 C CE    . MET D 143 ? 0.30265 0.28930 0.28948 -0.01001 -0.02072 0.01483  142 MET C CE    
5072 N N     . GLU D 144 ? 0.30035 0.33210 0.34060 -0.00157 0.00770  0.00488  143 GLU C N     
5073 C CA    . GLU D 144 ? 0.33432 0.37064 0.38508 -0.00785 0.01122  0.00676  143 GLU C CA    
5074 C C     . GLU D 144 ? 0.28543 0.33365 0.35580 -0.00872 0.01030  0.00318  143 GLU C C     
5075 O O     . GLU D 144 ? 0.32086 0.36933 0.39930 -0.01336 0.00719  0.00208  143 GLU C O     
5076 C CB    . GLU D 144 ? 0.31702 0.35342 0.36543 -0.00992 0.02036  0.01187  143 GLU C CB    
5077 C CG    . GLU D 144 ? 0.39833 0.43140 0.45190 -0.01621 0.02200  0.01499  143 GLU C CG    
5078 C CD    . GLU D 144 ? 0.33165 0.36250 0.38043 -0.01754 0.03014  0.02158  143 GLU C CD    
5079 O OE1   . GLU D 144 ? 0.39582 0.43315 0.44145 -0.01416 0.03622  0.02326  143 GLU C OE1   
5080 O OE2   . GLU D 144 ? 0.41098 0.43341 0.45770 -0.02080 0.02999  0.02484  143 GLU C OE2   
5081 N N     . ARG D 145 ? 0.28952 0.34837 0.36816 -0.00341 0.01158  0.00005  144 ARG C N     
5082 C CA    . ARG D 145 ? 0.32687 0.40087 0.42733 -0.00420 0.01028  -0.00382 144 ARG C CA    
5083 C C     . ARG D 145 ? 0.32748 0.39771 0.42892 -0.00218 -0.00194 -0.00888 144 ARG C C     
5084 O O     . ARG D 145 ? 0.30494 0.38620 0.42444 -0.00379 -0.00541 -0.01270 144 ARG C O     
5085 C CB    . ARG D 145 ? 0.33322 0.42482 0.44398 0.00202  0.01654  -0.00612 144 ARG C CB    
5086 C CG    . ARG D 145 ? 0.39308 0.48605 0.49470 0.00185  0.02810  -0.00057 144 ARG C CG    
5087 C CD    . ARG D 145 ? 0.47499 0.59251 0.58975 0.00604  0.03821  -0.00138 144 ARG C CD    
5088 N NE    . ARG D 145 ? 0.55124 0.66652 0.64772 0.01195  0.04547  0.00074  144 ARG C NE    
5089 C CZ    . ARG D 145 ? 0.50352 0.61806 0.58853 0.02469  0.04263  -0.00619 144 ARG C CZ    
5090 N NH1   . ARG D 145 ? 0.44780 0.56512 0.53924 0.03331  0.03362  -0.01497 144 ARG C NH1   
5091 N NH2   . ARG D 145 ? 0.45126 0.56058 0.51707 0.02975  0.04749  -0.00485 144 ARG C NH2   
5092 N N     . PHE D 146 ? 0.28205 0.33734 0.36443 0.00052  -0.00906 -0.00832 145 PHE C N     
5093 C CA    . PHE D 146 ? 0.24641 0.29709 0.32544 0.00175  -0.02029 -0.01096 145 PHE C CA    
5094 C C     . PHE D 146 ? 0.22554 0.27221 0.30021 -0.00437 -0.02204 -0.00990 145 PHE C C     
5095 O O     . PHE D 146 ? 0.26092 0.30539 0.33069 -0.00331 -0.03075 -0.01202 145 PHE C O     
5096 C CB    . PHE D 146 ? 0.23323 0.26971 0.29350 0.00648  -0.02775 -0.00920 145 PHE C CB    
5097 C CG    . PHE D 146 ? 0.21649 0.25431 0.28003 0.01551  -0.03007 -0.01304 145 PHE C CG    
5098 C CD1   . PHE D 146 ? 0.29800 0.34170 0.37144 0.02244  -0.03849 -0.01863 145 PHE C CD1   
5099 C CD2   . PHE D 146 ? 0.25586 0.28950 0.31213 0.01867  -0.02489 -0.01230 145 PHE C CD2   
5100 C CE1   . PHE D 146 ? 0.30308 0.34924 0.38018 0.03327  -0.04133 -0.02392 145 PHE C CE1   
5101 C CE2   . PHE D 146 ? 0.33875 0.37400 0.39697 0.02927  -0.02769 -0.01788 145 PHE C CE2   
5102 C CZ    . PHE D 146 ? 0.29817 0.34007 0.36733 0.03694  -0.03574 -0.02390 145 PHE C CZ    
5103 N N     . GLY D 147 ? 0.23266 0.27826 0.30777 -0.00945 -0.01467 -0.00718 146 GLY C N     
5104 C CA    . GLY D 147 ? 0.21497 0.25654 0.28532 -0.01291 -0.01674 -0.00787 146 GLY C CA    
5105 C C     . GLY D 147 ? 0.21242 0.25949 0.30073 -0.01608 -0.01915 -0.01281 146 GLY C C     
5106 O O     . GLY D 147 ? 0.22368 0.28031 0.33006 -0.01664 -0.02003 -0.01542 146 GLY C O     
5107 N N     . SER D 148 ? 0.19978 0.24136 0.28373 -0.01779 -0.02132 -0.01491 147 SER C N     
5108 C CA    . SER D 148 ? 0.21867 0.26105 0.31785 -0.02080 -0.02660 -0.02090 147 SER C CA    
5109 C C     . SER D 148 ? 0.22500 0.25742 0.31690 -0.02137 -0.02669 -0.02211 147 SER C C     
5110 O O     . SER D 148 ? 0.20331 0.23178 0.27928 -0.01890 -0.02257 -0.01866 147 SER C O     
5111 C CB    . SER D 148 ? 0.20523 0.25202 0.30460 -0.01706 -0.03769 -0.02836 147 SER C CB    
5112 O OG    . SER D 148 ? 0.22707 0.27014 0.30463 -0.01242 -0.04113 -0.02949 147 SER C OG    
5113 N N     . ARG D 149 ? 0.22551 0.25389 0.33015 -0.02413 -0.03293 -0.02799 148 ARG C N     
5114 C CA    . ARG D 149 ? 0.22090 0.23706 0.32058 -0.02329 -0.03538 -0.03097 148 ARG C CA    
5115 C C     . ARG D 149 ? 0.24282 0.25950 0.32072 -0.01473 -0.03788 -0.03549 148 ARG C C     
5116 O O     . ARG D 149 ? 0.26385 0.27464 0.33247 -0.01181 -0.03522 -0.03468 148 ARG C O     
5117 C CB    . ARG D 149 ? 0.25419 0.26444 0.37121 -0.02705 -0.04549 -0.03874 148 ARG C CB    
5118 C CG    . ARG D 149 ? 0.27246 0.26655 0.38497 -0.02454 -0.05160 -0.04438 148 ARG C CG    
5119 C CD    . ARG D 149 ? 0.27379 0.25761 0.40733 -0.03138 -0.06212 -0.05005 148 ARG C CD    
5120 N NE    . ARG D 149 ? 0.27156 0.23599 0.39886 -0.02711 -0.07007 -0.05669 148 ARG C NE    
5121 C CZ    . ARG D 149 ? 0.27281 0.22264 0.39739 -0.02892 -0.06593 -0.04966 148 ARG C CZ    
5122 N NH1   . ARG D 149 ? 0.30360 0.25622 0.43167 -0.03623 -0.05370 -0.03537 148 ARG C NH1   
5123 N NH2   . ARG D 149 ? 0.30227 0.23435 0.41887 -0.02174 -0.07487 -0.05772 148 ARG C NH2   
5124 N N     . ASN D 150 ? 0.22898 0.25415 0.29859 -0.01038 -0.04308 -0.03998 149 ASN C N     
5125 C CA    . ASN D 150 ? 0.22832 0.25854 0.27699 -0.00321 -0.04401 -0.04277 149 ASN C CA    
5126 C C     . ASN D 150 ? 0.25297 0.29021 0.28846 -0.00380 -0.03675 -0.03325 149 ASN C C     
5127 O O     . ASN D 150 ? 0.26838 0.31364 0.28730 0.00007  -0.03688 -0.03320 149 ASN C O     
5128 C CB    . ASN D 150 ? 0.26164 0.29641 0.30448 0.00247  -0.05454 -0.05304 149 ASN C CB    
5129 C CG    . ASN D 150 ? 0.26661 0.30789 0.30920 0.00162  -0.05814 -0.05090 149 ASN C CG    
5130 O OD1   . ASN D 150 ? 0.25524 0.29762 0.30255 -0.00254 -0.05319 -0.04252 149 ASN C OD1   
5131 N ND2   . ASN D 150 ? 0.32501 0.37014 0.36090 0.00706  -0.06823 -0.05954 149 ASN C ND2   
5132 N N     . GLY D 151 ? 0.20338 0.23854 0.24571 -0.00867 -0.03105 -0.02535 150 GLY C N     
5133 C CA    . GLY D 151 ? 0.20089 0.23876 0.23187 -0.00967 -0.02616 -0.01702 150 GLY C CA    
5134 C C     . GLY D 151 ? 0.20535 0.24590 0.23083 -0.00923 -0.03076 -0.01480 150 GLY C C     
5135 O O     . GLY D 151 ? 0.21405 0.25280 0.23223 -0.01089 -0.02834 -0.00769 150 GLY C O     
5136 N N     . LYS D 152 ? 0.21020 0.25328 0.23827 -0.00667 -0.03879 -0.02081 151 LYS C N     
5137 C CA    . LYS D 152 ? 0.22087 0.26443 0.24229 -0.00521 -0.04463 -0.01804 151 LYS C CA    
5138 C C     . LYS D 152 ? 0.23965 0.28020 0.27394 -0.00618 -0.04335 -0.01549 151 LYS C C     
5139 O O     . LYS D 152 ? 0.21955 0.26220 0.27225 -0.00768 -0.04043 -0.01859 151 LYS C O     
5140 C CB    . LYS D 152 ? 0.26716 0.31450 0.28810 -0.00099 -0.05488 -0.02582 151 LYS C CB    
5141 C CG    . LYS D 152 ? 0.35633 0.40900 0.36035 0.00258  -0.05696 -0.02968 151 LYS C CG    
5142 C CD    . LYS D 152 ? 0.39495 0.45131 0.37684 0.00139  -0.05300 -0.01980 151 LYS C CD    
5143 C CE    . LYS D 152 ? 0.48488 0.55247 0.44921 0.00613  -0.05405 -0.02380 151 LYS C CE    
5144 N NZ    . LYS D 152 ? 0.51174 0.58754 0.45793 0.00266  -0.04770 -0.01259 151 LYS C NZ    
5145 N N     . THR D 153 ? 0.24978 0.28565 0.27401 -0.00523 -0.04566 -0.00958 152 THR C N     
5146 C CA    . THR D 153 ? 0.25664 0.28943 0.28977 -0.00354 -0.04513 -0.00832 152 THR C CA    
5147 C C     . THR D 153 ? 0.28204 0.31647 0.32106 0.00193  -0.05527 -0.01243 152 THR C C     
5148 O O     . THR D 153 ? 0.29736 0.33014 0.32518 0.00400  -0.06386 -0.01250 152 THR C O     
5149 C CB    . THR D 153 ? 0.23628 0.25926 0.25524 -0.00499 -0.04308 -0.00043 152 THR C CB    
5150 O OG1   . THR D 153 ? 0.29773 0.31416 0.29923 -0.00537 -0.05071 0.00494  152 THR C OG1   
5151 C CG2   . THR D 153 ? 0.24706 0.27082 0.26143 -0.00969 -0.03442 0.00281  152 THR C CG2   
5152 N N     . SER D 154 ? 0.27061 0.31074 0.32785 0.00490  -0.05406 -0.01625 153 SER C N     
5153 C CA    . SER D 154 ? 0.27388 0.31916 0.34127 0.01145  -0.06378 -0.02166 153 SER C CA    
5154 C C     . SER D 154 ? 0.25550 0.28864 0.30934 0.01783  -0.07163 -0.01824 153 SER C C     
5155 O O     . SER D 154 ? 0.28908 0.32239 0.34464 0.02449  -0.08288 -0.02166 153 SER C O     
5156 C CB    . SER D 154 ? 0.30211 0.36347 0.39725 0.01204  -0.05865 -0.02738 153 SER C CB    
5157 O OG    . SER D 154 ? 0.27994 0.34147 0.37650 0.01261  -0.04901 -0.02440 153 SER C OG    
5158 N N     . LYS D 155 ? 0.27832 0.29970 0.31933 0.01624  -0.06739 -0.01204 154 LYS C N     
5159 C CA    . LYS D 155 ? 0.27041 0.27427 0.29550 0.02034  -0.07622 -0.00745 154 LYS C CA    
5160 C C     . LYS D 155 ? 0.26212 0.25423 0.26793 0.01188  -0.07257 0.00213  154 LYS C C     
5161 O O     . LYS D 155 ? 0.28776 0.28706 0.29562 0.00573  -0.06217 0.00319  154 LYS C O     
5162 C CB    . LYS D 155 ? 0.26361 0.26645 0.29799 0.02878  -0.07628 -0.01237 154 LYS C CB    
5163 C CG    . LYS D 155 ? 0.34438 0.36413 0.40061 0.03753  -0.07966 -0.02198 154 LYS C CG    
5164 C CD    . LYS D 155 ? 0.30586 0.32744 0.37000 0.04882  -0.08089 -0.02817 154 LYS C CD    
5165 C CE    . LYS D 155 ? 0.35861 0.39938 0.44482 0.05840  -0.08663 -0.03763 154 LYS C CE    
5166 N NZ    . LYS D 155 ? 0.42621 0.47214 0.52037 0.07206  -0.08806 -0.04531 154 LYS C NZ    
5167 N N     . LYS D 156 ? 0.28055 0.25478 0.26860 0.01130  -0.08187 0.00947  155 LYS C N     
5168 C CA    . LYS D 156 ? 0.29584 0.26122 0.26747 0.00154  -0.07931 0.01981  155 LYS C CA    
5169 C C     . LYS D 156 ? 0.28576 0.24379 0.25948 0.00079  -0.07498 0.01949  155 LYS C C     
5170 O O     . LYS D 156 ? 0.31467 0.25823 0.28703 0.00696  -0.08267 0.01748  155 LYS C O     
5171 C CB    . LYS D 156 ? 0.38363 0.33141 0.33581 -0.00095 -0.09147 0.02985  155 LYS C CB    
5172 C CG    . LYS D 156 ? 0.47005 0.42475 0.41343 -0.00114 -0.09570 0.03244  155 LYS C CG    
5173 C CD    . LYS D 156 ? 0.51222 0.44674 0.43550 -0.00250 -0.10904 0.04350  155 LYS C CD    
5174 C CE    . LYS D 156 ? 0.57358 0.51490 0.48661 0.00019  -0.11477 0.04482  155 LYS C CE    
5175 N NZ    . LYS D 156 ? 0.69967 0.61857 0.59727 0.00407  -0.13117 0.05224  155 LYS C NZ    
5176 N N     . ILE D 157 ? 0.25676 0.22380 0.23248 -0.00553 -0.06406 0.02074  156 ILE C N     
5177 C CA    . ILE D 157 ? 0.27797 0.24002 0.25461 -0.00611 -0.05964 0.01996  156 ILE C CA    
5178 C C     . ILE D 157 ? 0.27905 0.23177 0.24213 -0.01628 -0.06206 0.02993  156 ILE C C     
5179 O O     . ILE D 157 ? 0.27763 0.24199 0.23812 -0.02367 -0.05614 0.03469  156 ILE C O     
5180 C CB    . ILE D 157 ? 0.25345 0.23203 0.24192 -0.00604 -0.04676 0.01511  156 ILE C CB    
5181 C CG1   . ILE D 157 ? 0.26968 0.26090 0.27406 0.00041  -0.04428 0.00736  156 ILE C CG1   
5182 C CG2   . ILE D 157 ? 0.27920 0.25284 0.26632 -0.00507 -0.04288 0.01403  156 ILE C CG2   
5183 C CD1   . ILE D 157 ? 0.29968 0.28889 0.31157 0.01044  -0.04858 0.00093  156 ILE C CD1   
5184 N N     . THR D 158 ? 0.29992 0.23256 0.25516 -0.01670 -0.07138 0.03279  157 THR C N     
5185 C CA    . THR D 158 ? 0.31417 0.23755 0.25839 -0.02871 -0.07556 0.04385  157 THR C CA    
5186 C C     . THR D 158 ? 0.31873 0.22949 0.26190 -0.02996 -0.07848 0.04232  157 THR C C     
5187 O O     . THR D 158 ? 0.31515 0.21967 0.26202 -0.01967 -0.07972 0.03274  157 THR C O     
5188 C CB    . THR D 158 ? 0.37306 0.27814 0.30525 -0.03183 -0.08872 0.05257  157 THR C CB    
5189 O OG1   . THR D 158 ? 0.37052 0.25379 0.30184 -0.02158 -0.10046 0.04650  157 THR C OG1   
5190 C CG2   . THR D 158 ? 0.33560 0.25376 0.26568 -0.03043 -0.08693 0.05440  157 THR C CG2   
5191 N N     . ILE D 159 ? 0.32341 0.23227 0.26144 -0.04271 -0.07990 0.05175  158 ILE C N     
5192 C CA    . ILE D 159 ? 0.32868 0.22308 0.26478 -0.04629 -0.08610 0.05151  158 ILE C CA    
5193 C C     . ILE D 159 ? 0.39404 0.25851 0.32048 -0.04943 -0.10313 0.05731  158 ILE C C     
5194 O O     . ILE D 159 ? 0.43206 0.29095 0.35259 -0.06340 -0.10838 0.07071  158 ILE C O     
5195 C CB    . ILE D 159 ? 0.30912 0.21922 0.24793 -0.05896 -0.07976 0.05831  158 ILE C CB    
5196 C CG1   . ILE D 159 ? 0.31305 0.24975 0.26020 -0.05372 -0.06455 0.05222  158 ILE C CG1   
5197 C CG2   . ILE D 159 ? 0.34768 0.24367 0.28586 -0.06299 -0.08761 0.05706  158 ILE C CG2   
5198 C CD1   . ILE D 159 ? 0.32190 0.27894 0.27299 -0.06314 -0.05750 0.05736  158 ILE C CD1   
5199 N N     . ALA D 160 ? 0.36733 0.21297 0.29200 -0.03600 -0.11202 0.04757  159 ALA C N     
5200 C CA    . ALA D 160 ? 0.39681 0.20956 0.31156 -0.03622 -0.13068 0.05160  159 ALA C CA    
5201 C C     . ALA D 160 ? 0.43897 0.22973 0.34888 -0.04704 -0.14219 0.05651  159 ALA C C     
5202 O O     . ALA D 160 ? 0.45156 0.22424 0.35552 -0.05480 -0.15423 0.06353  159 ALA C O     
5203 C CB    . ALA D 160 ? 0.44102 0.24178 0.35636 -0.01629 -0.13758 0.03742  159 ALA C CB    
5204 N N     . ASP D 161 ? 0.40463 0.20409 0.31958 -0.04720 -0.13688 0.04991  160 ASP C N     
5205 C CA    . ASP D 161 ? 0.42802 0.21112 0.34101 -0.05898 -0.14744 0.05396  160 ASP C CA    
5206 C C     . ASP D 161 ? 0.37422 0.18342 0.29525 -0.06120 -0.13440 0.04982  160 ASP C C     
5207 O O     . ASP D 161 ? 0.38619 0.21720 0.31168 -0.05028 -0.12037 0.04150  160 ASP C O     
5208 C CB    . ASP D 161 ? 0.49841 0.24948 0.40468 -0.04762 -0.16502 0.04255  160 ASP C CB    
5209 C CG    . ASP D 161 ? 0.57846 0.31881 0.48424 -0.05953 -0.17714 0.04653  160 ASP C CG    
5210 O OD1   . ASP D 161 ? 0.52537 0.27887 0.43579 -0.07794 -0.17418 0.06059  160 ASP C OD1   
5211 O OD2   . ASP D 161 ? 0.60407 0.32438 0.50501 -0.04905 -0.18985 0.03529  160 ASP C OD2   
5212 N N     . CYS D 162 ? 0.40252 0.20960 0.32609 -0.07636 -0.13977 0.05676  161 CYS C N     
5213 C CA    . CYS D 162 ? 0.38268 0.21379 0.31402 -0.07908 -0.12990 0.05362  161 CYS C CA    
5214 C C     . CYS D 162 ? 0.39957 0.21841 0.33353 -0.09389 -0.14315 0.05837  161 CYS C C     
5215 O O     . CYS D 162 ? 0.43257 0.23901 0.36468 -0.10146 -0.15347 0.06654  161 CYS C O     
5216 C CB    . CYS D 162 ? 0.34930 0.21674 0.28841 -0.08436 -0.11163 0.06053  161 CYS C CB    
5217 S SG    . CYS D 162 ? 0.39352 0.27186 0.33389 -0.10402 -0.11019 0.08028  161 CYS C SG    
5218 N N     . GLY D 163 ? 0.40455 0.23687 0.34342 -0.09204 -0.13977 0.05125  162 GLY C N     
5219 C CA    . GLY D 163 ? 0.41244 0.23993 0.35629 -0.10332 -0.15073 0.05408  162 GLY C CA    
5220 C C     . GLY D 163 ? 0.38910 0.22290 0.33394 -0.09626 -0.15098 0.04133  162 GLY C C     
5221 O O     . GLY D 163 ? 0.38118 0.23446 0.32457 -0.08278 -0.13632 0.03434  162 GLY C O     
5222 N N     . GLN D 164 ? 0.39625 0.21973 0.34281 -0.09891 -0.16260 0.03932  163 GLN C N     
5223 C CA    . GLN D 164 ? 0.38995 0.22062 0.33723 -0.09310 -0.16443 0.02841  163 GLN C CA    
5224 C C     . GLN D 164 ? 0.43353 0.23518 0.36702 -0.07639 -0.17717 0.01325  163 GLN C C     
5225 O O     . GLN D 164 ? 0.51549 0.29152 0.44520 -0.07560 -0.18991 0.01400  163 GLN C O     
5226 C CB    . GLN D 164 ? 0.40075 0.24802 0.36282 -0.10840 -0.16650 0.03676  163 GLN C CB    
5227 C CG    . GLN D 164 ? 0.41261 0.27387 0.37738 -0.10300 -0.16684 0.02669  163 GLN C CG    
5228 C CD    . GLN D 164 ? 0.40297 0.28873 0.38596 -0.11824 -0.16600 0.03505  163 GLN C CD    
5229 O OE1   . GLN D 164 ? 0.41352 0.30817 0.40670 -0.13332 -0.16360 0.04907  163 GLN C OE1   
5230 N NE2   . GLN D 164 ? 0.40870 0.30633 0.39495 -0.11346 -0.16838 0.02627  163 GLN C NE2   
5231 N N     . LEU D 165 ? 0.45816 0.26585 0.38281 -0.06180 -0.17374 -0.00036 164 LEU C N     
5232 C CA    . LEU D 165 ? 0.47144 0.25815 0.38192 -0.04387 -0.18349 -0.01575 164 LEU C CA    
5233 C C     . LEU D 165 ? 0.60165 0.39097 0.51589 -0.04654 -0.19145 -0.01927 164 LEU C C     
5234 O O     . LEU D 165 ? 0.58814 0.40151 0.50744 -0.04987 -0.18439 -0.01850 164 LEU C O     
5235 C CB    . LEU D 165 ? 0.48077 0.27504 0.37634 -0.02411 -0.17325 -0.02787 164 LEU C CB    
5236 C CG    . LEU D 165 ? 0.50597 0.30211 0.40080 -0.01713 -0.16159 -0.02497 164 LEU C CG    
5237 C CD1   . LEU D 165 ? 0.52244 0.33752 0.40935 0.00139  -0.14378 -0.03193 164 LEU C CD1   
5238 C CD2   . LEU D 165 ? 0.57228 0.33453 0.46008 -0.01243 -0.17895 -0.03084 164 LEU C CD2   
5239 P PG    . GNP E .   ? 0.18714 0.18935 0.25167 -0.04849 0.03337  0.00734  201 GNP A PG    
5240 O O1G   . GNP E .   ? 0.21210 0.19829 0.26569 -0.04125 0.03229  0.00779  201 GNP A O1G   
5241 O O2G   . GNP E .   ? 0.20864 0.22861 0.27840 -0.04208 0.03334  0.00745  201 GNP A O2G   
5242 O O3G   . GNP E .   ? 0.22717 0.22590 0.29247 -0.05605 0.03931  0.01251  201 GNP A O3G   
5243 N N3B   . GNP E .   ? 0.18276 0.18616 0.25173 -0.05531 0.02814  0.00126  201 GNP A N3B   
5244 P PB    . GNP E .   ? 0.16814 0.16944 0.23243 -0.05131 0.02197  -0.00436 201 GNP A PB    
5245 O O1B   . GNP E .   ? 0.17945 0.16480 0.23375 -0.04443 0.02277  -0.00449 201 GNP A O1B   
5246 O O2B   . GNP E .   ? 0.16589 0.18530 0.23604 -0.04772 0.01763  -0.00480 201 GNP A O2B   
5247 O O3A   . GNP E .   ? 0.19165 0.18749 0.25618 -0.06183 0.01960  -0.00994 201 GNP A O3A   
5248 P PA    . GNP E .   ? 0.19024 0.16394 0.24569 -0.06486 0.02020  -0.01528 201 GNP A PA    
5249 O O1A   . GNP E .   ? 0.20744 0.16407 0.26068 -0.06514 0.02545  -0.01102 201 GNP A O1A   
5250 O O2A   . GNP E .   ? 0.20866 0.17936 0.25640 -0.05755 0.01805  -0.01903 201 GNP A O2A   
5251 O "O5'" . GNP E .   ? 0.20091 0.17945 0.26000 -0.07752 0.01655  -0.02106 201 GNP A "O5'" 
5252 C "C5'" . GNP E .   ? 0.19435 0.17890 0.26294 -0.08790 0.01804  -0.01839 201 GNP A "C5'" 
5253 C "C4'" . GNP E .   ? 0.23037 0.20805 0.29770 -0.10086 0.01488  -0.02589 201 GNP A "C4'" 
5254 O "O4'" . GNP E .   ? 0.21266 0.20466 0.27870 -0.10182 0.00765  -0.03154 201 GNP A "O4'" 
5255 C "C3'" . GNP E .   ? 0.26073 0.20823 0.31620 -0.10179 0.01737  -0.03158 201 GNP A "C3'" 
5256 O "O3'" . GNP E .   ? 0.28411 0.22259 0.34006 -0.11271 0.01591  -0.03369 201 GNP A "O3'" 
5257 C "C2'" . GNP E .   ? 0.27397 0.22219 0.32004 -0.09721 0.01336  -0.03967 201 GNP A "C2'" 
5258 O "O2'" . GNP E .   ? 0.29664 0.22320 0.33251 -0.10150 0.01396  -0.04927 201 GNP A "O2'" 
5259 C "C1'" . GNP E .   ? 0.21568 0.18999 0.26860 -0.10366 0.00638  -0.04047 201 GNP A "C1'" 
5260 N N9    . GNP E .   ? 0.22901 0.21373 0.27533 -0.09691 0.00195  -0.04268 201 GNP A N9    
5261 C C8    . GNP E .   ? 0.21772 0.20649 0.26204 -0.08439 0.00329  -0.03782 201 GNP A C8    
5262 N N7    . GNP E .   ? 0.20303 0.20000 0.24031 -0.08218 -0.00136 -0.04022 201 GNP A N7    
5263 C C5    . GNP E .   ? 0.22621 0.22553 0.25966 -0.09341 -0.00640 -0.04743 201 GNP A C5    
5264 C C6    . GNP E .   ? 0.27587 0.28355 0.29931 -0.09697 -0.01305 -0.05222 201 GNP A C6    
5265 O O6    . GNP E .   ? 0.26695 0.28116 0.28302 -0.09079 -0.01533 -0.05006 201 GNP A O6    
5266 N N1    . GNP E .   ? 0.27833 0.28589 0.29952 -0.11025 -0.01751 -0.05990 201 GNP A N1    
5267 C C2    . GNP E .   ? 0.26091 0.26014 0.28962 -0.11926 -0.01550 -0.06222 201 GNP A C2    
5268 N N2    . GNP E .   ? 0.31077 0.31010 0.33559 -0.12780 -0.02099 -0.06775 201 GNP A N2    
5269 N N3    . GNP E .   ? 0.26577 0.25625 0.30395 -0.11648 -0.00867 -0.05681 201 GNP A N3    
5270 C C4    . GNP E .   ? 0.21763 0.20926 0.25713 -0.10288 -0.00458 -0.04956 201 GNP A C4    
5346 P PG    . GNP I .   ? 0.17202 0.29145 0.20316 -0.03396 -0.01854 -0.01920 201 GNP B PG    
5347 O O1G   . GNP I .   ? 0.20125 0.29220 0.22376 -0.02983 -0.01783 -0.01478 201 GNP B O1G   
5348 O O2G   . GNP I .   ? 0.20824 0.34729 0.24382 -0.01922 -0.02375 -0.01465 201 GNP B O2G   
5349 O O3G   . GNP I .   ? 0.20740 0.34418 0.23927 -0.04711 -0.01864 -0.02943 201 GNP B O3G   
5350 N N3B   . GNP I .   ? 0.17146 0.27972 0.20411 -0.04048 -0.01235 -0.01839 201 GNP B N3B   
5351 P PB    . GNP I .   ? 0.16098 0.24610 0.18990 -0.03240 -0.01056 -0.01003 201 GNP B PB    
5352 O O1B   . GNP I .   ? 0.16817 0.22754 0.18975 -0.02764 -0.01143 -0.00572 201 GNP B O1B   
5353 O O2B   . GNP I .   ? 0.17342 0.27327 0.20840 -0.02190 -0.01231 -0.00665 201 GNP B O2B   
5354 O O3A   . GNP I .   ? 0.19177 0.26424 0.21625 -0.04453 -0.00342 -0.01194 201 GNP B O3A   
5355 P PA    . GNP I .   ? 0.19216 0.23036 0.20349 -0.05062 0.00167  -0.00998 201 GNP B PA    
5356 O O1A   . GNP I .   ? 0.20621 0.23648 0.21325 -0.05781 0.00304  -0.01513 201 GNP B O1A   
5357 O O2A   . GNP I .   ? 0.20727 0.22796 0.21416 -0.03894 -0.00114 -0.00217 201 GNP B O2A   
5358 O "O5'" . GNP I .   ? 0.19270 0.23113 0.20106 -0.06251 0.00949  -0.01245 201 GNP B "O5'" 
5359 C "C5'" . GNP I .   ? 0.19445 0.25343 0.20871 -0.07725 0.01393  -0.02172 201 GNP B "C5'" 
5360 C "C4'" . GNP I .   ? 0.23192 0.27367 0.23583 -0.09129 0.02469  -0.02309 201 GNP B "C4'" 
5361 O "O4'" . GNP I .   ? 0.23795 0.28065 0.24124 -0.08535 0.02612  -0.01756 201 GNP B "O4'" 
5362 C "C3'" . GNP I .   ? 0.27139 0.26935 0.25524 -0.09440 0.03016  -0.01922 201 GNP B "C3'" 
5363 O "O3'" . GNP I .   ? 0.27868 0.26359 0.25269 -0.11357 0.04194  -0.02516 201 GNP B "O3'" 
5364 C "C2'" . GNP I .   ? 0.26698 0.24649 0.24181 -0.08207 0.02868  -0.00873 201 GNP B "C2'" 
5365 O "O2'" . GNP I .   ? 0.30602 0.24754 0.25960 -0.08514 0.03588  -0.00389 201 GNP B "O2'" 
5366 C "C1'" . GNP I .   ? 0.23859 0.24431 0.22285 -0.08470 0.03062  -0.01051 201 GNP B "C1'" 
5367 N N9    . GNP I .   ? 0.23173 0.23584 0.21484 -0.07062 0.02577  -0.00313 201 GNP B N9    
5368 C C8    . GNP I .   ? 0.21111 0.21937 0.20026 -0.05565 0.01633  0.00075  201 GNP B C8    
5369 N N7    . GNP I .   ? 0.22052 0.22502 0.20574 -0.04753 0.01461  0.00553  201 GNP B N7    
5370 C C5    . GNP I .   ? 0.23566 0.23330 0.21094 -0.05649 0.02311  0.00556  201 GNP B C5    
5371 C C6    . GNP I .   ? 0.28599 0.27727 0.25147 -0.05378 0.02569  0.00924  201 GNP B C6    
5372 O O6    . GNP I .   ? 0.26285 0.25385 0.22710 -0.04320 0.02037  0.01240  201 GNP B O6    
5373 N N1    . GNP I .   ? 0.26338 0.24726 0.21826 -0.06659 0.03660  0.00806  201 GNP B N1    
5374 C C2    . GNP I .   ? 0.29703 0.27946 0.25158 -0.08163 0.04460  0.00312  201 GNP B C2    
5375 N N2    . GNP I .   ? 0.28843 0.26150 0.23075 -0.09462 0.05670  0.00228  201 GNP B N2    
5376 N N3    . GNP I .   ? 0.26619 0.25518 0.23040 -0.08499 0.04180  -0.00145 201 GNP B N3    
5377 C C4    . GNP I .   ? 0.23131 0.22795 0.20525 -0.07116 0.03064  0.00046  201 GNP B C4    
# 
